The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat - Wikidata - awgldk - TriplyDB

The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat

The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat

http://www.wikidata.org/entity/Q24558823

about

A generic system for the expression and purification of soluble and stable influenza neuraminidase Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP.Ena/VASP: towards resolving a pointed controversy at the barbed end Ena/VASP proteins enhance actin polymerization in the presence of barbed end capping proteins VASP, zyxin and TES are tension-dependent members of Focal Adherens Junctions independent of the α-catenin-vinculin module Structure determination of the 1918 H1N1 neuraminidase from a crystal with lattice-translocation defects.Structural Characterization of the 1918 Influenza Virus H1N1 Neuraminidase 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 The structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase Structural Insights into the Molecular Mechanisms of Cauliflower Mosaic Virus Transmission by Its Insect Vector Atomic structure of the vimentin central -helical domain and its implications for intermediate filament assembly Rotary ATPases: models, machine elements and technical specifications Molecular Characterizations of Surface Proteins Hemagglutinin and Neuraminidase from Recent H5Nx Avian Influenza Viruses.Fibrous Protein Structures: Hierarchy, History and Heroes.Role of Neuraminidase in Influenza A(H7N9) Virus Receptor Binding Ena/VASP proteins have an anti-capping independent function in filopodia formation.Ena/VASP Enabled is a highly processive actin polymerase tailored to self-assemble parallel-bundled F-actin networks with Fascin Structural and functional analysis of surface proteins from an A(H3N8) influenza virus isolated from New England harbor seals.The VASP-Spred-Sprouty domain puzzle.Collagen-like proteins in pathogenic E. coli strains.VASP is a processive actin polymerase that requires monomeric actin for barbed end association.VASP phosphorylation at serine239 regulates the effects of NO on smooth muscle cell invasion and contraction of collagen Rapid X-ray photoreduction of dimetal-oxygen cofactors in ribonucleotide reductase.Identification of invasion specific splice variants of the cytoskeletal protein Mena present in mammary tumor cells during invasion in vivo.Invasive breast carcinoma cells from patients exhibit MenaINV- and macrophage-dependent transendothelial migration.Dai Huang Fu Zi Tang could ameliorate intestinal injury in a rat model of hemorrhagic shock by regulating intestinal blood flow and intestinal expression of p-VASP and ZO-1.Molecular cloning of hMena (ENAH) and its splice variant hMena+11a: epidermal growth factor increases their expression and stimulates hMena+11a phosphorylation in breast cancer cell lines.Vasodilator-stimulated phosphoprotein (VASP) regulates actin polymerization and contraction in airway smooth muscle by a vinculin-dependent mechanism.Cytoskeleton assembly at endothelial cell-cell contacts is regulated by alphaII-spectrin-VASP complexes.Selectivity in subunit composition of Ena/VASP tetramers.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 Differential VASP phosphorylation controls remodeling of the actin cytoskeleton.Actin filament nucleation and elongation factors--structure-function relationships.Regulation of actin cytoskeleton dynamics in cells.Structural insights into de novo actin polymerization.Metastasis: tumor cells becoming MENAcing.Identification of Residues That Affect Oligomerization and/or Enzymatic Activity of Influenza Virus H5N1 Neuraminidase Proteins.Virulent Burkholderia species mimic host actin polymerases to drive actin-based motility.Crystallographic Studies of Intermediate Filament Proteins.

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The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat

http://www.wikidata.org/entity/Q24558823

description

2004 nî lūn-bûn

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2004 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年论文

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name

The VASP tetramerization domai ...... l based on a 15-residue repeat

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The VASP tetramerization domai ...... l based on a 15-residue repeat

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The VASP tetramerization domai ...... l based on a 15-residue repeat

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The VASP tetramerization domai ...... l based on a 15-residue repeat

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The VASP tetramerization domai ...... l based on a 15-residue repeat

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The VASP tetramerization domai ...... l based on a 15-residue repeat

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The VASP tetramerization domai ...... l based on a 15-residue repeat

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The VASP tetramerization domai ...... l based on a 15-residue repeat

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P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

The VASP tetramerization domai ...... l based on a 15-residue repeat

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P2093

Eva Wolf

http://www.w3.org/2001/XMLSchema#string

Karin Kühnel

http://www.w3.org/2001/XMLSchema#string

Sergei V Strelkov

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Thomas Jarchau

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Ulrich Walter

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P2860

The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain

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.

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

The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel beta-roll

Pivotal role of VASP in Arp2/3 complex-mediated actin nucleation, actin branch-formation, and Listeria monocytogenes motility

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

Improved methods for building protein models in electron density maps and the location of errors in these models

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

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Processing of X-ray diffraction data collected in oscillation mode

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17027-32

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scholarly article

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10.1073/PNAS.0403069101

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49

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P478

101

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Alfred Wittinghofer

Ilme Schlichting

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2004-12-07T00:00:00Z

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P5875

8157526

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15569942

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535362

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