Work

Regulation of Class I and Class II Myosins by Heavy Chain Phosphorylation

Year: 1996

Type: article

Abstract: Myosins have been traditionally viewed as mechanochemical, actin-activated MgATPases that convert the energy of ATP hydrolysis into force between actin and myosin filaments exhibited as either movement (isotonic contraction) or tension (isometric contraction). “Conventional” myosins, i.e. myosins that form filaments, consist of a pair of heavy chains (∼200 kDa) and two pairs of light chains, the regulatory light chain and the essential light chain. Each heavy chain has an N-terminal, globular head, where the actin-activated ATPase activity resides, and a C-terminal tail, through which the two heavy chains interact to form an α-helical coiled-coil rod.

Source: Journal of Biological Chemistry

DOI: 10.1074/jbc.271.29.16983

Authors: Hanna Brzeska, Edward D. Korn

Institutions: National Institutes of Health, National Heart, Lung, and Blood Institute

Language: English

Topic: Cardiomyopathy and Myosin Studies

Subfield: Cardiology and Cardiovascular Medicine

Field: Medicine

Domain: Health Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W1980148334

FWCI: 9.549

Cites: 60

Cited by: 96

Related to: 10