myosin


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Related to myosin: Myosin light chain kinase

myosin

 [mi´o-sin]
one of the two main proteins of muscle. Myosin and actin are the proteins involved in contraction of muscle fibers.

my·o·sin

(mī'ō-sin),
A globular protein present in muscle and in nonmuscle cells that has an ATPase activity; in combination with actin, it forms actomyosin; myosin forms the thick filaments in muscle.

myosin

(mī′ə-sĭn)
n.
Any of a class of proteins that bind with actin filaments and generate many kinds of cell movement, especially the contraction of myofibrils in muscle cells.

my·o·sin

(mī'ō-sin)
A globulin present in muscle; in combination with actin, it forms actomyosin; myosin forms the thick filaments in muscle.

myosin

a protein found in the thick filaments of the SARCOMERES OF MUSCLE. Myosin combines with ACTIN to produce ACTOMYOSIN during contraction.

my·o·sin

(mī'ō-sin)
A globulin present in muscle; in combination with actin, it forms actomyosin.
References in periodicals archive ?
Park and Lanier [31] found that there were three endothermic transition peaks for tilapia proteins after purification, mainly corresponding to myofibril (47.8[degrees]C), myosin (57.7[degrees]C), and actin (68[degrees]C).
"Considering that hundreds of these myosin molecules are doing this all the time, if they stay bound longer, at any given time you're going to have more myosin heads bound and pulling together than you otherwise would.
Han et al., "Solubilization of myosin in a solution of low ionic strength L-histidine: significance of the imidazole ring," Food Chemistry, vol.
Paul, "Myosin phosphorylation/ dephosphorylation and regulation of airway smooth muscle contractility," American Journal of Physiology-Lung Cellular and Molecular Physiology, vol.
Ichikawa et al., "Cellular force assay detects altered contractility caused by a nephritis-associated mutation in nonmuscle myosin IIA," Development, Growth & Differentiation, vol.
[121] mapped the pathogenic epitopes on the myosin molecules in 1996.
A 3D simulative structure (PDB ID:1g8xA) of MYO15A motor domain was built, which contained the myosin XVA protein residues 1261-1887.
Brain myosin-V is a two-headed unconventional myosin with motor activity.
This technique allowed us to monitor the sequence of events that result in ATP hydrolysis by the myosin molecule and the corresponding mechanical interactions between myosin and actin.
Myosin presence has been demonstrated in kidney descending vasa recta and in renal arterioles and could be involved in the regulation of the blood flow from descending vasa recta to capillary beds [55].
The origin of the force driving the retrograde movement has been attributed to the polymerization of actin and/or the motor function of nonmuscle myosin II.