Oligomerization of signaling complexes by the multipoint binding of GRB2 to both LAT and SOS1 (Q24299715)

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Language	Label	Description	Also known as
English	Oligomerization of signaling complexes by the multipoint binding of GRB2 to both LAT and SOS1	scientific article

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scholarly article

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Oligomerization of signaling complexes by the multipoint binding of GRB2 to both LAT and SOS1 (English)

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SOS Ras/Rac guanine nucleotide exchange factor 1

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GOA release 2020-03-11

6

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Mira Barda-Saad

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object named as

Mira Barda-Saad

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object named as

Peter Schuck

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author name string

Jon C D Houtman

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Alex Braiman

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Brent Bowden

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Lawrence E Samelson

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Hiroshi Yamaguchi

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language of work or name

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publication date

September 2006

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Nature Structural & Molecular Biology

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13

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9

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798-805

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Ligand-induced, receptor-mediated dimerization and activation of EGF receptor

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Assembly of Cell Regulatory Systems Through Protein Interaction Domains

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NMR structure of the N-terminal SH3 domain of GRB2 and its complex with a proline-rich peptide from Sos

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The Grb2-mSos1 complex binds phosphopeptides with higher affinity than Grb2

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The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1

1 reference

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Association of Grb2, Gads, and phospholipase C-gamma 1 with phosphorylated LAT tyrosine residues. Effect of LAT tyrosine mutations on T cell angigen receptor-mediated signaling

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Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation

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Molecular mechanisms of cytokine receptor activation

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G protein-coupled receptor oligomerization: implications for G protein activation and cell signaling

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The role of Grb2-associated proteins in T-cell activation

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Signal transduction mediated by the T cell antigen receptor: the role of adapter proteins

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Minimal requirement of tyrosine residues of linker for activation of T cells in TCR signaling and thymocyte development.

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Studying multiprotein complexes by multisignal sedimentation velocity analytical ultracentrifugation

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Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling

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Binding specificity of multiprotein signaling complexes is determined by both cooperative interactions and affinity preferences

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Sedimentation velocity analysis of heterogeneous protein-protein interactions: Lamm equation modeling and sedimentation coefficient distributions c(s)

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T cell receptor ligation induces the formation of dynamically regulated signaling assemblies

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High resolution mapping of mast cell membranes reveals primary and secondary domains of Fc(epsilon)RI and LAT.

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Dynamic changes in the mobility of LAT in aggregated lipid rafts upon T cell activation

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Lipid raft domains and protein networks in T-cell receptor signal transduction

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Human Sos1: a guanine nucleotide exchange factor for Ras that binds to GRB2

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Crystal structure of the mammalian Grb2 adaptor

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Solution structure of Grb2 reveals extensive flexibility necessary for target recognition

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Design of peptoid analogue dimers and measure of their affinity for Grb2 SH3 domains.

1 reference

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LAT regulates gammadelta T cell homeostasis and differentiation

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Trafficking of the ErbB receptors and its influence on signaling

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Internalization of the epidermal growth factor receptor: role in signalling

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ITC in the post-genomic era...? Priceless

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Boundary Problems in the Sedimentation and Electrophoresis of Complex Systems in Rapid Reversible Equilibrium

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10.1038/NSMB1133

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Consolidated OpenCitations Corpus – April 2017

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OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

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