Investigation of phosphotyrosine recognition by the SH2 domain of the Src kinase
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SRC Homology 2 Domain Binding Sites in Insulin, IGF-1 and FGF receptor mediated signaling networks reveal an extensive potential interactomeCsk homologous kinase (CHK) and ErbB-2 interactions are directly coupled with CHK negative growth regulatory function in breast cancerMeasurement of the formation of complexes in tyrosine kinase-mediated signal transductionTwo adaptor proteins differentially modulate the phosphorylation and biophysics of Kv1.3 ion channel by SRC kinaseTargeting SH2 domains in breast cancerA potent and highly specific FN3 monobody inhibitor of the Abl SH2 domainDifferential recognition of syk-binding sites by each of the two phosphotyrosine-binding pockets of the Vav SH2 domainSuperbinder SH2 domains act as antagonists of cell signalingTargeting Class A and C Serine β-Lactamases with a Broad-Spectrum Boronic Acid DerivativeInteraction domains: from simple binding events to complex cellular behaviorHigh-throughput analysis of peptide-binding modulesStructural and biophysical investigation of the interaction of a mutant Grb2 SH2 domain (W121G) with its cognate phosphopeptide.Conformational basis for SH2-Tyr(P)527 binding in Src inactivation.Genome-wide prediction of SH2 domain targets using structural information and the FoldX algorithm.Calculation of absolute protein-ligand binding free energy from computer simulations.Temperature-sensitive transformation by an Abelson virus mutant encoding an altered SH2 domain.Constraining binding hot spots: NMR and molecular dynamics simulations provide a structural explanation for enthalpy-entropy compensation in SH2-ligand bindingPhosphoryltyrosyl mimetics in the design of peptide-based signal transduction inhibitors.Distinct mechanisms of a phosphotyrosyl peptide binding to two SH2 domainsBinding interactions between peptides and proteins of the class II major histocompatibility complex.Absence of p53 complements defects in Abelson murine leukemia virus signalingStability and peptide binding specificity of Btk SH2 domain: molecular basis for X-linked agammaglobulinemiaSrc binds cortactin through an SH2 domain cystine-mediated linkage.Binding specificity of SH2 domains: insight from free energy simulations.Development of Grb2 SH2 Domain Signaling Antagonists: A Potential New Class of Antiproliferative AgentsMultipoint binding of the SLP-76 SH2 domain to ADAP is critical for oligomerization of SLP-76 signaling complexes in stimulated T cells.Structural basis for differential recognition of tyrosine-phosphorylated sites in the linker for activation of T cells (LAT) by the adaptor Gads.SH2 domains: modulators of nonreceptor tyrosine kinase activity.Single-cell imaging of mechanotransduction in endothelial cells.The energetics of phosphate binding to a protein complex.Synthesis of a phosphoserine mimetic prodrug with potent 14-3-3 protein inhibitory activity.Exact analysis of heterotropic interactions in proteins: Characterization of cooperative ligand binding by isothermal titration calorimetry.FRET imaging of calcium signaling in live cells in the microenvironment.Hierarchy of simulation models in predicting molecular recognition mechanisms from the binding energy landscapes: structural analysis of the peptide complexes with SH2 domains.Quantum mechanical binding free energy calculation for phosphopeptide inhibitors of the Lck SH2 domain.Elongin B/C recruitment regulates substrate binding by CIS.Creation of Phosphotyrosine Superbinders by Directed Evolution of an SH2 Domain.Targeting Lyn tyrosine kinase through protein fusions encompassing motifs of Cbp (Csk-binding protein) and the SOCS box of SOCS1.Development of SH2 probes and pull-down assays to detect pathogen-induced, site-specific tyrosine phosphorylation of the TLR adaptor SCIMP.A phosphoarginine containing peptide as an artificial SH2 ligand.
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P2860
Investigation of phosphotyrosine recognition by the SH2 domain of the Src kinase
description
im November 1999 veröffentlichter wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована в листопаді 1999
@uk
name
Investigation of phosphotyrosine recognition by the SH2 domain of the Src kinase
@en
Investigation of phosphotyrosine recognition by the SH2 domain of the Src kinase
@nl
type
label
Investigation of phosphotyrosine recognition by the SH2 domain of the Src kinase
@en
Investigation of phosphotyrosine recognition by the SH2 domain of the Src kinase
@nl
prefLabel
Investigation of phosphotyrosine recognition by the SH2 domain of the Src kinase
@en
Investigation of phosphotyrosine recognition by the SH2 domain of the Src kinase
@nl
P2093
P356
P1476
Investigation of phosphotyrosine recognition by the SH2 domain of the Src kinase
@en
P2093
J M Bradshaw
P304
P356
10.1006/JMBI.1999.3190
P407
P577
1999-11-05T00:00:00Z