Phosphorylation specificities of protein kinase C isozymes for bovine cardiac troponin I and troponin T and sites within these proteins and regulation of myofilament properties - Wikidata - awgldk - TriplyDB

Phosphorylation specificities of protein kinase C isozymes for bovine cardiac troponin I and troponin T and sites within these proteins and regulation of myofilament properties

Phosphorylation specificities of protein kinase C isozymes for bovine cardiac troponin I and troponin T and sites within these proteins and regulation of myofilament properties

http://www.wikidata.org/entity/Q28289247

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Gene regulation, alternative splicing, and posttranslational modification of troponin subunits in cardiac development and adaptation: a focused review Phosphorylation of cardiac troponin I by mammalian sterile 20-like kinase 1 Use of a novel method to find substrates of protein kinase C delta identifies M2 pyruvate kinase Identification of a functionally critical protein kinase C phosphorylation residue of cardiac troponin T Phosphorylation or glutamic acid substitution at protein kinase C sites on cardiac troponin I differentially depress myofilament tension and shortening velocity Phosphorylation, but not alternative splicing or proteolytic degradation, is conserved in human and mouse cardiac troponin T Protein kinase C alpha and epsilon phosphorylation of troponin and myosin binding protein C reduce Ca2+ sensitivity in human myocardium Interplay between troponin T phosphorylation and O-N-acetylglucosaminylation in ischaemic heart failure Perturbed length-dependent activation in human hypertrophic cardiomyopathy with missense sarcomeric gene mutations Troponin T isoforms and posttranscriptional modifications: Evolution, regulation and function Dephosphorylation specificities of protein phosphatase for cardiac troponin I, troponin T, and sites within troponin T.A preferred AMPK phosphorylation site adjacent to the inhibitory loop of cardiac and skeletal troponin I Adenoprotection of the heart involves phospholipase C-induced activation and translocation of PKC-epsilon to RACK2 in adult rat and mouse.Brief rapid pacing depresses contractile function via Ca(2+)/PKC-dependent signaling in cat ventricular myocytes.Regulation of fibre contraction in a rat model of myocardial ischemia.Reduced force production during low blood flow to the heart correlates with altered troponin I phosphorylation Deciphering modifications in swine cardiac troponin I by top-down high-resolution tandem mass spectrometry.PKCα-specific phosphorylation of the troponin complex in human myocardium: a functional and proteomics analysis.Structure of the NH2-terminal variable region of cardiac troponin T determines its sensitivity to restrictive cleavage in pathophysiological adaptation Ceramide-mediated depression in cardiomyocyte contractility through PKC activation and modulation of myofilament protein phosphorylation Interventricular differences in myofilament function in experimental congestive heart failure.Augmented 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.Negative charges at protein kinase C sites of troponin I stabilize the inactive state of actin ACE inhibition prevents diastolic Ca2+ overload and loss of myofilament Ca2+ sensitivity after myocardial infarction.Molecular defects in cardiac myofibrillar proteins due to thyroid hormone imbalance and diabetes.Cardiac enzymes, renal failure and renal transplantation.Myofibrillar remodeling in cardiac hypertrophy, heart failure and cardiomyopathies.Protein kinase C depresses cardiac myocyte power output and attenuates myofilament responses induced by protein kinase A Present and future biochemical markers for detection of acute coronary syndrome.Regulation of Na+/Ca2+ exchange current in the normal and failing heart.Myofilament incorporation and contractile function after gene transfer of cardiac troponin I Ser43/45Ala.Protein kinase C zeta. A novel regulator of both phosphorylation and de-phosphorylation of cardiac sarcomeric proteins.Interplay Between the Effects of Dilated Cardiomyopathy Mutation (R206L) and the Protein Kinase C Phosphomimic (T204E) of Rat Cardiac Troponin T Are Differently Modulated by α- and β-Myosin Heavy Chain Isoforms.Protection of the heart by treatment with a divalent-copper-selective chelator reveals a novel mechanism underlying cardiomyopathy in diabetic rats.Expression of protein kinase C beta in the heart causes hypertrophy in adult mice and sudden death in neonates.In vivo phosphorylation of cardiac troponin I by protein kinase Cbeta2 decreases cardiomyocyte calcium responsiveness and contractility in transgenic mouse hearts.TNNT1, TNNT2, and TNNT3: Isoform genes, regulation, and structure-function relationships.Oxidative stress and sarcomeric proteins.

P2860

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Phosphorylation specificities of protein kinase C isozymes for bovine cardiac troponin I and troponin T and sites within these proteins and regulation of myofilament properties

http://www.wikidata.org/entity/Q28289247

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1996 nî lūn-bûn

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P2860

Protein kinase C--a question of specificity

Protein kinase C isoform expression and regulation in the developing rat heart

Localization of protein kinase C isozymes in cardiac myocytes

Characterization of protein kinase C isotype expression in adult rat heart. Protein kinase C-epsilon is a major isotype present, and it is activated by phorbol esters, epinephrine, and endothelin

Cardiac troponin I mutants. Phosphorylation by protein kinases C and A and regulation of Ca(2+)-stimulated MgATPase of reconstituted actomyosin S-1

Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction.

Phosphorylation of the inhibitory subunit of troponin and its effect on the calcium dependence of cardiac myofibril adenosine triphosphatase.

Expression of protein kinase C isotypes using baculovirus vectors.

Phosphorylation of cardiac troponin inhibitory subunit (troponin I) and tropomyosin-binding subunit (troponin T) by cardiac phospholipid-sensitive Ca2+-dependent protein kinase.

Role of protein kinase C in the phosphorylation of cardiac myosin light chain 2

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