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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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Book ChapterDOI

Strategies and Methods for Proteome Analysis

TL;DR: In most cases the availability of protein and DNA sequences in public databases eliminates the need for complete protein sequence analysis and protein sequences are more rapidly identified by partial sequence analysis using tandem mass spectrometry which allows rapid, complete gene identification.
Journal ArticleDOI

Categorization of Phosphorylation Site Behavior during the Diauxic Shift in Saccharomyces cerevisiae .

TL;DR: In this article, the authors measured protein and phosphorylation site changes across 11 points of a time course and developed a method for categorizing protein and site behavior relative to protein level changes using the diauxic shift in yeast as a model.
Posted ContentDOI

Aging predisposes B cells to malignancy by activating c-Myc and perturbing the genome and epigenome

TL;DR: In this paper, the authors investigated how B-cell lymphoma develops as a consequence of the aging immune system and found that aged B cells undergo clonal expansions driven by genetic and epigenetic changes and established cell and spleen size as early markers of malignant transformation.
Journal ArticleDOI

Iron Deficiency and Recovery in Yeast: A Quantitative Proteomics Approach.

TL;DR: In this paper, the early (4 and 6 h) and late (12 h) response to iron deficiency was explored, where metabolic pathways like the Krebs cycle, amino acid, and ergosterol biosynthesis were affected.
Posted ContentDOI

Global proteomics of Ubqln2-based murine models of ALS

TL;DR: This study provides a deep understanding of the proteomic landscape of ALS-related Ubqln2 mutants and identifies candidate client proteins that are altered in vivo in disease models and whose degradation is promoted by UBQLN2.