Results 1 to 10 of about 424,053 (243)

Thick filament‐associated myosin undergoes frequent replacement at the tip of the thick filament [PDF]

open access: yesFEBS Open Bio, 2022
Myosin plays a fundamental role in muscle contraction. Approximately 300 myosins form a bipolar thick filament, in which myosin is continuously replaced by protein turnover.
Emi Ichimura   +4 more
doaj   +6 more sources

Thick-Filament-Based Regulation and the Determinants of Force Generation

open access: yesBiomedicines
Background/Objectives: Thick-filament-based regulation in muscle is generally conceived as processes that modulate the number of myosin heads capable of force generation.
Vivek P. Jani, Weikang Ma
doaj   +4 more sources

The Effects of Hsp90α1 Mutations on Myosin Thick Filament Organization. [PDF]

open access: yesPLoS ONE, 2015
Heat shock protein 90α plays a key role in myosin folding and thick filament assembly in muscle cells. To assess the structure and function of Hsp90α and its potential regulation by post-translational modification, we developed a combined knockdown and ...
Qiuxia He   +3 more
doaj   +2 more sources

Contiguity and Structural Impacts of a Non-Myosin Protein within the Thick Filament Myosin Layers

open access: yesBiology, 2021
Myosin dimers arranged in layers and interspersed with non-myosin densities have been described by cryo-EM 3D reconstruction of the thick filament in Lethocerus at 5.5 Å resolution.
Lynda M. Menard   +2 more
doaj   +3 more sources

Thick Filament Mechano-Sensing in Skeletal and Cardiac Muscles: A Common Mechanism Able to Adapt the Energetic Cost of the Contraction to the Task

open access: yesFrontiers in Physiology, 2018
A dual regulation of contraction operates in both skeletal and cardiac muscles. The first mechanism, based on Ca2+-dependent structural changes of the regulatory proteins in the thin filament, makes the actin sites available for binding of the myosin ...
Gabriella Piazzesi   +4 more
doaj   +3 more sources

Thin filament cardiomyopathies: A review of genetics, disease mechanisms, and emerging therapeutics

open access: yesFrontiers in Cardiovascular Medicine, 2022
All muscle contraction occurs due to the cyclical interaction between sarcomeric thin and thick filament proteins within the myocyte. The thin filament consists of the proteins actin, tropomyosin, Troponin C, Troponin I, and Troponin T.
Lucas K. Keyt   +7 more
doaj   +1 more source

Sarcomere lattice geometry influences cooperative myosin binding in muscle. [PDF]

open access: yesPLoS Computational Biology, 2007
In muscle, force emerges from myosin binding with actin (forming a cross-bridge). This actomyosin binding depends upon myofilament geometry, kinetics of thin-filament Ca(2+) activation, and kinetics of cross-bridge cycling.
Bertrand C W Tanner   +2 more
doaj   +1 more source

Myosin-based regulation of twitch and tetanic contractions in mammalian skeletal muscle

open access: yeseLife, 2021
Time-resolved X-ray diffraction of isolated fast-twitch muscles of mice was used to show how structural changes in the myosin-containing thick filaments contribute to the regulation of muscle contraction, extending the previous focus on regulation by the
Cameron Hill   +4 more
doaj   +1 more source

Head-head interactions of resting myosin crossbridges in intact frog skeletal muscles, revealed by synchrotron x-ray fiber diffraction. [PDF]

open access: yesPLoS ONE, 2012
The intensities of the myosin-based layer lines in the x-ray diffraction patterns from live resting frog skeletal muscles with full thick-thin filament overlap from which partial lattice sampling effects had been removed were analyzed to elucidate the ...
Kanji Oshima   +3 more
doaj   +1 more source

Force Measurements From Myofibril to Filament

open access: yesFrontiers in Physiology, 2022
Contractility, the generation of force and movement by molecular motors, is the hallmark of all muscles, including striated muscle. Contractility can be studied at every level of organization from a whole animal to single molecules.
Steven Marston
doaj   +1 more source

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