The formin DAD domain plays dual roles in autoinhibition and actin nucleation. - Wikidata - awgldk - TriplyDB

The formin DAD domain plays dual roles in autoinhibition and actin nucleation.

The formin DAD domain plays dual roles in autoinhibition and actin nucleation.

http://www.wikidata.org/entity/Q34683336

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The final cut: cell polarity meets cytokinesis at the bud neck in S. cerevisiae Formins at a glance Structure of the formin-interaction domain of the actin nucleation-promoting factor Bud6 FMNL3 FH2–actin structure gives insight into formin-mediated actin nucleation and elongation Rickettsia Sca2 has evolved formin-like activity through a different molecular mechanism The Bacterial Effector VopL Organizes Actin into Filament-like Structures The F-BAR protein Hof1 tunes formin activity to sculpt actin cables during polarized growth.Ligand-induced activation of a formin-NPF pair leads to collaborative actin nucleation Revisiting the Phylogeny of the Animal Formins: Two New Subtypes, Relationships with Multiple Wing Hairs Proteins, and a Lost Human Formin Rocket launcher mechanism of collaborative actin assembly defined by single-molecule imaging.The formins FMNL1 and mDia1 regulate coiling phagocytosis of Borrelia burgdorferi by primary human macrophages.Cell-cycle regulation of formin-mediated actin cable assembly.An optogenetic tool for the activation of endogenous diaphanous-related formins induces thickening of stress fibers without an increase in contractility The role of formin tails in actin nucleation, processive elongation, and filament bundling.Accelerated actin filament polymerization from microtubule plus ends.Nanostructured self-assembly of inverted formin 2 (INF2) and F-actin-INF2 complexes revealed by atomic force microscopy The C terminus of formin FMNL3 accelerates actin polymerization and contains a WH2 domain-like sequence that binds both monomers and filament barbed ends INF2-mediated severing through actin filament encirclement and disruption.Structure and function of the interacting domains of Spire and Fmn-family formins Cytoskeletal proteins in cortical development and disease: actin associated proteins in periventricular heterotopia.The functionally distinct fission yeast formins have specific actin-assembly properties.Mechanism and cellular function of Bud6 as an actin nucleation-promoting factor.Differential interactions of the formins INF2, mDia1, and mDia2 with microtubules.Structure of a Bud6/Actin Complex Reveals a Novel WH2-like Actin Monomer Recruitment Motif Z-line formins promote contractile lattice growth and maintenance in striated muscles of C. elegans.A specific FMNL2 isoform is up-regulated in invasive cells Formin DAAM1 Organizes Actin Filaments in the Cytoplasmic Nodal Actin Network.Autoinhibition of the formin Cappuccino in the absence of canonical autoinhibitory domains.Mutations to the formin homology 2 domain of INF2 protein have unexpected effects on actin polymerization and severing.Regulation of the formin Bnr1 by septins anda MARK/Par1-family septin-associated kinase.Drosophila homologues of adenomatous polyposis coli (APC) and the formin diaphanous collaborate by a conserved mechanism to stimulate actin filament assembly.The WH2 Domain and Actin Nucleation: Necessary but Insufficient Actin monomers activate inverted formin 2 by competing with its autoinhibitory interaction.INF2- and FHOD-related formins promote ovulation in the somatic gonad of C. elegans Interaction between microtubules and the Drosophila formin Cappuccino and its effect on actin assembly.Essential and nonredundant roles for Diaphanous formins in cortical microtubule capture and directed cell migration.Enabled negatively regulates diaphanous-driven actin dynamics in vitro and in vivo.Structural features and interfacial properties of WH2, β-thymosin domains and other intrinsically disordered domains in the regulation of actin cytoskeleton dynamics.Bacterial subversion of host cytoskeletal machinery: hijacking formins and the Arp2/3 complex.Formins as effector proteins of Rho GTPases

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The formin DAD domain plays dual roles in autoinhibition and actin nucleation.

http://www.wikidata.org/entity/Q34683336

description

2011 nî lūn-bûn

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2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2011年の論文

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2011年論文

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2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

The formin DAD domain plays dual roles in autoinhibition and actin nucleation.

@ast

The formin DAD domain plays dual roles in autoinhibition and actin nucleation.

@en

The formin DAD domain plays dual roles in autoinhibition and actin nucleation.

@nl

type

label

The formin DAD domain plays dual roles in autoinhibition and actin nucleation.

@ast

The formin DAD domain plays dual roles in autoinhibition and actin nucleation.

@en

The formin DAD domain plays dual roles in autoinhibition and actin nucleation.

@nl

prefLabel

The formin DAD domain plays dual roles in autoinhibition and actin nucleation.

@ast

The formin DAD domain plays dual roles in autoinhibition and actin nucleation.

@en

The formin DAD domain plays dual roles in autoinhibition and actin nucleation.

@nl

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J.CUB.2011.01.047

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Current Biology

P1476

The formin DAD domain plays dual roles in autoinhibition and actin nucleation

@en

P2093

Bruce L Goode

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

Christopher J Gould

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

Laurent Blanchoin

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

Sankar Maiti

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

P2860

Staying in shape with formins

Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture

Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1

Phylogenetic analysis of the formin homology 2 domain

Mechanism and function of formins in the control of actin assembly

The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition

Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy.

Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain.

Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy.

Structure of the autoinhibitory switch in formin mDia1.

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384-390

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scholarly article

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10.1016/J.CUB.2011.01.047

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5

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21

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Alphée Michelot

Brian R Graziano

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2011-02-17T00:00:00Z

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49847808

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21333540

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3058777

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