Gelsolin mediates calcium-dependent disassembly of Listeria actin tails. - Wikidata - wikimedia - TriplyDB

Gelsolin mediates calcium-dependent disassembly of Listeria actin tails.

Gelsolin mediates calcium-dependent disassembly of Listeria actin tails.

http://www.wikidata.org/entity/Q30856243

about

Villin severing activity enhances actin-based motility in vivo VSOP/Hv1 proton channels sustain calcium entry, neutrophil migration, and superoxide production by limiting cell depolarization and acidification.BCL2 inhibits cell adhesion, spreading, and motility by enhancing actin polymerization.Stimulation of actin polymerization by filament severing Local cytosolic Ca2+ elevations are required for stromal interaction molecule 1 (STIM1) de-oligomerization and termination of store-operated Ca2+ entry Pathogenic microbes manipulate cofilin activity to subvert actin cytoskeleton.Active contractions in single suspended epithelial cells.

P2860

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P2860

Gelsolin mediates calcium-dependent disassembly of Listeria actin tails.

http://www.wikidata.org/entity/Q30856243

description

2005 nî lūn-bûn

@nan

2005 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2005年の論文

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2005年論文

@yue

2005年論文

@zh-hant

2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

@wuu

name

Gelsolin mediates calcium-dependent disassembly of Listeria actin tails.

@ast

Gelsolin mediates calcium-dependent disassembly of Listeria actin tails.

@en

type

label

Gelsolin mediates calcium-dependent disassembly of Listeria actin tails.

@ast

Gelsolin mediates calcium-dependent disassembly of Listeria actin tails.

@en

prefLabel

Gelsolin mediates calcium-dependent disassembly of Listeria actin tails.

@ast

Gelsolin mediates calcium-dependent disassembly of Listeria actin tails.

@en

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PNAS.0409062102

P1433

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

P1476

Gelsolin mediates calcium-dependent disassembly of Listeria actin tails

@en

P2093

Binghua Hao

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

Bruce Gibson

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

Daniel P Lew

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

Frederick Southwick

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

James R Bamburg

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

Laura Larson

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

Ryoko Krause

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

Serge Arnaudeau

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

Wei Li

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

P2860

Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain

Gelsolin, a protein that caps the barbed ends and severs actin filaments, enhances the actin-based motility of Listeria monocytogenes in host cells

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

Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization

Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin

Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase

Proteins of the ADF/cofilin family: essential regulators of actin dynamics

The kinetics of chemotactic peptide-induced change in F-actin content, F-actin distribution, and the shape of neutrophils

Functions of gelsolin: motility, signaling, apoptosis, cancer.

Listeria monocytogenes moves rapidly through the host-cell cytoplasm by inducing directional actin assembly

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1921-1926

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scholarly article

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10.1073/PNAS.0409062102

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6

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102

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Nicolas Demaurex

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2005-01-25T00:00:00Z

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8060980

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15671163

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548556

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