"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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1995 | 1 | 0 | 1 |
1997 | 0 | 2 | 2 |
1999 | 1 | 1 | 2 |
2000 | 0 | 1 | 1 |
2001 | 3 | 2 | 5 |
2002 | 1 | 0 | 1 |
2004 | 0 | 1 | 1 |
2005 | 0 | 4 | 4 |
2006 | 0 | 1 | 1 |
2007 | 2 | 3 | 5 |
2008 | 1 | 2 | 3 |
2009 | 2 | 1 | 3 |
2010 | 3 | 1 | 4 |
2011 | 2 | 1 | 3 |
2014 | 0 | 1 | 1 |
2015 | 3 | 0 | 3 |
2016 | 2 | 1 | 3 |
2017 | 2 | 0 | 2 |
2018 | 0 | 2 | 2 |
2019 | 1 | 2 | 3 |
2020 | 2 | 1 | 3 |
2021 | 0 | 2 | 2 |
2022 | 0 | 2 | 2 |
2023 | 1 | 5 | 6 |
2024 | 1 | 1 | 2 |
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Below are the most recent publications written about "Myosins" by people in Profiles.
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Hundreds of myosin 10s are pushed to the tips of filopodia and could cause traffic jams on actin. Elife. 2024 Oct 31; 12.
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Dachsous and Fat coordinately repress the Dachs-Dlish-Approximated complex to control growth. J Cell Biol. 2024 Dec 02; 223(12).
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Myosin-binding protein H-like regulates myosin-binding protein distribution and function in atrial cardiomyocytes. Proc Natl Acad Sci U S A. 2023 Dec 19; 120(51):e2314920120.
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Limiting pool and actin architecture controls myosin cluster sizes in adherent cells. Biophys J. 2024 Jan 16; 123(2):157-171.
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Measuring response functions of active materials from data. Proc Natl Acad Sci U S A. 2023 10 17; 120(42):e2305283120.
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Septins regulate border cell surface geometry, shape, and motility downstream of Rho in Drosophila. Dev Cell. 2023 08 07; 58(15):1399-1413.e5.
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Acetylation of fission yeast tropomyosin does not promote differential association with cognate formins. Cytoskeleton (Hoboken). 2023 03; 80(3-4):77-92.
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Geometric control of myosin II orientation during axis elongation. Elife. 2023 01 30; 12.
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Aurora A and cortical flows promote polarization and cytokinesis by inducing asymmetric ECT-2 accumulation. Elife. 2022 12 19; 11.
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Partial and complete loss of myosin binding protein H-like cause cardiac conduction defects. J Mol Cell Cardiol. 2022 08; 169:28-40.