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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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Journal ArticleDOI
Ubiquitin-Dependent Modification of Skeletal Muscle by the Parasitic Nematode, Trichinella spiralis
Rhiannon R. White,Amy H. Ponsford,Michael P. Weekes,Rachel B. Rodrigues,David B. Ascher,Marco Mol,Murray E. Selkirk,Steven P. Gygi,Christopher M. Sanderson,Katerina Artavanis-Tsakonas,Katerina Artavanis-Tsakonas +10 more
TL;DR: These findings demonstrate the first example of host-parasite interactions via a parasite-derived Ub conjugating enzyme; an E2 that demonstrates a novel muscle protein stabilization function.
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High error rates in selenocysteine insertion in mammalian cells treated with the antibiotic doxycycline, chloramphenicol, or geneticin.
Ryuta Tobe,Salvador Naranjo-Suarez,Robert A. Everley,Bradley A. Carlson,Anton A. Turanov,Petra A. Tsuji,Min-Hyuk Yoo,Steven P. Gygi,Vadim N. Gladyshev,Dolph L. Hatfield +9 more
TL;DR: The data reveal widespread errors in inserting Sec into proteins and in dysregulation of selenoprotein expression and function upon antibiotic treatment, which is specific to mammalian cells in culture.
Journal ArticleDOI
Activation of PASK by mTORC1 is required for the onset of the terminal differentiation program.
Chintan K. Kikani,Xiaoying Wu,Sarah Fogarty,Seong A. Kang,Noah Dephoure,Steven P. Gygi,David M. Sabatini,Jared Rutter +7 more
TL;DR: A growth factor and nutrient-stimulated pathway, whereby mammalian target of rapamycin (mTOR) activates Per–Arnt–Sim domain kinase (PASK) protein kinase in muscle stem cells is described, showing that phosphorylation of PASK by mTORC1 is required for the activation of myogenin transcription, exit from self-renewal, and induction of the myogenesis program.
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Loss of the deubiquitinase USP36 destabilizes the RNA helicase DHX33 and causes preimplantation lethality in mice
Julia M. Fraile,Diana Campos-Iglesias,Francisco Rodríguez,Aurora Astudillo,Roser Vilarrasa-Blasi,Núria Verdaguer-Dot,Miguel A. Prado,Joao A. Paulo,Steven P. Gygi,José I. Martín-Subero,José M.P. Freije,Carlos López-Otín +11 more
TL;DR: It is shown that Usp36 depletion is lethal in preimplantation mouse embryos, where it blocks the transition from morula to blastocyst during embryonic development, and that reducing DHX33 levels through short hairpin RNA interference has the same effect.
Journal ArticleDOI
CD22 is a functional ligand for SH2 domain-containing protein-tyrosine phosphatase-1 in primary T cells
Jean G. Sathish,Jenna Walters,Jincai Luo,Kenneth G. Johnson,Frances Gertrude LeRoy,Paul Brennan,Kwang P. Kim,Steven P. Gygi,Benjamin G. Neel,R. James Matthews +9 more
TL;DR: CD22 is confirmed to be a T cell ligand for the SHP-1 SH2 domains and the co-engagement of CD3 and CD22 results in a raising of TCR signaling thresholds hence demonstrating a previously unsuspected functional role for CD22 in primary T cells.