"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 |
|---|
| 1997 | 1 | 0 | 1 |
| 1998 | 0 | 1 | 1 |
| 1999 | 1 | 0 | 1 |
| 2000 | 0 | 2 | 2 |
| 2001 | 1 | 2 | 3 |
| 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 |
| 2014 | 0 | 1 | 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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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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Autosomal-Dominant Multiple Pterygium Syndrome Is Caused by Mutations in MYH3. Am J Hum Genet. 2015 May 07; 96(5):841-9.
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Molecular and functional consequences of mutations in the central helix of cardiac troponin C. Arch Biochem Biophys. 2014 Apr 15; 548:46-53.
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Protein phosphatase 1? limits ring canal constriction during Drosophila germline cyst formation. PLoS One. 2013; 8(7):e70502.
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Whole-exome sequencing identifies ALMS1, IQCB1, CNGA3, and MYO7A mutations in patients with Leber congenital amaurosis. Hum Mutat. 2011 Dec; 32(12):1450-9.
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Differential turnover of myosin chaperone UNC-45A isoforms increases in metastatic human breast cancer. J Mol Biol. 2011 Sep 23; 412(3):365-78.
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Genomic analysis reveals few genetic alterations in pediatric acute myeloid leukemia. Proc Natl Acad Sci U S A. 2009 Aug 04; 106(31):12944-9.
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A locus on chromosome 1 promotes susceptibility of experimental autoimmune myocarditis and lymphocyte cell death. Clin Immunol. 2009 Jan; 130(1):74-82.
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Metastatic basal cell carcinoma exhibits reduced actin expression. Mod Pathol. 2008 May; 21(5):540-3.
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Sequential roles for myosin-X in BMP6-dependent filopodial extension, migration, and activation of BMP receptors. J Cell Biol. 2007 Dec 31; 179(7):1569-82.