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The Importance of Intrinsically Disordered Segments of Cardiac Troponin in Modulating Function by Phosphorylation and Disease-Causing MutationsPhosphorylation of the regulatory light chain of myosin in striated muscle: methodological perspectivesThe myosin super-relaxed state is disrupted by estradiol deficiency.Sequential myosin phosphorylation activates tarantula thick filament via a disorder-order transition.Intrinsic disorder and multiple phosphorylations constrain the evolution of the flightin N-terminal region.Phosphorylation and calcium antagonistically tune myosin-binding protein C's structure and function.Orientation of the N- and C-terminal lobes of the myosin regulatory light chain in cardiac muscle.Modulation of Skeletal Muscle Contraction by Myosin Phosphorylation.Molecular Defects in Cardiac Myofilament Ca2+-Regulation Due to Cardiomyopathy-Linked Mutations Can Be Reversed by Small Molecules Binding to Troponin.
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description
article científic
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article scientifique
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articol științific
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articolo scientifico
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artigo científico
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artigo científico
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artigo científico
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artikel ilmiah
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artikull shkencor
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artículo científico
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name
Structural dynamics of muscle protein phosphorylation.
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type
label
Structural dynamics of muscle protein phosphorylation.
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prefLabel
Structural dynamics of muscle protein phosphorylation.
@en
P2860
P1476
Structural dynamics of muscle protein phosphorylation
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P2093
Brett A Colson
Simon J Gruber
P2860
P2888
P304
P356
10.1007/S10974-012-9317-6
P577
2012-08-29T00:00:00Z
P5875
P6179
1004020802