S
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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Journal ArticleDOI
Fat cells directly sense temperature to activate thermogenesis
Li Ye,Jun Wu,Paul Cohen,Lawrence Kazak,Melin J. Khandekar,Mark P. Jedrychowski,Xing Zeng,Steven P. Gygi,Bruce M. Spiegelman +8 more
TL;DR: It is reported that cool temperature can directly activate a thermogenic gene program in adipocytes in a cell-autonomous manner, independent of the canonical cAMP/Protein Kinase A/cAMP response element-binding protein pathway downstream of the β-adrenergic receptors.
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Proteome analysis: Biological assay or data archive?
TL;DR: It is concluded that proteome analysis is an essential tool in the understanding of regulated biological systems and will continue to be enhanced by further improvements in analytical technology.
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Weighing in on ubiquitin: the expanding role of mass-spectrometry-based proteomics
TL;DR: This review summarizes advances involving the identification of ubiquitinated proteins, the elucidation of ubiqu itin-modification sites and the determination of polyubiquitin chain linkages, as well as offering a perspective on the application of emerging technologies for mechanistic and functional studies of protein ubiquitination.
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Quantitative proteomic analysis reveals posttranslational responses to aneuploidy in yeast
Noah Dephoure,Sunyoung Hwang,Ciara O’Sullivan,Stacie E Dodgson,Steven P. Gygi,Angelika Amon,Eduardo M. Torres +6 more
TL;DR: It is shown that although protein levels largely scale with gene copy number, subunits of multi-protein complexes are notable exceptions and posttranslational mechanisms attenuate their expression when their encoding genes are in excess.
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Quantitative phosphorylation profiling of the ERK/p90 ribosomal S6 kinase-signaling cassette and its targets, the tuberous sclerosis tumor suppressors
Bryan A. Ballif,Philippe P. Roux,Scott A. Gerber,Jeffrey P. MacKeigan,John Blenis,Steven P. Gygi +5 more
TL;DR: In this paper, stable isotope-based quantitative MS was used to globally monitor the kinetics of complex, ordered phosphorylation events on protein players in the canonical mitogen-activated protein kinase signaling pathway.