Myofibrillar Ca(2+) sensitivity is uncoupled from troponin I phosphorylation in hypertrophic obstructive cardiomyopathy due to abnormal troponin T.
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Why Is there a Limit to the Changes in Myofilament Ca2+-Sensitivity Associated with Myopathy Causing Mutations?Long term ablation of protein kinase A (PKA)-mediated cardiac troponin I phosphorylation leads to excitation-contraction uncoupling and diastolic dysfunction in a knock-in mouse model of hypertrophic cardiomyopathyFamilial dilated cardiomyopathy mutations uncouple troponin I phosphorylation from changes in myofibrillar Ca²⁺ sensitivityInvestigations into the Sarcomeric Protein and Ca2+-Regulation Abnormalities Underlying Hypertrophic Cardiomyopathy in Cats (Felix catus).Investigating the role of uncoupling of troponin I phosphorylation from changes in myofibrillar Ca(2+)-sensitivity in the pathogenesis of cardiomyopathy.Computational modeling of Takotsubo cardiomyopathy: effect of spatially varying β-adrenergic stimulation in the rat left ventricleZ-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrilsThe dilated cardiomyopathy-causing mutation ACTC E361G in cardiac muscle myofibrils specifically abolishes modulation of Ca(2+) regulation by phosphorylation of troponin IOBSCN Mutations Associated with Dilated Cardiomyopathy and Haploinsufficiency.Best Practice BioBanking of Human Heart TissueUncoupling of myofilament Ca2+ sensitivity from troponin I phosphorylation by mutations can be reversed by epigallocatechin-3-gallate.Mutations in troponin T associated with Hypertrophic Cardiomyopathy increase Ca(2+)-sensitivity and suppress the modulation of Ca(2+)-sensitivity by troponin I phosphorylation.TPM3 deletions cause a hypercontractile congenital muscle stiffness phenotype.Contribution of Post-translational Phosphorylation to Sarcomere-Linked Cardiomyopathy Phenotypes.Irisin regulates cardiac physiology in zebrafishPathogenesis associated with a restrictive cardiomyopathy mutant in cardiac troponin T is due to reduced protein stability and greatly increased myofilament Ca2+ sensitivity.Abnormal contractility in human heart myofibrils from patients with dilated cardiomyopathy due to mutations in TTN and contractile protein genes.Molecular Defects in Cardiac Myofilament Ca2+-Regulation Due to Cardiomyopathy-Linked Mutations Can Be Reversed by Small Molecules Binding to Troponin.
P2860
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P2860
Myofibrillar Ca(2+) sensitivity is uncoupled from troponin I phosphorylation in hypertrophic obstructive cardiomyopathy due to abnormal troponin T.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh
2012年學術文章
@zh-hant
name
Myofibrillar Ca
@nl
Myofibrillar Ca(2+) sensitivit ...... hy due to abnormal troponin T.
@en
type
label
Myofibrillar Ca
@nl
Myofibrillar Ca(2+) sensitivit ...... hy due to abnormal troponin T.
@en
prefLabel
Myofibrillar Ca
@nl
Myofibrillar Ca(2+) sensitivit ...... hy due to abnormal troponin T.
@en
P2093
P2860
P356
P1476
Myofibrillar Ca(2+) sensitivit ...... hy due to abnormal troponin T.
@en
P2093
Adam M Jacques
Andrew E Messer
Charles S Redwood
Christopher R Bayliss
Clare E Gallon
Cristobal Dos Remedios
Man-Ching Leung
O'Neal Copeland
Steven B Marston
P2860
P304
P356
10.1093/CVR/CVS322
P577
2012-10-24T00:00:00Z