Helical order in tarantula thick filaments requires the "closed" conformation of the myosin head.
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Three-Dimensional Reconstruction of Tarantula Myosin Filaments Suggests How Phosphorylation May Regulate Myosin ActivityThree-dimensional structure of vertebrate cardiac muscle myosin filaments.Direct demonstration of the cross-bridge recovery stroke in muscle thick filaments in aqueous solution by using the hydration chamber.The myosin inhibitor blebbistatin stabilizes the super-relaxed state in skeletal muscleBlebbistatin stabilizes the helical order of myosin filaments by promoting the switch 2 closed state.Stabilization of helical order in the thick filaments by blebbistatin: further evidence of coexisting multiple conformations of myosinStructural characterization of the binding of Myosin*ADP*Pi to actin in permeabilized rabbit psoas muscle.Conserved Intramolecular Interactions Maintain Myosin Interacting-Heads Motifs Explaining Tarantula Muscle Super-Relaxed State Structural Basis.Head-head and head-tail interaction: a general mechanism for switching off myosin II activity in cellsInvertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.Role of the tail in the regulated state of myosin 2.Lessons from a tarantula: new insights into muscle thick filament and myosin interacting-heads motif structure and function.Head-head interaction characterizes the relaxed state of Limulus muscle myosin filaments.Effects of myosin variants on interacting-heads motif explain distinct hypertrophic and dilated cardiomyopathy phenotypes.Millisecond time-resolved changes occurring in Ca2+-regulated myosin filaments upon relaxation.The Conformation of Myosin Heads in Relaxed Skeletal Muscle: Implications for Myosin-Based Regulation.Omecamtiv mercabil and blebbistatin modulate cardiac contractility by perturbing the regulatory state of the myosin filament.Effects of myosin inhibitors on the X-ray diffraction patterns of relaxed and calcium-activated rabbit skeletal muscle fibers.
P2860
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P2860
Helical order in tarantula thick filaments requires the "closed" conformation of the myosin head.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年學術文章
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2004年學術文章
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name
Helical order in tarantula thi ...... nformation of the myosin head.
@en
Helical order in tarantula thi ...... nformation of the myosin head.
@nl
type
label
Helical order in tarantula thi ...... nformation of the myosin head.
@en
Helical order in tarantula thi ...... nformation of the myosin head.
@nl
prefLabel
Helical order in tarantula thi ...... nformation of the myosin head.
@en
Helical order in tarantula thi ...... nformation of the myosin head.
@nl
P1476
Helical order in tarantula thi ...... onformation of the myosin head
@en
P2093
P304
P356
10.1016/J.JMB.2004.07.037
P407
P577
2004-09-01T00:00:00Z