Myosin-Light-Chain Kinase
"Myosin-Light-Chain Kinase" 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.
An enzyme that phosphorylates myosin light chains in the presence of ATP to yield myosin-light chain phosphate and ADP, and requires calcium and CALMODULIN. The 20-kDa light chain is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors. The enzyme plays a central role in the regulation of smooth muscle contraction.
| Descriptor ID |
D009219
|
| MeSH Number(s) |
D08.811.913.696.620.682.700.125.500 D12.644.360.100.500 D12.776.476.100.500
|
| Concept/Terms |
Myosin-Light-Chain Kinase- Myosin-Light-Chain Kinase
- Kinase, Myosin-Light-Chain
- Myosin Light Chain Kinase
- Myosin Regulatory Light-Chain Kinase
- Myosin Regulatory Light Chain Kinase
- Myosin Kinase
- Kinase, Myosin
- Myosin LCK
- LCK, Myosin
|
Below are MeSH descriptors whose meaning is more general than "Myosin-Light-Chain Kinase".
Below are MeSH descriptors whose meaning is more specific than "Myosin-Light-Chain Kinase".
This graph shows the total number of publications written about "Myosin-Light-Chain Kinase" by people in this website by year, and whether "Myosin-Light-Chain Kinase" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1995 | 0 | 1 | 1 |
| 1996 | 1 | 0 | 1 |
| 2011 | 1 | 1 | 2 |
| 2019 | 0 | 1 | 1 |
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Below are the most recent publications written about "Myosin-Light-Chain Kinase" by people in Profiles.
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Halder D, Saha S, Singh RK, Ghosh I, Mallick D, Dey SK, Ghosh A, Das BB, Ghosh S, Jana SS. Nonmuscle myosin IIA and IIB differentially modulate migration and alter gene expression in primary mouse tumorigenic cells. Mol Biol Cell. 2019 06 01; 30(12):1463-1476.
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Leitman EM, Tewari A, Horn M, Urbanski M, Damanakis E, Einheber S, Salzer JL, de Lanerolle P, Melendez-Vasquez CV. MLCK regulates Schwann cell cytoskeletal organization, differentiation and myelination. J Cell Sci. 2011 Nov 15; 124(Pt 22):3784-96.
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Butler SM, Abrassart JM, Hubbell MC, Adeoye O, Semotiuk A, Williams JM, Mata-Greenwood E, Khorram O, Pearce WJ. Contributions of VEGF to age-dependent transmural gradients in contractile protein expression in ovine carotid arteries. Am J Physiol Cell Physiol. 2011 Sep; 301(3):C653-66.
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Gao L, Grant AV, Rafaels N, Stockton-Porter M, Watkins T, Gao P, Chi P, Mu?oz M, Watson H, Dunston G, Togias A, Hansel N, Sevransky J, Maloney JP, Moss M, Shanholtz C, Brower R, Garcia JG, Grigoryev DN, Cheadle C, Beaty TH, Mathias RA, Barnes KC. Polymorphisms in the myosin light chain kinase gene that confer risk of severe sepsis are associated with a lower risk of asthma. J Allergy Clin Immunol. 2007 May; 119(5):1111-8.
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Levine RJ, Kensler RW, Yang Z, Stull JT, Sweeney HL. Myosin light chain phosphorylation affects the structure of rabbit skeletal muscle thick filaments. Biophys J. 1996 Aug; 71(2):898-907.
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Levine RJ, Kensler RW, Yang Z, Sweeney HL. Myosin regulatory light chain phosphorylation and the production of functionally significant changes in myosin head arrangement on striated muscle thick filaments. Biophys J. 1995 Apr; 68(4 Suppl):224S.
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Levine RJ, Chantler PD, Kensler RW, Woodhead JL. Effects of phosphorylation by myosin light chain kinase on the structure of Limulus thick filaments. J Cell Biol. 1991 May; 113(3):563-72.
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Jarrett HW, Madhavan R. Calmodulin-binding proteins also have a calmodulin-like binding site within their structure. The flip-flop model. J Biol Chem. 1991 Jan 05; 266(1):362-71.
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Persechini A, Blumenthal DK, Jarrett HW, Klee CB, Hardy DO, Kretsinger RH. The effects of deletions in the central helix of calmodulin on enzyme activation and peptide binding. J Biol Chem. 1989 May 15; 264(14):8052-8.