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Steven P. Gygi

Researcher at Harvard University

Publications -  778
Citations -  147003

Steven P. Gygi is an academic researcher from Harvard University. The author has contributed to research in topics: Proteome & Phosphorylation. The author has an hindex of 172, co-authored 704 publications receiving 129173 citations. Previous affiliations of Steven P. Gygi include University of Rochester Medical Center & Cell Signaling Technology.

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Expedited mapping of the ligandable proteome using fully functionalized enantiomeric probe pairs.

TL;DR: This work identifies numerous stereoselective protein–fragment interactions in cells and shows that these interactions occur at functional sites on proteins from diverse classes, indicating that incorporating chirality into fully functionalized fragment libraries provides a robust and streamlined method to discover ligandable proteins in cells.
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p90 Ribosomal S6 Kinase and p70 Ribosomal S6 Kinase Link Phosphorylation of the Eukaryotic Chaperonin Containing TCP-1 to Growth Factor, Insulin, and Nutrient Signaling

TL;DR: The findings demonstrate a link between oncogene and growth factor signaling and chaperonin CCT-mediated cellular activities and show that RNA interference-mediated knockdown of endogenous CCTβ causes impaired cell proliferation that can be rescued with ectopically expressed murine CCT β wild-type or phosphomimetic mutant S260D, but not the phosphorylation-deficient mutant S 260A.
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WDR20 Regulates Activity of the USP12·UAF1 Deubiquitinating Enzyme Complex

TL;DR: A model is provided in which WDR20 serves as a stimulatory subunit for preserving and regulating the activity of the subset of the UAF1·USP complexes, which contradicts the previous report that USP12 and USP46 do not regulate the FA pathway.
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Evidence that C9ORF72 Dipeptide Repeat Proteins Associate with U2 snRNP to Cause Mis-splicing in ALS/FTD Patients

TL;DR: It is shown that addition of proline-arginine (PR) and glycine-argarine (GR) toxic DPR peptides to nuclear extracts blocks spliceosome assembly and splicing, but not other types of RNA processing.
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Comprehensive Temporal Protein Dynamics during the Diauxic Shift in Saccharomyces cerevisiae

TL;DR: In this paper, the authors performed temporal quantitative proteomics to fully capture protein induction and repression during the diauxic shift in yeast and achieved accurate and sensitive quantitation at a high temporal resolution and depth of proteome coverage was achieved using TMT10 reagents and LC-MS3 analysis on an Orbitrap Fusion tribrid mass spectrometer deploying synchronous precursor selection.