The contraction of skeletal muscle is regulated by Ca 2+ binding to troponin C, which results
in an internal reorganization of the interactions within the troponin-tropomyosin complex …

Troponin (Tn), containing three subunits: Ca 2+ binding (TnC), inhibitory (TnI), and
tropomyosin binding (TnT), plays a crucial role in the Ca 2+ regulation of vertebrate striated …

In a wide variety of cellular settings, from organelle transport to muscle contraction, Ca2+
binding to members of the EF hand family of proteins controls the interaction between actin …

The in vitro Ca 2+ regulation of the actomyosin Mg 2+-ATPase at physiological ratios of
actin, tropomyosin, and troponin occurs only in the presence of troponin T. We have …

Calcium binding to regulatory sites located in the NH2-terminal domain of troponin C (TnC)
induces a conformational change that blocks the inhibitory action of troponin I (TnI) and …

The molecular switching mechanism governing skeletal and cardiac muscle contraction
couples the binding of Ca2+ on troponin to the movement of tropomyosin on actin filaments …

The troponin complex plays an essential role in the thin filament regulation of striated
muscle contraction. Of the three subunits of troponin, troponin I (TnI) is the actomyosin …

The primary structure of the COOH-terminal region of troponin I (TnI) is highly conserved
among the cardiac, slow, and fast skeletal muscle TnI isoforms and across species. Although …

Troponin and tropomyosin on actin filaments constitute a Ca2+-sensitive switch that
regulates the contraction of vertebrate striated muscle through a series of conformational …

Troponin T (TnT) binds to tropomyosin (Tm) to anchor the troponin complex in the thin
filament, and it thus serves as a vital link in the Ca2+ regulation of striated muscle …