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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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ATP is required for interactions between UAP56 and two conserved mRNA export proteins, Aly and CIP29, to assemble the TREX complex

TL;DR: Proteomic analysis of immunopurified human TREX complex identified the protein CIP29 as the only new component with a clear yeast relative (known as Tho1) and concluded that the interaction of two conserved export proteins, CIP 29 and Aly, with UAP56 is strictly regulated by ATP during assembly of the TREXcomplex.
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Evaluating multiplexed quantitative phosphopeptide analysis on a hybrid quadrupole mass filter/linear ion trap/orbitrap mass spectrometer

TL;DR: It is found that ratio distortion remained a problem for phosphopeptide analysis in multiplexed quantitative workflows, but the underlying cause of interference may not be due to coeluting and cofragmented peptides but instead from consistent, low level background fragmentation.
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Mechanism of adrenergic Ca V 1.2 stimulation revealed by proximity proteomics

TL;DR: An in vivo approach to identify proteins whose enrichment near cardiac CaV1.2 channels changes upon β-adrenergic stimulation finds the G protein Rad, which is phosphorylated by protein kinase A, thereby relieving channel inhibition by Rad and causing an increased Ca2+ current.
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Highly Multiplexed Quantitative Mass Spectrometry Analysis of Ubiquitylomes.

TL;DR: This analysis revealed the largest collection of PARKIN- and PINK1-dependent ubiquitylation targets to date in a single experiment, and it also revealed a subset of proteins recruited to the mitochondria during mitophagy.
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Full-featured, real-time database searching platform enables fast and accurate multiplexed quantitative proteomics

TL;DR: A new, real-time database search platform, Orbiter, is built to combat the SPS-MS3 method's longer duty cycles, and it is found that RTS enabled a two-fold increase in mass spectrometric data acquisition efficiency.