Defining the specificity space of the human SRC homology 2 domain
about
The conservation pattern of short linear motifs is highly correlated with the function of interacting protein domainsSRC Homology 2 Domain Binding Sites in Insulin, IGF-1 and FGF receptor mediated signaling networks reveal an extensive potential interactomeEnhanced prediction of Src homology 2 (SH2) domain binding potentials using a fluorescence polarization-derived c-Met, c-Kit, ErbB, and androgen receptor interactomeSequential phosphorylation of SLP-76 at tyrosine 173 is required for activation of T and mast cellsThe Tensin-3 protein, including its SH2 domain, is phosphorylated by Src and contributes to tumorigenesis and metastasisContributions of F-BAR and SH2 domains of Fes protein tyrosine kinase for coupling to the FcepsilonRI pathway in mast cells.Phospho-tyrosine dependent protein-protein interaction networkThe development and application of a quantitative peptide microarray based approach to protein interaction domain specificity spaceAn evolutionary perspective on the kinome of malaria parasitesShort linear motifs - ex nihilo evolution of protein regulationStructural Basis for c-KIT Inhibition by the Suppressor of Cytokine Signaling 6 (SOCS6) Ubiquitin LigaseStructure of Lipid Kinase p110β/p85β Elucidates an Unusual SH2-Domain-Mediated Inhibitory MechanismTwo Closely Spaced Tyrosines Regulate NFAT Signaling in B Cells via Syk Association with VavSimultaneous Binding of Two Peptidyl Ligands by a Src Homology 2 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 signalingTwo Amino Acid Residues Confer Different Binding Affinities of Abelson Family Kinase Src Homology 2 Domains for Phosphorylated CortactinStructural basis for a novel interaction between TXNIP and Vav2High-throughput analysis of peptide-binding modulesPhosphotyrosine signaling proteins that drive oncogenesis tend to be highly interconnectedA specific A/T polymorphism in Western tyrosine phosphorylation B-motifs regulates Helicobacter pylori CagA epithelial cell interactionsTime-resolved multimodal analysis of Src Homology 2 (SH2) domain binding in signaling by receptor tyrosine kinasesSH2 Domains Recognize Contextual Peptide Sequence Information to Determine SelectivityStructural and biophysical investigation of the interaction of a mutant Grb2 SH2 domain (W121G) with its cognate phosphopeptide.T cell specific adaptor protein (TSAd) promotes interaction of Nck with Lck and SLP-76 in T cells.Iterative tyrosine phosphorylation controls non-canonical domain utilization in Crk.SH3 interactome conserves general function over specific form.Domain-mediated protein interaction prediction: From genome to network.The identification of short linear motif-mediated interfaces within the human interactomeSrc tyrosine kinase phosphorylation of nuclear receptor HNF4α correlates with isoform-specific loss of HNF4α in human colon cancer.Proline isomerization preorganizes the Itk SH2 domain for binding to the Itk SH3 domain.An adaptor role for cytoplasmic Sam68 in modulating Src activity during cell polarization.Spatial exclusivity combined with positive and negative selection of phosphorylation motifs is the basis for context-dependent mitotic signaling.Exploring the pathogenetic association between schizophrenia and type 2 diabetes mellitus diseases based on pathway analysis.Dynamic steps in receptor tyrosine kinase mediated activation of class IA phosphoinositide 3-kinases (PI3K) captured by H/D exchange (HDX-MS).Prediction of phosphotyrosine signaling networks using a scoring matrix-assisted ligand identification approach.On-bead screening of combinatorial libraries: reduction of nonspecific binding by decreasing surface ligand density.Generating a panel of highly specific antibodies to 20 human SH2 domains by phage displayA regression framework incorporating quantitative and negative interaction data improves quantitative prediction of PDZ domain-peptide interaction from primary sequence.Mapping protein interactions by combining antibody affinity maturation and mass spectrometry.
P2860
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P2860
Defining the specificity space of the human SRC homology 2 domain
description
2008 nî lūn-bûn
@nan
2008 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Defining the specificity space of the human SRC homology 2 domain
@ast
Defining the specificity space of the human SRC homology 2 domain
@en
Defining the specificity space of the human SRC homology 2 domain
@nl
type
label
Defining the specificity space of the human SRC homology 2 domain
@ast
Defining the specificity space of the human SRC homology 2 domain
@en
Defining the specificity space of the human SRC homology 2 domain
@nl
prefLabel
Defining the specificity space of the human SRC homology 2 domain
@ast
Defining the specificity space of the human SRC homology 2 domain
@en
Defining the specificity space of the human SRC homology 2 domain
@nl
P2093
P2860
P3181
P1476
Defining the specificity space of the human SRC homology 2 domain
@en
P2093
Chenggang Wu
Chengjun Li
David Schibli
Haiming Huang
Krystina Ho
Protiva Roy
Shawn S-C Li
P2860
P304
P3181
P356
10.1074/MCP.M700312-MCP200
P407
P577
2008-04-01T00:00:00Z