Independent binding of peptide ligands to the SH2 and SH3 domains of Grb2
about
SRC Homology 2 Domain Binding Sites in Insulin, IGF-1 and FGF receptor mediated signaling networks reveal an extensive potential interactomeThe beta-subunit of the hepatocyte growth factor/scatter factor (HGF/SF) receptor phosphorylates and associates with CrkII: expression of CrkII enhances HGF/SF-induced mitogenesisInteraction between PAK and nck: a template for Nck targets and role of PAK autophosphorylationTight association of GRB2 with receptor protein-tyrosine phosphatase alpha is mediated by the SH2 and C-terminal SH3 domainsA signaling pathway involving TGF-beta2 and snail in hair follicle morphogenesisStructure of the SOCS4-ElonginB/C Complex Reveals a Distinct SOCS Box Interface and the Molecular Basis for SOCS-Dependent EGFR DegradationThe role of water molecules in the binding of class I and II peptides to the SH3 domain of the Fyn tyrosine kinaseRegions outside of conserved PxxPxR motifs drive the high affinity interaction of GRB2 with SH3 domain ligandsThe SH3 domain of Src tyrosyl protein kinase interacts with the N-terminal splice region of the PDE4A cAMP-specific phosphodiesterase RPDE-6 (RNPDE4A5)Multiple-state reactions between the epidermal growth factor receptor and Grb2 as observed by using single-molecule analysis.Live-cell fluorescence imaging reveals high stoichiometry of Grb2 binding to the EGF receptor sustained during endocytosisSpatio-temporal modeling of signaling protein recruitment to EGFR.Quantitative in vivo fluorescence cross-correlation analyses highlight the importance of competitive effects in the regulation of protein-protein interactionsThermodynamic characterization of the interaction between TRAF2 and tumor necrosis factor receptor peptides by isothermal titration calorimetryGrb2, a double-edged sword of receptor tyrosine kinase signalingThe adaptor protein LAT serves as an integration node for signaling pathways that drive T cell activation.Src homology 2 domains enhance tyrosine phosphorylation in vivo by protecting binding sites in their target proteins from dephosphorylation.Quantifying the Interaction between EGFR Dimers and Grb2 in Live Cells.
P2860
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P2860
Independent binding of peptide ligands to the SH2 and SH3 domains of Grb2
description
1994 nî lūn-bûn
@nan
1994 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Independent binding of peptide ligands to the SH2 and SH3 domains of Grb2
@ast
Independent binding of peptide ligands to the SH2 and SH3 domains of Grb2
@en
Independent binding of peptide ligands to the SH2 and SH3 domains of Grb2
@en-gb
Independent binding of peptide ligands to the SH2 and SH3 domains of Grb2
@nl
type
label
Independent binding of peptide ligands to the SH2 and SH3 domains of Grb2
@ast
Independent binding of peptide ligands to the SH2 and SH3 domains of Grb2
@en
Independent binding of peptide ligands to the SH2 and SH3 domains of Grb2
@en-gb
Independent binding of peptide ligands to the SH2 and SH3 domains of Grb2
@nl
prefLabel
Independent binding of peptide ligands to the SH2 and SH3 domains of Grb2
@ast
Independent binding of peptide ligands to the SH2 and SH3 domains of Grb2
@en
Independent binding of peptide ligands to the SH2 and SH3 domains of Grb2
@en-gb
Independent binding of peptide ligands to the SH2 and SH3 domains of Grb2
@nl
P2093
P1476
Independent binding of peptide ligands to the SH2 and SH3 domains of Grb2
@en
P2093
J E Ladbury
J Schlessinger
M A Lemmon
V Mandiyan
P304
P407
P577
1994-12-16T00:00:00Z