Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function - Wikidata - awgldk - TriplyDB

Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function

Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function

http://www.wikidata.org/entity/Q24679543

about

Association of villin with phosphatidylinositol 4,5-bisphosphate regulates the actin cytoskeleton Direct dynamin-actin interactions regulate the actin cytoskeleton.Coronin 1C harbours a second actin-binding site that confers co-operative binding to F-actin The ADF/cofilin family: actin-remodeling proteins.Specification of actin filament function and molecular composition by tropomyosin isoforms The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics Gelsolin and ADF/cofilin enhance the actin dynamics of motile cells Structural plasticity in actin and tubulin polymer dynamics.Muscle LIM protein interacts with cofilin 2 and regulates F-actin dynamics in cardiac and skeletal muscle The ADF homology (ADF-H) domain: a highly exploited actin-binding module Allele-specific effects of human deafness gamma-actin mutations (DFNA20/26) on the actin/cofilin interaction Regulation of cell migration and morphogenesis by Abl-family kinases: emerging mechanisms and physiological contexts The yeast actin cytoskeleton: from cellular function to biochemical mechanism Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics Aip1p interacts with cofilin to disassemble actin filaments Correlative nanoscale imaging of actin filaments and their complexes Roles of adaptor proteins in podocyte biology Cofilin oligomer formation occurs in vivo and is regulated by cofilin phosphorylation Coronin Enhances Actin Filament Severing by Recruiting Cofilin to Filament Sides and Altering F-Actin Conformation Loss of cofilin 1 disturbs actin dynamics, adhesion between enveloping and deep cell layers and cell movements during gastrulation in zebrafish Arp2/3 complex and cofilin modulate binding of tropomyosin to branched actin networks Stretching actin filaments within cells enhances their affinity for the myosin II motor domain Aip1 destabilizes cofilin-saturated actin filaments by severing and accelerating monomer dissociation from ends.A comparative structural analysis of the ADF/cofilin family Structure of an F-actin trimer disrupted by gelsolin and implications for the mechanism of severing The structure of nonvertebrate actin: Implications for the ATP hydrolytic mechanism The structure of Aip1p, a WD repeat protein that regulates Cofilin-mediated actin depolymerization Solution structure of human cofilin: actin binding, pH sensitivity, and relationship to actin-depolymerizing factor Crystallographic Conformers of Actin in a Biologically Active Bundle of Filaments Structure of the actin-depolymerizing factor homology domain in complex with actin Minimal requirements for actin filament disassembly revealed by structural analysis of malaria parasite actin-depolymerizing factor 1 Crystal Structures Explain Functional Differences in the Two Actin Depolymerization Factors of the Malaria Parasite Remodeling of actin filaments by ADF/cofilin proteins Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin Srv2/cyclase-associated protein forms hexameric shurikens that directly catalyze actin filament severing by cofilin.Deficiencies in the endoplasmic reticulum (ER)-membrane protein Gab1p perturb transfer of glycosylphosphatidylinositol to proteins and cause perinuclear ER-associated actin bar formation High-speed depolymerization at actin filament ends jointly catalysed by Twinfilin and Srv2/CAP.Reconstitution and protein composition analysis of endocytic actin patches.GMF severs actin-Arp2/3 complex branch junctions by a cofilin-like mechanism.Transglutaminase 2 has opposing roles in the regulation of cellular functions as well as cell growth and death

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P2860

Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function

http://www.wikidata.org/entity/Q24679543

description

1997 nî lūn-bûn

@nan

1997 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

1997 թվականի օգոստոսին հրատարակված գիտական հոդված

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1997年の論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年論文

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1997年论文

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name

Cofilin changes the twist of F ...... dynamics and cellular function

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Cofilin changes the twist of F ...... dynamics and cellular function

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Cofilin changes the twist of F ...... dynamics and cellular function

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type

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Cofilin changes the twist of F ...... dynamics and cellular function

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Cofilin changes the twist of F ...... dynamics and cellular function

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Cofilin changes the twist of F ...... dynamics and cellular function

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prefLabel

Cofilin changes the twist of F ...... dynamics and cellular function

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Cofilin changes the twist of F ...... dynamics and cellular function

@en

Cofilin changes the twist of F ...... dynamics and cellular function

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P1433

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Journal of Cell Biology

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Cofilin changes the twist of F ...... dynamics and cellular function

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P2093

A McGough

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

A Weeds

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B Pope

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W Chiu

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P2860

Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments

Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility

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

Tertiary structure of destrin and structural similarity between two actin-regulating protein families

Structure determination of yeast cofilin

Crystal structure of the actin-binding protein actophorin from Acanthamoeba

Cofilin is an essential component of the yeast cortical cytoskeleton.

Structure of the actin-myosin complex and its implications for muscle contraction

A conformational change in the actin subunit can change the flexibility of the actin filament

Partial purification and characterization of an actin depolymerizing factor from brain

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771-81

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2137560

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10.1083/JCB.138.4.771

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4

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138

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9265645

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2138052

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