"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 |
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1995 | 2 | 0 | 2 |
1997 | 1 | 0 | 1 |
1998 | 1 | 0 | 1 |
2001 | 0 | 1 | 1 |
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Below are the most recent publications written about "Myosin Subfragments" by people in Profiles.
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Functional roles of ionic and hydrophobic surface loops in smooth muscle myosin: their interactions with actin. Biochemistry. 2001 Jan 23; 40(3):657-64.
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Functional transitions in myosin: formation of a critical salt-bridge and transmission of effect to the sensitive tryptophan. Proc Natl Acad Sci U S A. 1998 Jun 09; 95(12):6653-8.
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Functional transitions in myosin: role of highly conserved Gly and Glu residues in the active site. Biochemistry. 1997 Apr 01; 36(13):3767-72.
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The putative actin-binding role of hydrophobic residues Trp546 and Phe547 in chicken gizzard heavy meromyosin. Proc Natl Acad Sci U S A. 1995 Dec 19; 92(26):11965-9.
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Functional chicken gizzard heavy meromyosin expression in and purification from baculovirus-infected insect cells. Proc Natl Acad Sci U S A. 1995 Jan 31; 92(3):704-8.
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Interaction between the heavy and the regulatory light chains in smooth muscle myosin subfragment 1. Biochemistry. 1992 Feb 04; 31(4):1201-10.
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Interaction between the heavy chain (HC) and the regulatory light chain (RLC) in smooth muscle myosin subfragment-1 (S-1). Jpn J Pharmacol. 1992; 58 Suppl 2:265P.
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Lys-65 and Glu-168 are the residues for carbodiimide-catalyzed cross-linking between the two heads of rigor smooth muscle heavy meromyosin. J Biol Chem. 1990 Nov 05; 265(31):19362-8.
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The rigor configuration of smooth muscle heavy meromyosin trapped by a zero-length cross-linker. Biochemistry. 1990 Mar 27; 29(12):3013-23.
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Carbodiimide-catalyzed cross-linking sites in the heads of gizzard heavy meromyosin attached to F-actin. Biochemistry. 1989 Feb 21; 28(4):1905-12.