Nonlinear viscoelasticity of actin transiently cross-linked with mutant α-actinin-4 - Wikidata - awgldk - TriplyDB

Nonlinear viscoelasticity of actin transiently cross-linked with mutant α-actinin-4

Nonlinear viscoelasticity of actin transiently cross-linked with mutant α-actinin-4

http://www.wikidata.org/entity/Q30404935

about

Alpha-actinin binding kinetics modulate cellular dynamics and force generation Synaptopodin couples epithelial contractility to α-actinin-4-dependent junction maturation Microrheology of highly crosslinked microtubule networks is dominated by force-induced crosslinker unbinding.The role of alpha-actinin-4 in human kidney disease.Actin and Actin-Binding Proteins.Biomimetic Stress Sensitive Hydrogel Controlled by DNA Nanoswitches.Filament turnover tunes both force generation and dissipation to control long-range flows in a model actomyosin cortex.Disease-causing mutation in α-actinin-4 promotes podocyte detachment through maladaptation to periodic stretch.Stress-enhanced gelation: a dynamic nonlinearity of elasticity.

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P2860

Nonlinear viscoelasticity of actin transiently cross-linked with mutant α-actinin-4

http://www.wikidata.org/entity/Q30404935

description

2011 nî lūn-bûn

@nan

2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հուլիսին 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

Nonlinear viscoelasticity of actin transiently cross-linked with mutant α-actinin-4

@ast

Nonlinear viscoelasticity of actin transiently cross-linked with mutant α-actinin-4

@en

type

label

Nonlinear viscoelasticity of actin transiently cross-linked with mutant α-actinin-4

@ast

Nonlinear viscoelasticity of actin transiently cross-linked with mutant α-actinin-4

@en

prefLabel

Nonlinear viscoelasticity of actin transiently cross-linked with mutant α-actinin-4

@ast

Nonlinear viscoelasticity of actin transiently cross-linked with mutant α-actinin-4

@en

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J.JMB.2011.06.049

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Journal of Molecular Biology

P1476

Nonlinear viscoelasticity of actin transiently cross-linked with mutant α-actinin-4

@en

P2093

Chase P Broedersz

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

Daniel J Becker

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

David A Weitz

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

Martin Depken

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

Martin R Pollak

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

P2860

Cell mechanics and the cytoskeleton

Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin beta4

Mutations in ACTN4, encoding alpha-actinin-4, cause familial focal segmental glomerulosclerosis

Mice deficient in alpha-actinin-4 have severe glomerular disease

Alpha-actinin and filamin cooperatively enhance the stiffness of actin filament networks.

F-actin, a model polymer for semiflexible chains in dilute, semidilute, and liquid crystalline solutions.

Affinity of alpha-actinin for actin determines the structure and mechanical properties of actin filament gels.

Actin filament length tunes elasticity of flexibly cross-linked actin networks.

Cross-linker dynamics determine the mechanical properties of actin gels.

Mechanical properties of actin filament networks depend on preparation, polymerization conditions, and storage of actin monomers

P304

1062-1071

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scholarly article

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10.1016/J.JMB.2011.06.049

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5

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411

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Frederick C MacKintosh

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2011-07-06T00:00:00Z

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51495995

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21762701

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5419588

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