Results 21 to 30 of about 53,903 (284)
Sarcomere lattice geometry influences cooperative myosin binding in muscle. [PDF]
PLoS 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
Cardiac thin filament regulation [PDF]
Pflügers Archiv - European Journal of Physiology, 2008 Myocardial contraction is initiated upon the release of calcium into the cytosol from the sarcoplasmic reticulum following membrane depolarization. The fundamental physiological role of the heart is to pump an amount blood that is determined by the prevailing requirements of the body.
Tomoyoshi, Kobayashi +2 more
openaire +2 more sources
Nebulin and Lmod2 are critical for specifying thin-filament length in skeletal muscle. [PDF]
Sci Adv, 2020 Regulating the thin-filament length in muscle is crucial for controlling the number of myosin motors that generate power. The giant protein nebulin forms a long slender filament that associates along the length of the thin filament in skeletal muscle ...
Kiss B +10 more
europepmc +2 more sources
PLoS Genetics, 2022 Myofibrils within skeletal muscle are composed of sarcomeres that generate force by contraction when their myosin-rich thick filaments slide past actin-based thin filaments.
Joachim Berger +5 more
doaj +1 more source
Cells, 2023 As an essential component of the sarcomere, actin thin filament stems from the Z-disk extend toward the middle of the sarcomere and overlaps with myosin thick filaments. Elongation of the cardiac thin filament is essential for normal sarcomere maturation
Reiri Sono +18 more
doaj +1 more source
Single-molecule imaging reveals the concerted release of myosin from regulated thin filaments
eLife, 2021 Regulated thin filaments (RTFs) tightly control striated muscle contraction through calcium binding to troponin, which enables tropomyosin to expose myosin-binding sites on actin. Myosin binding holds tropomyosin in an open position, exposing more myosin-
Quentin M Smith +4 more
doaj +1 more source
Leiomodin creates a leaky cap at the pointed end of actin-thin filaments.
PLoS Biology, 2020 Improper lengths of actin-thin filaments are associated with altered contractile activity and lethal myopathies. Leiomodin, a member of the tropomodulin family of proteins, is critical in thin filament assembly and maintenance; however, its role is under
Dmitri Tolkatchev +7 more
doaj +1 more source
Polymeric filament thinning and breakup in microchannels [PDF]
Physical Review E, 2008 The effects of elasticity on filament thinning and breakup are investigated in microchannel cross flow. When a viscous solution is stretched by an external immiscible fluid, a low 100 ppm polymer concentration strongly affects the breakup process, compared to the Newtonian case.
Arratia, Paulo E +2 more
openaire +5 more sources
Thermal Activation of Thin Filaments in Striated Muscle
Frontiers in Physiology, 2020 In skeletal and cardiac muscles, contraction is triggered by an increase in the intracellular Ca2+ concentration. During Ca2+ transients, Ca2+-binding to troponin C shifts the “on–off” equilibrium of the thin filament state toward the “on” sate ...
Shuya Ishii +7 more
doaj +1 more source
Cycling Cross-Bridges Contribute to Thin Filament Activation in Human Slow-Twitch Fibers
Frontiers in Physiology, 2020 It has been shown that not only calcium but also strong binding myosin heads contribute to thin filament activation in isometrically contracting animal fast-twitch and cardiac muscle preparations. This behavior has not been studied in human muscle fibers
Alfredo Jesus López-Dávila +9 more
doaj +1 more source