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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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Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is required for DNA repair

TL;DR: SLX4 assembles a modular toolkit for repair of specific types of DNA lesions and is critical for cellular responses to replication fork failure, and is identified as the human ortholog of the budding yeast DNA repair factor Slx4p and D. melanogaster MUS312.
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Human ISG15 conjugation targets both IFN-induced and constitutively expressed proteins functioning in diverse cellular pathways

TL;DR: Results indicate that ISG15 conjugation impacts nuclear as well as cytoplasmic functions and targeting a wide array of constitutively expressed proteins greatly extends the repertoire of cellular functions that are affected by IFN-alpha/beta.
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CHIP-Hsc70 Complex Ubiquitinates Phosphorylated Tau and Enhances Cell Survival

TL;DR: It is shown that Alzheimer tau binds to Hsc70, and its phosphorylation is a recognition requirement for the addition of ubiquitin (Ub) by the E3 Ub ligase CHIP and the E2 conjugating enzyme UbcH5B, and therefore the CHIP-Hsc70 complex may provide a new therapeutic target for the tauopathies.
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Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology

TL;DR: A reconstituted system and quantitative mass spectrometry are used to demonstrate that cyclin B1 is modified by ubiquitin chains of complex topology, rather than by homogeneous Lys 48-linked chains, and provide unique insights into the mechanisms of substrate ubiquitination.
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Toca-1 Mediates Cdc42-Dependent Actin Nucleation by Activating the N-WASP-WIP Complex

TL;DR: The biochemical purification of Toca-1 (transducer of CDC42-dependent actin assembly) is described as an essential component of the Cdc42 pathway and shed light on the pathogenesis of Wiskott-Aldrich syndrome.