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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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Time-resolved proximity labeling of protein networks associated with ligand-activated EGFR

TL;DR: In this paper , peroxidase-catalyzed proximity labeling, isobaric peptide tagging, and quantitative mass spectrometry were combined to define the dynamics of the proximity proteome of ligand-activated EGFR.
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Adiporedoxin, an upstream regulator of ER oxidative folding and protein secretion in adipocytes

TL;DR: Data support the notion that Adrx plays a critical role in adipocyte biology and in the regulation of mouse and human metabolism via its modulation of adipocyte protein secretion.
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Apolipoprotein E is a pancreatic extracellular factor that maintains mature β-cell gene expression.

TL;DR: It is shown that after isolation and during maintenance in culture, adherent rat islets reduce expression of key β-cell transcription factors necessary forβ-cell function and that soluble pancreatic decellularized matrix (DCM) can enhance β- cell gene expression.
Posted ContentDOI

Time resolved quantitative phosphoproteomics reveals distinct patterns of SHP2 dependence in EGFR signaling

TL;DR: Monitoring phosphoproteome dynamics when SHP2 is allosterically inhibited by the small molecule SHP099 reveals six distinct response signatures following SHp099 treatment and washout, highlighting how analysis of phospho-abundance dynamics can provide insight into transmembrane signaling responses.
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Fe3+-NTA magnetic beads as an alternative to spin column-based phosphopeptide enrichment.

TL;DR: In this article , a spin column-based Fe3+-NTA enrichment strategy was compared with one encompassing magnetic beads for global protein phosphorylation, and the results showed that the scalable and automation-friendly magnetic bead-based workflow is an equivalent, but more flexible, enrichment strategy for phosphoproteome profiling experiments.