"S-Adenosylmethionine" 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.
Physiologic methyl radical donor involved in enzymatic transmethylation reactions and present in all living organisms. It possesses anti-inflammatory activity and has been used in treatment of chronic liver disease. (From Merck, 11th ed)
| Descriptor ID |
D012436
|
| MeSH Number(s) |
D02.886.030.676.180 D03.633.100.759.590.138.264 D12.125.166.676.180 D13.570.583.138.264 D13.570.800.096.264
|
| Concept/Terms |
S-Adenosylmethionine- S-Adenosylmethionine
- S Adenosylmethionine
- SAM-e
- AdoMet
- S-Adenosyl-L-Methionine
- S Adenosyl L Methionine
- Ademetionine
|
Below are MeSH descriptors whose meaning is more general than "S-Adenosylmethionine".
Below are MeSH descriptors whose meaning is more specific than "S-Adenosylmethionine".
This graph shows the total number of publications written about "S-Adenosylmethionine" by people in this website by year, and whether "S-Adenosylmethionine" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1995 | 0 | 1 | 1 |
| 2011 | 1 | 0 | 1 |
| 2014 | 0 | 1 | 1 |
| 2016 | 1 | 0 | 1 |
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Below are the most recent publications written about "S-Adenosylmethionine" by people in Profiles.
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Functional AdoMet Isosteres Resistant to Classical AdoMet Degradation Pathways. ACS Chem Biol. 2016 09 16; 11(9):2484-91.
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Characterization of the calicheamicin orsellinate C2-O-methyltransferase CalO6. Chembiochem. 2014 Jul 07; 15(10):1418-21.
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S-adenosyl-L-methionine inhibits collagen secretion in hepatic stellate cells via increased ubiquitination. Liver Int. 2011 Jul; 31(6):891-901.
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Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses. Plant Cell. 2006 Dec; 18(12):3656-69.
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Purification, crystallization, and preliminary X-ray diffraction analyses of the bacterial chemotaxis receptor modifying enzymes. Proteins. 1995 Apr; 21(4):345-50.