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people and pub update
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colganwi committed Oct 18, 2023
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6 changes: 6 additions & 0 deletions README.md
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## Weissman Lab Website

### Local testing

```
bundle exec jekyll serve
```




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16 changes: 10 additions & 6 deletions _data/people.yml
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alum: false

- name: Jaspreet Sandhu
pos: Visiting Scientist
pos: Post-doc
email: [email protected]
id: JaspreetSandhu
alum: false
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pos: Post-doc
email: [email protected]
id: DianYang
alum: false
alum: true
now: Assistant Professor of Molecular Pharmacology and Therapeutics | Coulmbia
University

- name: Chen Weng
pos: Post-doc
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pos: Grad student
email: [email protected]
id: AlexanderLeNail
alum: false
alum: true
now: Grad Student | Heiman Lab MIT

- name: Yi Hua Chen
pos: Grad student
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pos: Undergrad
email: [email protected]
id: ThaoNguyen
alum: false
alum: true
now: PhD Student | Stanford Genetics

- name: Jacob Shapiro
pos: Undergrad
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pos: Grad student
id: JoshuaDunn
alum: true
now: Head of Design | Ginkgo Bioworks
now: Senior Director of Design and Computational Biology | Ginkgo Bioworks

- name: Alexander Fields
pos: Post-doc
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pos: Grad student
id: MaxHorlbeck
alum: true
now: "Pediatrics Medical Genetics Resident | Boston Children\u2019s Hospital"
now: "Pediatrics/Medical Genetics Resident| Boston Children\u2019s Hospital"

- name: Siew Ho-Schleyer
pos: Post-doc
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70 changes: 70 additions & 0 deletions _data/publications.yml
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- title: Systematic functional interrogation of SARS-CoV-2 host factors using Perturb-seq.
authors:
- Sara Sunshine
- Andreas S Puschnik
- Joseph M Replogle
- Matthew T Laurie
- Jamin Liu
- Beth Shoshana Zha
- "James K Nu\xF1ez"
- Janie R Byrum
- Aidan H McMorrow
- Matthew B Frieman
- Juliane Winkler
- Xiaojie Qiu
- Oren S Rosenberg
- Manuel D Leonetti
- Chun Jimmie Ye
- Jonathan S Weissman
- Joseph L DeRisi
- Marco Y Hein
publication_date: 07/10/23
publication_year: '2023'
pubmed_id: '37803001'
abstract: "Genomic and proteomic screens have identified numerous host factors of\
\ SARS-CoV-2, but efficient delineation of their molecular roles during infection\
\ remains a challenge. Here we use Perturb-seq, combining genetic perturbations\
\ with a single-cell readout, to investigate how inactivation of host factors\
\ changes the course of SARS-CoV-2 infection and the host response in human lung\
\ epithelial cells. Our high-dimensional data resolve complex phenotypes such\
\ as shifts in the stages of infection and modulations of the interferon response.\
\ However, only a small percentage of host factors showed such phenotypes upon\
\ perturbation. We further identified the NF-\u03BAB inhibitor I\u03BAB\u03B1\
\ (NFKBIA), as well as the translation factors EIF4E2 and EIF4H as strong host\
\ dependency factors acting early in infection. Overall, our study provides massively\
\ parallel functional characterization of host factors of SARS-CoV-2 and quantitatively\
\ defines their roles both in virus-infected and bystander cells."
doi: 10.1038/s41467-023-41788-4
journal: Nature communications
- title: "Triaging of \u237A-helical proteins to the mitochondrial outer membrane\
\ by distinct chaperone machinery based on substrate topology."
authors:
- Gayathri Muthukumar
- Taylor A Stevens
- Alison J Inglis
- Theodore K Esantsi
- Reuben A Saunders
- Fabian Schulte
- Rebecca M Voorhees
- Alina Guna
- Jonathan S Weissman
publication_date: 30/08/23
publication_year: '2023'
pubmed_id: '37645817'
abstract: "Mitochondrial outer membrane \u237A-helical proteins play critical roles\
\ in mitochondrial-cytoplasmic communication, but the rules governing the targeting\
\ and insertion of these biophysically diverse substrates remain unknown. Here,\
\ we first defined the complement of required mammalian biogenesis machinery through\
\ genome-wide CRISPRi screens using topologically distinct membrane proteins.\
\ Systematic analysis of nine identified factors across 21 diverse \u237A-helical\
\ substrates reveals that these components are organized into distinct targeting\
\ pathways which act on substrates based on their topology. NAC is required for\
\ efficient targeting of polytopic proteins whereas signal-anchored proteins require\
\ TTC1, a novel cytosolic chaperone which physically engages substrates. Biochemical\
\ and mutational studies reveal that TTC1 employs a conserved TPR domain and a\
\ hydrophobic groove in its C-terminal domain to support substrate solubilization\
\ and insertion into mitochondria. Thus, targeting of diverse mitochondrial membrane\
\ proteins is achieved through topological triaging in the cytosol using principles\
\ with similarities to ER membrane protein biogenesis systems."
doi: 10.1101/2023.08.16.553624
journal: biorxiv
- title: FET fusion oncoproteins disrupt physiologic DNA repair networks and induce
ATR synthetic lethality in cancer.
authors:
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