Multiplex kinase signaling modifies cardiac function at the level of sarcomeric proteins.
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Integration of troponin I phosphorylation with cardiac regulatory networksSmall G proteins in the cardiovascular system: physiological and pathological aspectsDynamic Alterations to α-Actinin Accompanying Sarcomere Disassembly and Reassembly during Cardiomyocyte MitosisLong 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 cardiomyopathyTop-down quantitative proteomics identified phosphorylation of cardiac troponin I as a candidate biomarker for chronic heart failureDistinct sarcomeric substrates are responsible for protein kinase D-mediated regulation of cardiac myofilament Ca2+ sensitivity and cross-bridge cyclingNew insights into the functional significance of the acidic region of the unique N-terminal extension of cardiac troponin ICardiac myosin light chain kinase is necessary for myosin regulatory light chain phosphorylation and cardiac performance in vivoNovel role for p90 ribosomal S6 kinase in the regulation of cardiac myofilament phosphorylationRegulation of fibre contraction in a rat model of myocardial ischemia.Cardiac troponin I is abnormally expressed in non-small cell lung cancer tissues and human cancer cells.Cardiac myosin is a substrate for zipper-interacting protein kinase (ZIPK)Cardiac troponin T, a sarcomeric AKAP, tethers protein kinase A at the myofilaments.Proteomics analysis of the cardiac myofilament subproteome reveals dynamic alterations in phosphatase subunit distributionPhosphorylation of cardiac troponin I at protein kinase C site threonine 144 depresses cooperative activation of thin filaments.Rescue of familial cardiomyopathies by modifications at the level of sarcomere and Ca2+ fluxes.Excision of titin's cardiac PEVK spring element abolishes PKCalpha-induced increases in myocardial stiffnessWhat we know and do not know about sex and cardiac disease.Combined troponin I Ser-150 and Ser-23/24 phosphorylation sustains thin filament Ca(2+) sensitivity and accelerates deactivation in an acidic environment.The curious role of sarcomeric proteins in control of diverse processes in cardiac myocytes.Phosphorylation of tropomodulin1 contributes to the regulation of actin filament architecture in cardiac muscle.Top-down proteomics reveals concerted reductions in myofilament and Z-disc protein phosphorylation after acute myocardial infarction.Novel function of cardiac protein kinase D1 as a dynamic regulator of Ca2+ sensitivity of contractionStrong cross-bridges potentiate the Ca(2+) affinity changes produced by hypertrophic cardiomyopathy cardiac troponin C mutants in myofilaments: a fast kinetic approach.Top-down mass spectrometry of cardiac myofilament proteins in health and disease.The giant protein titin: a regulatory node that integrates myocyte signaling pathways.Protein phosphorylation and signal transduction in cardiac thin filaments.Insights into modulation of calcium signaling by magnesium in calmodulin, troponin C and related EF-hand proteinsCeramide-mediated depression in cardiomyocyte contractility through PKC activation and modulation of myofilament protein phosphorylationAugmented phosphorylation of cardiac troponin I in hypertensive heart failure.Single amino acid sequence polymorphisms in rat cardiac troponin revealed by top-down tandem mass spectrometry.In vivo phosphorylation site mapping in mouse cardiac troponin I by high resolution top-down electron capture dissociation mass spectrometry: Ser22/23 are the only sites basally phosphorylated.Removal of Abnormal Myofilament O-GlcNAcylation Restores Ca2+ Sensitivity in Diabetic Cardiac Muscle.Novel roles of PAK1 in the heart.The impact of antibody selection on the detection of cardiac troponin I.Post-translational modifications of myofilament proteins involved in length-dependent prolongation of relaxation in rabbit right ventricular myocardiumS-glutathiolation impairs phosphoregulation and function of cardiac myosin-binding protein C in human heart failure.Loss of enigma homolog protein results in dilated cardiomyopathy.Myosin light chain phosphorylation enhances contraction of heart muscle via structural changes in both thick and thin filamentsFunctional phosphorylation sites in cardiac myofilament proteins are evolutionarily conserved in skeletal myofilament proteins
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Multiplex kinase signaling modifies cardiac function at the level of sarcomeric proteins.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 19 June 2008
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Multiplex kinase signaling modifies cardiac function at the level of sarcomeric proteins.
@en
Multiplex kinase signaling modifies cardiac function at the level of sarcomeric proteins.
@nl
type
label
Multiplex kinase signaling modifies cardiac function at the level of sarcomeric proteins.
@en
Multiplex kinase signaling modifies cardiac function at the level of sarcomeric proteins.
@nl
prefLabel
Multiplex kinase signaling modifies cardiac function at the level of sarcomeric proteins.
@en
Multiplex kinase signaling modifies cardiac function at the level of sarcomeric proteins.
@nl
P2860
P356
P1476
Multiplex kinase signaling modifies cardiac function at the level of sarcomeric proteins.
@en
P2093
R John Solaro
P2860
P304
26829-26833
P356
10.1074/JBC.R800037200
P407
P577
2008-06-19T00:00:00Z