thesis.bib

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@article{Timmerman:1996p528,
	Abstract = {Cells need to distinguish between transient Ca2+ signals that induce events such as muscle contraction, secretion, adhesion and synaptic transmission, and sustained Ca2+ signals that are involved in cell proliferation and differentiation. The latter class of events is blocked in lymphocytes by the immunosuppressive drugs cyclosporin A and FK506, which inhibit calcineurin, a Ca2+-activated serine/threonine phosphatase necessary for the nuclear import of NF-AT transcription factors. Here we report that sustained high concentrations of Ca2+, but not transient pulses, are required to maintain NF-AT transcription factors in the nucleus, where they participate in Ca2+-dependent induction of genes required for lymphocyte activation and proliferation. Furthermore, overexpression and constitutive nuclear localization of NF-AT, but not Jun, Fos, NF-kappaB, Oct or Ets family members, renders the interleukin-2 enhancer in Jurkat T lymphocytes resistant to FK506 and cyclosporin A. Thus a primary effect of these immunosuppressive reagents is to control the subcellular localization of the NF-AT family of transcription factors.},
	Author = {Timmerman, L A and Clipstone, N A and Ho, S N and Northrop, J P and Crabtree, G R},
	Doi = {10.1038/383837a0},
	File = {:Users/orville/Dropbox/Papers/1996/Timmerman/Nature 1996 Timmerman.pdf:pdf},
	Journal = {Nature},
	Keywords = {Animals, Calcineurin, Calcium, Calmodulin-Binding Proteins, Cell Line, Cell Nucleus, Cyclosporine, DNA-Binding Proteins, Humans, Immunosuppressive Agents, Interleukin-2, Jurkat Cells, Lymphocyte Activation, Mice, NFATC Transcription Factors, Nuclear Proteins, Phosphoprotein Phosphatases, Signal Transduction, T-Lymphocytes, Tacrolimus, Transcription Factors, Transfection,Biological Transport},
	Month = oct,
	Number = {6603},
	Pages = {837--840},
	Pmid = {8893011},
	Title = {{Rapid shuttling of NF-AT in discrimination of Ca2+ signals and immunosuppression}},
	Volume = {383},
	Year = {1996},
	Bdsk-Url-1 = {http://dx.doi.org/10.1038/383837a0}}

@article{Motiani2010,
	Abstract = {Store-operated calcium (Ca(2+)) entry (SOCE) mediated by STIM/Orai proteins is a ubiquitous pathway that controls many important cell functions including proliferation and migration. STIM proteins are Ca(2+) sensors in the endoplasmic reticulum and Orai proteins are channels expressed at the plasma membrane. The fall in endoplasmic reticulum Ca(2+) causes translocation of STIM1 to subplasmalemmal puncta where they activate Orai1 channels that mediate the highly Ca(2+)-selective Ca(2+) release-activated Ca(2+) current (I(CRAC)). Whereas Orai1 has been clearly shown to encode SOCE channels in many cell types, the role of Orai2 and Orai3 in native SOCE pathways remains elusive. Here we analyzed SOCE in ten breast cell lines picked in an unbiased way. We used a combination of Ca(2+) imaging, pharmacology, patch clamp electrophysiology, and molecular knockdown to show that native SOCE and I(CRAC) in estrogen receptor-positive (ER(+)) breast cancer cell lines are mediated by STIM1/2 and Orai3 while estrogen receptor-negative (ER(-)) breast cancer cells use the canonical STIM1/Orai1 pathway. The ER(+) breast cancer cells represent the first example where the native SOCE pathway and I(CRAC) are mediated by Orai3. Future studies implicating Orai3 in ER(+) breast cancer progression might establish Orai3 as a selective target in therapy of ER(+) breast tumors.},
	Annote = {cellular processes influenced by SOCE. 
3 refs.},
	Author = {Motiani, Rajender K and Abdullaev, Iskandar F and Trebak, Mohamed},
	Doi = {10.1074/jbc.M110.102582},
	File = {:Users/orville/Desktop/papers/J. Biol. Chem.-2010-Motiani-19173-83.pdf:pdf},
	Issn = {1083-351X},
	Journal = {The Journal of biological chemistry},
	Keywords = {Breast Neoplasms,Breast Neoplasms: metabolism,Calcium,Calcium Channels,Calcium Channels: metabolism,Calcium: metabolism,Cell Adhesion Molecules,Cell Adhesion Molecules: metabolism,Cell Line, Tumor,Disease Progression,Endoplasmic Reticulum,Endoplasmic Reticulum: metabolism,Gene Expression Regulation, Neoplastic,Humans,Membrane Proteins,Membrane Proteins: metabolism,Neoplasm Proteins,Neoplasm Proteins: metabolism,Patch-Clamp Techniques,Protein Transport,Receptors, Estrogen,Receptors, Estrogen: metabolism},
	Month = jun,
	Number = {25},
	Pages = {19173--83},
	Pmid = {20395295},
	Title = {{A novel native store-operated calcium channel encoded by Orai3: selective requirement of Orai3 versus Orai1 in estrogen receptor-positive versus estrogen receptor-negative breast cancer cells.}},
	Url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2885196\&tool=pmcentrez\&rendertype=abstract},
	Volume = {285},
	Year = {2010},
	Bdsk-Url-1 = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2885196%5C&tool=pmcentrez%5C&rendertype=abstract},
	Bdsk-Url-2 = {http://dx.doi.org/10.1074/jbc.M110.102582}}

@article{Zhang2006,
	Abstract = {Recent studies by our group and others demonstrated a required and conserved role of Stim in store-operated Ca(2+) influx and Ca(2+) release-activated Ca(2+) (CRAC) channel activity. By using an unbiased genome-wide RNA interference screen in Drosophila S2 cells, we now identify 75 hits that strongly inhibited Ca(2+) influx upon store emptying by thapsigargin. Among these hits are 11 predicted transmembrane proteins, including Stim, and one, olf186-F, that upon RNA interference-mediated knockdown exhibited a profound reduction of thapsigargin-evoked Ca(2+) entry and CRAC current, and upon overexpression a 3-fold augmentation of CRAC current. CRAC currents were further increased to 8-fold higher than control and developed more rapidly when olf186-F was cotransfected with Stim. olf186-F is a member of a highly conserved family of four-transmembrane spanning proteins with homologs from Caenorhabditis elegans to human. The endoplasmic reticulum (ER) Ca(2+) pump sarco-/ER calcium ATPase (SERCA) and the single transmembrane-soluble N-ethylmaleimide-sensitive (NSF) attachment receptor (SNARE) protein Syntaxin5 also were required for CRAC channel activity, consistent with a signaling pathway in which Stim senses Ca(2+) depletion within the ER, translocates to the plasma membrane, and interacts with olf186-F to trigger CRAC channel activity.},
	Author = {Zhang, Shenyuan L and Yeromin, Andriy V and Zhang, Xiang H-F and Yu, Ying and Safrina, Olga and Penna, Aubin and Roos, Jack and Stauderman, Kenneth a and Cahalan, Michael D},
	Doi = {10.1073/pnas.0603161103},
	File = {:Users/orville/Desktop/papers/PNAS-2006-Zhang-9357-62.pdf:pdf},
	Isbn = {0603161103},
	Issn = {0027-8424},
	Journal = {Proceedings of the National Academy of Sciences of the United States of America},
	Keywords = {Animals,Calcium,Calcium Channels,Calcium Channels: genetics,Calcium Channels: metabolism,Calcium: metabolism,Double-Stranded,Double-Stranded: metabolism,Drosophila Proteins,Drosophila Proteins: genetics,Drosophila Proteins: metabolism,Drosophila melanogaster,Drosophila melanogaster: genetics,Drosophila melanogaster: metabolism,Enzyme Inhibitors,Enzyme Inhibitors: metabolism,Genome,Humans,Insect,Patch-Clamp Techniques,RNA,RNA Interference,Recombinant Fusion Proteins,Recombinant Fusion Proteins: genetics,Recombinant Fusion Proteins: metabolism,Signal Transduction,Signal Transduction: physiology,Thapsigargin,Thapsigargin: metabolism},
	Month = jun,
	Number = {24},
	Pages = {9357--62},
	Pmid = {16751269},
	Title = {{Genome-wide RNAi screen of Ca(2+) influx identifies genes that regulate Ca(2+) release-activated Ca(2+) channel activity.}},
	Url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1482614\&tool=pmcentrez\&rendertype=abstract},
	Volume = {103},
	Year = {2006},
	Bdsk-Url-1 = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1482614%5C&tool=pmcentrez%5C&rendertype=abstract},
	Bdsk-Url-2 = {http://dx.doi.org/10.1073/pnas.0603161103}}

@article{Hoth:1992p527,
	Abstract = {In many cell types, receptor-mediated Ca2+ release from internal stores is followed by Ca2+ influx across the plasma membrane. The sustained entry of Ca2+ is thought to result partly from the depletion of intracellular Ca2+ pools. Most investigations have characterized Ca2+ influx indirectly by measuring Ca(2+)-activated currents or using Fura-2 quenching by Mn2+, which in some cells enters the cells by the same influx pathway. But only a few studies have investigated this Ca2+ entry pathway more directly. We have combined patch-clamp and Fura-2 measurements to monitor membrane currents in mast cells under conditions where intracellular Ca2+ stores were emptied by either inositol 1,4,5-trisphosphate, ionomycin, or excess of the Ca2+ chelator EGTA. The depletion of Ca2+ pools by these independent mechanisms commonly induced activation of a sustained calcium inward current that was highly selective for Ca2+ ions over Ba2+, Sr2+ and Mn2+. This Ca2+ current, which we term ICRAC (calcium release-activated calcium), is not voltage-activated and shows a characteristic inward rectification. It may be the mechanism by which electrically nonexcitable cells maintain raised intracellular Ca2+ concentrations and replenish their empty Ca2+ stores after receptor stimulation.},
	Author = {Hoth, M and Penner, R},
	Doi = {10.1038/355353a0},
	File = {:Users/orville/Desktop/papers/355353a0.pdf:pdf},
	Journal = {Nature},
	Keywords = {Animals, Calcium Channel Blockers, Calcium Channels, Cations: Divalent, Cell Membrane Permeability, Cells: Cultured, Egtazic Acid, Inositol 1:4:5-Trisphosphate, Ionomycin, Mast Cells, Membrane Potentials, Rats, Terpenes, Thapsigargin,Calcium},
	Month = jan,
	Number = {6358},
	Pages = {353--356},
	Pmid = {1309940},
	Title = {{Depletion of intracellular calcium stores activates a calcium current in mast cells}},
	Volume = {355},
	Year = {1992},
	Bdsk-Url-1 = {http://dx.doi.org/10.1038/355353a0}}

@article{Dellis2011,
	Abstract = {Store-Operated Calcium Entry (SOCE) is the major Ca2+ ion entry pathway in lymphocytes and is responsible of a severe combined immunodeficiency (SCID) when deficient. It has recently been observed or highlighted in other cell types such as myoblasts and neurons, suggesting a wider physiological role of this pathway. Whereas Orai1 protein is considered to be the channel allowing the SOCE in T cells, it is hypothesized that other proteins like TRPC could associate with Orai1 to form SOCE with different pharmacology and kinetics in other cell types. Unraveling SOCE cell functions requires specific effectors to be identified, just as dihydropyridines were crucial for the study of Ca2+ voltage-gated channels, or spider/snake toxins for other ion channel classes. To identify novel SOCE effectors, we analyzed the effects of 2-aminoethyl diphenylborinate (2-APB) and its analogues. 2-APB is a molecule known to both potentiate and inhibit T cell SOCE, but it is also an effector of TRP channels and endoplasmic reticulum Ca2+-ATPase.},
	Author = {Dellis, Olivier and Mercier, Pierre and Chomienne, Christine},
	Doi = {10.1186/1471-2210-11-1},
	File = {:Users/orville/Desktop/papers/1471-2210-11-1.pdf:pdf},
	Issn = {1471-2210},
	Journal = {BMC pharmacology},
	Keywords = {Boron Compounds,Boron Compounds: chemistry,Boron Compounds: pharmacology,Calcium,Calcium Channels,Calcium Channels: genetics,Calcium Channels: metabolism,Calcium-Transporting ATPases,Calcium-Transporting ATPases: antagonists \& inhibi,Calcium: metabolism,Cell Line,Cell Line, Tumor,Dose-Response Relationship, Drug,Drug Synergism,Endoplasmic Reticulum,Endoplasmic Reticulum: drug effects,Endoplasmic Reticulum: metabolism,Enzyme Inhibitors,Enzyme Inhibitors: pharmacology,Gene Expression,Gene Expression: drug effects,Humans,Jurkat Cells,Molecular Structure,Reverse Transcriptase Polymerase Chain Reaction,Thapsigargin,Thapsigargin: pharmacology,U937 Cells},
	Month = jan,
	Number = {1},
	Pages = {1},
	Pmid = {21266088},
	Title = {{The boron-oxygen core of borinate esters is responsible for the store-operated calcium entry potentiation ability.}},
	Url = {http://www.biomedcentral.com/1471-2210/11/1},
	Volume = {11},
	Year = {2011},
	Bdsk-Url-1 = {http://www.biomedcentral.com/1471-2210/11/1},
	Bdsk-Url-2 = {http://dx.doi.org/10.1186/1471-2210-11-1}}

@article{Prakriya2001,
	Abstract = {1. The effects of the IP(3)-receptor antagonist 2-aminoethyldiphenyl borate (2-APB) on the Ca(2+) release-activated Ca(2+) current (I(CRAC)) in Jurkat human T cells, DT40 chicken B cells and rat basophilic leukaemia (RBL) cells were examined. 2. 2-APB elicited both stimulatory and inhibitory effects on Ca(2+) influx through CRAC channels. At concentrations of 1-5 microM, 2-APB enhanced Ca(2+) entry in intact cells and increased I(CRAC) amplitude by up to fivefold. At levels > or = 10 microM, 2-APB caused a transient enhancement of I(CRAC) followed by inhibition. 3. 2-APB altered the kinetics of fast Ca(2+)-dependent inactivation of I(CRAC). At concentrations of 1-5 microM, 2-APB increased the rate of fast inactivation. In contrast, 2-APB at higher concentrations (> or = 10 microM) reduced or completely blocked inactivation. 4. 2-APB inhibited Ca(2+) efflux from mitochondria. 5. 2-APB inhibited I(CRAC) more potently when applied extracellularly than intracellularly. Furthermore, increased protonation of 2-APB at low pH did not affect potentiation or inhibition. Thus, 2-APB may have an extracellular site of action. 6. Neither I(CRAC) activation by passive store depletion nor the effects of 2-APB were altered by intracellular dialysis with 500 microg ml(-1) heparin. 7. I(CRAC) is present in wild-type as well as mutant DT40 B cells lacking all three IP(3) receptor isoforms. 2-APB also potentiates and inhibits I(CRAC) in both cell types, indicating that 2-APB exerts its effects independently of IP(3) receptors. 8. Our results show that CRAC channel activation does not require physical interaction with IP(3) receptors as proposed in the conformational coupling model. Potentiation of I(CRAC) by 2-APB may be a useful diagnostic feature for positive identification of putative CRAC channel genes, and provides a novel tool for exploring the physiological functions of store-operated channels.},
	Annote = {Prakriya, M., \& Lewis, R. S. (2001). Potentiation and inhibition of Ca(2+) release-activated Ca(2+) channels by 2-aminoethyldiphenyl borate (2-APB) occurs independently of IP(3) receptors. The Journal of physiology, 536(Pt 1), 3-19. },
	Author = {Prakriya, M and Lewis, R S},
	File = {:Users/orville/Dropbox/Papers/2001/Prakriya/J Physiol 2001 Prakriya.pdf:pdf},
	Issn = {0022-3751},
	Journal = {The Journal of physiology},
	Keywords = {Animals,Boron Compounds,Boron Compounds: pharmacology,Calcium,Calcium Channels,Calcium Channels: metabolism,Calcium: metabolism,Chickens,Dose-Response Relationship, Drug,Humans,Inositol 1,4,5-Trisphosphate Receptors,Ion Channel Gating,Ion Channel Gating: drug effects,Ion Channel Gating: physiology,Jurkat Cells,Kinetics,Mitochondria,Mitochondria: drug effects,Mitochondria: metabolism,Patch-Clamp Techniques,Rats,Receptors, Cytoplasmic and Nuclear,Receptors, Cytoplasmic and Nuclear: metabolism},
	Month = oct,
	Number = {Pt 1},
	Pages = {3--19},
	Pmid = {11579153},
	Title = {{Potentiation and inhibition of Ca(2+) release-activated Ca(2+) channels by 2-aminoethyldiphenyl borate (2-APB) occurs independently of IP(3) receptors.}},
	Url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2278849\&tool=pmcentrez\&rendertype=abstract},
	Volume = {536},
	Year = {2001},
	Bdsk-Url-1 = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2278849%5C&tool=pmcentrez%5C&rendertype=abstract}}

@article{Lis2007,
	Abstract = {STIM1 in the endoplasmic reticulum and CRACM1 in the plasma membrane are essential molecular components for controlling the store-operated CRAC current. CRACM1 proteins multimerize and bind STIM1, and the combined overexpression of STIM1 and CRACM1 reconstitutes amplified CRAC currents. Mutations in CRACM1 determine the selectivity of CRAC currents, demonstrating that CRACM1 forms the CRAC channel's ion-selective pore, but the CRACM1 homologs CRACM2 and CRACM3 are less well characterized. Here, we show that both CRACM2 and CRACM3, when overexpressed in HEK293 cells stably expressing STIM1, potentiate I(CRAC) to current amplitudes 15-20 times larger than native I(CRAC). A nonconducting mutation of CRACM1 (E106Q) acts as a dominant negative for all three CRACM homologs, suggesting that they can form heteromultimeric channel complexes. All three CRACM homologs exhibit distinct properties in terms of selectivity for Ca(2+) and Na(+), differential pharmacological effects in response to 2-APB, and strikingly different feedback regulation by intracellular Ca(2+). Each of the CRAC channel proteins' specific functional features and the potential heteromerization provide for flexibility in shaping Ca(2+) signals, and their characteristic biophysical and pharmacological properties will aid in identifying CRAC-channel species in native cells that express them.},
	Author = {Lis, Annette and Peinelt, Christine and Beck, Andreas and Parvez, Suhel and Monteilh-Zoller, Mahealani and Fleig, Andrea and Penner, Reinhold},
	Doi = {10.1016/j.cub.2007.03.065},
	File = {:Users/orville/Dropbox/S2 stuff/CRACM1, CRACM2, and CRACM3 Are Store-Operated Ca2+ Channels with Distinct Functional Properties.pdf:pdf},
	Issn = {0960-9822},
	Journal = {Current biology : CB},
	Keywords = {Boron Compounds,Calcium,Calcium Channels,Calcium Channels: genetics,Calcium Channels: metabolism,Calcium: metabolism,Cell Line,Humans,Membrane Potentials,Membrane Potentials: physiology,Membrane Proteins,Membrane Proteins: metabolism,Multiprotein Complexes,Multiprotein Complexes: metabolism,Mutation,Mutation: genetics,Neoplasm Proteins,Neoplasm Proteins: metabolism},
	Month = may,
	Number = {9},
	Pages = {794--800},
	Pmid = {17442569},
	Title = {{CRACM1, CRACM2, and CRACM3 are store-operated Ca2+ channels with distinct functional properties.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/17442569},
	Volume = {17},
	Year = {2007},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/17442569},
	Bdsk-Url-2 = {http://dx.doi.org/10.1016/j.cub.2007.03.065}}

@article{Schindl2008,
	Abstract = {Stim1 in the endoplasmic reticulum and the three Orai (also termed CRACM) channels in the plasma-membrane are main components of native Ca(2+) release-activated Ca(2+) channels. A pharmacological hallmark of these channels is their distinct sensitivity to 2-aminoethoxydiphenyl borate (2-APB). Here we report that Orai3 currents can be robustly stimulated by 75 microm 2-APB independent of Stim1, whereas 2-APB at similar concentrations inhibited store-operated Orai1 currents. 2-APB did not only promote currents through Orai3 channels but also dramatically altered ion selectivity of Orai3 channels. This allowed for permeation of monovalent cations both in the inward as well as outward direction, which is in sharp contrast to the high Ca(2+) selectivity of store-operated Orai3 currents. An Orai3-R66W mutant, which lacked in analogy to the severe combined immune deficiency mutant Orai1-R91W store-operated activation, was also found to be resistant to 2-APB stimulation. The change in selectivity by 2-APB was associated with an increase in Orai3 minimum pore size from about 3.8A to more than 5.34 A. In line with a potential interaction of 2-APB with the Orai3 pore, among three pore mutants tested, the Orai3 E165Q mutant particularly resembled in its permeation properties those of 2-APB stimulated Orai3 and additionally exhibited a reduced response to 2-APB. In aggregate, stimulation of Orai3 currents by 2-APB occurred along with an alteration of the permeation pathway that represents a unique mechanism for regulating ion channel selectivity by chemical compounds.},
	Author = {Schindl, Rainer and Bergsmann, Judith and Frischauf, Irene and Derler, Isabella and Fahrner, Marc and Muik, Martin and Fritsch, Reinhard and Groschner, Klaus and Romanin, Christoph},
	Doi = {10.1074/jbc.M803101200},
	File = {:Users/orville/Dropbox/S2 stuff/specific CRAC inhibitors/J. Biol. Chem.-2008-Schindl-20261-7.pdf:pdf},
	Isbn = {4373224689280},
	Issn = {0021-9258},
	Journal = {The Journal of biological chemistry},
	Keywords = {Boron Compounds,Boron Compounds: pharmacology,Calcium Channels,Calcium Channels: genetics,Calcium Channels: metabolism,Cell Line,Cell Membrane,Cell Membrane: drug effects,Cell Membrane: metabolism,Electrophysiology,Glutamic Acid,Glutamic Acid: genetics,Glutamic Acid: metabolism,Humans,Membrane Proteins,Membrane Proteins: genetics,Membrane Proteins: metabolism,Mutation,Mutation: genetics,Neoplasm Proteins,Neoplasm Proteins: genetics,Neoplasm Proteins: metabolism,Patch-Clamp Techniques,Porosity},
	Month = jul,
	Number = {29},
	Pages = {20261--7},
	Pmid = {18499656},
	Title = {{2-aminoethoxydiphenyl borate alters selectivity of Orai3 channels by increasing their pore size.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/18499656},
	Volume = {283},
	Year = {2008},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/18499656},
	Bdsk-Url-2 = {http://dx.doi.org/10.1074/jbc.M803101200}}

@article{Schneider1972,
	Author = {Schneider, I},
	File = {:Users/orville/Dropbox/S2 stuff/schneider\_353.full.pdf:pdf},
	Issn = {0022-0752},
	Journal = {Journal of embryology and experimental morphology},
	Keywords = {Abdomen,Abdomen: growth \& development,Anal Canal,Anal Canal: growth \& development,Animals,Cell Count,Cell Line,Chitin,Drosophila melanogaster,Drosophila melanogaster: growth \& development,Female,Larva,Macrophages,Metamorphosis, Biological,Methods,Ovum,Sensory Receptor Cells,Sensory Receptor Cells: growth \& development,Time Factors,Trypsin},
	Month = apr,
	Number = {2},
	Pages = {353--65},
	Pmid = {4625067},
	Title = {{Cell lines derived from late embryonic stages of Drosophila melanogaster.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/4625067},
	Volume = {27},
	Year = {1972},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/4625067}}

@article{Hurwitz:1991p276,
	Abstract = {This book presents a current review of the biophysics, physiology, pharmacology, and clinical role of calcium channels.},
	Author = {Hurwitz, Leon and Partridge, L Donald and Leach, John K},
	Month = jan,
	Pages = {491},
	Title = {{Calcium channels: their properties, functions, regulation, and clinical relevance}},
	Url = {http://books.google.com/books?id=QzdhtNwTWUgC\&printsec=frontcover},
	Year = {1991},
	Bdsk-Url-1 = {http://books.google.com/books?id=QzdhtNwTWUgC%5C&printsec=frontcover}}

@book{WPutney:2006p130,
	Abstract = {Several new chapters have been added and in many cases, where chapters from the first edition were retained, new researchers were recruited to offer a fresh perspective.As calcium signaling involves such a breadth of technical approaches ...},
	Address = {Boca Raton, FL},
	Annote = {Putney, J. W. (2006). Calcium signaling, 509. },
	Author = {Putney, James W},
	Date-Modified = {2011-11-30 15:47:11 +0000},
	Edition = {2nd},
	Pages = {509},
	Publisher = {CRC Press},
	Series = {Methods in signal transduction},
	Title = {{Calcium signaling}},
	Url = {http://books.google.com/books?id=jkOOmdVkYQEC\&printsec=frontcover},
	Year = {2006},
	Bdsk-Url-1 = {http://books.google.com/books?id=jkOOmdVkYQEC%5C&printsec=frontcover}}

@book{GLambert:2006p191,
	Abstract = {This extensively updated and expanded second edition contains new chapters on the elctrophysiological measurement of Ca2+ channel activity, enhanced coverage of confocal microscopy, and practical tutorials on two of the most common ...},
	Address = {Totowa, NJ},
	Author = {Lambert, David G},
	Date-Modified = {2011-11-30 15:46:42 +0000},
	Edition = {2nd},
	Pages = {359},
	Publisher = {Humana Press},
	Series = {Methods in molecular biology},
	Title = {{Calcium signaling protocols}},
	Url = {http://books.google.com/books?id=bkugGjyVYdkC\&printsec=frontcover},
	Year = {2006},
	Bdsk-Url-1 = {http://books.google.com/books?id=bkugGjyVYdkC%5C&printsec=frontcover}}

@article{Putney:1986p283,
	Abstract = {A model is proposed for the mechanism by which activation of surface membrane receptors causes sustained Ca2+ entry into cells from the extracellular space. Reassessment of previously published findings on the behavior of receptor-regulated intracellular Ca2+ pools leads to the conclusion that when such pools are empty, a pathway from the extracellular space to the pool is opened; conversely when the pool is filled, the pathway is closed and it becomes relatively stable to depletion by low Ca2+ media or chelating agents. The biphasic nature of agonist-activated Ca2+-mobilization is thus seen as an initial emptying of the intracellular Ca2+ pool by inositol (1,4,5) trisphosphate, followed by rapid entry of Ca2+ into the pool and, in the continued presence of inositol (1,4,5) trisphosphate, into the cytosol. On withdrawal of agonist, inositol (1,4,5) trisphosphate is then rapidly degraded, the pathway from the pool to the cytosol is closed, and rapid entry from the outside continues until the Ca2+ content of the pool reaches a level that inactivates Ca2+ entry. This capacitative model allows for Ca2+ release and Ca2+ entry to be controlled by a single messenger, inositol (1,4,5) trisphosphate.},
	Author = {Putney, James W},
	File = {:Users/orville/Dropbox/S2 stuff/putney\_jr.pdf:pdf},
	Journal = {Cell Calcium},
	Keywords = {Animals,Calcium,Cell Membrane,Hydrolysis,Inositol 1:4:5-Trisphosphate,Inositol Phosphates,Ion Channels,Lipid Metabolism,Models: Biological,Phosphatidic Acids,Receptors: Cell Surface},
	Month = feb,
	Number = {1},
	Pages = {1--12},
	Pmid = {2420465},
	Title = {{A model for receptor-regulated calcium entry}},
	Url = {http://www.ncbi.nlm.nih.gov/sites/entrez?Db=pubmed\&Cmd=Retrieve\&list\_uids=2420465\&dopt=abstractplus},
	Volume = {7},
	Year = {1986},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/sites/entrez?Db=pubmed%5C&Cmd=Retrieve%5C&list%5C_uids=2420465%5C&dopt=abstractplus}}

@article{Streb:1983p278,
	Abstract = {Activation of receptors for a wide variety of hormones and neurotransmitters leads to an increase in the intracellular level of calcium. Much of this calcium is released from intracellular stores but the link between surface receptors and this internal calcium reservoir is unknown. Hydrolysis of the phosphoinositides, which is another characteristic feature of these receptors, has been implicated in calcium mobilization. The primary lipid substrates for the receptor mechanism seem to be two polyphosphoinositides, phosphatidylinositol 4-phosphate (PtdIns4P) and phosphatidylinositol 4,5-bisphosphate (PtdIns4,5P2), which are rapidly hydrolysed following receptor activation in various cells and tissues. The action of phospholipase C on these polyphosphoinositides results in the rapid formation of the water-soluble products inositol 1,4-bisphosphate (Ins1,4P2) and inositol 1,4,5-trisphosphate (Ins1,4,5P3). In the insect salivary gland, where changes in Ins1,4P2 and Ins1,4,5P2 have been studied at early time periods, increases in these inositol phosphates are sufficiently rapid to suggest that they might mobilize internal calcium. We report here that micromolar concentrations of Ins1,4,5P3 release Ca2+ from a nonmitochondrial intracellular Ca2+ store in pancreatic acinar cells. Our results strongly suggest that this is the same Ca2+ store that is released by acetylcholine.},
	Author = {Streb, H and Irvine, R F and Berridge, M J and Schulz, I},
	Doi = {doi:10.1038/306067a0},
	Journal = {Nature},
	Keywords = {Animals, Calcium, Carbachol, Cell Compartmentation, Inositol 1:4:5-Trisphosphate, Inositol Phosphates, Mitochondria, Pancreas, Rats, Structure-Activity Relationship, Sugar Phosphates,Adenosine Triphosphate},
	Month = nov,
	Number = {5938},
	Pages = {67--69},
	Pmid = {6605482},
	Title = {{Release of Ca2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate}},
	Volume = {306},
	Year = {1983},
	Bdsk-Url-1 = {http://dx.doi.org/10.1038/306067a0}}

@article{Smyth2010,
	Annote = {What is SOCE? 
- Store-operated calcium entry (SOCE) is the process of extracellular Ca2+, coming into the cell, due to depletion of the cell's internal Ca2+ stores. This increases the intracellular Ca2+ and allows for replenishing the stores, as well as providing Ca2+ necessary for various cellular processes.
        
What is the known function of SOCE?- Changing the Ca2+ concentration can occur by allowing Ca2+ into or out of the cell. SOCE is one way in which Ca2+ may enter. As was mentioned above, SOCE is a result of emptying Ca2+ stores, specifically endoplasmic reticulum (ER) stores. 
- In 1983 $\backslash$cite\{Streb:1983p278\} showed that inositol(1,4,5)-triphosphate (IP3) production lead to an increase in intracellular Ca2+ $\backslash$cite\{Taylor2006\} . 
The general mechanism presented for this involved receptor activation leading to production of phosphatidylinositol 4,5-bisphosphate (PIP2), which was then hydrolyzed by the enzyme phospholipase C (PLC) resulting in soluble IP3, and membrane bound diacyl glycerol (DAG) [reviews]. The IP3 goes on to  open the IP3 receptor (IP3R) allowing Ca2+ out of the ER $\backslash$cite\{Smyth2010\} $\backslash$cite\{Taylor2006\} [other reviews]. The decrease in ER calcium somehow acts as a signal for extracellular ca2+ to come in through the plasma membrane (PM) $\backslash$cite\{Smyth2010\}. 
The idea that intracellular ca2+ store depletion signaled the plasma membrane Ca2+ channel to open was put forth by Putney in 1986 $\backslash$cite\{Putney:1986p283\} $\backslash$cite\{Taylor2006\}. There had been little progress in the way of identifying the players carrying out SOCE until recently. The have Recent experiments have identified the molecular players involved in this process. 
        
What causes SOCE?
- STIM1 has been shown to act as a sensor for Ca2+ within the ER. Upon depletion, the ER-localized STIM1 will migrate to sites at or near the plasma membrane and, through interactions with SOCE channels, will somehow help in activation of these channels. Once activated, channels in the Orai family, with Orai1 being the only one which is both necessary and sufficient [cite],  allow Ca2+ passage into the cell.
        
What are its identifying characteristics? 
SOCE is defined by its requirement for depletion of ER [Ca2+] and this depletion does not need to be IP3-mediated. There is also a current associated with Ca2+ entry across the membrane, denoted as /emph\{I\}\$\_CRAC\$ for Ca2+ release-activated current [ + paper (nature, liu, kozak, gwack - first CRAC)]. 
Inhibition of SOCE by certain ions and pharmaceuticals is also a defining characteristic [BJP]. 
        
In order to better understand SOCE, we'll take a look t some of the important components below.
      },
	Author = {Smyth, J.T. and Hwang, S.Y. and Tomita, T. and DeHaven, W.I. and Mercer, J.C. and Putney, J.W.},
	Doi = {10.1111/j.1582-4934.2010.01168.x},
	File = {:Users/orville/Dropbox/S2 stuff/Journal of Cellular and Molecular Medicine 2010 Smyth.pdf:pdf},
	Journal = {Journal of Cellular and Molecular Medicine},
	Keywords = {ca cellular regulation,ca signaling mechanism,calcium signaling},
	Mendeley-Tags = {ca cellular regulation,ca signaling mechanism,calcium signaling},
	Number = {10},
	Pages = {2337--2349},
	Publisher = {Wiley Online Library},
	Title = {{Activation and regulation of store-operated calcium entry}},
	Url = {http://onlinelibrary.wiley.com/doi/10.1111/j.1582-4934.2010.01168.x/full},
	Volume = {14},
	Year = {2010},
	Bdsk-Url-1 = {http://onlinelibrary.wiley.com/doi/10.1111/j.1582-4934.2010.01168.x/full},
	Bdsk-Url-2 = {http://dx.doi.org/10.1111/j.1582-4934.2010.01168.x}}

@article{Putney2011,
	Abstract = {Store-operated Ca(2+) entry is a process whereby the depletion of intracellular Ca(2+) stores signals the opening of plasma membrane Ca(2+) channels. It has long been thought that the main function of store-operated Ca(2+) entry was the replenishment of intracellular Ca(2+) stores following their discharge during intracellular Ca(2+) signaling. Recent results, however, suggest that the primary function of these channels may be to provide direct Ca(2+) signals to recipients localized to spatially restricted areas close to the sites of Ca(2+) entry in order to initiate specific signaling pathways.},
	Author = {Putney, James W},
	Doi = {10.1007/s11064-010-0383-0},
	File = {:Users/orville/Dropbox/S2 stuff/Neurochem Res 2011 Putney.pdf:pdf},
	Issn = {1573-6903},
	Journal = {Neurochemical research},
	Keywords = {calcium channels \'{a} store-operated,calcium signaling \'{a} ion,channels \'{a},channels \'{a} orai \'{a},stim \'{a} calcium},
	Month = jul,
	Number = {7},
	Pages = {1157--65},
	Pmid = {21234676},
	Title = {{The physiological function of store-operated calcium entry.}},
	Url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3112236\&tool=pmcentrez\&rendertype=abstract},
	Volume = {36},
	Year = {2011},
	Bdsk-Url-1 = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3112236%5C&tool=pmcentrez%5C&rendertype=abstract},
	Bdsk-Url-2 = {http://dx.doi.org/10.1007/s11064-010-0383-0}}

@article{Taylor2006,
	Author = {Taylor, C.W.},
	File = {:Users/orville/Dropbox/S2 stuff/SOCE-a\_STIMulating\_stORAI.pdf:pdf},
	Journal = {Trends in biochemical sciences},
	Number = {11},
	Pages = {597--601},
	Publisher = {Elsevier},
	Title = {{Store-operated Ca2+ entry: a STIMulating stOrai}},
	Url = {http://www.sciencedirect.com/science/article/pii/S0968000406002702},
	Volume = {31},
	Year = {2006},
	Bdsk-Url-1 = {http://www.sciencedirect.com/science/article/pii/S0968000406002702}}

@article{Wilhelm2005,
	Abstract = {Translational regulation plays an essential role in many phases of the Drosophila life cycle. During embryogenesis, specification of the developing body pattern requires co-ordination of the translation of oskar, gurken and nanos mRNAs with their subcellular localization. In addition, dosage compensation is controlled by Sex-lethal-mediated translational regulation while dFMR1 (the Drosophila homologue of the fragile X mental retardation protein) controls translation of various mRNAs which function in the nervous system. Here we describe some of the mechanisms that are utilized to regulate these various processes. Our review highlights the complexity that can be involved with multiple factors employing different mechanisms to control the translation of a single mRNA.},
	Author = {Wilhelm, James E and Smibert, Craig a},
	Doi = {10.1042/BC20040097},
	File = {:Users/orville/Dropbox/S2 stuff/mechanisms of translatinal regulation in drosophila.pdf:pdf},
	Issn = {0248-4900},
	Journal = {Biology of the cell / under the auspices of the European Cell Biology Organization},
	Keywords = {Animals,Drosophila,Drosophila Proteins,Drosophila Proteins: biosynthesis,Drosophila Proteins: genetics,Drosophila Proteins: physiology,Drosophila: genetics,Drosophila: growth \& development,Drosophila: metabolism,Eukaryotic Initiation Factor-4E,Eukaryotic Initiation Factor-4E: physiology,Fragile X Mental Retardation Protein,Gene Expression Regulation, Developmental,Models, Genetic,Peptide Initiation Factors,Peptide Initiation Factors: physiology,RNA Interference,RNA-Binding Proteins,RNA-Binding Proteins: biosynthesis,RNA-Binding Proteins: genetics,RNA-Binding Proteins: physiology,Transforming Growth Factor alpha,Transforming Growth Factor alpha: biosynthesis,Transforming Growth Factor alpha: genetics},
	Month = apr,
	Number = {4},
	Pages = {235--52},
	Pmid = {15762846},
	Title = {{Mechanisms of translational regulation in Drosophila.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/15762846},
	Volume = {97},
	Year = {2005},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/15762846},
	Bdsk-Url-2 = {http://dx.doi.org/10.1042/BC20040097}}

@article{Millar1995,
	Abstract = {A cloned Drosophila muscarinic acetylcholine receptor (mAChR) has been stably expressed in a Drosophila cell line (S2) under the control of an inducible Drosophila metallothionein promoter. A clonal cell line (S2-Dm1-1) has been isolated which, after induction of mAChR expression with CuSO4, exhibits high-affinity, saturable, specific binding of the muscarinic antagonist N-methyl scopolamine (NMS). The apparent molecular mass of the expressed protein, calculated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), is in good agreement with the apparent molecular mass of mAChRs purified from Drosophila brain. Functional expression of the cloned mAChR in this stable cell line has been demonstrated by quantitative fluorescence ratio-imaging of Fura-2-loaded cells. We have observed transient, agonist-induced elevations in intracellular Ca2+ levels which can be completely blocked by atropine, whereas AFDX-116, a muscarinic antagonist which binds preferentially to the vertebrate mAChR M2 subtype, has little effect at 100 mumol l-1. The suitability of this stable Drosophila expression system for the characterization of neurotransmitter receptors is discussed.},
	Author = {Millar, N S and Baylis, H a and Reaper, C and Bunting, R and Mason, W T and Sattelle, D B},
	File = {:Users/orville/Dropbox/S2 stuff/1843.full.pdf:pdf},
	Issn = {0022-0949},
	Journal = {The Journal of experimental biology},
	Keywords = {Animals,Calcium,Calcium: metabolism,Cell Line,Cloning,Drosophila melanogaster,Drosophila melanogaster: cytology,Drosophila melanogaster: genetics,Drosophila melanogaster: metabolism,Electrophoresis,Fluorescence,Fluorescent Dyes,Fura-2,Gene Expression Regulation,Gene Expression Regulation: physiology,Microscopy,Molecular,Molecular Weight,Muscarinic,Muscarinic: biosynthesis,Muscarinic: genetics,N-Methylscopolamine,Parasympatholytics,Parasympatholytics: metabolism,Pirenzepine,Pirenzepine: analogs \& derivatives,Pirenzepine: pharmacology,Polyacrylamide Gel,Receptors,Scopolamine Derivatives,Scopolamine Derivatives: metabolism,cuso4 quenching of fura2,drosophila s2,fura2 quench},
	Mendeley-Tags = {cuso4 quenching of fura2,drosophila s2,fura2 quench},
	Month = sep,
	Number = {Pt 9},
	Pages = {1843--50},
	Pmid = {7595159},
	Title = {{Functional expression of a cloned Drosophila muscarinic acetylcholine receptor in a stable Drosophila cell line.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/7595159},
	Volume = {198},
	Year = {1995},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/7595159}}

@article{Moncoq2007,
	Abstract = {The sarcoplasmic reticulum Ca(2+)-ATPase is essential for calcium reuptake in the muscle contraction-relaxation cycle. Here we present structures of a calcium-free state with bound cyclopiazonic acid (CPA) and magnesium fluoride at 2.65 A resolution and a calcium-free state with bound CPA and ADP at 3.4A resolution. In both structures, CPA occupies the calcium access channel delimited by transmembrane segments M1-M4. Inhibition of Ca(2+)-ATPase is stabilized by a polar pocket that surrounds the tetramic acid of CPA and a hydrophobic platform that cradles the inhibitor. The calcium pump residues involved include Gln(56), Leu(61), Val(62), and Asn(101). We conclude that CPA inhibits the calcium pump by blocking the calcium access channel and immobilizing a subset of transmembrane helices. In the E2(CPA) structure, ADP is bound in a distinct orientation within the nucleotide binding pocket. The adenine ring is sandwiched between Arg(489) of the nucleotide-binding domain and Arg(678) of the phosphorylation domain. This mode of binding conforms to an adenine recognition motif commonly found in ATP-dependent proteins.},
	Author = {Moncoq, Karine and Trieber, Catharine a and Young, Howard S},
	Doi = {10.1074/jbc.M611653200},
	File = {:Users/orville/Dropbox/S2 stuff/J Biol Chem 2007 Moncoq.pdf:pdf},
	Issn = {0021-9258},
	Journal = {The Journal of biological chemistry},
	Keywords = {Animals,Binding Sites,Crystallography, X-Ray,Indoles,Indoles: chemistry,Indoles: pharmacology,Protein Binding,Protein Conformation,Rabbits,Sarcoplasmic Reticulum Calcium-Transporting ATPase},
	Month = mar,
	Number = {13},
	Pages = {9748--57},
	Pmid = {17259168},
	Title = {{The molecular basis for cyclopiazonic acid inhibition of the sarcoplasmic reticulum calcium pump.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/17259168},
	Volume = {282},
	Year = {2007},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/17259168},
	Bdsk-Url-2 = {http://dx.doi.org/10.1074/jbc.M611653200}}

@article{Frischauf2009,
	Author = {Frischauf, I. and Muik, M. and Derler, I. and Bergsmann, J. and Fahrner, M. and Schindl, R. and Groschner, K. and Romanin, C.},
	Doi = {10.1074/jbc.M109.018408},
	File = {:Users/orville/Downloads/J. Biol. Chem.-2009-Frischauf-21696-706.pdf:pdf},
	Issn = {0021-9258},
	Journal = {Journal of Biological Chemistry},
	Keywords = {methods,methods write-up,orai,orai methods},
	Mendeley-Tags = {methods,methods write-up,orai,orai methods},
	Month = jun,
	Number = {32},
	Pages = {21696--21706},
	Title = {{Molecular Determinants of the Coupling between STIM1 and Orai Channels: DIFFERENTIAL ACTIVATION OF Orai1-3 CHANNELS BY A STIM1 COILED-COIL MUTANT}},
	Url = {http://www.jbc.org/cgi/doi/10.1074/jbc.M109.018408},
	Volume = {284},
	Year = {2009},
	Bdsk-Url-1 = {http://www.jbc.org/cgi/doi/10.1074/jbc.M109.018408},
	Bdsk-Url-2 = {http://dx.doi.org/10.1074/jbc.M109.018408}}

@article{Masereeuw2000,
	Author = {Masereeuw, Rosalinde and {Van Pelt}, A.P. and {Van Os}, S.H.G. and Willems, P.H.G.M. and Smits, Paul and Russel, F.G.M.},
	File = {:Users/orville/Documents/Papers/2000/Masereeuw/Br J Pharmacol 2000 Masereeuw.pdf:pdf},
	Journal = {British journal of pharmacology},
	Keywords = {drug interaction,membrane potential,renal drug handling,respiratory control,uncoupling oxidative},
	Number = {1},
	Pages = {57--62},
	Publisher = {Wiley Online Library},
	Title = {{Probenecid interferes with renal oxidative metabolism: A potential pitfall in its use as an inhibitor of drug transport}},
	Url = {http://onlinelibrary.wiley.com/doi/10.1038/sj.bjp.0703541/full},
	Volume = {131},
	Year = {2000},
	Bdsk-Url-1 = {http://onlinelibrary.wiley.com/doi/10.1038/sj.bjp.0703541/full}}

@article{Bunch1988,
	Author = {Bunch, T.A. and Grinblat, Y. and Goldstein, L.S.B.},
	File = {:Users/orville/Dropbox/S2 stuff/characterization and use of the drosophila metallothionein promoter in cultured D. melo cells.pdf:pdf},
	Journal = {Nucleic acids research},
	Number = {3},
	Pages = {1043},
	Publisher = {Oxford Univ Press},
	Title = {{Characterization and use of the Drosophila metallothionein promoter in cultured Drosophila melanogaster cells.}},
	Url = {http://nar.oxfordjournals.org/content/16/3/1043.short},
	Volume = {16},
	Year = {1988},
	Bdsk-Url-1 = {http://nar.oxfordjournals.org/content/16/3/1043.short}}

@article{Luce-Fedrow2008,
	Abstract = {Ehrlichia chaffeensis is an obligate intracellular bacterium and the causative agent of human monocytic ehrlichiosis. Although this pathogen grows in several mammalian cell lines, no general model for eukaryotic cellular requirements for bacteria replication has yet been proposed. We found that Drosophila S2 cells are permissive for the growth of E. chaffeensis. We saw morulae (aggregates of bacteria) by microscopy, detected the E. chaffeensis 16S rRNA gene by reverse transcriptase PCR, and used immunocytochemistry to detect E. chaffeensis in S2 and mammalian cells. Bacteria grown in S2 cells reinfected mammalian macrophages. S2 cells were made nonpermissive for E. chaffeensis through incubation with lipopolysaccharide. Our results demonstrate that S2 cells are an appropriate system for studying the pathogenesis of E. chaffeensis. The use of a Drosophila system has the potential to serve as a model system for studying Ehrlichia due to its completed genome, ease of genetic manipulation, and the availability of mutants.},
	Author = {Luce-Fedrow, Alison and {Von Ohlen}, Tonia and Boyle, Daniel and Ganta, Roman R and Chapes, Stephen K},
	Doi = {10.1128/AEM.02467-07},
	File = {:Users/orville/Downloads/1886.pdf:pdf},
	Issn = {1098-5336},
	Journal = {Applied and environmental microbiology},
	Keywords = {Animals,Cell Line,Drosophila,Ehrlichia chaffeensis,Ehrlichia chaffeensis: drug effects,Ehrlichia chaffeensis: genetics,Ehrlichia chaffeensis: growth \& development,Immunohistochemistry,Lipopolysaccharides,Lipopolysaccharides: pharmacology,Microscopy, Electron, Transmission,RNA, Ribosomal, 16S,RNA, Ribosomal, 16S: genetics,Reverse Transcriptase Polymerase Chain Reaction},
	Month = mar,
	Number = {6},
	Pages = {1886--91},
	Pmid = {18245255},
	Title = {{Use of Drosophila S2 cells as a model for studying Ehrlichia chaffeensis infections.}},
	Url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2268305\&tool=pmcentrez\&rendertype=abstract},
	Volume = {74},
	Year = {2008},
	Bdsk-Url-1 = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2268305%5C&tool=pmcentrez%5C&rendertype=abstract},
	Bdsk-Url-2 = {http://dx.doi.org/10.1128/AEM.02467-07}}

@article{Eble1998,
	Abstract = {Using insect cells, we expressed large quantities of soluble human integrin alpha 3 beta 1 ectodomain heterodimers, in which cytoplasmic and transmembrane domains were replaced by Fos and Jun dimerization motifs. In direct ligand binding assays, soluble alpha 3 beta 1 specifically bound to laminin-5 and laminin-10, but not to laminin-1, laminin-2, fibronectin, various collagens, nidogen, thrombospondin, or complement factors C3 and C3b. Soluble alpha 3 beta1 integrin also bound to invasin, a bacterial surface protein, that mediates entry of Yersinia species into the eukaryotic host cell. Invasin completely displaced laminin-5 from the alpha 3 beta 1 integrin, suggesting sterically overlapping or identical binding sites. In the presence of 2 mM Mg2+, alpha 3 beta 1's binding affinity for invasin (Kd = 3.1 nM) was substantially greater than its affinity for laminin-5 (Kd > 600 nM). Upon addition of 1 mM Mn2+, or activating antibody 9EG7, binding affinity for both laminin-5 and invasin increased by about 10-fold, whereas the affinity decreased upon addition of 2 mM Ca2+. Thus, functional regulation of the purified soluble integrin alpha 3 beta 1 ectodomain heterodimer resembles that of wild-type membrane-anchored beta 1 integrins. The integrin alpha 3 subunit was entirely cleaved into disulfide-linked heavy and light chains, at a newly defined cleavage site located C-terminal of a tetrabasic RRRR motif. Within the alpha 3 light chain, all potential N-glycosylation sites bear N-linked mannose-rich carbohydrate chains, suggesting an important structural role of these sugar residues in the stalk-like region of the integrin heterodimer. In conclusion, studies of our recombinant alpha 3 beta 1 integrin have provided new insights into alpha 3 beta1 structure, ligand binding function, specificity, and regulation.},
	Annote = {Paper used insect cells to express human surface proteins. 
How complex are these proteins compared to the proteins we wish to express?
Hydropathy plots and glycosylation points are good places to start comparisons. 
        
Pick the most complex protein used in this paper and compare to all of ours? 
        
================================
        
Expressed soluble  heterodimers
Purification of integrin achieved using immobilized IBD of invasin, a pathogenic ligand.
 - similar exp't using orais and stims possible to  determine whether binding between these is direct or indirect. 
        
puc-hygMT-a3-Fos construction
Method: fuse int a3 ectodomain w/ dimerizing a helix of Fos
1. Pcr from AvrII of a3 to end of ectodomain, adding spacer and first few AA of Fos, at end
2. PCR Fos with a3 C-terminus and spacer before first few AA of Fos in fwd primer, and end of Fos + XbaI site in rev primer. 
        
So far :
        
AvrII site + a3 + salI + fos + xbaI
        
3. Do PCR with outer primers to get from AvrII to XbaI site in one amplicon
4. Digest with AvrII and XbaI and replace WT a3. The TM domains now replaced w/ Fos dimerization domains. 
        
\~{} 690 bp inserted. No sequencing done afterward. 
      },
	Author = {Eble, J a and Wucherpfennig, K W and Gauthier, L and Dersch, P and Krukonis, E and Isberg, R R and Hemler, M E},
	Doi = {10.1021/bi980175+},
	File = {:Users/orville/Dropbox/S2 stuff/hygromycin b/bi980175\%2B.pdf:pdf},
	Issn = {0006-2960},
	Journal = {Biochemistry},
	Keywords = {Acute,Adhesins,Animals,Bacterial,Bacterial Proteins,Bacterial Proteins: metabolism,Cell Adhesion Molecules,Cell Adhesion Molecules: metabolism,Cell Line,Cultured,Drosophila,Erythroblastic,Genetic Vectors,Genetic Vectors: chemical synthesis,Genetic Vectors: metabolism,Humans,Integrin alpha3beta1,Integrins,Integrins: genetics,Integrins: isolation \& purification,Integrins: metabolism,Leukemia,Protein Binding,Rats,Recombinant Fusion Proteins,Recombinant Fusion Proteins: biosynthesis,Recombinant Fusion Proteins: isolation \& purificat,Recombinant Fusion Proteins: metabolism,Solubility,Titrimetry,Tumor Cells,Yersinia,Yersinia: physiology,pucHyg-MT,pucHygMT,pucHygroMT,puchygro-MT,use of puchygMT},
	Mendeley-Tags = {pucHyg-MT,pucHygMT,pucHygroMT,puchygro-MT,use of puchygMT},
	Month = aug,
	Number = {31},
	Pages = {10945--55},
	Pmid = {9692987},
	Title = {{Recombinant soluble human alpha 3 beta 1 integrin: purification, processing, regulation, and specific binding to laminin-5 and invasin in a mutually exclusive manner.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/9692987},
	Volume = {37},
	Year = {1998},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/9692987},
	Bdsk-Url-2 = {http://dx.doi.org/10.1021/bi980175+}}

@article{Johanson1995,
	Abstract = {Human interleukin 5 (hIL5) and soluble forms of its receptor $\alpha$ subunit were expressed in Drosophila cells and purified to homogeneity, allowing a detailed structural and functional analysis. B cell proliferation confirmed that the hIL5 was biologically active. Deglycosylated hIL5 remained active, while similarly deglycosylated receptor $\alpha$ subunit lost activity. The crystal structure of the deglycosylated hIL5 was determined to 2.6-\AA resolution and found to be similar to that of the protein produced in Escherichia coli. Human IL5 was shown by analytical ultracentrifugation to form a 1:1 complex with the soluble domain of the hIL5 receptor $\alpha$ subunit (shIL5R$\alpha$). Additionally, the relative abundance of ligand and receptor in the hIL5·shIL5R$\alpha$ complex was determined to be 1:1 by both titration calorimetry and SDS-polyacrylamide gel electrophoresis analysis of dissolved cocrystals of the complex. Titration microcalorimetry yielded equilibrium dissociation constants of 3.1 and 2.0 n M, respectively, for the binding of hIL5 to shIL5R$\alpha$ and to a chimeric form of the receptor containing shIL5R$\alpha$ fused to the immunoglobulin Fc domain (shIL5R$\alpha$-Fc). Analysis of the binding thermodynamics of IL5 and its soluble receptor indicates that conformational changes are coupled to the binding reaction. Kinetic analysis using surface plasmon resonance yielded data consistent with the Kdvalues from calorimetry and also with the possibility of conformational isomerization in the interaction of hIL5 with the receptor $\alpha$ subunit. Using a radioligand binding assay, the affinity of hIL5 with full-length hIL5R$\alpha$ in Drosophila membranes was found to be 6 n M, in accord with the affinities measured for the soluble receptor forms. Hence, most of the binding energy of the $\alpha$ receptor is supplied by the soluble domain. Taken with other aspects of hIL5 structure and biological activity, the data obtained allow a prediction for how 1:1 stoichiometry and conformational change can lead to the formation of hIL5·receptor $\alpha$$\beta$ complex and signal transduction.},
	Author = {Johanson, K. and Appelbaum, E. and Doyle, M. and Hensley, P. and Zhao, B. and Abdel-Meguid, S.S. and Young, P. and Cook, R. and Carr, S. and Matico, R. and Others},
	File = {:Users/orville/Dropbox/S2 stuff/unsorted/J. Biol. Chem.-1995-Johanson-9459-71.pdf:pdf},
	Journal = {Journal of Biological Chemistry},
	Number = {16},
	Pages = {9459},
	Publisher = {ASBMB},
	Title = {{Binding Interactions of Human Interleukin 5 with Its Receptor $\alpha$ Subunit}},
	Url = {http://www.jbc.org/content/270/16/9459.short},
	Volume = {270},
	Year = {1995},
	Bdsk-Url-1 = {http://www.jbc.org/content/270/16/9459.short}}

@article{Mignen2008a,
	Abstract = {Agonist-activated Ca(2+) signals in non-excitable cells are profoundly influenced by calcium entry via both store-operated and store-independent conductances. Recent studies have demonstrated that STIM1 plays a key role in the activation of store-operated conductances including the Ca(2+)-release-activated Ca(2+) (CRAC) channels, and that Orai1 comprises the pore-forming component of these channels. We recently demonstrated that STIM1 also regulates the activity of the store-independent, arachidonic acid-regulated Ca(2+) (ARC) channels, but does so in a manner entirely distinct from its regulation of the CRAC channels. This shared ability to be regulated by STIM1, together with their similar biophysical properties, suggested that these two distinct conductances may be molecularly related. Here, we report that whilst the levels of Orai1 alone determine the magnitude of the CRAC channel currents, both Orai1 and the closely related Orai3 are critical for the corresponding currents through ARC channels. Thus, in cells stably expressing STIM1, overexpression of Orai1 increases both CRAC and ARC channel currents. Whilst similar overexpression of Orai3 alone has no effect, ARC channel currents are specifically increased by expression of Orai3 in cells stably expressing Orai1. Moreover, expression of a dominant-negative mutant Orai3, either alone or in cells expressing wild-type Orai1, profoundly and specifically reduces currents through the ARC channels without affecting those through the CRAC channels, and siRNA-mediated knockdown of either Orai1 or Orai3 markedly inhibits ARC channel currents. Importantly, our data also show that the precise effects observed critically depend on which of the three proteins necessary for effective ARC channel activity (STIM1, Orai1 and Orai3) are rate limiting under the specific conditions employed.},
	Annote = {RT-PCR Methods},
	Author = {Mignen, Olivier and Thompson, Jill L and Shuttleworth, Trevor J},
	Doi = {10.1113/jphysiol.2007.146258},
	File = {:Users/orville/Dropbox/S2 stuff/unsorted/tjp0586-0185.pdf:pdf},
	Issn = {0022-3751},
	Journal = {The Journal of physiology},
	Keywords = {Arachidonic Acid,Arachidonic Acid: pharmacology,Calcium,Calcium Channels,Calcium Channels: drug effects,Calcium Channels: metabolism,Calcium Signaling,Calcium Signaling: physiology,Calcium: metabolism,Cell Line,Electrophysiology,Humans,Membrane Proteins,Membrane Proteins: metabolism,Neoplasm Proteins,Neoplasm Proteins: metabolism,Patch-Clamp Techniques,Transfection,cell line methods,methods write-up,rtpcr methods},
	Mendeley-Tags = {cell line methods,methods write-up,rtpcr methods},
	Month = jan,
	Number = {1},
	Pages = {185--95},
	Pmid = {17991693},
	Title = {{Both Orai1 and Orai3 are essential components of the arachidonate-regulated Ca2+-selective (ARC) channels.}},
	Url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2375546\&tool=pmcentrez\&rendertype=abstract},
	Volume = {586},
	Year = {2008},
	Bdsk-Url-1 = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2375546%5C&tool=pmcentrez%5C&rendertype=abstract},
	Bdsk-Url-2 = {http://dx.doi.org/10.1113/jphysiol.2007.146258}}

@article{Potier2009,
	Abstract = {The identity of store-operated calcium (Ca(2+)) entry (SOCE) channels in vascular smooth muscle cells (VSMCs) remains a highly contentious issue. Whereas previous studies have suggested that SOCE in VSMCs is mediated by the nonselective transient receptor potential canonical (TRPC) 1 protein, the identification of STIM1 and Orai1 as essential components of I(CRAC), a highly Ca(2+)-selective SOCE current in leukocytes, has challenged that view. Here we show that cultured proliferative migratory VSMCs isolated from rat aorta (called "synthetic") display SOCE with classic features, namely inhibition by 2-aminoethoxydiphenyl borate, ML-9, and low concentrations of lanthanides. On store depletion, synthetic VSMCs and A7r5 cells display currents with characteristics of I(CRAC). Protein knockdown of either STIM1 or Orai1 in synthetic VSMCs greatly reduced SOCE, whereas Orai2, Orai3, TRPC1, TRPC4, and TRPC6 knockdown had no effect. Orai1 knockdown reduced I(CRAC) in synthetic VSMCs and A7r5 cells. Synthetic VSMCs showed up-regulated STIM1/Orai1 proteins and SOCE compared with quiescent freshly isolated VSMC. Knockdown of STIM1 and Orai1 inhibited synthetic VSMC proliferation and migration, whereas STIM2, Orai2, and Orai3 knockdown had no effect. To our knowledge, these results are the first to show I(CRAC) in VSMCs and resolve a long-standing controversy by identifying CRAC as the elusive VSMC SOCE channel important for proliferation and migration.},
	Annote = { rtpcr methods; ca imaging methods},
	Author = {Potier, Marie and Gonzalez, Jos\'{e} C and Motiani, Rajender K and Abdullaev, Iskandar F and Bisaillon, Jonathan M and Singer, Harold a and Trebak, Mohamed},
	Doi = {10.1096/fj.09-131128},
	File = {:Users/orville/Dropbox/S2 stuff/unsorted/Evidence for STIM1- and Orai1-dependent store-operated calcium influx.full.pdf:pdf},
	Issn = {1530-6860},
	Journal = {The FASEB journal : official publication of the Federation of American Societies for Experimental Biology},
	Keywords = {Animals,Calcium Channels,Calcium Channels: drug effects,Calcium Channels: genetics,Calcium Channels: metabolism,Calcium Signaling,Cell Movement,Cell Movement: physiology,Cell Proliferation,Cells,Cultured,Membrane Glycoproteins,Membrane Glycoproteins: antagonists \& inhibitors,Membrane Glycoproteins: genetics,Membrane Glycoproteins: metabolism,Muscle,Myocytes,Patch-Clamp Techniques,RNA,Rats,Small Interfering,Small Interfering: genetics,Smooth,Smooth Muscle,Smooth Muscle: cytology,Smooth Muscle: drug effects,Smooth Muscle: physiology,Thapsigargin,Thapsigargin: pharmacology,Vascular,Vascular: cytology,Vascular: drug effects,Vascular: physiology,ca imaging methods,cell line methods,methods write-up,rtpcr methods},
	Mendeley-Tags = {ca imaging methods,cell line methods,methods write-up,rtpcr methods},
	Month = aug,
	Number = {8},
	Pages = {2425--37},
	Pmid = {19364762},
	Title = {{Evidence for STIM1- and Orai1-dependent store-operated calcium influx through ICRAC in vascular smooth muscle cells: role in proliferation and migration.}},
	Url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2717784\&tool=pmcentrez\&rendertype=abstract},
	Volume = {23},
	Year = {2009},
	Bdsk-Url-1 = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2717784%5C&tool=pmcentrez%5C&rendertype=abstract},
	Bdsk-Url-2 = {http://dx.doi.org/10.1096/fj.09-131128}}

@article{Schetz2004,
	Abstract = {The Schneider-2 (S2) Drosophila cell line is well suited for the stable overexpression of recombinant proteins using plasmid-based protein expression vectors. Following drug selection, a polyclonal S2 cell line can be induced to express on the order of 2 to 100 pmol/mg membrane protein for G-coupled protein receptors, 4000 to 100,000 sites/cell for other membrane receptors and 3 to 35 mg/liter for soluble and secreted proteins.},
	Author = {Schetz, John a and Shankar, Eswar P N},
	Doi = {10.1002/0471142301.ns0416s27},
	File = {:Users/orville/Dropbox/S2 stuff/hygromycin b/209202.pdf:pdf},
	Issn = {1934-8576},
	Journal = {Current protocols in neuroscience / editorial board, Jacqueline N. Crawley ... [et al.]},
	Keywords = {Animals,Biomedical Research,Biomedical Research: methods,Cell Line,Cell Surface,Cell Surface: metabolism,Drosophila,Drosophila: genetics,Drosophila: metabolism,G-Protein-Coupled,G-Protein-Coupled: metabolism,Gene Transfer Techniques,Genetic Vectors,Membrane Proteins,Membrane Proteins: metabolism,Neurosciences,Neurosciences: methods,Plasmids,Receptors,Recombinant Proteins,Recombinant Proteins: genetics,Recombinant Proteins: metabolism,Up-Regulation},
	Month = sep,
	Pages = {Unit 4.16},
	Pmid = {18428600},
	Title = {{Protein expression in the Drosophila Schneider 2 cell system.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/18428600},
	Volume = {Chapter 4},
	Year = {2004},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/18428600},
	Bdsk-Url-2 = {http://dx.doi.org/10.1002/0471142301.ns0416s27}}

@article{Xu2010,
	Abstract = {Natural resistance of wheat against Fusarium head blight (FHB) is inadequate and new strategies for controlling the disease are required. Chitin synthases that catalyze chitin biosynthesis would be an ideal target for antifungal agents. In this study, a class I chitin synthase gene (CHS1) from Fusarium asiaticum, the predominant species of FHB pathogens on wheat in China, was functionally disrupted via Agrobacterium tumefaciens-mediated transformation. Specific disruption of the CHS1 gene resulted in a 58\% reduction of chitin synthase activity, accompanied by decreases of 35\% in chitin content, 22\% in conidiation, and 16\% in macroconidium length. The Deltachs1 mutant strain had a growth rate comparable to that of the wild-type on PDA medium but had a 35\% increase in the number of nuclear cellulae and exhibited a remarkably increased sensitivity to osmosis stresses. Electron microscopy revealed substantial changes occurring in cell wall structures of the macroconidium, ascospore, and mycelium, with the most profound changes in the mycelium. Furthermore, the Deltachs1 mutant displayed significantly reduced pathogenicity on wheat spikes and seedlings. Re-introduction of a functional CHS1 gene into the Deltachs1 mutant strain restored the wild-type phenotype. These results reveal an important in vivo role played by a CHS1 gene in a FHB pathogen whose mycelial chitin could serve as a target for controlling the disease.},
	Author = {Xu, Yu-Bin and Li, He-Ping and Zhang, Jing-Bo and Song, Bo and Chen, Fang-Fang and Duan, Xiao-Jun and Xu, Huai-Qian and Liao, Yu-Cai},
	Doi = {10.1016/j.fgb.2009.11.003},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Xu et al. - 2010 - Disruption of the chitin synthase gene CHS1 from Fusarium asiaticum results in an altered structure of cell walls and reduced virulence..pdf:pdf},
	Issn = {1096-0937},
	Journal = {Fungal genetics and biology : FG \& B},
	Keywords = {Amino Acid Sequence,Antibodies,Cell Wall,Cell Wall: ultrastructure,China,Chitin,Chitin Synthase,Chitin Synthase: genetics,Chitin Synthase: metabolism,Chitin: analysis,DNA,Fungal,Fungal Proteins,Fungal Proteins: analysis,Fungal Proteins: genetics,Fungal: analysis,Fungal: genetics,Fungal: metabolism,Fusarium,Fusarium: genetics,Fusarium: pathogenicity,Fusarium: ultrastructure,Gene Expression Regulation,Genes,Genetic Complementation Test,Genetic Engineering,Genetic Engineering: methods,Glucosyltransferases,Glucosyltransferases: analysis,Glucosyltransferases: genetics,Mutation,Recombinant Fusion Proteins,Recombinant Fusion Proteins: analysis,Recombinant Fusion Proteins: genetics,Spores,Triticum,Triticum: microbiology,Virulence,Virulence: genetics,hygb rtpcr primers},
	Mendeley-Tags = {hygb rtpcr primers},
	Month = mar,
	Number = {3},
	Pages = {205--15},
	Pmid = {19941967},
	Publisher = {Elsevier Inc.},
	Title = {{Disruption of the chitin synthase gene CHS1 from Fusarium asiaticum results in an altered structure of cell walls and reduced virulence.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/19941967},
	Volume = {47},
	Year = {2010},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/19941967},
	Bdsk-Url-2 = {http://dx.doi.org/10.1016/j.fgb.2009.11.003}}

@misc{TheMendeleySupportTeam2011,
	Abstract = {A quick introduction to Mendeley. Learn how Mendeley creates your personal digital library, how to organize and annotate documents, how to collaborate and share with colleagues, and how to generate citations and bibliographies.},
	Address = {London},
	Author = {{The Mendeley Support Team}},
	Booktitle = {Mendeley Desktop},
	File = {:Users/orville/Applications/Mendeley Desktop.app/Contents/Resources/FAQ.pdf:pdf},
	Keywords = {Mendeley,how-to,user manual},
	Pages = {1--16},
	Publisher = {Mendeley Ltd.},
	Title = {{Getting Started with Mendeley}},
	Url = {http://www.mendeley.com},
	Year = {2011},
	Bdsk-Url-1 = {http://www.mendeley.com}}

@misc{Kim2010,
	Abstract = {In this study, we developed an efficient electroporation-mediated transformation system featuring Flammulina velutipes. The flammutoxin (ftx) gene of F. velutipes was isolated by reverse transcription-PCR. pFTXHg plasmid was constructed using the partial ftx gene (410 bp) along with the hygromycin B phosphotransferase gene (hygB) downstream of the glyceralde- hydes-3-phosphate dehydrogenase (gpd) promoter. The plasmid was transformed into protoplasts of monokaryotic strain 4019-20 of F. velutipes by electroporation. High transformation efficiency was obtained with an electric-pulse of 1.25 kV/cm by using 177 transformants/µg of DNA in 1× 107 protoplasts. PCR and Southern blot hybridization indicated that a single copy of the plasmid DNA was inserted at different locations in the F. velutipes genome by non-homologous recombination. Therefore, this transformation system could be used as a useful tool for gene function analysis of F. velutipes.},
	Annote = {Not imp't for thesis},
	Author = {Kim, Jong-Kun and Park, Young-Jin and Kong, Won-Sik and Kang, Hee-Wan},
	Booktitle = {Mycobiology},
	Doi = {10.4489/MYCO.2010.38.4.331},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Kim, , Young Jin Park - 2010 - Highly Efficient Electroporation-mediated Transformation into Edible Mushroom Flammulina velutipes.pdf:pdf},
	Keywords = {Electroporation,Flammulina velutipes,Flammutoxin gene,Hygromycin B gene,Protoplast,full length PCR,hygb,hygb fl pcr,whole primers},
	Mendeley-Tags = {full length PCR,hygb,hygb fl pcr,whole primers},
	Pages = {331--335},
	Title = {{Highly Efficient Electroporation-mediated Transformation into Edible Mushroom Flammulina velutipes}},
	Url = {http://www.mycobiology.or.kr/Upload/files/MYCOBIOLOGY/38(4) 331-335.pdf},
	Year = {2010},
	Bdsk-Url-1 = {http://www.mycobiology.or.kr/Upload/files/MYCOBIOLOGY/38(4)%20331-335.pdf},
	Bdsk-Url-2 = {http://dx.doi.org/10.4489/MYCO.2010.38.4.331}}

@article{DiVirgilio1990,
	Abstract = {Fura-2 is widely used to measure the concentration of cytosolic free calcium, but in many cells the dye does not remain localized within the cytoplasmic matrix. In these cells, Fura-2 is sequestered within intracellular organelles, secreted into the extracellular medium, or both. We have found that, in mouse peritoneal macrophages, J774 cells, PC12 cells, and N2A cells, Fura-2 sequestration and secretion are mediated by organic anion transport systems and are blocked by the inhibitors probenecid and sulfinpyrazone. Under appropriate conditions these agents have little affect on calcium transients, and may facilitate the use of Fura-2 in a variety of cell types.},
	Annote = {Fura2 widely used to measure intracellular ca2+ concentration
        
Possible locations for where Fura-2 goes:
1. AM form diffuses across cytosolic organelle membranes 
2. Fura-2-AM uptake by pinocytosis into endocytic pathway
3. Active transport of acid form by organic anion transporters
        
Summary: 
Fura-2 sequestered as a result of active transport by anion transporters. Probenecid blocks this, allowing cytosolic levels t remain experimentally relevant.
        
Noticed no unexpected effects on cell viability after 3 hr incubation w/ probenecid. 
Did notice that [Ca2+]i was 20\% higher in macrophages incubated with probenecid. 
        
Probenecid is soluble in alkali solution. It is therefore dissolved in a solution of NaOH and the dye loading solution is titrated back to the desired pH, after adding probenecid. },
	Author = {{Di Virgilio}, F and Steinberg, T H and Silverstein, S C},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Di Virgilio, Steinberg, Silverstein - 1990 - Inhibition of Fura-2 sequestration and secretion with organic anion transport blockers..pdf:pdf},
	Issn = {0143-4160},
	Journal = {Cell calcium},
	Keywords = {Animals,Benzofurans,Benzofurans: metabolism,Biological Transport,Calcium,Calcium: metabolism,Cell Line,Cytoplasm,Cytoplasm: metabolism,Fluorescent Dyes,Fluorescent Dyes: metabolism,Fura-2,Macrophages,Macrophages: metabolism,Organelles,Organelles: metabolism,Probenecid,Probenecid: pharmacology,Sulfinpyrazone,Sulfinpyrazone: pharmacology,probenecid},
	Mendeley-Tags = {probenecid},
	Number = {2-3},
	Pages = {57--62},
	Pmid = {2191781},
	Title = {{Inhibition of Fura-2 sequestration and secretion with organic anion transport blockers.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/19501673},
	Volume = {11},
	Year = {1990},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/19501673}}

@article{Prakriya2006,
	Abstract = {Stimulation of immune cells causes depletion of Ca2+ from endoplasmic reticulum (ER) stores, thereby triggering sustained Ca2+ entry through store-operated Ca2+ release-activated Ca2+ (CRAC) channels, an essential signal for lymphocyte activation and proliferation. Recent evidence indicates that activation of CRAC current is initiated by STIM proteins, which sense ER Ca2+ levels through an EF-hand located in the ER lumen and relocalize upon store depletion into puncta closely associated with the plasma membrane. We and others recently identified Drosophila Orai and human Orai1 (also called TMEM142A) as critical components of store-operated Ca2+ entry downstream of STIM. Combined overexpression of Orai and Stim in Drosophila cells, or Orai1 and STIM1 in mammalian cells, leads to a marked increase in CRAC current. However, these experiments did not establish whether Orai is an essential intracellular link between STIM and the CRAC channel, an accessory protein in the plasma membrane, or an actual pore subunit. Here we show that Orai1 is a plasma membrane protein, and that CRAC channel function is sensitive to mutation of two conserved acidic residues in the transmembrane segments. E106D and E190Q substitutions in transmembrane helices 1 and 3, respectively, diminish Ca2+ influx, increase current carried by monovalent cations, and render the channel permeable to Cs+. These changes in ion selectivity provide strong evidence that Orai1 is a pore subunit of the CRAC channel.},
	Author = {Prakriya, Murali and Feske, Stefan and Gwack, Yousang and Srikanth, Sonal and Rao, Anjana and Hogan, Patrick G},
	Institution = {Department of Molecular Pharmacology and Biological Chemistry, Northwestern University, Feinberg School of Medicine, Chicago, Illinois 60611, USA.},
	Journal = {Nature},
	Number = {7108},
	Pages = {230--233},
	Pmid = {16921383},
	Title = {{Orai1 is an essential pore subunit of the CRAC channel.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/16921383},
	Volume = {443},
	Year = {2006},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/16921383}}

@article{Zhang2005,
	Abstract = {As the sole Ca2+ entry mechanism in a variety of non-excitable cells, store-operated calcium (SOC) influx is important in Ca2+ signalling and many other cellular processes. A calcium-release-activated calcium (CRAC) channel in T lymphocytes is the best-characterized SOC influx channel and is essential to the immune response, sustained activity of CRAC channels being required for gene expression and proliferation. The molecular identity and the gating mechanism of SOC and CRAC channels have remained elusive. Previously we identified Stim and the mammalian homologue STIM1 as essential components of CRAC channel activation in Drosophila S2 cells and human T lymphocytes. Here we show that the expression of EF-hand mutants of Stim or STIM1 activates CRAC channels constitutively without changing Ca2+ store content. By immunofluorescence, EM localization and surface biotinylation we show that STIM1 migrates from endoplasmic-reticulum-like sites to the plasma membrane upon depletion of the Ca2+ store. We propose that STIM1 functions as the missing link between Ca2+ store depletion and SOC influx, serving as a Ca2+ sensor that translocates upon store depletion to the plasma membrane to activate CRAC channels.},
	Author = {Zhang, Shenyuan L and Yu, Ying and Roos, Jack and Kozak, J Ashot and Deerinck, Thomas J and Ellisman, Mark H and Stauderman, Kenneth A and Cahalan, Michael D},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Zhang et al. - 2005 - STIM1 is a Ca2 sensor that activates CRAC channels and migrates from the Ca2 store to the plasma membrane..pdf:pdf},
	Institution = {Department of Physiology and Biophysics and Center for Immunology, University of California, Irvine, California 92697, USA.},
	Journal = {Nature},
	Keywords = {STIM1 CRAC subunit interaction image},
	Mendeley-Tags = {STIM1 CRAC subunit interaction image},
	Number = {7060},
	Pages = {902--905},
	Publisher = {Nature Publishing Group},
	Title = {{STIM1 is a Ca2+ sensor that activates CRAC channels and migrates from the Ca2+ store to the plasma membrane.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/16208375},
	Volume = {437},
	Year = {2005},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/16208375}}

@article{Liou2005,
	Abstract = {Ca(2+) signaling in nonexcitable cells is typically initiated by receptor-triggered production of inositol-1,4,5-trisphosphate and the release of Ca(2+) from intracellular stores. An elusive signaling process senses the Ca(2+) store depletion and triggers the opening of plasma membrane Ca(2+) channels. The resulting sustained Ca(2+) signals are required for many physiological responses, such as T cell activation and differentiation. Here, we monitored receptor-triggered Ca(2+) signals in cells transfected with siRNAs against 2,304 human signaling proteins, and we identified two proteins required for Ca(2+)-store-depletion-mediated Ca(2+) influx, STIM1 and STIM2. These proteins have a single transmembrane region with a putative Ca(2+) binding domain in the lumen of the endoplasmic reticulum. Ca(2+) store depletion led to a rapid translocation of STIM1 into puncta that accumulated near the plasma membrane. Introducing a point mutation in the STIM1 Ca(2+) binding domain resulted in prelocalization of the protein in puncta, and this mutant failed to respond to store depletion. Our study suggests that STIM proteins function as Ca(2+) store sensors in the signaling pathway connecting Ca(2+) store depletion to Ca(2+) influx.},
	Author = {Liou, Jen and Kim, Man Lyang and Heo, Won Do and Jones, Joshua T and Myers, Jason W and Ferrell, James E and Meyer, Tobias},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Liou et al. - 2005 - STIM is a Ca2 sensor essential for Ca2-store-depletion-triggered Ca2 influx..pdf:pdf},
	Institution = {Department of Molecular Pharmacology, Stanford University Medical School, California 94305, USA.},
	Journal = {Current Biology},
	Number = {13},
	Pages = {1235--1241},
	Pmid = {16005298},
	Title = {{STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered Ca2+ influx.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/16005298},
	Volume = {15},
	Year = {2005},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/16005298}}

@article{Berridge2000,
	Abstract = {The universality of calcium as an intracellular messenger depends on its enormous versatility. Cells have a calcium signalling toolkit with many components that can be mixed and matched to create a wide range of spatial and temporal signals. This versatility is exploited to control processes as diverse as fertilization, proliferation, development, learning and memory, contraction and secretion, and must be accomplished within the context of calcium being highly toxic. Exceeding its normal spatial and temporal boundaries can result in cell death through both necrosis and apoptosis.},
	Annote = {Is NAADP channel still unknown?
How close is structure to that of ORAI3 stimulator 2-APB?
        
NFAT action summary
        
Prolonged Calcium signal is a requirement of NFAT},
	Author = {Berridge, M J and Lipp, P and Bootman, M D},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Berridge, Lipp, Bootman - 2000 - The versatility and universality of calcium signalling..pdf:pdf},
	Institution = {The Babraham Institute, Laboratory of Molecular Signalling, Babraham Hall, Babraham, Cambridge, CB2 4AT, UK. michael.berridge@bbsrc.ac.uk},
	Journal = {Nature Reviews Molecular Cell Biology},
	Keywords = {2-apb/naadp,IP3 signal,ca review,calcium processes,calcium sensitive processes,calcium signaling},
	Mendeley-Tags = {2-apb/naadp,IP3 signal,ca review,calcium processes,calcium sensitive processes,calcium signaling},
	Number = {1},
	Pages = {11--21},
	Pmid = {11413485},
	Publisher = {Nature Publishing Group},
	Title = {{The versatility and universality of calcium signalling.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/11413485},
	Volume = {1},
	Year = {2000},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/11413485}}

@article{Soboloff2006,
	Abstract = {The coupling mechanism between endoplasmic reticulum (ER) Ca(2+) stores and plasma membrane (PM) store-operated channels (SOCs) remains elusive 1-3. STIM1 was shown to play a crucial role in this coupling process 4-7; however, the role of the closely related STIM2 protein remains undetermined. We reveal that STIM2 is a powerful SOC inhibitor when expressed in HEK293, PC12, A7r5, and Jurkat T cells. This contrasts with gain of SOC function in STIM1-expressing cells. While STIM1 is expressed in both the ER and plasma membrane, STIM2 is expressed only intracellularly. Store depletion induces redistribution of STIM1 into distinct "puncta." STIM2 translocates into puncta upon store depletion only when coexpressed with STIM1. Double labeling shows coincidence of STIM1 and STIM2 within puncta, and immunoprecipitation reveals direct interactions between STIM1 and STIM2. Independent of store depletion, STIM2 colocalizes with and blocks the function of a STIM1 EF-hand mutant that preexists in puncta and is constitutively coupled to activate SOCs. Thus, whereas STIM1 is a required mediator of SOC activation, STIM2 is a powerful inhibitor of this process, interfering with STIM1-mediated SOC activation at a point downstream of puncta formation. The opposing functions of STIM1 and STIM2 suggest they may play a coordinated role in controlling SOC-mediated Ca(2+) entry signals.},
	Author = {Soboloff, Jonathan and Spassova, Maria A and Hewavitharana, Thamara and He, Li-Ping and Xu, Wen and Johnstone, Lorna S and Dziadek, Marie A and Gill, Donald L},
	Institution = {Department of Biochemistry and Molecular Biology, School of Medicine, University of Maryland, Baltimore, 21201, USA. jsobo001@umaryland.edu},
	Journal = {Current Biology},
	Number = {14},
	Pages = {1465--1470},
	Pmid = {16860747},
	Title = {{STIM2 is an inhibitor of STIM1-mediated store-operated Ca2+ Entry.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/16860747},
	Volume = {16},
	Year = {2006},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/16860747}}

@article{Berridge2003,
	Abstract = {Ca2+ is a highly versatile intracellular signal that operates over a wide temporal range to regulate many different cellular processes. An extensive Ca2+-signalling toolkit is used to assemble signalling systems with very different spatial and temporal dynamics. Rapid highly localized Ca2+ spikes regulate fast responses, whereas slower responses are controlled by repetitive global Ca2+ transients or intracellular Ca2+ waves. Ca2+ has a direct role in controlling the expression patterns of its signalling systems that are constantly being remodelled in both health and disease.},
	Annote = {Calcium signaling regulates many different cellular processes; apoptosis, exocytosis, muscle contraction, cell proliferation, and even gene transcription are among these. (1)
        
Gene transcription is among the many processes it regulates; a process which has been shown to get it's Calcium from SOCE (cite crac/orai papers). 
        
Note affinities of channels/ and binding proteins when discussing Ca. Also very important for drugs used to bind Ca2+. +++
        
Go into gene transcription regulation via SOCE Ca (2) 
        
Diff pumping mechanisms affecting Ca2++: PMCA - plasma mem ca-atpase
NCX - Na+/Ca2+ exch
SERCA
MitoC Uniporter (1)        
1. Berridge, M. J., Bootman, M. D., \& Roderick, H. L. (2003). Calcium signalling: dynamics, homeostasis and remodelling. Nat Rev Mol Cell Biol, 4(7), 517-529. doi: 10.1038/nrm1155 nrm1155.
2. Lewis, R. S. (2001). Calcium signaling mechanisms in T lymphocytes. Annual review of immunology, 19(Figure 1), 497-521. doi: 10.1146/annurev.immunol.19.1.497.},
	Author = {Berridge, M J and Bootman, M D and Roderick, H L},
	Doi = {10.1038/nrm1155 nrm1155},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Berridge, Bootman, Roderick - 2003 - Calcium signalling dynamics, homeostasis and remodelling.pdf:pdf},
	Issn = {14710072},
	Journal = {Nature Reviews Molecular Cell Biology},
	Keywords = {*physiology,animals,biological,ca review,calcium,calcium channels,calcium processes,calcium sensitive processes,calcium signaling,homeostasis,humans,metabolism,models,second messenger systems},
	Mendeley-Tags = {ca review,calcium processes,calcium sensitive processes,calcium signaling},
	Number = {7},
	Pages = {517--529},
	Title = {{Calcium signalling: dynamics, homeostasis and remodelling}},
	Url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list\_uids=12838335},
	Volume = {4},
	Year = {2003},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve%5C&db=PubMed%5C&dopt=Citation%5C&list%5C_uids=12838335},
	Bdsk-Url-2 = {http://dx.doi.org/10.1038/nrm1155%20nrm1155}}

@article{Hewavitharana2007,
	Abstract = {Ca(2+) signals are universal among cells in regulating a spectrum of cellular responses. Phospholipase C-coupled receptors activate two components of Ca(2+) signals-rapid Ca(2+) release from ER stores, followed by slower Ca(2+) entry from outside the cell. The coupling process between ER and PM to mediate this "store-operated" Ca(2+) entry process remained until recently a molecular mystery. The recent discovery of the necessity for STIM1 and Orai proteins in this process has provided crucial information on the coupling mechanism between stores and PM Ca(2+) entry. STIM1 is a single spanning membrane protein with an unpaired Ca(2+) binding EF-hand and appears to function as the sensor of ER luminal Ca(2+), and, through redistribution in the ER, transduces information directly to the PM. Orai1 is a tetra-spanning PM protein and functions as the highly Ca(2+)-selective channel in the PM that is gated through interactions with the store-activated ER Ca(2+) sensor. Recent evidence shows the two proteins together are necessary and sufficient for the function of store-operated Ca(2+) entry. However, many questions arise about how and where the interactions of the STIM1 and Orai1 proteins occur within cells. Here we discuss recent information and ideas about the coupling between these proteins that leads to store-operated channel activation.},
	Author = {Hewavitharana, Thamara and Deng, Xiaoxiang and Soboloff, Jonathan and Gill, Donald L},
	Institution = {Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 North Greene Street, Baltimore, MD 21201, United States.},
	Journal = {Cell Calcium},
	Number = {2},
	Pages = {173--182},
	Pmid = {17602740},
	Title = {{Role of STIM and Orai proteins in the store-operated calcium signaling pathway.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/17602740},
	Volume = {42},
	Year = {2007},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/17602740}}

@article{Putney2007,
	Abstract = {Activation of phospholipase C by G-protein-coupled receptors results in release of intracellular Ca(2+) and activation of Ca(2+) channels in the plasma membrane. The intracellular release of Ca(2+) is signaled by the second messenger, inositol 1,4,5-trisphosphate. Ca(2+) entry involves signaling from depleted intracellular stores to plasma membrane Ca(2+) channels, a process referred to as capacitative calcium entry or store-operated calcium entry. The electrophysiological current associated with capacitative calcium entry is the calcium-release-activated calcium current, or I(crac). In the 20 years since the inception of the concept of capacitative calcium entry, a variety of activation mechanisms have been proposed, and there has been considerable interest in the possibility of transient receptor potential channels functioning as store-operated channels. However, in the past 2 years, two major players in both the signaling and permeation mechanisms for store-operated channels have been discovered: Stim1 (and possibly Stim2) and the Orai proteins. Activation of store-operated channels involves an endoplasmic reticulum Ca(2+) sensor called Stim1. Stim1 acts by redistributing within a small component of the endoplasmic reticulum, approaching the plasma membrane, but does not appear to translocate into the plasma membrane. Stim1, either directly or indirectly, signals to plasma membrane Orai proteins which constitute pore-forming subunits of store-operated channels.},
	Author = {Putney, James W},
	Institution = {National Institute of Environmental Health Sciences, NIH, P.O. Box 12233, Research Triangle Park, NC 27709, United States. putney@niehs.nih.gov},
	Journal = {Cell Calcium},
	Number = {2},
	Pages = {103--110},
	Title = {{Recent breakthroughs in the molecular mechanism of capacitative calcium entry (with thoughts on how we got here).}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/17349691},
	Volume = {42},
	Year = {2007},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/17349691}}

@article{Feske2006,
	Abstract = {Antigen stimulation of immune cells triggers Ca2+ entry through Ca2+ release-activated Ca2+ (CRAC) channels, promoting the immune response to pathogens by activating the transcription factor NFAT. We have previously shown that cells from patients with one form of hereditary severe combined immune deficiency (SCID) syndrome are defective in store-operated Ca2+ entry and CRAC channel function. Here we identify the genetic defect in these patients, using a combination of two unbiased genome-wide approaches: a modified linkage analysis with single-nucleotide polymorphism arrays, and a Drosophila RNA interference screen designed to identify regulators of store-operated Ca2+ entry and NFAT nuclear import. Both approaches converged on a novel protein that we call Orai1, which contains four putative transmembrane segments. The SCID patients are homozygous for a single missense mutation in ORAI1, and expression of wild-type Orai1 in SCID T cells restores store-operated Ca2+ influx and the CRAC current (I(CRAC)). We propose that Orai1 is an essential component or regulator of the CRAC channel complex.},
	Annote = {75 uM 2-APB inhibits orai13 uM 2-APB activates orai1},
	Author = {Feske, Stefan and Gwack, Yousang and Prakriya, Murali and Srikanth, Sonal and Puppel, Sven-Holger and Tanasa, Bogdan and Hogan, Patrick G and Lewis, Richard S and Daly, Mark and Rao, Anjana},
	File = {:Users/orville/Desktop/papers/nature04702.pdf:pdf},
	Institution = {The CBR Institute for Biomedical Research, and the Department of Pediatrics, Harvard Medical School, 200 Longwood Avenue, Boston, Massachusetts 02115, USA.},
	Journal = {Nature},
	Keywords = {2-apb activation,2-apb inhibition},
	Mendeley-Tags = {2-apb activation,2-apb inhibition},
	Number = {7090},
	Pages = {179--185},
	Pmid = {16582901},
	Publisher = {Nature Publishing Group},
	Title = {{A mutation in Orai1 causes immune deficiency by abrogating CRAC channel function.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/16582901},
	Volume = {441},
	Year = {2006},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/16582901}}

@article{Li2010,
	Abstract = {The Ca(2+) release-activated Ca(2+) (CRAC) channel pore is formed by Orai1 and gated by STIM1 after intracellular Ca(2+) store depletion. To resolve how many STIM1 molecules are required to open a CRAC channel, we fused different numbers of Orai1 subunits with functional two-tandem cytoplasmic domains of STIM1 (residues 336-485, designated as S domain). Whole-cell patch clamp recordings of these chimeric molecules revealed that CRAC current reached maximum at a stoichiometry of four Orai1 and eight S domains. Further experiments indicate that two-tandem S domains specifically interact with the C-terminus of one Orai1 subunit, and CRAC current can be gradually increased as more Orai1 subunits can interact with S domains or STIM1 proteins. Our data suggest that maximal opening of one CRAC channel requires eight STIM1 molecules, and support a model that the CRAC channel activation is not in an "all-or-none" fashion but undergoes a graded process via binding of different numbers of STIM1.Cell Research advance online publication 14 September 2010; doi:10.1038/cr.2010.131.},
	Author = {Li, Zhengzheng and Liu, Lin and Deng, Yongqiang and Ji, Wei and Du, Wen and Xu, Pingyong and Chen, Liangyi and Xu, Tao},
	Doi = {10.1038/cr.2010.131},
	Issn = {17487838},
	Journal = {Cell Research},
	Keywords = {10,1038,131,2010,calcium store,cell research advance online,cr,crac channel,doi,orai1,publication 14 september 2010,stim1,stoichiometry},
	Pages = {1--11},
	Pmid = {20838418},
	Publisher = {Nature Publishing Group},
	Title = {{Graded activation of CRAC channel by binding of different numbers of STIM1 to Orai1 subunits.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/20838418},
	Year = {2010},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/20838418},
	Bdsk-Url-2 = {http://dx.doi.org/10.1038/cr.2010.131}}

@article{Abdullaev2008,
	Abstract = {Recent breakthroughs in the store-operated calcium (Ca(2+)) entry (SOCE) pathway have identified Stim1 as the endoplasmic reticulum Ca(2+) sensor and Orai1 as the pore forming subunit of the highly Ca(2+)-selective CRAC channel expressed in hematopoietic cells. Previous studies, however, have suggested that endothelial cell (EC) SOCE is mediated by the nonselective canonical transient receptor potential channel (TRPC) family, TRPC1 or TRPC4. Here, we show that passive store depletion by thapsigargin or receptor activation by either thrombin or the vascular endothelial growth factor activates the same pathway in primary ECs with classical SOCE pharmacological features. ECs possess the archetypical Ca(2+) release-activated Ca(2+) current (I(CRAC)), albeit of a very small amplitude. Using a maneuver that amplifies currents in divalent-free bath solutions, we show that EC CRAC has similar characteristics to that recorded from rat basophilic leukemia cells, namely a similar time course of activation, sensitivity to 2-aminoethoxydiphenyl borate, and low concentrations of lanthanides, and large Na(+) currents displaying the typical depotentiation. RNA silencing of either Stim1 or Orai1 essentially abolished SOCE and I(CRAC) in ECs, which were rescued by ectopic expression of either Stim1 or Orai1, respectively. Surprisingly, knockdown of either TRPC1 or TRPC4 proteins had no effect on SOCE and I(CRAC). Ectopic expression of Stim1 in ECs increased their I(CRAC) to a size comparable to that in rat basophilic leukemia cells. Knockdown of Stim1, Stim2, or Orai1 inhibited EC proliferation and caused cell cycle arrest at S and G2/M phase, although Orai1 knockdown was more efficient than that of Stim proteins. These results are first to our knowledge to establish the requirement of Stim1/Orai1 in the endothelial SOCE pathway.},
	Author = {Abdullaev, Iskandar F and Bisaillon, Jonathan M and Potier, Marie and Gonzalez, Jose C and Motiani, Rajender K and Trebak, Mohamed},
	Institution = {Cardiovascular Sciences, MC8, Albany Medical College, 47 New Scotland Avenue, MC-8, Albany, NY 12208, USA.},
	Journal = {Circulation Research},
	Number = {11},
	Pages = {1289--1299},
	Title = {{Stim1 and Orai1 mediate CRAC currents and store-operated calcium entry important for endothelial cell proliferation.}},
	Url = {http://circres.ahajournals.org/cgi/content/full/103/11/1289},
	Volume = {103},
	Year = {2008},
	Bdsk-Url-1 = {http://circres.ahajournals.org/cgi/content/full/103/11/1289}}

@article{Feske2010,
	Abstract = {Store-operated Ca2+ entry (SOCE) is an important Ca2+ influx pathway in many non-excitable and some excitable cells. It is regulated by the filling state of intracellular Ca2+ stores, notably the endoplasmic reticulum (ER). Reduction in Ca2+ER results in activation of plasma membrane Ca2+ channels that mediate sustained Ca2+ influx which is required for many cell functions as well as refilling of Ca2+ stores. The Ca2+ release activated Ca2+ (CRAC) channel is the best characterized SOC channel with well-defined electrophysiological properties. In recent years, the molecular components of the CRAC channel, long mysterious, have been defined. ORAI1 (or CRACM1) acts as the pore-forming subunit of the CRAC channel in the plasma membrane. Stromal interaction molecule (STIM) 1 is localized in the ER, senses Ca2+ER, and activates the CRAC channel upon store depletion by binding to ORAI1. Both proteins are widely expressed in many tissues in both human and mouse consistent with the widespread prevalence of SOCE and CRAC channel currents in many cells types. CRAC channelopathies in human patients with mutations in STIM1 and ORAI1 are characterized by abolished CRAC channel currents, lack of SOCE and-clinically-immunodeficiency, congenital myopathy, and anhydrotic ectodermal dysplasia. This article reviews the role of ORAI and STIM proteins for SOCE and CRAC channel function in a variety of cell types and tissues and compares the phenotypes of ORAI1 and STIM1-deficient human patients and mice with targeted deletion of Orai and Stim genes.},
	Author = {Feske, Stefan},
	Institution = {Department of Pathology, New York University, Langone Medical Center, SRB314, New York, NY 10016, USA. feskes01@nyumc.org},
	Journal = {Pflugers Archiv European journal of physiology},
	Number = {2},
	Pages = {417--435},
	Title = {{CRAC channelopathies.}},
	Url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2885504\&tool=pmcentrez\&rendertype=abstract},
	Volume = {460},
	Year = {2010},
	Bdsk-Url-1 = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2885504%5C&tool=pmcentrez%5C&rendertype=abstract}}

@article{Feske2009,
	Abstract = {Store-operated Ca2+ entry (SOCE) is a mechanism used by many cells types including lymphocytes and other immune cells to increase intracellular Ca2+ concentrations to initiate signal transduction. Activation of immunoreceptors such as the T-cell receptor, B-cell receptor, or Fc receptors results in the release of Ca2+ ions from endoplasmic reticulum (ER) Ca2+ stores and subsequent activation of plasma membrane Ca2+ channels such as the well-characterized Ca2+ release-activated Ca2+ (CRAC) channel. Two genes have been identified that are essential for SOCE: ORAI1 as the pore-forming subunit of the CRAC channel in the plasma membrane and stromal interaction molecule-1 (STIM1) sensing the ER Ca2+ concentration and activating ORAI1-CRAC channels. Intense efforts in the past several years have focused on understanding the molecular mechanism of SOCE and the role it plays for cell functions in vitro and in vivo. A number of transgenic mouse models have been generated to investigate the role of ORAI1 and STIM1 in immunity. In addition, mutations in ORAI1 and STIM1 identified in immunodeficient patients provide valuable insight into the role of both genes and SOCE. This review focuses on the role of ORAI1 and STIM1 in vivo, discussing the phenotypes of ORAI1- and STIM1-deficient human patients and mice.},
	Author = {Feske, Stefan},
	Institution = {Department of Pathology, New York University School of Medicine, New York, NY 10016, USA. feskes01@nyumc.org},
	Journal = {Immunological Reviews},
	Number = {1},
	Pages = {189--209},
	Pmid = {19754898},
	Title = {{ORAI1 and STIM1 deficiency in human and mice: roles of store-operated Ca2+ entry in the immune system and beyond.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/19754898},
	Volume = {231},
	Year = {2009},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/19754898}}

@article{Mignen2008,
	Abstract = {Agonist-activated Ca2+ entry plays a critical role in Ca2+ signalling in non-excitable cells. One mode of such entry is activated as a consequence of the depletion of intracellular Ca2+ stores. This depletion is sensed by the protein STIM1 in the endoplasmic reticulum, which then translocates to regions close to the plasma membrane where it induces the activation of store-operated conductances. The most thoroughly studied of these conductances are the Ca2+ release-activated Ca2+ (CRAC) channels, and recent studies have identified the protein Orai1 as comprising the essential pore-forming subunit of these channels. Although evidence suggests that Orai1 can assemble as homomultimers, whether this assembly is necessary for the formation of functional CRAC channels and, if so, their relevant stoichiometry is unknown. To examine this, we have used an approach involving the expression of preassembled tandem Orai1 multimers comprising different numbers of subunits into cells stably overexpressing STIM1, followed by the recording of maximally activated CRAC channel currents. In each case, any necessity for recruitment of additional Orai1 units to these preassembled multimers in order to form functional channels was evaluated by coexpression with a dominant-negative Orai1 mutant. In this way we were able to demonstrate, for the first time, that the functional CRAC channel pore is formed by a tetrameric assembly of Orai1 subunits.},
	Author = {Mignen, Olivier and Thompson, Jill L and Shuttleworth, Trevor J},
	Institution = {Department of Pharmacology and Physiology, University of Rochester Medical Center, Rochester, NY 14642, USA.},
	Journal = {The Journal of Physiology},
	Number = {2},
	Pages = {419--425},
	Publisher = {The Rockefeller University Press},
	Title = {{Orai1 subunit stoichiometry of the mammalian CRAC channel pore.}},
	Url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2229396\&tool=pmcentrez\&rendertype=abstract},
	Volume = {586},
	Year = {2008},
	Bdsk-Url-1 = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2229396%5C&tool=pmcentrez%5C&rendertype=abstract}}

@article{Eid2008,
	Abstract = {BACKGROUND: Mammalian STIM1 and STIM2 and the single Drosophila homologue dSTIM have been identified as key regulators of store-operated Ca2+ entry in cells. STIM proteins function both as molecular sensors of Ca2+concentration in the endoplasmic reticulum (ER) and the molecular triggers that activate SOC channels in the plasma membrane. Ca2+ is a crucial intracellular messenger utilised in many cellular processes, and regulators of Ca2+ homeostasis in the ER and cytosol are likely to play important roles in developmental processes. STIM protein expression is altered in several tumour types but the role of these proteins in developmental signalling pathways has not been thoroughly examined. RESULTS: We have investigated the expression and developmental function of dSTIM in Drosophila and shown that dSTIM is widely expressed in embryonic and larval tissues. Using the UAS-Gal4 induction system, we have expressed full-length dSTIM protein and a dsRNAi construct in different tissues. We demonstrate an essential role for dSTIM in larval development and survival, and a tissue-specific role in specification of mechanosensory bristles in the notum and specification of wing vein thickness. CONCLUSION: Our studies show that dSTIM regulates growth and patterning of imaginal discs and indicate potential interactions with the Notch and Wingless signaling pathways. These interactions may be relevant to studies implicating STIM family proteins in tumorigenesis.},
	Author = {Eid, Jean-Pierre and Arias, Alfonso Martinez and Robertson, Hannah and Hime, Gary R and Dziadek, Marie},
	Doi = {10.1186/1471-213X-8-104},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Eid et al. - 2008 - The Drosophila STIM1 orthologue, dSTIM, has roles in cell fate specification and tissue patterning..pdf:pdf},
	Issn = {1471-213X},
	Journal = {BMC developmental biology},
	Keywords = {Animals,Animals, Genetically Modified,Body Patterning,Body Patterning: genetics,Calcium,Calcium: metabolism,Cell Differentiation,Drosophila,Drosophila Proteins,Drosophila Proteins: genetics,Drosophila Proteins: metabolism,Drosophila Proteins: physiology,Drosophila: embryology,Drosophila: genetics,Drosophila: growth \& development,Embryo, Nonmammalian,Embryo, Nonmammalian: metabolism,Endoplasmic Reticulum,Endoplasmic Reticulum: metabolism,In Situ Hybridization, Fluorescence,Membrane Proteins,Membrane Proteins: genetics,Membrane Proteins: metabolism,Membrane Proteins: physiology,RNA Interference,Receptors, Notch,Receptors, Notch: genetics,Receptors, Notch: metabolism,Signal Transduction,Wnt1 Protein,Wnt1 Protein: genetics,Wnt1 Protein: metabolism},
	Month = jan,
	Number = {1},
	Pages = {104},
	Pmid = {18950512},
	Title = {{The Drosophila STIM1 orthologue, dSTIM, has roles in cell fate specification and tissue patterning.}},
	Url = {http://www.biomedcentral.com/1471-213X/8/104},
	Volume = {8},
	Year = {2008},
	Bdsk-Url-1 = {http://www.biomedcentral.com/1471-213X/8/104},
	Bdsk-Url-2 = {http://dx.doi.org/10.1186/1471-213X-8-104}}

@article{Lewis2001,
	Abstract = {Elevation of intracellular free Ca(2+) is one of the key triggering signals for T-cell activation by antigen. A remarkable variety of Ca(2+) signals in T cells, ranging from infrequent spikes to sustained oscillations and plateaus, derives from the interactions of multiple Ca(2+) sources and sinks in the cell. Following engagement of the T cell receptor, intracellular channels (IP3 and ryanodine receptors) release Ca(2+) from intracellular stores, and by depleting the stores trigger prolonged Ca(2+) influx through store-operated Ca(2+) (CRAC) channels in the plasma membrane. The amplitude and dynamics of the Ca(2+) signal are shaped by several mechanisms, including K(+) channels and membrane potential, slow modulation of the plasma membrane Ca(2+)-ATPase, and mitochondria that buffer Ca(2+) and prevent the inactivation of CRAC channels. Ca(2+) signals have a number of downstream targets occurring on multiple time scales. At short times, Ca(2+) signals help to stabilize contacts between T cells and antigen-presenting cells through changes in motility and cytoskeletal reorganization. Over periods of minutes to hours, the amplitude, duration, and kinetic signature of Ca(2+) signals increase the efficiency and specificity of gene activation events. The complexity of Ca(2+) signals contains a wealth of information that may help to instruct lymphocytes to choose between alternate fates in response to antigenic stimulation.},
	Annote = {SOCE and T-cells
        
ionomycin, a lipophilic ionophore that transports Ca2+ out of the ER;
        
Stopped at page 510},
	Author = {Lewis, R S},
	Doi = {10.1146/annurev.immunol.19.1.497},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Lewis - 2001 - Calcium signaling mechanisms in T lymphocytes..pdf:pdf},
	Issn = {0732-0582},
	Journal = {Annual review of immunology},
	Keywords = {4,5-Trisphosphate Receptors,Animals,Antigen,Antigen Presentation,Calcineurin,Calcineurin: physiology,Calcium,Calcium Channels,Calcium Channels: metabolism,Calcium Channels: physiology,Calcium Signaling,Calcium Signaling: physiology,Calcium-Transporting ATPases,Calcium-Transporting ATPases: physiology,Calcium: metabolism,Cell Compartmentation,Cytoplasmic and Nuclear,Cytoplasmic and Nuclear: physiology,DNA-Binding Proteins,DNA-Binding Proteins: physiology,Endoplasmic Reticulum,Endoplasmic Reticulum: metabolism,Gene Expression Regulation,Gene Expression Regulation: physiology,Humans,Inositol 1,Ion Transport,Jurkat Cells,Membrane Potentials,Mitochondria,Mitochondria: physiology,NFATC Transcription Factors,Nuclear Proteins,Patch-Clamp Techniques,Receptors,T-Cell,T-Cell: immunology,T-Lymphocytes,T-Lymphocytes: physiology,Transcription Factors,Transcription Factors: physiology,Transcriptional Activation,ca review,calcium processes,calcium sensitive processes,calcium signaling},
	Mendeley-Tags = {ca review,calcium processes,calcium sensitive processes,calcium signaling},
	Month = jan,
	Number = {Figure 1},
	Pages = {497--521},
	Pmid = {11244045},
	Title = {{Calcium signaling mechanisms in T lymphocytes.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/11244045},
	Volume = {19},
	Year = {2001},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/11244045},
	Bdsk-Url-2 = {http://dx.doi.org/10.1146/annurev.immunol.19.1.497}}

@article{Gwack2007,
	Annote = {Store operated Ca2+ channels in lymphocytes are responsible for /em/ sustained Ca2+ coming in from the outside the cell. This sustained Ca2+ influx is necessary for gene transcription driven by the NFAT transcription factor. 
        
NFAT (nuclear factor of activated transcription) is activated when an immune response is necessary, and drives the transcription of proteins necessary for raising an immune response. 
        
The importance of Ca2+ to this process is a result of NFAT's dependence on calcineurin for activation. The Ca2+ release triggered by SOCE results in Ca2+ and calmodulin binding to calcineurin activating it. Activated calcineurin then dephosphorylates NFAT, allowing it to get into the nucleus. Once in the nucleus NFAT is able to bind to the promoter region of cytokines and other immune response/proliferation genes enabling their transcription.  In effect triggering the immune system response. 
        
STIM1 and STIM2 are transmembrane proteins (20.). They are ER localized proteins, until emptying the ER Ca2+ store causes translocation into, or close to, the plasma membrane (20.).
        
Notice that for NFAT activation to occur, the Ca2+ influx which occurs needs to be sustained. In experiments, overexpression of ORAI1 allows Ca2+ influx on the order of minutes. Ca2+ influx on the order of hours is necessary for gene transcription however. 
        
This is why studying ORAI3 is important. In this study we will seek to determine some properties of ORAI3. 
In the mammalian system, a drug named 2-APB will, at low concentrations activate ORAI1 but at higher concentrations inactivate it. At any concentration in the mammalian system however, it will actiate ORAI3. 
        
The Orai family of proteins displays a wide expression profile, including T-cells and Kidney (20). In HEK293 cells, knock down Orai1 via siRNA reduced SOCE (20). Similar knock down experiments using Orai2 or Orai3 did not significantly affect SOCE (20). These HEK experiments are suggestive of Orai1's importance in initiating SOCE. As long as Orai1 is around, then SOCE takes place normally. It also suggests that ORAI2 and/or Orai3 can partially substitute in Orai1's absence since SOCE was reduced, but completely stopped. 
Also suggestive of this, is an experiment by Gwack et al (20.) showing that siRNA kncokdown of Orai3 in HEK cells results in a 3 fold increase in Orai1 mRNA. Another experiment showed that expressing Orai3 and STIM1 SCID T-cells rescues SOCE, but not as much as when Orai1 and Stim1 are used. In contrast, Orai2 and Stim1 expression did not result in any increase over the basal SCID T-cell levels. If it is mainly Orai3 that is able to substitute for Orai1-mediated initiation of  SOCE, mechanisms may well be in place in the cell to adjust to the absence of Orai3 signal.
        
It suggests the importance of Orai3 to SOCE, not as a main player, but as backup, pinch hitting if you will if Orai1 is not around to do its function.
        
OF NOTE: 
        
Our ORAI1 ALONE transfection in drosophila did not show significant CRAC current 
STIM1 in drosophila did show an increase in Icrac.
ORAI1 and STIM1 in JURKAT cells did show a significant increase in Icrac.
Will ORAI1 and STIM1 in drosophila show this as well?
        
If so it suggests that human stim1 can complement dSTIM for dORAI activation, 
but dSTIM cannot substitute for human STIM1 with human ORAI1.
        
        
      },
	Author = {Gwack, Y. and Srikanth, S. and Feske, S. and Cruz-Guilloty, F. and Oh-hora, M. and Neems, D.S. and Hogan, P.G. and Rao, A.},
	File = {:Users/orville/Dropbox/S2 stuff/J. Biol. Chem.-2007-Gwack-16232-43.pdf:pdf},
	Issn = {0021-9258},
	Journal = {Journal of Biological Chemistry},
	Keywords = {glycosylation,orai glycosylation,stim intro,stim1,stim1 intro,stim2},
	Mendeley-Tags = {glycosylation,orai glycosylation,stim intro,stim1,stim1 intro,stim2},
	Number = {22},
	Pages = {16232},
	Publisher = {ASBMB},
	Title = {{Biochemical and functional characterization of Orai proteins}},
	Url = {http://www.jbc.org/content/282/22/16232.short},
	Volume = {282},
	Year = {2007},
	Bdsk-Url-1 = {http://www.jbc.org/content/282/22/16232.short}}

@article{Navarro-Borelly2008,
	Abstract = {Ca(2+) entry through store-operated Ca(2+) release-activated Ca(2+) (CRAC) channels initiates key functions such as gene expression and exocytosis of inflammatory mediators. Activation of CRAC channels by store depletion involves the redistribution of the ER Ca(2+) sensor, stromal interaction molecule 1 (STIM1), to peripheral sites where it co-clusters with the CRAC channel subunit, Orai1. However, how STIM1 communicates with the CRAC channel and initiates the subsequent events culminating in channel opening is unclear. Here, we show that redistribution of STIM1 and Orai1 occurs in parallel with a pronounced increase in fluorescence resonance energy transfer (FRET) between STIM1 and Orai1, supporting the idea that activation of CRAC channels occurs through physical interactions with STIM1. Co-expression of Orai1-CFP and Orai1-YFP results in a high degree of FRET in resting cells, indicating that Orai1 exists as a multimer. However, store depletion triggers molecular rearrangements in Orai1 resulting in a decline in Orai1-Orai1 FRET. The decline in Orai1-Orai1 FRET is not seen in the absence of STIM1 co-expression and is abolished in Orai1 mutants with impaired STIM1 interaction. Both the STIM1-Orai1 interaction as well as the molecular rearrangements in Orai1 are altered by two powerful modulators of CRAC channel activity: extracellular Ca(2+) and 2-APB. These studies identify a STIM1-dependent conformational change in Orai1 during the activation of CRAC channels and reveal that STIM1-Orai1 interaction and the downstream Orai1 conformational change can be independently modulated to fine-tune CRAC channel activity.},
	Annote = {This paper - 
cloning methods
Intro
        
Lewis RS (2001). Calcium signalingmechanisms in T lymphocytes. Annu Rev Immunol 19, 497--521.
        
PrakriyaM\& Lewis RS (2001). Potentiation and inhibition of Ca2+ release-activated Ca2+ channels by 2-aminoethyldiphenyl borate (2-APB) occurs independently of IP3 receptors. JPhysiol 536, 3--19
        
Parekh AB \& Putney JWJr (2005). Store-operated calcium channels. Physiol Rev 85, 757--810.
        
Zhang SL, Yu Y, Roos J, Kozak JA, Deerinck TJ, EllismanMH, Stauderman KA \& CahalanMD(2005). STIM1 is a Ca2+ sensor that activates CRAC channels andmigrates fromthe Ca2+ store to the plasma membrane. Nature 437, 902-- 905.
        
Prakriya M, Feske S, Gwack Y, Srikanth S, Rao A \&Hogan PG (2006). Orai1 is an essential pore subunit of the CRAC channel. Nature 443, 230--233.
        
Lewis RS (2007). The molecular choreography of a store-operated calcium channel. Nature 446, 284--287.
        
Liou J, KimML, HeoWD, Jones JT,Myers JW, Ferrell JE Jr \& Meyer T (2005). STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered Ca2+ influx. Curr Biol 15, 1235--1241.
        
Luik RM,Wang B, Prakriya M,WuMM\& Lewis RS (2008). Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation. Nature 454, 538--542.
        
      },
	Author = {Navarro-Borelly, Laura and Somasundaram, Agila and Yamashita, Megumi and Ren, Dongjun and Miller, Richard J and Prakriya, Murali},
	Doi = {10.1113/jphysiol.2008.162503},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Navarro-Borelly et al. - 2008 - STIM1-Orai1 interactions and Orai1 conformational changes revealed by live-cell FRET microscopy..pdf:pdf},
	Issn = {1469-7793},
	Journal = {The Journal of physiology},
	Keywords = {Bacterial Proteins,Bacterial Proteins: chemistry,Bacterial Proteins: genetics,Bacterial Proteins: metabolism,Calcium Channels,Calcium Channels: chemistry,Calcium Channels: genetics,Calcium Channels: metabolism,Calcium Signaling,Cell Line,Endoplasmic Reticulum,Endoplasmic Reticulum: metabolism,Fluorescence Resonance Energy Transfer,Green Fluorescent Proteins,Green Fluorescent Proteins: chemistry,Green Fluorescent Proteins: genetics,Green Fluorescent Proteins: metabolism,Humans,Ion Channel Gating,Luminescent Proteins,Luminescent Proteins: chemistry,Luminescent Proteins: genetics,Luminescent Proteins: metabolism,Membrane Proteins,Membrane Proteins: chemistry,Membrane Proteins: genetics,Membrane Proteins: metabolism,Multiprotein Complexes,Mutagenesis, Site-Directed,Neoplasm Proteins,Neoplasm Proteins: chemistry,Neoplasm Proteins: genetics,Neoplasm Proteins: metabolism,Protein Conformation,Protein Interaction Domains and Motifs,Protein Structure, Quaternary,Protein Subunits,Recombinant Fusion Proteins,Recombinant Fusion Proteins: chemistry,Recombinant Fusion Proteins: genetics,Recombinant Fusion Proteins: metabolism,Severe Combined Immunodeficiency,Severe Combined Immunodeficiency: genetics,Severe Combined Immunodeficiency: metabolism},
	Month = nov,
	Number = {Pt 22},
	Pages = {5383--401},
	Pmid = {18832420},
	Title = {{STIM1-Orai1 interactions and Orai1 conformational changes revealed by live-cell FRET microscopy.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/18832420},
	Volume = {586},
	Year = {2008},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/18832420},
	Bdsk-Url-2 = {http://dx.doi.org/10.1113/jphysiol.2008.162503}}

@article{Armknecht2005,
	Author = {Armknecht, S. and Boutros, M. and Kiger, A. and Nybakken, K. and Mathey-Prevot, B. and Perrimon, N.},
	File = {:Users/orville/Dropbox/S2 stuff/RNAiScreensinDrosophila.pdf:pdf},
	Journal = {Methods in enzymology},
	Pages = {55--73},
	Publisher = {Elsevier},
	Title = {{High-throughput RNA interference screens in Drosophila tissue culture cells.}},
	Url = {http://www.sciencedirect.com/science/article/pii/S0076687904920046},
	Volume = {392},
	Year = {2005},
	Bdsk-Url-1 = {http://www.sciencedirect.com/science/article/pii/S0076687904920046}}

@article{Invitrogen,
	Author = {Invitrogen},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Invitrogen - Unknown - RNAi and epigenetics sourcebook.pdf:pdf},
	Issn = {0039-9450},
	Keywords = {DNA Methylation,Epigenesis,Gene Expression Regulation,Gene Silencing,Genetic,Histones,Histones: metabolism,Messenger,Messenger: metabolism,Plant,Plant: genetics,Plant: physiology,Plants,Plants: genetics,RNA,RNA Interference,Small Interfering,Small Interfering: physiology},
	Pmid = {18536343},
	Title = {{[RNAi and epigenetics sourcebook].}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/19188930},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/19188930}}

@article{Mignen2009,
	Abstract = {The activation of Ca(2+) entry is a critical component of agonist-induced cytosolic Ca(2+) signals in non-excitable cells. Although a variety of different channels may be involved in such entry, the recent identification of the STIM and Orai proteins has focused attention on the channels in which these proteins play a key role. To date, two distinct highly Ca(2+)-selective STIM1-regulated and Orai-based channels have been identified - the store-operated CRAC channels and the store-independent arachidonic acid activated ARC channels. In contrast to the CRAC channels, where the channel pore is composed of only Orai1 subunits, both Orai1 and Orai3 subunits are essential components of the ARC channel pore. Using an approach involving the co-expression of a dominant-negative Orai1 monomer along with different preassembled concatenated Orai1 constructs, we recently demonstrated that the functional CRAC channel pore is formed by a homotetrameric assembly of Orai1 subunits. Here, we use a similar approach to demonstrate that the functional ARC channel pore is a heteropentameric assembly of three Orai1 subunits and two Orai3 subunits. Expression of concatenated pentameric constructs with this stoichiometry results in the appearance of large currents that display all the key biophysical and pharmacological features of the endogenous ARC channels. They also replicate the essential regulatory characteristics of native ARC channels including specific activation by low concentrations of arachidonic acid, complete independence of store depletion, and an absolute requirement for the pool of STIM1 that constitutively resides in the plasma membrane.},
	Author = {Mignen, Olivier and Thompson, Jill L and Shuttleworth, Trevor J},
	Doi = {10.1113/jphysiol.2009.174193},
	Issn = {1469-7793},
	Journal = {The Journal of physiology},
	Keywords = {Arachidonic Acid,Arachidonic Acid: metabolism,Calcium,Calcium Channels,Calcium Channels: chemistry,Calcium Channels: metabolism,Calcium: metabolism,Cell Line,Dimerization,Humans,Ion Channel Gating,Ion Channel Gating: physiology,Kidney,Kidney: chemistry,Kidney: metabolism,Membrane Potentials,Membrane Potentials: physiology,Protein Subunits,Structure-Activity Relationship},
	Month = sep,
	Number = {Pt 17},
	Pages = {4181--97},
	Pmid = {19622606},
	Title = {{The molecular architecture of the arachidonate-regulated Ca2+-selective ARC channel is a pentameric assembly of Orai1 and Orai3 subunits.}},
	Url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2754359\&tool=pmcentrez\&rendertype=abstract},
	Volume = {587},
	Year = {2009},
	Bdsk-Url-1 = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2754359%5C&tool=pmcentrez%5C&rendertype=abstract},
	Bdsk-Url-2 = {http://dx.doi.org/10.1113/jphysiol.2009.174193}}

@article{Chien2006,
	Abstract = {Mutations in human bestrophin-1 (VMD2) are genetically linked to several forms of retinal degeneration but the underlying mechanisms are unknown. Bestrophin-1 (hBest1) has been proposed to be a Cl(-) channel involved in ion and fluid transport by the retinal pigment epithelium (RPE). To date, however, bestrophin currents have only been described in overexpression systems and not in any native cells. To test whether bestrophins function as Ca(2+)-activated Cl(-) (CaC) channels physiologically, we used interfering RNA (RNAi) in the Drosophila S2 cell line. S2 cells express four bestrophins (dbest1-4) and have an endogenous CaC current. The CaC current is abolished by several RNAi constructs to dbest1 and dbest2, but not dbest3 or dbest4. The endogenous CaC current was mimicked by expression of dbest1 in HEK cells, and the rectification and relative permeability of the current were altered by replacing F81 with cysteine. Single channel analysis of the S2 bestrophin currents revealed an approximately 2-pS single channel with fast gating kinetics and linear current-voltage relationship. A similar channel was observed in CHO cells transfected with dbest1, but no such channel was seen in S2 cells treated with RNAi to dbest1. This provides definitive evidence that bestrophins are components of native CaC channels at the plasma membrane.},
	Annote = {RNAi paper
Methods},
	Author = {Chien, Li-Ting and Zhang, Zhi-Ren and Hartzell, H Criss},
	Doi = {10.1085/jgp.200609581},
	Issn = {0022-1295},
	Journal = {The Journal of general physiology},
	Keywords = {Animals,CHO Cells,Calcium,Calcium Signaling,Calcium: metabolism,Cells, Cultured,Chloride Channels,Chloride Channels: genetics,Chloride Channels: metabolism,Cricetinae,Drosophila,Drosophila Proteins,Drosophila Proteins: genetics,Drosophila Proteins: metabolism,Drosophila: genetics,Drosophila: physiology,Eye Proteins,Eye Proteins: genetics,Eye Proteins: metabolism,Gene Expression Regulation,Humans,Mutagenesis,Patch-Clamp Techniques,RNA Interference,Transfection},
	Month = sep,
	Number = {3},
	Pages = {247--59},
	Pmid = {16940553},
	Title = {{Single Cl- channels activated by Ca2+ in Drosophila S2 cells are mediated by bestrophins.}},
	Url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2151570\&tool=pmcentrez\&rendertype=abstract},
	Volume = {128},
	Year = {2006},
	Bdsk-Url-1 = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2151570%5C&tool=pmcentrez%5C&rendertype=abstract},
	Bdsk-Url-2 = {http://dx.doi.org/10.1085/jgp.200609581}}

@article{Pfeifer1998,
	Abstract = {Stable transformed insect cell lines have been used for producing many highly processed heterologous proteins. Current research has focused on development of new expression and selection systems, and enhancement of vector stability. Defining the variation of modification and processing capabilities between cell lines will further enhance complex protein production from insect cells.},
	Author = {Pfeifer, T a},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Pfeifer - 1998 - Expression of heterologous proteins in stable insect cell culture..pdf:pdf},
	Issn = {0958-1669},
	Journal = {Current opinion in biotechnology},
	Keywords = {Animals,Biotechnology,Cell Line, Transformed,Gene Expression,Genetic Vectors,Insects,Nucleopolyhedrovirus,Nucleopolyhedrovirus: genetics,Protein Processing, Post-Translational,Recombinant Proteins,Recombinant Proteins: genetics},
	Month = oct,
	Number = {5},
	Pages = {518--21},
	Pmid = {9821282},
	Title = {{Expression of heterologous proteins in stable insect cell culture.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/9821282},
	Volume = {9},
	Year = {1998},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/9821282}}

@article{Tolias1999,
	Abstract = {In eukaryotic cells, phosphatidylinositol can be phosphorylated on the inositol ring by a series of kinases to produce at least seven distinct phosphoinositides. These lipids have been implicated in a variety of cellular processes, including calcium regulation, actin rearrangement, vesicle trafficking, cell survival and mitogenesis. The phosphorylated lipids can act as precursors of second messengers or act directly to recruit specific signaling proteins to the membrane. A number of the kinases responsible for producing these lipids have been purified and their cDNA clones have been isolated. The most well characterized of these enzymes are the phosphoinositide 3-kinases. However, progress has also been made in the characterization of phosphatidylinositol 4-kinases and phosphatidylinositol-4-phosphate 5-kinases. In addition, new pathways involving phosphatidylinositol-5-phosphate 4-kinases, phosphatidylinositol-3-phosphate 5-kinases and phosphatidylinositol-3-phosphate 4-kinases have recently been described. The various enzymes and pathways involved in the synthesis of cellular phosphoinositides will be discussed.},
	Author = {Tolias, K F and Cantley, L C},
	File = {:Users/orville/Dropbox/Papers/1999/Tolias/Chemistry and physics of lipids 1999 Tolias.pdf:pdf},
	Issn = {0009-3084},
	Journal = {Chemistry and physics of lipids},
	Keywords = {Animals,Calcium,Calcium: metabolism,Chemical,Humans,Models,Phosphatidylinositols,Phosphatidylinositols: biosynthesis,Phosphatidylinositols: metabolism,Phosphorylation,Phosphotransferases,Phosphotransferases: metabolism,Saccharomyces cerevisiae,Saccharomyces cerevisiae: physiology,Signal Transduction},
	Month = apr,
	Number = {1-2},
	Pages = {69--77},
	Pmid = {10358929},
	Title = {{Pathways for phosphoinositide synthesis.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/10358929},
	Volume = {98},
	Year = {1999},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/10358929}}

@article{Millar1994,
	Abstract = {A cloned Drosophila gamma-aminobutyric acid GABA receptor subunit (Rdl) has been stably expressed as a functional homo-oligomeric ion channel in a Drosophila cell line. Stably-transfected clonal cell lines which expressed high levels of GABA receptor were identified by specific [3H]-muscimol binding. Expression of functional GABA-gated ion channels in these cell lines was demonstrated by electrophysiological recording. Rapid and pronounced rundown of responses to GABA during whole-cell patch clamp recordings was overcome by the inclusion of EGTA in the pipette solution, indicating a possible role for calcium-dependent processes in the functional regulation of this GABA receptor. Relative agonist potencies of the expressed receptor were found to be in the order GABA = TACA > CACA. We have observed a reversible block of the receptor by the convulsant antagonists, picrotoxinin and EBOB, and by the insecticide fipronil. Potentiation of GABA responses was seen with the anaesthetic steroid 5 alpha-pregnan-3 alpha-ol-20-one. No significant effects (either agonist, antagonist or modulatory) were observed with bicuculline (a vertebrate GABAAR antagonist), benzodiazepines or barbiturates (vertebrate GABAAR modulators), or with glycine agonist of the closely related vertebrate glycine receptors). The suitability of this Drosophila stable expression system for the characterization of receptors and ion channels is discussed.},
	Author = {Millar, N S and Buckingham, S D and Sattelle, D B},
	Doi = {10.1098/rspb.1994.0178},
	Issn = {0962-8452},
	Journal = {Proceedings. Biological sciences / The Royal Society},
	Keywords = {Animals,Cell Line,Drosophila,Drosophila: metabolism,Ion Channels,Ion Channels: antagonists \& inhibitors,Ion Channels: biosynthesis,Patch-Clamp Techniques,Receptors, GABA,Receptors, GABA: biosynthesis},
	Month = dec,
	Number = {1353},
	Pages = {307--14},
	Pmid = {7533909},
	Title = {{Stable expression of a functional homo-oligomeric Drosophila GABA receptor in a Drosophila cell line.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/7533909},
	Volume = {258},
	Year = {1994},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/7533909},
	Bdsk-Url-2 = {http://dx.doi.org/10.1098/rspb.1994.0178}}

@article{Byerly1988,
	Abstract = {Drosophila offers a unique opportunity to determine how the genome codes for ionic channels in an organized nervous system. Considerable progress has already been made in studying the molecular biology of Drosophila K channels. In order for similar progress to be made on neuronal voltage-dependent Ca channels, a physiological preparation is needed in which the function of these channels can be directly studied. The patch-clamp studies reported here show that cultures of embryonic Drosophila cells (Seecof and Unanue, 1968) meet this need. These cultures provide the first opportunity to study with voltage-clamp techniques the Ca and Na currents of Drosophila neurons. The focus of these studies is on the Ca current; however, descriptions of the K and Na currents are also given since they help to characterize the cells studied and the quality of the voltage clamp. The voltage-dependent K, Na, and Ca currents of Drosophila neurons are very similar to those of molluscan neurons and other better studied neurons. The K currents are the largest currents in these neurons, averaging over 300 pA at +20 mV. There are 2 classes of Ca-independent K currents, inactivating currents that are 4-AP sensitive, and noninactivating currents that are insensitive to 4-AP. A large fraction of the K currents are located in the somal membrane. The Na currents are TTX sensitive and probably located in the processes. The peak amplitudes of the Ca currents vary from 0 to over 100 pA in these neurons, averaging 40 pA. With 5 mM external Ca2+ or Ba2+, the Ba currents are about twice as large as the Ca currents. Although 100 microM Cd2+ completely blocks the Ca current, organic blockers have very little effect. Variable inactivation characteristics and sensitivity to washout suggest the possibility of multiple types of Ca channels. A search for single-channel Ba currents in the somal membrane was unsuccessful.},
	Annote = {Interesting, but not useful
        
States that 4-AP is good for blocking inactivation K+ currents},
	Author = {Byerly, L and Leung, H T},
	Issn = {0270-6474},
	Journal = {The Journal of neuroscience : the official journal of the Society for Neuroscience},
	Keywords = {Animals,Calcium Channels,Calcium Channels: physiology,Cells, Cultured,Drosophila melanogaster,Electrophysiology,Ion Channels,Ion Channels: physiology,Larva,Neurons,Neurons: physiology,Potassium Channels,Potassium Channels: physiology,Sodium Channels,Sodium Channels: physiology},
	Month = nov,
	Number = {11},
	Pages = {4379--93},
	Pmid = {2460598},
	Title = {{Ionic currents of Drosophila neurons in embryonic cultures.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/2460598},
	Volume = {8},
	Year = {1988},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/2460598}}

@article{Makridou2003,
	Abstract = {Here we report the generation of stable, selectable Drosophila S2 cell lines using the UAS-GAL4 system. Cloning of the hygromycin resistance gene into the pUAST vector and cotransfection with other pUAST constructs in S2 cells results in coexpression of up to four different proteins under hygromycin selection. Protein expression is driven by the ubiquitous Actin5C-GAL4 driver and cell cultures are maintained in hygromycin-supplemented, serum-free media to ensure constitutive protein production. Visual comparison of cells cotransfected with GFP and RFP demonstrates a uniform cell population expressing both markers simultaneously, while Western blot analysis shows concurrent expression of MYC3-tagged proteins. In addition, fluorescent cell sorting (FACS) analysis shows that 80\% of the total cell population express the GFP marker. Our data indicate that using this technique it is possible to establish stable, selectable cell lines that provide a pool of readily accessible protein. This facilitates protein-based studies and abolishes the need to carry out time-consuming and expensive transfections.},
	Annote = {S2 methods},
	Author = {Makridou, Panagiota and Burnett, Camilla and Landy, Tim and Howard, Ken},
	Doi = {10.1002/gene.10196},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Makridou et al. - 2003 - Hygromycin B-selected cell lines from GAL4-regulated pUAST constructs..pdf:pdf},
	Issn = {1526-954X},
	Journal = {Genesis (New York, N.Y. : 2000)},
	Keywords = {Animals,Blotting,Cell Line,Cloning,Culture Media,Drosophila,Green Fluorescent Proteins,Hygromycin B,Hygromycin B: pharmacology,Luminescent Proteins,Luminescent Proteins: genetics,Molecular,Serum-Free,Transcription Factors,Transcription Factors: genetics,Western,effectene,hygb,hygromycin b,methods,selection,stable},
	Mendeley-Tags = {effectene,hygb,hygromycin b,methods,selection,stable},
	Month = jun,
	Number = {2},
	Pages = {83--7},
	Pmid = {12820169},
	Title = {{Hygromycin B-selected cell lines from GAL4-regulated pUAST constructs.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/12820169},
	Volume = {36},
	Year = {2003},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/12820169},
	Bdsk-Url-2 = {http://dx.doi.org/10.1002/gene.10196}}

@article{Lee1988,
	Abstract = {We isolated and characterized two related ubiquitin genes from Drosophila melanogaster, polyubiquitin and UB3-D. The polyubiquitin gene contained 18 repeats of the 228-base-pair monomeric ubiquitin-encoding unit arranged in tandem. This gene was localized to a minor heat shock puff site, 63F, and it encoded a constitutively expressed 4.4-kilobase polyubiquitin-encoding mRNA, whose level was induced threefold by heat shock. To investigate the pattern of expression of the polyubiquitin gene in developing animals, a polyubiquitin-lacZ fusion gene was introduced into the Drosophila genome by germ line transformation. The fusion gene was expressed at high levels in a tissue-general manner at all life stages assayed. The ubiquitin-encoding gene, UB3-D, consisted of one ubiquitin-encoding unit directly fused, in frame, to a nonhomologous tail sequence. The amino acid sequence of the tail portion of the protein had 65\% positional identity with that of yeast UBI3 protein, including a region that contained a potential nucleic acid-binding motif. The Drosophila UB3-D gene hybridized to a 0.9-kilobase mRNA that was constitutively expressed, and in contrast to the polyubiquitin gene, it was not inducible by heat shock.},
	Author = {Lee, H S and Simon, J a and Lis, J T},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Lee, Simon, Lis - 1988 - Structure and expression of ubiquitin genes of Drosophila melanogaster..pdf:pdf},
	Issn = {0270-7306},
	Journal = {Molecular and cellular biology},
	Keywords = {Amino Acid Sequence,Animals,Base Sequence,Cloning, Molecular,DNA,DNA: genetics,Drosophila melanogaster,Drosophila melanogaster: genetics,Drosophila melanogaster: metabolism,Gene Expression Regulation,Molecular Sequence Data,RNA,RNA: genetics,Repetitive Sequences, Nucleic Acid,Tissue Distribution,Ubiquitins,Ubiquitins: genetics,Ubiquitins: metabolism},
	Month = nov,
	Number = {11},
	Pages = {4727--35},
	Pmid = {2463465},
	Title = {{Structure and expression of ubiquitin genes of Drosophila melanogaster.}},
	Url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=365564\&tool=pmcentrez\&rendertype=abstract},
	Volume = {8},
	Year = {1988},
	Bdsk-Url-1 = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=365564%5C&tool=pmcentrez%5C&rendertype=abstract}}

@article{Johansen1989,
	Annote = {CuSO4 better than CdCl2 for induction due to ability to produce a more "graduated" response
        
Paper contains Induction Params for  metallothionein
        
hygromycin b protocol
        
      },
	Author = {Johansen, H and van der Straten, A and Sweet, R and Otto, E and Maroni, G and Rosenberg, M},
	Doi = {10.1101/gad.3.6.882},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Johansen et al. - 1989 - Regulated expression at high copy number allows production of a growth-inhibitory oncogene product in Drosophila Schneider cells..pdf:pdf},
	Issn = {0890-9369},
	Journal = {Genes \& Development},
	Keywords = {1989,7,although,are low-molecular-weight,cys-,gene regulation,heavy metals,high copy number,hyg b,hygb,hygromycin b,induction,insect cell,metallothioneins,mts,oncogene,received january 26,revised version accepted april,teine-rich proteins that bind,vector map diagram},
	Mendeley-Tags = {hyg b,hygb,hygromycin b,induction,vector map diagram},
	Month = jun,
	Number = {6},
	Pages = {882--889},
	Title = {{Regulated expression at high copy number allows production of a growth-inhibitory oncogene product in Drosophila Schneider cells.}},
	Url = {http://www.genesdev.org/cgi/doi/10.1101/gad.3.6.882},
	Volume = {3},
	Year = {1989},
	Bdsk-Url-1 = {http://www.genesdev.org/cgi/doi/10.1101/gad.3.6.882},
	Bdsk-Url-2 = {http://dx.doi.org/10.1101/gad.3.6.882}}

@article{Vig2006,
	Abstract = {Store-operated Ca2+ entry is mediated by Ca2+ release-activated Ca2+ (CRAC) channels following Ca2+ release from intracellular stores. We performed a genome-wide RNA interference (RNAi) screen in Drosophila cells to identify proteins that inhibit store-operated Ca2+ influx. A secondary patch-clamp screen identified CRACM1 and CRACM2 (CRAC modulators 1 and 2) as modulators of Drosophila CRAC currents. We characterized the human ortholog of CRACM1, a plasma membrane-resident protein encoded by gene FLJ14466. Although overexpression of CRACM1 did not affect CRAC currents, RNAi-mediated knockdown disrupted its activation. CRACM1 could be the CRAC channel itself, a subunit of it, or a component of the CRAC signaling machinery.},
	Author = {Vig, M and Peinelt, C and Beck, a and Koomoa, D L and Rabah, D and Koblan-Huberson, M and Kraft, S and Turner, H and Fleig, a and Penner, R and Kinet, J-P},
	Doi = {10.1126/science.1127883},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Vig et al. - 2006 - CRACM1 is a plasma membrane protein essential for store-operated Ca2 entry..pdf:pdf},
	Issn = {1095-9203},
	Journal = {Science (New York, N.Y.)},
	Keywords = {Animals,Calcium,Calcium Channels,Calcium Channels: metabolism,Calcium: metabolism,Cell Line,Cell Membrane,Cell Membrane: metabolism,Drosophila Proteins,Drosophila Proteins: genetics,Drosophila Proteins: metabolism,Drosophila melanogaster,Drosophila melanogaster: metabolism,Endoplasmic Reticulum,Endoplasmic Reticulum: metabolism,Humans,Ion Transport,Jurkat Cells,Membrane Proteins,Membrane Proteins: genetics,Membrane Proteins: metabolism,Patch-Clamp Techniques,RNA Interference,RNA, Small Interfering,Reverse Transcriptase Polymerase Chain Reaction},
	Month = may,
	Number = {5777},
	Pages = {1220--3},
	Pmid = {16645049},
	Title = {{CRACM1 is a plasma membrane protein essential for store-operated Ca2+ entry.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/16645049},
	Volume = {312},
	Year = {2006},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/16645049},
	Bdsk-Url-2 = {http://dx.doi.org/10.1126/science.1127883}}

@article{Luik2008,
	Abstract = {Ca(2+)-release-activated Ca(2+) (CRAC) channels generate sustained Ca(2+) signals that are essential for a range of cell functions, including antigen-stimulated T lymphocyte activation and proliferation. Recent studies have revealed that the depletion of Ca(2+) from the endoplasmic reticulum (ER) triggers the oligomerization of stromal interaction molecule 1 (STIM1), the ER Ca(2+) sensor, and its redistribution to ER-plasma membrane (ER-PM) junctions where the CRAC channel subunit ORAI1 accumulates in the plasma membrane and CRAC channels open. However, how the loss of ER Ca(2+) sets into motion these coordinated molecular rearrangements remains unclear. Here we define the relationships among Ca(2+)(ER), STIM1 redistribution and CRAC channel activation and identify STIM1 oligomerization as the critical Ca(2+)(ER)-dependent event that drives store-operated Ca(2+) entry. In human Jurkat leukaemic T cells expressing an ER-targeted Ca(2+) indicator, CRAC channel activation and STIM1 redistribution follow the same function of Ca(2+)(ER), reaching half-maximum at approximately 200 microM with a Hill coefficient of approximately 4. Because STIM1 binds only a single Ca(2+) ion, the high apparent cooperativity suggests that STIM1 must first oligomerize to enable its accumulation at ER-PM junctions. To assess directly the causal role of STIM1 oligomerization in store-operated Ca(2+) entry, we replaced the luminal Ca(2+)-sensing domain of STIM1 with the 12-kDa FK506- and rapamycin-binding protein (FKBP12, also known as FKBP1A) or the FKBP-rapamycin binding (FRB) domain of the mammalian target of rapamycin (mTOR, also known as FRAP1). A rapamycin analogue oligomerizes the fusion proteins and causes them to accumulate at ER-PM junctions and activate CRAC channels without depleting Ca(2+) from the ER. Thus, STIM1 oligomerization is the critical transduction event through which Ca(2+) store depletion controls store-operated Ca(2+) entry, acting as a switch that triggers the self-organization and activation of STIM1-ORAI1 clusters at ER-PM junctions.},
	Annote = {
        From Duplicate 1 ( 
        
          Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.
        
         - Luik, Riina M; Wang, Bin; Prakriya, Murali; Wu, Minnie M; Lewis, Richard S )

        
        

        

        

        From Duplicate 2 ( 
        
          Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.
        
         - Luik, Riina M; Wang, Bin; Prakriya, Murali; Wu, Minnie M; Lewis, Richard S )

        
        
linked from STIM1-Orai1 interactions and Orai1 conformational changes revealed by live-cell FRET microscopy.

        

      },
	Author = {Luik, Riina M and Wang, Bin and Prakriya, Murali and Wu, Minnie M and Lewis, Richard S},
	Doi = {10.1038/nature07065},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Luik et al. - 2008 - Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation..pdf:pdf},
	Institution = {Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, California 94305, USA.},
	Issn = {1476-4687},
	Journal = {Nature},
	Keywords = {Calcium,Calcium Channels,Calcium Channels: metabolism,Calcium: metabolism,Cell Membrane,Cell Membrane: metabolism,Endoplasmic Reticulum,Endoplasmic Reticulum: metabolism,Humans,Jurkat Cells,Membrane Proteins,Membrane Proteins: chemistry,Membrane Proteins: genetics,Membrane Proteins: metabolism,Neoplasm Proteins,Neoplasm Proteins: chemistry,Neoplasm Proteins: genetics,Neoplasm Proteins: metabolism},
	Month = jul,
	Number = {7203},
	Pages = {538--542},
	Pmid = {18596693},
	Title = {{Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation.}},
	Url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2712442\&tool=pmcentrez\&rendertype=abstract},
	Volume = {454},
	Year = {2008},
	Bdsk-Url-1 = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2712442%5C&tool=pmcentrez%5C&rendertype=abstract},
	Bdsk-Url-2 = {http://dx.doi.org/10.1038/nature07065}}

@article{Cordova2003a,
	Abstract = {A muscarinic acetylcholine receptor (mAChR), DM1, expressed in the nervous system of Drosophila melanogaster, has been stably expressed in a Drosophila S2 cell line (S2-DM1) and used to investigate spatiotemporal calcium changes following agonist activation. Carbamylcholine (CCh) and oxotremorine are potent agonists, whereas application of the vertebrate M1 mAChR agonist, McN-A-343, results in a weak response. Activation of S2-DM1 receptors using CCh resulted in an increase in intracellular calcium ([Ca(2+)](i)) that was biphasic. Two distinct calcium sources were found to contribute to calcium signaling: (1) internal stores that are sensitive to both thapsigargin and 2-aminoethoxydiphenyl borate and (2) capacitative calcium entry. Spatiotemporal imaging of individual S2-DM1 cells showed that the CCh-induced [Ca(2+)](i) transient resulted from a homogeneous calcium increase throughout the cell, indicative of calcium release from internal stores. In contrast, ionomycin induced the formation of a "calcium ring" at the cell periphery, consistent with external calcium influx.},
	Annote = {Transfection of membrane proteins into drosophila s2 cells.
Spatiotemporal images of [Ca2+]i },
	Author = {Cordova, D and Delpech, V Raymond and Sattelle, D B and Rauh, J J},
	Doi = {10.1007/s10158-003-0024-2},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Cordova et al. - 2003 - Spatiotemporal calcium signaling in a Drosophila melanogaster cell line stably expressing a Drosophila muscarinic acetylcholine receptor..pdf:pdf},
	Issn = {1354-2516},
	Journal = {Invertebrate neuroscience : IN},
	Keywords = {2-APB,Animals,Boron Compounds,Boron Compounds: pharmacology,Calcium,Calcium Signaling,Calcium Signaling: physiology,Calcium: metabolism,Cell Line,Cholinergic Agonists,Cholinergic Agonists: pharmacology,Dose-Response Relationship,Drosophila melanogaster,Drug,Drug Interactions,Enzyme Inhibitors,Enzyme Inhibitors: pharmacology,Extracellular Space,Extracellular Space: drug effects,Extracellular Space: metabolism,Fura-2,Fura-2: metabolism,Ionomycin,Ionomycin: pharmacology,Ionophores,Ionophores: pharmacology,Muscarinic,Muscarinic: drug effects,Muscarinic: metabolism,Receptors,Thapsigargin,Thapsigargin: pharmacology,Time Factors,ca imaging methods,hygb selection,membrane protein,probenecid,s2 cell line,stable expression,stable transfection methods,thapsigargin},
	Mendeley-Tags = {2-APB,ca imaging methods,hygb selection,membrane protein,probenecid,s2 cell line,stable expression,stable transfection methods,thapsigargin},
	Month = nov,
	Number = {1},
	Pages = {19--28},
	Pmid = {12827518},
	Title = {{Spatiotemporal calcium signaling in a Drosophila melanogaster cell line stably expressing a Drosophila muscarinic acetylcholine receptor.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/12827518},
	Volume = {5},
	Year = {2003},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/12827518},
	Bdsk-Url-2 = {http://dx.doi.org/10.1007/s10158-003-0024-2}}

@article{Lansdell2008,
	Abstract = {RIC-3 is a transmembrane protein which enhances maturation (folding and assembly) of neuronal nicotinic acetylcholine receptors (nAChRs). In this study, we report the cloning and characterisation of 11 alternatively spliced isoforms of Drosophila melanogaster RIC-3 (DmRIC-3). Heterologous expression studies of alternatively spliced DmRIC-3 isoforms demonstrate that nAChR chaperone activity does not require a predicted coiled-coil domain which is located entirely within exon 7. In contrast, isoforms containing an additional exon (exon 2), which is located within a proline-rich N-terminal region, have a greatly reduced ability to enhance nAChR maturation. The ability of DmRIC-3 to influence nAChR maturation was examined in co-expression studies with human alpha7 nAChRs and with hybrid nAChRs containing both Drosophila and rat nAChR subunits. When expressed in a Drosophila cell line, several of the DmRIC-3 splice variants enhanced nAChR maturation to a significantly greater extent than observed with human RIC-3. In contrast, when expressed in a human cell line, human RIC-3 enhanced nAChR maturation more efficiently than DmRIC-3. The cloning and characterisation of 11 alternatively spliced DmRIC-3 isoforms has helped to identify domains influencing RIC-3 chaperone activity. In addition, studies conducted in different expression systems suggest that additional host cell factors may modulate the chaperone activity of RIC-3.},
	Author = {Lansdell, Stuart J and Collins, Toby and Yabe, Arisa and Gee, Veronica J and Gibb, Alasdair J and Millar, Neil S},
	Doi = {10.1111/j.1471-4159.2008.05235.x},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Lansdell et al. - 2008 - Host-cell specific effects of the nicotinic acetylcholine receptor chaperone RIC-3 revealed by a comparison of human and Drosophila RIC-3 homologues..pdf:pdf},
	Issn = {1471-4159},
	Journal = {Journal of neurochemistry},
	Keywords = {Animals,Cell Line,Drosophila Proteins,Drosophila Proteins: biosynthesis,Drosophila Proteins: genetics,Drosophila Proteins: physiology,Drosophila melanogaster,Humans,Intracellular Signaling Peptides and Proteins,Intracellular Signaling Peptides and Proteins: gen,Intracellular Signaling Peptides and Proteins: met,Intracellular Signaling Peptides and Proteins: phy,Molecular Chaperones,Molecular Chaperones: biosynthesis,Molecular Chaperones: genetics,Molecular Chaperones: physiology,Protein Isoforms,Protein Isoforms: biosynthesis,Protein Isoforms: genetics,Protein Isoforms: physiology,Rats,Receptors, Nicotinic,Receptors, Nicotinic: biosynthesis,Receptors, Nicotinic: genetics,Receptors, Nicotinic: physiology,Sequence Homology, Amino Acid,Species Specificity},
	Month = jun,
	Number = {5},
	Pages = {1573--81},
	Pmid = {18208544},
	Title = {{Host-cell specific effects of the nicotinic acetylcholine receptor chaperone RIC-3 revealed by a comparison of human and Drosophila RIC-3 homologues.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/18208544},
	Volume = {105},
	Year = {2008},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/18208544},
	Bdsk-Url-2 = {http://dx.doi.org/10.1111/j.1471-4159.2008.05235.x}}

@article{Huang2000,
	Abstract = {Nicotinic acetylcholine receptors (nAChRs) play a major role in excitatory synaptic transmission in insects and are also the target site for chloronicotinyl insecticides such as imidacloprid. Here we report the cloning and characterization of a novel nAChR beta subunit, Mpbeta1, from the aphid Myzus persicae, an economically important pest species. Sequence analysis has identified an open reading frame of 509 amino acids with features typical of nAChR subunits. The Mpbeta1 gene is expressed as a single major transcript of 4.6 kb, considerably larger than the predicted length of the Mpbeta1 open reading frame (1527 bp). By heterologous expression in Drosophila S2 cells, the Mpbeta1 subunit has been shown to co-assemble with the previously cloned nAChR subunits Mpalpha1 and Mpalpha2. In contrast, no co-assembly of Mpbeta1 could be detected with either Mpalpha3 or Mpalpha4. With the aim of gaining a clearer insight into the influence of subunit composition upon assembly, the ability of M. persicae nAChR subunits to co-assemble with vertebrate nAChR subunits has also been examined.},
	Author = {Huang, Y and Williamson, M S and Devonshire, a L and Windass, J D and Lansdell, S J and Millar, N S},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Huang et al. - 2000 - Cloning, heterologous expression and co-assembly of Mpbeta1, a nicotinic acetylcholine receptor subunit from the aphid Myzus persicae..pdf:pdf},
	Issn = {0304-3940},
	Journal = {Neuroscience letters},
	Keywords = {Animals,Aphids,Aphids: genetics,Aphids: metabolism,Cloning, Molecular,Ganglia, Invertebrate,Ganglia, Invertebrate: drug effects,Ganglia, Invertebrate: metabolism,Gene Expression Regulation,Gene Expression Regulation: physiology,Molecular Sequence Data,Nervous System,Nervous System: drug effects,Nervous System: metabolism,Receptors, Nicotinic,Receptors, Nicotinic: biosynthesis,Receptors, Nicotinic: chemistry,Receptors, Nicotinic: genetics,Sequence Homology, Amino Acid},
	Month = apr,
	Number = {1-2},
	Pages = {116--20},
	Pmid = {10771176},
	Title = {{Cloning, heterologous expression and co-assembly of Mpbeta1, a nicotinic acetylcholine receptor subunit from the aphid Myzus persicae.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/10771176},
	Volume = {284},
	Year = {2000},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/10771176}}

@article{Asmild2000,
	Abstract = {We evaluated the suitability of the S2 foetal Drosophila cell line as an expression system for vertebrate anion channel proteins (e.g. cystic fibrosis transmembrane conductance regulator, CFTR) in patch-clamp studies of the endogenous ion channels. In the inside-out configuration (symmetric 150 mM Cl-) we found most frequently an inwardly rectifying Cl- channel with single-channel conductances (gamma) of 57, 45 and 17 pS at -80, 0 and 80 mV, respectively. Reduction of bath [Cl-] to 40 mM caused a shift in reversal potential (Vrev) to -22.5 mV indicating pronounced Cl- selectivity. In the outside-out configuration ([Cl-]pipette = 40 mM, [Cl-]bath = 150 mM) we observed a Cl- channel with a linear unitary current/voltage (i/V) relation for which gamma was 30 pS. The kinetics were quite slow in both configurations. Cl-selectivity was also observed in whole-cell experiments ([Cl-]pipette = 40 mM) in which a Vrev of -43.8 mV, i.e. close to the Cl- equilibrium potential, demonstrated that the membrane current was dominated by Cl-. We conclude that the important features making S2 cells suitable as an expression system for heterologous expressed anion channel proteins are: small total whole-cell currents (less than 100 pA), single-channel and whole-cell currents that, unlike those of CFTR, cannot be described by the Goldman-Hodgkin-Katz regime, and slow kinetics distinctly different from those of CFTR.},
	Author = {Asmild, M and Willumsen, N J},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Asmild, Willumsen - 2000 - Chloride channels in the plasma membrane of a foetal Drosophila cell line, S2..pdf:pdf},
	Issn = {0031-6768},
	Journal = {Pfl\"{u}gers Archiv : European journal of physiology},
	Keywords = {Animals,Cell Line,Cell Membrane,Cell Membrane: metabolism,Chloride Channels,Chloride Channels: metabolism,Chloride Channels: physiology,Drosophila,Drosophila: cytology,Drosophila: embryology,Electric Conductivity,Embryo, Nonmammalian,Embryo, Nonmammalian: metabolism,Embryo, Nonmammalian: physiology,Patch-Clamp Techniques},
	Month = apr,
	Number = {6},
	Pages = {759--64},
	Pmid = {10784350},
	Title = {{Chloride channels in the plasma membrane of a foetal Drosophila cell line, S2.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/10784350},
	Volume = {439},
	Year = {2000},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/10784350}}

@article{Zhang2008a,
	Abstract = {We evaluated currents induced by expression of human homologs of Orai together with STIM1 in human embryonic kidney cells. When co-expressed with STIM1, Orai1 induced a large inwardly rectifying Ca(2+)-selective current with Ca(2+)-induced slow inactivation. A point mutation of Orai1 (E106D) altered the ion selectivity of the induced Ca(2+) release-activated Ca(2+) (CRAC)-like current while retaining an inwardly rectifying I-V characteristic. Expression of the C-terminal portion of STIM1 with Orai1 was sufficient to generate CRAC current without store depletion. 2-APB activated a large relatively nonselective current in STIM1 and Orai3 co-expressing cells. 2-APB also induced Ca(2+) influx in Orai3-expressing cells without store depletion or co-expression of STIM1. The Orai3 current induced by 2-APB exhibited outward rectification and an inward component representing a mixed calcium and monovalent current. A pore mutant of Orai3 inhibited store-operated Ca(2+) entry and did not carry significant current in response to either store depletion or addition of 2-APB. Analysis of a series of Orai1-3 chimeras revealed the structural determinant responsible for 2-APB-induced current within the sequence from the second to third transmembrane segment of Orai3. The Orai3 current induced by 2-APB may reflect a store-independent mode of CRAC channel activation that opens a relatively nonselective cation pore.},
	Annote = {mETHODS write-up 
cloning, RNAi
total rna isolation
rt-pcr
        
ref 34
Fanger, C. M., Rauer, H., Neben, A. L., Miller, M. J., Wulff, H., Rosa, J. C., Ganellin, C. R., Chandy, K. G., and Cahalan, M. D. (2001) J. Biol. Chem. 276, 12249--12256
        
Region of Orai3 responsible for 2-APB action narrowed down to TM3. 
COMPARE to DROSOPHILA ORAI      
Fig 8. Supp S5 + S6 + S7},
	Author = {Zhang, Shenyuan L and Kozak, J Ashot and Jiang, Weihua and Yeromin, Andriy V and Chen, Jing and Yu, Ying and Penna, Aubin and Shen, Wei and Chi, Victor and Cahalan, Michael D},
	Doi = {10.1074/jbc.M801536200},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Zhang et al. - 2008 - Store-dependent and -independent modes regulating Ca2 release-activated Ca2 channel activity of human Orai1 and Orai3..pdf:pdf},
	Issn = {0021-9258},
	Journal = {The Journal of biological chemistry},
	Keywords = {Biological,Boron Compounds,Boron Compounds: pharmacology,Calcium,Calcium Channels,Calcium Channels: metabolism,Calcium: metabolism,Cloning,Dominant,Gene Expression Regulation,Genes,Humans,Membrane Proteins,Membrane Proteins: metabolism,Models,Molecular,Mutation,Neoplasm Proteins,Neoplasm Proteins: metabolism,Patch-Clamp Techniques,Point Mutation,Protein Conformation,Protein Structure,Tertiary},
	Month = jun,
	Number = {25},
	Pages = {17662--71},
	Pmid = {18420579},
	Title = {{Store-dependent and -independent modes regulating Ca2+ release-activated Ca2+ channel activity of human Orai1 and Orai3.}},
	Url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2427323\&tool=pmcentrez\&rendertype=abstract},
	Volume = {283},
	Year = {2008},
	Bdsk-Url-1 = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2427323%5C&tool=pmcentrez%5C&rendertype=abstract},
	Bdsk-Url-2 = {http://dx.doi.org/10.1074/jbc.M801536200}}

@incollection{OConnor2007,
	Annote = {imp't
read until memorized},
	Author = {O'Connor, Nathan and Silver, Randi B},
	Booktitle = {Methods in cell biology},
	Doi = {10.1016/S0091-679X(06)81019-8},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/O'Connor, Silver - 2007 - Ratio imaging practical considerations for measuring intracellular Ca2 and pH in living cells.pdf:pdf},
	Issn = {0091-679X},
	Keywords = {Animals,Biological,Calcium,Calcium: analysis,Cells,Cells: ultrastructure,Computer-Assisted,Computer-Assisted: instrumentation,Fluoresceins,Fluoresceins: pharmacology,Fluorescence,Fluorescence: instrumentation,Fluorescence: methods,Fluorescent Dyes,Fluorescent Dyes: pharmacology,Fura-2,Fura-2: pharmacology,Humans,Hydrogen-Ion Concentration,Image Enhancement,Image Enhancement: methods,Infusion Pumps,Intracellular Fluid,Intracellular Fluid: chemistry,Intracellular Fluid: drug effects,Microscopy,Models,Signal Processing},
	Month = jan,
	Pages = {415--33},
	Pmid = {17519177},
	Title = {{Ratio imaging: practical considerations for measuring intracellular Ca2+ and pH in living cells}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/17519177},
	Volume = {81},
	Year = {2007},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/17519177},
	Bdsk-Url-2 = {http://dx.doi.org/10.1016/S0091-679X(06)81019-8}}

@article{McGuigan1991,
	Abstract = {In measurements of the intracellular free calcium concentration ([Ca2+]) using either microelectrodes or fluorescent probes, calibration is normally carried out in EGTA calcium buffer solutions. In the first part of the article the general properties of calcium buffer solutions are discussed, the equations used to calculate the apparent calcium binding constant (Kapp) are derived, and the difficulties in the calculation are discussed. The effects of the purity of EGTA as well as the influence of calcium contamination on the buffer solutions are explained. Because of the difficulties in calculating Kapp, and the importance of EGTA purity and calcium contamination, it is suggested that it is easier to measure all three under the appropriate experimental conditions using the method of Bers (1982). In the second part a do-it-yourself guide to the preparation of EGTA calcium buffer solutions is given. An experimental example is provided using the Bers method to measure purity, contamination, and Kapp. It is concluded that unless all three factors are known it is not possible to prepare accurate EGTA calcium buffer solutions.},
	Author = {McGuigan, JAS and L\"{u}thi, D and Buri, A.},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/McGuigan, L\"{u}thi, Buri - 1991 - Calcium buffer solutions and how to make them a do it yourself guide.pdf:pdf},
	Journal = {Canadian journal of Physiology \& Pharmacology},
	Number = {11},
	Pages = {1733--49},
	Pmid = {1804518},
	Title = {{Calcium buffer solutions and how to make them: a do it yourself guide}},
	Url = {http://article.pubs.nrc-cnrc.gc.ca/ppv/RPViewDoc?issn=1205-7541\&volume=69\&issue=11\&startPage=1733\&ab=y},
	Volume = {69},
	Year = {1991},
	Bdsk-Url-1 = {http://article.pubs.nrc-cnrc.gc.ca/ppv/RPViewDoc?issn=1205-7541%5C&volume=69%5C&issue=11%5C&startPage=1733%5C&ab=y}}

@article{Bird2008,
	Abstract = {Activation of surface membrane receptors coupled to phospholipase C results in the generation of cytoplasmic Ca2+ signals comprised of both intracellular Ca2+ release, and enhanced entry of Ca2+ across the plasma membrane. A primary mechanism for this Ca2+ entry process is attributed to store-operated Ca2+ entry, a process that is activated by depletion of Ca2+ ions from an intracellular store by inositol 1,4,5-trisphosphate. Our understanding of the mechanisms underlying both Ca2+ release and store-operated Ca2+ entry have evolved from experimental approaches that include the use of fluorescent Ca2+ indicators and electrophysiological techniques. Pharmacological manipulation of this Ca2+ signaling process has been somewhat limited; but recent identification of key molecular players, STIM and Orai family proteins, has provided new approaches. Here we describe practical methods involving fluorescent Ca2+ indicators and electrophysiological approaches for dissecting the observed intracellular Ca2+ signal to reveal characteristics of store-operated Ca2+ entry, highlighting the advantages, and limitations, of these approaches.},
	Annote = {Ca2+ regulation diseases
F.M. La Ferla, Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease. Nat. Rev. Neurosci.        3 (2002), pp. 862--872.
        
Apoptosis - S.P. Yu, L.M. Canzoniero and D.W. Choi, Ion homeostasis and apoptosis. Curr. Opin. Cell Biol.        13 (2001), pp. 405--411. 
        
Contraction - D.M. Bers, Cardiac excitation--contraction coupling. Nature        10 (2002), pp. 198--205
        
Proliferation - N. Agell, O. Bachs, N. Rocamora and P. Villalonga, Modulation of the Ras/Raf/MEK/ERK pathway by Ca2+ , and calmodulin. Cell. Signal.        14 (2002), pp. 649--654. 
        
Cancer (overproliferation) - D.M. Haverstick, T.N. Heady, T.L. Macdonald and L.S. Gray, Inhibition of human prostate cancer proliferation in vitro and in a mouse model by a compound synthesized to block Ca2+ entry. Cancer Res.        60 (2000), pp. 1002--1008.},
	Author = {Bird, Gary S and DeHaven, Wayne I and Smyth, Jeremy T and Putney, James W},
	Doi = {10.1016/j.ymeth.2008.09.009},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Bird et al. - 2008 - Methods for studying store-operated calcium entry..pdf:pdf},
	Issn = {1095-9130},
	Journal = {Methods (San Diego, Calif.)},
	Keywords = {5-Trisphosphate,5-Trisphosphate: metabolism,Animals,Calcium,Calcium Channels,Calcium Channels: metabolism,Calcium Signaling,Calcium Signaling: drug effects,Calcium Signaling: physiology,Calcium-Sensing,Calcium-Sensing: metabolism,Calcium: metabolism,Fluorescent Dyes,Fluorescent Dyes: pharmacology,Humans,Inositol 1,Receptors,Sarcoplasmic Reticulum Calcium-Transporting ATPase},
	Month = nov,
	Number = {3},
	Pages = {204--12},
	Pmid = {18929662},
	Publisher = {Elsevier Inc.},
	Title = {{Methods for studying store-operated calcium entry.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/18929662},
	Volume = {46},
	Year = {2008},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/18929662},
	Bdsk-Url-2 = {http://dx.doi.org/10.1016/j.ymeth.2008.09.009}}

@article{Thomas2000,
	Abstract = {Quantifying the magnitude of Ca2+ signals from changes in the emission of fluorescent indicators relies on assumptions about the indicator behaviour in situ. Factors such as osmolarity, pH, ionic strength and protein environment can affect indicator properties making it advantageous to calibrate indicators within the required cellular or subcellular environment. Selecting Ca2+ indicators appropriate for a particular application depends upon several considerations including Ca2+ binding affinity, dynamic range and ease of loading. These factors are usually best determined empirically. This study describes the in-situ calibration of a number of frequently used fluorescent Ca2+ indicators (Fluo-3, Fluo-4, Calcium Green-1, Calcium Orange, Oregon Green 488 BAPTA-1 and Fura-Red) and their use in reporting low- and high-amplitude Ca2+ signals in HeLa cells. All Ca2+ indicators exhibited lower in-situ Ca2+ binding affinities than suggested by previously published in-vitro determinations. Furthermore, for some of the indicators, there were significant differences in the apparent Ca2+ binding affinities between nuclear and cytoplasmic compartments. Variation between indicators was also found in their dynamic ranges, compartmentalization, leakage and photostability. Overall, Fluo-3 proved to be the generally most applicable Ca2+ indicator, since it displayed a large dynamic range, low compartmentalization and an appropriate apparent Ca2+ binding affinity. However, it was more susceptible to photobleaching than many of the other Ca2+ indicators.},
	Annote = {Suggests that nuclear to cytoplasmic calcium gradients may be artifactual in nature.Result of not properly calibrating cells for Ca imaging expt's. 
Fig \#5.},
	Author = {Thomas, D and Tovey, S C and Collins, T J and Bootman, M D and Berridge, M J and Lipp, P},
	Doi = {10.1054/ceca.2000.0152},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Thomas et al. - 2000 - A comparison of fluorescent Ca2 indicator properties and their use in measuring elementary and global Ca2 signals..pdf:pdf},
	Issn = {0143-4160},
	Journal = {Cell calcium},
	Keywords = {Aniline Compounds,Benzofurans,Calcium,Calcium Signaling,Calcium: metabolism,Calibration,Cell Compartmentation,Cell Nucleus,Cell Nucleus: metabolism,Cytosol,Cytosol: metabolism,Fluorescent Dyes,Hela Cells,Humans,Imidazoles,Organic Chemicals,Xanthenes},
	Month = oct,
	Number = {4},
	Pages = {213--23},
	Pmid = {11032777},
	Title = {{A comparison of fluorescent Ca2+ indicator properties and their use in measuring elementary and global Ca2+ signals.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/11032777},
	Volume = {28},
	Year = {2000},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/11032777},
	Bdsk-Url-2 = {http://dx.doi.org/10.1054/ceca.2000.0152}}

@article{Grynkiewicz1985,
	Abstract = {A new family of highly fluorescent indicators has been synthesized for biochemical studies of the physiological role of cytosolic free Ca2+. The compounds combine an 8-coordinate tetracarboxylate chelating site with stilbene chromophores. Incorporation of the ethylenic linkage of the stilbene into a heterocyclic ring enhances the quantum efficiency and photochemical stability of the fluorophore. Compared to their widely used predecessor, "quin2", the new dyes offer up to 30-fold brighter fluorescence, major changes in wavelength not just intensity upon Ca2+ binding, slightly lower affinities for Ca2+, slightly longer wavelengths of excitation, and considerably improved selectivity for Ca2+ over other divalent cations. These properties, particularly the wavelength sensitivity to Ca2+, should make these dyes the preferred fluorescent indicators for many intracellular applications, especially in single cells, adherent cell layers, or bulk tissues.},
	Author = {Grynkiewicz, G and Poenie, M and Tsien, R Y},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Grynkiewicz, Poenie, Tsien - 1985 - A new generation of Ca2 indicators with greatly improved fluorescence properties..pdf:pdf},
	Issn = {0021-9258},
	Journal = {The Journal of biological chemistry},
	Keywords = {Aminoquinolines,Benzofurans,Benzofurans: chemical synthesis,Calcium,Calcium: analysis,Erythrocyte Membrane,Erythrocyte Membrane: analysis,Flow Cytometry,Fluorescence,Fluorescent Dyes,Fluorescent Dyes: chemical synthesis,Fura-2,Humans,Hydrogen-Ion Concentration,Indoles,Indoles: chemical synthesis,Magnesium,Magnesium: pharmacology,Mathematics,Spectrometry,Stilbenes,Stilbenes: chemical synthesis},
	Month = mar,
	Number = {6},
	Pages = {3440--50},
	Pmid = {3838314},
	Title = {{A new generation of Ca2+ indicators with greatly improved fluorescence properties.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/3838314},
	Volume = {260},
	Year = {1985},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/3838314}}

@article{Roos2005,
	Abstract = {Store-operated Ca2+ (SOC) channels regulate many cellular processes, but the underlying molecular components are not well defined. Using an RNA interference (RNAi)-based screen to identify genes that alter thapsigargin (TG)-dependent Ca2+ entry, we discovered a required and conserved role of Stim in SOC influx. RNAi-mediated knockdown of Stim in Drosophila S2 cells significantly reduced TG-dependent Ca2+ entry. Patch-clamp recording revealed nearly complete suppression of the Drosophila Ca2+ release-activated Ca2+ (CRAC) current that has biophysical characteristics similar to CRAC current in human T cells. Similarly, knockdown of the human homologue STIM1 significantly reduced CRAC channel activity in Jurkat T cells. RNAi-mediated knockdown of STIM1 inhibited TG- or agonist-dependent Ca2+ entry in HEK293 or SH-SY5Y cells. Conversely, overexpression of STIM1 in HEK293 cells modestly enhanced TG-induced Ca2+ entry. We propose that STIM1, a ubiquitously expressed protein that is conserved from Drosophila to mammalian cells, plays an essential role in SOC influx and may be a common component of SOC and CRAC channels.},
	Author = {Roos, Jack and DiGregorio, Paul J and Yeromin, Andriy V and Ohlsen, Kari and Lioudyno, Maria and Zhang, Shenyuan and Safrina, Olga and Kozak, J Ashot and Wagner, Steven L and Cahalan, Michael D and Veli\c{c}elebi, G\"{o}n\"{u}l and Stauderman, Kenneth a},
	Doi = {10.1083/jcb.200502019},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Roos et al. - 2005 - STIM1, an essential and conserved component of store-operated Ca2 channel function..pdf:pdf},
	Issn = {0021-9525},
	Journal = {The Journal of cell biology},
	Keywords = {Animals,Calcium,Calcium Channels,Calcium Channels: metabolism,Calcium Signaling,Calcium Signaling: drug effects,Calcium Signaling: physiology,Calcium: metabolism,Cell Line,Cell Membrane,Cell Membrane: metabolism,Conserved Sequence,Conserved Sequence: physiology,Drosophila,Drosophila Proteins,Drosophila Proteins: genetics,Drosophila Proteins: isolation \& purification,Drosophila Proteins: metabolism,Enzyme Inhibitors,Enzyme Inhibitors: pharmacology,Evolution,Humans,Jurkat Cells,Membrane Proteins,Membrane Proteins: genetics,Membrane Proteins: isolation \& purification,Membrane Proteins: metabolism,Molecular,Neoplasm Proteins,Neoplasm Proteins: genetics,Neoplasm Proteins: metabolism,Patch-Clamp Techniques,RNA Interference,Thapsigargin,Thapsigargin: pharmacology,used probenecid},
	Mendeley-Tags = {used probenecid},
	Month = may,
	Number = {3},
	Pages = {435--45},
	Pmid = {15866891},
	Title = {{STIM1, an essential and conserved component of store-operated Ca2+ channel function.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/15866891},
	Volume = {169},
	Year = {2005},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/15866891},
	Bdsk-Url-2 = {http://dx.doi.org/10.1083/jcb.200502019}}

@article{Goto2010,
	Abstract = {Store-operated calcium entry (SOCE) or calcium release-activated calcium current (I(CRAC)) is a critical pathway to replenish intracellular calcium stores, and plays indispensable roles in cellular functions such as antigen-induced T lymphocyte activation. Despite the importance of I(CRAC) in cellular functions, lack of potent and specific inhibitor has limited the approaches to the function of I(CRAC) in native cells. 2-Aminoethyl diphenylborinate (2-APB) is a widely used SOCE/I(CRAC) inhibitor, while its effect is rather unspecific. In the attempt to develop more potent and selective compounds here we identified two structurally isomeric 2-APB analogues that are 100-fold more potent than 2-APB itself. One of the 2-APB analogues activates and inhibits endogenous SOCE depending on the concentration while the other only inhibits it. The 2-APB analogue inhibits store depletion-mediated STIM1 clustering as well as heterologously expressed CRAC current. Together with the observation that, unlike 2-APB, the analogue compounds failed to activate CRACM3/Orai3 current in the absence of STIM, our results suggest that inhibition and activation of SOCE/I(CRAC) by the 2-APB analogues is mediated by STIM.},
	Author = {Goto, Jun-Ichi and Suzuki, Akinobu Z and Ozaki, Shoichiro and Matsumoto, Nagisa and Nakamura, Takeshi and Ebisui, Etsuko and Fleig, Andrea and Penner, Reinhold and Mikoshiba, Katsuhiko},
	Doi = {10.1016/j.ceca.2009.10.004},
	File = {:Users/orville/Dropbox/Papers/2010/Goto/Cell calcium 2010 Goto.pdf:pdf},
	Issn = {1532-1991},
	Journal = {Cell calcium},
	Keywords = {Animals,Boron Compounds,Boron Compounds: chemistry,Boron Compounds: pharmacology,CHO Cells,Calcium Channels,Calcium Channels: metabolism,Calcium Signaling,Calcium Signaling: drug effects,Calcium Signaling: physiology,Chickens,Cricetinae,Cricetulus,Hela Cells,Humans,Ion Channel Gating,Ion Channel Gating: drug effects,Ion Channel Gating: physiology,Jurkat Cells,Male,Membrane Proteins,Membrane Proteins: genetics,Membrane Proteins: metabolism,Mice,Neoplasm Proteins,Neoplasm Proteins: genetics,Neoplasm Proteins: metabolism,Patch-Clamp Techniques,TRPC Cation Channels,TRPC Cation Channels: metabolism},
	Month = jan,
	Number = {1},
	Pages = {1--10},
	Pmid = {19945161},
	Title = {{Two novel 2-aminoethyl diphenylborinate (2-APB) analogues differentially activate and inhibit store-operated Ca(2+) entry via STIM proteins.}},
	Url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2905153\&tool=pmcentrez\&rendertype=abstract},
	Volume = {47},
	Year = {2010},
	Bdsk-Url-1 = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2905153%5C&tool=pmcentrez%5C&rendertype=abstract},
	Bdsk-Url-2 = {http://dx.doi.org/10.1016/j.ceca.2009.10.004}}

@misc{Baum2008,
	Abstract = {Given the power of Drosophila genetics, it may seem surprising to discover that many fly researchers are turning to Drosophila cell culture as an experimental system. However, as we will show in this chapter, there are many benefits to be gained by using cell lines as a complement to studies in a tissue and developmental context in the fly. Moreover, one can argue that Drosophila cell culture, in itself, provides an excellent model system for the study of many fundamental questions in molecular and cellular biology. In this review, we offer a summary of techniques that should be useful to researchers in the Drosophila community working with fly cell lines. These include techniques for growing and maintaining cell lines, transient and stable transfection, RNA interference, imaging, immunostaining, fluorescence-activated cell sorting, and for the isolation of RNA and protein from fly cells.},
	Author = {Baum, Buzz and Cherbas, Lucy},
	Booktitle = {Methods in molecular biology (Clifton, N.J.)},
	Doi = {10.1007/978-1-59745-583-1\_25},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Baum, Cherbas - 2008 - Drosophila cell lines as model systems and as an experimental tool..pdf:pdf},
	Issn = {1064-3745},
	Keywords = {Animals,Cell Line,Cell Line, Transformed,Cell Nucleus,Cell Nucleus: metabolism,Cell Separation,Developmental Biology,Developmental Biology: methods,Drosophila melanogaster,Flow Cytometry,Genetic Techniques,Microscopy, Fluorescence,Microscopy, Fluorescence: methods,Molecular Biology,Molecular Biology: methods,RNA,RNA Interference,RNA, Double-Stranded,RNA, Double-Stranded: metabolism,RNA: metabolism,Transgenes},
	Month = jan,
	Pages = {391--424},
	Pmid = {18641962},
	Title = {{Drosophila cell lines as model systems and as an experimental tool.}},
	Url = {http://www.ncbi.nlm.nih.gov/pubmed/18641962},
	Volume = {420},
	Year = {2008},
	Bdsk-Url-1 = {http://www.ncbi.nlm.nih.gov/pubmed/18641962},
	Bdsk-Url-2 = {http://dx.doi.org/10.1007/978-1-59745-583-1%5C_25}}

@article{Duncker1997,
	Author = {Duncker, B P and Davies, P L and Walker, V K},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Duncker, Davies, Walker - 1997 - Introns boost transgene expression in Drosophila melanogaster..pdf:pdf},
	Issn = {0026-8925},
	Journal = {Molecular \& general genetics : MGG},
	Keywords = {Animals,Antifreeze Proteins,Base Sequence,Drosophila melanogaster,Drosophila melanogaster: genetics,Fishes,Gene Expression Regulation,Gene Transfer Techniques,Glycoproteins,Glycoproteins: genetics,Introns,Introns: genetics,Molecular Sequence Data,Transgenes},
	Month = apr,
	Number = {3},
	Pages = {291--6},
	Pmid = {9150263},
	Title = {{Introns boost transgene expression in Drosophila melanogaster.}},
	Volume = {254},
	Year = {1997}}

@article{Buckingham1996,
	Abstract = {RDL is an ionotropic GABA receptor subunit, a product of the Rdl gene, originally identified in the Maryland strain of Drosophila melanogaster. Here, we report the generation of a Drosophila melanogaster cell line (S2-RDLA302S) stably expressing a mutated, dieldrin-resistant (A302S) form of RDL. The properties of this dieldrin-resistant, homo-oligomeric receptor have been compared with those of the stably expressed, wild-type form (S2-RDL). Using these stable lines, a striking reduction in sensitivity to both picrotoxinin and dieldrin was observed for responses to GABA of S2-RDLA302S compared to S2-RDL. To determine if these stable insect cell lines generate results similar to those obtained by transient expression in Xenopus laevis oocytes, we have examined the actions of two widely used convulsants, EBOB and TBPS, and a recently developed convulsant BIDN, on RDL-mediated GABA responses in the two expression systems. In both oocytes and S2 cells, the three convulsants suppressed the amplitude of responses to GABA. Thus, in accord with earlier work on agonist and allosteric sites, the S2-RDL cell line is found to yield similar pharmacological results to those obtained in transient expression studies. Stable cell lines are now available expressing susceptible and resistant forms of an ionotropic receptor by GABAergic insecticides.},
	Author = {Buckingham, S D and Matsuda, K and Hosie, A M and Baylis, H A and Squire, M D and Lansdell, S J and Millar, N S and Sattelle, B},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Buckingham et al. - 1996 - Wild-type and insecticide-resistant homo-oligomeric GABA receptors of Drosophila melanogaster stably expressed in a Drosophila cell line..pdf:pdf},
	Issn = {0028-3908},
	Journal = {Neuropharmacology},
	Keywords = {Animals,Cell Line,Dieldrin,Dieldrin: pharmacology,Drosophila melanogaster,Electrophysiology,GABA,GABA Agonists,GABA Agonists: pharmacology,GABA: biosynthesis,GABA: drug effects,GABA: genetics,Insecticide Resistance,Insecticide Resistance: genetics,Insecticides,Insecticides: pharmacology,Membrane Potentials,Membrane Potentials: drug effects,Oocytes,Oocytes: metabolism,Patch-Clamp Techniques,Receptors,Transfection,Xenopus laevis},
	Month = jan,
	Number = {9-10},
	Pages = {1393--401},
	Pmid = {9014156},
	Title = {{Wild-type and insecticide-resistant homo-oligomeric GABA receptors of Drosophila melanogaster stably expressed in a Drosophila cell line.}},
	Volume = {35},
	Year = {1996}}

@article{Lenhard1997,
	Abstract = {The baculovirus-insect cell expression system has proven to be a valuable tool for the high level production of a multitude of recombinant proteins. However, production of membrane proteins in infected insect cells is often hampered by incorrect folding and processing which results in the accumulation of non-functional protein. Here, we report the construction of a Sf9 insect cell line stably transformed with the ninaA gene from D. melanogaster (Sfn cell line). The ninaA protein is a membrane bound cyclophilin which acts as a peptidyl-prolyl cis/trans isomerase during the folding process of rhodopsin 1 in D. melanogaster rhabdomere. Engineered Sfn insect cells infected with a recombinant baculovirus bearing the human dopamine transporter gene under the control of the polyhedrin promoter showed a > or = 5 times enhanced uptake of [3H]dopamine in comparison to similarly infected Sf9 cells. This increase in specific transport activity was not due to an altered Km value in the Sfn cell line. The uptake in infected Sfn cells was blocked by the peptidyl-prolyl cis/trans isomerase inhibitor cyclosporin A which had no effect on infected Sf9 cells. From these results we conclude that the prolyl-cis/trans isomerase activity of the ninaA in the stably transformed Sfn cell line was responsible, directly or indirectly, for the improved folding of the heterologously produced human dopamine transporter.},
	Author = {Lenhard, T and Reil\"{a}nder, H},
	Doi = {10.1006/bbrc.1997.7395},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Lenhard, Reil\"{a}nder - 1997 - Engineering the folding pathway of insect cells generation of a stably transformed insect cell line showing improved folding of a recombinant membrane protein..pdf:pdf},
	Issn = {0006-291X},
	Journal = {Biochemical and biophysical research communications},
	Keywords = {Animals,Baculoviridae,Baculoviridae: genetics,Carrier Proteins,Carrier Proteins: biosynthesis,Carrier Proteins: drug effects,Carrier Proteins: immunology,Cell Culture Techniques,Cell Culture Techniques: methods,Cell Line,Cyclosporine,Cyclosporine: pharmacology,Dopamine,Dopamine Plasma Membrane Transport Proteins,Dopamine: metabolism,Drosophila Proteins,Drosophila melanogaster,Drosophila melanogaster: genetics,Humans,Insect Proteins,Insect Proteins: biosynthesis,Insect Proteins: genetics,Membrane Glycoproteins,Membrane Proteins,Membrane Proteins: biosynthesis,Membrane Proteins: chemistry,Membrane Proteins: genetics,Membrane Transport Proteins,Molecular Chaperones,Nerve Tissue Proteins,Precipitin Tests,Protein Engineering,Protein Folding,Recombinant Proteins,Recombinant Proteins: biosynthesis,Recombinant Proteins: chemistry,Spodoptera,Spodoptera: cytology,Spodoptera: genetics,Transformed,Tunicamycin,Tunicamycin: pharmacology},
	Month = sep,
	Number = {3},
	Pages = {823--30},
	Pmid = {9325175},
	Title = {{Engineering the folding pathway of insect cells: generation of a stably transformed insect cell line showing improved folding of a recombinant membrane protein.}},
	Volume = {238},
	Year = {1997},
	Bdsk-Url-1 = {http://dx.doi.org/10.1006/bbrc.1997.7395}}

@article{Santos2007,
	Abstract = {Drosophila melanogaster S2 cells were co-transfected with plasmid vectors containing the enhanced green fluorescent protein gene (EGFP), under the control of metallothionein promoter (pMt), and the hygromycin selection gene, in view of establishing parameters for optimized gene expression. A protocol of transfection was worked out, leading after hygromycin selection, to approximately 90\% of S2MtEGFP fluorescent cells at day 5 after copper sulfate (CuSO(4)) induction. As analyzed by confocal microscopy, S2MtEGFP cell cultures were shown to be quite heterogeneous regarding the intensity and cell localization of fluorescence among the EGFP expressing cells. Spectrofluorimetry kinetic studies of CuSO(4) induced S2MtEGFP cells showed the EGFP expression at 510 nm as soon as 5 h after induction, the fluorescence increasing progressively from this time to attain values of 4.6 x 10(5) counts/s after 72 h of induction. Induction with 700 muM of CuSO(4) performed at the exponential phase of the S2MtEGFP culture (10(6) cells/mL) led to a better performance in terms of cell growth, percent of fluorescent cells and culture intensity of fluorescence. Sodium butyrate (NaBu) treatment of CuSO(4) induced S2MtEGFP cell cultures, although leading to a loss of cell culture viability, increased the percent of EGFP expressing cells and sharply enhanced the cell culture fluorescence intensity. The present study established parameters for improving heterologous protein expression in stably transfected Drosophila S2 cells, as assessed by the EGFP expression.},
	Annote = {Methods
Hygromycin B transfection
        
Variance F test used for statistical analysis 
- check out},
	Author = {Santos, Mariza G and Jorge, Soraia a C and Brillet, Karl and Pereira, Carlos a},
	Doi = {10.1007/s10616-007-9060-9},
	File = {:Users/orville/Library/Application Support/Mendeley Desktop/Downloaded/Santos et al. - 2007 - Improving heterologous protein expression in transfected Drosophila S2 cells as assessed by EGFP expression..pdf:pdf},
	Issn = {0920-9069},
	Journal = {Cytotechnology},
	Keywords = {cell transfection \'{a} gene,egfp \'{a},expression \'{a} sodium,schneider drosophila cells \'{a}},
	Number = {1},
	Pages = {15--24},
	Pmid = {19003014},
	Title = {{Improving heterologous protein expression in transfected Drosophila S2 cells as assessed by EGFP expression.}},
	Volume = {54},
	Year = {2007},
	Bdsk-Url-1 = {http://dx.doi.org/10.1007/s10616-007-9060-9}}