Phasic phosphorylation of caldesmon and ERK 1/2 during contractions in human myometrium. - Wikidata - awgldk - TriplyDB

Phasic phosphorylation of caldesmon and ERK 1/2 during contractions in human myometrium.

Phasic phosphorylation of caldesmon and ERK 1/2 during contractions in human myometrium.

http://www.wikidata.org/entity/Q31022425

about

Role of serine-threonine phosphoprotein phosphatases in smooth muscle contractility Modulation of Progesterone Receptor Isoform Expression in Pregnant Human Myometrium The expression of genes involved in myometrial contractility changes during ex situ culture of pregnant human uterine smooth muscle tissue.Phasic contractions of isolated human myometrium are associated with Rho-kinase (ROCK)-dependent phosphorylation of myosin phosphatase-targeting subunit (MYPT1).Amino acid mutations in the caldesmon COOH-terminal functional domain increase force generation in bladder smooth muscle.The importance of the smooth muscle cytoskeleton to preterm labour.Notoginsenoside R1 attenuates hypoxia and hypercapnia-induced vasoconstriction in isolated rat pulmonary arterial rings by reducing the expression of ERK.ERK and p38MAPK pathways regulate myosin light chain phosphatase and contribute to Ca2+ sensitization of intestinal smooth muscle contraction.Diminished hERG K+ channel activity facilitates strong human labour contractions but is dysregulated in obese women

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Phasic phosphorylation of caldesmon and ERK 1/2 during contractions in human myometrium.

http://www.wikidata.org/entity/Q31022425

description

2011 nî lūn-bûn

@nan

2011 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

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

Phasic phosphorylation of caldesmon and ERK 1/2 during contractions in human myometrium.

@ast

Phasic phosphorylation of caldesmon and ERK 1/2 during contractions in human myometrium.

@en

type

label

Phasic phosphorylation of caldesmon and ERK 1/2 during contractions in human myometrium.

@ast

Phasic phosphorylation of caldesmon and ERK 1/2 during contractions in human myometrium.

@en

prefLabel

Phasic phosphorylation of caldesmon and ERK 1/2 during contractions in human myometrium.

@ast

Phasic phosphorylation of caldesmon and ERK 1/2 during contractions in human myometrium.

@en

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JOURNAL.PONE.0021542

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Phasic phosphorylation of caldesmon and ERK 1/2 during contractions in human myometrium.

@en

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Eng-Cheng Chan

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

Jonathan Paul

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

Julia Smith

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

Kaushik Maiti

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

Mark Read

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

Roger Smith

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

P2860

Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin

Interaction between caldesmon and tropomyosin in the presence and absence of smooth muscle actin

Stretch activates human myometrium via ERK, caldesmon and focal adhesion signaling

Invited review: cross-bridge regulation by thin filament-associated proteins

The molecular anatomy of caldesmon

Caldesmon binding to actin is regulated by calmodulin and phosphorylation via different mechanisms.

Caldesmon, a novel regulatory protein in smooth muscle and nonmuscle actomyosin systems.

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e21542

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10.1371/JOURNAL.PONE.0021542

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6

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phosphorylation

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