S-Adenosylmethionine
"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
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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
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Concept/Terms |
S-Adenosylmethionine- S-Adenosylmethionine
- S Adenosylmethionine
- SAM-e
- AdoMet
- S-Adenosyl-L-Methionine
- S Adenosyl L Methionine
- Ademetionine
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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 |
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1996 | 0 | 1 | 1 | 1997 | 1 | 0 | 1 | 2000 | 0 | 2 | 2 | 2002 | 0 | 3 | 3 | 2003 | 1 | 1 | 2 | 2004 | 2 | 1 | 3 | 2005 | 2 | 2 | 4 | 2006 | 4 | 3 | 7 | 2007 | 2 | 3 | 5 | 2008 | 1 | 2 | 3 | 2009 | 2 | 1 | 3 | 2010 | 0 | 1 | 1 | 2011 | 3 | 1 | 4 | 2014 | 1 | 1 | 2 | 2015 | 1 | 0 | 1 | 2016 | 0 | 1 | 1 | 2017 | 0 | 1 | 1 | 2020 | 0 | 1 | 1 |
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Below are the most recent publications written about "S-Adenosylmethionine" by people in Profiles.
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Ko?ich V, Stabler S. Lessons Learned from Inherited Metabolic Disorders of Sulfur-Containing Amino Acids Metabolism. J Nutr. 2020 10 01; 150(Suppl 1):2506S-2517S.
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Mirihana Arachchilage G, Sherlock ME, Weinberg Z, Breaker RR. SAM-VI RNAs selectively bind S-adenosylmethionine and exhibit similarities to SAM-III riboswitches. RNA Biol. 2018 03 04; 15(3):371-378.
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Gim?nez-Mascarell P, Majtan T, Oyenarte I, Ere?o-Orbea J, Majtan J, Klaudiny J, Kraus JP, Mart?nez-Cruz LA. Crystal structure of cystathionine ?-synthase from honeybee Apis mellifera. J Struct Biol. 2018 04; 202(1):82-93.
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Miao Z, Adamiak RW, Antczak M, Batey RT, Becka AJ, Biesiada M, Boniecki MJ, Bujnicki JM, Chen SJ, Cheng CY, Chou FC, Ferr?-D'Amar? AR, Das R, Dawson WK, Ding F, Dokholyan NV, Dunin-Horkawicz S, Geniesse C, Kappel K, Kladwang W, Krokhotin A, Lach GE, Major F, Mann TH, Magnus M, Pachulska-Wieczorek K, Patel DJ, Piccirilli JA, Popenda M, Purzycka KJ, Ren A, Rice GM, Santalucia J, Sarzynska J, Szachniuk M, Tandon A, Trausch JJ, Tian S, Wang J, Weeks KM, Williams B, Xiao Y, Xu X, Zhang D, Zok T, Westhof E. RNA-Puzzles Round III: 3D RNA structure prediction of five riboswitches and one ribozyme. RNA. 2017 05; 23(5):655-672.
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Pey AL, Mart?nez-Cruz LA, Kraus JP, Majtan T. Oligomeric status of human cystathionine beta-synthase modulates AdoMet binding. FEBS Lett. 2016 Dec; 590(24):4461-4471.
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Osna NA, Feng D, Ganesan M, Maillacheruvu PF, Orlicky DJ, French SW, Tuma DJ, Kharbanda KK. Prolonged feeding with guanidinoacetate, a methyl group consumer, exacerbates ethanol-induced liver injury. World J Gastroenterol. 2016 Oct 14; 22(38):8497-8508.
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Majtan T, Pey AL, Kraus JP. Kinetic stability of cystathionine beta-synthase can be modulated by structural analogs of S-adenosylmethionine: Potential approach to pharmacological chaperone therapy for homocystinuria. Biochimie. 2016 Jul; 126:6-13.
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Wostenberg C, Ceres P, Polaski JT, Batey RT. A Highly Coupled Network of Tertiary Interactions in the SAM-I Riboswitch and Their Role in Regulatory Tuning. J Mol Biol. 2015 Nov 06; 427(22):3473-3490.
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Bikkavilli RK, Avasarala S, Van Scoyk M, Karuppusamy Rathinam MK, Tauler J, Borowicz S, Winn RA. In vitro methylation assay to study protein arginine methylation. J Vis Exp. 2014 Oct 05; (92):e51997.
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Ere?o-Orbea J, Majtan T, Oyenarte I, Kraus JP, Mart?nez-Cruz LA. Structural insight into the molecular mechanism of allosteric activation of human cystathionine ?-synthase by S-adenosylmethionine. Proc Natl Acad Sci U S A. 2014 Sep 16; 111(37):E3845-52.
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