G
Gerry Gish
Researcher at Mount Sinai Hospital
Publications - 4
Citations - 2553
Gerry Gish is an academic researcher from Mount Sinai Hospital. The author has contributed to research in topics: SH2 domain & Binding site. The author has an hindex of 4, co-authored 4 publications receiving 2475 citations.
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Journal ArticleDOI
Backbone Dynamics of a Free and a Phosphopeptide-Complexed Src Homology 2 Domain Studied by 15N NMR Relaxation
Neil A. Farrow,Ranjith Muhandiram,Alex U. Singer,Steven M. Pascal,Cyril M. Kay,Gerry Gish,Steven E. Shoelson,Tony Pawson,Julie D. Forman-Kay,Lewis E. Kay +9 more
TL;DR: Overall, higher order parameters were not found in the peptide-bound form, indicating that on average, picosecond-time-scale disorder is not reduced upon binding peptide, and the relaxation data of the SH2-phosphopeptide complex were fit with fewer exchange terms than the uncomplexed form.
Journal ArticleDOI
Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide.
Steven M. Pascal,Alex U. Singer,Gerry Gish,Toshio Yamazaki,Steven E. Shoelson,Steven E. Shoelson,Tony Pawson,Lewis E. Kay,Julie D. Forman-Kay +8 more
TL;DR: The solution structure of the C-terminal SH2 domain of phospholipase C-Gamma 1 (PLC-gamma 1), in complex with a phosphopeptide corresponding to its Tyr-1021 high affinity binding site on the platelet-derived growth factor receptor, has been determined by nuclear magnetic resonance spectroscopy.
Journal Article
Regulation of c-Src tyrosine kinase activity by the Src SH2 domain.
TL;DR: Data provide direct evidence that the c-Src tail has an intrinsic affinity for the Src SH2 domain, and suggest that such an interaction in the intact molecule contributes to maintaining c- Src in an inactive form.
Journal Article
Identification of residues in the beta platelet-derived growth factor receptor that confer specificity for binding to phospholipase C-gamma 1.
TL;DR: Results indicate that phosphorylation at Tyr-1021 in the tail of the PDGFR creates a specific binding site for PLC-gamma 1, suggesting that additional residues other than the three residues immediately following the phosphotyrosine may contribute to the association of P LC-Gamma 1 with thePDGFR.