In cardiac and skeletal muscles, myofilaments are key molecular regulators of the contraction. Indeed, thick-thin filament interactions (via the formation of myosin cross-bridges) lead to force ...

The giant striated muscle protein titin integrates into the developing sarcomere to form a stable myofilament system that is extended as myocytes fuse. The logistics underlying myofilament assembly ...

† Department of Bioengineering, University of California at San Diego, La Jolla, California 92093, United States ‡ Department of Chemistry & Biochemistry, Ohio State University, Columbus, Ohio 43210, ...

Phosphorylation of sarcomeric proteins has been implicated in heart failure with preserved ejection fraction (HFpEF); such changes may contribute to diastolic dysfunction by altering contractility, ...

The Frank–Starling law of the heart describes the heart’s ability to enhance contractility in response to increased cardiac filling. This property is fundamental to how humans maintain cardiovascular ...

Titin-based myofilament stiffness is largely modulated by phosphorylation of its elastic I-band regions N2-Bus (decreases passive stiffness, PT) and PEVK (increases PT). Here, we tested the hypothesis ...

Cell cortex remodeling during cell division is a result of myofilament-driven contractility of the cortical membrane-bound actin meshwork. Little is known about the interaction between individual ...

Ca binding to the troponin complex represents a major portion of cytosolic Ca buffering. Troponin mutations that increase myofilament Ca sensitivity are associated with familial hypertrophic ...

We investigated the influence of cardiac myosin binding protein-C (cMyBP-C) and its constitutively unphosphorylated status on the radial and longitudinal stiffnesses of the myofilament lattice in ...

Mutations in myofilament proteins, most commonly MYBPC3-encoded myosin-binding protein C and MYH7-encoded beta-myosin heavy chain, can cause hypertrophic cardiomyopathy (HCM). Despite significant ...