Enabled negatively regulates diaphanous-driven actin dynamics in vitro and in vivo. - Wikidata - awgldk - TriplyDB

Enabled negatively regulates diaphanous-driven actin dynamics in vitro and in vivo.

Enabled negatively regulates diaphanous-driven actin dynamics in vitro and in vivo.

http://www.wikidata.org/entity/Q37712462

about

Unravelling the Actin Cytoskeleton: A New Competitive Edge?Cell type-dependent mechanisms for formin-mediated assembly of filopodia.Profilin-1 serves as a gatekeeper for actin assembly by Arp2/3-dependent and -independent pathways.Topographic Cues Reveal Two Distinct Spreading Mechanisms in Blood Platelets.The actin regulators Enabled and Diaphanous direct distinct protrusive behaviors in different tissues during Drosophila development.The alternatively-included 11a sequence modifies the effects of Mena on actin cytoskeletal organization and cell behavior Loss of Gα12/13 exacerbates apical area dependence of actomyosin contractility.Ena/VASP regulates mDia2-initiated filopodial length, dynamics, and function.Lamellipodin promotes actin assembly by clustering Ena/VASP proteins and tethering them to actin filaments.Crumbs is an essential regulator of cytoskeletal dynamics and cell-cell adhesion during dorsal closure in Drosophila.Vasodilator-stimulated phosphoprotein restricts cell-to-cell spread of Shigella flexneri at the cell periphery Diaphanous regulates SCAR complex localization during Drosophila myoblast fusion.CellGeo: a computational platform for the analysis of shape changes in cells with complex geometries.Macrophage Functions in Tissue Patterning and Disease: New Insights from the Fly.Drosophila blood cell chemotaxis Self-organization of protrusions and polarity during eukaryotic chemotaxis.Filopodyan: An open-source pipeline for the analysis of filopodia.Visualization of Actin Assembly and Filament Turnover by In Vitro Multicolor TIRF Microscopy.Modulation of formin processivity by profilin and mechanical tension.Computational modeling highlights the role of the disordered Formin Homology 1 domain in profilin-actin transfer.

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Enabled negatively regulates diaphanous-driven actin dynamics in vitro and in vivo.

http://www.wikidata.org/entity/Q37712462

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on February 2014

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Enabled negatively regulates diaphanous-driven actin dynamics in vitro and in vivo.

@en

Enabled negatively regulates diaphanous-driven actin dynamics in vitro and in vivo.

@nl

type

label

Enabled negatively regulates diaphanous-driven actin dynamics in vitro and in vivo.

@en

Enabled negatively regulates diaphanous-driven actin dynamics in vitro and in vivo.

@nl

prefLabel

Enabled negatively regulates diaphanous-driven actin dynamics in vitro and in vivo.

@en

Enabled negatively regulates diaphanous-driven actin dynamics in vitro and in vivo.

@nl

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P356

J.DEVCEL.2014.01.015

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Developmental Cell

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Enabled negatively regulates diaphanous-driven actin dynamics in vitro and in vivo.

@en

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Colleen G Bilancia

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

David R Kovar

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Jennifer A Sees

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

Jonathan D Winkelman

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

Kate Comber

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Stephanie H Nowotarski

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

Timothy C Elston

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Vinal Lakhani

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

P2860

A conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilin

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

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

Formins at a glance

Novel roles of formin mDia2 in lamellipodia and filopodia formation in motile cells

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

Displacement of formins from growing barbed ends by bud14 is critical for actin cable architecture and function.

Role of formins in actin assembly: nucleation and barbed-end association.

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394-408

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scholarly article

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10.1016/J.DEVCEL.2014.01.015

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4

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28

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Iwan Robert Evans

Denis Tsygankov

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2014-02-01T00:00:00Z

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260429835

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24576424

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3992947

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