Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity - Wikidata - awgldk - TriplyDB

Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity

Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity

http://www.wikidata.org/entity/Q24630138

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Mammalian Fat1 cadherin regulates actin dynamics and cell-cell contact The intracellular domain of the human protocadherin hFat1 interacts with Homer signalling scaffolding proteins GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta A WASp-VASP complex regulates actin polymerization at the plasma membrane.Actin-based motility of intracellular microbial pathogens Clustering of VASP actively drives processive, WH2 domain-mediated actin filament elongation.Crystal structure of Dcp1p and its functional implications in mRNA decapping The solution structure of pGolemi, a high affinity Mena EVH1 binding miniature protein, suggests explanations for paralog-specific binding to Ena/VASP homology (EVH) 1 domains A direct interaction between DCP1 and XRN1 couples mRNA decapping to 5' exonucleolytic degradation Arp2/3 complex requires hydrolyzable ATP for nucleation of new actin filaments A modular toolkit to inhibit proline-rich motif-mediated protein-protein interactions.The structure and function of proline recognition domains.5'-Inositol phosphatase SHIP2 recruits Mena to stabilize invadopodia for cancer cell invasion.Contextual specificity in peptide-mediated protein interactions.Pax6-dependent Shroom3 expression regulates apical constriction during lens placode invagination Ena/VASP regulates mDia2-initiated filopodial length, dynamics, and function.EVH1 domains: structure, function and interactions.Ena/VASP proteins cooperate with the WAVE complex to regulate the actin cytoskeleton.Dcp1 links coactivators of mRNA decapping to Dcp2 by proline recognition.Zyxin is a transforming growth factor-β (TGF-β)/Smad3 target gene that regulates lung cancer cell motility via integrin α5β1.Cytoskeleton assembly at endothelial cell-cell contacts is regulated by alphaII-spectrin-VASP complexes.VASP increases hepatic fatty acid oxidation by activating AMPK in mice.Cellulose-bound peptide arrays: preparation and applications.Fat3 and Ena/VASP proteins influence the emergence of asymmetric cell morphology in the developing retina Protein kinase G as a therapeutic target for the treatment of metastatic colorectal cancer.Protein kinase D1-mediated phosphorylations regulate vasodilator-stimulated phosphoprotein (VASP) localization and cell migration Miniature protein ligands for EVH1 domains: interplay between affinity, specificity, and cell motility Adapter protein SH2B1beta cross-links actin filaments and regulates actin cytoskeleton Diversity of polyproline recognition by EVH1 domains.Differential VASP phosphorylation controls remodeling of the actin cytoskeleton.Enabled negatively regulates diaphanous-driven actin dynamics in vitro and in vivo.Polyproline and triple helix motifs in host-pathogen recognition.ActA of Listeria monocytogenes and Its Manifold Activities as an Important Listerial Virulence Factor.Yersinia protein kinase A phosphorylates vasodilator-stimulated phosphoprotein to modify the host cytoskeleton.Hyperphosphorylation of microfilament-associated proteins is involved in microcystin-LR-induced toxicity in HL7702 cells.Identification of a pivotal endocytosis motif in c-Met and selective modulation of HGF-dependent aggressiveness of cancer using the 16-mer endocytic peptide.Structure-based synthetic mimicry of discontinuous protein binding sites: inhibitors of the interaction of Mena EVH1 domain with proline-rich ligands.Functional analysis of type 1alpha cGMP-dependent protein kinase using green fluorescent fusion proteins.Regulation of VASP by phosphorylation: consequences for cell migration.Abl-1-bridged tyrosine phosphorylation of VASP by Abelson kinase impairs association of VASP to focal adhesions and regulates leukaemic cell adhesion.

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Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity

http://www.wikidata.org/entity/Q24630138

description

2000 nî lūn-bûn

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2000 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2000 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2000年の論文

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2000年論文

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2000年論文

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Dual epitope recognition by th ...... ecificity and binding affinity

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Dual epitope recognition by th ...... ecificity and binding affinity

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Dual epitope recognition by th ...... ecificity and binding affinity

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The EMBO Journal

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Dual epitope recognition by th ...... ecificity and binding affinity

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A Häfner

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B Hoffmann

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J Schneider-Mergener

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U Walter

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P2860

Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP

The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the proline-rich domain in vinculin

A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family.

A novel bacterial virulence gene in Listeria monocytogenes required for host cell microfilament interaction with homology to the proline-rich region of vinculin

Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein)

The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins

Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly

Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function

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18

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19

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Hartmut Oschkinat

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232799204

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10990454

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314220

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