Unphosphorylated calponin enhances the binding force of unphosphorylated myosin to actin. - Wikidata - awgldk - TriplyDB

Unphosphorylated calponin enhances the binding force of unphosphorylated myosin to actin.

Unphosphorylated calponin enhances the binding force of unphosphorylated myosin to actin.

http://www.wikidata.org/entity/Q34762850

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Airway hyperresponsiveness; smooth muscle as the principal actor Filamentous actin accumulates during plant cell penetration and cell wall plug formation in Phytophthora infestans.The role of caldesmon and its phosphorylation by ERK on the binding force of unphosphorylated myosin to actin.Peripheral Airway Smooth Muscle, but Not the Trachealis, Is Hypercontractile in an Equine Model of Asthma.Avian synaptopodin 2 (fesselin) stabilizes myosin filaments and actomyosin in the presence of ATP.

P2860

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Unphosphorylated calponin enhances the binding force of unphosphorylated myosin to actin.

http://www.wikidata.org/entity/Q34762850

description

2013 nî lūn-bûn

@nan

2013 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

Unphosphorylated calponin enhances the binding force of unphosphorylated myosin to actin.

@ast

Unphosphorylated calponin enhances the binding force of unphosphorylated myosin to actin.

@en

Unphosphorylated calponin enhances the binding force of unphosphorylated myosin to actin.

@nl

type

label

Unphosphorylated calponin enhances the binding force of unphosphorylated myosin to actin.

@ast

Unphosphorylated calponin enhances the binding force of unphosphorylated myosin to actin.

@en

Unphosphorylated calponin enhances the binding force of unphosphorylated myosin to actin.

@nl

altLabel

Unphosphorylated calponin enhances the binding force of unphosphorylated myosin to actin

@en

prefLabel

Unphosphorylated calponin enhances the binding force of unphosphorylated myosin to actin.

@ast

Unphosphorylated calponin enhances the binding force of unphosphorylated myosin to actin.

@en

Unphosphorylated calponin enhances the binding force of unphosphorylated myosin to actin.

@nl

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J.BBAGEN.2013.05.042

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Biochimica et Biophysica Acta

P1476

Unphosphorylated calponin enhances the binding force of unphosphorylated myosin to actin.

@en

P2093

Andrea Benedetti

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

Anne-Marie Lauzon

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Gijs Ijpma

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Horia Nicolae Roman

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Linda Kachmar

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Nedjma B Zitouni

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Oleg Matusovsky

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P2860

Smooth muscle calponin. Inhibition of actomyosin MgATPase and regulation by phosphorylation

Identification of a novel smooth muscle myosin heavy chain cDNA: isoform diversity in the S1 head region

Contractile properties and proteins of smooth muscles of a calponin knockout mouse.

The role of MgADP in force maintenance by dephosphorylated cross-bridges in smooth muscle: a flash photolysis study.

Flash photolysis studies of relaxation and cross-bridge detachment: higher sensitivity of tonic than phasic smooth muscle to MgADP.

The Qdot-labeled actin super-resolution motility assay measures low-duty cycle muscle myosin step size.

A 7-amino-acid insert in the heavy chain nucleotide binding loop alters the kinetics of smooth muscle myosin in the laser trap.

Affinity for MgADP and force of unbinding from actin of myosin purified from tonic and phasic smooth muscle.

Regulation of shortening velocity by calponin in intact contracting smooth muscles.

Force measurements by micromanipulation of a single actin filament by glass needles.

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4634-4641

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scholarly article

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10.1016/J.BBAGEN.2013.05.042

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10

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Apolinary Sobieszek

Lennart Hilbert

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2013-06-06T00:00:00Z

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23747303

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3740034

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