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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.

Papers
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Journal ArticleDOI

Mass Spectrometric Analysis of Type 1 Inositol 1,4,5-Trisphosphate Receptor Ubiquitination

TL;DR: Data show that endogenous IP3R1 is tagged with an array of ubiquitin conjugates at multiple sites and that both IP3 R1 ubiquitination and degradation are highly complex processes.
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Selection of Heating Temperatures Improves the Sensitivity of the Proteome Integral Solubility Alteration Assay

TL;DR: Simulation and experimental results show that the selection of a subset of heating temperatures ameliorates the small difference problem and improves the PISA assay.
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Phosphorylation of FANCD2 Inhibits the FANCD2/FANCI Complex and Suppresses the Fanconi Anemia Pathway in the Absence of DNA Damage.

TL;DR: A regulatory mechanism operating as a molecular switch is described, where in the absence of DNA damage, the FANCD2/FANCI complex is prevented from loading onto DNA, effectively suppressing the FA pathway.
Patent

Automated capillary liquid chromatography small volume analysis system

TL;DR: In this article, the authors proposed a system for automatically performing liquid chromatography analysis of low volume liquid chemical samples at nanosecond flow rates using an analysis column that integrates a pre-concentration trapping column and a chromatography separation column terminating at an electrospray nozzle of an online mass spectrometer.
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Abelson phosphorylation of CLASP2 modulates its association with microtubules and actin.

TL;DR: It is shown in vertebrate cells that Abl binds to CLASP and phosphorylates it in response to serum or PDGF stimulation, and the data suggest that the functional relationship between Abl and CLASp2 is conserved and provides a means to control theCLASP2 association with the cytoskeleton.