"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.
To see the data from this visualization as text,
click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1996 | 0 | 1 | 1 |
| 2002 | 1 | 0 | 1 |
| 2004 | 1 | 0 | 1 |
| 2006 | 0 | 2 | 2 |
| 2009 | 1 | 1 | 2 |
| 2010 | 0 | 2 | 2 |
| 2011 | 0 | 1 | 1 |
| 2013 | 1 | 1 | 2 |
| 2014 | 1 | 1 | 2 |
| 2015 | 0 | 2 | 2 |
| 2016 | 1 | 1 | 2 |
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click here.
Below are the most recent publications written about "S-Adenosylmethionine" by people in Profiles.
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Christian T, Sakaguchi R, Perlinska AP, Lahoud G, Ito T, Taylor EA, Yokoyama S, Sulkowska JI, Hou YM. Methyl transfer by substrate signaling from a knotted protein fold. Nat Struct Mol Biol. 2016 Oct; 23(10):941-948.
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Hou YM. Single-Turnover Kinetics of Methyl Transfer to tRNA by Methyltransferases. Methods Mol Biol. 2016; 1421:79-96.
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Ito T, Masuda I, Yoshida K, Goto-Ito S, Sekine S, Suh SW, Hou YM, Yokoyama S. Structural basis for methyl-donor-dependent and sequence-specific binding to tRNA substrates by knotted methyltransferase TrmD. Proc Natl Acad Sci U S A. 2015 Aug 04; 112(31):E4197-205.
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Hou YM, Masuda I. Kinetic Analysis of tRNA Methyltransferases. Methods Enzymol. 2015; 560:91-116.
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Sakaguchi R, Lahoud G, Christian T, Gamper H, Hou YM. A divalent metal ion-dependent N(1)-methyl transfer to G37-tRNA. Chem Biol. 2014 Oct 23; 21(10):1351-1360.
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Drake KM, Watson VG, Kisielewski A, Glynn R, Napper AD. A sensitive luminescent assay for the histone methyltransferase NSD1 and other SAM-dependent enzymes. Assay Drug Dev Technol. 2014 Jun; 12(5):258-71.
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Christian T, Gamper H, Hou YM. Conservation of structure and mechanism by Trm5 enzymes. RNA. 2013 Sep; 19(9):1192-9.
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Gana R, Rao S, Huang H, Wu C, Vasudevan S. Structural and functional studies of S-adenosyl-L-methionine binding proteins: a ligand-centric approach. BMC Struct Biol. 2013 Apr 25; 13:6.
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Lahoud G, Goto-Ito S, Yoshida K, Ito T, Yokoyama S, Hou YM. Differentiating analogous tRNA methyltransferases by fragments of the methyl donor. RNA. 2011 Jul; 17(7):1236-46.
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Christian T, Lahoud G, Liu C, Hoffmann K, Perona JJ, Hou YM. Mechanism of N-methylation by the tRNA m1G37 methyltransferase Trm5. RNA. 2010 Dec; 16(12):2484-92.