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Three-Dimensional Reconstruction of Tarantula Myosin Filaments Suggests How Phosphorylation May Regulate Myosin ActivityUnderstanding the organisation and role of myosin binding protein C in normal striated muscle by comparison with MyBP-C knockout cardiac muscleDirect visualization of myosin-binding protein C bridging myosin and actin filaments in intact muscle.A method for 3D-reconstruction of a muscle thick filament using the tilt series images of a single filament electron tomogramA molecular model of phosphorylation-based activation and potentiation of tarantula muscle thick filamentsPurification of native myosin filaments from muscle.Blebbistatin stabilizes the helical order of myosin filaments by promoting the switch 2 closed state.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.Conserved Intramolecular Interactions Maintain Myosin Interacting-Heads Motifs Explaining Tarantula Muscle Super-Relaxed State Structural Basis.Different head environments in tarantula thick filaments support a cooperative activation process.Matching structural densities from different biophysical origins with gain and bias.Lessons from a tarantula: new insights into muscle thick filament and myosin interacting-heads motif structure and function.Atomic model of a myosin filament in the relaxed state.Effects of myosin variants on interacting-heads motif explain distinct hypertrophic and dilated cardiomyopathy phenotypes.Mechanism of phosphorylation of the regulatory light chain of myosin from tarantula striated muscle.Helical order in tarantula thick filaments requires the "closed" conformation of the myosin head.Lessons from a tarantula: new insights into myosin interacting-heads motif evolution and its implications on disease.Interacting-heads motif has been conserved as a mechanism of myosin II inhibition since before the origin of animals.Structure of the myosin filaments of relaxed and rigor vertebrate striated muscle studied by rapid freezing electron microscopyX-ray diffraction study of the structural changes accompanying phosphorylation of tarantula muscleVisualization of myosin helices in sections of rapidly frozen relaxed tarantula muscleThe effect of the ATP analogue AMPPNP on the structure of crossbridges in vertebrate skeletal muscles: X-ray diffraction and mechanical studiesThree-dimensional reconstruction of thick filaments from rapidly frozen, freeze-substituted tarantula muscleDirect visualization of myosin filament symmetry in tarantula striated muscle by electron microscopyA new model for the surface arrangement of myosin molecules in tarantula thick filamentsHeterogeneity of Z-band structure within a single muscle sarcomere: implications for sarcomere assemblyMyosin Sequestration Regulates Sarcomere Function, Cardiomyocyte Energetics, and Metabolism, Informing the Pathogenesis of Hypertrophic Cardiomyopathy18O labeling on Ser45 but not on Ser35 supports the cooperative phosphorylation mechanism on tarantula thick filament activationThe myosin interacting-heads motif present in live tarantula muscle explains tetanic and posttetanic phosphorylation mechanisms
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description
hulumtues
@sq
onderzoeker
@nl
researcher
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հետազոտող
@hy
name
Raúl Padrón
@ast
Raúl Padrón
@en
Raúl Padrón
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Raúl Padrón
@nl
Raúl Padrón
@sl
type
label
Raúl Padrón
@ast
Raúl Padrón
@en
Raúl Padrón
@es
Raúl Padrón
@nl
Raúl Padrón
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prefLabel
Raúl Padrón
@ast
Raúl Padrón
@en
Raúl Padrón
@es
Raúl Padrón
@nl
Raúl Padrón
@sl
P106
P1153
7006981954
P21
P31
P496
0000-0002-1412-2450