"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 | 1 | 0 | 1 |
| 1996 | 1 | 0 | 1 |
| 1999 | 1 | 0 | 1 |
| 2000 | 1 | 0 | 1 |
| 2002 | 1 | 0 | 1 |
| 2004 | 0 | 1 | 1 |
| 2006 | 1 | 0 | 1 |
| 2010 | 1 | 0 | 1 |
| 2011 | 2 | 1 | 3 |
| 2012 | 2 | 2 | 4 |
| 2013 | 1 | 0 | 1 |
| 2014 | 1 | 1 | 2 |
| 2015 | 1 | 0 | 1 |
| 2016 | 0 | 1 | 1 |
| 2020 | 0 | 1 | 1 |
| 2021 | 0 | 1 | 1 |
| 2022 | 0 | 1 | 1 |
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click here.
Below are the most recent publications written about "Myosins" by people in Profiles.
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Asante-Asamani E, Grange D, Rawal D, Santiago Z, Loustau J, Brazill D. A role for myosin II clusters and membrane energy in cortex rupture for Dictyostelium discoideum. PLoS One. 2022; 17(4):e0265380.
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M?ndez I, Fern?ndez AI, Espinosa M?, Cuenca S, Lorca R, Rodr?guez JF, Tamargo M, Garc?a-Montero M, G?mez C, Vilches S, V?zquez N, ?lvarez R, Medrano C, Yotti R, Fern?ndez-Avil?s F, Bermejo J. Founder mutation in myosin-binding protein C with an early onset and a high penetrance in males. Open Heart. 2021 09; 8(2).
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Domingues HS, Urbanski MM, Macedo-Ribeiro S, Almaktari A, Irfan A, Hernandez Y, Wang H, Relvas JB, Rubinstein B, Melendez-Vasquez CV, Pinto IM. Pushing myelination - developmental regulation of myosin expression drives oligodendrocyte morphological differentiation. J Cell Sci. 2020 08 05; 133(15).
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Rodr?Guez-Reyes N, Rodr?Guez-Zayas AE, Javadov S, Frontera WR. Single muscle fiber contractile properties in diabetic RAT muscle. Muscle Nerve. 2016 06; 53(6):958-64.
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Li C, Xiong YL. Disruption of secondary structure by oxidative stress alters the cross-linking pattern of myosin by microbial transglutaminase. Meat Sci. 2015 Oct; 108:97-105.
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Lu H, Zhao Q, Jiang H, Zhu T, Xia P, Seffens W, Aikhionbare F, Wang D, Dou Z, Yao X. Characterization of ring-like F-actin structure as a mechanical partner for spindle positioning in mitosis. PLoS One. 2014; 9(10):e102547.
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Gonz?lez-Sol? M, Al-Khayat HA, Behra M, Kensler RW. Zebrafish cardiac muscle thick filaments: isolation technique and three-dimensional structure. Biophys J. 2014 Apr 15; 106(8):1671-80.
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Li C, Xiong YL, Chen J. Protein oxidation at different salt concentrations affects the cross-linking and gelation of pork myofibrillar protein catalyzed by microbial transglutaminase. J Food Sci. 2013 Jun; 78(6):C823-31.
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Al-Khayat HA, Kensler RW, Squire JM, Marston SB, Morris EP. Atomic model of the human cardiac muscle myosin filament. Proc Natl Acad Sci U S A. 2013 Jan 02; 110(1):318-23.
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Li C, Xiong YL, Chen J. Oxidation-induced unfolding facilitates Myosin cross-linking in myofibrillar protein by microbial transglutaminase. J Agric Food Chem. 2012 Aug 15; 60(32):8020-7.