Revisiting Frank-Starling: regulatory light chain phosphorylation alters the rate of force redevelopment (ktr ) in a length-dependent fashion

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Effects of myosin variants on interacting-heads motif explain distinct hypertrophic and dilated cardiomyopathy phenotypes.

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Q42204804-407001D0-F035-4237-BDED-049C509ADC4C

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Revisiting Frank-Starling: regulatory light chain phosphorylation alters the rate of force redevelopment (ktr ) in a length-dependent fashion

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article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 13 June 2016

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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Revisiting Frank-Starling: reg ...... in a length-dependent fashion

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Revisiting Frank-Starling: reg ...... he rate of force redevelopment

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Revisiting Frank-Starling: reg ...... in a length-dependent fashion

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Revisiting Frank-Starling: reg ...... he rate of force redevelopment

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Revisiting Frank-Starling: reg ...... in a length-dependent fashion

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Revisiting Frank-Starling: reg ...... he rate of force redevelopment

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P1476

Revisiting Frank-Starling: reg ...... in a length-dependent fashion

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Timothy G West

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Mouse and computational models link Mlc2v dephosphorylation to altered myosin kinetics in early cardiac disease

Getting the skinny on thick filament regulation in cardiac muscle biology and disease

Abnormal cardiac structure and function in mice expressing nonphosphorylatable cardiac regulatory myosin light chain 2

Effects of different expression and posttranslational modifications of myosin light chains on contractility of skinned human cardiac fibers

The overall pattern of cardiac contraction depends on a spatial gradient of myosin regulatory light chain phosphorylation

Ernest Henry Starling, his predecessors, and the "Law of the Heart"

The effect of myosin RLC phosphorylation in normal and cardiomyopathic mouse hearts

Variations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers. Implications for twitch potentiation in intact muscle

Myosin light chain phosphorylation is critical for adaptation to cardiac stress.

Basal myosin light chain phosphorylation is a determinant of Ca2+ sensitivity of force and activation dependence of the kinetics of myocardial force development

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5237-5254

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scholarly article

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10.1113/JP272441

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English

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594

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Christopher N Toepfer

Michael A Ferenczi

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2016-06-13T00:00:00Z

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27291932

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phosphorylation

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5023691

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Revisiting Frank-Starling: regulatory light chain phosphorylation alters the rate of force redevelopment (ktr ) in a length-dependent fashion

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P2860

Revisiting Frank-Starling: regulatory light chain phosphorylation alters the rate of force redevelopment (ktr ) in a length-dependent fashion

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type

label

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P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

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P921

P932