Tropomyosin (Tm) bound to actin induces cooperative activation of actomyosin subfragment
1 (actin-S1) ATPase, observed as a sigmoid ATPase vs [S1] dependence. The activation is …

Ca2+ binding to myofibrillar regulatory sites can produce conformational changes allowing
cross-bridge attachment and cycling. Measurements of smooth muscle actomyosin ATPase …

For the past half century, the sliding filament-based cross-bridge theory has been the
cornerstone of our understanding of how muscles contract. According to this theory, active …

A mechanism for contraction in skeletal muscle is proposed in which the tension-generating
site is located within the core of the thick (myosin) filament, specifically within the trypsin …

Ca 2+ is the primary regulator of force generation by cross-bridges in striated muscle
activation and relaxation. Relaxation is as necessary as contraction and, while the kinetics of …

Force generation in striated muscle is primarily controlled by structural changes in the actin-
containing thin filaments triggered by an increase in intracellular calcium concentration …

Myosin light chain phosphorylation in permeable skeletal muscle fibers increases isometric
force and the rate of force production at submaximal levels of calcium activation; myosin light …

Length-dependent steady-state and dynamic responses of five models of isometric force
generation in cardiac myofilaments were compared with similar experimental data from the …

The ability of strong-binding myosin heads to activate the thin filament was investigated by
incubating skinned single muscle fibers with N-ethylmaleimide-(NEM) modified myosin …

During the past century, physiologists have made steady progress in elucidating the
molecular mechanisms of muscle contraction. However, this progress has so far failed to …