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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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Quantitative proteomic analysis using a MALDI quadrupole time-of-flight mass spectrometer.

TL;DR: The effectiveness of this approach is demonstrated in the quantification and identification of peptides from a control mixture of proteins of known relative concentrations and also in the comparative analysis of protein expression in Saccharomyces cerevisiae grown on two different carbon sources.
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On the Relationship of Protein and mRNA Dynamics in Vertebrate Embryonic Development

TL;DR: It is found that most protein levels change little and duplicated genes are expressed similarly, and a mass action kinetics model parameterized using protein synthesis and degradation rates regresses protein dynamics to RNA dynamics, corrected for initial protein concentration.
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A Quantitative Tissue-Specific Landscape of Protein Redox Regulation during Aging

TL;DR: Oximouse is developed, a comprehensive and quantitative mapping of the mouse cysteine redox proteome in vivo that comprehensively identifies redox-modified disease networks that remodel in aged mice, establishing a systemic molecular basis for the long-standing proposed links between redox dysregulation and tissue aging.
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Correct Interpretation of Comprehensive Phosphorylation Dynamics Requires Normalization by Protein Expression Changes

TL;DR: Combinedprotein expression and phosphorylation surveys uncovered both independent and concerted changes in protein expression andosphorylation, while highlighting the partially redundant role of a second MAPK (Kss1) in the mating pathway.
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UAF1 Is a Subunit of Multiple Deubiquitinating Enzyme Complexes

TL;DR: This work presents the isolation of two novel multisubunit deubiquitinating enzyme complexes containing USP12 and USP46, respectively, and notes that UAF1 regulates the enzymatic activity of both enzyme complexes, suggesting that this activator protein may regulate a subclass of human deubiqueitinating enzymes.