"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
|
| 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 |
|---|
| 2001 | 2 | 0 | 2 |
| 2002 | 0 | 1 | 1 |
| 2003 | 1 | 0 | 1 |
| 2006 | 1 | 0 | 1 |
| 2007 | 1 | 0 | 1 |
| 2009 | 0 | 1 | 1 |
| 2010 | 1 | 0 | 1 |
| 2011 | 0 | 1 | 1 |
| 2014 | 1 | 1 | 2 |
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Below are the most recent publications written about "Myosins" by people in Profiles.
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Menko AS, Bleaken BM, Libowitz AA, Zhang L, Stepp MA, Walker JL. A central role for vimentin in regulating repair function during healing of the lens epithelium. Mol Biol Cell. 2014 Mar; 25(6):776-90.
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Menko AS, Bleaken BM, Walker JL. Regional-specific alterations in cell-cell junctions, cytoskeletal networks and myosin-mediated mechanical cues coordinate collectivity of movement of epithelial cells in response to injury. Exp Cell Res. 2014 Mar 10; 322(1):133-48.
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Belo A, Cheng K, Chahdi A, Shant J, Xie G, Khurana S, Raufman JP. Muscarinic receptor agonists stimulate human colon cancer cell migration and invasion. Am J Physiol Gastrointest Liver Physiol. 2011 May; 300(5):G749-60.
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Butler TM, Siegman MJ. Mechanism of catch force: tethering of thick and thin filaments by twitchin. J Biomed Biotechnol. 2010; 2010:725207.
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Mori S, Iwaoka R, Eto M, Ohki SY. Solution structure of the inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1. Proteins. 2009 Nov 15; 77(3):732-5.
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Franke AS, Mooers SU, Narayan SR, Siegman MJ, Butler TM. Myosin cross-bridge kinetics and the mechanism of catch. Biophys J. 2007 Jul 15; 93(2):554-65.
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Butler TM, Mooers SU, Siegman MJ. Catch force links and the low to high force transition of myosin. Biophys J. 2006 May 1; 90(9):3193-202.
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Nemoto H, Bhopale MK, Constantinescu CS, Schotland D, Rostami A. Skeletal muscle myosin is the autoantigen for experimental autoimmune myositis. Exp Mol Pathol. 2003 Jun; 74(3):238-43.
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Ding J, Wexler AS, Binder-Macleod SA. A mathematical model that predicts the force-frequency relationship of human skeletal muscle. Muscle Nerve. 2002 Oct; 26(4):477-85.
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Le Goff L, Amblard F, Furst EM. Motor-driven dynamics in actin-myosin networks. Phys Rev Lett. 2002 Jan 7; 88(1):018101.