"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.
To see the data from this visualization as text,
click here.
Year | Major Topic | Minor Topic | Total |
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1994 | 2 | 0 | 2 |
1995 | 1 | 0 | 1 |
1996 | 0 | 1 | 1 |
1997 | 1 | 0 | 1 |
2002 | 0 | 2 | 2 |
2003 | 0 | 2 | 2 |
2005 | 0 | 2 | 2 |
2006 | 0 | 1 | 1 |
2010 | 0 | 1 | 1 |
2011 | 1 | 1 | 2 |
2012 | 2 | 1 | 3 |
2013 | 0 | 1 | 1 |
2014 | 0 | 1 | 1 |
2016 | 1 | 1 | 2 |
2020 | 0 | 1 | 1 |
2022 | 0 | 1 | 1 |
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Below are the most recent publications written about "Myosins" by people in Profiles.
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Unique and shared systemic biomarkers for emphysema in Alpha-1 Antitrypsin deficiency and chronic obstructive pulmonary disease. EBioMedicine. 2022 Oct; 84:104262.
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Study of the Expression Transition of Cardiac Myosin Using Polarization-Dependent SHG Microscopy. Biophys J. 2020 03 10; 118(5):1058-1066.
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Nucleoside-Diphosphate-Kinase of P. gingivalis is Secreted from Epithelial Cells In the Absence of a Leader Sequence Through a Pannexin-1 Interactome. Sci Rep. 2016 11 24; 6:37643.
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Disassembly of myofibrils and potential imbalanced forces on Z-discs in cultured adult cardiomyocytes. Cytoskeleton (Hoboken). 2016 May; 73(5):246-57.
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Scaffold-free tissue engineering: organization of the tissue cytoskeleton and its effects on tissue shape. Ann Biomed Eng. 2014 May; 42(5):1049-61.
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Inhibitor ?B kinase 2 is a myosin light chain kinase in vascular smooth muscle. Circ Res. 2013 Aug 16; 113(5):562-70.
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Myosin filament assembly onto myofibrils in live neonatal cardiomyocytes observed by TPEF-SHG microscopy. Cardiovasc Res. 2013 Feb 01; 97(2):262-70.
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Myosin cross-bridge dynamics in patients with hypertension and concentric left ventricular remodeling. Circ Heart Fail. 2012 Nov; 5(6):803-11.
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Direct imaging of RAB27B-enriched secretory vesicle biogenesis in lacrimal acinar cells reveals origins on a nascent vesicle budding site. PLoS One. 2012; 7(2):e31789.
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Rab27b regulates exocytosis of secretory vesicles in acinar epithelial cells from the lacrimal gland. Am J Physiol Cell Physiol. 2011 Aug; 301(2):C507-21.