The Tiam1 PDZ domain couples to Syndecan1 and promotes cell-matrix adhesion
about
Syndecans as Cell Surface Receptors in Cancer Biology. A Focus on their Interaction with PDZ Domain ProteinsA quasi-exclusive European ancestry in the Senepol tropical cattle breed highlights the importance of the slick locus in tropical adaptationStereochemical Determinants of C-terminal Specificity in PDZ Peptide-binding Domains: A NOVEL CONTRIBUTION OF THE CARBOXYLATE-BINDING LOOPThe Structure of the Tiam1 PDZ Domain/ Phospho-Syndecan1 Complex Reveals a Ligand Conformation that Modulates Protein DynamicsThe invasive capacity of HPV transformed cells requires the hDlg-dependent enhancement of SGEF/RhoG activity.Distinct ligand specificity of the Tiam1 and Tiam2 PDZ domainsStructural and thermodynamic analysis of PDZ-ligand interactions.Cytoplasmic domain interactions of syndecan-1 and syndecan-4 with α6β4 integrin mediate human epidermal growth factor receptor (HER1 and HER2)-dependent motility and survival.Identification of amino acid residues important for heparan sulfate proteoglycan interaction within variable region 3 of the feline immunodeficiency virus surface glycoprotein.A novel pathway spatiotemporally activates Rac1 and redox signaling in response to fluid shear stressDeconstructing signal transduction pathways that regulate the actin cytoskeleton in dendritic spines.Uncovering new aspects of protein interactions through analysis of specificity landscapes in peptide recognition domains.Syndecan and integrin interactomes: large complexes in small spaces.A cytoplasmic C-terminal fragment of Syndecan-1 is generated by sequential proteolysis and antagonizes Syndecan-1 dependent lung tumor cell migration.Distinct Roles for Conformational Dynamics in Protein-Ligand Interactions.A Simple PB/LIE Free Energy Function Accurately Predicts the Peptide Binding Specificity of the Tiam1 PDZ DomainThe phosphomimetic mutation of syndecan-4 binds and inhibits Tiam1 modulating Rac1 activity in PDZ interaction-dependent manner.The Tiam1 guanine nucleotide exchange factor is auto-inhibited by its pleckstrin homology coiled-coil extension domain.Accurate PDZ/Peptide Binding Specificity with Additive and Polarizable Free Energy Simulations.
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P2860
The Tiam1 PDZ domain couples to Syndecan1 and promotes cell-matrix adhesion
description
2010 nî lūn-bûn
@nan
2010 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մարտին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
The Tiam1 PDZ domain couples to Syndecan1 and promotes cell-matrix adhesion
@ast
The Tiam1 PDZ domain couples to Syndecan1 and promotes cell-matrix adhesion
@en
The Tiam1 PDZ domain couples to Syndecan1 and promotes cell-matrix adhesion
@en-gb
The Tiam1 PDZ domain couples to Syndecan1 and promotes cell-matrix adhesion
@nl
type
label
The Tiam1 PDZ domain couples to Syndecan1 and promotes cell-matrix adhesion
@ast
The Tiam1 PDZ domain couples to Syndecan1 and promotes cell-matrix adhesion
@en
The Tiam1 PDZ domain couples to Syndecan1 and promotes cell-matrix adhesion
@en-gb
The Tiam1 PDZ domain couples to Syndecan1 and promotes cell-matrix adhesion
@nl
prefLabel
The Tiam1 PDZ domain couples to Syndecan1 and promotes cell-matrix adhesion
@ast
The Tiam1 PDZ domain couples to Syndecan1 and promotes cell-matrix adhesion
@en
The Tiam1 PDZ domain couples to Syndecan1 and promotes cell-matrix adhesion
@en-gb
The Tiam1 PDZ domain couples to Syndecan1 and promotes cell-matrix adhesion
@nl
P2093
P2860
P1476
The Tiam1 PDZ domain couples to Syndecan1 and promotes cell-matrix adhesion
@en
P2093
Kris A DeMali
S Ramaswamy
Suzi M Klaus
P2860
P304
P356
10.1016/J.JMB.2010.03.047
P407
P577
2010-03-31T00:00:00Z