"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 |
|---|
| 1992 | 2 | 1 | 3 |
| 1993 | 2 | 1 | 3 |
| 1994 | 2 | 1 | 3 |
| 1996 | 1 | 0 | 1 |
| 1997 | 1 | 1 | 2 |
| 1998 | 1 | 0 | 1 |
| 2000 | 0 | 1 | 1 |
| 2001 | 4 | 1 | 5 |
| 2002 | 3 | 0 | 3 |
| 2003 | 1 | 3 | 4 |
| 2004 | 3 | 2 | 5 |
| 2005 | 2 | 0 | 2 |
| 2006 | 3 | 1 | 4 |
| 2008 | 7 | 1 | 8 |
| 2009 | 1 | 3 | 4 |
| 2010 | 1 | 0 | 1 |
| 2011 | 2 | 1 | 3 |
| 2012 | 2 | 0 | 2 |
| 2013 | 3 | 1 | 4 |
| 2014 | 1 | 2 | 3 |
| 2015 | 4 | 2 | 6 |
| 2016 | 1 | 0 | 1 |
| 2017 | 0 | 1 | 1 |
| 2018 | 2 | 0 | 2 |
| 2019 | 4 | 1 | 5 |
| 2020 | 4 | 0 | 4 |
| 2021 | 4 | 1 | 5 |
| 2022 | 2 | 0 | 2 |
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click here.
Below are the most recent publications written about "Myosins" by people in Profiles.
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Debold EP. Recent insights into the relative timing of myosin's powerstroke and release of phosphate. Cytoskeleton (Hoboken). 2021 Sep; 78(9):448-458.
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Koubassova NA, Tsaturyan AK, Bershitsky SY, Ferenczi MA, Padrón R, Craig R. Interacting-heads motif explains the X-ray diffraction pattern of relaxed vertebrate skeletal muscle. Biophys J. 2022 Apr 19; 121(8):1354-1366.
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Craig R, Padrón R. Structural basis of the super- and hyper-relaxed states of myosin II. J Gen Physiol. 2022 01 03; 154(1).
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Scott B, Marang C, Woodward M, Debold EP. Myosin's powerstroke occurs prior to the release of phosphate from the active site. Cytoskeleton (Hoboken). 2021 05; 78(5):185-198.
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Song T, McNamara JW, Ma W, Landim-Vieira M, Lee KH, Martin LA, Heiny JA, Lorenz JN, Craig R, Pinto JR, Irving T, Sadayappan S. Fast skeletal myosin-binding protein-C regulates fast skeletal muscle contraction. Proc Natl Acad Sci U S A. 2021 04 27; 118(17).
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Ma W, Duno-Miranda S, Irving T, Craig R, Padrón R. Relaxed tarantula skeletal muscle has two ATP energy-saving mechanisms. J Gen Physiol. 2021 03 01; 153(3).
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Shi T, Xiong Z, Liu H, Jin W, Mu J, Yuan L, Sun Q, McClements DJ, Gao R. Ameliorative effects of L-arginine? On heat-induced phase separation of Aristichthys nobilis myosin are associated with the absence of ordered secondary structures of myosin. Food Res Int. 2021 03; 141:110154.
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Orr RG, Furt F, Warner EL, Agar EM, Garbarino JM, Cabral SE, Dubuke ML, Butt AM, Munson M, Vidali L. Rab-E and its interaction with myosin XI are essential for polarised cell growth. New Phytol. 2021 02; 229(4):1924-1936.
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Shi T, Liu H, Song T, Xiong Z, Yuan L, McClements DJ, Jin W, Sun Q, Gao R. Use of l-arginine-assisted ultrasonic treatment to change the molecular and interfacial characteristics of fish myosin and enhance the physical stability of the emulsion. Food Chem. 2021 Apr 16; 342:128314.
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Woodward M, Ostrander E, Jeong SP, Liu X, Scott B, Unger M, Chen J, Venkataraman D, Debold EP. Positional Isomers of a Non-Nucleoside Substrate Differentially Affect Myosin Function. Biophys J. 2020 08 04; 119(3):567-580.