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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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Hexameric assembly of the proteasomal ATPases is templated through their C termini

TL;DR: This work identifies a previously unknown function of the Rpt proteins in proteasome biogenesis through deleting the C-terminal residue from each Rpt in the yeast Saccharomyces cerevisiae, and proposes that Rpt4 and Rpt6 form a nucleating complex to initiate base assembly, and that this complex is subsequently joined by BP1 to complete the RPT ring.
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The Tumor Suppressor DAP Kinase Is a Target of RSK-Mediated Survival Signaling

TL;DR: The results suggest that RSK-mediated phosphorylation of DAPK is a unique mechanism for suppressing the proapoptotic function of this death kinase in healthy cells as well as Ras/Raf-transformed cells.
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APC/C-mediated multiple monoubiquitylation provides an alternative degradation signal for cyclin B1.

TL;DR: It is demonstrated that multiple monoubiquitylation of cyclin B1, catalysed by UBCH10 or UBC4/5, is sufficient to target cyclinB1 for destruction by the proteasome.
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A Triple Knockout (TKO) Proteomics Standard for Diagnosing Ion Interference in Isobaric Labeling Experiments.

TL;DR: The need to investigate further ion interference-generated ratio distortion and promote the TKO standard as a tool to investigate such issues is emphasized.
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QIL1 is a novel mitochondrial protein required for MICOS complex stability and cristae morphology

TL;DR: Using quantitative proteomics, this work uncovers a previously unrecognized subunit of the MICOS complex, necessary for CJ integrity, cristae morphology, and mitochondrial function and provides a resource for further analysis of MICOS architecture.