Ena/VASP Enabled is a highly processive actin polymerase tailored to self-assemble parallel-bundled F-actin networks with Fascin - Test2 - elhamkhani - TriplyDB

Ena/VASP Enabled is a highly processive actin polymerase tailored to self-assemble parallel-bundled F-actin networks with Fascin

Ena/VASP Enabled is a highly processive actin polymerase tailored to self-assemble parallel-bundled F-actin networks with Fascin

http://www.wikidata.org/entity/Q30574577

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Unravelling the Actin Cytoskeleton: A New Competitive Edge?Dynamic reorganization of the actin cytoskeleton Capping protein regulators fine-tune actin assembly dynamics The F-actin bundler α-actinin Ain1 is tailored for ring assembly and constriction during cytokinesis in fission yeast VASP, zyxin and TES are tension-dependent members of Focal Adherens Junctions independent of the α-catenin-vinculin module Cell type-dependent mechanisms for formin-mediated assembly of filopodia.Disassembly activity of actin-depolymerizing factor (ADF) is associated with distinct cellular processes in apicomplexan parasites.Profilin-1 serves as a gatekeeper for actin assembly by Arp2/3-dependent and -independent pathways.A biomechanical perspective on stress fiber structure and function WAVE binds Ena/VASP for enhanced Arp2/3 complex-based actin assembly.The actin regulators Enabled and Diaphanous direct distinct protrusive behaviors in different tissues during Drosophila development.Prostaglandins regulate nuclear localization of Fascin and its function in nucleolar architecture.Fascin Rigidity and L-plastin Flexibility Cooperate in Cancer Cell Invadopodia and Filopodia.A requirement for filopodia extension toward Slit during Robo-mediated axon repulsion Ena/VASP regulates mDia2-initiated filopodial length, dynamics, and function.Profilin regulates F-actin network homeostasis by favoring formin over Arp2/3 complex Genome-Wide siRNA Screen Identifies Complementary Signaling Pathways Involved in Listeria Infection and Reveals Different Actin Nucleation Mechanisms during Listeria Cell Invasion and Actin Comet Tail Formation The E3 Ubiquitin Ligase TRIM9 Is a Filopodia Off Switch Required for Netrin-Dependent Axon Guidance.Selectivity in subunit composition of Ena/VASP tetramers.The Strip-Hippo Pathway Regulates Synaptic Terminal Formation by Modulating Actin Organization at the Drosophila Neuromuscular Synapses.Cytoskeletal and signaling mechanisms of neurite formation.Fascin1 in carcinomas: Its regulation and prognostic value.Signaling filopodia in vertebrate embryonic development.ACTIN-DIRECTED TOXIN. ACD toxin-produced actin oligomers poison formin-controlled actin polymerization.Virulent Burkholderia species mimic host actin polymerases to drive actin-based motility.Recent advances in understanding Listeria monocytogenes infection: the importance of subcellular and physiological context.The bacterial virulence factors VopL and VopF nucleate actin from the pointed end.Signalling Pathways Controlling Cellular Actin Organization.Fascin, may the Forked be with you.Mechanoregulated inhibition of formin facilitates contractile actomyosin ring assembly Competition between Tropomyosin, Fimbrin, and ADF/Cofilin drives their sorting to distinct actin filament networks.Fascin- and α-Actinin-Bundled Networks Contain Intrinsic Structural Features that Drive Protein Sorting.Actin-based motility of bacterial pathogens: mechanistic diversity and its impact on virulence.Actin assembly mechanisms at a glance.LlFH1-mediated interaction between actin fringe and exocytic vesicles is involved in pollen tube tip growth.Distinct VASP tetramers synergize in the processive elongation of individual actin filaments from clustered arrays.CRMP-1 enhances EVL-mediated actin elongation to build lamellipodia and the actin cortex.Internetwork competition for monomers governs actin cytoskeleton organization.Partitioning and Enhanced Self-Assembly of Actin in Polypeptide Coacervates.Discovery of functional interactions among actin regulators by analysis of image fluctuations in an unperturbed motile cell system.

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Ena/VASP Enabled is a highly processive actin polymerase tailored to self-assemble parallel-bundled F-actin networks with Fascin

http://www.wikidata.org/entity/Q30574577

description

2014 nî lūn-bûn

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2014 թուականի Մարտին հրատարակուած գիտական յօդուած

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2014 թվականի մարտին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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Ena/VASP Enabled is a highly p ...... d F-actin networks with Fascin

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Ena/VASP Enabled is a highly p ...... d F-actin networks with Fascin

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Ena/VASP Enabled is a highly p ...... d F-actin networks with Fascin

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

P1476

Ena/VASP Enabled is a highly p ...... d F-actin networks with Fascin

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P2093

Colleen G Bilancia

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David R Kovar

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Jonathan D Winkelman

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Mark Peifer

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P2860

Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP.

CDC42 switches IRSp53 from inhibition of actin growth to elongation by clustering of VASP

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

Ena/VASP: towards resolving a pointed controversy at the barbed end

Clustering of VASP actively drives processive, WH2 domain-mediated actin filament elongation.

Ena/VASP proteins enhance actin polymerization in the presence of barbed end capping proteins

Structure of the profilin-poly-L-proline complex involved in morphogenesis and cytoskeletal regulation

Cellular motility driven by assembly and disassembly of actin filaments

Repulsive axon guidance: Abelson and Enabled play opposing roles downstream of the roundabout receptor

The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates tetramerization, F-actin binding, and actin bundle formation

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scholarly article

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11

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111

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2014-03-03T00:00:00Z

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3964058

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