In 1864, Kühne named a protein extracted from nematode muscle in high salt myosin and in 1939, Engelhardt and Ljubimowa determined that this protein possessed an ATPase activity. Later studies would determine that myosin is the major component of muscle thick filaments, and that its cyclic interactions with actin-containing thin filaments are the basis for muscle contraction. It would eventually be renamed myosin II to signify that the molecule is a dimer consisting of two polypeptide chains each with a globular head region and a long α-helical tail (Szent-Györgyi 2004). In 1969, a molecule resembling muscle myosin II was identified in slime mold, showing that myosin is a component of nonmuscle cells, too (Adelman and Taylor 1969). Subsequently, in 1973 a molecule with actin-activated ATPase activity resembling skeletal muscle myosin, although smaller in molecular weight and...
- El-Mezgueldi M, Bagshaw CR. The myosin family: biochemical and kientic properties. Protein. Cell Regul. 2008;7:55–93.Google Scholar
- Holmes KC. Myosin structure. In: Coluccio LM, editor. Myosins: a superfamily of molecular motors. Dordrecht: Springer; 2008. p. 35–54.Google Scholar
- Mooseker MS, Foth BJ. The structural and functional diversity of the myosin family. Protein Cell Regul. 2008;7:1–34. (Myosins: a superfamily of molecular motors [L.M. Coluccio, ed.]).Google Scholar
- Sellers JR, Weisman LS, Myosin V. Protein. Cell Regul. 2008;7:289–323.Google Scholar