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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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Tome-1, a trigger of mitotic entry, is degraded during G1 via the APC

TL;DR: Tome-1 appears to be acting as part of an SCF-type E3 for wee1, providing a critical link between the APC and SCF pathways in regulation of cdk1/cyclin B activity and thus mitotic entry and exit.
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Phosphorylation by Casein Kinase I promotes the turnover of the Mdm2 oncoprotein via the SCFβ-TRCP ubiquitin ligase

TL;DR: It is reported that Mdm2 is rapidly degraded after DNA damage and that phosphorylation of MDM2 by casein kinase I (CKI) at multiple sites triggers its interaction with, and subsequent ubiquitination and destruction, by SCF(beta-TRCP).
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A SIRT1-LSD1 Corepressor Complex Regulates Notch Target Gene Expression and Development

TL;DR: A SIRT1 corepressor complex containing the histone H3K4 demethylase LSD1/KDM1A and several other LSD1-associated proteins is described, offering new insights into conserved mechanisms of epigenetic gene repression and regulation of development by Sirt1 in metazoans.
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A novel role for RIP1 kinase in mediating TNFα production

TL;DR: A novel role for RIP1 kinase in regulating TNFα production after caspase inhibition is proposed and this pathway is independent of nuclear factor κB and also occurs after Smac mimetic/IAP antagonist treatment or the loss of TNF receptor-associated factor 2 (Traf2).
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Chaperone-mediated pathway of proteasome regulatory particle assembly

TL;DR: It is shown that in the yeast Saccharomyces cerevisiae three proteins are found associated with RP but not with the RP–CP holoenzyme: Nas6, Rpn14 and Hsm3 are RP chaperones, and it is shown in an accompanying study that RP assembly is templated through the Rpt C termini, apparently by their insertion into binding pockets in the CP.