Sequential myosin phosphorylation activates tarantula thick filament via a disorder-order transition.
about
Phosphorylation of the regulatory light chain of myosin in striated muscle: methodological perspectivesTarantula myosin free head regulatory light chain phosphorylation stiffens N-terminal extension, releasing it and blocking its docking back.Spectroscopic Studies of the Super Relaxed State of Skeletal Muscle.Conserved Intramolecular Interactions Maintain Myosin Interacting-Heads Motifs Explaining Tarantula Muscle Super-Relaxed State Structural Basis.Hypertrophic cardiomyopathy and the myosin mesa: viewing an old disease in a new light.Lessons from a tarantula: new insights into muscle thick filament and myosin interacting-heads motif structure and function.Effects of myosin variants on interacting-heads motif explain distinct hypertrophic and dilated cardiomyopathy phenotypes.Modulation of Skeletal Muscle Contraction by Myosin Phosphorylation.
P2860
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P2860
Sequential myosin phosphorylation activates tarantula thick filament via a disorder-order transition.
description
2015 nî lūn-bûn
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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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2015年論文
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2015年論文
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2015年論文
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2015年论文
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2015年论文
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name
Sequential myosin phosphorylat ...... a a disorder-order transition.
@ast
Sequential myosin phosphorylat ...... a a disorder-order transition.
@en
type
label
Sequential myosin phosphorylat ...... a a disorder-order transition.
@ast
Sequential myosin phosphorylat ...... a a disorder-order transition.
@en
prefLabel
Sequential myosin phosphorylat ...... a a disorder-order transition.
@ast
Sequential myosin phosphorylat ...... a a disorder-order transition.
@en
P2860
P50
P356
P1433
P1476
Sequential myosin phosphorylat ...... ia a disorder-order transition
@en
P2093
L Michel Espinoza-Fonseca
Lorenzo Alamo
P2860
P304
P356
10.1039/C5MB00162E
P577
2015-08-01T00:00:00Z