Myosins
"Myosins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain.
Descriptor ID |
D009218
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MeSH Number(s) |
D05.750.078.730.475 D08.811.277.040.025.193.750 D12.776.210.500.600 D12.776.220.525.475
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Concept/Terms |
Myosins- Myosins
- Adenosine Triphosphatase, Myosin
- Myosin Adenosine Triphosphatase
- Adenosinetriphosphatase, Myosin
- Myosin ATPase
- ATPase, Myosin
- Myosin
- Myosin Adenosinetriphosphatase
- Actin-Activated ATPase
- Actin Activated ATPase
- ATPase, Actin-Activated
- ATPase, Actin Activated
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Below are MeSH descriptors whose meaning is more general than "Myosins".
Below are MeSH descriptors whose meaning is more specific than "Myosins".
This graph shows the total number of publications written about "Myosins" by people in this website by year, and whether "Myosins" was a major or minor topic of these publications.
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Year | Major Topic | Minor Topic | Total |
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1983 | 0 | 1 | 1 | 1994 | 0 | 2 | 2 | 1995 | 0 | 1 | 1 | 2001 | 0 | 1 | 1 |
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Below are the most recent publications written about "Myosins" by people in Profiles.
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Sprung J, Ogletree-Hughes ML, McConnell BK, Zakhary DR, Smolsky SM, Moravec CS. The effects of propofol on the contractility of failing and nonfailing human heart muscles. Anesth Analg. 2001 Sep; 93(3):550-9.
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Milano CA, Allen LF, Dolber PC, Johnson TD, Rockman HA, Bond RA, Lefkowitz RJ. Marked enhancement in myocardial function resulting from overexpression of a human beta-adrenergic receptor gene. J Thorac Cardiovasc Surg. 1995 Feb; 109(2):236-41.
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Milano CA, Dolber PC, Rockman HA, Bond RA, Venable ME, Allen LF, Lefkowitz RJ. Myocardial expression of a constitutively active alpha 1B-adrenergic receptor in transgenic mice induces cardiac hypertrophy. Proc Natl Acad Sci U S A. 1994 Oct 11; 91(21):10109-13.
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Milano CA, Allen LF, Rockman HA, Dolber PC, McMinn TR, Chien KR, Johnson TD, Bond RA, Lefkowitz RJ. Enhanced myocardial function in transgenic mice overexpressing the beta 2-adrenergic receptor. Science. 1994 Apr 22; 264(5158):582-6.
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Schwartz RJ, Stone EM. Cloning of contractile protein genes. Cell Muscle Motil. 1983; 3:195-257.
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