 Myosin Subfragments
"Myosin Subfragments" 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.
Parts of the myosin molecule resulting from cleavage by proteolytic enzymes (PAPAIN; TRYPSIN; or CHYMOTRYPSIN) at well-localized regions. Study of these isolated fragments helps to delineate the functional roles of different parts of myosin. Two of the most common subfragments are myosin S-1 and myosin S-2. S-1 contains the heads of the heavy chains plus the light chains and S-2 contains part of the double-stranded, alpha-helical, heavy chain tail (myosin rod).
| Descriptor ID |
D015879
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| MeSH Number(s) |
D05.750.078.730.475.300 D12.776.210.500.600.300 D12.776.220.525.475.300
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| Concept/Terms |
Heavy Meromyosin Subfragment-2- Heavy Meromyosin Subfragment-2
- Heavy Meromyosin Subfragment 2
- Meromyosin Subfragment-2, Heavy
- Subfragment-2, Heavy Meromyosin
- Myosin Subfragment-2
- Myosin Subfragment 2
- Subfragment-2, Myosin
- Myosin S-2
- Myosin S 2
Heavy Meromyosin Subfragment-1- Heavy Meromyosin Subfragment-1
- Heavy Meromyosin Subfragment 1
- Meromyosin Subfragment-1, Heavy
- Subfragment-1, Heavy Meromyosin
- Myosin Subfragment-1
- Myosin Subfragment 1
- Subfragment-1, Myosin
- ATPase, Actin-S1
- Actin-S1 ATPase
- Myosin S-1
- Myosin S 1
- Actin S1 ATPase
- ATPase, Actin S1
- Actomyosin Subfragment 1 ATPase
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Below are MeSH descriptors whose meaning is more general than "Myosin Subfragments".
Below are MeSH descriptors whose meaning is more specific than "Myosin Subfragments".
This graph shows the total number of publications written about "Myosin Subfragments" by people in this website by year, and whether "Myosin Subfragments" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1994 | 1 | 0 | 1 | | 2004 | 0 | 1 | 1 | | 2008 | 0 | 1 | 1 | | 2009 | 0 | 1 | 1 | | 2012 | 0 | 1 | 1 | | 2015 | 1 | 0 | 1 | | 2016 | 1 | 0 | 1 |
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Below are the most recent publications written about "Myosin Subfragments" by people in Profiles.
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Walklate J, Vera C, Bloemink MJ, Geeves MA, Leinwand L. The Most Prevalent Freeman-Sheldon Syndrome Mutations in the Embryonic Myosin Motor Share Functional Defects. J Biol Chem. 2016 May 06; 291(19):10318-31.
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Taylor KC, Buvoli M, Korkmaz EN, Buvoli A, Zheng Y, Heinze NT, Cui Q, Leinwand LA, Rayment I. Skip residues modulate the structural properties of the myosin rod and guide thick filament assembly. Proc Natl Acad Sci U S A. 2015 Jul 21; 112(29):E3806-15.
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Thompson RC, Buvoli M, Buvoli A, Leinwand LA. Myosin filament assembly requires a cluster of four positive residues located in the rod domain. FEBS Lett. 2012 Sep 21; 586(19):3008-12.
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Armel TZ, Leinwand LA. Mutations at the same amino acid in myosin that cause either skeletal or cardiac myopathy have distinct molecular phenotypes. J Mol Cell Cardiol. 2010 May; 48(5):1007-13.
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Resnicow DI, Hooft AM, Harrison BC, Baker JE, Leinwand LA. GFP fails to inhibit actin-myosin interactions in vitro. Nat Methods. 2008 Mar; 5(3):212-3; author reply 213-4.
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Stelzer JE, Patel JR, Olsson MC, Fitzsimons DP, Leinwand LA, Moss RL. Expression of cardiac troponin T with COOH-terminal truncation accelerates cross-bridge interaction kinetics in mouse myocardium. Am J Physiol Heart Circ Physiol. 2004 Oct; 287(4):H1756-61.
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Allen DL, Monke SR, Talmadge RJ, Roy RR, Edgerton VR. Plasticity of myonuclear number in hypertrophied and atrophied mammalian skeletal muscle fibers. J Appl Physiol (1985). 1995 May; 78(5):1969-76.
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LeBlanc-Straceski JM, Fukui Y, Sohn RL, Spudich JA, Leinwand LA. Functional analysis of a cardiac myosin rod in Dictyostelium discoideum. Cell Motil Cytoskeleton. 1994; 27(4):313-26.
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Frid MG, Shekhonin BV, Koteliansky VE, Glukhova MA. Phenotypic changes of human smooth muscle cells during development: late expression of heavy caldesmon and calponin. Dev Biol. 1992 Oct; 153(2):185-93.
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McNally E, Sohn R, Frankel S, Leinwand L. Expression of myosin and actin in Escherichia coli. Methods Enzymol. 1991; 196:368-89.
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