Tyrosine phosphorylation modifies protein kinase C delta-dependent phosphorylation of cardiac troponin I. - Wikidata - awgldk - TriplyDB

Tyrosine phosphorylation modifies protein kinase C delta-dependent phosphorylation of cardiac troponin I.

Tyrosine phosphorylation modifies protein kinase C delta-dependent phosphorylation of cardiac troponin I.

http://www.wikidata.org/entity/Q41851995

about

Raf-1: a novel cardiac troponin T kinase Integration of troponin I phosphorylation with cardiac regulatory networks Protein kinase C mechanisms that contribute to cardiac remodelling Serine-910 phosphorylation of focal adhesion kinase is critical for sarcomere reorganization in cardiomyocyte hypertrophy Distinct sarcomeric substrates are responsible for protein kinase D-mediated regulation of cardiac myofilament Ca2+ sensitivity and cross-bridge cycling Why does troponin I have so many phosphorylation sites? Fact and fancy Phosphorylation of cardiac troponin I at protein kinase C site threonine 144 depresses cooperative activation of thin filaments.Left ventricular and myocardial function in mice expressing constitutively pseudophosphorylated cardiac troponin I.Structural basis of protein kinase C isoform function H2O2 alters rat cardiac sarcomere function and protein phosphorylation through redox signaling Protein kinase C-{delta} regulates the subcellular localization of Shc in H2O2-treated cardiomyocytes.Nuclear localization of a1A-adrenergic receptors is required for signaling in cardiac myocytes: an “inside-out” a1-AR signaling pathway.Molecular systems pharmacology: isoelectric focusing signature of protein kinase Cδ provides an integrated measure of its modulation in response to ligands Novel function of cardiac protein kinase D1 as a dynamic regulator of Ca2+ sensitivity of contraction Protein kinase D isoforms are activated in an agonist-specific manner in cardiomyocytes.Redox signaling and cardiac sarcomeres Protein phosphorylation and signal transduction in cardiac thin filaments.The C2 Domain and Altered ATP-Binding Loop Phosphorylation at Ser³⁵⁹ Mediate the Redox-Dependent Increase in Protein Kinase C-δ Activity Interventricular differences in myofilament function in experimental congestive heart failure.Augmented phosphorylation of cardiac troponin I in hypertensive heart failure.Overview: the maturing of proteomics in cardiovascular research.Cardiac actions of protein kinase C isoforms Functionally conservative substitutions at cardiac troponin I S43/45.Multiplex kinase signaling modifies cardiac function at the level of sarcomeric proteins.A novel phosphorylation site at Ser130 adjacent to the pseudosubstrate domain contributes to the activation of protein kinase C-δ.Regulatory autophosphorylation sites on protein kinase C-delta at threonine-141 and threonine-295.Overexpression of diacylglycerol kinase η enhances Gαq-coupled G protein-coupled receptor signaling.Regional variation in myofilament length-dependent activation.Oxidative stress and sarcomeric proteins.Mechanisms for redox-regulation of protein kinase C.Multifunctional roles of PKCδ: Opportunities for targeted therapy in human disease Targeted activation of conventional and novel protein kinases C through differential translocation patterns Deep Coverage of Global Protein Expression and Phosphorylation in Breast Tumor Cell Lines Using TMT 10-plex Isobaric Labeling.The role of protein kinase C-mediated phosphorylation of sarcomeric proteins in the heart-detrimental or beneficial?Cardiomyopathy-causing deletion K210 in cardiac troponin T alters phosphorylation propensity of sarcomeric proteins.LysoPCs induce Hck- and PKCδ-mediated activation of PKCγ causing p47phox phosphorylation and membrane translocation in neutrophils.Stage-specific changes in myofilament protein phosphorylation following myocardial infarction in mice.Differential effects of phosphorylation of regions of troponin I in modifying cooperative activation of cardiac thin filaments.CLEAVAGE ALTERS THE MOLECULAR DETERMINANTS OF PROTEIN KINASE C-δ CATALYTIC ACTIVITY.Functional communication between PKC-targeted cardiac troponin I phosphorylation sites.

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P2860

Tyrosine phosphorylation modifies protein kinase C delta-dependent phosphorylation of cardiac troponin I.

http://www.wikidata.org/entity/Q41851995

description

2008 nî lūn-bûn

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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2008年论文

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2008年论文

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name

Tyrosine phosphorylation modif ...... ylation of cardiac troponin I.

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type

label

Tyrosine phosphorylation modif ...... ylation of cardiac troponin I.

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Tyrosine phosphorylation modif ...... ylation of cardiac troponin I.

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P1433

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P1433

Journal of Biological Chemistry

P1476

Tyrosine phosphorylation modif ...... ylation of cardiac troponin I.

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P2093

Aaron C Hinken

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

C William Balke

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Chaojian Wang

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Erin Harleton

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Gail Sievert

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Marius P Sumandea

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R John Solaro

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Steven J Feinmark

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Susan F Steinberg

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Tomoyoshi Kobayashi

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P2860

Protein kinase cascades in the regulation of cardiac hypertrophy

Phosphorylation-dependent conformational transition of the cardiac specific N-extension of troponin I in cardiac troponin

Loaded shortening, power output, and rate of force redevelopment are increased with knockout of cardiac myosin binding protein-C

Phosphorylation or glutamic acid substitution at protein kinase C sites on cardiac troponin I differentially depress myofilament tension and shortening velocity

Calcium, thin filaments, and the integrative biology of cardiac contractility

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

Differential contribution of troponin I phosphorylation sites to the endothelin-modulated contractile response

PKA accelerates rate of force development in murine skinned myocardium expressing alpha- or beta-tropomyosin

Cardiac troponin I gene knockout: a mouse model of myocardial troponin I deficiency

Protein kinase Cepsilon (PKCepsilon) and Src control PKCdelta activation loop phosphorylation in cardiomyocytes

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22680-22689

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scholarly article

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10.1074/JBC.M802396200

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33

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283

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2008-06-12T00:00:00Z

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18550549

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phosphorylation

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2504892

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