"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 |
|---|
| 1995 | 0 | 1 | 1 |
| 1997 | 1 | 0 | 1 |
| 1998 | 0 | 1 | 1 |
| 1999 | 1 | 0 | 1 |
| 2000 | 0 | 2 | 2 |
| 2001 | 1 | 1 | 2 |
| 2002 | 1 | 1 | 2 |
| 2004 | 0 | 2 | 2 |
| 2005 | 0 | 1 | 1 |
| 2007 | 1 | 0 | 1 |
| 2008 | 0 | 1 | 1 |
| 2011 | 1 | 0 | 1 |
| 2013 | 1 | 0 | 1 |
| 2015 | 1 | 0 | 1 |
| 2016 | 1 | 0 | 1 |
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Below are the most recent publications written about "Myosins" by people in Profiles.
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Bioinformatics reveal elevated levels of Myosin Vb in uterine corpus endometrial carcinoma patients which correlates to increased cell metabolism and poor prognosis. PLoS One. 2023; 18(1):e0280428.
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A postnatal role for embryonic myosin revealed by MYH3 mutations that alter TGF? signaling and cause autosomal dominant spondylocarpotarsal synostosis. Sci Rep. 2017 02 16; 7:41803.
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Harnessing molecular motors for nanoscale pulldown in live cells. Mol Biol Cell. 2017 Feb 01; 28(3):463-475.
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-Back-to-back mechanisms drive actomyosin ring closure during Drosophila embryo cleavage. J Cell Biol. 2016 Nov 07; 215(3):335-344.
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Genome-Wide miRNA Analysis Identifies miR-188-3p as a Novel Prognostic Marker and Molecular Factor Involved in Colorectal Carcinogenesis. Clin Cancer Res. 2017 Mar 01; 23(5):1323-1333.
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Mutational Spectrum of MYO15A and the Molecular Mechanisms of DFNB3 Human Deafness. Hum Mutat. 2016 10; 37(10):991-1003.
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The E3 ligase Ubr3 regulates Usher syndrome and MYH9 disorder proteins in the auditory organs of Drosophila and mammals. Elife. 2016 06 22; 5.
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DNA Diagnostics of Hereditary Hearing Loss: A Targeted Resequencing Approach Combined with a Mutation Classification System. Hum Mutat. 2016 08; 37(8):812-9.
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Mass Spectrometry and Antibody-Based Characterization of Blood Vessels from Brachylophosaurus canadensis. J Proteome Res. 2015 Dec 04; 14(12):5252-62.
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Autosomal-Dominant Multiple Pterygium Syndrome Is Caused by Mutations in MYH3. Am J Hum Genet. 2015 May 07; 96(5):841-9.