"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
|
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
|
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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1994 | 1 | 0 | 1 |
1995 | 0 | 1 | 1 |
1999 | 0 | 1 | 1 |
2013 | 1 | 0 | 1 |
2014 | 1 | 0 | 1 |
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Below are the most recent publications written about "Myosins" by people in Profiles.
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Processing-body movement in Arabidopsis depends on an interaction between myosins and DECAPPING PROTEIN1. Plant Physiol. 2014 Apr; 164(4):1879-92.
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A common variant in myosin-18B contributes to mathematical abilities in children with dyslexia and intraparietal sulcus variability in adults. Transl Psychiatry. 2013 Feb 19; 3:e229.
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Rescue of high expression beta-tropomyosin transgenic mice by 5-propyl-2-thiouracil. Regulating the alpha-myosin heavy chain promoter. J Biol Chem. 1999 Oct 08; 274(41):29558-63.
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Rapid synthesis of hybrid RNA molecules associated with leukemia-specific chromosomal translocations. Leukemia. 1995 Apr; 9(4):719-22.
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Caffeine and Ca2+ stimulate mitochondrial oxidative phosphorylation in saponin-skinned human skeletal muscle fibers due to activation of actomyosin ATPase. Biochim Biophys Acta. 1994 Dec 30; 1188(3):373-9.
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Mitochondrial oxidative phosphorylation in saponin-skinned human muscle fibers is stimulated by caffeine. FEBS Lett. 1993 May 24; 323(1-2):188-90.
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Induction of endogenous myosin light chain 1 and cardiac alpha-actin expression in L6E9 cells by MyoD1. J Biol Chem. 1992 Sep 15; 267(26):18728-34.
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Reprogramming of myosin light chain 1/3 expression in muscle heterokaryons. Dev Biol. 1991 May; 145(1):28-39.