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Three-Dimensional Reconstruction of Tarantula Myosin Filaments Suggests How Phosphorylation May Regulate Myosin ActivityA 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 filamentsTarantula 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.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.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.18O 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
@en
հետազոտող
@hy
name
Antonio Pinto
@ast
Antonio Pinto
@en
Antonio Pinto
@es
Antonio Pinto
@nl
Antonio Pinto
@sl
type
label
Antonio Pinto
@ast
Antonio Pinto
@en
Antonio Pinto
@es
Antonio Pinto
@nl
Antonio Pinto
@sl
prefLabel
Antonio Pinto
@ast
Antonio Pinto
@en
Antonio Pinto
@es
Antonio Pinto
@nl
Antonio Pinto
@sl
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P21
P31
P496
0000-0002-0665-9872