Structural changes accompanying phosphorylation of tarantula muscle myosin filaments.
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Myosin light chain kinase and the role of myosin light chain phosphorylation in skeletal muscleStructure of myosin filaments from relaxed Lethocerus flight muscle by cryo-EM at 6 Å resolution.Three-Dimensional Reconstruction of Tarantula Myosin Filaments Suggests How Phosphorylation May Regulate Myosin ActivityPhosphorylation of the regulatory light chain of myosin in striated muscle: methodological perspectivesStructural basis of the relaxed state of a Ca2+-regulated myosin filament and its evolutionary implications.A method for 3D-reconstruction of a muscle thick filament using the tilt series images of a single filament electron tomogramAnalysis of tarantula skeletal muscle protein sequences and identification of transcriptional isoformsPhosphorylation-dependent power output of transgenic flies: an integrated study.The kinetics underlying the velocity of smooth muscle myosin filament sliding on actin filaments in vitro.A molecular model of phosphorylation-based activation and potentiation of tarantula muscle thick filamentsDisorder induced in nonoverlap myosin cross-bridges by loss of adenosine triphosphate.Function of the N terminus of the myosin essential light chain of vertebrate striated muscle.Multiple structures of thick filaments in resting cardiac muscle and their influence on cross-bridge interactions.Purification of native myosin filaments from muscle.Kinetic effects of myosin regulatory light chain phosphorylation on skeletal muscle contraction.Auxotonic to isometric contraction transitioning in a beating heart causes myosin step-size to down shift.Blebbistatin stabilizes the helical order of myosin filaments by promoting the switch 2 closed state.Charge replacement near the phosphorylatable serine of the myosin regulatory light chain mimics aspects of phosphorylation.Tarantula myosin free head regulatory light chain phosphorylation stiffens N-terminal extension, releasing it and blocking its docking back.Sequential myosin phosphorylation activates tarantula thick filament via a disorder-order transition.An invertebrate smooth muscle with striated muscle myosin filaments.Arrangement of myosin heads on Limulus thick filaments.Multiple phosphorylated variants of the high molecular mass subunit of neurofilaments in axons of retinal cell neurons: characterization and evidence for their differential association with stationary and moving neurofilaments.Structural changes induced in Ca2+-regulated myosin filaments by Ca2+ and ATP.Drosophila non-muscle myosin II motor activity determines the rate of tissue foldingComparison of orientation and rotational motion of skeletal muscle cross-bridges containing phosphorylated and dephosphorylated myosin regulatory light chain.Conserved Intramolecular Interactions Maintain Myosin Interacting-Heads Motifs Explaining Tarantula Muscle Super-Relaxed State Structural Basis.X-ray diffraction analysis of the effects of myosin regulatory light chain phosphorylation and butanedione monoxime on skinned skeletal muscle fibers.Myosin filament 3D structure in mammalian cardiac muscleVarious Themes of Myosin Regulation.Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.Different head environments in tarantula thick filaments support a cooperative activation process.Regulatory and catalytic domain dynamics of smooth muscle myosin filaments.Isolation, electron microscopy and 3D reconstruction of invertebrate muscle myofilamentsMesoscopic analysis of motion and conformation of cross-bridges.Hypertrophic cardiomyopathy and the myosin mesa: viewing an old disease in a new light.Myosin regulatory light chain phosphorylation and the production of functionally significant changes in myosin head arrangement on striated muscle thick filaments.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.Atomic model of a myosin filament in the relaxed state.
P2860
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P2860
Structural changes accompanying phosphorylation of tarantula muscle myosin filaments.
description
1987 nî lūn-bûn
@nan
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
1987年论文
@zh
1987年论文
@zh-cn
name
Structural changes accompanying phosphorylation of tarantula muscle myosin filaments.
@ast
Structural changes accompanying phosphorylation of tarantula muscle myosin filaments.
@en
type
label
Structural changes accompanying phosphorylation of tarantula muscle myosin filaments.
@ast
Structural changes accompanying phosphorylation of tarantula muscle myosin filaments.
@en
prefLabel
Structural changes accompanying phosphorylation of tarantula muscle myosin filaments.
@ast
Structural changes accompanying phosphorylation of tarantula muscle myosin filaments.
@en
P2093
P2860
P356
P1476
Structural changes accompanying phosphorylation of tarantula muscle myosin filaments.
@en
P2093
J Kendrick-Jones
P2860
P304
P356
10.1083/JCB.105.3.1319
P407
P577
1987-09-01T00:00:00Z