Phosphorylation of C-protein, troponin I and phospholamban in isolated rabbit hearts. - Wikidata - wikimedia - TriplyDB

Phosphorylation of C-protein, troponin I and phospholamban in isolated rabbit hearts.

Phosphorylation of C-protein, troponin I and phospholamban in isolated rabbit hearts.

http://www.wikidata.org/entity/Q41346387

about

The inotropic effect of the active metabolite of levosimendan, OR-1896, is mediated through inhibition of PDE3 in rat ventricular myocardium Myomegalin is a novel A-kinase anchoring protein involved in the phosphorylation of cardiac myosin binding protein C A-kinase anchoring protein 100 (AKAP100) is localized in multiple subcellular compartments in the adult rat heart Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: a modulator of cardiac contraction?Cardiac myosin binding protein C phosphorylation is cardioprotective Cardiac myosin-binding protein-C phosphorylation and cardiac function PKA accelerates rate of force development in murine skinned myocardium expressing alpha- or beta-tropomyosin Alterations to myofibrillar protein function in nonischemic regions of the heart early after myocardial infarction.The structure of isolated cardiac Myosin thick filaments from cardiac Myosin binding protein-C knockout mice.Regulation of fibre contraction in a rat model of myocardial ischemia.Zebrafish cardiac muscle thick filaments: isolation technique and three-dimensional structure.Control of sarcomeric assembly: the flow of information on titin.What we know and do not know about sex and cardiac disease.Multiple structures of thick filaments in resting cardiac muscle and their influence on cross-bridge interactions.Mammalian cardiac muscle thick filaments: their periodicity and interactions with actin.Type 1 phosphatase, a negative regulator of cardiac function.Porcine left atrial and sinoatrial 5-HT(4) receptor-induced responses: fading of the response and influence of development.Cardiac myosin binding protein-C: redefining its structure and function.Knockout of p21-activated kinase-1 attenuates exercise-induced cardiac remodelling through altered calcineurin signalling Thin filament remodeling in failing myocardium.Phosphorylation of titin modulates passive stiffness of cardiac muscle in a titin isoform-dependent manner.Compartmentalized cAMP/PKA signalling regulates cardiac excitation-contraction coupling.Cardiac Myosin Binding Protein-C Phosphorylation Modulates Myofilament Length-Dependent Activation Myofibrillar remodeling in cardiac hypertrophy, heart failure and cardiomyopathies.Cardiac Myosin-binding protein C modulates the tuning of the molecular motor in the heart Calcium sensitivity and myofilament lattice structure in titin N2B KO mice.Molecule specific effects of PKA-mediated phosphorylation on rat isolated heart and cardiac myofibrillar function Expression of active p21-activated kinase-1 induces Ca2+ flux modification with altered regulatory protein phosphorylation in cardiac myocytes Alterations in Multi-Scale Cardiac Architecture in Association With Phosphorylation of Myosin Binding Protein-C.Ontogenic changes of the control by phosphodiesterase-3 and -4 of 5-HT responses in porcine heart and relevance to human atrial 5-HT(4) receptors.Selective desensitization of the 5-HT4 receptor-mediated response in pig atrium but not in stomach.Cardiac-specific overexpression of phospholamban alters calcium kinetics and resultant cardiomyocyte mechanics in transgenic mice.Human heart failure is accompanied by altered protein kinase A subunit expression and post-translational state.Effects of contractile protein phosphorylation on force development in permeabilized rat cardiac myocytes.Cardiac myosin binding protein-C as a central target of cardiac sarcomere signaling: a special mini review series.PKCepsilon increases phosphorylation of the cardiac myosin binding protein C at serine 302 both in vitro and in vivo.Cardiac myosin binding protein-C Ser302 phosphorylation regulates cardiac β-adrenergic reserve Effect of troponin I Ser23/24 phosphorylation on Ca2+-sensitivity in human myocardium depends on the phosphorylation background.The death of transcriptional chauvinism in the control and regulation of cardiac contractility.Role of intracellular calcium handling in force-interval relationships of human ventricular myocardium

P2860

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P2860

Phosphorylation of C-protein, troponin I and phospholamban in isolated rabbit hearts.

http://www.wikidata.org/entity/Q41346387

description

1988 nî lūn-bûn

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1988年の論文

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1988年論文

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1988年論文

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1988年論文

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1988年論文

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1988年論文

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1988年论文

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1988年论文

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1988年论文

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name

Phosphorylation of C-protein, troponin I and phospholamban in isolated rabbit hearts.

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type

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Phosphorylation of C-protein, troponin I and phospholamban in isolated rabbit hearts.

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prefLabel

Phosphorylation of C-protein, troponin I and phospholamban in isolated rabbit hearts.

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Biochemical Journal

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Phosphorylation of C-protein, troponin I and phospholamban in isolated rabbit hearts.

@en

P2093

E G Kranias

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J L Garvey

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R J Solaro

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P2860

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Effects of cholinergic and adrenergic agonists on phosphorylation of a 165,000-dalton myofibrillar protein in intact cardiac muscle

Phosphorylation of C-protein in intact amphibian cardiac muscle. Correlation between 32P incorporation and twitch relaxation.

Role of the contractile proteins and sarcoplasmic reticulum in the response of the heart to catecholamines: an historical review.

The location of C-protein in rabbit skeletal muscle.

Phosphorylation of cardiac troponin by cyclic adenosine 3':5'-monophosphate-dependent protein kinase.

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

Thick-filament-linked calcium regulation in vertebrate striated muscle.

Phosphorylation of a bovine cardiac actin complex.

Regulation of calcium transport by the ATPase-phospholamban system.

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709-714

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scholarly article

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10.1042/BJ2490709

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3

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249

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1988-02-01T00:00:00Z

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phosphorylation

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