Binding specificity of multiprotein signaling complexes is determined by both cooperative interactions and affinity preferences.
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Efficient T-cell receptor signaling requires a high-affinity interaction between the Gads C-SH3 domain and the SLP-76 RxxK motifOligomerization of signaling complexes by the multipoint binding of GRB2 to both LAT and SOS1Cooperative interactions at the SLP-76 complex are critical for actin polymerizationp53 and TFIIEalpha share a common binding site on the Tfb1/p62 subunit of TFIIHCD6 regulates T-cell responses through activation-dependent recruitment of the positive regulator SLP-76Structural basis for recognition of centromere histone variant CenH3 by the chaperone Scm3Structural and functional evidence that Rad4 competes with Rad2 for binding to the Tfb1 subunit of TFIIH in NERStructural Basis for Activation of ZAP-70 by Phosphorylation of the SH2-Kinase LinkerStructural and functional characterization of interactions involving the Tfb1 subunit of TFIIH and the NER factor Rad2Structural and Functional Characterization of a Complex between the Acidic Transactivation Domain of EBNA2 and the Tfb1/p62 Subunit of TFIIHSLP76 and SLP65: complex regulation of signalling in lymphocytes and beyondQuantifying intramolecular binding in multivalent interactions: a structure-based synergistic study on Grb2-Sos1 complexPhosphorylation site dynamics of early T-cell receptor signalingRegions outside of conserved PxxPxR motifs drive the high affinity interaction of GRB2 with SH3 domain ligandsGRB2 Nucleates T Cell Receptor-Mediated LAT Clusters That Control PLC-γ1 Activation and Cytokine Production.Studies of novel interactions between Nck and VAV SH3 domains.Competition between SLP76 and LAT for PLCγ1 binding in resting T cells.Nck adapter proteins: functional versatility in T cellsThe phosphotyrosine peptide binding specificity of Nck1 and Nck2 Src homology 2 domains.T cell receptor-induced activation of phospholipase C-gamma1 depends on a sequence-independent function of the P-I region of SLP-76.Persistence of cooperatively stabilized signaling clusters drives T-cell activationF-actin polymerization and retrograde flow drive sustained PLCγ1 signaling during T cell activationPhosphotyrosine-mediated LAT assembly on membranes drives kinetic bifurcation in recruitment dynamics of the Ras activator SOS.T Cell Costimulation by CD6 Is Dependent on Bivalent Binding of a GADS/SLP-76 Complex.Receptor-stimulated oxidation of SHP-2 promotes T-cell adhesion through SLP-76-ADAPModeling and simulation of aggregation of membrane protein LAT with molecular variability in the number of binding sites for cytosolic Grb2-SOS1-Grb2.Sedimentation velocity analysis of heterogeneous protein-protein interactions: Lamm equation modeling and sedimentation coefficient distributions c(s)Early phosphorylation kinetics of proteins involved in proximal TCR-mediated signaling pathways.Examining multiprotein signaling complexes from all anglesThe ability of Sos1 to oligomerize the adaptor protein LAT is separable from its guanine nucleotide exchange activity in vivo.A conserved amphipathic helix in the N-terminal regulatory region of the papillomavirus E1 helicase is required for efficient viral DNA replication.In silico modeling of Itk activation kinetics in thymocytes suggests competing positive and negative IP4 mediated feedbacks increase robustness.Endocytic events in TCR signaling: focus on adapters in microclustersAn Interaction Library for the FcεRI Signaling NetworkA novel pathway down-modulating T cell activation involves HPK-1-dependent recruitment of 14-3-3 proteins on SLP-76.The linker for activation of T cells (LAT) signaling hub: from signaling complexes to microclustersOrigin of the sharp boundary that discriminates positive and negative selection of thymocytesAggregation of membrane proteins by cytosolic cross-linkers: theory and simulation of the LAT-Grb2-SOS1 systemMultipoint binding of the SLP-76 SH2 domain to ADAP is critical for oligomerization of SLP-76 signaling complexes in stimulated T cells.An electrostatic selection mechanism controls sequential kinase signaling downstream of the T cell receptor.
P2860
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P2860
Binding specificity of multiprotein signaling complexes is determined by both cooperative interactions and affinity preferences.
description
2004 nî lūn-bûn
@nan
2004 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Binding specificity of multipr ...... ions and affinity preferences.
@ast
Binding specificity of multipr ...... ions and affinity preferences.
@en
type
label
Binding specificity of multipr ...... ions and affinity preferences.
@ast
Binding specificity of multipr ...... ions and affinity preferences.
@en
prefLabel
Binding specificity of multipr ...... ions and affinity preferences.
@ast
Binding specificity of multipr ...... ions and affinity preferences.
@en
P2093
P50
P356
P1433
P1476
Binding specificity of multipr ...... ions and affinity preferences.
@en
P2093
Brent Bowden
Carole Regan
Ettore Appella
Hiroshi Yamaguchi
Jon C D Houtman
Lawrence E Samelson
Nazzareno Dimasi
Roy Mariuzza
Sangwoo Cho
P304
P356
10.1021/BI0357311
P407
P577
2004-04-01T00:00:00Z