Phosphorylation of cardiac Myosin-binding protein-C is a critical mediator of diastolic function
about
Cardiac-specific deletion of protein phosphatase 1β promotes increased myofilament protein phosphorylation and contractile alterationsMolecular Screen Identifies Cardiac Myosin-Binding Protein-C as a Protein Kinase G-Iα Substrate.Molecular effects of the myosin activator omecamtiv mecarbil on contractile properties of skinned myocardium lacking cardiac myosin binding protein-CCardiac Myosin-binding Protein C and Troponin-I Phosphorylation Independently Modulate Myofilament Length-dependent Activation.Cardiac Myosin Binding Protein-C Phosphorylation Modulates Myofilament Length-Dependent ActivationSite-directed spectroscopy of cardiac myosin-binding protein C reveals effects of phosphorylation on protein structural dynamics.Cardiac myosin-binding protein C: A protein once at loose ends finds its regulatory groove.Simultaneous imaging of local calcium and single sarcomere length in rat neonatal cardiomyocytes using yellow Cameleon-Nano140.Phosphorylation of cardiac myosin binding protein C releases myosin heads from the surface of cardiac thick filamentsUsefulness of Released Cardiac Myosin Binding Protein-C as a Predictor of Cardiovascular Events.Heart failure with preserved ejection fraction and skeletal muscle physiology.Molecular Approaches in HFpEF: MicroRNAs and iPSC-Derived Cardiomyocytes.Loss of myocardial retinoic acid receptor α induces diastolic dysfunction by promoting intracellular oxidative stress and calcium mishandling in adult mice.The contributions of cardiac myosin binding protein C and troponin I phosphorylation to β-adrenergic enhancement of in vivo cardiac function.An integrative translational approach to study heart failure with preserved ejection fraction: a position paper from the Working Group on Myocardial Function of the European Society of Cardiology.Cyclic Nucleotide-Directed Protein Kinases in Cardiovascular Inflammation and Growth.Relaxation and the Role of Calcium in Isolated Contracting Myocardium From Patients With Hypertensive Heart Disease and Heart Failure With Preserved Ejection Fraction.Diastolic dysfunction is more apparent in STZ-induced diabetic female mice, despite less pronounced hyperglycemia.The HCM-linked W792R mutation in cardiac myosin binding protein-C reduces C6 FnIII domain stability.Histone deacetylase activity governs diastolic dysfunction through a nongenomic mechanism.Lycium barbarum polysaccharides restore adverse structural remodelling and cardiac contractile dysfunction induced by overexpression of microRNA-1
P2860
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P2860
Phosphorylation of cardiac Myosin-binding protein-C is a critical mediator of diastolic function
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
Phosphorylation of cardiac Myo ...... mediator of diastolic function
@ast
Phosphorylation of cardiac Myo ...... mediator of diastolic function
@en
type
label
Phosphorylation of cardiac Myo ...... mediator of diastolic function
@ast
Phosphorylation of cardiac Myo ...... mediator of diastolic function
@en
prefLabel
Phosphorylation of cardiac Myo ...... mediator of diastolic function
@ast
Phosphorylation of cardiac Myo ...... mediator of diastolic function
@en
P2093
P2860
P1476
Phosphorylation of cardiac Myo ...... mediator of diastolic function
@en
P2093
Bindiya G Patel
Brett M Mitchell
Candice M Thomas
Carl W Tong
Chad M Warren
Daniel P Fitzsimons
David T Kidwell
Giuseppina F Dusio
Kenneth M Baker
Mohamed I Abdalla
P2860
P304
P356
10.1161/CIRCHEARTFAILURE.114.001550
P577
2015-03-04T00:00:00Z