scispace - formally typeset
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.

Papers
More filters
Journal ArticleDOI

Defining the consequences of genetic variation on a proteome-wide scale

TL;DR: A multiplexed, mass spectrometry-based method for protein quantification with an emerging outbred mouse model containing extensive genetic variation from eight inbred founder strains identifies 2,866 protein quantitative trait loci (pQTL) with twice as many local as distant genetic variants.
Journal ArticleDOI

Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities.

TL;DR: A proteasome-dependent conjugating activity of Hul5 is reported that endows proteasomes with the capacity to extend ubiquitin chains and proposes that through dynamic remodeling of ubiquit in chains, prote asomes actively regulate substrate commitment to degradation.
Journal ArticleDOI

Proteome analysis of low-abundance proteins using multidimensional chromatography and isotope-coded affinity tags.

TL;DR: It is demonstrated that the combination of isotope coded affinity protein tags and multidimensional chromatography/mass spectrometry of tryptic peptide mixtures is capable of detecting and quantifying proteins of low abundance in complex samples.
Journal ArticleDOI

A function for cyclin D1 in DNA repair uncovered by protein interactome analyses in human cancers

TL;DR: Reduction of cyclin D1 levels in human cancer cells impaired recruitment of RAD51 to damaged DNA, impeded the homologous recombination-mediated DNA repair, and increased sensitivity of cells to radiation in vitro and in vivo, revealing an unexpected function of a core cell cycle protein in DNA repair.