The contributions of cardiac myosin binding protein C and troponin I phosphorylation to β-adrenergic enhancement of in vivo cardiac function.
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MYBPC1, an Emerging Myopathic Gene: What We Know and What We Need to LearnCardiac Myosin Binding Protein-C Phosphorylation Modulates Myofilament Length-Dependent ActivationCardiac myosin binding protein-C Ser302 phosphorylation regulates cardiac β-adrenergic reserveMolecular Approaches in HFpEF: MicroRNAs and iPSC-Derived Cardiomyocytes.Genetically Encoded Biosensors Reveal PKA Hyperphosphorylation on the Myofilaments in Rabbit Heart Failure.Hypertrophic cardiomyopathy mutation in cardiac troponin T (R95H) attenuates length-dependent activation in guinea pig cardiac muscle fibers.Sarcomeric protein modification during adrenergic stress enhances cross-bridge kinetics and cardiac output.β-Adrenergic augmentation of cardiac contractility is dependent on PKA-mediated phosphorylation of myosin-binding protein C and troponin I.Phosphorylation of cardiac myosin binding protein-C regulates heart contraction and dilatation in vivo during β-adrenergic receptor activation.
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The contributions of cardiac myosin binding protein C and troponin I phosphorylation to β-adrenergic enhancement of in vivo cardiac function.
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2015年の論文
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2015年論文
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2015年論文
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name
The contributions of cardiac m ...... t of in vivo cardiac function.
@en
type
label
The contributions of cardiac m ...... t of in vivo cardiac function.
@en
prefLabel
The contributions of cardiac m ...... t of in vivo cardiac function.
@en
P2860
P356
P1476
The contributions of cardiac m ...... t of in vivo cardiac function.
@en
P2093
Julian E Stelzer
Kenneth S Gresham
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P304
P356
10.1113/JP270959
P407
P577
2015-12-04T00:00:00Z