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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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Signaling networks assembled by oncogenic EGFR and c-Met

TL;DR: Comparing non-small-cell lung cancer cell lines driven by EGFR-activating mutations and genomic amplifications using a global proteomic analysis of phospho-tyrosine signaling identifies an extensive receptor tyrosine kinase signaling network established in cells expressing mutated and activated EGFR or expressing amplified c-Met.
PatentDOI

Dual inhibition of sister chromatide separation at metaphase

TL;DR: It is proposed that separase activation at the metaphase-anaphase transition requires the removal of both securin and an inhibitory phosphate.
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Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages.

TL;DR: It is found that the U-box E3, CHIP, and Ring finger E3s, MuRF1 and Mdm2, with the E2, UbcH5, form a novel type of Ub chain that contains all seven possible linkages, but predominantly Lys48, Lys63, and Lys11 linkages.
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Semiquantitative proteomic analysis of rat forebrain postsynaptic density fractions by mass spectrometry

TL;DR: A comprehensive analysis of purified PSD fractions by liquid chromatography coupled with tandem mass spectrometry reveals crucial information about molecular abundance as well as molecular diversity in the PSD, and provides a basis for further studies on the molecular mechanisms of synaptic function and plasticity.
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A molecular determinant for the establishment of sister chromatid cohesion.

TL;DR: In budding yeast, the head domain of the Smc3p subunit of cohesin is acetylated by the Eco1p acetyltransferase at two evolutionarily conserved residues, promoting the chromatin-bound cohes in to tether sister chromatids.