PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
2552290-0	1989	Elements involved in S-adenosylmethionine-mediated regulation of the Saccharomyces cerevisiae MET25 gene.	S-Adenosylmethionine	21-41	bifunctional cysteine synthase/O-acetylhomoserine aminocarboxypropyltransferase MET17	Saccharomyces cerevisiae S288C	94-99
2777770-1	1989	Protein L-isoaspartyl methyltransferase (PIMT) transfers the methyl group of S-adenosyl-L-methionine to free alpha-carboxyl groups of atypical L-isoaspartyl residues in proteins.	S-Adenosylmethionine	77-100	protein-L-isoaspartate (D-aspartate) O-methyltransferase	Bos taurus	0-39
2777770-1	1989	Protein L-isoaspartyl methyltransferase (PIMT) transfers the methyl group of S-adenosyl-L-methionine to free alpha-carboxyl groups of atypical L-isoaspartyl residues in proteins.	S-Adenosylmethionine	77-100	protein-L-isoaspartate (D-aspartate) O-methyltransferase	Bos taurus	41-45
2552290-4	1989	The results revealed a regulatory region, acting as an upstream activation site, that activated transcription of MET25 in the absence of methionine or AdoMet.	S-Adenosylmethionine	151-157	bifunctional cysteine synthase/O-acetylhomoserine aminocarboxypropyltransferase MET17	Saccharomyces cerevisiae S288C	113-118
2684666-10	1989	This activity could be distinguished from those remaining in the pem1 disruptant by its different pH optimum and apparent Km for S-adenosyl-L-methionine.	S-Adenosylmethionine	129-152	phosphatidylethanolamine N-methyltransferase	Saccharomyces cerevisiae S288C	65-69
2498524-2	1989	It is reasoned that perturbation of a second regulatory element in polyamine biosynthesis, i.e., the generation of propylamine groups from S-adenosylmethionine (AdoMet), would potentiate the effectiveness of DFMO.	S-Adenosylmethionine	139-159	methionine adenosyltransferase 1A	Rattus norvegicus	161-167
2792190-2	1989	The treatment of aged rabbits for 30 days with S-adenosyl-L-methionine (SAM) restored the number of PRL binding sites to levels found in the hypothalamus and substantia nigra from young animals.	S-Adenosylmethionine	47-70	prolactin	Oryctolagus cuniculus	100-103
2451507-1	1988	The enzyme S-adenosylmethionine (AdoMet): myelin basic protein (MBP) methyltransferase was purified 250-fold from bovine brain with an overall yield of 130%, relative to crude supernatant.	S-Adenosylmethionine	11-31	myelin basic protein	Bos taurus	42-62
2630176-6	1989	Results from kinetic studies indicate that the above compounds are inhibitors that compete for both the histamine and the S-adenosylmethionine (SAM) binding sites of HNMT.	S-Adenosylmethionine	122-142	histamine N-methyltransferase	Oryctolagus cuniculus	166-170
2630176-6	1989	Results from kinetic studies indicate that the above compounds are inhibitors that compete for both the histamine and the S-adenosylmethionine (SAM) binding sites of HNMT.	S-Adenosylmethionine	144-147	histamine N-methyltransferase	Oryctolagus cuniculus	166-170
3223955-3	1988	The only known mammalian pathway for the synthesis de novo of choline molecules is catalysed by phosphatidylethanolamine N-methyltransferase (PeMT), which synthesizes phosphatidylcholine (PtdCho) via sequential methylation of phosphatidylethanolamine (PtdEtn) using S-adenosylmethionine (AdoMet) as a methyl donor.	S-Adenosylmethionine	266-286	phosphatidylethanolamine N-methyltransferase	Homo sapiens	96-140
3223955-3	1988	The only known mammalian pathway for the synthesis de novo of choline molecules is catalysed by phosphatidylethanolamine N-methyltransferase (PeMT), which synthesizes phosphatidylcholine (PtdCho) via sequential methylation of phosphatidylethanolamine (PtdEtn) using S-adenosylmethionine (AdoMet) as a methyl donor.	S-Adenosylmethionine	266-286	phosphatidylethanolamine N-methyltransferase	Homo sapiens	142-146
3223955-3	1988	The only known mammalian pathway for the synthesis de novo of choline molecules is catalysed by phosphatidylethanolamine N-methyltransferase (PeMT), which synthesizes phosphatidylcholine (PtdCho) via sequential methylation of phosphatidylethanolamine (PtdEtn) using S-adenosylmethionine (AdoMet) as a methyl donor.	S-Adenosylmethionine	288-294	phosphatidylethanolamine N-methyltransferase	Homo sapiens	96-140
3223955-3	1988	The only known mammalian pathway for the synthesis de novo of choline molecules is catalysed by phosphatidylethanolamine N-methyltransferase (PeMT), which synthesizes phosphatidylcholine (PtdCho) via sequential methylation of phosphatidylethanolamine (PtdEtn) using S-adenosylmethionine (AdoMet) as a methyl donor.	S-Adenosylmethionine	288-294	phosphatidylethanolamine N-methyltransferase	Homo sapiens	142-146
3417662-2	1988	Rat liver glycine methyltransferase, a homotetramer, exhibits sigmoidal rate behavior with respect to S-adenosylmethionine (Ogawa, H., and Fujioka, M. (1982) J. Biol.	S-Adenosylmethionine	102-122	glycine N-methyltransferase	Rattus norvegicus	10-35
3417662-6	1988	Limited proteolysis of glycine methyltransferase with trypsin in the presence of S-adenosylmethionine yields an enzyme lacking the NH2-terminal 8 residues.	S-Adenosylmethionine	81-101	glycine N-methyltransferase	Rattus norvegicus	23-48
3042777-10	1988	Both this toxin-resistant EF-2 and its modifying enzyme have been partially purified and evidence is presented that the modifying enzyme is a specific S-adenosylmethionine:EF-2 methyltransferase.	S-Adenosylmethionine	151-171	elongation factor 2	Saccharomyces cerevisiae S288C	26-30
3042777-10	1988	Both this toxin-resistant EF-2 and its modifying enzyme have been partially purified and evidence is presented that the modifying enzyme is a specific S-adenosylmethionine:EF-2 methyltransferase.	S-Adenosylmethionine	151-171	elongation factor 2	Saccharomyces cerevisiae S288C	172-176
3042777-13	1988	We conclude that the S-adenosylmethionine:EF-2 methyltransferase adds at least the last two of the three methyl groups present in diphthine and that this modification is sufficient to create diphtheria toxin sensitivity.	S-Adenosylmethionine	23-41	elongation factor 2	Saccharomyces cerevisiae S288C	42-46
3359424-4	1988	In LC3 cells, periodate-oxidized adenosine, 3-deaza-adenosine and 3-deaza-(+/-)aristeromycin reduced the intracellular ratio of S-adenosylmethionine/S-adenosylhomocysteine approximately 20-, 6- and 16-fold, respectively.	S-Adenosylmethionine	128-148	microtubule associated protein 1 light chain 3 alpha	Homo sapiens	3-6
2722775-9	1989	The Km for S-adenosylmethionine (AdoMet) was 5-9 microM with PME and 4 microM with PDE as substrates.	S-Adenosylmethionine	11-31	cystatin B	Homo sapiens	61-64
2722775-9	1989	The Km for S-adenosylmethionine (AdoMet) was 5-9 microM with PME and 4 microM with PDE as substrates.	S-Adenosylmethionine	11-31	aldehyde dehydrogenase 7 family member A1	Homo sapiens	83-86
2722775-9	1989	The Km for S-adenosylmethionine (AdoMet) was 5-9 microM with PME and 4 microM with PDE as substrates.	S-Adenosylmethionine	33-39	cystatin B	Homo sapiens	61-64
2722775-9	1989	The Km for S-adenosylmethionine (AdoMet) was 5-9 microM with PME and 4 microM with PDE as substrates.	S-Adenosylmethionine	33-39	aldehyde dehydrogenase 7 family member A1	Homo sapiens	83-86
2565101-11	1989	Since the elimination reactions take place under mild conditions, they may occur in vivo following oxidation at the alpha-C of L-canavanine (ingested or formed endogenously) or of other amino acids with a good leaving group in the gamma-position (e.g., S-adenosylmethionine, methionine sulfoximine, homocyst(e)ine, or cysteine-homocysteine mixed disulfide) by an L-amino acid oxidase, a transaminase, or a dehydrogenase.	S-Adenosylmethionine	253-273	interleukin 4 induced 1	Homo sapiens	363-383
2703919-3	1989	Accordingly, the enzyme glycine N-methyltransferase (GNMT, EC 2.1.1.20) may play a major role in maintaining the levels of S-adenosylmethionine in liver in response to changes in dietary methionine.	S-Adenosylmethionine	123-143	glycine N-methyltransferase	Rattus norvegicus	24-51
2703919-3	1989	Accordingly, the enzyme glycine N-methyltransferase (GNMT, EC 2.1.1.20) may play a major role in maintaining the levels of S-adenosylmethionine in liver in response to changes in dietary methionine.	S-Adenosylmethionine	123-143	glycine N-methyltransferase	Rattus norvegicus	53-57
2736320-4	1989	Human erythrocyte soluble form of COMT had Km values of 6.1 microM and 26.0 microM for S-adenosyl-L-methionine and dihydroxybenzoic acid, respectively.	S-Adenosylmethionine	87-110	catechol-O-methyltransferase	Homo sapiens	34-38
3076439-1	1988	S-Adenosylmethionine (SAM)-dependent activations of pyruvate formate-lyase, lysine 2,3-aminomutase and cobalamin-dependent methionine synthase are discussed.	S-Adenosylmethionine	0-20	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	103-142
3076439-1	1988	S-Adenosylmethionine (SAM)-dependent activations of pyruvate formate-lyase, lysine 2,3-aminomutase and cobalamin-dependent methionine synthase are discussed.	S-Adenosylmethionine	22-25	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	103-142
2451507-1	1988	The enzyme S-adenosylmethionine (AdoMet): myelin basic protein (MBP) methyltransferase was purified 250-fold from bovine brain with an overall yield of 130%, relative to crude supernatant.	S-Adenosylmethionine	11-31	myelin basic protein	Bos taurus	64-67
2451507-1	1988	The enzyme S-adenosylmethionine (AdoMet): myelin basic protein (MBP) methyltransferase was purified 250-fold from bovine brain with an overall yield of 130%, relative to crude supernatant.	S-Adenosylmethionine	33-39	myelin basic protein	Bos taurus	42-62
2451507-1	1988	The enzyme S-adenosylmethionine (AdoMet): myelin basic protein (MBP) methyltransferase was purified 250-fold from bovine brain with an overall yield of 130%, relative to crude supernatant.	S-Adenosylmethionine	33-39	myelin basic protein	Bos taurus	64-67
3337727-0	1988	S-adenosyl-L-methionine protects the hippocampal CA1 neurons from the ischemic neuronal death in rat.	S-Adenosylmethionine	0-23	carbonic anhydrase 1	Rattus norvegicus	49-52
3338105-2	1988	Intraperitoneal injection of ethionine to male rats for up to 12 days caused a pronounced fall in S-adenosylmethionine (AdoMet) in liver, but did not or only slightly affect AdoMet in kidney and spleen.	S-Adenosylmethionine	98-118	methionine adenosyltransferase 1A	Rattus norvegicus	120-126
3580137-1	1987	The effect of disulfiram and S-adenosyl-L-methionine (SAM) administration to acute ethanol intoxicated mice on the hepatic glutathione (GSH) concentration and aminolevulinic and dehydratase (ALA-D) activity was investigated.	S-Adenosylmethionine	29-52	aminolevulinate, delta-, dehydratase	Mus musculus	159-189
3380525-1	1988	Two chemoattractants for retinal pigment epithelial (RPE) cells, fibronectin (FN) and platelet-derived growth factor (PDGF) were found to enhance protein carboxymethylation mediated by S-adenosyl-L-methionine in RPE cells measured by [3H]methanol hydrolyzed from TCA precipitable protein methyl esters labelled with [3H]methionine.	S-Adenosylmethionine	185-208	fibronectin 1	Homo sapiens	65-76
3380525-1	1988	Two chemoattractants for retinal pigment epithelial (RPE) cells, fibronectin (FN) and platelet-derived growth factor (PDGF) were found to enhance protein carboxymethylation mediated by S-adenosyl-L-methionine in RPE cells measured by [3H]methanol hydrolyzed from TCA precipitable protein methyl esters labelled with [3H]methionine.	S-Adenosylmethionine	185-208	fibronectin 1	Homo sapiens	78-80
3680298-1	1987	Phosphatidylethanolamine (PE) N-methyltransferase catalyzes the synthesis of phosphatidylcholine by the stepwise transfer of methyl groups from S-adenosylmethionine to the amino head group of PE.	S-Adenosylmethionine	144-164	phosphatidylethanolamine N-methyltransferase	Rattus norvegicus	0-49
3433277-0	1987	Inhibitory effect of FO-1561 (S-adenosyl-L-methionine sulfate tosylate) on phospholipase A2.	S-Adenosylmethionine	21-28	phospholipase A2 group IB	Rattus norvegicus	75-91
3433277-3	1987	FO-1561 inhibited mitochondrial swelling induced by Ca2+ added exogenously or by addition of snake venom phospholipase A2.	S-Adenosylmethionine	0-7	phospholipase A2 group IB	Rattus norvegicus	105-121
3322100-3	1987	PPA is converted to N[methyl-3H]ephedrine ([3H]EPD) by the enzyme phenylethanolamine N-methyltransferase (PNMT) and S-[methyl-3H]adenosyl-L-methionine ([3H]AdoMet).	S-Adenosylmethionine	156-162	phenylethanolamine N-methyltransferase	Homo sapiens	66-104
3322100-3	1987	PPA is converted to N[methyl-3H]ephedrine ([3H]EPD) by the enzyme phenylethanolamine N-methyltransferase (PNMT) and S-[methyl-3H]adenosyl-L-methionine ([3H]AdoMet).	S-Adenosylmethionine	156-162	phenylethanolamine N-methyltransferase	Homo sapiens	106-110
3442671-8	1987	The arginine-modified glycine methyltransferase appears to bind S-adenosylmethionine as the native enzyme does, as seen from quenching of the protein fluorescence by S-adenosylmethionine.	S-Adenosylmethionine	64-84	glycine N-methyltransferase	Rattus norvegicus	22-47
3442671-8	1987	The arginine-modified glycine methyltransferase appears to bind S-adenosylmethionine as the native enzyme does, as seen from quenching of the protein fluorescence by S-adenosylmethionine.	S-Adenosylmethionine	166-186	glycine N-methyltransferase	Rattus norvegicus	22-47
3426538-1	1987	Treatment of cultured L1210 cells with 1 mM-L-2-amino-4-methoxy-cis-but-3-enoic acid (L-cisAMB), a methionine-analogue inhibitor of S-adenosylmethionine (AdoMet) synthetase (EC 2.5.1.6), produced a rapid and near-total depletion of AdoMet by 4 h. After this, the pools recovered to 60% of control by 48 h, apparently because of an increase in AdoMet synthetase activity.	S-Adenosylmethionine	154-160	methionine adenosyltransferase I, alpha	Mus musculus	132-152
2884049-1	1987	Liver ornithine decarboxylase (ODC) activity and content of S-adenosyl-L-methionine (SAM) and its catabolite 5"-methylthioadenosine (5"-MTA) were determined in the late stages of hepatocarcinogenesis.	S-Adenosylmethionine	85-88	ornithine decarboxylase 1	Rattus norvegicus	31-34
3580137-1	1987	The effect of disulfiram and S-adenosyl-L-methionine (SAM) administration to acute ethanol intoxicated mice on the hepatic glutathione (GSH) concentration and aminolevulinic and dehydratase (ALA-D) activity was investigated.	S-Adenosylmethionine	29-52	aminolevulinate, delta-, dehydratase	Mus musculus	191-196
2434089-1	1987	In the presence of excess S-adenosylmethionine (AdoMet), the extent of methylation of myelin basic protein (MBP) by partially purified AdoMet:MBP methyltransferase is a non-linear function of time, reaching a limiting value as available MBP is depleted and then decreasing monotonically.	S-Adenosylmethionine	26-46	myelin basic protein	Bos taurus	108-111
3818603-0	1987	Allosteric inhibition of methylenetetrahydrofolate reductase by adenosylmethionine.	S-Adenosylmethionine	64-82	methylenetetrahydrofolate reductase	Homo sapiens	25-60
3493704-2	1987	The effect of peptides on ODC and S-adenosylmethionine (SAMDC) activities (key enzymes in polyamine biosynthesis) in isolated enterocytes is unknown.	S-Adenosylmethionine	34-54	adenosylmethionine decarboxylase 1	Rattus norvegicus	56-61
2434089-1	1987	In the presence of excess S-adenosylmethionine (AdoMet), the extent of methylation of myelin basic protein (MBP) by partially purified AdoMet:MBP methyltransferase is a non-linear function of time, reaching a limiting value as available MBP is depleted and then decreasing monotonically.	S-Adenosylmethionine	26-46	myelin basic protein	Bos taurus	86-106
2434089-1	1987	In the presence of excess S-adenosylmethionine (AdoMet), the extent of methylation of myelin basic protein (MBP) by partially purified AdoMet:MBP methyltransferase is a non-linear function of time, reaching a limiting value as available MBP is depleted and then decreasing monotonically.	S-Adenosylmethionine	26-46	myelin basic protein	Bos taurus	142-145
2434089-1	1987	In the presence of excess S-adenosylmethionine (AdoMet), the extent of methylation of myelin basic protein (MBP) by partially purified AdoMet:MBP methyltransferase is a non-linear function of time, reaching a limiting value as available MBP is depleted and then decreasing monotonically.	S-Adenosylmethionine	26-46	myelin basic protein	Bos taurus	142-145
2434089-1	1987	In the presence of excess S-adenosylmethionine (AdoMet), the extent of methylation of myelin basic protein (MBP) by partially purified AdoMet:MBP methyltransferase is a non-linear function of time, reaching a limiting value as available MBP is depleted and then decreasing monotonically.	S-Adenosylmethionine	48-54	myelin basic protein	Bos taurus	86-106
2434089-1	1987	In the presence of excess S-adenosylmethionine (AdoMet), the extent of methylation of myelin basic protein (MBP) by partially purified AdoMet:MBP methyltransferase is a non-linear function of time, reaching a limiting value as available MBP is depleted and then decreasing monotonically.	S-Adenosylmethionine	48-54	myelin basic protein	Bos taurus	108-111
2434089-1	1987	In the presence of excess S-adenosylmethionine (AdoMet), the extent of methylation of myelin basic protein (MBP) by partially purified AdoMet:MBP methyltransferase is a non-linear function of time, reaching a limiting value as available MBP is depleted and then decreasing monotonically.	S-Adenosylmethionine	48-54	myelin basic protein	Bos taurus	142-145
2434089-1	1987	In the presence of excess S-adenosylmethionine (AdoMet), the extent of methylation of myelin basic protein (MBP) by partially purified AdoMet:MBP methyltransferase is a non-linear function of time, reaching a limiting value as available MBP is depleted and then decreasing monotonically.	S-Adenosylmethionine	48-54	myelin basic protein	Bos taurus	142-145
3025802-1	1986	Human lymphocyte and granulocyte membranes contain an enzyme, phosphatidylethanolamine N-methyltransferase (PEMT), which catalyzes the transfer of a methyl group from S-adenosylmethionine to the polar head group of phosphatidylethanolamine to form phosphatidylmonomethylethanolamine.	S-Adenosylmethionine	167-187	phosphatidylethanolamine N-methyltransferase	Homo sapiens	62-106
3625461-2	1987	Copper inhibition of HIOMT can be classified as partial, classic noncompetitive inhibition with respect to S-adenosyl methionine and as partial, mixed noncompetitive inhibition with respect to N-acetylserotonin.	S-Adenosylmethionine	107-128	acetylserotonin O-methyltransferase	Bos taurus	21-26
2445177-12	1987	Our studies demonstrate that CH3-H4PteGlu6, and suggest that incorporation of plasma CH3-H4PteGlu1 will only occur when methylenetetrahydrofolate reductase is inhibited by adenosylmethionine and cellular pools of CH3-H4PteGlu6 are at very low levels.	S-Adenosylmethionine	172-190	methylenetetrahydrofolate reductase	Sus scrofa	120-155
3025802-1	1986	Human lymphocyte and granulocyte membranes contain an enzyme, phosphatidylethanolamine N-methyltransferase (PEMT), which catalyzes the transfer of a methyl group from S-adenosylmethionine to the polar head group of phosphatidylethanolamine to form phosphatidylmonomethylethanolamine.	S-Adenosylmethionine	167-187	phosphatidylethanolamine N-methyltransferase	Homo sapiens	108-112
3025802-3	1986	Granulocyte membrane PEMT has Km for S-adenosylmethionine of 4.4 microM and specific activity 0.54 +/- 0.51 pmol/mg protein/15 min, is inhibited by S-adenosylhomocysteine, displays optimal activity at pH 8.0-9.5, and is stimulated by isoproterenol greater than epinephrine greater than norepinephrine, but not by prostaglandin E1, serum-treated zymosan, formyl-methionyl-leucyl-phenylalanine, or adenosine 3":5" cyclic monophosphate.	S-Adenosylmethionine	37-57	phosphatidylethanolamine N-methyltransferase	Homo sapiens	21-25
3530324-1	1986	The chirality of biologically active S-adenosyl-L-methionine (AdoMet) is S,S, where the designations refer to the sulfur and the alpha-carbon, respectively.	S-Adenosylmethionine	62-68	methionine adenosyltransferase I, alpha	Mus musculus	37-60
3091083-2	1986	The first step in diphthamide biosynthesis may involve the transfer of aminocarboxypropyl moiety from S-adenosylmethionine to the imidazole ring of histidine in EF-2, to yield 2-(3-carboxy-3-aminopropyl)histidine and 5"-deoxy-5"-methylthioadenosine (MeSAdo).	S-Adenosylmethionine	102-122	eukaryotic translation elongation factor 2	Mus musculus	161-165
3738936-1	1986	S-Adenosyl-L-methionine (Ado-met) administration to rats significantly improved liver necrosis induced by thioacetamide (TAA) as evidenced by reduction of TAA-elevated catalytic activity of serum aspartate aminotransferase (AST) and alanine aminotransferase (ALAT).	S-Adenosylmethionine	0-23	glutamic-oxaloacetic transaminase 2	Rattus norvegicus	196-222
3091070-7	1986	These results and those from experiments in which these spermine synthesis inhibitors were combined with inhibitors of spermidine synthase and ornithine decarboxylase indicated that the cells compensated for the inhibition of the aminopropyltransferases by increasing the production of decarboxylated S-adenosylmethionine and putrescine.	S-Adenosylmethionine	301-321	ornithine decarboxylase, structural 1	Mus musculus	143-166
3738936-1	1986	S-Adenosyl-L-methionine (Ado-met) administration to rats significantly improved liver necrosis induced by thioacetamide (TAA) as evidenced by reduction of TAA-elevated catalytic activity of serum aspartate aminotransferase (AST) and alanine aminotransferase (ALAT).	S-Adenosylmethionine	0-23	glutamic-oxaloacetic transaminase 2	Rattus norvegicus	224-227
3738936-1	1986	S-Adenosyl-L-methionine (Ado-met) administration to rats significantly improved liver necrosis induced by thioacetamide (TAA) as evidenced by reduction of TAA-elevated catalytic activity of serum aspartate aminotransferase (AST) and alanine aminotransferase (ALAT).	S-Adenosylmethionine	25-32	glutamic-oxaloacetic transaminase 2	Rattus norvegicus	196-222
3738936-1	1986	S-Adenosyl-L-methionine (Ado-met) administration to rats significantly improved liver necrosis induced by thioacetamide (TAA) as evidenced by reduction of TAA-elevated catalytic activity of serum aspartate aminotransferase (AST) and alanine aminotransferase (ALAT).	S-Adenosylmethionine	25-32	glutamic-oxaloacetic transaminase 2	Rattus norvegicus	224-227
3006760-3	1986	The acetylation of decarboxylated S-adenosylmethionine occurred in vivo in SV-3T3 cells exposed to the ornithine decarboxylase inhibitor 2-(difluoromethyl)ornithine.	S-Adenosylmethionine	34-54	ornithine decarboxylase, structural 1	Mus musculus	103-126
3754872-1	1986	Methylenetetrahydrofolate reductase commits tetrahydrofolate-bound one carbon units to use in the regeneration of the methyl group of adenosylmethionine (AdoMet) in eucaryotes and its activity is allosterically inhibited by AdoMet.	S-Adenosylmethionine	134-152	methylenetetrahydrofolate reductase	Homo sapiens	0-35
3754872-1	1986	Methylenetetrahydrofolate reductase commits tetrahydrofolate-bound one carbon units to use in the regeneration of the methyl group of adenosylmethionine (AdoMet) in eucaryotes and its activity is allosterically inhibited by AdoMet.	S-Adenosylmethionine	154-160	methylenetetrahydrofolate reductase	Homo sapiens	0-35
3720835-1	1986	The effect of l-isoproterenol on S-adenosyl-L-methionine (Adomet)-mediated phospholipid methylation in rat brain cortex was examined.	S-Adenosylmethionine	58-64	methionine adenosyltransferase 1A	Rattus norvegicus	33-56
3754465-1	1986	In order to investigate the pH dependence of catechol O-methyltransferase (S-adenosyl-L-methionine:catechol O-methyltransferase, EC 2.1.1.6), kinetic parameters have been determined for the highly purified enzyme from pig liver over the pH range 6.75-8.20 using the substrates S-adenosylmethionine (AdoMet) and 3,4-dihydroxyphenylacetic acid (DOPAC).	S-Adenosylmethionine	277-297	catechol-O-methyltransferase	Sus scrofa	45-73
3754465-1	1986	In order to investigate the pH dependence of catechol O-methyltransferase (S-adenosyl-L-methionine:catechol O-methyltransferase, EC 2.1.1.6), kinetic parameters have been determined for the highly purified enzyme from pig liver over the pH range 6.75-8.20 using the substrates S-adenosylmethionine (AdoMet) and 3,4-dihydroxyphenylacetic acid (DOPAC).	S-Adenosylmethionine	277-297	catechol-O-methyltransferase	Sus scrofa	99-127
3754465-1	1986	In order to investigate the pH dependence of catechol O-methyltransferase (S-adenosyl-L-methionine:catechol O-methyltransferase, EC 2.1.1.6), kinetic parameters have been determined for the highly purified enzyme from pig liver over the pH range 6.75-8.20 using the substrates S-adenosylmethionine (AdoMet) and 3,4-dihydroxyphenylacetic acid (DOPAC).	S-Adenosylmethionine	299-305	catechol-O-methyltransferase	Sus scrofa	45-73
3754465-1	1986	In order to investigate the pH dependence of catechol O-methyltransferase (S-adenosyl-L-methionine:catechol O-methyltransferase, EC 2.1.1.6), kinetic parameters have been determined for the highly purified enzyme from pig liver over the pH range 6.75-8.20 using the substrates S-adenosylmethionine (AdoMet) and 3,4-dihydroxyphenylacetic acid (DOPAC).	S-Adenosylmethionine	299-305	catechol-O-methyltransferase	Sus scrofa	99-127
3081646-0	1986	Selective augmentation by recombinant interferon-gamma of the intracellular content of S-adenosylmethionine in murine macrophages.	S-Adenosylmethionine	87-107	interferon gamma	Mus musculus	38-54
3081646-1	1986	Treatment of mouse peritoneal macrophages with IFN-gamma augmented the intracellular content of S-adenosylmethionine, as measured by quantitative high-performance liquid chromatography.	S-Adenosylmethionine	96-116	interferon gamma	Mus musculus	47-56
3081646-5	1986	The increased content of S-adenosylmethionine was associated with the acquisition of tumoricidal activity by macrophages upon IFN-gamma treatment.	S-Adenosylmethionine	25-45	interferon gamma	Mus musculus	126-135
3081646-6	1986	LPS also augmented the cellular content of S-adenosylmethionine and activated macrophages to become cytotoxic, suggesting a common mechanism of action for IFN-gamma and LPS in macrophage activation.	S-Adenosylmethionine	43-63	toll-like receptor 4	Mus musculus	0-3
3081646-6	1986	LPS also augmented the cellular content of S-adenosylmethionine and activated macrophages to become cytotoxic, suggesting a common mechanism of action for IFN-gamma and LPS in macrophage activation.	S-Adenosylmethionine	43-63	interferon gamma	Mus musculus	155-164
3081646-6	1986	LPS also augmented the cellular content of S-adenosylmethionine and activated macrophages to become cytotoxic, suggesting a common mechanism of action for IFN-gamma and LPS in macrophage activation.	S-Adenosylmethionine	43-63	toll-like receptor 4	Mus musculus	169-172
3006760-6	1986	Furthermore, the inhibition of histone acetylation by decarboxylated S-adenosylmethionine could contribute to the biological effects brought about by inhibitors of ornithine decarboxylase.	S-Adenosylmethionine	69-89	ornithine decarboxylase 1	Homo sapiens	164-187
3753600-11	1986	Based on the above results, a catechol-binding site model for catechol O-methyltransferase is proposed in which the two phenolic hydroxyl groups of catechol substrates are postulated to be approximately equally spaced from the methyl group of the cosubstrate S-adenosylmethionine.	S-Adenosylmethionine	259-279	catechol-O-methyltransferase	Homo sapiens	62-90
2998482-0	1985	Modulation by the ratio S-adenosylmethionine/S-adenosylhomocysteine of cyclic AMP-dependent phosphorylation of the 50 kDa protein of rat liver phospholipid methyltransferase.	S-Adenosylmethionine	24-44	phosphatidylethanolamine N-methyltransferase	Rattus norvegicus	143-173
3455877-1	1986	Methylglyoxal bis(butylamidinohydrazone) (MGBB) inhibited S-adenosylmethionine decarboxylase (SAMDC) activity competitively with S-adenosylmethionine (SAM) showing the Ki value of 1.8 X 10(-5) M. MGBB showed less SAMDC-stabilizing effect in rat liver in vivo than did methylglyoxal bis-(guanylhydrazone) (MGBG).	S-Adenosylmethionine	58-78	adenosylmethionine decarboxylase 1	Homo sapiens	94-99
3455877-1	1986	Methylglyoxal bis(butylamidinohydrazone) (MGBB) inhibited S-adenosylmethionine decarboxylase (SAMDC) activity competitively with S-adenosylmethionine (SAM) showing the Ki value of 1.8 X 10(-5) M. MGBB showed less SAMDC-stabilizing effect in rat liver in vivo than did methylglyoxal bis-(guanylhydrazone) (MGBG).	S-Adenosylmethionine	58-78	adenosylmethionine decarboxylase 1	Rattus norvegicus	213-218
4091805-1	1985	The activity of phosphatidylethanolamine N-methyltransferase (PeMT), an enzymic system that catalyses the synthesis of phosphatidylcholine (PtdCho) via sequential methylation of phosphatidylethanolamine (PtdEtn) using S-adenosylmethionine (AdoMet) as a methyl donor, was examined in brain homogenates from rats of various ages.	S-Adenosylmethionine	218-238	phosphatidylethanolamine N-methyltransferase	Homo sapiens	16-60
2866045-6	1985	An increase in ornithine decarboxylase activity, associated with a decrease in the liver S-adenosyl-L-methionine pool, also occurred in normal animals on the first day following a partial hepatectomy and was enhanced by phenobarbital.	S-Adenosylmethionine	91-112	ornithine decarboxylase 1	Rattus norvegicus	15-38
4091805-1	1985	The activity of phosphatidylethanolamine N-methyltransferase (PeMT), an enzymic system that catalyses the synthesis of phosphatidylcholine (PtdCho) via sequential methylation of phosphatidylethanolamine (PtdEtn) using S-adenosylmethionine (AdoMet) as a methyl donor, was examined in brain homogenates from rats of various ages.	S-Adenosylmethionine	240-246	phosphatidylethanolamine N-methyltransferase	Homo sapiens	16-60
2985192-1	1985	This report examines the possibility that glucocorticoids control the degradation of adrenal phenylethanolamine N-methyltransferase and pineal hydroxyindole O-methyltransferase by regulating endogenous concentrations of the cosubstrate, S-adenosylmethionine, via its metabolic enzymes, methionine adenosyltransferase and S-adenosylhomocysteine hydrolase.	S-Adenosylmethionine	237-257	acetylserotonin O-methyltransferase	Homo sapiens	143-176
3890958-0	1985	Unmasking of insulin receptors in rat submaxillary gland microsomes: effect of high ionic strength, phospholipase C and S-adenosyl-L-methionine.	S-Adenosylmethionine	122-143	insulin	Homo sapiens	13-20
3890958-6	1985	Methylation of rat submaxillary gland microsomes by using S-adenosyl-L-methionine as the methyl donor significantly increased [125I]insulin binding.	S-Adenosylmethionine	58-81	insulin	Homo sapiens	132-139
3890958-7	1985	Scatchard analysis of the equilibrium binding data showed that addition of S-adenosyl-L-methionine (0.46 mM) to microsomes resulted in an enhancement of the total binding capacity (from 990 to 1520 fmol/mg protein) with no change in the affinity constants, which suggests the exposure of masked insulin receptors under such conditions.	S-Adenosylmethionine	75-98	insulin	Homo sapiens	295-302
3890958-8	1985	Both the methyl group incorporation into membrane phospholipids and the effect on insulin binding were dependent on the S-adenosyl-L-methionine concentration used and were partially suppressed in the presence of S-adenosyl-L-homocysteine, a specific competitive inhibitor of the methyltransferases activity.	S-Adenosylmethionine	120-143	insulin	Homo sapiens	82-89
3890958-10	1985	The effects of phospholipase C, S-adenosyl-L-methionine and high ionic strength on insulin binding were not additive, suggesting that these procedures unmask receptors from the same pool.	S-Adenosylmethionine	32-55	insulin	Homo sapiens	83-90
3860729-4	1985	Preceding the phenotypic changes was the preferential inhibition of RNA and DNA methylation in comparison to inhibition of their synthesis which coincided with the formation of a metabolite of NPC with the chromatographic characteristics of S-adenosyl-L-methionine (AdoMet).	S-Adenosylmethionine	241-264	NPC intracellular cholesterol transporter 1	Homo sapiens	193-196
3860729-4	1985	Preceding the phenotypic changes was the preferential inhibition of RNA and DNA methylation in comparison to inhibition of their synthesis which coincided with the formation of a metabolite of NPC with the chromatographic characteristics of S-adenosyl-L-methionine (AdoMet).	S-Adenosylmethionine	266-272	NPC intracellular cholesterol transporter 1	Homo sapiens	193-196
3838667-1	1985	Glycine N-methyltransferase, an enzyme that uses S-adenosylmethionine to methylate glycine with the production of sarcosine, was recently shown to be identical with a major folate binding protein of rat liver (Cook, R.J. and Wagner, C. (1984) Proc.	S-Adenosylmethionine	51-69	glycine N-methyltransferase	Rattus norvegicus	0-27
3974415-2	1985	This binding interferes with a NE assay that employs PNMT to catalyze the transfer of a tritiated methyl group from S-adenosyl-L-methionine to the amine group of NE.	S-Adenosylmethionine	116-139	phenylethanolamine N-methyltransferase	Bos taurus	53-57
3927946-5	1985	The sparing effect of methionine can be explained by adenosylmethionine inhibition of methylenetetrahydrofolate reductase, which would prevent the buildup of 5-methyl-H4PteGlun.	S-Adenosylmethionine	53-71	methylenetetrahydrofolate reductase	Homo sapiens	86-121
2859176-5	1985	3-Methoxydenopamine (M-2) and 3-hydroxy-4-O-methyldenopamine (iso-M-2) were formed via the catechol intermediate M-4, when denopamine was incubated with the rat liver 9000g supernatant fraction in the presence of the NADPH-generating system and S-adenosyl-L-methionine.	S-Adenosylmethionine	245-268	cholinergic receptor, muscarinic 4	Rattus norvegicus	113-116
6333423-8	1984	Metabolites of NPC were measured by reverse-phase high-performance liquid chromatography and it was found that the major drug metabolite was the drug analog of S-adenosylmethionine with little formation of the respective, S-adenosylhomocysteine metabolite.	S-Adenosylmethionine	160-180	NPC intracellular cholesterol transporter 1	Homo sapiens	15-18
3836703-3	1985	2.1.1.8; HMT) in the presence of the natural donor of methyl groups, [3H]-methyl-S-adenosyl-L-methionine ([3H]-SAMe).	S-Adenosylmethionine	81-104	histamine N-methyltransferase	Homo sapiens	9-12
6333423-10	1984	These results indicate that NPC is metabolized to a metabolite of S-adenosylmethionine which is a poor methyl donor for RNA methyltransferases, and that the accompanying decrease in RNA methylation and protein synthesis appears to be related to its cytocidal activity.	S-Adenosylmethionine	66-86	NPC intracellular cholesterol transporter 1	Homo sapiens	28-31
6434675-8	1984	However, incubation of inner medullary microsomes with S-adenosyl-L-methionine under conditions leading to phospholipid methylation increased both Ca2+ responsive phospholipase A2 and C activities approximately twofold.	S-Adenosylmethionine	55-78	phospholipase A2 group IB	Rattus norvegicus	163-179
6149973-1	1984	Phenylethanolamine N-methyltransferase (PNMT) is the enzyme that catalyzes the S-adenosyl-L-methionine-dependent methylation of (-)norepinephrine to (-)epinephrine in the adrenal medulla.	S-Adenosylmethionine	79-102	phenylethanolamine-N-methyltransferase	Rattus norvegicus	0-38
6149973-1	1984	Phenylethanolamine N-methyltransferase (PNMT) is the enzyme that catalyzes the S-adenosyl-L-methionine-dependent methylation of (-)norepinephrine to (-)epinephrine in the adrenal medulla.	S-Adenosylmethionine	79-102	phenylethanolamine-N-methyltransferase	Rattus norvegicus	40-44
6084164-4	1984	The specific mechanism is theorized to be as follows: the adenine moiety of S-adenosyl-L-methionine base-pairs with thymine of a specific structural area of the alpha-fetoprotein gene.	S-Adenosylmethionine	76-99	alpha fetoprotein	Homo sapiens	161-178
6084164-6	1984	This weak hydrogen bonding situation allows the methylation by protein methylases of a precursor chromatin protein that after methylation by the S-adenosyl-L-methionine which is base-paired to the specific DNA site, conformationally is set or locked into place and acts as a specific repressor for the alpha-fetoprotein gene.	S-Adenosylmethionine	145-168	alpha fetoprotein	Homo sapiens	302-319
6084164-9	1984	But if the S-adenosyl-L-methionine pool concentration is lowered to a level below that required for base-pairing by the adenine moiety, then the repressed conformational condition of the alpha-fetoprotein gene is altered allowing transcription.	S-Adenosylmethionine	11-34	alpha fetoprotein	Homo sapiens	187-204
6509362-1	1984	The formation of a stably linked complex of tritiated S-adenosyl-L-methionine (AdoMet) and catechol O-methyltransferase (COMT) has been achieved by irradiating the enzyme and ligand in Tris-HCl buffer (pH 7.5) with ultraviolet light at 254 nm.	S-Adenosylmethionine	54-77	catechol-O-methyltransferase	Homo sapiens	121-125
6509362-1	1984	The formation of a stably linked complex of tritiated S-adenosyl-L-methionine (AdoMet) and catechol O-methyltransferase (COMT) has been achieved by irradiating the enzyme and ligand in Tris-HCl buffer (pH 7.5) with ultraviolet light at 254 nm.	S-Adenosylmethionine	79-85	catechol-O-methyltransferase	Homo sapiens	121-125
6380498-1	1984	Radioactivity from 3H-[methyl]-S-adenosyl-L-methionine (AdoMet) was covalently bound to protein-O-carboxylmethyltransferase and phenylethanolamine N-methyltransferase following 10-15 min irradiation by short-wave ultraviolet light.	S-Adenosylmethionine	56-62	phenylethanolamine N-methyltransferase	Homo sapiens	128-166
6491941-1	1984	Catechol derivatives, covalently joined to homocysteine by sulfide or sulfonium linkages, were synthesized as potential catechol O-methyltransferase multisubstrate inhibitors which might bridge the enzymatic binding sites for the catechol substrate and the amino acid portion of the methyl donor S-adenosylmethionine.	S-Adenosylmethionine	296-316	catechol-O-methyltransferase	Homo sapiens	120-148
6496925-1	1984	A high-performance liquid chromatographic method was devised that separates S-adenosylmethionine and related sulfur metabolites on a Radial-PAK SCX cation-exchange column using a four-step NH4COOH/(NH4)2SO4 elution gradient.	S-Adenosylmethionine	76-96	scleraxis bHLH transcription factor	Rattus norvegicus	144-147
6330482-4	1984	The concentration of S-adenosylmethionine (AdoMet) and S-adenosylhomocysteine (AdoHcy), the substrate and physiological inhibitor of transmethylation reactions, respectively, were measured in the spleens of control and viral infected mice.	S-Adenosylmethionine	21-41	methionine adenosyltransferase I, alpha	Mus musculus	43-49
6327688-1	1984	Carboxylmethylation of several preparations of cAMP phosphodiesterase by the enzyme protein O- carboxylmethyltransferase and S-adenosylmethionine reduces the extent to which the enzyme was activated by native calmodulin.	S-Adenosylmethionine	125-145	calmodulin	Bos taurus	209-219
6696933-2	1984	Kinetically, three apparent Km values for S-adenosyl-L-methionine (AdoMet) were obtained when the total [3H]methyl groups incorporation into the phospholipids was examined in the presence of 0.01-250 microM AdoMet.	S-Adenosylmethionine	67-73	methionine adenosyltransferase 1A	Rattus norvegicus	42-65
6722172-9	1984	Hydroxyindole O-methyltransferase cannot form a stable complex with S-adenosylmethionine, and the addition of excess amounts of S-adenosylmethionine impairs the binding of S-adenosylhomocysteine to the enzyme.	S-Adenosylmethionine	68-88	acetylserotonin O-methyltransferase	Bos taurus	0-33
6722172-9	1984	Hydroxyindole O-methyltransferase cannot form a stable complex with S-adenosylmethionine, and the addition of excess amounts of S-adenosylmethionine impairs the binding of S-adenosylhomocysteine to the enzyme.	S-Adenosylmethionine	128-148	acetylserotonin O-methyltransferase	Bos taurus	0-33
6721499-1	1984	The stereochemical course of the methyl group transfer catalyzed by histamine N-methyltransferase was studied using S-adenosylmethionine (AdoMet), which carried a chiral methyl group.	S-Adenosylmethionine	116-136	histamine N-methyltransferase	Cavia porcellus	68-97
6721499-1	1984	The stereochemical course of the methyl group transfer catalyzed by histamine N-methyltransferase was studied using S-adenosylmethionine (AdoMet), which carried a chiral methyl group.	S-Adenosylmethionine	138-144	histamine N-methyltransferase	Cavia porcellus	68-97
6680524-1	1983	The catalysis by phosphatidylethanolamine methyltransferase (PEMT) of phosphatidylcholine (PC) synthesis by the successive methylation of phosphatidylethanolamine in the presence of S-adenosylmethionine (AdoMet) as methyl donor, was detected in actively myelinating mouse brains.	S-Adenosylmethionine	182-202	phosphatidylethanolamine N-methyltransferase	Homo sapiens	17-59
6319050-4	1984	In a novel technique designed to determine the specific activity of small quantities of tritiated S-adenosylmethionine, high performance liquid chromatography with electrochemical detection was used to measure the amount of adrenaline formed from unlabelled noradrenaline, in the presence of phenylethanolamine-N-methyltransferase and tritiated S-adenosylmethionine.	S-Adenosylmethionine	98-118	phenylethanolamine N-methyltransferase	Homo sapiens	292-330
6696751-0	1984	Inactivation of betaine-homocysteine methyltransferase by adenosylmethionine and adenosylethionine.	S-Adenosylmethionine	58-76	betaine-homocysteine S-methyltransferase	Rattus norvegicus	16-54
6696751-1	1984	Preincubation of betaine-homocysteine methyltransferase, prepared from rat liver, with either S-adenosylmethionine or S-adenosylethionine results in a marked loss of enzyme activity.	S-Adenosylmethionine	94-114	betaine-homocysteine S-methyltransferase	Rattus norvegicus	17-55
6607471-7	1984	Effects of ADA inhibition on leukemia cells during treatment included expansion of the deoxyadenosine nucleotide pool and accumulation of S-adenosylhomocysteine, a potent inhibitor of S-adenosylmethionine-dependent methylation.	S-Adenosylmethionine	186-204	adenosine deaminase	Homo sapiens	11-14
6680524-1	1983	The catalysis by phosphatidylethanolamine methyltransferase (PEMT) of phosphatidylcholine (PC) synthesis by the successive methylation of phosphatidylethanolamine in the presence of S-adenosylmethionine (AdoMet) as methyl donor, was detected in actively myelinating mouse brains.	S-Adenosylmethionine	182-202	phosphatidylethanolamine N-methyltransferase	Homo sapiens	61-65
6680524-1	1983	The catalysis by phosphatidylethanolamine methyltransferase (PEMT) of phosphatidylcholine (PC) synthesis by the successive methylation of phosphatidylethanolamine in the presence of S-adenosylmethionine (AdoMet) as methyl donor, was detected in actively myelinating mouse brains.	S-Adenosylmethionine	204-210	phosphatidylethanolamine N-methyltransferase	Homo sapiens	17-59
6140010-0	1983	Activation and inactivation of striatal tyrosine hydroxylase: the effects of pH, ATP and cyclic AMP, S-adenosylmethionine and S-adenosylhomocysteine.	S-Adenosylmethionine	101-121	tyrosine hydroxylase	Rattus norvegicus	40-60
6680524-1	1983	The catalysis by phosphatidylethanolamine methyltransferase (PEMT) of phosphatidylcholine (PC) synthesis by the successive methylation of phosphatidylethanolamine in the presence of S-adenosylmethionine (AdoMet) as methyl donor, was detected in actively myelinating mouse brains.	S-Adenosylmethionine	204-210	phosphatidylethanolamine N-methyltransferase	Homo sapiens	61-65
6343748-5	1983	The use of purified HNMT in the Hm assay has allowed the inclusion of high specific activity tritiated S-adenosyl-L-methionine ([3H]SAME) and the development of a simplified solvent extraction product isolation procedure.	S-Adenosylmethionine	103-126	histamine N-methyltransferase	Homo sapiens	20-24
6882473-8	1983	Cytosolic PCM had an apparent Km of 13.9 x 10(-6) M for AdoMet and a Vmax of 33 pmoles per min per mg protein.	S-Adenosylmethionine	56-62	solute carrier family 40 (iron-regulated transporter), member 1	Mus musculus	10-13
6345158-1	1983	As a tool for the study of the capping-methylation process of yeast mRNA, we developed a procedure for the purification of the mRNA (guanine-7-)methyltransferase using the commercial cap analog guanosine(5")triphospho(5")guanosine as a substrate and radioactive S-adenosylmethionine (AdoMet) as the methyl group donor.	S-Adenosylmethionine	262-282	RNA (guanine-7-) methyltransferase	Mus musculus	127-161
6345158-1	1983	As a tool for the study of the capping-methylation process of yeast mRNA, we developed a procedure for the purification of the mRNA (guanine-7-)methyltransferase using the commercial cap analog guanosine(5")triphospho(5")guanosine as a substrate and radioactive S-adenosylmethionine (AdoMet) as the methyl group donor.	S-Adenosylmethionine	284-290	RNA (guanine-7-) methyltransferase	Mus musculus	127-161
6838886-1	1983	S-Adenosyl-L-methionine, the common methyl donor in enzymatic methylation systems, has been directly cross-linked to phenylethanolamine-N-methyltransferase from bovine adrenal medulla.	S-Adenosylmethionine	0-23	phenylethanolamine N-methyltransferase	Homo sapiens	117-155
6838886-7	1983	The results suggest that the cross-linking occurs at the specific active S-adenosyl-L-methionine-binding site of phenylethanolamine-N-methyltransferase.	S-Adenosylmethionine	75-96	phenylethanolamine N-methyltransferase	Homo sapiens	113-151
6337144-5	1983	These results indicate that the incorporation is occurring at the S-adenosylmethionine binding site in the catechol O-methyltransferase.	S-Adenosylmethionine	66-86	catechol-O-methyltransferase	Homo sapiens	107-135
6303764-0	1982	The effect of S-adenosyl methionine on the TSH receptor function in human thyroid tissue: increase in binding of TSH and decrease in adenylate cyclase coupling.	S-Adenosylmethionine	14-35	thyroid stimulating hormone receptor	Homo sapiens	43-55
6303764-1	1982	To determine the effects of S-Adenosyl methionine (AdoMet) on TSH receptor function and adenylate cyclase coupling, human thyroidal crude membrane fraction was pretreated with AdoMet and with S-Adenosyl homocysteine (AdoHcy), separately or in combination.	S-Adenosylmethionine	51-57	thyroid stimulating hormone receptor	Homo sapiens	62-74
6288234-0	1982	S-Adenosyl-L-methionine is a carbon donor in the conversion of benzo[alpha]pyrene to 6-hydroxymethylbenzo[alpha]pyrene by rat liver S-9.	S-Adenosylmethionine	0-23	ribosomal protein S9	Homo sapiens	132-135
7103990-0	1982	L-2-Amino-4-methoxy-cis-but-3-enoic acid, a potent inhibitor of the enzymatic synthesis of S-adenosylmethionine.	S-Adenosylmethionine	91-111	immunoglobulin kappa variable 3-15	Homo sapiens	0-3
6288234-3	1982	We now report that S-adenosyl-L-methionine (SAM) can serve as a carbon donor in the metabolic formation of 6-hydroxymethylbenzo[alpha]pyrene from benzo[alpha]pyrene by the S-9 fraction of rat liver.	S-Adenosylmethionine	19-42	ribosomal protein S9	Homo sapiens	172-175
6288234-3	1982	We now report that S-adenosyl-L-methionine (SAM) can serve as a carbon donor in the metabolic formation of 6-hydroxymethylbenzo[alpha]pyrene from benzo[alpha]pyrene by the S-9 fraction of rat liver.	S-Adenosylmethionine	44-47	ribosomal protein S9	Homo sapiens	172-175
6807294-2	1982	The content of decarboxylated S-adenosylmethionine (AdoMet) in transformed mouse fibroblasts (SV-3T3 cells) was increased 500-fold to about 0.4fmol/cell when ornithine decarboxylase was inhibited by alpha-difluoromethylornithine.	S-Adenosylmethionine	30-50	ornithine decarboxylase, structural 1	Mus musculus	158-181
7086841-1	1982	Structural analogues of decarboxylated S-adenosyl-L-methionine (dc-SAM), product of the reaction catalyzed by S-adenosyl-L-methionine decarboxylase (SAM-DC), with modifications in the side-chain portion of the molecule have been synthesized, and their ability to inhibit SAM-DC has been investigated.	S-Adenosylmethionine	39-62	adenosylmethionine decarboxylase 1	Homo sapiens	110-147
7086841-1	1982	Structural analogues of decarboxylated S-adenosyl-L-methionine (dc-SAM), product of the reaction catalyzed by S-adenosyl-L-methionine decarboxylase (SAM-DC), with modifications in the side-chain portion of the molecule have been synthesized, and their ability to inhibit SAM-DC has been investigated.	S-Adenosylmethionine	39-62	adenosylmethionine decarboxylase 1	Homo sapiens	149-155
7086841-1	1982	Structural analogues of decarboxylated S-adenosyl-L-methionine (dc-SAM), product of the reaction catalyzed by S-adenosyl-L-methionine decarboxylase (SAM-DC), with modifications in the side-chain portion of the molecule have been synthesized, and their ability to inhibit SAM-DC has been investigated.	S-Adenosylmethionine	39-62	adenosylmethionine decarboxylase 1	Homo sapiens	271-277
6807294-2	1982	The content of decarboxylated S-adenosylmethionine (AdoMet) in transformed mouse fibroblasts (SV-3T3 cells) was increased 500-fold to about 0.4fmol/cell when ornithine decarboxylase was inhibited by alpha-difluoromethylornithine.	S-Adenosylmethionine	52-58	ornithine decarboxylase, structural 1	Mus musculus	158-181
7241150-1	1981	The circadian rhythm of methionine S-adenosyltransferase, which catalyzes the formation of S-adenosylmethionine, a cosubstrate for melatonin in the pineal gland, follows the pattern of hydroxyindole-O-methyltransferase.	S-Adenosylmethionine	91-111	acetylserotonin O-methyltransferase	Homo sapiens	185-218
7051769-0	1982	Modulation of methylenetetrahydrofolate reductase activity by S-adenosylmethionine and by dihydrofolate and its polyglutamate analogues.	S-Adenosylmethionine	62-82	methylenetetrahydrofolate reductase	Homo sapiens	14-49
7051769-6	1982	A priori, one might expect that methylenetetrahydrofolate reductase activity would be modulated by cellular requirements for de novo biosynthesis of purines and pyrimidines, as well as by cellular levels of adenosylmethionine.	S-Adenosylmethionine	207-225	methylenetetrahydrofolate reductase	Homo sapiens	32-67
7051769-12	1982	We have also examined the inhibition of methylenetetrahydrofolate reductase by adenosylmethionine, which serves as an allosteric effector of the enzymatic activity.	S-Adenosylmethionine	79-97	methylenetetrahydrofolate reductase	Homo sapiens	40-75
6272977-7	1981	When the Ames mutagenesis assay was supplemented with COMT/SAM, a 36% reduction was observed in the number of revertant colonies induced by the microsomal oxidation of BP.	S-Adenosylmethionine	59-62	catechol-O-methyltransferase	Homo sapiens	54-58
7296530-0	1981	An inverse correlation between hepatic ornithine decarboxylase and S-adenosylmethionine in rats.	S-Adenosylmethionine	67-87	ornithine decarboxylase 1	Rattus norvegicus	39-62
7219528-3	1981	Recently we and others have demonstrated that various preparations of mammalian brain contain enzymes, the phosphatidylethanolamine N-methyltransferase (PeMT), which catalyse the synthesis of phosphatidylcholine (PC), using S-adenosylmethionine (SAM) as a methyl donor for the stepwise methylation of phosphatidylethanolamine (PE).	S-Adenosylmethionine	224-244	phosphatidylethanolamine N-methyltransferase	Homo sapiens	107-151
7219528-3	1981	Recently we and others have demonstrated that various preparations of mammalian brain contain enzymes, the phosphatidylethanolamine N-methyltransferase (PeMT), which catalyse the synthesis of phosphatidylcholine (PC), using S-adenosylmethionine (SAM) as a methyl donor for the stepwise methylation of phosphatidylethanolamine (PE).	S-Adenosylmethionine	224-244	phosphatidylethanolamine N-methyltransferase	Homo sapiens	153-157
7219528-3	1981	Recently we and others have demonstrated that various preparations of mammalian brain contain enzymes, the phosphatidylethanolamine N-methyltransferase (PeMT), which catalyse the synthesis of phosphatidylcholine (PC), using S-adenosylmethionine (SAM) as a methyl donor for the stepwise methylation of phosphatidylethanolamine (PE).	S-Adenosylmethionine	246-249	phosphatidylethanolamine N-methyltransferase	Homo sapiens	107-151
7219528-3	1981	Recently we and others have demonstrated that various preparations of mammalian brain contain enzymes, the phosphatidylethanolamine N-methyltransferase (PeMT), which catalyse the synthesis of phosphatidylcholine (PC), using S-adenosylmethionine (SAM) as a methyl donor for the stepwise methylation of phosphatidylethanolamine (PE).	S-Adenosylmethionine	246-249	phosphatidylethanolamine N-methyltransferase	Homo sapiens	153-157
7432488-3	1980	In the belief that the key to biological Pb(II) methylation lies in methyl transfer to Pb(II) from a carbonium ion donor (for example, S-adenosylmethionine), we recently initiated chemical and biological studies on the reactions of CH3+ donors with neutral and anionic Pb(II) compounds.	S-Adenosylmethionine	135-155	submaxillary gland androgen regulated protein 3B	Homo sapiens	41-47
6164021-2	1981	Cycloleucine, an inhibitor of the formation of S-adenosylmethionine, decreased the incorporation of methyl groups into methylarginine in myelin basic protein in vivo.	S-Adenosylmethionine	47-67	myelin basic protein	Homo sapiens	137-157
6777088-2	1980	The assay is based on the conversion of NMN or OCT to radiolabeled metanephrine (MN) or synephrine (SYN) by phenylethanolamine-N-methyl transferase (PNMT), using tritium-labeled S-adenosyl-methionine [3H]SAM as methyl donor.	S-Adenosylmethionine	178-199	phenylethanolamine N-methyltransferase	Homo sapiens	149-153
6257844-4	1981	gamma-Aminobutyric acid, diazepine, noradrenaline and alpha antagonists are without any effect; S-adenosyl-L-methionine, adenosine and adenosine triphosphate inhibit SAH binding.	S-Adenosylmethionine	96-119	acyl-CoA synthetase medium-chain family member 3	Rattus norvegicus	166-169
7437264-7	1980	4 Kinetic studies with pooled uraemic plasma demonstrate that inhibition of COMT by uraemic plasma is uncompetitive with respect to both the catechol substrate and the methyl donor for the reaction, S-adenosyl-L-methionine.	S-Adenosylmethionine	199-222	catechol-O-methyltransferase	Homo sapiens	76-80
7432488-3	1980	In the belief that the key to biological Pb(II) methylation lies in methyl transfer to Pb(II) from a carbonium ion donor (for example, S-adenosylmethionine), we recently initiated chemical and biological studies on the reactions of CH3+ donors with neutral and anionic Pb(II) compounds.	S-Adenosylmethionine	135-155	submaxillary gland androgen regulated protein 3B	Homo sapiens	87-93
7432488-3	1980	In the belief that the key to biological Pb(II) methylation lies in methyl transfer to Pb(II) from a carbonium ion donor (for example, S-adenosylmethionine), we recently initiated chemical and biological studies on the reactions of CH3+ donors with neutral and anionic Pb(II) compounds.	S-Adenosylmethionine	135-155	submaxillary gland androgen regulated protein 3B	Homo sapiens	87-93
6997310-1	1980	The steric course of the methyl group transfer catalyzed by catechol O-methyltransferase was studied using S-adenosylmethionine (AdoMet) carrying a methyl group made chiral by labeling with 1H, 2H, and 3H in an asymmetrical arrangement.	S-Adenosylmethionine	107-127	catechol-O-methyltransferase	Rattus norvegicus	60-88
7371936-0	1980	Influence of exogenous L-3,4,-dihydroxyphenylalanine (L-dopa) on the methionine and s-adenosylmethionine concentrations in the brain and other tissues [proceedings].	S-Adenosylmethionine	84-104	immunoglobulin kappa variable 2-14 (pseudogene)	Homo sapiens	23-52
6997310-1	1980	The steric course of the methyl group transfer catalyzed by catechol O-methyltransferase was studied using S-adenosylmethionine (AdoMet) carrying a methyl group made chiral by labeling with 1H, 2H, and 3H in an asymmetrical arrangement.	S-Adenosylmethionine	129-135	catechol-O-methyltransferase	Rattus norvegicus	60-88
6997310-5	1980	The catechol O-methyltransferase reaction thus involves a direct transfer of the methyl group from the sulfur of AdoMet to the oxygen of the catechol in an SN2 process, without a methylated enzyme intermediate.	S-Adenosylmethionine	113-119	catechol-O-methyltransferase	Rattus norvegicus	4-32
7452273-0	1980	Regulation of rat pineal hydroxyindole-O-methyltransferase: evidence of S-adenosylmethionine-mediated glucocorticoid control.	S-Adenosylmethionine	74-92	acetylserotonin O-methyltransferase	Rattus norvegicus	25-58
6254019-2	1980	dAdo also inactivates the enzyme S-adenosylhomocysteine hydrolase (AdoHcyase; S-adenosyl-L-homocystein hydrolase EC 3.3.1.1) which is involved in the catabolism of S-adenosyl-L-homocysteine (AdoHcy), both a product and a potent inhibitor of S-adenosylmethionine-dependent transmethylation.	S-Adenosylmethionine	241-261	adenosylhomocysteinase	Homo sapiens	33-65
6254019-2	1980	dAdo also inactivates the enzyme S-adenosylhomocysteine hydrolase (AdoHcyase; S-adenosyl-L-homocystein hydrolase EC 3.3.1.1) which is involved in the catabolism of S-adenosyl-L-homocysteine (AdoHcy), both a product and a potent inhibitor of S-adenosylmethionine-dependent transmethylation.	S-Adenosylmethionine	241-261	adenosylhomocysteinase	Homo sapiens	67-76
509240-3	1979	This enzyme(s), phosphatidylethanolamine-N-methyltransferase (EC 2.1.1.17), is localized in the synaptosomal fraction of bovine caudate nucleus, uses S-adenosylmethionine as the methyl donor (apparent Km = 20 micrometers), and has a Vmax of 50--60 pmol/mg protein X h (i.e. about 1% of that found in rat liver).	S-Adenosylmethionine	150-170	phosphatidylethanolamine N-methyltransferase	Bos taurus	16-60
228299-1	1979	Addition of the methyl donor S-adenosyl-L-methionine to membranes prepared from mammary glands of lactating mice results in increased binding of 25I-labeled human growth hormone to the lactogenic receptors.	S-Adenosylmethionine	29-52	growth hormone 1	Homo sapiens	163-177
499082-1	1979	Protein carboxyl-methylase (PCM), the enzyme that transfers methyl groups from S-adenosyl-methionine to free carboxyl groups on proteins, is highly localized in testes.	S-Adenosylmethionine	79-100	protein-L-isoaspartate (D-aspartate) O-methyltransferase 1	Rattus norvegicus	0-26
499082-1	1979	Protein carboxyl-methylase (PCM), the enzyme that transfers methyl groups from S-adenosyl-methionine to free carboxyl groups on proteins, is highly localized in testes.	S-Adenosylmethionine	79-100	protein-L-isoaspartate (D-aspartate) O-methyltransferase 1	Rattus norvegicus	28-31
487592-2	1979	Noradrenaline and adrenaline are converted to their O-methylated analogues, normethanephrine and metanephrine, by the enzyme catechol O-methyltransferase in the presence of tritiated S-adenosyl-L-methionine.	S-Adenosylmethionine	183-206	catechol-O-methyltransferase	Homo sapiens	125-153
531079-2	1979	Norepinephrine N-methyltransferase (NMT; the epinephrine-forming enzyme) from pigeon brain had Km values for S-adenosyl-L-methionine and L-norepinephrine of 24 +/- 1 and 101 +/- 4 micrometer, respectively.	S-Adenosylmethionine	109-132	N-myristoyltransferase 1	Homo sapiens	36-39
514254-2	1979	Stabilization of PNMT against thermal and tryptic degradation by S-adenosylmethionine.	S-Adenosylmethionine	65-85	phenylethanolamine-N-methyltransferase	Rattus norvegicus	17-21
228299-4	1979	Scatchard analysis shows that treatment with S-adenosyl-L-methionine results in an increase in the number of lactogenic binding sites without changing the apparent affinity constant for 125I-labeled human growth hormone.	S-Adenosylmethionine	45-68	growth hormone 1	Homo sapiens	205-219
455720-1	1979	A radiometric assay for catechol-O-methyltransferase (COMT) activity in human erythrocytes is described that employs 2-hydroxy[3H]estrone, and non-radiolabeled S-adenosylmethionine (SAM) as the cosubstrates.	S-Adenosylmethionine	160-180	catechol-O-methyltransferase	Homo sapiens	24-52
455720-1	1979	A radiometric assay for catechol-O-methyltransferase (COMT) activity in human erythrocytes is described that employs 2-hydroxy[3H]estrone, and non-radiolabeled S-adenosylmethionine (SAM) as the cosubstrates.	S-Adenosylmethionine	160-180	catechol-O-methyltransferase	Homo sapiens	54-58
455720-1	1979	A radiometric assay for catechol-O-methyltransferase (COMT) activity in human erythrocytes is described that employs 2-hydroxy[3H]estrone, and non-radiolabeled S-adenosylmethionine (SAM) as the cosubstrates.	S-Adenosylmethionine	182-185	catechol-O-methyltransferase	Homo sapiens	24-52
455720-1	1979	A radiometric assay for catechol-O-methyltransferase (COMT) activity in human erythrocytes is described that employs 2-hydroxy[3H]estrone, and non-radiolabeled S-adenosylmethionine (SAM) as the cosubstrates.	S-Adenosylmethionine	182-185	catechol-O-methyltransferase	Homo sapiens	54-58
737254-4	1978	The increased S-adenosylmethionine concentrations in the livers of methionine-treated rats also account for the observed inhibition of N5,N10-methylenetetrahydrofolate reductase activity in this tissue.	S-Adenosylmethionine	14-34	methylenetetrahydrofolate reductase	Rattus norvegicus	142-177
683413-8	1978	Also, when normetanephrine and S-adenosyl-L-methionine were used as substrates, the apparent Km values found with PNMT from rat adrenals and rat brain were similar.	S-Adenosylmethionine	31-54	phenylethanolamine-N-methyltransferase	Rattus norvegicus	114-118
719895-0	1978	Influence of endogenous S-adenosylmethionine on the determination of catechol O-methyltransferase activity in red blood cells.	S-Adenosylmethionine	24-44	catechol-O-methyltransferase	Homo sapiens	69-97
708699-0	1978	Affinity labeling of histamine N-methyltransferase by 2",3"-dialdehyde derivatives of S-adenosylhomocysteine and S-adenosylmethionine.	S-Adenosylmethionine	113-133	histamine N-methyltransferase	Homo sapiens	21-50
659428-2	1978	S-adenosyl-methionine:mRNA (guanine-7)-methyltransferase copurified with guanylyltransferase activity through chromatography on DNA agarose, phosphocellulose, and centrifugation in glycerol gradients, suggesting that the two activities are closely associated.	S-Adenosylmethionine	0-21	RNA (guanine-7-) methyltransferase	Mus musculus	22-56
891794-0	1977	Effect of trypsin, S-adenosylmethionine and ethionine on L-serine sulfhydrase activity.	S-Adenosylmethionine	19-39	cystathionine beta synthase	Rattus norvegicus	59-77
743957-2	1978	The HIOMT preparation was incubated with E2 and [3H]-S-adenosylmethionine (SAM).	S-Adenosylmethionine	75-78	acetylserotonin O-methyltransferase	Bos taurus	4-9
597242-12	1977	They further suggest that glycine N-methyltransferase may have a regulatory role in the utilization of S-adenosylmethionine in the liver.	S-Adenosylmethionine	103-123	glycine N-methyltransferase	Rattus norvegicus	26-53
891794-2	1977	Trypsin also decreases an elevation of serine sulfhydrase activity caused by S-adenosylmethionine.	S-Adenosylmethionine	77-97	cystathionine beta synthase	Rattus norvegicus	39-57
985432-21	1976	On the other hand when the concentration of methionine, and hence adenosylmethionine, is high and there is a surplus of C1 units as a result of excess of dietary supply, formyltetrahydrofolate dehydrogenase disposes of the excess.	S-Adenosylmethionine	66-84	aldehyde dehydrogenase 1 family, member L1	Rattus norvegicus	170-206
907871-2	1977	Degradation of histamine by homogenized human skin in vitro, in the presence of the cofactor S-adenosyl methionine, indicates the presence of the histamine metabolizing enzyme histamine-N-methyl transferase in human skin.	S-Adenosylmethionine	95-114	histamine N-methyltransferase	Homo sapiens	176-206
320194-9	1977	Thus, the affect of metK mutations on the regulation of glycine and methionine synthesis in Salmonella typhimurium appears to be due to either an altered S-adenosylmethionine synthetase or altered S-adenosylmethionine pools.	S-Adenosylmethionine	154-174	methionine adenosyltransferase	Salmonella enterica subsp. enterica serovar Typhimurium str. LT2	20-24
978675-3	1976	Structural analogues of S-adenosyl-L-methionine (SAM), with modifications in the amino acid, sugar, or base portions of the molecule, have been synthesized and evaluated as either inhibitors and/or substrates for the enzymes catechol O-methyltransferase, phenylethanolamine N-methyltransferase, histamine N-methyltransferase, and hydroxyindole O-methyltransferase.	S-Adenosylmethionine	24-47	catechol-O-methyltransferase	Homo sapiens	225-253
978675-3	1976	Structural analogues of S-adenosyl-L-methionine (SAM), with modifications in the amino acid, sugar, or base portions of the molecule, have been synthesized and evaluated as either inhibitors and/or substrates for the enzymes catechol O-methyltransferase, phenylethanolamine N-methyltransferase, histamine N-methyltransferase, and hydroxyindole O-methyltransferase.	S-Adenosylmethionine	24-47	phenylethanolamine N-methyltransferase	Homo sapiens	255-293
978675-3	1976	Structural analogues of S-adenosyl-L-methionine (SAM), with modifications in the amino acid, sugar, or base portions of the molecule, have been synthesized and evaluated as either inhibitors and/or substrates for the enzymes catechol O-methyltransferase, phenylethanolamine N-methyltransferase, histamine N-methyltransferase, and hydroxyindole O-methyltransferase.	S-Adenosylmethionine	24-47	histamine N-methyltransferase	Homo sapiens	295-363
978675-3	1976	Structural analogues of S-adenosyl-L-methionine (SAM), with modifications in the amino acid, sugar, or base portions of the molecule, have been synthesized and evaluated as either inhibitors and/or substrates for the enzymes catechol O-methyltransferase, phenylethanolamine N-methyltransferase, histamine N-methyltransferase, and hydroxyindole O-methyltransferase.	S-Adenosylmethionine	49-52	catechol-O-methyltransferase	Homo sapiens	225-253
978675-3	1976	Structural analogues of S-adenosyl-L-methionine (SAM), with modifications in the amino acid, sugar, or base portions of the molecule, have been synthesized and evaluated as either inhibitors and/or substrates for the enzymes catechol O-methyltransferase, phenylethanolamine N-methyltransferase, histamine N-methyltransferase, and hydroxyindole O-methyltransferase.	S-Adenosylmethionine	49-52	phenylethanolamine N-methyltransferase	Homo sapiens	255-293
978675-3	1976	Structural analogues of S-adenosyl-L-methionine (SAM), with modifications in the amino acid, sugar, or base portions of the molecule, have been synthesized and evaluated as either inhibitors and/or substrates for the enzymes catechol O-methyltransferase, phenylethanolamine N-methyltransferase, histamine N-methyltransferase, and hydroxyindole O-methyltransferase.	S-Adenosylmethionine	49-52	histamine N-methyltransferase	Homo sapiens	295-363
3250-1	1976	Catechol O-methyltransferase of lysed human red blood cells was assayed under optimal conditions, using saturating concentrations of the substrates, S-adenosyl-L-methionine and 3-4-dihydroxybenzoic acid.	S-Adenosylmethionine	149-172	catechol-O-methyltransferase	Homo sapiens	0-28
6786-1	1976	SK&F 64139 is a potent, reversible inhibitor of phenylethanolamine N-methyltransferase; its IC50 concentration in our standard assay system was 1 X 10(-7) M. Kinetically, the compound is a competitive inhibitor with respect to norepinephrine but is uncompetitive when S-adenosylmethionine is the variable substrate.	S-Adenosylmethionine	272-292	phenylethanolamine-N-methyltransferase	Rattus norvegicus	52-90
1058472-4	1975	In the presence of S-adenosylmethionine, the methyl transferases convert the blocked 5"-termini to m7G(5")ppp(5")Gmp- and m7G(5")ppp(5")Amp-.	S-Adenosylmethionine	19-39	5'-nucleotidase, cytosolic II	Homo sapiens	113-116
1194286-4	1975	The second activity transfers a methyl group from S-adenosylmethionine to position 7 of the added guanosine and is designated a S-adenosylmethionine: mRNA (guanine-7-)methyltransferase.	S-Adenosylmethionine	50-70	RNA (guanine-7-) methyltransferase	Mus musculus	150-184
1194286-4	1975	The second activity transfers a methyl group from S-adenosylmethionine to position 7 of the added guanosine and is designated a S-adenosylmethionine: mRNA (guanine-7-)methyltransferase.	S-Adenosylmethionine	52-70	RNA (guanine-7-) methyltransferase	Mus musculus	150-184
1092682-5	1975	The Michaelis constants determined for S-adenosyl-L-methionine and 7-keto-8-aminopelargonic acid were 0.20 mM and 1.2 muM, respectively.	S-Adenosylmethionine	39-62	latexin	Homo sapiens	118-121
4371757-1	1974	Saccharomyces cerevisiae 4094-B (alpha, ade-2, ura-1) in potassium phosphate buffer with glucose under aerobic conditions took up (-)S-adenosyl-l-methionine from the medium in sufficient quantity to permit the demonstration of its accumulation in the vacuole by ultraviolet micrography.	S-Adenosylmethionine	135-156	phosphoribosylaminoimidazole carboxylase ADE2	Saccharomyces cerevisiae S288C	40-45
1092359-7	1975	Its rate was low in the S-adenosylmethionine : N-acetylserotonin O-methyltransferase system (EC 2.1.1.4), and below recognition with S-adenosylmethionine : guanidinoacetate methyltransferase (EC 2.1.1.2) and S-adenosylmethionine : histamine N-methyltransferase (EC 2.1.1.8).	S-Adenosylmethionine	26-44	histamine N-methyltransferase	Homo sapiens	231-260
239677-6	1975	Human catechol O-methyltransferase exhibited lower Km values than did the rat enzyme for S-adenosyl-L-methionine, dopamine and dihydroxybenzoic acid.	S-Adenosylmethionine	89-112	catechol-O-methyltransferase	Homo sapiens	6-34
4371757-1	1974	Saccharomyces cerevisiae 4094-B (alpha, ade-2, ura-1) in potassium phosphate buffer with glucose under aerobic conditions took up (-)S-adenosyl-l-methionine from the medium in sufficient quantity to permit the demonstration of its accumulation in the vacuole by ultraviolet micrography.	S-Adenosylmethionine	135-156	dihydroorotate dehydrogenase	Saccharomyces cerevisiae S288C	47-52
4155290-9	1974	Methylenetetrahydrofolate reductase (EC 1.1.1.68) from sheep liver was inhibited by S-adenosyl-l-methionine in vitro, but not by concentrations of S-adenosyl-l-methionine found in the liver of vitamin B(12)-deficient animals after injection of physiological amounts of l-methionine.	S-Adenosylmethionine	84-107	methylenetetrahydrofolate reductase	Ovis aries	0-35
33894237-1	2021	Methylation of arsenic compounds in the human body occurs following a series of biochemical reactions in the presence of methyl donor S-adenosylmethionine (SAM) and catalyzed by arsenite methyltransferase (AS3MT).	S-Adenosylmethionine	134-154	arsenite methyltransferase	Homo sapiens	206-211
14258724-2	1965	Pineal hydroxyindole-O-methyltransferase, with S-adenosylmethionine, converts 5-hydroxytryptophol to 5-methoxytryptophol.	S-Adenosylmethionine	47-67	acetylserotonin O-methyltransferase	Bos taurus	7-40
33850334-3	2021	This study aimed to identify small molecules binding to the SAM-binding site of the nsp10-nsp16 heterodimer for potential inhibition of methyltransferase activity.	S-Adenosylmethionine	60-63	ORF1a polyprotein;ORF1ab polyprotein	Severe acute respiratory syndrome coronavirus 2	84-89
5420953-12	1970	Injection of testosterone propionate into animals castrated 7 days previously induced a rapid increase in both enzymic activities: ornithine decarboxylase was doubled in 6h, and increased three- to four-fold within 48h, whereas the putrescine-dependent decarboxylation of S-adenosyl-l-methionine doubled in 3h and increased tenfold within 48h of commencement of daily androgen treatments.	S-Adenosylmethionine	272-295	ornithine decarboxylase 1	Rattus norvegicus	131-154
13795316-1	1960	An enzyme, hydroxyindole-O-methyl transferase, that can transfer the methyl group of S-adenosylmethionine to the hydroxy group of N-acetylserotonin to form the hormone melatonin is described.	S-Adenosylmethionine	85-105	acetylserotonin O-methyltransferase	Homo sapiens	11-45
33894237-1	2021	Methylation of arsenic compounds in the human body occurs following a series of biochemical reactions in the presence of methyl donor S-adenosylmethionine (SAM) and catalyzed by arsenite methyltransferase (AS3MT).	S-Adenosylmethionine	156-159	arsenite methyltransferase	Homo sapiens	206-211
34058194-9	2021	As observed in diabetic db/db mice, lean mice treated with 5"-AMP displayed enhanced Foxo1 transcription, involving an increase in cellular adenosine levels and a decrease in the S-adenosylmethionine to S-adenosylhomocysteine ratio.	S-Adenosylmethionine	181-199	forkhead box O1	Mus musculus	85-90
33423577-6	2021	In this process, we purified the nsp10-nsp16 complex to higher than 95% purity and confirmed its binding to the methyl donor SAM, the product of the reaction, S-adenosyl-l-homocysteine (SAH), and a common methyltransferase inhibitor, sinefungin, using isothermal titration calorimetry (ITC).	S-Adenosylmethionine	125-128	ORF1a polyprotein;ORF1ab polyprotein	Severe acute respiratory syndrome coronavirus 2	33-38
33972410-2	2021	These modifications are performed by the Nsp10/14 and Nsp10/16 heterodimers using S-adenosylmethionine as the methyl donor.	S-Adenosylmethionine	82-102	ORF1a polyprotein;ORF1ab polyprotein	Severe acute respiratory syndrome coronavirus 2	41-49
34045189-4	2021	LKB1-deficient tumors showed depletion of S-adenosyl-methionine (SAM-e), which is the primary substrate for DNMT1 activity.	S-Adenosylmethionine	42-63	DNA methyltransferase 1	Homo sapiens	108-113
34045189-4	2021	LKB1-deficient tumors showed depletion of S-adenosyl-methionine (SAM-e), which is the primary substrate for DNMT1 activity.	S-Adenosylmethionine	65-70	DNA methyltransferase 1	Homo sapiens	108-113
33972410-2	2021	These modifications are performed by the Nsp10/14 and Nsp10/16 heterodimers using S-adenosylmethionine as the methyl donor.	S-Adenosylmethionine	82-102	ORF1a polyprotein;ORF1ab polyprotein	Severe acute respiratory syndrome coronavirus 2	54-62
33756106-2	2021	We found that mTORC1 stimulates the synthesis of the major methyl donor, S-adenosylmethionine (SAM), through the control of methionine adenosyltransferase 2 alpha (MAT2A) expression.	S-Adenosylmethionine	73-93	CREB regulated transcription coactivator 1	Mus musculus	14-20
33756106-2	2021	We found that mTORC1 stimulates the synthesis of the major methyl donor, S-adenosylmethionine (SAM), through the control of methionine adenosyltransferase 2 alpha (MAT2A) expression.	S-Adenosylmethionine	73-93	methionine adenosyltransferase 2A	Homo sapiens	124-162
33756106-2	2021	We found that mTORC1 stimulates the synthesis of the major methyl donor, S-adenosylmethionine (SAM), through the control of methionine adenosyltransferase 2 alpha (MAT2A) expression.	S-Adenosylmethionine	73-93	methionine adenosyltransferase 2A	Homo sapiens	164-169
33756106-2	2021	We found that mTORC1 stimulates the synthesis of the major methyl donor, S-adenosylmethionine (SAM), through the control of methionine adenosyltransferase 2 alpha (MAT2A) expression.	S-Adenosylmethionine	95-98	CREB regulated transcription coactivator 1	Mus musculus	14-20
33756106-2	2021	We found that mTORC1 stimulates the synthesis of the major methyl donor, S-adenosylmethionine (SAM), through the control of methionine adenosyltransferase 2 alpha (MAT2A) expression.	S-Adenosylmethionine	95-98	methionine adenosyltransferase 2A	Homo sapiens	124-162
33756106-2	2021	We found that mTORC1 stimulates the synthesis of the major methyl donor, S-adenosylmethionine (SAM), through the control of methionine adenosyltransferase 2 alpha (MAT2A) expression.	S-Adenosylmethionine	95-98	methionine adenosyltransferase 2A	Homo sapiens	164-169
33993848-7	2022	Our study uncovers a new axis of SAH-AHCYL1-PIK3C3, which senses the intracellular level of SAH to inhibit autophagy in an MTORC1-independent manner.Abbreviations: ADOX: adenosine dialdehyde; AHCY: adenosylhomocysteinase; AHCYL1: adenosylhomocysteinase like 1; cLEU: cycloleucine; PIK3C3: phosphatidylinositol 3-kinase catalytic subunit type 3; PtdIns3P: phosphatidylinositol-3-phosphate; SAH: S-adenosyl-l-homocysteine; SAM: S-adenosyl-l-methionine.	S-Adenosylmethionine	426-449	acyl-CoA synthetase medium chain family member 3	Homo sapiens	33-36
33993848-7	2022	Our study uncovers a new axis of SAH-AHCYL1-PIK3C3, which senses the intracellular level of SAH to inhibit autophagy in an MTORC1-independent manner.Abbreviations: ADOX: adenosine dialdehyde; AHCY: adenosylhomocysteinase; AHCYL1: adenosylhomocysteinase like 1; cLEU: cycloleucine; PIK3C3: phosphatidylinositol 3-kinase catalytic subunit type 3; PtdIns3P: phosphatidylinositol-3-phosphate; SAH: S-adenosyl-l-homocysteine; SAM: S-adenosyl-l-methionine.	S-Adenosylmethionine	426-449	adenosylhomocysteinase like 1	Homo sapiens	37-43
33993848-7	2022	Our study uncovers a new axis of SAH-AHCYL1-PIK3C3, which senses the intracellular level of SAH to inhibit autophagy in an MTORC1-independent manner.Abbreviations: ADOX: adenosine dialdehyde; AHCY: adenosylhomocysteinase; AHCYL1: adenosylhomocysteinase like 1; cLEU: cycloleucine; PIK3C3: phosphatidylinositol 3-kinase catalytic subunit type 3; PtdIns3P: phosphatidylinositol-3-phosphate; SAH: S-adenosyl-l-homocysteine; SAM: S-adenosyl-l-methionine.	S-Adenosylmethionine	426-449	phosphatidylinositol 3-kinase catalytic subunit type 3	Homo sapiens	44-50
33993848-7	2022	Our study uncovers a new axis of SAH-AHCYL1-PIK3C3, which senses the intracellular level of SAH to inhibit autophagy in an MTORC1-independent manner.Abbreviations: ADOX: adenosine dialdehyde; AHCY: adenosylhomocysteinase; AHCYL1: adenosylhomocysteinase like 1; cLEU: cycloleucine; PIK3C3: phosphatidylinositol 3-kinase catalytic subunit type 3; PtdIns3P: phosphatidylinositol-3-phosphate; SAH: S-adenosyl-l-homocysteine; SAM: S-adenosyl-l-methionine.	S-Adenosylmethionine	426-449	acyl-CoA synthetase medium chain family member 3	Homo sapiens	92-95
33993848-7	2022	Our study uncovers a new axis of SAH-AHCYL1-PIK3C3, which senses the intracellular level of SAH to inhibit autophagy in an MTORC1-independent manner.Abbreviations: ADOX: adenosine dialdehyde; AHCY: adenosylhomocysteinase; AHCYL1: adenosylhomocysteinase like 1; cLEU: cycloleucine; PIK3C3: phosphatidylinositol 3-kinase catalytic subunit type 3; PtdIns3P: phosphatidylinositol-3-phosphate; SAH: S-adenosyl-l-homocysteine; SAM: S-adenosyl-l-methionine.	S-Adenosylmethionine	426-449	adenosylhomocysteinase	Homo sapiens	37-41
33993848-7	2022	Our study uncovers a new axis of SAH-AHCYL1-PIK3C3, which senses the intracellular level of SAH to inhibit autophagy in an MTORC1-independent manner.Abbreviations: ADOX: adenosine dialdehyde; AHCY: adenosylhomocysteinase; AHCYL1: adenosylhomocysteinase like 1; cLEU: cycloleucine; PIK3C3: phosphatidylinositol 3-kinase catalytic subunit type 3; PtdIns3P: phosphatidylinositol-3-phosphate; SAH: S-adenosyl-l-homocysteine; SAM: S-adenosyl-l-methionine.	S-Adenosylmethionine	426-449	acyl-CoA synthetase medium chain family member 3	Homo sapiens	92-95
33823156-6	2021	In contrast, the MLL4 complex adopts an ordered sequential bi-bi mechanism, in which the cofactor S-adenosylmethionine (AdoMet) binds to the enzyme prior to the H3 peptide, and the methylated H3 peptide dissociates from the enzyme before S-adenosylhomocysteine (AdoHcy) detaches after methylation.	S-Adenosylmethionine	98-118	lysine methyltransferase 2B	Homo sapiens	17-21
34027136-1	2021	Catechol O-methyltransferase, an enzyme involved in the metabolism of catechol containing compounds, catalyzes the transfer of a methyl group between S-adenosylmethionine and the hydroxyl groups of the catechol.	S-Adenosylmethionine	150-170	catechol-O-methyltransferase	Homo sapiens	0-28
33829783-4	2021	Fragment screening followed by iterative structure-guided design enabled >10 000-fold improvement in potency of a family of allosteric MAT2A inhibitors that are substrate noncompetitive and inhibit release of the product, S-adenosyl methionine (SAM), from the enzyme"s active site.	S-Adenosylmethionine	222-243	methionine adenosyltransferase 2A	Homo sapiens	135-140
33829783-4	2021	Fragment screening followed by iterative structure-guided design enabled >10 000-fold improvement in potency of a family of allosteric MAT2A inhibitors that are substrate noncompetitive and inhibit release of the product, S-adenosyl methionine (SAM), from the enzyme"s active site.	S-Adenosylmethionine	245-248	methionine adenosyltransferase 2A	Homo sapiens	135-140
33893330-3	2021	5"-Methylthioadenosine (MTA), the substrate for MTAP, is formed in polyamine synthesis and is recycled by MTAP to S-adenosyl-L-methionine (SAM) via salvage pathways.	S-Adenosylmethionine	114-137	methylthioadenosine phosphorylase	Homo sapiens	48-52
33893330-3	2021	5"-Methylthioadenosine (MTA), the substrate for MTAP, is formed in polyamine synthesis and is recycled by MTAP to S-adenosyl-L-methionine (SAM) via salvage pathways.	S-Adenosylmethionine	114-137	methylthioadenosine phosphorylase	Homo sapiens	106-110
33893330-3	2021	5"-Methylthioadenosine (MTA), the substrate for MTAP, is formed in polyamine synthesis and is recycled by MTAP to S-adenosyl-L-methionine (SAM) via salvage pathways.	S-Adenosylmethionine	139-142	methylthioadenosine phosphorylase	Homo sapiens	48-52
33893330-3	2021	5"-Methylthioadenosine (MTA), the substrate for MTAP, is formed in polyamine synthesis and is recycled by MTAP to S-adenosyl-L-methionine (SAM) via salvage pathways.	S-Adenosylmethionine	139-142	methylthioadenosine phosphorylase	Homo sapiens	106-110
33912173-0	2021	Taurine Antagonizes Macrophages M1 Polarization by Mitophagy-Glycolysis Switch Blockage via Dragging SAM-PP2Ac Transmethylation.	S-Adenosylmethionine	101-104	protein phosphatase 2 catalytic subunit alpha	Homo sapiens	105-110
33827820-4	2021	Mechanistically, GAT2 deficiency boosts the betaine/S-adenosylmethionine (SAM)/hypoxanthine metabolic pathway to inhibit transcription factor KID3 expression through the increased DNA methylation in its promoter region.	S-Adenosylmethionine	52-72	solute carrier family 6 member 13	Homo sapiens	17-21
33827820-4	2021	Mechanistically, GAT2 deficiency boosts the betaine/S-adenosylmethionine (SAM)/hypoxanthine metabolic pathway to inhibit transcription factor KID3 expression through the increased DNA methylation in its promoter region.	S-Adenosylmethionine	74-77	solute carrier family 6 member 13	Homo sapiens	17-21
33823156-6	2021	In contrast, the MLL4 complex adopts an ordered sequential bi-bi mechanism, in which the cofactor S-adenosylmethionine (AdoMet) binds to the enzyme prior to the H3 peptide, and the methylated H3 peptide dissociates from the enzyme before S-adenosylhomocysteine (AdoHcy) detaches after methylation.	S-Adenosylmethionine	120-126	lysine methyltransferase 2B	Homo sapiens	17-21
33476699-2	2021	Intersecting these two cycles, 5,10-methylenetetrahydrofolate reductase (MTHFR) directs one-carbon units from the folate to methionine cycle, to be exclusively used for methionine and S-adenosylmethionine (AdoMet) synthesis.	S-Adenosylmethionine	184-204	methylenetetrahydrofolate reductase	Homo sapiens	31-71
33476699-2	2021	Intersecting these two cycles, 5,10-methylenetetrahydrofolate reductase (MTHFR) directs one-carbon units from the folate to methionine cycle, to be exclusively used for methionine and S-adenosylmethionine (AdoMet) synthesis.	S-Adenosylmethionine	184-204	methylenetetrahydrofolate reductase	Homo sapiens	73-78
33476699-2	2021	Intersecting these two cycles, 5,10-methylenetetrahydrofolate reductase (MTHFR) directs one-carbon units from the folate to methionine cycle, to be exclusively used for methionine and S-adenosylmethionine (AdoMet) synthesis.	S-Adenosylmethionine	206-212	methylenetetrahydrofolate reductase	Homo sapiens	31-71
33476699-2	2021	Intersecting these two cycles, 5,10-methylenetetrahydrofolate reductase (MTHFR) directs one-carbon units from the folate to methionine cycle, to be exclusively used for methionine and S-adenosylmethionine (AdoMet) synthesis.	S-Adenosylmethionine	206-212	methylenetetrahydrofolate reductase	Homo sapiens	73-78
33040301-9	2021	Inactivation of SAMdc enhances the transformation of S-adenosylmethionine to homocysteine and then to methionine.	S-Adenosylmethionine	53-73	adenosylmethionine decarboxylase 1	Homo sapiens	16-21
33753727-0	2021	S-adenosylmethionine upregulates the angiotensin receptor-binding protein ATRAP via the methylation of HuR in NAFLD.	S-Adenosylmethionine	0-20	angiotensin II receptor associated protein	Homo sapiens	74-79
33753727-0	2021	S-adenosylmethionine upregulates the angiotensin receptor-binding protein ATRAP via the methylation of HuR in NAFLD.	S-Adenosylmethionine	0-20	ELAV like RNA binding protein 1	Homo sapiens	103-106
33753727-4	2021	Herein, we explored the effect of supplementary S-adenosylmethionine (SAM), which is the main biological methyl donor in mammalian cells, in regulating AT1R-associated protein (ATRAP), which is the negative regulator of AT1R.	S-Adenosylmethionine	48-68	angiotensin II receptor associated protein	Homo sapiens	152-175
33753727-4	2021	Herein, we explored the effect of supplementary S-adenosylmethionine (SAM), which is the main biological methyl donor in mammalian cells, in regulating AT1R-associated protein (ATRAP), which is the negative regulator of AT1R.	S-Adenosylmethionine	48-68	angiotensin II receptor associated protein	Homo sapiens	177-182
33753727-4	2021	Herein, we explored the effect of supplementary S-adenosylmethionine (SAM), which is the main biological methyl donor in mammalian cells, in regulating AT1R-associated protein (ATRAP), which is the negative regulator of AT1R.	S-Adenosylmethionine	48-68	angiotensin II receptor type 1	Homo sapiens	152-156
33753727-4	2021	Herein, we explored the effect of supplementary S-adenosylmethionine (SAM), which is the main biological methyl donor in mammalian cells, in regulating AT1R-associated protein (ATRAP), which is the negative regulator of AT1R.	S-Adenosylmethionine	70-73	angiotensin II receptor associated protein	Homo sapiens	152-175
33753727-4	2021	Herein, we explored the effect of supplementary S-adenosylmethionine (SAM), which is the main biological methyl donor in mammalian cells, in regulating AT1R-associated protein (ATRAP), which is the negative regulator of AT1R.	S-Adenosylmethionine	70-73	angiotensin II receptor associated protein	Homo sapiens	177-182
33753727-4	2021	Herein, we explored the effect of supplementary S-adenosylmethionine (SAM), which is the main biological methyl donor in mammalian cells, in regulating AT1R-associated protein (ATRAP), which is the negative regulator of AT1R.	S-Adenosylmethionine	70-73	angiotensin II receptor type 1	Homo sapiens	152-156
33656855-1	2021	S-Adenosyl-l-methionine (AdoMet) is synthesized by the MAT2A isozyme of methionine adenosyltransferase in most human tissues and in cancers.	S-Adenosylmethionine	0-23	methionine adenosyltransferase 2A	Homo sapiens	55-60
33656855-1	2021	S-Adenosyl-l-methionine (AdoMet) is synthesized by the MAT2A isozyme of methionine adenosyltransferase in most human tissues and in cancers.	S-Adenosylmethionine	25-31	methionine adenosyltransferase 2A	Homo sapiens	55-60
33649426-2	2021	Here we demonstrate with a range of experimental approaches using cell lines, in vitro systems, and recombinantly expressed enzyme, that human methyltransferase-like protein 7B (METTL7B) catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to hydrogen sulfide (H2S) and other exogenous thiol small molecules.	S-Adenosylmethionine	233-256	methyltransferase like 7B	Homo sapiens	143-176
33453420-3	2021	Nicotinamide N-methyltransferase (NNMT) is a metabolic enzyme that catalyzes the methylation of nicotinamide (NAM) using the universal methyl donor S-adenosyl methionine (SAM), directly linking one-carbon metabolism with a cell"s methylation balance and nicotinamide adenine dinucleotide (NAD+) levels.	S-Adenosylmethionine	148-169	nicotinamide N-methyltransferase	Homo sapiens	0-32
33453420-3	2021	Nicotinamide N-methyltransferase (NNMT) is a metabolic enzyme that catalyzes the methylation of nicotinamide (NAM) using the universal methyl donor S-adenosyl methionine (SAM), directly linking one-carbon metabolism with a cell"s methylation balance and nicotinamide adenine dinucleotide (NAD+) levels.	S-Adenosylmethionine	148-169	nicotinamide N-methyltransferase	Homo sapiens	34-38
33453420-3	2021	Nicotinamide N-methyltransferase (NNMT) is a metabolic enzyme that catalyzes the methylation of nicotinamide (NAM) using the universal methyl donor S-adenosyl methionine (SAM), directly linking one-carbon metabolism with a cell"s methylation balance and nicotinamide adenine dinucleotide (NAD+) levels.	S-Adenosylmethionine	171-174	nicotinamide N-methyltransferase	Homo sapiens	0-32
33453420-3	2021	Nicotinamide N-methyltransferase (NNMT) is a metabolic enzyme that catalyzes the methylation of nicotinamide (NAM) using the universal methyl donor S-adenosyl methionine (SAM), directly linking one-carbon metabolism with a cell"s methylation balance and nicotinamide adenine dinucleotide (NAD+) levels.	S-Adenosylmethionine	171-174	nicotinamide N-methyltransferase	Homo sapiens	34-38
33649426-2	2021	Here we demonstrate with a range of experimental approaches using cell lines, in vitro systems, and recombinantly expressed enzyme, that human methyltransferase-like protein 7B (METTL7B) catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to hydrogen sulfide (H2S) and other exogenous thiol small molecules.	S-Adenosylmethionine	233-256	methyltransferase like 7B	Homo sapiens	178-185
33649426-2	2021	Here we demonstrate with a range of experimental approaches using cell lines, in vitro systems, and recombinantly expressed enzyme, that human methyltransferase-like protein 7B (METTL7B) catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to hydrogen sulfide (H2S) and other exogenous thiol small molecules.	S-Adenosylmethionine	258-264	methyltransferase like 7B	Homo sapiens	143-176
33649426-2	2021	Here we demonstrate with a range of experimental approaches using cell lines, in vitro systems, and recombinantly expressed enzyme, that human methyltransferase-like protein 7B (METTL7B) catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to hydrogen sulfide (H2S) and other exogenous thiol small molecules.	S-Adenosylmethionine	258-264	methyltransferase like 7B	Homo sapiens	178-185
33482580-3	2021	Furthermore, S-adenosylmethionine (SAM) sensor upstream of mTORC1 indirectly inhibits mTORC1 activity via the methionine metabolite SAM.	S-Adenosylmethionine	13-33	CREB regulated transcription coactivator 1	Mus musculus	59-65
32492698-1	2021	BACKGROUND: The S-adenosyl-methionine (SAM) availability is crucial for DNA methylation, an epigenetic mechanism involved in nonsyndromic cleft lip with or without cleft palate (NSCL/P) expression.	S-Adenosylmethionine	16-37	nescient helix-loop-helix 1	Homo sapiens	178-182
32492698-1	2021	BACKGROUND: The S-adenosyl-methionine (SAM) availability is crucial for DNA methylation, an epigenetic mechanism involved in nonsyndromic cleft lip with or without cleft palate (NSCL/P) expression.	S-Adenosylmethionine	39-42	nescient helix-loop-helix 1	Homo sapiens	178-182
33482580-3	2021	Furthermore, S-adenosylmethionine (SAM) sensor upstream of mTORC1 indirectly inhibits mTORC1 activity via the methionine metabolite SAM.	S-Adenosylmethionine	13-33	CREB regulated transcription coactivator 1	Mus musculus	86-92
33482580-3	2021	Furthermore, S-adenosylmethionine (SAM) sensor upstream of mTORC1 indirectly inhibits mTORC1 activity via the methionine metabolite SAM.	S-Adenosylmethionine	35-38	CREB regulated transcription coactivator 1	Mus musculus	59-65
33482580-3	2021	Furthermore, S-adenosylmethionine (SAM) sensor upstream of mTORC1 indirectly inhibits mTORC1 activity via the methionine metabolite SAM.	S-Adenosylmethionine	35-38	CREB regulated transcription coactivator 1	Mus musculus	86-92
33668468-1	2021	Nicotinamide-N-methyltransferase (NNMT) is a cytosolic enzyme catalyzing the transfer of a methyl group from S-adenosyl-methionine (SAM) to nicotinamide (Nam).	S-Adenosylmethionine	109-130	nicotinamide N-methyltransferase	Homo sapiens	0-32
33668468-1	2021	Nicotinamide-N-methyltransferase (NNMT) is a cytosolic enzyme catalyzing the transfer of a methyl group from S-adenosyl-methionine (SAM) to nicotinamide (Nam).	S-Adenosylmethionine	109-130	nicotinamide N-methyltransferase	Homo sapiens	34-38
33668468-1	2021	Nicotinamide-N-methyltransferase (NNMT) is a cytosolic enzyme catalyzing the transfer of a methyl group from S-adenosyl-methionine (SAM) to nicotinamide (Nam).	S-Adenosylmethionine	132-135	nicotinamide N-methyltransferase	Homo sapiens	0-32
33668468-1	2021	Nicotinamide-N-methyltransferase (NNMT) is a cytosolic enzyme catalyzing the transfer of a methyl group from S-adenosyl-methionine (SAM) to nicotinamide (Nam).	S-Adenosylmethionine	132-135	nicotinamide N-methyltransferase	Homo sapiens	34-38
33450196-4	2021	We report the characterization of potent MAT2A inhibitors that substantially reduce levels of S-adenosylmethionine (SAM) and demonstrate antiproliferative activity in MTAP-deleted cancer cells and tumors.	S-Adenosylmethionine	94-114	methionine adenosyltransferase 2A	Homo sapiens	41-46
33450196-4	2021	We report the characterization of potent MAT2A inhibitors that substantially reduce levels of S-adenosylmethionine (SAM) and demonstrate antiproliferative activity in MTAP-deleted cancer cells and tumors.	S-Adenosylmethionine	116-119	methionine adenosyltransferase 2A	Homo sapiens	41-46
33510167-4	2021	We show that oxidative stress activates FOXO3 and its transcriptional target glycine-N-methyltransferase (GNMT) whose upregulation triggers depletion of s-adenosylmethionine (SAM), a key co-substrate involved in methyl group transfer reactions.	S-Adenosylmethionine	153-173	forkhead box O3	Homo sapiens	40-45
33562493-1	2021	Lipoyl synthase (LIAS) is an iron-sulfur cluster protein and a member of the radical S-adenosylmethionine (SAM) superfamily that catalyzes the final step of lipoic acid biosynthesis.	S-Adenosylmethionine	85-105	lipoic acid synthetase	Homo sapiens	0-15
33562493-1	2021	Lipoyl synthase (LIAS) is an iron-sulfur cluster protein and a member of the radical S-adenosylmethionine (SAM) superfamily that catalyzes the final step of lipoic acid biosynthesis.	S-Adenosylmethionine	85-105	lipoic acid synthetase	Homo sapiens	17-21
33562493-1	2021	Lipoyl synthase (LIAS) is an iron-sulfur cluster protein and a member of the radical S-adenosylmethionine (SAM) superfamily that catalyzes the final step of lipoic acid biosynthesis.	S-Adenosylmethionine	107-110	lipoic acid synthetase	Homo sapiens	0-15
33562493-1	2021	Lipoyl synthase (LIAS) is an iron-sulfur cluster protein and a member of the radical S-adenosylmethionine (SAM) superfamily that catalyzes the final step of lipoic acid biosynthesis.	S-Adenosylmethionine	107-110	lipoic acid synthetase	Homo sapiens	17-21
33510167-4	2021	We show that oxidative stress activates FOXO3 and its transcriptional target glycine-N-methyltransferase (GNMT) whose upregulation triggers depletion of s-adenosylmethionine (SAM), a key co-substrate involved in methyl group transfer reactions.	S-Adenosylmethionine	153-173	glycine N-methyltransferase	Homo sapiens	77-104
33510167-4	2021	We show that oxidative stress activates FOXO3 and its transcriptional target glycine-N-methyltransferase (GNMT) whose upregulation triggers depletion of s-adenosylmethionine (SAM), a key co-substrate involved in methyl group transfer reactions.	S-Adenosylmethionine	153-173	glycine N-methyltransferase	Homo sapiens	106-110
33510167-4	2021	We show that oxidative stress activates FOXO3 and its transcriptional target glycine-N-methyltransferase (GNMT) whose upregulation triggers depletion of s-adenosylmethionine (SAM), a key co-substrate involved in methyl group transfer reactions.	S-Adenosylmethionine	175-178	forkhead box O3	Homo sapiens	40-45
33510167-4	2021	We show that oxidative stress activates FOXO3 and its transcriptional target glycine-N-methyltransferase (GNMT) whose upregulation triggers depletion of s-adenosylmethionine (SAM), a key co-substrate involved in methyl group transfer reactions.	S-Adenosylmethionine	175-178	glycine N-methyltransferase	Homo sapiens	77-104
33510167-4	2021	We show that oxidative stress activates FOXO3 and its transcriptional target glycine-N-methyltransferase (GNMT) whose upregulation triggers depletion of s-adenosylmethionine (SAM), a key co-substrate involved in methyl group transfer reactions.	S-Adenosylmethionine	175-178	glycine N-methyltransferase	Homo sapiens	106-110
32940141-4	2021	The expression of serine metabolism-related enzymes phosphoserine aminotransferase 1 (PSAT1) and phosphoglycerate (PHGDH) decreased in A-DPSCs and provided less methyl donor S-adenosylmethionine (SAM) for DNA methylation, leading to the hypomethylation of the senescence marker p16 (CDNK2A).	S-Adenosylmethionine	174-194	phosphoserine aminotransferase 1	Homo sapiens	52-84
33523930-4	2021	Despite the elevated levels of MNA in T cells, the expression of nicotinamide N-methyltransferase, the enzyme that catalyzes the transfer of a methyl group from S-adenosylmethionine to nicotinamide, was restricted to fibroblasts and tumor cells.	S-Adenosylmethionine	161-181	nicotinamide N-methyltransferase	Homo sapiens	65-97
32816178-11	2021	Compared with the control group, treatment of A549 cells with NaAsO2/S-adenosylmethionine (SAM) and NaAsO2/glutathione (GSH) combination increased HOTAIR and LincRNA-p21 expression.	S-Adenosylmethionine	69-89	HOX transcript antisense RNA	Homo sapiens	147-153
32816178-11	2021	Compared with the control group, treatment of A549 cells with NaAsO2/S-adenosylmethionine (SAM) and NaAsO2/glutathione (GSH) combination increased HOTAIR and LincRNA-p21 expression.	S-Adenosylmethionine	69-89	tumor protein p53 pathway corepressor 1	Homo sapiens	158-169
32816178-11	2021	Compared with the control group, treatment of A549 cells with NaAsO2/S-adenosylmethionine (SAM) and NaAsO2/glutathione (GSH) combination increased HOTAIR and LincRNA-p21 expression.	S-Adenosylmethionine	91-94	HOX transcript antisense RNA	Homo sapiens	147-153
32816178-11	2021	Compared with the control group, treatment of A549 cells with NaAsO2/S-adenosylmethionine (SAM) and NaAsO2/glutathione (GSH) combination increased HOTAIR and LincRNA-p21 expression.	S-Adenosylmethionine	91-94	tumor protein p53 pathway corepressor 1	Homo sapiens	158-169
33532242-0	2021	Co-therapy with S-adenosylmethionine and nicotinamide riboside improves t-cell survival and function in Arts Syndrome (PRPS1 deficiency).	S-Adenosylmethionine	16-36	phosphoribosyl pyrophosphate synthetase 1	Homo sapiens	119-124
33464427-0	2021	Increasing glycolysis by deletion of kcs1 and arg82 improved S-adenosyl-L-methionine production in Saccharomyces cerevisiae.	S-Adenosylmethionine	61-84	inositol polyphosphate kinase KCS1	Saccharomyces cerevisiae S288C	37-41
33464427-0	2021	Increasing glycolysis by deletion of kcs1 and arg82 improved S-adenosyl-L-methionine production in Saccharomyces cerevisiae.	S-Adenosylmethionine	61-84	inositol polyphosphate multikinase	Saccharomyces cerevisiae S288C	46-51
32940141-4	2021	The expression of serine metabolism-related enzymes phosphoserine aminotransferase 1 (PSAT1) and phosphoglycerate (PHGDH) decreased in A-DPSCs and provided less methyl donor S-adenosylmethionine (SAM) for DNA methylation, leading to the hypomethylation of the senescence marker p16 (CDNK2A).	S-Adenosylmethionine	174-194	phosphoserine aminotransferase 1	Homo sapiens	86-91
32940141-4	2021	The expression of serine metabolism-related enzymes phosphoserine aminotransferase 1 (PSAT1) and phosphoglycerate (PHGDH) decreased in A-DPSCs and provided less methyl donor S-adenosylmethionine (SAM) for DNA methylation, leading to the hypomethylation of the senescence marker p16 (CDNK2A).	S-Adenosylmethionine	174-194	phosphoglycerate dehydrogenase	Homo sapiens	115-120
32940141-4	2021	The expression of serine metabolism-related enzymes phosphoserine aminotransferase 1 (PSAT1) and phosphoglycerate (PHGDH) decreased in A-DPSCs and provided less methyl donor S-adenosylmethionine (SAM) for DNA methylation, leading to the hypomethylation of the senescence marker p16 (CDNK2A).	S-Adenosylmethionine	196-199	phosphoserine aminotransferase 1	Homo sapiens	52-84
32940141-4	2021	The expression of serine metabolism-related enzymes phosphoserine aminotransferase 1 (PSAT1) and phosphoglycerate (PHGDH) decreased in A-DPSCs and provided less methyl donor S-adenosylmethionine (SAM) for DNA methylation, leading to the hypomethylation of the senescence marker p16 (CDNK2A).	S-Adenosylmethionine	196-199	phosphoserine aminotransferase 1	Homo sapiens	86-91
32940141-4	2021	The expression of serine metabolism-related enzymes phosphoserine aminotransferase 1 (PSAT1) and phosphoglycerate (PHGDH) decreased in A-DPSCs and provided less methyl donor S-adenosylmethionine (SAM) for DNA methylation, leading to the hypomethylation of the senescence marker p16 (CDNK2A).	S-Adenosylmethionine	196-199	phosphoglycerate dehydrogenase	Homo sapiens	115-120
33035507-1	2020	3-Deazadenosine (3-DA) is a general methylation inhibitor that depletes S-adenosylmethionine, a methyl donor, by blocking S-adenosylhomocysteine hydrolase (SAHH).	S-Adenosylmethionine	72-92	adenosylhomocysteinase	Homo sapiens	122-154
33328229-4	2020	SAH is a potent feedback inhibitor of S-adenosylmethionine (SAM)-dependent methyltransferases, and timely hydrolysis of SAH by AHCY is critical to sustain methylation reactions.	S-Adenosylmethionine	38-58	adenosylhomocysteinase	Homo sapiens	127-131
33328229-4	2020	SAH is a potent feedback inhibitor of S-adenosylmethionine (SAM)-dependent methyltransferases, and timely hydrolysis of SAH by AHCY is critical to sustain methylation reactions.	S-Adenosylmethionine	60-63	adenosylhomocysteinase	Homo sapiens	127-131
33241846-8	2020	Importantly, we found that GNMT, a multiple functional protein that regulates the cellular pool of methyl groups by controlling the ratio of S-adenosylmethionine (SAM) to S-adenosylhomocysteine (SAH), was down-regulated significantly in the serum of Type 1 DM patients and renal tissues of DN mice.	S-Adenosylmethionine	141-161	glycine N-methyltransferase	Homo sapiens	27-31
33241846-8	2020	Importantly, we found that GNMT, a multiple functional protein that regulates the cellular pool of methyl groups by controlling the ratio of S-adenosylmethionine (SAM) to S-adenosylhomocysteine (SAH), was down-regulated significantly in the serum of Type 1 DM patients and renal tissues of DN mice.	S-Adenosylmethionine	163-166	glycine N-methyltransferase	Homo sapiens	27-31
33396625-0	2020	S-Adenosylmethionine Inhibits Cell Growth and Migration of Triple Negative Breast Cancer Cells through Upregulating MiRNA-34c and MiRNA-449a.	S-Adenosylmethionine	0-20	microRNA 34c	Homo sapiens	116-125
33374288-0	2020	S-Adenosyl-l-Methionine Overcomes uL3-Mediated Drug Resistance in p53 Deleted Colon Cancer Cells.	S-Adenosylmethionine	0-23	tumor protein p53	Homo sapiens	66-69
33374288-1	2020	PURPOSE: In order to study novel therapeutic approaches taking advantage of natural compounds showing anticancer and anti-proliferative effects, we focused our interest on S-adenosyl-l-methionine, a naturally occurring sulfur-containing nucleoside synthesized from adenosine triphosphate and methionine by methionine adenosyltransferase, and its potential in overcoming drug resistance in colon cancer cells devoid of p53.	S-Adenosylmethionine	172-195	tumor protein p53	Homo sapiens	418-421
33374288-2	2020	RESULTS: In the present study, we demonstrated that S-adenosyl-l-methionine overcomes uL3-mediated drug resistance in p53 deleted colon cancer cells.	S-Adenosylmethionine	52-75	tumor protein p53	Homo sapiens	118-121
33374288-4	2020	CONCLUSIONS: Results reported in this paper led us to propose S-adenosyl-l-methionine as a potential promising agent for cancer therapy by examining p53 and uL3 profiles in tumors to yield a better clinical outcomes.	S-Adenosylmethionine	62-85	tumor protein p53	Homo sapiens	149-152
33437781-2	2020	S-adenosyl-L-homocysteine hydrolase (SAHH) inhibitors prevent the feedback of transmethylation reactions by S-adenosyl-L-homocysteine (SAH) accumulation, a competitive antagonist of S-adenosylmethionine (SAM)-dependent methyltransferases.	S-Adenosylmethionine	182-202	S-adenosylhomocysteine hydrolase	Mus musculus	0-35
33437781-2	2020	S-adenosyl-L-homocysteine hydrolase (SAHH) inhibitors prevent the feedback of transmethylation reactions by S-adenosyl-L-homocysteine (SAH) accumulation, a competitive antagonist of S-adenosylmethionine (SAM)-dependent methyltransferases.	S-Adenosylmethionine	182-202	S-adenosylhomocysteine hydrolase	Mus musculus	37-41
33437781-2	2020	S-adenosyl-L-homocysteine hydrolase (SAHH) inhibitors prevent the feedback of transmethylation reactions by S-adenosyl-L-homocysteine (SAH) accumulation, a competitive antagonist of S-adenosylmethionine (SAM)-dependent methyltransferases.	S-Adenosylmethionine	204-207	S-adenosylhomocysteine hydrolase	Mus musculus	0-35
33437781-2	2020	S-adenosyl-L-homocysteine hydrolase (SAHH) inhibitors prevent the feedback of transmethylation reactions by S-adenosyl-L-homocysteine (SAH) accumulation, a competitive antagonist of S-adenosylmethionine (SAM)-dependent methyltransferases.	S-Adenosylmethionine	204-207	S-adenosylhomocysteine hydrolase	Mus musculus	37-41
33035507-1	2020	3-Deazadenosine (3-DA) is a general methylation inhibitor that depletes S-adenosylmethionine, a methyl donor, by blocking S-adenosylhomocysteine hydrolase (SAHH).	S-Adenosylmethionine	72-92	adenosylhomocysteinase	Homo sapiens	156-160
33263851-3	2020	In rats treated with ademetionine, AST activity decreased as soon as on day 7 and remained at this level until the end of the experiment; ALT, alkaline phosphatase, and gamma-glutamyl transferase activities decreased on days 21 and 28 of the study.	S-Adenosylmethionine	21-33	gamma-glutamyltransferase 1	Rattus norvegicus	169-195
32808710-11	2020	S-adenosylmethionine, an established methyl donor, reversed TNFR-1 up-regulation and restored cell viability against high-glucose concentration and TNF-alpha.	S-Adenosylmethionine	0-20	TNF receptor superfamily member 1A	Homo sapiens	60-66
32808710-11	2020	S-adenosylmethionine, an established methyl donor, reversed TNFR-1 up-regulation and restored cell viability against high-glucose concentration and TNF-alpha.	S-Adenosylmethionine	0-20	tumor necrosis factor	Homo sapiens	148-157
32255258-6	2020	The interaction of WBSCR27 with the cofactor S-(5"-adenosyl)-L-methionine (SAM) and its metabolic products - SAH, MTA and 5"dAdo - was studied by NMR and isothermal titration calorimetry.	S-Adenosylmethionine	75-78	methyltransferase like 27	Mus musculus	19-26
32219484-0	2020	S-adenosylmethionine induces apoptosis and cycle arrest of gallbladder carcinoma cells by suppression of JAK2/STAT3 pathways.	S-Adenosylmethionine	0-20	Janus kinase 2	Homo sapiens	105-109
32916306-9	2020	Furthermore, changes in the plasma metabolites glycine, betaine, methionine and lysine (associated with the S-adenosylmethionine cycle) were also associated with altered striatal DAT expression.	S-Adenosylmethionine	110-128	solute carrier family 6 member 3	Homo sapiens	179-182
32219484-0	2020	S-adenosylmethionine induces apoptosis and cycle arrest of gallbladder carcinoma cells by suppression of JAK2/STAT3 pathways.	S-Adenosylmethionine	0-20	signal transducer and activator of transcription 3	Homo sapiens	110-115
33185982-3	2021	We demonstrate that the metabolites generated by metalloenzymes nitric oxide synthase and the radical S-adenosylmethionine (SAM) enzyme RSAD2 inhibit the activity of the housekeeping and glycolytic enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH).	S-Adenosylmethionine	102-122	radical S-adenosyl methionine domain containing 2	Homo sapiens	136-141
33245113-6	2020	We demonstrated that licochalcone A is a non-S-adenosyl L-methionine (SAM) binding site competitive inhibitor of PRMT6.	S-Adenosylmethionine	70-73	protein arginine methyltransferase 6	Homo sapiens	113-118
33252031-5	2022	Fourteen out of fifty-eight compounds were exhibited binding affinity higher than co-crystal bound ligand s-adenosylmethionine (SAM) toward Nsp16-Nsp10.	S-Adenosylmethionine	106-126	ORF1a polyprotein;ORF1ab polyprotein	Severe acute respiratory syndrome coronavirus 2	146-151
33252031-5	2022	Fourteen out of fifty-eight compounds were exhibited binding affinity higher than co-crystal bound ligand s-adenosylmethionine (SAM) toward Nsp16-Nsp10.	S-Adenosylmethionine	128-131	ORF1a polyprotein;ORF1ab polyprotein	Severe acute respiratory syndrome coronavirus 2	146-151
32912785-5	2020	PEMT converts PE into PC using methyl group by S-adenosylmethionine (SAM) thus converted in S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	47-67	phosphatidylethanolamine N-methyltransferase	Homo sapiens	0-4
32912785-5	2020	PEMT converts PE into PC using methyl group by S-adenosylmethionine (SAM) thus converted in S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	69-72	phosphatidylethanolamine N-methyltransferase	Homo sapiens	0-4
33185982-3	2021	We demonstrate that the metabolites generated by metalloenzymes nitric oxide synthase and the radical S-adenosylmethionine (SAM) enzyme RSAD2 inhibit the activity of the housekeeping and glycolytic enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH).	S-Adenosylmethionine	102-122	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	247-252
33185982-3	2021	We demonstrate that the metabolites generated by metalloenzymes nitric oxide synthase and the radical S-adenosylmethionine (SAM) enzyme RSAD2 inhibit the activity of the housekeeping and glycolytic enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH).	S-Adenosylmethionine	124-127	radical S-adenosyl methionine domain containing 2	Homo sapiens	136-141
33185982-3	2021	We demonstrate that the metabolites generated by metalloenzymes nitric oxide synthase and the radical S-adenosylmethionine (SAM) enzyme RSAD2 inhibit the activity of the housekeeping and glycolytic enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH).	S-Adenosylmethionine	124-127	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	205-245
33185982-3	2021	We demonstrate that the metabolites generated by metalloenzymes nitric oxide synthase and the radical S-adenosylmethionine (SAM) enzyme RSAD2 inhibit the activity of the housekeeping and glycolytic enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH).	S-Adenosylmethionine	102-122	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	205-245
32994211-3	2020	We determined the structures for nsp16-nsp10 heterodimers bound to the methyl donor S-adenosylmethionine (SAM), the reaction product S-adenosylhomocysteine (SAH), or the SAH analog sinefungin (SFG).	S-Adenosylmethionine	84-104	ORF1a polyprotein;ORF1ab polyprotein	Severe acute respiratory syndrome coronavirus 2	39-44
33185982-3	2021	We demonstrate that the metabolites generated by metalloenzymes nitric oxide synthase and the radical S-adenosylmethionine (SAM) enzyme RSAD2 inhibit the activity of the housekeeping and glycolytic enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH).	S-Adenosylmethionine	124-127	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	247-252
33074454-7	2022	Folate, vitamin B6, vitamin B12, and S-adenosylmethionine (SAM) are vital cofactors involved in DNA methylation modification; 5-azacytidine (AZA) is the most widely studied DNA methyltransferase (DNMT) inhibitor, and dietary polyphenols are DNMT inhibitors in vitro.	S-Adenosylmethionine	37-57	DNA methyltransferase 1	Homo sapiens	196-200
33074454-7	2022	Folate, vitamin B6, vitamin B12, and S-adenosylmethionine (SAM) are vital cofactors involved in DNA methylation modification; 5-azacytidine (AZA) is the most widely studied DNA methyltransferase (DNMT) inhibitor, and dietary polyphenols are DNMT inhibitors in vitro.	S-Adenosylmethionine	37-57	DNA methyltransferase 1	Homo sapiens	241-245
33074454-7	2022	Folate, vitamin B6, vitamin B12, and S-adenosylmethionine (SAM) are vital cofactors involved in DNA methylation modification; 5-azacytidine (AZA) is the most widely studied DNA methyltransferase (DNMT) inhibitor, and dietary polyphenols are DNMT inhibitors in vitro.	S-Adenosylmethionine	59-62	DNA methyltransferase 1	Homo sapiens	173-194
33074454-7	2022	Folate, vitamin B6, vitamin B12, and S-adenosylmethionine (SAM) are vital cofactors involved in DNA methylation modification; 5-azacytidine (AZA) is the most widely studied DNA methyltransferase (DNMT) inhibitor, and dietary polyphenols are DNMT inhibitors in vitro.	S-Adenosylmethionine	59-62	DNA methyltransferase 1	Homo sapiens	196-200
33074454-7	2022	Folate, vitamin B6, vitamin B12, and S-adenosylmethionine (SAM) are vital cofactors involved in DNA methylation modification; 5-azacytidine (AZA) is the most widely studied DNA methyltransferase (DNMT) inhibitor, and dietary polyphenols are DNMT inhibitors in vitro.	S-Adenosylmethionine	59-62	DNA methyltransferase 1	Homo sapiens	241-245
32750467-5	2020	The whole three-step process follows a particular order: (i) transfer of a methyl group from S-adenosyl methionine (SAM) onto a GTP forming m7GTP; (ii) guanylylation of the enzyme to form a m7GMP-nsP1adduct; (iii) transfer of m7GMP onto 5"-diphosphate RNA to yield capped RNA.	S-Adenosylmethionine	93-114	SH2 domain containing 3A	Homo sapiens	196-200
32750467-5	2020	The whole three-step process follows a particular order: (i) transfer of a methyl group from S-adenosyl methionine (SAM) onto a GTP forming m7GTP; (ii) guanylylation of the enzyme to form a m7GMP-nsP1adduct; (iii) transfer of m7GMP onto 5"-diphosphate RNA to yield capped RNA.	S-Adenosylmethionine	116-119	SH2 domain containing 3A	Homo sapiens	196-200
32389809-1	2020	BACKGROUND & AIM: Abundantly expressed in the metabolically active cells including hepatocytes, N-nicotinamide methyltransferase (NNMT) catalyzes S-adenosylmethionine (SAM)-dependent methylation/degradation of nicotinamide, the predominant precursor for intracellular nicotinamide adenine dinucleotide (NAD+) regeneration via the salvage pathway.	S-Adenosylmethionine	146-166	nicotinamide N-methyltransferase	Mus musculus	96-128
32389809-1	2020	BACKGROUND & AIM: Abundantly expressed in the metabolically active cells including hepatocytes, N-nicotinamide methyltransferase (NNMT) catalyzes S-adenosylmethionine (SAM)-dependent methylation/degradation of nicotinamide, the predominant precursor for intracellular nicotinamide adenine dinucleotide (NAD+) regeneration via the salvage pathway.	S-Adenosylmethionine	146-166	nicotinamide N-methyltransferase	Mus musculus	130-134
32389809-1	2020	BACKGROUND & AIM: Abundantly expressed in the metabolically active cells including hepatocytes, N-nicotinamide methyltransferase (NNMT) catalyzes S-adenosylmethionine (SAM)-dependent methylation/degradation of nicotinamide, the predominant precursor for intracellular nicotinamide adenine dinucleotide (NAD+) regeneration via the salvage pathway.	S-Adenosylmethionine	168-171	nicotinamide N-methyltransferase	Mus musculus	96-128
32389809-1	2020	BACKGROUND & AIM: Abundantly expressed in the metabolically active cells including hepatocytes, N-nicotinamide methyltransferase (NNMT) catalyzes S-adenosylmethionine (SAM)-dependent methylation/degradation of nicotinamide, the predominant precursor for intracellular nicotinamide adenine dinucleotide (NAD+) regeneration via the salvage pathway.	S-Adenosylmethionine	168-171	nicotinamide N-methyltransferase	Mus musculus	130-134
32855526-4	2020	Mechanistically, DNMT1 promotes ERRalpha stability which in turn couples DNMT1 transcription with that of the methionine cycle and S-adenosylmethionine synthesis to drive DNA methylation.	S-Adenosylmethionine	131-151	DNA methyltransferase (cytosine-5) 1	Mus musculus	17-22
32855526-4	2020	Mechanistically, DNMT1 promotes ERRalpha stability which in turn couples DNMT1 transcription with that of the methionine cycle and S-adenosylmethionine synthesis to drive DNA methylation.	S-Adenosylmethionine	131-151	estrogen related receptor, alpha	Mus musculus	32-40
33214833-1	2020	Protein arginine methyltransferase 5 (PRMT5) is an enzyme that can symmetrically dimethylate arginine residues in histones and nonhistone proteins by using S-adenosyl methionine (SAM) as the methyl donating cofactor.	S-Adenosylmethionine	156-177	protein arginine methyltransferase 5	Homo sapiens	0-36
33214833-1	2020	Protein arginine methyltransferase 5 (PRMT5) is an enzyme that can symmetrically dimethylate arginine residues in histones and nonhistone proteins by using S-adenosyl methionine (SAM) as the methyl donating cofactor.	S-Adenosylmethionine	156-177	protein arginine methyltransferase 5	Homo sapiens	38-43
33214833-1	2020	Protein arginine methyltransferase 5 (PRMT5) is an enzyme that can symmetrically dimethylate arginine residues in histones and nonhistone proteins by using S-adenosyl methionine (SAM) as the methyl donating cofactor.	S-Adenosylmethionine	179-182	protein arginine methyltransferase 5	Homo sapiens	0-36
33214833-1	2020	Protein arginine methyltransferase 5 (PRMT5) is an enzyme that can symmetrically dimethylate arginine residues in histones and nonhistone proteins by using S-adenosyl methionine (SAM) as the methyl donating cofactor.	S-Adenosylmethionine	179-182	protein arginine methyltransferase 5	Homo sapiens	38-43
33214833-2	2020	We have designed a library of SAM analogues and discovered potent, cell-active, and selective spiro diamines as inhibitors of the enzymatic function of PRMT5.	S-Adenosylmethionine	30-33	protein arginine methyltransferase 5	Homo sapiens	152-157
33175851-1	2020	S-adenosyl methionine synthetase (SAMS) catalyzes the biosynthesis of S-adenosyl methionine (SAM), which serves as a universal methyl group donor for numerous biochemical reactions.	S-Adenosylmethionine	0-21	methionine adenosyltransferase 1A	Homo sapiens	34-38
33168819-0	2020	MiR-22, regulated by MeCP2, suppresses gastric cancer cell proliferation by inducing a deficiency in endogenous S-adenosylmethionine.	S-Adenosylmethionine	112-132	microRNA 22	Homo sapiens	0-6
33168819-0	2020	MiR-22, regulated by MeCP2, suppresses gastric cancer cell proliferation by inducing a deficiency in endogenous S-adenosylmethionine.	S-Adenosylmethionine	112-132	methyl-CpG binding protein 2	Homo sapiens	21-26
33168819-8	2020	Knockdown of MTHFD2 and MTHFR, two key enzymes in folate metabolism and methyl donor SAM production, significantly suppressed GC cell proliferation.	S-Adenosylmethionine	85-88	methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase	Homo sapiens	13-19
33168819-8	2020	Knockdown of MTHFD2 and MTHFR, two key enzymes in folate metabolism and methyl donor SAM production, significantly suppressed GC cell proliferation.	S-Adenosylmethionine	85-88	methylenetetrahydrofolate reductase	Homo sapiens	24-29
33170152-0	2020	S-adenosylmethionine administration inhibits levodopa-induced vascular endothelial growth factor-A expression.	S-Adenosylmethionine	0-20	vascular endothelial growth factor A	Homo sapiens	62-98
33170152-2	2020	RESULTS: S-adenosylmethionine and levodopa had opposite effects on the protein stability of vascular endothelial growth factor-A.	S-Adenosylmethionine	9-29	vascular endothelial growth factor A	Homo sapiens	92-128
33170152-5	2020	S-adenosylmethionine resulted in G1/S phase arrest, with decreased cyclin dependent kinase 4/6 and increased p16, a specific cyclin dependent kinase inhibitor.	S-Adenosylmethionine	0-20	cyclin dependent kinase 4	Homo sapiens	67-94
33170152-5	2020	S-adenosylmethionine resulted in G1/S phase arrest, with decreased cyclin dependent kinase 4/6 and increased p16, a specific cyclin dependent kinase inhibitor.	S-Adenosylmethionine	0-20	cyclin dependent kinase inhibitor 2A	Homo sapiens	109-112
33170152-7	2020	S-adenosylmethionine could be fitted into the predicted docking pocket in the crystal structure of vascular endothelial growth factor-A, enhancing its acetylation level and reducing half-life.	S-Adenosylmethionine	0-20	vascular endothelial growth factor A	Homo sapiens	99-135
33170152-8	2020	CONCLUSIONS: These observations suggested that methyl donor S-adenosylmethionine could act as a potential agent against vascular endothelial growth factor-A-related diseases induced by levodopa treatment.	S-Adenosylmethionine	60-80	vascular endothelial growth factor A	Homo sapiens	120-156
33170152-9	2020	METHODS: We performed in vitro cytological analyses to assess whether S-adenosylmethionine intake could influence levodopa-induced vascular endothelial growth factor-A expression in human umbilical vein endothelial cells.	S-Adenosylmethionine	70-90	vascular endothelial growth factor A	Homo sapiens	131-167
32738342-11	2020	This study provided evidences for the effect of curcumin on the expression of MAT2B, an enzyme for the biosynthesis of methyl donor S-adenosylmethionine, in HSCs and demonstrated the function significance of curcumin-induced downregulation of MAT2B in curcumin inhibition of liver fibrosis.	S-Adenosylmethionine	132-152	methionine adenosyltransferase II, beta	Mus musculus	78-83
33125487-4	2020	Carboxyl-terminal methylation is catalyzed by Leucine carboxyl methyltransferase-1 (LCMT1) that utilizes S-adenosyl-methionine (SAM) as the methyl donor and removed by protein phosphatase methylesterase 1 (PME1).	S-Adenosylmethionine	105-126	leucine carboxyl methyltransferase 1	Homo sapiens	46-82
33125487-4	2020	Carboxyl-terminal methylation is catalyzed by Leucine carboxyl methyltransferase-1 (LCMT1) that utilizes S-adenosyl-methionine (SAM) as the methyl donor and removed by protein phosphatase methylesterase 1 (PME1).	S-Adenosylmethionine	105-126	leucine carboxyl methyltransferase 1	Homo sapiens	84-89
33125487-4	2020	Carboxyl-terminal methylation is catalyzed by Leucine carboxyl methyltransferase-1 (LCMT1) that utilizes S-adenosyl-methionine (SAM) as the methyl donor and removed by protein phosphatase methylesterase 1 (PME1).	S-Adenosylmethionine	105-126	protein phosphatase methylesterase 1	Homo sapiens	176-204
33125487-4	2020	Carboxyl-terminal methylation is catalyzed by Leucine carboxyl methyltransferase-1 (LCMT1) that utilizes S-adenosyl-methionine (SAM) as the methyl donor and removed by protein phosphatase methylesterase 1 (PME1).	S-Adenosylmethionine	105-126	protein phosphatase methylesterase 1	Homo sapiens	206-210
33125487-4	2020	Carboxyl-terminal methylation is catalyzed by Leucine carboxyl methyltransferase-1 (LCMT1) that utilizes S-adenosyl-methionine (SAM) as the methyl donor and removed by protein phosphatase methylesterase 1 (PME1).	S-Adenosylmethionine	128-131	leucine carboxyl methyltransferase 1	Homo sapiens	46-82
33125487-4	2020	Carboxyl-terminal methylation is catalyzed by Leucine carboxyl methyltransferase-1 (LCMT1) that utilizes S-adenosyl-methionine (SAM) as the methyl donor and removed by protein phosphatase methylesterase 1 (PME1).	S-Adenosylmethionine	128-131	leucine carboxyl methyltransferase 1	Homo sapiens	84-89
33125487-4	2020	Carboxyl-terminal methylation is catalyzed by Leucine carboxyl methyltransferase-1 (LCMT1) that utilizes S-adenosyl-methionine (SAM) as the methyl donor and removed by protein phosphatase methylesterase 1 (PME1).	S-Adenosylmethionine	128-131	protein phosphatase methylesterase 1	Homo sapiens	176-204
33125487-4	2020	Carboxyl-terminal methylation is catalyzed by Leucine carboxyl methyltransferase-1 (LCMT1) that utilizes S-adenosyl-methionine (SAM) as the methyl donor and removed by protein phosphatase methylesterase 1 (PME1).	S-Adenosylmethionine	128-131	protein phosphatase methylesterase 1	Homo sapiens	206-210
32492152-1	2020	Human catechol-O-methyltransferase (COMT), a key enzyme related to neurotransmitter metabolism, catalyzes a methyl transfer from S-adenosylmethionine (SAM) to catechol.	S-Adenosylmethionine	129-149	catechol-O-methyltransferase	Homo sapiens	6-34
32492152-1	2020	Human catechol-O-methyltransferase (COMT), a key enzyme related to neurotransmitter metabolism, catalyzes a methyl transfer from S-adenosylmethionine (SAM) to catechol.	S-Adenosylmethionine	129-149	catechol-O-methyltransferase	Homo sapiens	36-40
32492152-1	2020	Human catechol-O-methyltransferase (COMT), a key enzyme related to neurotransmitter metabolism, catalyzes a methyl transfer from S-adenosylmethionine (SAM) to catechol.	S-Adenosylmethionine	151-154	catechol-O-methyltransferase	Homo sapiens	6-34
32492152-1	2020	Human catechol-O-methyltransferase (COMT), a key enzyme related to neurotransmitter metabolism, catalyzes a methyl transfer from S-adenosylmethionine (SAM) to catechol.	S-Adenosylmethionine	151-154	catechol-O-methyltransferase	Homo sapiens	36-40
33000151-2	2020	The further metabolism of Hcy by the transsulfuration pathway is facilitated by activation of cystathionine beta-synthase (CBS) by S-adenosylmethionine (SAM) as well as the relatively high KM of CBS for Hcy.	S-Adenosylmethionine	131-151	cystathionine beta-synthase	Homo sapiens	94-121
33000151-2	2020	The further metabolism of Hcy by the transsulfuration pathway is facilitated by activation of cystathionine beta-synthase (CBS) by S-adenosylmethionine (SAM) as well as the relatively high KM of CBS for Hcy.	S-Adenosylmethionine	131-151	cystathionine beta-synthase	Homo sapiens	123-126
33000151-2	2020	The further metabolism of Hcy by the transsulfuration pathway is facilitated by activation of cystathionine beta-synthase (CBS) by S-adenosylmethionine (SAM) as well as the relatively high KM of CBS for Hcy.	S-Adenosylmethionine	153-156	cystathionine beta-synthase	Homo sapiens	94-121
33000151-2	2020	The further metabolism of Hcy by the transsulfuration pathway is facilitated by activation of cystathionine beta-synthase (CBS) by S-adenosylmethionine (SAM) as well as the relatively high KM of CBS for Hcy.	S-Adenosylmethionine	153-156	cystathionine beta-synthase	Homo sapiens	123-126
32994211-3	2020	We determined the structures for nsp16-nsp10 heterodimers bound to the methyl donor S-adenosylmethionine (SAM), the reaction product S-adenosylhomocysteine (SAH), or the SAH analog sinefungin (SFG).	S-Adenosylmethionine	106-109	ORF1a polyprotein;ORF1ab polyprotein	Severe acute respiratory syndrome coronavirus 2	39-44
32850834-7	2020	As the mechanism of methionine sensing on mTORC1, SAMTOR was identified as a sensor of S-adenosyl methionine (SAM), a metabolite of methionine, in the cytoplasm.	S-Adenosylmethionine	87-108	CREB regulated transcription coactivator 1	Mus musculus	42-48
32155663-6	2020	Metabolomics showed a decrease in glycolysis and tricarboxylic acid cycle metabolites, and inhibited the formation of creatine and phosphocreatine by the reaction of S-adenosylmethionine (SAM) with amino acids mediated by demethyladenosine transferase 1, mitochondrial (TFB1M) and reduced energy storage substances.	S-Adenosylmethionine	166-186	transcription factor B1, mitochondrial	Homo sapiens	270-275
32787210-1	2020	A unique member of the family of cobalamin (Cbl)-dependent radical S-adenosylmethionine (SAM) enzymes, OxsB, catalyzes the ring constriction of deoxyadenosine triphosphate (dATP) to the base oxetane aldehyde phosphate, a crucial precursor for oxetanocin A (OXT-A), which is an antitumor, antiviral, and antibacterial compound.	S-Adenosylmethionine	67-87	oxytocin/neurophysin I prepropeptide	Homo sapiens	257-260
32787210-1	2020	A unique member of the family of cobalamin (Cbl)-dependent radical S-adenosylmethionine (SAM) enzymes, OxsB, catalyzes the ring constriction of deoxyadenosine triphosphate (dATP) to the base oxetane aldehyde phosphate, a crucial precursor for oxetanocin A (OXT-A), which is an antitumor, antiviral, and antibacterial compound.	S-Adenosylmethionine	89-92	oxytocin/neurophysin I prepropeptide	Homo sapiens	257-260
32983966-8	2020	Indeed, SAM+anti-PD-1 reversed the aberrant expression of some known melanoma genes.	S-Adenosylmethionine	8-12	programmed cell death 1	Mus musculus	17-21
32622979-3	2020	Nicotinamide N-methyltransferase (NNMT) is a major metabolic enzyme involved in epigenetic regulation through catalysis of methyl transfer from the cofactor S-adenosyl-L-methionine onto nicotinamide and other pyridines.	S-Adenosylmethionine	157-180	nicotinamide N-methyltransferase	Homo sapiens	0-32
32622979-3	2020	Nicotinamide N-methyltransferase (NNMT) is a major metabolic enzyme involved in epigenetic regulation through catalysis of methyl transfer from the cofactor S-adenosyl-L-methionine onto nicotinamide and other pyridines.	S-Adenosylmethionine	157-180	nicotinamide N-methyltransferase	Homo sapiens	34-38
32371093-9	2020	Genetic and pharmacological Mafg inhibition by liver delivery of siRNA antisense or S-adenosylmethionine effectively rescued from damage caused by ANIT/OCA.	S-Adenosylmethionine	84-104	MAF bZIP transcription factor G	Rattus norvegicus	28-32
32384389-6	2020	In accordance, exercise triggered hypermethylation of alpha1c and beta1 gene in SHR, with concomitant decreasing TET1, increasing DNMT1 and DNMT3b expression in mesenteric arteries, as well as altering peripheral alpha-KG and S-adenosylmethionine/ S-adenosylhomocysteine ratio.	S-Adenosylmethionine	226-246	UDP glucuronosyltransferase family 1 member A6	Rattus norvegicus	54-71
32737159-9	2020	S-adenosylmethionine, the methyl donor of many methylation reactions, including histones, is synthesized from methionine by S-adenosylmethionine synthase; inactivation of the sams-1 S-adenosylmethionine synthase also suppresses the drp-1 fission defect, suggesting that vitamin B12 regulates mitochondrial biogenesis and then affects mitochondrial fission via chromatin pathways.	S-Adenosylmethionine	0-20	Dynamin GTPase	Caenorhabditis elegans	232-237
32850834-7	2020	As the mechanism of methionine sensing on mTORC1, SAMTOR was identified as a sensor of S-adenosyl methionine (SAM), a metabolite of methionine, in the cytoplasm.	S-Adenosylmethionine	50-53	CREB regulated transcription coactivator 1	Mus musculus	42-48
32366675-6	2020	The other mTOR complex, mTORC2, regulates production of S-adenosylmethionine (SAM), an essential substrate for histone methylation.	S-Adenosylmethionine	56-76	mechanistic target of rapamycin kinase	Homo sapiens	10-14
32759981-3	2020	Either phosphorylation or substitution of the Y324 residue suppresses PRMT5 activity by preventing its binding with the methyl donor S-adenosyl-L-methionine.	S-Adenosylmethionine	133-156	protein arginine methyltransferase 5	Homo sapiens	70-75
32784836-7	2020	SAM-induced gamma-H2AX elevation could be associated with activated DNA repair pathway showing upregulated gene expression (e.g., HUS1).	S-Adenosylmethionine	0-3	HUS1 checkpoint clamp component	Homo sapiens	130-134
32944135-4	2020	Previously, four different modes of PRMT5 inhibition were known-competing (covalently or non-covalently) with the essential cofactor S-adenosyl methionine (SAM), blocking the substrate binding pocket, or blocking both simultaneously.	S-Adenosylmethionine	133-154	protein arginine methyltransferase 5	Homo sapiens	36-41
32944135-4	2020	Previously, four different modes of PRMT5 inhibition were known-competing (covalently or non-covalently) with the essential cofactor S-adenosyl methionine (SAM), blocking the substrate binding pocket, or blocking both simultaneously.	S-Adenosylmethionine	156-159	protein arginine methyltransferase 5	Homo sapiens	36-41
32366675-6	2020	The other mTOR complex, mTORC2, regulates production of S-adenosylmethionine (SAM), an essential substrate for histone methylation.	S-Adenosylmethionine	56-76	CREB regulated transcription coactivator 2	Mus musculus	24-30
32366675-6	2020	The other mTOR complex, mTORC2, regulates production of S-adenosylmethionine (SAM), an essential substrate for histone methylation.	S-Adenosylmethionine	78-81	mechanistic target of rapamycin kinase	Homo sapiens	10-14
32366675-6	2020	The other mTOR complex, mTORC2, regulates production of S-adenosylmethionine (SAM), an essential substrate for histone methylation.	S-Adenosylmethionine	78-81	CREB regulated transcription coactivator 2	Mus musculus	24-30
32559753-7	2020	We demonstrate flexible mTG-mediated assembly of a three-enzyme biosynthetic pathway that converts S-adenosylmethionine (SAM) to autoinducer-2 (AI-2), a bacterial signal molecule that mediates quorum sensing behavior.	S-Adenosylmethionine	99-119	protease, serine 3	Mus musculus	24-27
32559753-7	2020	We demonstrate flexible mTG-mediated assembly of a three-enzyme biosynthetic pathway that converts S-adenosylmethionine (SAM) to autoinducer-2 (AI-2), a bacterial signal molecule that mediates quorum sensing behavior.	S-Adenosylmethionine	121-124	protease, serine 3	Mus musculus	24-27
32691671-6	2021	Initially, we analyzed the flexibility of COMT and defined its main conformations in solution regarding the absence (system I) and presence of the S-adenosyl-L-methionine (SAM) cofactor (system II) through molecular dynamics (MD) simulations.	S-Adenosylmethionine	147-170	catechol-O-methyltransferase	Homo sapiens	42-46
32709886-3	2020	We report here the high-resolution structure of a ternary complex of SARS-CoV-2 nsp16 and nsp10 in the presence of cognate RNA substrate analogue and methyl donor, S-adenosyl methionine (SAM).	S-Adenosylmethionine	164-185	ORF1a polyprotein;ORF1ab polyprotein	Severe acute respiratory syndrome coronavirus 2	90-95
32709886-3	2020	We report here the high-resolution structure of a ternary complex of SARS-CoV-2 nsp16 and nsp10 in the presence of cognate RNA substrate analogue and methyl donor, S-adenosyl methionine (SAM).	S-Adenosylmethionine	187-190	ORF1a polyprotein;ORF1ab polyprotein	Severe acute respiratory syndrome coronavirus 2	90-95
32691671-6	2021	Initially, we analyzed the flexibility of COMT and defined its main conformations in solution regarding the absence (system I) and presence of the S-adenosyl-L-methionine (SAM) cofactor (system II) through molecular dynamics (MD) simulations.	S-Adenosylmethionine	172-175	catechol-O-methyltransferase	Homo sapiens	42-46
31959915-8	2020	In addition, we demonstrated that some SAM-dependent HCC-promoting genes could be regulated by LINC00662 by altering the methylation status of their promoters via the LINC00662-coupled axes of MAT1A/SAM and AHCY/SAH.	S-Adenosylmethionine	39-42	long intergenic non-protein coding RNA 662	Homo sapiens	95-104
32651404-2	2020	NNMT methylates nicotinamide to N1-methylnicotidamide (MNA-1) using S-adenosyl methionine.	S-Adenosylmethionine	68-89	nicotinamide N-methyltransferase	Homo sapiens	0-4
32673148-5	2021	Here, we investigated the structural dynamics of ZIKV NS5 MTase domain free and bound to Guanosine-5"-triphosphate (GTP) and S-Adenosyl-Lmethionine (SAM), to identify the molecular dynamics changes related to ligand binding and methyl transfer reaction.	S-Adenosylmethionine	149-152	Raf-1 proto-oncogene, serine/threonine kinase	Homo sapiens	54-57
31959915-8	2020	In addition, we demonstrated that some SAM-dependent HCC-promoting genes could be regulated by LINC00662 by altering the methylation status of their promoters via the LINC00662-coupled axes of MAT1A/SAM and AHCY/SAH.	S-Adenosylmethionine	39-42	long intergenic non-protein coding RNA 662	Homo sapiens	167-176
31959915-6	2020	Moreover, we determined that LINC00662 could lead to genome-wide hypomethylation and alter the genomic methylation profile by synchronously reducing the S-adenosylmethionine (SAM) level and enhancing the S-adenosylhomocysteine (SAH) level.	S-Adenosylmethionine	153-173	long intergenic non-protein coding RNA 662	Homo sapiens	29-38
31959915-6	2020	Moreover, we determined that LINC00662 could lead to genome-wide hypomethylation and alter the genomic methylation profile by synchronously reducing the S-adenosylmethionine (SAM) level and enhancing the S-adenosylhomocysteine (SAH) level.	S-Adenosylmethionine	175-178	long intergenic non-protein coding RNA 662	Homo sapiens	29-38
31959915-8	2020	In addition, we demonstrated that some SAM-dependent HCC-promoting genes could be regulated by LINC00662 by altering the methylation status of their promoters via the LINC00662-coupled axes of MAT1A/SAM and AHCY/SAH.	S-Adenosylmethionine	39-42	methionine adenosyltransferase 1A	Homo sapiens	193-198
31959915-7	2020	Mechanistically, LINC00662 was determined to regulate the key enzymes influencing SAM and SAH levels, namely, methionine adenosyltransferase 1A (MAT1A) and S-adenosylhomocysteine hydrolase (AHCY), by RNA-RNA and RNA-protein interactions.	S-Adenosylmethionine	82-85	long intergenic non-protein coding RNA 662	Homo sapiens	17-26
31959915-7	2020	Mechanistically, LINC00662 was determined to regulate the key enzymes influencing SAM and SAH levels, namely, methionine adenosyltransferase 1A (MAT1A) and S-adenosylhomocysteine hydrolase (AHCY), by RNA-RNA and RNA-protein interactions.	S-Adenosylmethionine	82-85	methionine adenosyltransferase 1A	Homo sapiens	110-143
31959915-8	2020	In addition, we demonstrated that some SAM-dependent HCC-promoting genes could be regulated by LINC00662 by altering the methylation status of their promoters via the LINC00662-coupled axes of MAT1A/SAM and AHCY/SAH.	S-Adenosylmethionine	39-42	adenosylhomocysteinase	Homo sapiens	207-211
31959915-7	2020	Mechanistically, LINC00662 was determined to regulate the key enzymes influencing SAM and SAH levels, namely, methionine adenosyltransferase 1A (MAT1A) and S-adenosylhomocysteine hydrolase (AHCY), by RNA-RNA and RNA-protein interactions.	S-Adenosylmethionine	82-85	methionine adenosyltransferase 1A	Homo sapiens	145-150
31959915-7	2020	Mechanistically, LINC00662 was determined to regulate the key enzymes influencing SAM and SAH levels, namely, methionine adenosyltransferase 1A (MAT1A) and S-adenosylhomocysteine hydrolase (AHCY), by RNA-RNA and RNA-protein interactions.	S-Adenosylmethionine	82-85	adenosylhomocysteinase	Homo sapiens	156-188
31959915-8	2020	In addition, we demonstrated that some SAM-dependent HCC-promoting genes could be regulated by LINC00662 by altering the methylation status of their promoters via the LINC00662-coupled axes of MAT1A/SAM and AHCY/SAH.	S-Adenosylmethionine	199-202	long intergenic non-protein coding RNA 662	Homo sapiens	95-104
31959915-7	2020	Mechanistically, LINC00662 was determined to regulate the key enzymes influencing SAM and SAH levels, namely, methionine adenosyltransferase 1A (MAT1A) and S-adenosylhomocysteine hydrolase (AHCY), by RNA-RNA and RNA-protein interactions.	S-Adenosylmethionine	82-85	adenosylhomocysteinase	Homo sapiens	190-194
31959915-8	2020	In addition, we demonstrated that some SAM-dependent HCC-promoting genes could be regulated by LINC00662 by altering the methylation status of their promoters via the LINC00662-coupled axes of MAT1A/SAM and AHCY/SAH.	S-Adenosylmethionine	199-202	long intergenic non-protein coding RNA 662	Homo sapiens	167-176
31959915-8	2020	In addition, we demonstrated that some SAM-dependent HCC-promoting genes could be regulated by LINC00662 by altering the methylation status of their promoters via the LINC00662-coupled axes of MAT1A/SAM and AHCY/SAH.	S-Adenosylmethionine	199-202	adenosylhomocysteinase	Homo sapiens	207-211
31857119-5	2020	Human CBS is a complex intracellular multimeric enzyme that relies on three cofactors (heme, pyridoxal-5"-phosphate and S-adenosylmethionine) for proper function.	S-Adenosylmethionine	120-140	cystathionine beta-synthase	Homo sapiens	6-9
32416059-7	2020	Inhibiting ALR and COX17 increases mitochondrial copper levels which in turn inhibit S-adenosylhomocysteine hydrolase (SAHH) and lower levels of S-adenosylmethionine (SAM), DNA methylation, and chromatin accessibility to lower LSC viability.	S-Adenosylmethionine	145-165	growth factor, augmenter of liver regeneration	Homo sapiens	11-14
32416059-7	2020	Inhibiting ALR and COX17 increases mitochondrial copper levels which in turn inhibit S-adenosylhomocysteine hydrolase (SAHH) and lower levels of S-adenosylmethionine (SAM), DNA methylation, and chromatin accessibility to lower LSC viability.	S-Adenosylmethionine	145-165	cytochrome c oxidase copper chaperone COX17	Homo sapiens	19-24
32416059-7	2020	Inhibiting ALR and COX17 increases mitochondrial copper levels which in turn inhibit S-adenosylhomocysteine hydrolase (SAHH) and lower levels of S-adenosylmethionine (SAM), DNA methylation, and chromatin accessibility to lower LSC viability.	S-Adenosylmethionine	167-170	growth factor, augmenter of liver regeneration	Homo sapiens	11-14
32416059-7	2020	Inhibiting ALR and COX17 increases mitochondrial copper levels which in turn inhibit S-adenosylhomocysteine hydrolase (SAHH) and lower levels of S-adenosylmethionine (SAM), DNA methylation, and chromatin accessibility to lower LSC viability.	S-Adenosylmethionine	167-170	cytochrome c oxidase copper chaperone COX17	Homo sapiens	19-24
31951306-0	2020	Mechanism of diol dehydration by a promiscuous radical-SAM enzyme homologue of the antiviral enzyme viperin (RSAD2).	S-Adenosylmethionine	55-58	radical S-adenosyl methionine domain containing 2	Homo sapiens	100-107
31951306-0	2020	Mechanism of diol dehydration by a promiscuous radical-SAM enzyme homologue of the antiviral enzyme viperin (RSAD2).	S-Adenosylmethionine	55-58	radical S-adenosyl methionine domain containing 2	Homo sapiens	109-114
31951306-3	2020	Here, using a combination of HPLC, high-resolution mass spectrometry, and NMR spectroscopy we demonstrate that a thermostable fungal radical S-adenosylmethionine (SAM) enzyme with similarity to the vertebrate antiviral enzyme viperin (RSAD2) can catalyze transformation of CTP, UTP, and 5-bromo-UTP to their 3"-deoxy-3",4"-didehydro analogues.	S-Adenosylmethionine	141-161	radical S-adenosyl methionine domain containing 2	Homo sapiens	226-233
31951306-3	2020	Here, using a combination of HPLC, high-resolution mass spectrometry, and NMR spectroscopy we demonstrate that a thermostable fungal radical S-adenosylmethionine (SAM) enzyme with similarity to the vertebrate antiviral enzyme viperin (RSAD2) can catalyze transformation of CTP, UTP, and 5-bromo-UTP to their 3"-deoxy-3",4"-didehydro analogues.	S-Adenosylmethionine	141-161	radical S-adenosyl methionine domain containing 2	Homo sapiens	235-240
31951306-3	2020	Here, using a combination of HPLC, high-resolution mass spectrometry, and NMR spectroscopy we demonstrate that a thermostable fungal radical S-adenosylmethionine (SAM) enzyme with similarity to the vertebrate antiviral enzyme viperin (RSAD2) can catalyze transformation of CTP, UTP, and 5-bromo-UTP to their 3"-deoxy-3",4"-didehydro analogues.	S-Adenosylmethionine	163-166	radical S-adenosyl methionine domain containing 2	Homo sapiens	226-233
31951306-3	2020	Here, using a combination of HPLC, high-resolution mass spectrometry, and NMR spectroscopy we demonstrate that a thermostable fungal radical S-adenosylmethionine (SAM) enzyme with similarity to the vertebrate antiviral enzyme viperin (RSAD2) can catalyze transformation of CTP, UTP, and 5-bromo-UTP to their 3"-deoxy-3",4"-didehydro analogues.	S-Adenosylmethionine	163-166	radical S-adenosyl methionine domain containing 2	Homo sapiens	235-240
32371482-1	2020	Human catechol O-methyltransferase (COMT) has emerged as a model for understanding enzyme-catalyzed methyl transfer from S-adenosylmethionine (AdoMet) to small-molecule catecholate acceptors.	S-Adenosylmethionine	121-141	catechol-O-methyltransferase	Homo sapiens	6-34
32334045-2	2020	Riboflavin (FAD) is a cofactor for methylenetetrahydrofolate reductase (MTHFR), a critical enzyme in folate recycling, which generates methyl groups for homocysteine remethylation to methionine, the pre-cursor to the universal methyl donor S-adenosylmethionine (SAM).	S-Adenosylmethionine	240-260	methylenetetrahydrofolate reductase	Homo sapiens	35-70
32334045-2	2020	Riboflavin (FAD) is a cofactor for methylenetetrahydrofolate reductase (MTHFR), a critical enzyme in folate recycling, which generates methyl groups for homocysteine remethylation to methionine, the pre-cursor to the universal methyl donor S-adenosylmethionine (SAM).	S-Adenosylmethionine	240-260	methylenetetrahydrofolate reductase	Homo sapiens	72-77
32334045-2	2020	Riboflavin (FAD) is a cofactor for methylenetetrahydrofolate reductase (MTHFR), a critical enzyme in folate recycling, which generates methyl groups for homocysteine remethylation to methionine, the pre-cursor to the universal methyl donor S-adenosylmethionine (SAM).	S-Adenosylmethionine	262-265	methylenetetrahydrofolate reductase	Homo sapiens	35-70
32334045-2	2020	Riboflavin (FAD) is a cofactor for methylenetetrahydrofolate reductase (MTHFR), a critical enzyme in folate recycling, which generates methyl groups for homocysteine remethylation to methionine, the pre-cursor to the universal methyl donor S-adenosylmethionine (SAM).	S-Adenosylmethionine	262-265	methylenetetrahydrofolate reductase	Homo sapiens	72-77
32448097-3	2022	MTHFR plays a critical role in the synthesis of S-adenosylmethionine (SAM), a global methyl donor.	S-Adenosylmethionine	48-68	methylenetetrahydrofolate reductase	Mus musculus	0-5
32448097-3	2022	MTHFR plays a critical role in the synthesis of S-adenosylmethionine (SAM), a global methyl donor.	S-Adenosylmethionine	70-73	methylenetetrahydrofolate reductase	Mus musculus	0-5
32456310-2	2020	S-adenosylmethionine (SAM) is the universal methyl donor in human cells and is synthesized by methionine adenosyltransferase 2A (MAT2A), which is deregulated in different cancer types.	S-Adenosylmethionine	0-20	methionine adenosyltransferase 2A	Homo sapiens	94-127
32456310-2	2020	S-adenosylmethionine (SAM) is the universal methyl donor in human cells and is synthesized by methionine adenosyltransferase 2A (MAT2A), which is deregulated in different cancer types.	S-Adenosylmethionine	0-20	methionine adenosyltransferase 2A	Homo sapiens	129-134
32456310-2	2020	S-adenosylmethionine (SAM) is the universal methyl donor in human cells and is synthesized by methionine adenosyltransferase 2A (MAT2A), which is deregulated in different cancer types.	S-Adenosylmethionine	22-25	methionine adenosyltransferase 2A	Homo sapiens	94-127
32456310-2	2020	S-adenosylmethionine (SAM) is the universal methyl donor in human cells and is synthesized by methionine adenosyltransferase 2A (MAT2A), which is deregulated in different cancer types.	S-Adenosylmethionine	22-25	methionine adenosyltransferase 2A	Homo sapiens	129-134
32371482-1	2020	Human catechol O-methyltransferase (COMT) has emerged as a model for understanding enzyme-catalyzed methyl transfer from S-adenosylmethionine (AdoMet) to small-molecule catecholate acceptors.	S-Adenosylmethionine	121-141	catechol-O-methyltransferase	Homo sapiens	36-40
32551023-3	2020	Herein, we report the design, synthesis, and evaluation of an S-adenosylmethionine-based focused chemical library which led to the discovery of potent small-molecule inhibitors directly targeting the MLL SET domain.	S-Adenosylmethionine	62-82	lysine methyltransferase 2A	Homo sapiens	200-203
32429436-2	2020	Recently, it was reported that, in bacteria, a cyclopropane-containing NPA 1-aminocyclopropanecarboxylic acid (ACC) is produced from the L-methionine moiety of S-adenosyl-L-methionine (SAM) by non-canonical ACC-forming enzymes.	S-Adenosylmethionine	160-183	URB1 ribosome biogenesis homolog	Homo sapiens	71-76
32429436-2	2020	Recently, it was reported that, in bacteria, a cyclopropane-containing NPA 1-aminocyclopropanecarboxylic acid (ACC) is produced from the L-methionine moiety of S-adenosyl-L-methionine (SAM) by non-canonical ACC-forming enzymes.	S-Adenosylmethionine	185-188	URB1 ribosome biogenesis homolog	Homo sapiens	71-76
32061099-0	2020	Viperin, through its radical-SAM activity, depletes cellular nucleotide pools and interferes with mitochondrial metabolism to inhibit viral replication.	S-Adenosylmethionine	29-32	radical S-adenosyl methionine domain containing 2	Homo sapiens	0-7
32159918-1	2020	The RNA methylase METTL3 catalyzes the transfer of a methyl group from the cofactor S-adenosyl-L-methionine (SAM) to the N6 atom of adenine.	S-Adenosylmethionine	84-107	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	18-24
32159918-1	2020	The RNA methylase METTL3 catalyzes the transfer of a methyl group from the cofactor S-adenosyl-L-methionine (SAM) to the N6 atom of adenine.	S-Adenosylmethionine	109-112	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	18-24
32187373-3	2020	Time-course expression measurements captured dynamic network-level adaptation of cells to DNMT3B1-induced DNA methylation stress and showed that coordinately modulating the availability of S-adenosyl methionine (SAM), the essential metabolite for DNMT-catalyzed methylation, is an evolutionarily conserved epigenetic stress response, also implicated in several human diseases.	S-Adenosylmethionine	189-210	DNA methyltransferase 1	Homo sapiens	90-94
32187373-3	2020	Time-course expression measurements captured dynamic network-level adaptation of cells to DNMT3B1-induced DNA methylation stress and showed that coordinately modulating the availability of S-adenosyl methionine (SAM), the essential metabolite for DNMT-catalyzed methylation, is an evolutionarily conserved epigenetic stress response, also implicated in several human diseases.	S-Adenosylmethionine	212-215	DNA methyltransferase 1	Homo sapiens	90-94
32566619-0	2020	FOXP3 promotes colorectal carcinoma liver metastases by evaluating MMP9 expression via regulating S-adenosylmethionine metabolism.	S-Adenosylmethionine	98-118	forkhead box P3	Homo sapiens	0-5
32566619-0	2020	FOXP3 promotes colorectal carcinoma liver metastases by evaluating MMP9 expression via regulating S-adenosylmethionine metabolism.	S-Adenosylmethionine	98-118	matrix metallopeptidase 9	Homo sapiens	67-71
32061099-1	2020	Viperin (RSAD2) is an antiviral radical S-adenosylmethionine (SAM) enzyme highly expressed in different cell types upon viral infection.	S-Adenosylmethionine	62-65	radical S-adenosyl methionine domain containing 2	Homo sapiens	9-14
32061099-2	2020	Recently, it has been reported that the radical-SAM activity of viperin transforms cytidine triphosphate (CTP) to its analogue 3"-deoxy-3",4"-didehydro-CTP (ddhCTP).	S-Adenosylmethionine	48-51	radical S-adenosyl methionine domain containing 2	Homo sapiens	64-71
32061099-5	2020	Our analysis is consistent with a unifying view of the antiviral and radical-SAM activities of viperin.	S-Adenosylmethionine	77-80	radical S-adenosyl methionine domain containing 2	Homo sapiens	95-102
32061099-1	2020	Viperin (RSAD2) is an antiviral radical S-adenosylmethionine (SAM) enzyme highly expressed in different cell types upon viral infection.	S-Adenosylmethionine	40-60	radical S-adenosyl methionine domain containing 2	Homo sapiens	0-7
32061099-1	2020	Viperin (RSAD2) is an antiviral radical S-adenosylmethionine (SAM) enzyme highly expressed in different cell types upon viral infection.	S-Adenosylmethionine	40-60	radical S-adenosyl methionine domain containing 2	Homo sapiens	9-14
32061099-1	2020	Viperin (RSAD2) is an antiviral radical S-adenosylmethionine (SAM) enzyme highly expressed in different cell types upon viral infection.	S-Adenosylmethionine	62-65	radical S-adenosyl methionine domain containing 2	Homo sapiens	0-7
32419814-5	2020	The results presented here show that S-adenosyl-l-methionine (SAM), an allosteric activator of cystathionine-beta-synthetase (CBS), may reverse the therapeutic effect of EA.	S-Adenosylmethionine	62-65	cystathionine beta-synthase	Homo sapiens	126-129
32218733-4	2020	During the synthesis of spermidine and spermine, an amino-propyl group is provided by decarboxylated S-adenosylmethionine, and the latter is generated from S-adenosylmethionine by AdoMetDC (AdoMet decarboxylase).	S-Adenosylmethionine	101-121	adenosylmethionine decarboxylase 1	Homo sapiens	190-210
32145700-5	2020	Additionally, the increased levels of S-adenosylmethionine (SAM) in renal tubular cells, which are associated with the reduced expression of glycine N-methyltransferase (Gnmt) and non-restricted Met intake, contributes to the activation of mechanistic target of rapamycin complex 1 (mTORC1) and impaired autophagy, in diabetic kidney.	S-Adenosylmethionine	60-63	glycine N-methyltransferase	Rattus norvegicus	141-168
32145700-5	2020	Additionally, the increased levels of S-adenosylmethionine (SAM) in renal tubular cells, which are associated with the reduced expression of glycine N-methyltransferase (Gnmt) and non-restricted Met intake, contributes to the activation of mechanistic target of rapamycin complex 1 (mTORC1) and impaired autophagy, in diabetic kidney.	S-Adenosylmethionine	60-63	glycine N-methyltransferase	Rattus norvegicus	170-174
32145700-5	2020	Additionally, the increased levels of S-adenosylmethionine (SAM) in renal tubular cells, which are associated with the reduced expression of glycine N-methyltransferase (Gnmt) and non-restricted Met intake, contributes to the activation of mechanistic target of rapamycin complex 1 (mTORC1) and impaired autophagy, in diabetic kidney.	S-Adenosylmethionine	60-63	MET proto-oncogene, receptor tyrosine kinase	Rattus norvegicus	195-198
32145700-5	2020	Additionally, the increased levels of S-adenosylmethionine (SAM) in renal tubular cells, which are associated with the reduced expression of glycine N-methyltransferase (Gnmt) and non-restricted Met intake, contributes to the activation of mechanistic target of rapamycin complex 1 (mTORC1) and impaired autophagy, in diabetic kidney.	S-Adenosylmethionine	60-63	CREB regulated transcription coactivator 1	Mus musculus	283-289
32193337-7	2020	Blocking glycosylation of AHCY decreases the ratio of S-adenosylmethionine versus S-adenosylhomocysteine (SAM/SAH), reduces the level of H3K4me3, and poises mESC for differentiation.	S-Adenosylmethionine	54-74	S-adenosylhomocysteine hydrolase	Mus musculus	26-30
32244625-2	2020	Our investigation identifies and functionally characterizes the orthologue of S-adenosylmethionine (SAM) binding methyltransferase enzyme, disruptor of telomeric silencing 1-like (DOT1L) in Ornithodoros moubata (OmDOT1L), a soft tick vector for the relapsing fever pathogen Borrelia duttonii and the African swine fever virus.	S-Adenosylmethionine	78-98	DOT1 like histone lysine methyltransferase	Homo sapiens	180-185
32244625-2	2020	Our investigation identifies and functionally characterizes the orthologue of S-adenosylmethionine (SAM) binding methyltransferase enzyme, disruptor of telomeric silencing 1-like (DOT1L) in Ornithodoros moubata (OmDOT1L), a soft tick vector for the relapsing fever pathogen Borrelia duttonii and the African swine fever virus.	S-Adenosylmethionine	100-103	DOT1 like histone lysine methyltransferase	Homo sapiens	180-185
32218733-4	2020	During the synthesis of spermidine and spermine, an amino-propyl group is provided by decarboxylated S-adenosylmethionine, and the latter is generated from S-adenosylmethionine by AdoMetDC (AdoMet decarboxylase).	S-Adenosylmethionine	156-176	adenosylmethionine decarboxylase 1	Homo sapiens	190-210
32195181-2	2020	ATTM is also an identified H2S donor and endogenous H2S facilitates VitB12-induced S-adenosylmethionine (SAM) generation, which have been confirmed in m6A methylation and lung cancer development.	S-Adenosylmethionine	83-103	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	151-154
31991084-8	2020	Second, we determined the methylation of arsenicals and the expression levels of the methylation enzyme As(III) S-adenosylmethionine (SAM) methyltransferase (AS3MT) in several types of brain cells.	S-Adenosylmethionine	104-132	arsenite methyltransferase	Homo sapiens	158-163
32195181-2	2020	ATTM is also an identified H2S donor and endogenous H2S facilitates VitB12-induced S-adenosylmethionine (SAM) generation, which have been confirmed in m6A methylation and lung cancer development.	S-Adenosylmethionine	105-108	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	151-154
32184941-10	2020	The comparator-controlled randomized study, which had a number of notable limitations, reported significant reductions in serum ALT and AST levels with AdoMet vs potassium magnesium aspartate within 4 wk, but not within2 wk.	S-Adenosylmethionine	152-158	solute carrier family 17 member 5	Homo sapiens	136-139
31004229-6	2020	Decarboxylated S-adenosylmethionine, converted from S-adenosylmethionine by S-adenosylmethionine decarboxylase, provides an aminopropyl group to synthesize spermine and spermidine and acts to inhibit DNMT activity.	S-Adenosylmethionine	15-35	DNA methyltransferase (cytosine-5) 1	Mus musculus	200-204
31917549-1	2020	Viperin is a radical S-adenosylmethionine (SAM) enzyme that inhibits viral replication by converting cytidine triphosphate (CTP) into 3"-deoxy-3",4"-didehydro-CTP and by additional undefined mechanisms operating through its N- and C-terminal domains.	S-Adenosylmethionine	21-41	radical S-adenosyl methionine domain containing 2	Homo sapiens	0-7
31917549-1	2020	Viperin is a radical S-adenosylmethionine (SAM) enzyme that inhibits viral replication by converting cytidine triphosphate (CTP) into 3"-deoxy-3",4"-didehydro-CTP and by additional undefined mechanisms operating through its N- and C-terminal domains.	S-Adenosylmethionine	43-46	radical S-adenosyl methionine domain containing 2	Homo sapiens	0-7
31004229-6	2020	Decarboxylated S-adenosylmethionine, converted from S-adenosylmethionine by S-adenosylmethionine decarboxylase, provides an aminopropyl group to synthesize spermine and spermidine and acts to inhibit DNMT activity.	S-Adenosylmethionine	52-72	DNA methyltransferase (cytosine-5) 1	Mus musculus	200-204
31004229-8	2020	In vitro studies demonstrated that spermine reversed changes induced by the inhibition of ornithine decarboxylase (e.g., increased decarboxylated S-adenosylmethionine, decreased DNA methyltransferase activity, increased aberrant DNA methylation), whose activity decreases with aging.	S-Adenosylmethionine	146-166	ornithine decarboxylase, structural 1	Mus musculus	90-113
31708229-8	2020	A detailed guide regarding inhibition of S-adenosyl-l-methionine, catalyzing the transfer of the methyl group by COMT is also represented.	S-Adenosylmethionine	41-64	catechol-O-methyltransferase	Homo sapiens	113-117
31971508-7	2020	Finally, we find that G418-induced miscoding alters gene expression with substantial effects on translation of histone genes, selenoprotein genes, and S-adenosylmethionine decarboxylase (AMD1).	S-Adenosylmethionine	151-171	adenosylmethionine decarboxylase 1	Homo sapiens	187-191
31657500-2	2020	Herein, it is demonstrated that reconstituted HpnH, a putative radical S-adenosyl-l-methionine (SAM) enzyme, commonly encoded in the hopanoid biosynthetic gene cluster, converts diploptene into adenosylhopane in the presence of SAM, flavodoxin, flavodoxin reductase, and NADPH.	S-Adenosylmethionine	96-99	2,4-dienoyl-CoA reductase 1	Homo sapiens	271-276
31869215-3	2020	HTS with a drug repositioning library revealed the importance of catechol-O-methyltransferase (COMT) and its substrates in controlling the SAM concentrations and histone methylation levels in colorectal tumor cells.	S-Adenosylmethionine	139-142	catechol-O-methyltransferase	Homo sapiens	65-93
31869215-3	2020	HTS with a drug repositioning library revealed the importance of catechol-O-methyltransferase (COMT) and its substrates in controlling the SAM concentrations and histone methylation levels in colorectal tumor cells.	S-Adenosylmethionine	139-142	catechol-O-methyltransferase	Homo sapiens	95-99
31552788-1	2020	S-adenosylmethionine (SAM), biosynthesis from methionine and ATP, is markedly decreased in hepatocellularular carcinoma (HCC) for a diminution in ATP levels, and the down regulation of the liver specific MAT1a enzyme.	S-Adenosylmethionine	0-20	methionine adenosyltransferase 1A	Homo sapiens	204-209
31552788-1	2020	S-adenosylmethionine (SAM), biosynthesis from methionine and ATP, is markedly decreased in hepatocellularular carcinoma (HCC) for a diminution in ATP levels, and the down regulation of the liver specific MAT1a enzyme.	S-Adenosylmethionine	22-25	methionine adenosyltransferase 1A	Homo sapiens	204-209
32378542-2	2020	All clinically approved COMT inhibitors bring a 5-substituted-3-nitrocatechol ring as a pharmacophore, and they bind to COMT with S-adenosylmethionine (SAM) and an Mg2+ ion to form a quaternary complex (COMT/SAM/Mg2+/inhibitor).	S-Adenosylmethionine	130-150	catechol-O-methyltransferase	Homo sapiens	24-28
32378542-2	2020	All clinically approved COMT inhibitors bring a 5-substituted-3-nitrocatechol ring as a pharmacophore, and they bind to COMT with S-adenosylmethionine (SAM) and an Mg2+ ion to form a quaternary complex (COMT/SAM/Mg2+/inhibitor).	S-Adenosylmethionine	130-150	catechol-O-methyltransferase	Homo sapiens	120-124
32378542-2	2020	All clinically approved COMT inhibitors bring a 5-substituted-3-nitrocatechol ring as a pharmacophore, and they bind to COMT with S-adenosylmethionine (SAM) and an Mg2+ ion to form a quaternary complex (COMT/SAM/Mg2+/inhibitor).	S-Adenosylmethionine	130-150	catechol-O-methyltransferase	Homo sapiens	120-124
32378542-2	2020	All clinically approved COMT inhibitors bring a 5-substituted-3-nitrocatechol ring as a pharmacophore, and they bind to COMT with S-adenosylmethionine (SAM) and an Mg2+ ion to form a quaternary complex (COMT/SAM/Mg2+/inhibitor).	S-Adenosylmethionine	152-155	catechol-O-methyltransferase	Homo sapiens	24-28
32378542-2	2020	All clinically approved COMT inhibitors bring a 5-substituted-3-nitrocatechol ring as a pharmacophore, and they bind to COMT with S-adenosylmethionine (SAM) and an Mg2+ ion to form a quaternary complex (COMT/SAM/Mg2+/inhibitor).	S-Adenosylmethionine	152-155	catechol-O-methyltransferase	Homo sapiens	120-124
32378542-2	2020	All clinically approved COMT inhibitors bring a 5-substituted-3-nitrocatechol ring as a pharmacophore, and they bind to COMT with S-adenosylmethionine (SAM) and an Mg2+ ion to form a quaternary complex (COMT/SAM/Mg2+/inhibitor).	S-Adenosylmethionine	152-155	catechol-O-methyltransferase	Homo sapiens	120-124
32378542-4	2020	Here, a new crystal structure of COMT complexed with nitecapone (5), SAM and Mg2+ is revealed.	S-Adenosylmethionine	69-72	catechol-O-methyltransferase	Homo sapiens	33-37
32378542-10	2020	This interaction seems to play a critical role in the affinity of the inhibitor and to stabilize the COMT/SAM/Mg2+/nitrocatechol inhibitor complex by fixing the flexible alpha2alpha3-loop.	S-Adenosylmethionine	106-109	catechol-O-methyltransferase	Homo sapiens	101-105
32597804-5	2020	Our previous in vivo study revealed that SAM administration attenuated oxidative stress induced by amyloid-beta (Abeta) through the enhancement of GSH.	S-Adenosylmethionine	41-44	amyloid beta (A4) precursor protein	Mus musculus	113-118
32925070-0	2020	S-Adenosylmethionine Rescues Cognitive Deficits in the rTg4510 Animal Model by Stabilizing Protein Phosphatase 2A and Reducing Phosphorylated Tau.	S-Adenosylmethionine	0-20	microtubule associated protein tau	Homo sapiens	142-145
32925070-11	2020	CONCLUSION: This study shows that supplementation with S-adenosylmethionine stabilizes the heterotrimeric form of PP2A resulting in an increase the enzymatic activity, a reduced level of pathological tau, and improved cognition.	S-Adenosylmethionine	55-75	protein phosphatase 2 (formerly 2A), catalytic subunit, alpha isoform	Mus musculus	114-118
32925070-11	2020	CONCLUSION: This study shows that supplementation with S-adenosylmethionine stabilizes the heterotrimeric form of PP2A resulting in an increase the enzymatic activity, a reduced level of pathological tau, and improved cognition.	S-Adenosylmethionine	55-75	microtubule associated protein tau	Homo sapiens	200-203
32014433-4	2019	Although glycolysis supplies S-adenosylmethionine for histone methyltransferase Set1 to catalyze H3K4me3, glucose induces H3K4me3 primarily by inhibiting histone demethylase Jhd2-catalyzed H3K4 demethylation.	S-Adenosylmethionine	29-49	histone methyltransferase SET1	Saccharomyces cerevisiae S288C	80-84
33569544-6	2020	SHMT2 catalyzes the conversion of serine to glycine and produces an activated one-carbon unit that can be used to support S-adenosyl methionine synthesis.	S-Adenosylmethionine	122-143	serine hydroxymethyltransferase 2	Homo sapiens	0-5
32046373-1	2020	The methionine adenosyltransferase 2beta gene (Mat2b) encodes for the regulatory subunit of methionine adenosyltransferase (MAT), which catalyzes the biosynthesis of S-adenosylmethionine.	S-Adenosylmethionine	166-186	methionine adenosyltransferase II, beta	Mus musculus	47-52
31821864-6	2020	Next, by employing a juvenile hormone acid O-methyltransferase (DmJHAMT) from Drosophila melanogaster and S-adenosylmethionine (SAM) as a methyl donor, FFAs were converted into corresponding FAMEs.	S-Adenosylmethionine	106-126	juvenile hormone acid methyltransferase	Drosophila melanogaster	64-71
31821864-6	2020	Next, by employing a juvenile hormone acid O-methyltransferase (DmJHAMT) from Drosophila melanogaster and S-adenosylmethionine (SAM) as a methyl donor, FFAs were converted into corresponding FAMEs.	S-Adenosylmethionine	128-131	juvenile hormone acid methyltransferase	Drosophila melanogaster	64-71
31821864-9	2020	Quantification of key proteins and metabolites, together with constructs over-expressing SAM synthetase (MetK), indicated that "UcFatB1, MetK, and DmJHAMT were the main factors limiting pathway flux.	S-Adenosylmethionine	89-92	juvenile hormone acid methyltransferase	Drosophila melanogaster	147-154
31968288-2	2020	Regulation of MTHFR is pivotal for maintaining the cellular concentrations of methionine and SAM (S-adenosyl methionine) which are essential for the synthesis of nucleotides and amino acids, respectively.	S-Adenosylmethionine	93-96	methylenetetrahydrofolate reductase	Homo sapiens	14-19
31968288-2	2020	Regulation of MTHFR is pivotal for maintaining the cellular concentrations of methionine and SAM (S-adenosyl methionine) which are essential for the synthesis of nucleotides and amino acids, respectively.	S-Adenosylmethionine	98-119	methylenetetrahydrofolate reductase	Homo sapiens	14-19
31539805-7	2020	S-adenosylmethionine administration enhanced Nos2 mRNA expression and cystathionine beta-synthase nitration and triggered homocysteine accumulation in acute pancreatitis.	S-Adenosylmethionine	0-20	nitric oxide synthase 2, inducible	Mus musculus	45-49
31539805-7	2020	S-adenosylmethionine administration enhanced Nos2 mRNA expression and cystathionine beta-synthase nitration and triggered homocysteine accumulation in acute pancreatitis.	S-Adenosylmethionine	0-20	cystathionine beta-synthase	Mus musculus	70-97
31539805-8	2020	Furthermore, S-adenosylmethionine administration promoted enrichment of the euchromatin marker H3K4me3 in the promoters of Tnf-alpha, Il-6, and Nos2 and enhanced the mRNA up-regulation of these genes.	S-Adenosylmethionine	13-33	tumor necrosis factor	Mus musculus	123-132
31539805-8	2020	Furthermore, S-adenosylmethionine administration promoted enrichment of the euchromatin marker H3K4me3 in the promoters of Tnf-alpha, Il-6, and Nos2 and enhanced the mRNA up-regulation of these genes.	S-Adenosylmethionine	13-33	interleukin 6	Mus musculus	134-138
31539805-8	2020	Furthermore, S-adenosylmethionine administration promoted enrichment of the euchromatin marker H3K4me3 in the promoters of Tnf-alpha, Il-6, and Nos2 and enhanced the mRNA up-regulation of these genes.	S-Adenosylmethionine	13-33	nitric oxide synthase 2, inducible	Mus musculus	144-148
31539805-10	2020	In conclusion, tyrosine-nitration of cystathionine beta-synthase blockades the trans-sulfuration pathway in acute pancreatitis promoting homocysteine accumulation upon S-adenosylmethionine treatment.	S-Adenosylmethionine	168-188	cystathionine beta-synthase	Mus musculus	37-64
31455609-1	2019	Mitochondrial RNase P Protein 3 (MRPP3), a protein-only RNase P (PRORP), is the nuclease component of the mtRNase P complex and requires a two-protein S-adenosyl-methionine (SAM)-dependent methyltransferase MRPP1/2 subcomplex to function.	S-Adenosylmethionine	151-172	protein only RNase P catalytic subunit	Homo sapiens	0-31
31848333-5	2019	MRK-740 binds in the substrate-binding pocket, with unusually extensive interactions with the cofactor S-adenosylmethionine (SAM), conferring SAM-dependent substrate-competitive inhibition.	S-Adenosylmethionine	103-123	mitogen-activated protein kinase kinase kinase 20	Homo sapiens	0-3
31848333-5	2019	MRK-740 binds in the substrate-binding pocket, with unusually extensive interactions with the cofactor S-adenosylmethionine (SAM), conferring SAM-dependent substrate-competitive inhibition.	S-Adenosylmethionine	125-128	mitogen-activated protein kinase kinase kinase 20	Homo sapiens	0-3
31848333-5	2019	MRK-740 binds in the substrate-binding pocket, with unusually extensive interactions with the cofactor S-adenosylmethionine (SAM), conferring SAM-dependent substrate-competitive inhibition.	S-Adenosylmethionine	142-145	mitogen-activated protein kinase kinase kinase 20	Homo sapiens	0-3
31848333-7	2019	The discovery of MRK-740 as a chemical probe for the PRDM subfamily of methyltransferases highlights the potential for exploiting SAM in targeting SAM-dependent methyltransferases.	S-Adenosylmethionine	130-133	mitogen-activated protein kinase kinase kinase 20	Homo sapiens	17-20
31848333-7	2019	The discovery of MRK-740 as a chemical probe for the PRDM subfamily of methyltransferases highlights the potential for exploiting SAM in targeting SAM-dependent methyltransferases.	S-Adenosylmethionine	147-150	mitogen-activated protein kinase kinase kinase 20	Homo sapiens	17-20
31724854-1	2019	Nicotinamide N-methyltransferase (NNMT) catalyzes the methyl transfer from the cofactor S-adenosylmethionine to nicotinamide and other pyridine-containing compounds.	S-Adenosylmethionine	88-108	nicotinamide N-methyltransferase	Homo sapiens	0-32
31724854-1	2019	Nicotinamide N-methyltransferase (NNMT) catalyzes the methyl transfer from the cofactor S-adenosylmethionine to nicotinamide and other pyridine-containing compounds.	S-Adenosylmethionine	88-108	nicotinamide N-methyltransferase	Homo sapiens	34-38
31077594-1	2019	Methionine adenosyltransferase alpha1 (MATalpha1, encoded by MAT1A) is responsible for hepatic biosynthesis of S-adenosyl methionine, the principal methyl donor.	S-Adenosylmethionine	111-132	methionine adenosyltransferase 1A	Homo sapiens	61-66
31455609-1	2019	Mitochondrial RNase P Protein 3 (MRPP3), a protein-only RNase P (PRORP), is the nuclease component of the mtRNase P complex and requires a two-protein S-adenosyl-methionine (SAM)-dependent methyltransferase MRPP1/2 subcomplex to function.	S-Adenosylmethionine	151-172	protein only RNase P catalytic subunit	Homo sapiens	33-38
31455609-1	2019	Mitochondrial RNase P Protein 3 (MRPP3), a protein-only RNase P (PRORP), is the nuclease component of the mtRNase P complex and requires a two-protein S-adenosyl-methionine (SAM)-dependent methyltransferase MRPP1/2 subcomplex to function.	S-Adenosylmethionine	151-172	protein only RNase P catalytic subunit	Homo sapiens	65-70
31455609-1	2019	Mitochondrial RNase P Protein 3 (MRPP3), a protein-only RNase P (PRORP), is the nuclease component of the mtRNase P complex and requires a two-protein S-adenosyl-methionine (SAM)-dependent methyltransferase MRPP1/2 subcomplex to function.	S-Adenosylmethionine	151-172	tRNA methyltransferase 10C, mitochondrial RNase P subunit	Homo sapiens	207-214
31455609-1	2019	Mitochondrial RNase P Protein 3 (MRPP3), a protein-only RNase P (PRORP), is the nuclease component of the mtRNase P complex and requires a two-protein S-adenosyl-methionine (SAM)-dependent methyltransferase MRPP1/2 subcomplex to function.	S-Adenosylmethionine	174-177	protein only RNase P catalytic subunit	Homo sapiens	0-31
31455609-1	2019	Mitochondrial RNase P Protein 3 (MRPP3), a protein-only RNase P (PRORP), is the nuclease component of the mtRNase P complex and requires a two-protein S-adenosyl-methionine (SAM)-dependent methyltransferase MRPP1/2 subcomplex to function.	S-Adenosylmethionine	174-177	protein only RNase P catalytic subunit	Homo sapiens	33-38
31455609-1	2019	Mitochondrial RNase P Protein 3 (MRPP3), a protein-only RNase P (PRORP), is the nuclease component of the mtRNase P complex and requires a two-protein S-adenosyl-methionine (SAM)-dependent methyltransferase MRPP1/2 subcomplex to function.	S-Adenosylmethionine	174-177	protein only RNase P catalytic subunit	Homo sapiens	65-70
31455609-1	2019	Mitochondrial RNase P Protein 3 (MRPP3), a protein-only RNase P (PRORP), is the nuclease component of the mtRNase P complex and requires a two-protein S-adenosyl-methionine (SAM)-dependent methyltransferase MRPP1/2 subcomplex to function.	S-Adenosylmethionine	174-177	tRNA methyltransferase 10C, mitochondrial RNase P subunit	Homo sapiens	207-214
31586407-5	2019	We have solved the crystal structures of the apo and S-adenosyl-L-methionine bound forms of Trm7-Trm734.	S-Adenosylmethionine	53-76	tRNA methyltransferase TRM7	Saccharomyces cerevisiae S288C	92-96
31849941-3	2019	The functions of these enzymes highly depend on the availability of key products of cellular metabolism pathways such as acetyl-CoA, NAD (Nicotinamide adenine dinucleotide) and SEM (S-adenosylmethionine), suggesting that there is a close crosstalk between the metabolic and the epigenetic regulation of CD8+ T cells.	S-Adenosylmethionine	177-180	CD8a molecule	Homo sapiens	303-306
31849941-3	2019	The functions of these enzymes highly depend on the availability of key products of cellular metabolism pathways such as acetyl-CoA, NAD (Nicotinamide adenine dinucleotide) and SEM (S-adenosylmethionine), suggesting that there is a close crosstalk between the metabolic and the epigenetic regulation of CD8+ T cells.	S-Adenosylmethionine	182-202	CD8a molecule	Homo sapiens	303-306
31586407-5	2019	We have solved the crystal structures of the apo and S-adenosyl-L-methionine bound forms of Trm7-Trm734.	S-Adenosylmethionine	53-76	Rtt10p	Saccharomyces cerevisiae S288C	97-103
31589440-1	2019	Nicotinamide N-methyltransferase (NNMT) is a metabolic enzyme that methylates nicotinamide (NAM) using cofactor S-adenosylmethionine (SAM).	S-Adenosylmethionine	112-132	nicotinamide N-methyltransferase	Homo sapiens	0-32
31589440-1	2019	Nicotinamide N-methyltransferase (NNMT) is a metabolic enzyme that methylates nicotinamide (NAM) using cofactor S-adenosylmethionine (SAM).	S-Adenosylmethionine	112-132	nicotinamide N-methyltransferase	Homo sapiens	34-38
31589440-1	2019	Nicotinamide N-methyltransferase (NNMT) is a metabolic enzyme that methylates nicotinamide (NAM) using cofactor S-adenosylmethionine (SAM).	S-Adenosylmethionine	134-137	nicotinamide N-methyltransferase	Homo sapiens	0-32
31589440-1	2019	Nicotinamide N-methyltransferase (NNMT) is a metabolic enzyme that methylates nicotinamide (NAM) using cofactor S-adenosylmethionine (SAM).	S-Adenosylmethionine	134-137	nicotinamide N-methyltransferase	Homo sapiens	34-38
31589440-4	2019	The reported nicotinamide-SAM conjugate (named NS1) features an alkyne as a key design element that closely mimics the linear, 180  transition state geometry found in the NNMT-catalyzed SAM   NAM methyl transfer reaction.	S-Adenosylmethionine	26-29	influenza virus NS1A binding protein	Homo sapiens	47-50
31589440-4	2019	The reported nicotinamide-SAM conjugate (named NS1) features an alkyne as a key design element that closely mimics the linear, 180  transition state geometry found in the NNMT-catalyzed SAM   NAM methyl transfer reaction.	S-Adenosylmethionine	26-29	nicotinamide N-methyltransferase	Homo sapiens	171-175
31589440-4	2019	The reported nicotinamide-SAM conjugate (named NS1) features an alkyne as a key design element that closely mimics the linear, 180  transition state geometry found in the NNMT-catalyzed SAM   NAM methyl transfer reaction.	S-Adenosylmethionine	186-189	influenza virus NS1A binding protein	Homo sapiens	47-50
31589440-4	2019	The reported nicotinamide-SAM conjugate (named NS1) features an alkyne as a key design element that closely mimics the linear, 180  transition state geometry found in the NNMT-catalyzed SAM   NAM methyl transfer reaction.	S-Adenosylmethionine	186-189	nicotinamide N-methyltransferase	Homo sapiens	171-175
31662455-5	2019	Our data demonstrate that the expression of CTH leads to defective macrophage activation by (i) dysregulation of polyamine metabolism by depletion of S-adenosylmethionine, resulting in immunosuppressive putrescine accumulation and inhibition of spermidine and spermine synthesis, and (ii) increased histone H3K9, H3K27, and H3K36 di/trimethylation, which is associated with gene expression silencing.	S-Adenosylmethionine	150-170	cystathionine gamma-lyase	Homo sapiens	44-47
31548311-3	2019	Yeast strains deficient in polyamine biosynthesis (spe1 , lacking ornithine decarboxylase, and spe2 , lacking S-adenosylmethionine decarboxylase) require externally supplied polyamines, but supplementation with as little as 10-8 M spermidine restores their growth.	S-Adenosylmethionine	110-130	adenosylmethionine decarboxylase SPE2	Saccharomyces cerevisiae S288C	95-99
31450076-5	2019	The chief enzyme which synthesizes H2S in brain parenchyma, cystathionine beta-synthase (CBS), employs cysteine as its rate-limiting substrate, and is allosterically activated by S-adenosylmethionine (SAM).	S-Adenosylmethionine	179-199	cystathionine beta-synthase	Homo sapiens	60-87
31450076-5	2019	The chief enzyme which synthesizes H2S in brain parenchyma, cystathionine beta-synthase (CBS), employs cysteine as its rate-limiting substrate, and is allosterically activated by S-adenosylmethionine (SAM).	S-Adenosylmethionine	201-204	cystathionine beta-synthase	Homo sapiens	60-87
31058319-7	2019	PARTICLE may provide a buffering riboswitch platform for S-adenosylmethionine.	S-Adenosylmethionine	57-77	promoter of MAT2A antisense radiation-induced circulating long non-coding RNA	Homo sapiens	0-8
31668391-2	2019	The enzyme glycine N-methyltransferase (GNMT), the most important enzyme implicated in S-adenosylmethionine catabolism in the liver, is downregulated during NAFLD progression.	S-Adenosylmethionine	87-107	glycine N-methyltransferase	Homo sapiens	11-38
31668391-2	2019	The enzyme glycine N-methyltransferase (GNMT), the most important enzyme implicated in S-adenosylmethionine catabolism in the liver, is downregulated during NAFLD progression.	S-Adenosylmethionine	87-107	glycine N-methyltransferase	Homo sapiens	40-44
31717699-0	2019	Perturbation of Methionine/S-adenosylmethionine Metabolism as a Novel Vulnerability in MLL Rearranged Leukemia.	S-Adenosylmethionine	27-47	lysine methyltransferase 2A	Homo sapiens	87-90
31463593-2	2019	In the first step of diphthamide biosynthesis, a [4Fe-4S] cluster-containing radical SAM enzyme, Dph1-Dph2 heterodimer in eukaryotes or Dph2 homodimer in archaea, cleaves S-adenosylmethionine and transfers the 3-amino-3-carboxypropyl group to EF2.	S-Adenosylmethionine	171-191	diphthamide biosynthesis 1	Homo sapiens	97-101
31420217-5	2019	Mechanistically, SAM generation maintains a relatively high SAM:S-adenosylhomocysteine ratio to support histone H3 lysine 36 trimethylation for IL-1beta production.	S-Adenosylmethionine	17-20	interleukin 1 alpha	Homo sapiens	144-152
31293025-2	2019	MAT2A and MAT2B coordinately catalyzes the synthesis of the major biological methyl donor S-adenosylmethionine (SAMe).	S-Adenosylmethionine	90-110	methionine adenosyltransferase 2A	Homo sapiens	0-5
31293025-2	2019	MAT2A and MAT2B coordinately catalyzes the synthesis of the major biological methyl donor S-adenosylmethionine (SAMe).	S-Adenosylmethionine	90-110	methionine adenosyltransferase 2B	Homo sapiens	10-15
31302162-6	2019	Different micronutrients (i.e. folate and vitamin B12) are required to properly generate S-adenosylmethionine, making nutrition a strong regulating factor.	S-Adenosylmethionine	89-109	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	50-53
31494172-6	2019	MNAM is one of potential therapeutic factor, which produced by nicotinamide N-methyltransferase (NNMT) via consumption of S-adenosyl methionine (SAM) and nicotinamide.	S-Adenosylmethionine	122-143	nicotinamide N-methyltransferase	Homo sapiens	63-95
31494172-6	2019	MNAM is one of potential therapeutic factor, which produced by nicotinamide N-methyltransferase (NNMT) via consumption of S-adenosyl methionine (SAM) and nicotinamide.	S-Adenosylmethionine	122-143	nicotinamide N-methyltransferase	Homo sapiens	97-101
31494172-6	2019	MNAM is one of potential therapeutic factor, which produced by nicotinamide N-methyltransferase (NNMT) via consumption of S-adenosyl methionine (SAM) and nicotinamide.	S-Adenosylmethionine	145-148	nicotinamide N-methyltransferase	Homo sapiens	63-95
31494172-6	2019	MNAM is one of potential therapeutic factor, which produced by nicotinamide N-methyltransferase (NNMT) via consumption of S-adenosyl methionine (SAM) and nicotinamide.	S-Adenosylmethionine	145-148	nicotinamide N-methyltransferase	Homo sapiens	97-101
31350635-1	2019	The cobalamin-dependent radical S-adenosylmethionine (SAM) enzyme TsrM catalyzes the methylation of C2 of L-tryptophan to form 2-methyltryptophan during the biosynthesis of thiostrepton A.	S-Adenosylmethionine	32-52	TSRM	Homo sapiens	66-70
31350635-1	2019	The cobalamin-dependent radical S-adenosylmethionine (SAM) enzyme TsrM catalyzes the methylation of C2 of L-tryptophan to form 2-methyltryptophan during the biosynthesis of thiostrepton A.	S-Adenosylmethionine	54-57	TSRM	Homo sapiens	66-70
31463593-2	2019	In the first step of diphthamide biosynthesis, a [4Fe-4S] cluster-containing radical SAM enzyme, Dph1-Dph2 heterodimer in eukaryotes or Dph2 homodimer in archaea, cleaves S-adenosylmethionine and transfers the 3-amino-3-carboxypropyl group to EF2.	S-Adenosylmethionine	171-191	diphthamide biosynthesis 2	Homo sapiens	102-106
31463593-2	2019	In the first step of diphthamide biosynthesis, a [4Fe-4S] cluster-containing radical SAM enzyme, Dph1-Dph2 heterodimer in eukaryotes or Dph2 homodimer in archaea, cleaves S-adenosylmethionine and transfers the 3-amino-3-carboxypropyl group to EF2.	S-Adenosylmethionine	171-191	diphthamide biosynthesis 2	Homo sapiens	136-140
31463593-2	2019	In the first step of diphthamide biosynthesis, a [4Fe-4S] cluster-containing radical SAM enzyme, Dph1-Dph2 heterodimer in eukaryotes or Dph2 homodimer in archaea, cleaves S-adenosylmethionine and transfers the 3-amino-3-carboxypropyl group to EF2.	S-Adenosylmethionine	171-191	eukaryotic translation elongation factor 2	Homo sapiens	243-246
31251801-5	2019	Here we report the crystal structures of a ternary complex of human (hs) TFB1M-h45-S-adenosyl-methionine and a binary complex hsTFB1M-h45.	S-Adenosylmethionine	85-104	transcription factor B1, mitochondrial	Homo sapiens	73-78
31331996-6	2019	The ATMS1 mutation caused a significant decrease in the ratio of S-adenosylmethionine to S-adenosylhomocysteine.	S-Adenosylmethionine	65-85	Cobalamin-independent synthase family protein	Arabidopsis thaliana	4-9
31353838-10	2019	Preoperative supplementation with VB12 and folic acid (FA) in the diet or S-adenosylmethionine (SAM) injection reduced perioperative serum Hcy level and inhibited the development of PND in aged mice.	S-Adenosylmethionine	74-94	natriuretic peptide type A	Mus musculus	182-185
31390828-1	2019	Protein arginine methyltransferase 1 (PRMT1) can catalyze protein arginine methylation by transferring the methyl group from S-adenosyl-L-methionine (SAM) to the guanidyl nitrogen atom of protein arginine, which influences a variety of biological processes.	S-Adenosylmethionine	125-148	protein arginine methyltransferase 1	Homo sapiens	0-36
31390828-1	2019	Protein arginine methyltransferase 1 (PRMT1) can catalyze protein arginine methylation by transferring the methyl group from S-adenosyl-L-methionine (SAM) to the guanidyl nitrogen atom of protein arginine, which influences a variety of biological processes.	S-Adenosylmethionine	125-148	protein arginine methyltransferase 1	Homo sapiens	38-43
31353838-10	2019	Preoperative supplementation with VB12 and folic acid (FA) in the diet or S-adenosylmethionine (SAM) injection reduced perioperative serum Hcy level and inhibited the development of PND in aged mice.	S-Adenosylmethionine	96-99	natriuretic peptide type A	Mus musculus	182-185
30686113-0	2019	Breeding of a cordycepin-resistant and adenosine kinase-deficient sake yeast strain that accumulates high levels of S-adenosylmethionine.	S-Adenosylmethionine	116-136	adenosine kinase	Saccharomyces cerevisiae S288C	39-55
30686113-1	2019	Adenosine kinase (ADO1)-deficient mutants can be obtained from cordycepin-resistant strains, and the disruption of ADO1 causes S-adenosylmethionine (SAM) accumulation.	S-Adenosylmethionine	129-147	adenosine kinase	Saccharomyces cerevisiae S288C	0-16
30686113-1	2019	Adenosine kinase (ADO1)-deficient mutants can be obtained from cordycepin-resistant strains, and the disruption of ADO1 causes S-adenosylmethionine (SAM) accumulation.	S-Adenosylmethionine	129-147	adenosine kinase	Saccharomyces cerevisiae S288C	18-22
30686113-1	2019	Adenosine kinase (ADO1)-deficient mutants can be obtained from cordycepin-resistant strains, and the disruption of ADO1 causes S-adenosylmethionine (SAM) accumulation.	S-Adenosylmethionine	129-147	adenosine kinase	Saccharomyces cerevisiae S288C	115-119
30676783-1	2019	Methionine synthase encoded by the MTR gene is one of the key enzymes involved in the SAM (S- Adenosyl Methionine) cycle catalyzing the conversion of homocysteine to methionine.	S-Adenosylmethionine	92-113	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	0-19
30575033-5	2019	We demonstrated that AdoMet induced apoptosis in Cal-33 and JHU-SCC-011 cells, involving a caspase-dependent mechanism paralleled by an increased Bax/Bcl-2 ratio.	S-Adenosylmethionine	21-27	BCL2 associated X, apoptosis regulator	Homo sapiens	146-149
30575033-5	2019	We demonstrated that AdoMet induced apoptosis in Cal-33 and JHU-SCC-011 cells, involving a caspase-dependent mechanism paralleled by an increased Bax/Bcl-2 ratio.	S-Adenosylmethionine	21-27	BCL2 apoptosis regulator	Homo sapiens	150-155
31248224-6	2019	Indeed, AMPKalpha2 deletion in macrophages increased the ratio of S-adenosyl methionine to S-adenosyl homocysteine and increased global DNA cytosine methylation.	S-Adenosylmethionine	66-87	protein kinase, AMP-activated, alpha 2 catalytic subunit	Mus musculus	8-18
31086990-6	2019	In in vitro experiments, we demonstrated that one of the consequences of GNMT inhibition was an increase in genome methylation facilitated by an elevated level of S-adenosyl-L-methionine.	S-Adenosylmethionine	163-186	glycine N-methyltransferase	Homo sapiens	73-77
30693532-4	2019	Methionine synthase catalyzes the methyl-Cbl dependent (re)methylation of homocysteine to methionine within the methionine cycle; a reaction required to produce this essential amino acid and generate S-adenosylmethionine, the most important cellular methyl-donor.	S-Adenosylmethionine	200-220	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	0-19
30693532-4	2019	Methionine synthase catalyzes the methyl-Cbl dependent (re)methylation of homocysteine to methionine within the methionine cycle; a reaction required to produce this essential amino acid and generate S-adenosylmethionine, the most important cellular methyl-donor.	S-Adenosylmethionine	200-220	Cbl proto-oncogene	Homo sapiens	41-44
31234428-8	2019	Furthermore, SAM enhances the IFN-alpha antiviral activity and protects against hepatic ischemia-reperfusion injury during hepatectomy in HCC patients with chronic hepatitis B virus (HBV) infection.	S-Adenosylmethionine	13-16	interferon alpha 1	Homo sapiens	30-39
31354356-1	2019	Background: In conjunction with the methionine adenosyltransferase 2A (MAT2A), MAT2B protein catalyses the formation of methyl donor S-adenosylmethionine to mediate cell metabolism, including proliferation and apoptosis.	S-Adenosylmethionine	133-153	methionine adenosyltransferase 2A	Homo sapiens	36-69
31354356-1	2019	Background: In conjunction with the methionine adenosyltransferase 2A (MAT2A), MAT2B protein catalyses the formation of methyl donor S-adenosylmethionine to mediate cell metabolism, including proliferation and apoptosis.	S-Adenosylmethionine	133-153	methionine adenosyltransferase 2A	Homo sapiens	71-76
31354356-1	2019	Background: In conjunction with the methionine adenosyltransferase 2A (MAT2A), MAT2B protein catalyses the formation of methyl donor S-adenosylmethionine to mediate cell metabolism, including proliferation and apoptosis.	S-Adenosylmethionine	133-153	methionine adenosyltransferase 2B	Homo sapiens	79-84
30951287-5	2019	The compound displays high selectivity for DOT1L over other S-adenosylmethionine (SAM)-dependent PMTs.	S-Adenosylmethionine	60-80	DOT1 like histone lysine methyltransferase	Homo sapiens	43-48
31191592-4	2019	In a first reaction, S-adenosyl-L-methionine (SAM) is converted into 1-aminocyclopropane-1-carboxylic acid (ACC) by ACC-synthase (ACS).	S-Adenosylmethionine	21-44	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	116-128
31191592-4	2019	In a first reaction, S-adenosyl-L-methionine (SAM) is converted into 1-aminocyclopropane-1-carboxylic acid (ACC) by ACC-synthase (ACS).	S-Adenosylmethionine	21-44	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	130-133
31191592-4	2019	In a first reaction, S-adenosyl-L-methionine (SAM) is converted into 1-aminocyclopropane-1-carboxylic acid (ACC) by ACC-synthase (ACS).	S-Adenosylmethionine	46-49	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	116-128
31191592-4	2019	In a first reaction, S-adenosyl-L-methionine (SAM) is converted into 1-aminocyclopropane-1-carboxylic acid (ACC) by ACC-synthase (ACS).	S-Adenosylmethionine	46-49	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	130-133
30935952-4	2019	Oleacein could be superimposed onto the catechol-binding site of COMT, maintaining the interactions with the atomic positions involved in methyl transfer from the S-adenosyl-L-methionine cofactor.	S-Adenosylmethionine	163-186	catechol-O-methyltransferase	Homo sapiens	65-69
31069954-1	2019	Smyd2 lysine methyltransferase regulates monomethylation of histone and nonhistone lysine residues using S-adenosylmethionine cofactor as the methyl donor.	S-Adenosylmethionine	105-125	SET and MYND domain containing 2	Homo sapiens	0-5
30951287-5	2019	The compound displays high selectivity for DOT1L over other S-adenosylmethionine (SAM)-dependent PMTs.	S-Adenosylmethionine	82-85	DOT1 like histone lysine methyltransferase	Homo sapiens	43-48
30712196-1	2019	PURPOSE: Many transformed cells and embryonic stem cells are dependent on the biosynthesis of the universal methyl-donor S-adenosylmethionine (SAM) from methionine by the enzyme MAT2A to maintain their epigenome.	S-Adenosylmethionine	121-141	methionine adenosyltransferase 2A	Homo sapiens	178-183
30827843-6	2019	Dynamics of the autoinhibitory loop can be attributed to subtle structural changes of the S-adenosylmethionine (SAM) binding pocket induced by Mrg15 binding, implicating a mechanism of conformational coupling between SAM and substrate binding sites.	S-Adenosylmethionine	90-110	mortality factor 4 like 1	Homo sapiens	143-148
30827843-6	2019	Dynamics of the autoinhibitory loop can be attributed to subtle structural changes of the S-adenosylmethionine (SAM) binding pocket induced by Mrg15 binding, implicating a mechanism of conformational coupling between SAM and substrate binding sites.	S-Adenosylmethionine	112-115	mortality factor 4 like 1	Homo sapiens	143-148
31234761-4	2019	Succinimide conversion into Asp is spontaneous, while isoAsp is restored by PIMT using S-adenosylmethionine as a methyl donor.	S-Adenosylmethionine	87-107	protein-L-isoaspartate (D-aspartate) O-methyltransferase 1	Mus musculus	76-80
30712196-1	2019	PURPOSE: Many transformed cells and embryonic stem cells are dependent on the biosynthesis of the universal methyl-donor S-adenosylmethionine (SAM) from methionine by the enzyme MAT2A to maintain their epigenome.	S-Adenosylmethionine	143-146	methionine adenosyltransferase 2A	Homo sapiens	178-183
31043742-7	2019	Expression of NNMT in CAFs led to depletion of S-adenosyl methionine and reduction in histone methylation associated with widespread gene expression changes in the tumour stroma.	S-Adenosylmethionine	47-68	nicotinamide N-methyltransferase	Homo sapiens	14-18
30683944-0	2019	S-Adenosylmethionine synergistically enhances the antitumor effect of gemcitabine against pancreatic cancer through JAK2/STAT3 pathway.	S-Adenosylmethionine	0-20	Janus kinase 2	Homo sapiens	116-120
30683944-0	2019	S-Adenosylmethionine synergistically enhances the antitumor effect of gemcitabine against pancreatic cancer through JAK2/STAT3 pathway.	S-Adenosylmethionine	0-20	signal transducer and activator of transcription 3	Homo sapiens	121-126
31043742-7	2019	Expression of NNMT in CAFs led to depletion of S-adenosyl methionine and reduction in histone methylation associated with widespread gene expression changes in the tumour stroma.	S-Adenosylmethionine	47-68	T-box transcription factor 1	Homo sapiens	22-26
30933557-1	2019	Nicotinamide N-methyltransferase (NNMT) catalyzes the S-adenosyl-l-methionine-dependent methylation of nicotinamide to form N-methylnicotinamide.	S-Adenosylmethionine	54-77	nicotinamide N-methyltransferase	Homo sapiens	0-32
30933557-1	2019	Nicotinamide N-methyltransferase (NNMT) catalyzes the S-adenosyl-l-methionine-dependent methylation of nicotinamide to form N-methylnicotinamide.	S-Adenosylmethionine	54-77	nicotinamide N-methyltransferase	Homo sapiens	34-38
30901734-3	2019	An ultraperformance liquid chromatography (UPLC) method was developed and validated for the quantification of TPMT enzyme activity based on the conversion of 6-mercaptopurine (6-MP) to 6-methylmercaptopurine (6-MMP) using S-adenosyl-L-methionine (SAM) as methyl donor in red blood cell lysates (RBC).	S-Adenosylmethionine	222-245	thiopurine S-methyltransferase	Homo sapiens	110-114
30901734-3	2019	An ultraperformance liquid chromatography (UPLC) method was developed and validated for the quantification of TPMT enzyme activity based on the conversion of 6-mercaptopurine (6-MP) to 6-methylmercaptopurine (6-MMP) using S-adenosyl-L-methionine (SAM) as methyl donor in red blood cell lysates (RBC).	S-Adenosylmethionine	247-250	thiopurine S-methyltransferase	Homo sapiens	110-114
30860833-4	2019	Human 5"-methylthioadenosine phosphorylase (MTAP), a reported anticancer target, catalyzes phosphorolysis of 5"-methylthioadenosine to salvage S-adenosylmethionine.	S-Adenosylmethionine	143-163	methylthioadenosine phosphorylase	Homo sapiens	6-42
30860833-4	2019	Human 5"-methylthioadenosine phosphorylase (MTAP), a reported anticancer target, catalyzes phosphorolysis of 5"-methylthioadenosine to salvage S-adenosylmethionine.	S-Adenosylmethionine	143-163	methylthioadenosine phosphorylase	Homo sapiens	44-48
30265288-1	2019	Methionine adenosyltransferase II (MAT2A) is essential to the synthesis of S-adenosylmethionine, a major methyl donor, from L-methionine and ATP.	S-Adenosylmethionine	75-95	methionine adenosyltransferase 2A	Homo sapiens	35-40
30926424-7	2019	Mechanistically, TGF-beta1 induces phosphorylation of p65, i.e., activation of NF-kappaB, thereby promoting mRNA transcription and protein expression of MAT2A and reduces S-adenosylmethionine (SAM) concentration in HSCs.	S-Adenosylmethionine	173-191	transforming growth factor, beta 1	Mus musculus	17-26
30926424-7	2019	Mechanistically, TGF-beta1 induces phosphorylation of p65, i.e., activation of NF-kappaB, thereby promoting mRNA transcription and protein expression of MAT2A and reduces S-adenosylmethionine (SAM) concentration in HSCs.	S-Adenosylmethionine	173-191	v-rel reticuloendotheliosis viral oncogene homolog A (avian)	Mus musculus	54-57
30926424-7	2019	Mechanistically, TGF-beta1 induces phosphorylation of p65, i.e., activation of NF-kappaB, thereby promoting mRNA transcription and protein expression of MAT2A and reduces S-adenosylmethionine (SAM) concentration in HSCs.	S-Adenosylmethionine	173-191	nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105	Mus musculus	79-88
30858354-0	2019	The methionine salvage pathway-involving ADI1 inhibits hepatoma growth by epigenetically altering genes expression via elevating S-adenosylmethionine.	S-Adenosylmethionine	129-149	acireductone dioxygenase 1	Homo sapiens	41-45
30858354-8	2019	Suppression of CAV1 expression was mediated by an increase of S-adenosylmethionine (SAMe) level.	S-Adenosylmethionine	62-82	caveolin 1	Homo sapiens	15-19
30862944-2	2019	While MTHFR has long been known to be allosterically inhibited by S-adenosylmethionine (SAM), only relatively recently has N-terminal multisite phosphorylation been shown to provide an additional layer of regulation.	S-Adenosylmethionine	66-86	methylenetetrahydrofolate reductase	Homo sapiens	6-11
30862944-2	2019	While MTHFR has long been known to be allosterically inhibited by S-adenosylmethionine (SAM), only relatively recently has N-terminal multisite phosphorylation been shown to provide an additional layer of regulation.	S-Adenosylmethionine	88-91	methylenetetrahydrofolate reductase	Homo sapiens	6-11
30657139-6	2019	As a result, SAMS from cell lysate achieved about 95% activity recovery in the biosynthesis of S-adenosylmethionine (SAM) under high temperature conditions (70  C) with a simple mixing step.	S-Adenosylmethionine	95-115	methionine adenosyltransferase 1A	Homo sapiens	13-17
29122967-3	2019	Metabolomics and transcriptomics integrated analyses of livers revealed an unexpected accumulation of hepatic S-Adenosylmethionine (SAM) when compared with healthy livers likely due to diminished methylation reactions and repression of GNMT.	S-Adenosylmethionine	110-130	glycine N-methyltransferase	Mesocricetus auratus	236-240
30709491-7	2019	The corresponding data confirm the closed interaction of CDC48 with components of the UPS and shed light on its putative regulatory function of S-adenosyl-methionine synthesis and metabolism.	S-Adenosylmethionine	144-165	AAA family ATPase CDC48	Saccharomyces cerevisiae S288C	57-62
30427579-0	2019	Protein Arginine Methyltransferase 1-Dependent Labeling and Isolation of Histone H4 through N-Mustard Analogues of S-Adenosyl-l-methionine.	S-Adenosylmethionine	115-138	protein arginine methyltransferase 1	Homo sapiens	0-36
30427579-0	2019	Protein Arginine Methyltransferase 1-Dependent Labeling and Isolation of Histone H4 through N-Mustard Analogues of S-Adenosyl-l-methionine.	S-Adenosylmethionine	115-138	H4 clustered histone 6	Homo sapiens	73-83
30408316-5	2019	On both diets, MTHFR deficiency results in decreased S-adenosylmethionine, increased S-adenosylhomocysteine, and decreased betaine with reduced methylation capacity, and changes in expression of several inflammatory or anti-inflammatory mediators (Saa1, Apoa1, and Pon1).	S-Adenosylmethionine	53-73	methylenetetrahydrofolate reductase	Mus musculus	15-20
30704107-1	2019	The tRNA methyltransferase Trm10, conserved throughout Eukarya and Archaea, catalyzes N1-methylation of purine residues at position 9 using S-adenosyl methionine as the methyl donor.	S-Adenosylmethionine	140-161	tRNA methyltransferase 10A	Homo sapiens	27-32
30606816-0	2019	MTHFR C677T polymorphism increases MTX sensitivity via the inhibition of S-adenosylmethionine and de novo purine synthesis.	S-Adenosylmethionine	73-93	methylenetetrahydrofolate reductase	Homo sapiens	0-5
30407230-0	2019	Epigenetical Targeting of the FOXP3 Gene by S-Adenosylmethionine Diminishes the Suppressive Capacity of Regulatory T Cells Ex Vivo and Alters the Expression Profiles.	S-Adenosylmethionine	44-64	forkhead box P3	Homo sapiens	30-35
30646578-3	2019	MTHFR is critical for production of S-adenosyl-l-methionine (SAM), the principal methyl donor.	S-Adenosylmethionine	36-59	methylenetetrahydrofolate reductase	Homo sapiens	0-5
30646578-3	2019	MTHFR is critical for production of S-adenosyl-l-methionine (SAM), the principal methyl donor.	S-Adenosylmethionine	61-64	methylenetetrahydrofolate reductase	Homo sapiens	0-5
30513135-1	2019	Protein arginine methyltransferase 7 (PRMT7) is a member of a family of enzymes that catalyze the transfer of methyl groups from S-adenosyl-l-methionine to nitrogen atoms on arginine residues.	S-Adenosylmethionine	129-152	protein arginine methyltransferase 7	Homo sapiens	0-36
30513135-1	2019	Protein arginine methyltransferase 7 (PRMT7) is a member of a family of enzymes that catalyze the transfer of methyl groups from S-adenosyl-l-methionine to nitrogen atoms on arginine residues.	S-Adenosylmethionine	129-152	protein arginine methyltransferase 7	Homo sapiens	38-43
30308221-5	2019	By comparing binding characteristics of Sec in the absence and in the presence of methyl donor, we confirmed S-adenosylmethionine (SAM)-induced conformational changes in TPMT.	S-Adenosylmethionine	109-129	thiopurine S-methyltransferase	Homo sapiens	170-174
30591370-6	2019	FINDINGS: AKBA directly interacts with methionine adenosyltransferase 2A (MAT2A), inhibited its enzyme activity, decreased level of S-adenosylmethionine (SAM) and SAM/SAH ratio, and reprogrammed one-carbon metabolism in HaCaT cells.	S-Adenosylmethionine	132-152	methionine adenosyltransferase 2A	Homo sapiens	74-79
30391174-13	2019	Expression of glycine N-methyltransferase, the enzyme that controls transmethylation flux from S-adenosyl-methionine, was not affected by Met concentration.	S-Adenosylmethionine	95-116	glycine N-methyltransferase	Bos taurus	14-41
29913347-6	2018	RNA methyltransferases, including METTL3/METTL14 responsible for N6-methyladensosine (m6A) formation, share a common structural core and utilize S-adenosyl methionine as a methyl donor.	S-Adenosylmethionine	145-166	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	34-40
30535232-3	2019	Merm1 interacts with Dnmt3a and represses its methyltransferase activity with the requirement of the binding motif for S-adenosyl-L-methionine.	S-Adenosylmethionine	119-142	BUD23 rRNA methyltransferase and ribosome maturation factor	Homo sapiens	0-5
30535232-3	2019	Merm1 interacts with Dnmt3a and represses its methyltransferase activity with the requirement of the binding motif for S-adenosyl-L-methionine.	S-Adenosylmethionine	119-142	DNA methyltransferase 3 alpha	Homo sapiens	21-27
31379141-5	2019	Recently, several sensors of leucine, arginine, and S-adenosylmethionine for the amino acid-stimulated mTORC1 pathway have been coming to light.	S-Adenosylmethionine	52-72	CREB regulated transcription coactivator 1	Mus musculus	103-109
30533999-10	2018	We also showed that miR-486-5p inhibitor induces autophagy and enhances AdoMet-induced autophagic process by increasing PTEN expression and by inhibiting AKT signaling.	S-Adenosylmethionine	72-78	phosphatase and tensin homolog	Homo sapiens	120-124
29913347-6	2018	RNA methyltransferases, including METTL3/METTL14 responsible for N6-methyladensosine (m6A) formation, share a common structural core and utilize S-adenosyl methionine as a methyl donor.	S-Adenosylmethionine	145-166	methyltransferase 14, N6-adenosine-methyltransferase subunit	Homo sapiens	41-48
29913347-6	2018	RNA methyltransferases, including METTL3/METTL14 responsible for N6-methyladensosine (m6A) formation, share a common structural core and utilize S-adenosyl methionine as a methyl donor.	S-Adenosylmethionine	145-166	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	65-89
30076902-1	2018	The mitochondrial S-adenosylmethionine carrier (SAMC), encoded by the SLC25A26 gene, catalyzes the uptake of S-adenosylmethionine (SAM) from the cytosol into mitochondria in exchange for S-adenosylhomocysteine (SAH), produced inside the mitochondria.	S-Adenosylmethionine	18-38	solute carrier family 25 member 26	Homo sapiens	48-52
30368163-0	2018	An augmentation study of MSI-195 (S-adenosylmethionine) in Major Depressive Disorder.	S-Adenosylmethionine	34-54	RB binding protein 4, chromatin remodeling factor	Homo sapiens	25-28
30206180-9	2018	To our knowledge, this is the first study to reveal an association between Hmt1p and phosphate homeostasis and one which suggests a regulatory link between S-adenosyl methionine and intracellular phosphate.	S-Adenosylmethionine	156-177	protein-arginine omega-N methyltransferase HMT1	Saccharomyces cerevisiae S288C	75-80
30076902-1	2018	The mitochondrial S-adenosylmethionine carrier (SAMC), encoded by the SLC25A26 gene, catalyzes the uptake of S-adenosylmethionine (SAM) from the cytosol into mitochondria in exchange for S-adenosylhomocysteine (SAH), produced inside the mitochondria.	S-Adenosylmethionine	18-38	solute carrier family 25 member 26	Homo sapiens	70-78
30076902-1	2018	The mitochondrial S-adenosylmethionine carrier (SAMC), encoded by the SLC25A26 gene, catalyzes the uptake of S-adenosylmethionine (SAM) from the cytosol into mitochondria in exchange for S-adenosylhomocysteine (SAH), produced inside the mitochondria.	S-Adenosylmethionine	48-51	solute carrier family 25 member 26	Homo sapiens	18-46
30076902-1	2018	The mitochondrial S-adenosylmethionine carrier (SAMC), encoded by the SLC25A26 gene, catalyzes the uptake of S-adenosylmethionine (SAM) from the cytosol into mitochondria in exchange for S-adenosylhomocysteine (SAH), produced inside the mitochondria.	S-Adenosylmethionine	48-51	solute carrier family 25 member 26	Homo sapiens	70-78
30347410-8	2018	In addition, alpha-pinealocytes have transcriptomic differences that likely enhance melatonin formation by increasing the availability of the Asmt cofactor S-adenosylmethionine, resulting from increased production of a precursor of S-adenosylmethionine, ATP.	S-Adenosylmethionine	156-176	acetylserotonin O-methyltransferase	Homo sapiens	142-146
29868988-5	2018	Here we report nearly complete 1H, 15N, and 13C chemical shifts assignments of the 26 kDa WBSCR27 protein from Mus musculus in complex with the cofactor S-adenosyl-L-methionine (SAM).	S-Adenosylmethionine	155-176	methyltransferase like 27	Mus musculus	90-97
30189201-5	2018	Specifically, we demonstrate that SETD6 monomeric, dimeric and trimeric forms are stabilized by the methyl donor, S-adenosyl-l-methionine.	S-Adenosylmethionine	114-137	SET domain containing 6, protein lysine methyltransferase	Homo sapiens	34-39
30309036-2	2018	The methylation of DNA is regulated by DNA methyltransferases (DNMT1, DNMT3a, and DNMT3b) in the presence of S-adenosylmethionine (SAM), which serves as a methyl group donor.	S-Adenosylmethionine	109-129	DNA methyltransferase 1	Homo sapiens	63-68
30309036-2	2018	The methylation of DNA is regulated by DNA methyltransferases (DNMT1, DNMT3a, and DNMT3b) in the presence of S-adenosylmethionine (SAM), which serves as a methyl group donor.	S-Adenosylmethionine	109-129	DNA methyltransferase 3 alpha	Homo sapiens	70-76
30309036-2	2018	The methylation of DNA is regulated by DNA methyltransferases (DNMT1, DNMT3a, and DNMT3b) in the presence of S-adenosylmethionine (SAM), which serves as a methyl group donor.	S-Adenosylmethionine	109-129	DNA methyltransferase 3 beta	Homo sapiens	82-88
30309036-2	2018	The methylation of DNA is regulated by DNA methyltransferases (DNMT1, DNMT3a, and DNMT3b) in the presence of S-adenosylmethionine (SAM), which serves as a methyl group donor.	S-Adenosylmethionine	131-134	DNA methyltransferase 1	Homo sapiens	63-68
30309036-2	2018	The methylation of DNA is regulated by DNA methyltransferases (DNMT1, DNMT3a, and DNMT3b) in the presence of S-adenosylmethionine (SAM), which serves as a methyl group donor.	S-Adenosylmethionine	131-134	DNA methyltransferase 3 alpha	Homo sapiens	70-76
30309036-2	2018	The methylation of DNA is regulated by DNA methyltransferases (DNMT1, DNMT3a, and DNMT3b) in the presence of S-adenosylmethionine (SAM), which serves as a methyl group donor.	S-Adenosylmethionine	131-134	DNA methyltransferase 3 beta	Homo sapiens	82-88
30309036-3	2018	Increased availability of SAM enhances DNMT activity, while its metabolites, S-adenosyl-l-homocysteine (SAH) and decarboxylated S-adenosylmethionine (dcSAM), act to inhibit DNMT activity.	S-Adenosylmethionine	128-148	DNA methyltransferase 1	Homo sapiens	173-177
30044909-1	2018	Nicotinamide- N-methyltransferase (NNMT) catalyzes the irreversible methylation of nicotinamide (NAM) to form N-methyl nicotinamide using S-adenosyl methionine as a methyl donor.	S-Adenosylmethionine	138-159	nicotinamide N-methyltransferase	Homo sapiens	0-33
30063253-0	2018	Improved S-adenosylmethionine and glutathione biosynthesis by heterologous expression of an ATP6 gene in Candida utilis.	S-Adenosylmethionine	9-29	atp6	Cyberlindnera jadinii	92-96
30157632-1	2018	Catechol- O-methyltransferase is an enzyme that catalyzes the methylation reaction of dopamine by S-adenosylmethionine, increasing the reaction rate by almost 16 orders of magnitude compared to the reaction in aqueous solution.	S-Adenosylmethionine	98-118	catechol-O-methyltransferase	Homo sapiens	0-29
30148963-1	2018	Nicotinamide N-methyltransferase (NNMT) catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to nicotinamide, pyridine, and other structural analogues.	S-Adenosylmethionine	86-106	nicotinamide N-methyltransferase	Homo sapiens	0-32
30148963-1	2018	Nicotinamide N-methyltransferase (NNMT) catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to nicotinamide, pyridine, and other structural analogues.	S-Adenosylmethionine	86-106	nicotinamide N-methyltransferase	Homo sapiens	34-38
30148963-1	2018	Nicotinamide N-methyltransferase (NNMT) catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to nicotinamide, pyridine, and other structural analogues.	S-Adenosylmethionine	108-111	nicotinamide N-methyltransferase	Homo sapiens	0-32
30148963-1	2018	Nicotinamide N-methyltransferase (NNMT) catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to nicotinamide, pyridine, and other structural analogues.	S-Adenosylmethionine	108-111	nicotinamide N-methyltransferase	Homo sapiens	34-38
30044909-1	2018	Nicotinamide- N-methyltransferase (NNMT) catalyzes the irreversible methylation of nicotinamide (NAM) to form N-methyl nicotinamide using S-adenosyl methionine as a methyl donor.	S-Adenosylmethionine	138-159	nicotinamide N-methyltransferase	Homo sapiens	35-39
29431335-7	2018	Ademetionine showed significant improvements in primary efficacy parameters alkaline phosphatase (ALP) and gamma-glutamyltransferase (gammaGT) (P<0.0001).	S-Adenosylmethionine	0-12	alkaline phosphatase, placental	Homo sapiens	76-96
32254503-3	2018	The OECT gate electrode is functionalized with an oligo(ethylene glycol)-terminated self-assembled alkanethiolate monolayer (SAM) for both the immobilization of anti IL-6 antibodies and the inhibition of non-specific biomolecule binding.	S-Adenosylmethionine	125-128	interleukin 6	Homo sapiens	166-170
29731364-1	2018	Nicotinamide N-methyltransferase (NNMT) catalyzes the N-methylation of nicotinamide using S-adenosyl-L-methionine (SAM) as a methyl donor and, through doing so, can modulate cellular methylation potential to impact diverse epigenetic processes.	S-Adenosylmethionine	90-113	nicotinamide N-methyltransferase	Homo sapiens	0-32
29731364-1	2018	Nicotinamide N-methyltransferase (NNMT) catalyzes the N-methylation of nicotinamide using S-adenosyl-L-methionine (SAM) as a methyl donor and, through doing so, can modulate cellular methylation potential to impact diverse epigenetic processes.	S-Adenosylmethionine	90-113	nicotinamide N-methyltransferase	Homo sapiens	34-38
29731364-1	2018	Nicotinamide N-methyltransferase (NNMT) catalyzes the N-methylation of nicotinamide using S-adenosyl-L-methionine (SAM) as a methyl donor and, through doing so, can modulate cellular methylation potential to impact diverse epigenetic processes.	S-Adenosylmethionine	115-118	nicotinamide N-methyltransferase	Homo sapiens	0-32
29731364-1	2018	Nicotinamide N-methyltransferase (NNMT) catalyzes the N-methylation of nicotinamide using S-adenosyl-L-methionine (SAM) as a methyl donor and, through doing so, can modulate cellular methylation potential to impact diverse epigenetic processes.	S-Adenosylmethionine	115-118	nicotinamide N-methyltransferase	Homo sapiens	34-38
29431335-7	2018	Ademetionine showed significant improvements in primary efficacy parameters alkaline phosphatase (ALP) and gamma-glutamyltransferase (gammaGT) (P<0.0001).	S-Adenosylmethionine	0-12	alkaline phosphatase, placental	Homo sapiens	98-101
29431335-8	2018	Although decreases of ALP were higher for subjects initially treated with IV ademetionine, these subjects also had higher baseline values.	S-Adenosylmethionine	77-89	alkaline phosphatase, placental	Homo sapiens	22-25
29880640-4	2018	An MRPP1-MRPP2 subcomplex also catalyzes the formation of 1-methyladenosine/1-methylguanosine at position 9 using S-adenosyl-l-methionine as methyl donor.	S-Adenosylmethionine	114-137	tRNA methyltransferase 10C, mitochondrial RNase P subunit	Homo sapiens	3-8
29880640-4	2018	An MRPP1-MRPP2 subcomplex also catalyzes the formation of 1-methyladenosine/1-methylguanosine at position 9 using S-adenosyl-l-methionine as methyl donor.	S-Adenosylmethionine	114-137	hydroxysteroid 17-beta dehydrogenase 10	Homo sapiens	9-14
29880640-7	2018	The MRPP1 N terminus is involved in tRNA binding and monomer-monomer self-interaction, whereas the C-terminal SPOUT fold contains key residues for S-adenosyl-l-methionine binding and N1-methylation.	S-Adenosylmethionine	147-170	tRNA methyltransferase 10C, mitochondrial RNase P subunit	Homo sapiens	4-9
30093610-1	2018	Nicotinamide N-methyl transferase (NNMT) transfers a methyl group from S-adenosyl-L-methionine (SAM) to nicotinamide (NAM), producing 1-methylnicotinamide (1MNA).	S-Adenosylmethionine	71-94	nicotinamide N-methyltransferase	Homo sapiens	0-33
30093610-1	2018	Nicotinamide N-methyl transferase (NNMT) transfers a methyl group from S-adenosyl-L-methionine (SAM) to nicotinamide (NAM), producing 1-methylnicotinamide (1MNA).	S-Adenosylmethionine	71-94	nicotinamide N-methyltransferase	Homo sapiens	35-39
30093610-1	2018	Nicotinamide N-methyl transferase (NNMT) transfers a methyl group from S-adenosyl-L-methionine (SAM) to nicotinamide (NAM), producing 1-methylnicotinamide (1MNA).	S-Adenosylmethionine	96-99	nicotinamide N-methyltransferase	Homo sapiens	0-33
30093610-1	2018	Nicotinamide N-methyl transferase (NNMT) transfers a methyl group from S-adenosyl-L-methionine (SAM) to nicotinamide (NAM), producing 1-methylnicotinamide (1MNA).	S-Adenosylmethionine	96-99	nicotinamide N-methyltransferase	Homo sapiens	35-39
29891549-1	2018	Glycine N-methyltransferase (GNMT) is the most abundant liver methyltransferase regulating the availability of the biological methyl donor, S-adenosylmethionine (SAM).	S-Adenosylmethionine	140-160	glycine N-methyltransferase	Homo sapiens	0-27
29733835-4	2018	We studied mechanisms of MAFG up-regulation in cholestatic tissues and the pathways by which S-adenosylmethionine (SAMe) and ursodeoxycholic acid (UDCA) prevent the increase in MAFG expression.	S-Adenosylmethionine	93-113	MAF bZIP transcription factor G	Homo sapiens	177-181
30088182-0	2018	The high degree of cystathionine beta-synthase (CBS) activation by S-adenosylmethionine (SAM) may explain naked mole-rat"s distinct methionine metabolite profile compared to mouse.	S-Adenosylmethionine	67-87	cystathionine beta-synthase	Heterocephalus glaber	19-46
30088182-0	2018	The high degree of cystathionine beta-synthase (CBS) activation by S-adenosylmethionine (SAM) may explain naked mole-rat"s distinct methionine metabolite profile compared to mouse.	S-Adenosylmethionine	67-87	cystathionine beta-synthase	Heterocephalus glaber	48-51
29891549-1	2018	Glycine N-methyltransferase (GNMT) is the most abundant liver methyltransferase regulating the availability of the biological methyl donor, S-adenosylmethionine (SAM).	S-Adenosylmethionine	140-160	glycine N-methyltransferase	Homo sapiens	29-33
29891549-1	2018	Glycine N-methyltransferase (GNMT) is the most abundant liver methyltransferase regulating the availability of the biological methyl donor, S-adenosylmethionine (SAM).	S-Adenosylmethionine	162-165	glycine N-methyltransferase	Homo sapiens	0-27
29844127-0	2018	SNHG6 Acts as a Genome-Wide Hypomethylation Trigger via Coupling of miR-1297-Mediated S-Adenosylmethionine-Dependent Positive Feedback Loops.	S-Adenosylmethionine	88-106	small nucleolar RNA host gene 6	Homo sapiens	0-5
29891549-1	2018	Glycine N-methyltransferase (GNMT) is the most abundant liver methyltransferase regulating the availability of the biological methyl donor, S-adenosylmethionine (SAM).	S-Adenosylmethionine	162-165	glycine N-methyltransferase	Homo sapiens	29-33
29844127-0	2018	SNHG6 Acts as a Genome-Wide Hypomethylation Trigger via Coupling of miR-1297-Mediated S-Adenosylmethionine-Dependent Positive Feedback Loops.	S-Adenosylmethionine	88-106	microRNA 1297	Homo sapiens	68-76
29733595-0	2018	Water-Mediated Carbon-Oxygen Hydrogen Bonding Facilitates S-Adenosylmethionine Recognition in the Reactivation Domain of Cobalamin-Dependent Methionine Synthase.	S-Adenosylmethionine	58-78	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	121-160
29896230-1	2018	The aim of the present study was to investigate the effects of S-adenosyl methionine (SAMe) on infectious premature inflammatory factors and uterine contraction, and to further explore its mechanism of action via the transient receptor protein 3 (TRPC3)/protein kinase Cbeta (PKCbeta)/C-kinase-activated protein phosphatase-1 inhibitor of 17 kDa (CPI-17) signaling pathway, following intervention by a TRPC3 inhibitor.	S-Adenosylmethionine	63-84	transient receptor potential cation channel, subfamily C, member 3	Rattus norvegicus	247-252
30116142-2	2018	The physiological actions of methyl donors, such as folic acid, choline, and vitamin B12 on inflammation-related disease have been associated with the synthesis of the universal methyl donor S-adenosyl methionine (SAM).	S-Adenosylmethionine	191-212	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	85-88
30116142-2	2018	The physiological actions of methyl donors, such as folic acid, choline, and vitamin B12 on inflammation-related disease have been associated with the synthesis of the universal methyl donor S-adenosyl methionine (SAM).	S-Adenosylmethionine	214-217	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	85-88
29223141-11	2018	Furthermore, CTL2 may be involved in choline uptake in mitochondria, which is the rate-limiting step in S-adenosylmethionine (SAM) synthesis and DNA methylation.	S-Adenosylmethionine	104-124	solute carrier family 44 member 2	Homo sapiens	13-17
29223141-11	2018	Furthermore, CTL2 may be involved in choline uptake in mitochondria, which is the rate-limiting step in S-adenosylmethionine (SAM) synthesis and DNA methylation.	S-Adenosylmethionine	126-129	solute carrier family 44 member 2	Homo sapiens	13-17
29748795-0	2018	Role of lncRNAs as prognostic markers of hepatic cancer and potential therapeutic targeting by S-adenosylmethionine via inhibiting PI3K/Akt signaling pathways.	S-Adenosylmethionine	95-115	AKT serine/threonine kinase 1	Rattus norvegicus	136-139
29685976-5	2018	Crystal structures showed that compound 4 binds to the PRMT4 active site, displacing strongly the S-adenosyl-l-methionine cofactor, occupying its binding site, and interacting with the arginine substrate site through the cytosine moiety that probes the space filled by a substrate peptide methylation intermediate.	S-Adenosylmethionine	98-121	coactivator associated arginine methyltransferase 1	Homo sapiens	55-60
29904056-3	2018	Pyridone-containing inhibitors such as GSK126 compete with S-adenosylmethionine (SAM) for Ezh2 binding and effectively inhibit PRC2 activity.	S-Adenosylmethionine	59-79	enhancer of zeste 2 polycomb repressive complex 2 subunit	Homo sapiens	90-94
29904056-3	2018	Pyridone-containing inhibitors such as GSK126 compete with S-adenosylmethionine (SAM) for Ezh2 binding and effectively inhibit PRC2 activity.	S-Adenosylmethionine	81-84	enhancer of zeste 2 polycomb repressive complex 2 subunit	Homo sapiens	90-94
29891918-0	2018	Structural basis for the regulation of human 5,10-methylenetetrahydrofolate reductase by phosphorylation and S-adenosylmethionine inhibition.	S-Adenosylmethionine	111-129	methylenetetrahydrofolate reductase	Homo sapiens	45-85
30050996-1	2018	The under-regulation of liver-specific MAT1A gene codifying for S-adenosylmethionine (SAM) synthesizing isozymes MATI/III, and the up-regulation of widely expressed MAT2A, MATII isozyme occurs in hepatocellular carcinoma (HCC).	S-Adenosylmethionine	64-84	methionine adenosyltransferase 1A	Homo sapiens	39-44
30050996-1	2018	The under-regulation of liver-specific MAT1A gene codifying for S-adenosylmethionine (SAM) synthesizing isozymes MATI/III, and the up-regulation of widely expressed MAT2A, MATII isozyme occurs in hepatocellular carcinoma (HCC).	S-Adenosylmethionine	86-89	methionine adenosyltransferase 1A	Homo sapiens	39-44
29802323-2	2018	Viperin belongs to the S-Adenosylmethionine (SAM) superfamily of enzymes known to catalyze a wide variety of radical-mediated reactions.	S-Adenosylmethionine	23-43	radical S-adenosyl methionine domain containing 2	Homo sapiens	0-7
29925952-2	2018	Viperin, a member of the radical S-adenosyl-L-methionine (SAM) superfamily of enzymes, is an interferon-inducible protein implicated in the inhibition of replication of a broad range of RNA and DNA viruses, including dengue virus, West Nile virus, hepatitis C virus, influenza A virus, rabies virus 2 and HIV3,4.	S-Adenosylmethionine	35-56	radical S-adenosyl methionine domain containing 2	Homo sapiens	0-7
29925952-2	2018	Viperin, a member of the radical S-adenosyl-L-methionine (SAM) superfamily of enzymes, is an interferon-inducible protein implicated in the inhibition of replication of a broad range of RNA and DNA viruses, including dengue virus, West Nile virus, hepatitis C virus, influenza A virus, rabies virus 2 and HIV3,4.	S-Adenosylmethionine	58-61	radical S-adenosyl methionine domain containing 2	Homo sapiens	0-7
29872122-1	2018	Nicotinamide N-methyltransferase (NNMT) catalyses the reaction between nicotinamide (NAM) and S-adenosylmethionine to produce 1-methylnicotinamide and S-adenosylhomocysteine.	S-Adenosylmethionine	94-114	nicotinamide N-methyltransferase	Mus musculus	0-32
29872122-1	2018	Nicotinamide N-methyltransferase (NNMT) catalyses the reaction between nicotinamide (NAM) and S-adenosylmethionine to produce 1-methylnicotinamide and S-adenosylhomocysteine.	S-Adenosylmethionine	94-114	nicotinamide N-methyltransferase	Mus musculus	34-38
29802323-2	2018	Viperin belongs to the S-Adenosylmethionine (SAM) superfamily of enzymes known to catalyze a wide variety of radical-mediated reactions.	S-Adenosylmethionine	45-48	radical S-adenosyl methionine domain containing 2	Homo sapiens	0-7
29556105-2	2018	Here we report the toluene-producing enzyme PhdB, a glycyl radical enzyme of bacterial origin that catalyzes phenylacetate decarboxylation, and its cognate activating enzyme PhdA, a radical S-adenosylmethionine enzyme, discovered in two distinct anoxic microbial communities that produce toluene.	S-Adenosylmethionine	190-210	prolyl 4-hydroxylase subunit beta	Homo sapiens	44-48
29724193-10	2018	Of note, in both cell lines CIN knockdown increased active vitamin B6 levels with vitamin B6 being known to be important for S-adenosylmethionine biosynthesis.	S-Adenosylmethionine	127-145	pyridoxal phosphatase	Homo sapiens	28-31
29453849-5	2018	Furthermore, we demonstrate that this process requires conversion of methionine into S-adenosyl methionine (SAM) and its decarboxylation by Spe2.	S-Adenosylmethionine	85-106	salivary protein electrophoretic 2	Mus musculus	140-144
29453849-5	2018	Furthermore, we demonstrate that this process requires conversion of methionine into S-adenosyl methionine (SAM) and its decarboxylation by Spe2.	S-Adenosylmethionine	108-111	salivary protein electrophoretic 2	Mus musculus	140-144
29194039-3	2018	METHODS: We further optimized a previously established high-performance liquid chromatography (HPLC) method by measuring TPMT activity in whole blood instead of isolated erythrocytes, which is based on conversion of 6-mercaptopurine to 6-methylmercaptopurine using S-adenosyl-methionine as methyl donor.	S-Adenosylmethionine	265-286	thiopurine S-methyltransferase	Homo sapiens	121-125
29277012-5	2018	After the double-stranded RNA (dsRNA) with 2 nt 3" overhangs was treated with HENMT1 in the presence of S-adenosyl-L-methionine, the 3" terminal nucleotide of the unmethylated dsRNA could be extended under the catalysis of the poly(U) polymerase in the existence of UTP.	S-Adenosylmethionine	104-127	HEN methyltransferase 1	Homo sapiens	78-84
29519735-4	2018	For proper folding and enzymatic activity, G9a and GLP contain structural zinc fingers, one of them being adjacent to the S-adenosylmethionine binding site.	S-Adenosylmethionine	124-142	euchromatic histone lysine methyltransferase 2	Homo sapiens	43-46
29568838-1	2018	RSAD2 (cig-5), also known as viperin (virus inhibitory protein, endoplasmic reticulum associated, interferon inducible), is a member of the radical S-adenosylmethionine (SAM) superfamily of enzymes.	S-Adenosylmethionine	148-168	radical S-adenosyl methionine domain containing 2	Homo sapiens	0-5
29568838-1	2018	RSAD2 (cig-5), also known as viperin (virus inhibitory protein, endoplasmic reticulum associated, interferon inducible), is a member of the radical S-adenosylmethionine (SAM) superfamily of enzymes.	S-Adenosylmethionine	148-168	radical S-adenosyl methionine domain containing 2	Homo sapiens	7-12
29568838-1	2018	RSAD2 (cig-5), also known as viperin (virus inhibitory protein, endoplasmic reticulum associated, interferon inducible), is a member of the radical S-adenosylmethionine (SAM) superfamily of enzymes.	S-Adenosylmethionine	148-168	radical S-adenosyl methionine domain containing 2	Homo sapiens	29-36
29568838-1	2018	RSAD2 (cig-5), also known as viperin (virus inhibitory protein, endoplasmic reticulum associated, interferon inducible), is a member of the radical S-adenosylmethionine (SAM) superfamily of enzymes.	S-Adenosylmethionine	148-168	radical S-adenosyl methionine domain containing 2	Homo sapiens	38-119
29414770-1	2018	S-Adenosyl-l-homocysteine hydrolase (AdoHcy hydrolase; Sah1 in yeast/AHCY in mammals) degrades AdoHcy, a by-product and strong product inhibitor of S-adenosyl-l-methionine (AdoMet)-dependent methylation reactions, to adenosine and homocysteine (Hcy).	S-Adenosylmethionine	148-171	adenosylhomocysteinase	Saccharomyces cerevisiae S288C	55-59
29414770-1	2018	S-Adenosyl-l-homocysteine hydrolase (AdoHcy hydrolase; Sah1 in yeast/AHCY in mammals) degrades AdoHcy, a by-product and strong product inhibitor of S-adenosyl-l-methionine (AdoMet)-dependent methylation reactions, to adenosine and homocysteine (Hcy).	S-Adenosylmethionine	173-179	adenosylhomocysteinase	Saccharomyces cerevisiae S288C	55-59
29483571-1	2018	Nicotinamide N-methyltransferase (NNMT) is a cytosolic enzyme that catalyzes the transfer of a methyl group from the co-factor S-adenosyl-L-methionine (SAM) onto the substrate, nicotinamide (NA) to form 1-methyl-nicotinamide (MNA).	S-Adenosylmethionine	127-150	nicotinamide N-methyltransferase	Mus musculus	0-32
29275181-4	2018	In mammals, CBS is activated by S-adenosylmethionine (AdoMet), where it can adopt two different conformations (basal and activated), but exists as a unique highly active species in fruit fly Drosophila melanogaster.	S-Adenosylmethionine	32-52	cystathionine beta-synthase	Apis mellifera	12-15
29275181-4	2018	In mammals, CBS is activated by S-adenosylmethionine (AdoMet), where it can adopt two different conformations (basal and activated), but exists as a unique highly active species in fruit fly Drosophila melanogaster.	S-Adenosylmethionine	54-60	cystathionine beta-synthase	Apis mellifera	12-15
29275181-6	2018	In addition, comparison of available CBS structures unveils a substrate-induced closure of the catalytic cavity, which in humans is affected by the AdoMet-dependent regulation and likely impaired by the homocystinuria causing mutation T191M.	S-Adenosylmethionine	148-154	cystathionine beta-synthase	Homo sapiens	37-40
29562169-1	2018	Vitamin B12 functions as a cofactor for methionine synthase to produce the anabolic methyl donor S-adenosylmethionine (SAM) and for methylmalonyl-CoA mutase to catabolize the short-chain fatty acid propionate.	S-Adenosylmethionine	97-117	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	8-11
29562169-1	2018	Vitamin B12 functions as a cofactor for methionine synthase to produce the anabolic methyl donor S-adenosylmethionine (SAM) and for methylmalonyl-CoA mutase to catabolize the short-chain fatty acid propionate.	S-Adenosylmethionine	97-117	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	40-59
29562600-11	2018	The levels of TOC1-positive oligomeric tau were increased in brain lysates from HHCy mice, and treating HHCy mice with S-adenosylmethionine, an intermediate of Hcy, reduced the levels of oligomeric tau to control levels.	S-Adenosylmethionine	119-139	microtubule associated protein tau	Homo sapiens	39-42
29562600-11	2018	The levels of TOC1-positive oligomeric tau were increased in brain lysates from HHCy mice, and treating HHCy mice with S-adenosylmethionine, an intermediate of Hcy, reduced the levels of oligomeric tau to control levels.	S-Adenosylmethionine	119-139	microtubule associated protein tau	Homo sapiens	198-201
29488986-4	2018	Combining this structural sampling with NOE fitting, we demonstrate, for S-adenosylmethionine (aqueous solution at pH 7.0), significant improvements are made to the fit of populations to the experimental data, revealing a strong overall preference for the syn conformation of the adenosyl group relative to the ribose ring, but with less discrimination for the conformation of the ribose ring itself.	S-Adenosylmethionine	73-93	synemin	Homo sapiens	256-259
29545752-3	2018	EPZ015666 is a recently reported PRMT5 inhibitor with a new binding site, which is different from S-adenosylmethionine (SAM)-binding pocket.	S-Adenosylmethionine	98-118	protein arginine methyltransferase 5	Homo sapiens	33-38
29545752-3	2018	EPZ015666 is a recently reported PRMT5 inhibitor with a new binding site, which is different from S-adenosylmethionine (SAM)-binding pocket.	S-Adenosylmethionine	120-123	protein arginine methyltransferase 5	Homo sapiens	33-38
29428575-10	2018	SAM administration significantly inhibited macrophage infiltration in liver and bile duct tissues, down-regulated TNF-alpha levels and up-regulated IL-10 expression in bile duct tissues compared to the IRI group (P < .05).	S-Adenosylmethionine	0-3	tumor necrosis factor	Rattus norvegicus	114-123
29428575-10	2018	SAM administration significantly inhibited macrophage infiltration in liver and bile duct tissues, down-regulated TNF-alpha levels and up-regulated IL-10 expression in bile duct tissues compared to the IRI group (P < .05).	S-Adenosylmethionine	0-3	interleukin 10	Rattus norvegicus	148-153
29483571-1	2018	Nicotinamide N-methyltransferase (NNMT) is a cytosolic enzyme that catalyzes the transfer of a methyl group from the co-factor S-adenosyl-L-methionine (SAM) onto the substrate, nicotinamide (NA) to form 1-methyl-nicotinamide (MNA).	S-Adenosylmethionine	127-150	nicotinamide N-methyltransferase	Mus musculus	34-38
29483571-1	2018	Nicotinamide N-methyltransferase (NNMT) is a cytosolic enzyme that catalyzes the transfer of a methyl group from the co-factor S-adenosyl-L-methionine (SAM) onto the substrate, nicotinamide (NA) to form 1-methyl-nicotinamide (MNA).	S-Adenosylmethionine	152-155	nicotinamide N-methyltransferase	Mus musculus	0-32
29483571-1	2018	Nicotinamide N-methyltransferase (NNMT) is a cytosolic enzyme that catalyzes the transfer of a methyl group from the co-factor S-adenosyl-L-methionine (SAM) onto the substrate, nicotinamide (NA) to form 1-methyl-nicotinamide (MNA).	S-Adenosylmethionine	152-155	nicotinamide N-methyltransferase	Mus musculus	34-38
29320176-1	2018	Nicotinamide N-methyltransferase (NNMT) catalyzes the N-methylation of pyridine-containing compounds using the cofactor S-5"-adenosyl-l-methionine (SAM) as the methyl group donor.	S-Adenosylmethionine	148-151	nicotinamide N-methyltransferase	Homo sapiens	0-32
29320176-1	2018	Nicotinamide N-methyltransferase (NNMT) catalyzes the N-methylation of pyridine-containing compounds using the cofactor S-5"-adenosyl-l-methionine (SAM) as the methyl group donor.	S-Adenosylmethionine	148-151	nicotinamide N-methyltransferase	Homo sapiens	34-38
29416063-0	2018	AhR and SHP regulate phosphatidylcholine and S-adenosylmethionine levels in the one-carbon cycle.	S-Adenosylmethionine	45-65	aryl hydrocarbon receptor	Homo sapiens	0-3
29416063-0	2018	AhR and SHP regulate phosphatidylcholine and S-adenosylmethionine levels in the one-carbon cycle.	S-Adenosylmethionine	45-65	nuclear receptor subfamily 0 group B member 2	Homo sapiens	8-11
29416063-7	2018	This study identifies AhR and SHP as new physiological regulators of PC/SAM levels.	S-Adenosylmethionine	72-75	aryl hydrocarbon receptor	Homo sapiens	22-25
29416063-7	2018	This study identifies AhR and SHP as new physiological regulators of PC/SAM levels.	S-Adenosylmethionine	72-75	nuclear receptor subfamily 0 group B member 2	Homo sapiens	30-33
29305263-0	2018	S-adenosylmethionine reduces the inhibitory effect of Abeta on BDNF expression through decreasing methylation level of BDNF exon IV in rats.	S-Adenosylmethionine	0-20	amyloid beta precursor protein	Rattus norvegicus	54-59
29323674-2	2018	MeC is produced via enzymatic methylation of the C-5 position of cytosine by DNA-methyltransferases (DNMT) which use S-adenosylmethionine (SAM) as a cofactor.	S-Adenosylmethionine	117-137	DNA methyltransferase 1	Homo sapiens	77-99
29323674-2	2018	MeC is produced via enzymatic methylation of the C-5 position of cytosine by DNA-methyltransferases (DNMT) which use S-adenosylmethionine (SAM) as a cofactor.	S-Adenosylmethionine	117-137	DNA methyltransferase 1	Homo sapiens	101-105
29323674-2	2018	MeC is produced via enzymatic methylation of the C-5 position of cytosine by DNA-methyltransferases (DNMT) which use S-adenosylmethionine (SAM) as a cofactor.	S-Adenosylmethionine	139-142	DNA methyltransferase 1	Homo sapiens	77-99
29323674-2	2018	MeC is produced via enzymatic methylation of the C-5 position of cytosine by DNA-methyltransferases (DNMT) which use S-adenosylmethionine (SAM) as a cofactor.	S-Adenosylmethionine	139-142	DNA methyltransferase 1	Homo sapiens	101-105
29209878-0	2018	Cell-Type-Specific Spatiotemporal Expression of Creatine Biosynthetic Enzyme S-adenosylmethionine:guanidinoacetate N-methyltransferase in Developing Mouse Brain.	S-Adenosylmethionine	79-97	guanidinoacetate methyltransferase	Mus musculus	98-134
29209878-1	2018	Creatine is synthesized by S-adenosylmethionine:guanidinoacetate N-methyltransferase (GAMT), and the creatine/phosphocreatine shuttle system mediated by creatine kinase (CK) is essential for storage and regeneration of high-energy phosphates in cells.	S-Adenosylmethionine	27-47	guanidinoacetate methyltransferase	Mus musculus	48-84
29209878-1	2018	Creatine is synthesized by S-adenosylmethionine:guanidinoacetate N-methyltransferase (GAMT), and the creatine/phosphocreatine shuttle system mediated by creatine kinase (CK) is essential for storage and regeneration of high-energy phosphates in cells.	S-Adenosylmethionine	27-47	guanidinoacetate methyltransferase	Mus musculus	86-90
29305263-0	2018	S-adenosylmethionine reduces the inhibitory effect of Abeta on BDNF expression through decreasing methylation level of BDNF exon IV in rats.	S-Adenosylmethionine	0-20	brain-derived neurotrophic factor	Rattus norvegicus	63-67
29305263-0	2018	S-adenosylmethionine reduces the inhibitory effect of Abeta on BDNF expression through decreasing methylation level of BDNF exon IV in rats.	S-Adenosylmethionine	0-20	brain-derived neurotrophic factor	Rattus norvegicus	119-123
29155147-10	2018	NNMT inhibitors reduced intracellular 1-MNA, increased intracellular NAD+ and S-(5"-adenosyl)-l-methionine (SAM), and suppressed lipogenesis in adipocytes.	S-Adenosylmethionine	108-111	nicotinamide N-methyltransferase	Mus musculus	0-4
29154828-0	2018	Interaction assessments of the first S-adenosylmethionine competitive inhibitor and the essential interacting partner methylosome protein 50 with protein arginine methyltransferase 5 by combined computational methods.	S-Adenosylmethionine	39-57	WD repeat domain 77	Homo sapiens	118-140
30097105-3	2018	Our previous work has shown that generating the critical, glycine-centered radical species on CutC requires posttranslational modification by an S-adenosyl-l-methionine (SAM)-dependent radical-activating protein (CutD) harboring an oxygen-sensitive [4Fe-4S] cofactor.	S-Adenosylmethionine	145-168	cutC copper transporter	Homo sapiens	94-98
29154828-0	2018	Interaction assessments of the first S-adenosylmethionine competitive inhibitor and the essential interacting partner methylosome protein 50 with protein arginine methyltransferase 5 by combined computational methods.	S-Adenosylmethionine	39-57	protein arginine methyltransferase 5	Homo sapiens	146-182
29154828-2	2018	In this study, based on the first S-adenosylmethionine (SAM) competitive small molecule inhibitor (17, compound number is from original paper) of PRMT5 reported in our recent paper, we determined the molecular mechanism of 17 interacting with PRMT5 by computational methods.	S-Adenosylmethionine	34-54	protein arginine methyltransferase 5	Homo sapiens	146-151
29154828-2	2018	In this study, based on the first S-adenosylmethionine (SAM) competitive small molecule inhibitor (17, compound number is from original paper) of PRMT5 reported in our recent paper, we determined the molecular mechanism of 17 interacting with PRMT5 by computational methods.	S-Adenosylmethionine	34-54	protein arginine methyltransferase 5	Homo sapiens	243-248
29154828-2	2018	In this study, based on the first S-adenosylmethionine (SAM) competitive small molecule inhibitor (17, compound number is from original paper) of PRMT5 reported in our recent paper, we determined the molecular mechanism of 17 interacting with PRMT5 by computational methods.	S-Adenosylmethionine	56-59	protein arginine methyltransferase 5	Homo sapiens	146-151
29154828-2	2018	In this study, based on the first S-adenosylmethionine (SAM) competitive small molecule inhibitor (17, compound number is from original paper) of PRMT5 reported in our recent paper, we determined the molecular mechanism of 17 interacting with PRMT5 by computational methods.	S-Adenosylmethionine	56-59	protein arginine methyltransferase 5	Homo sapiens	243-248
29119254-5	2018	In this review, we summarize the complex nature of CBS, its multi-domain architecture, the interplay between the three cofactors required for CBS function [heme, pyridoxal-5"-phosphate (PLP), and S-adenosylmethionine (SAM)], as well as the intricate allosteric regulatory mechanism only recently understood, thanks to advances in CBS crystallography.	S-Adenosylmethionine	196-216	cystathionine beta-synthase	Homo sapiens	51-54
29119254-5	2018	In this review, we summarize the complex nature of CBS, its multi-domain architecture, the interplay between the three cofactors required for CBS function [heme, pyridoxal-5"-phosphate (PLP), and S-adenosylmethionine (SAM)], as well as the intricate allosteric regulatory mechanism only recently understood, thanks to advances in CBS crystallography.	S-Adenosylmethionine	218-221	cystathionine beta-synthase	Homo sapiens	51-54
29119254-5	2018	In this review, we summarize the complex nature of CBS, its multi-domain architecture, the interplay between the three cofactors required for CBS function [heme, pyridoxal-5"-phosphate (PLP), and S-adenosylmethionine (SAM)], as well as the intricate allosteric regulatory mechanism only recently understood, thanks to advances in CBS crystallography.	S-Adenosylmethionine	218-221	cystathionine beta-synthase	Homo sapiens	142-145
29119254-5	2018	In this review, we summarize the complex nature of CBS, its multi-domain architecture, the interplay between the three cofactors required for CBS function [heme, pyridoxal-5"-phosphate (PLP), and S-adenosylmethionine (SAM)], as well as the intricate allosteric regulatory mechanism only recently understood, thanks to advances in CBS crystallography.	S-Adenosylmethionine	218-221	cystathionine beta-synthase	Homo sapiens	142-145
29262316-0	2017	S-Adenosylmethionine Synthesis Is Regulated by Selective N6-Adenosine Methylation and mRNA Degradation Involving METTL16 and YTHDC1.	S-Adenosylmethionine	0-20	methyltransferase 16, N6-methyladenosine	Homo sapiens	113-120
29379364-3	2018	S-adenosyl-l-methionine (SAM) is an important intermediate of folic acid pathway and acts as methyl donor and substrate for DNA (cytosine-5)-methyltransferase 3B (DNMT3B - EC 2.1.1.37) de novo methylation processes during embryogenesis.	S-Adenosylmethionine	0-23	DNA methyltransferase 3 beta	Homo sapiens	124-161
29379364-3	2018	S-adenosyl-l-methionine (SAM) is an important intermediate of folic acid pathway and acts as methyl donor and substrate for DNA (cytosine-5)-methyltransferase 3B (DNMT3B - EC 2.1.1.37) de novo methylation processes during embryogenesis.	S-Adenosylmethionine	0-23	DNA methyltransferase 3 beta	Homo sapiens	163-169
29379364-3	2018	S-adenosyl-l-methionine (SAM) is an important intermediate of folic acid pathway and acts as methyl donor and substrate for DNA (cytosine-5)-methyltransferase 3B (DNMT3B - EC 2.1.1.37) de novo methylation processes during embryogenesis.	S-Adenosylmethionine	25-28	DNA methyltransferase 3 beta	Homo sapiens	124-161
29379364-3	2018	S-adenosyl-l-methionine (SAM) is an important intermediate of folic acid pathway and acts as methyl donor and substrate for DNA (cytosine-5)-methyltransferase 3B (DNMT3B - EC 2.1.1.37) de novo methylation processes during embryogenesis.	S-Adenosylmethionine	25-28	DNA methyltransferase 3 beta	Homo sapiens	163-169
29262316-0	2017	S-Adenosylmethionine Synthesis Is Regulated by Selective N6-Adenosine Methylation and mRNA Degradation Involving METTL16 and YTHDC1.	S-Adenosylmethionine	0-20	YTH domain containing 1	Homo sapiens	125-131
29416626-1	2018	Glycine N-methyltransferase is a tumor suppressor gene for hepatocellular carcinoma, which can activate DNA methylation by inducing the S-adenosylmethionine to S-adenosylhomocystine.	S-Adenosylmethionine	136-156	glycine N-methyltransferase	Mus musculus	0-27
29232372-6	2017	Serum levels of S-adenosyl methionine (SAM), the downstream product of MTR, were also decreased in PNA mice and women with the hyperandrogenic phenotype of PCOS.	S-Adenosylmethionine	16-37	telomerase RNA component	Mus musculus	71-74
29096064-7	2017	A crystal structure of the AprA MT1-GNAT di-domain with bound Mn2+, malonate, and the methyl donor S-adenosylmethionine (SAM) reveals that the malonyl substrate is a bidentate metal ligand, indicating that the metal acts as a Lewis acid to promote methylation of the malonyl alpha-carbon.	S-Adenosylmethionine	99-119	metallothionein 1I, pseudogene	Homo sapiens	32-35
29099132-6	2017	Using biotinylated histone H4 as a substrate, and S-adenosyl-l-methionine as a methyl donor, PRMT5 symmetrically dimethylated H4 at arginine (R) 3.	S-Adenosylmethionine	50-73	protein arginine methyltransferase 5	Homo sapiens	93-98
29037594-8	2017	Methyl donor S-adenosyl-L-methionine (SAM) corrected miR-200b promoter hypomethylaton and rescued endothelial function.	S-Adenosylmethionine	13-36	microRNA 200b	Homo sapiens	53-61
29037594-8	2017	Methyl donor S-adenosyl-L-methionine (SAM) corrected miR-200b promoter hypomethylaton and rescued endothelial function.	S-Adenosylmethionine	38-41	microRNA 200b	Homo sapiens	53-61
29225734-8	2017	In fact, downregulation of S-adenosylmethionine synthesis is the first functional effect directly ascribed to PDRG1.	S-Adenosylmethionine	27-47	p53 and DNA damage regulated 1	Homo sapiens	110-115
29123071-0	2017	SAMTOR is an S-adenosylmethionine sensor for the mTORC1 pathway.	S-Adenosylmethionine	15-33	CREB regulated transcription coactivator 1	Mus musculus	49-55
28818801-1	2017	A liquid chromatography-tandem mass spectrometry (LC-MS/MS) method was developed for the determination of thiopurine methyltransferase (TPMT) activity in human whole blood lysate, based on conversion of 6-mercaptopurine (6-MP) by TPMT to 6-methylmercaptopurine (6-MMP) using S-adenosyl-l-methionine (SAM) as the methyl donor.	S-Adenosylmethionine	275-298	thiopurine S-methyltransferase	Homo sapiens	106-134
29076773-1	2017	PRMT5 catalyzes the mono- and symmetric dimethylation of the arginine N-guanidine group of a wide variety of target proteins including histones, transcriptional elongation factors, kinases and tumor suppressors by utilizing the essential co-factor S-adenosylmethionine as methyl source.	S-Adenosylmethionine	250-268	protein arginine methyltransferase 5	Homo sapiens	0-5
29021282-6	2017	Mechanistically, we discover that the enzyme converting methionine to S-adenosylmethionine in mESCs, methionine adenosyltransferase 2a (MAT2a), is under control of Myc and SIRT1.	S-Adenosylmethionine	70-90	methionine adenosyltransferase II, alpha	Mus musculus	136-141
29021282-6	2017	Mechanistically, we discover that the enzyme converting methionine to S-adenosylmethionine in mESCs, methionine adenosyltransferase 2a (MAT2a), is under control of Myc and SIRT1.	S-Adenosylmethionine	70-90	myelocytomatosis oncogene	Mus musculus	164-167
29021282-6	2017	Mechanistically, we discover that the enzyme converting methionine to S-adenosylmethionine in mESCs, methionine adenosyltransferase 2a (MAT2a), is under control of Myc and SIRT1.	S-Adenosylmethionine	70-90	sirtuin 1	Mus musculus	172-177
28726800-1	2017	Nicotinamide N-methyltransferase (NNMT) transfers the methyl from S-adenosyl-L-methionine (SAM) to nicotinamide (NA) to produce S-adenosyl-L-homocysteine (SAH) and 1-methylnicotinamide (MeN).	S-Adenosylmethionine	66-89	nicotinamide N-methyltransferase	Homo sapiens	0-32
28726800-1	2017	Nicotinamide N-methyltransferase (NNMT) transfers the methyl from S-adenosyl-L-methionine (SAM) to nicotinamide (NA) to produce S-adenosyl-L-homocysteine (SAH) and 1-methylnicotinamide (MeN).	S-Adenosylmethionine	66-89	nicotinamide N-methyltransferase	Homo sapiens	34-38
28726800-1	2017	Nicotinamide N-methyltransferase (NNMT) transfers the methyl from S-adenosyl-L-methionine (SAM) to nicotinamide (NA) to produce S-adenosyl-L-homocysteine (SAH) and 1-methylnicotinamide (MeN).	S-Adenosylmethionine	91-94	nicotinamide N-methyltransferase	Homo sapiens	0-32
28726800-1	2017	Nicotinamide N-methyltransferase (NNMT) transfers the methyl from S-adenosyl-L-methionine (SAM) to nicotinamide (NA) to produce S-adenosyl-L-homocysteine (SAH) and 1-methylnicotinamide (MeN).	S-Adenosylmethionine	91-94	nicotinamide N-methyltransferase	Homo sapiens	34-38
28726800-5	2017	Lentivirus-mediated knockdown of Nnmt in the dorsomedial striatum (DMS) attenuated cocaine conditioned place preference (CPP) reward, but increased striatal SAM/SAH ratio levels as well as Rac1 and RhoA activities.	S-Adenosylmethionine	157-160	nicotinamide N-methyltransferase	Homo sapiens	33-37
28818801-1	2017	A liquid chromatography-tandem mass spectrometry (LC-MS/MS) method was developed for the determination of thiopurine methyltransferase (TPMT) activity in human whole blood lysate, based on conversion of 6-mercaptopurine (6-MP) by TPMT to 6-methylmercaptopurine (6-MMP) using S-adenosyl-l-methionine (SAM) as the methyl donor.	S-Adenosylmethionine	275-298	thiopurine S-methyltransferase	Homo sapiens	136-140
28818801-1	2017	A liquid chromatography-tandem mass spectrometry (LC-MS/MS) method was developed for the determination of thiopurine methyltransferase (TPMT) activity in human whole blood lysate, based on conversion of 6-mercaptopurine (6-MP) by TPMT to 6-methylmercaptopurine (6-MMP) using S-adenosyl-l-methionine (SAM) as the methyl donor.	S-Adenosylmethionine	300-303	thiopurine S-methyltransferase	Homo sapiens	106-134
28818801-1	2017	A liquid chromatography-tandem mass spectrometry (LC-MS/MS) method was developed for the determination of thiopurine methyltransferase (TPMT) activity in human whole blood lysate, based on conversion of 6-mercaptopurine (6-MP) by TPMT to 6-methylmercaptopurine (6-MMP) using S-adenosyl-l-methionine (SAM) as the methyl donor.	S-Adenosylmethionine	300-303	thiopurine S-methyltransferase	Homo sapiens	136-140
28927791-1	2017	Protein arginine methyltransferase 1 (PRMT1) catalyses the methylation of substrate arginine by transferring the methyl group from SAM (S-adenosyl-l-methionine), which leads to the formation of S-adenosyl homocysteine (SAH) and methylated arginine.	S-Adenosylmethionine	136-159	protein arginine methyltransferase 1	Homo sapiens	0-36
28927791-1	2017	Protein arginine methyltransferase 1 (PRMT1) catalyses the methylation of substrate arginine by transferring the methyl group from SAM (S-adenosyl-l-methionine), which leads to the formation of S-adenosyl homocysteine (SAH) and methylated arginine.	S-Adenosylmethionine	136-159	protein arginine methyltransferase 1	Homo sapiens	38-43
29056905-3	2017	Deficiency of adenosyl methionine results from increased polyamine biosynthesis by infected host cells, causing increased activity of ornithine decarboxylase, decreased nitric oxide and peroxynitrate formation and impaired immune reactions.	S-Adenosylmethionine	14-33	ornithine decarboxylase 1	Homo sapiens	134-157
28923203-7	2017	Accordingly, treatment with the EZH2 inhibitor, selective S-adenosyl-methionine-competitive small-molecule (GSK126), or the DNA methylation inhibitor, 5-Aza-2"-deoxycytidine, partially restored miR-34a levels in human CCA cells.	S-Adenosylmethionine	58-79	microRNA 34a	Homo sapiens	194-201
28880543-1	2017	Human methionine S-adenosyltransferase (MAT2A) catalyzes the formation of S-adenosylmethionine (SAM) from ATP and methionine.	S-Adenosylmethionine	74-94	methionine adenosyltransferase 2A	Homo sapiens	40-45
28880543-1	2017	Human methionine S-adenosyltransferase (MAT2A) catalyzes the formation of S-adenosylmethionine (SAM) from ATP and methionine.	S-Adenosylmethionine	96-99	methionine adenosyltransferase 2A	Homo sapiens	40-45
28747433-3	2017	TsrM is a member of the radical S-adenosylmethionine (SAM) superfamily of enzymes, but it does not catalyze the formation of 5"-deoxyadenosin-5"-yl or any other SAM-derived radical.	S-Adenosylmethionine	32-52	TSRM	Homo sapiens	0-4
28720493-1	2017	Nicotinamide N-methyltransferase (NNMT) is a S-adenosyl-l-methionine (SAM)-dependent enzyme that catalyzes N-methylation of nicotinamide (NA) and other pyridines to form N-methyl pyridinium ions.	S-Adenosylmethionine	45-68	nicotinamide N-methyltransferase	Mus musculus	0-32
28720493-1	2017	Nicotinamide N-methyltransferase (NNMT) is a S-adenosyl-l-methionine (SAM)-dependent enzyme that catalyzes N-methylation of nicotinamide (NA) and other pyridines to form N-methyl pyridinium ions.	S-Adenosylmethionine	45-68	nicotinamide N-methyltransferase	Mus musculus	34-38
28720493-1	2017	Nicotinamide N-methyltransferase (NNMT) is a S-adenosyl-l-methionine (SAM)-dependent enzyme that catalyzes N-methylation of nicotinamide (NA) and other pyridines to form N-methyl pyridinium ions.	S-Adenosylmethionine	70-73	nicotinamide N-methyltransferase	Mus musculus	0-32
28720493-1	2017	Nicotinamide N-methyltransferase (NNMT) is a S-adenosyl-l-methionine (SAM)-dependent enzyme that catalyzes N-methylation of nicotinamide (NA) and other pyridines to form N-methyl pyridinium ions.	S-Adenosylmethionine	70-73	nicotinamide N-methyltransferase	Mus musculus	34-38
28870318-7	2017	Furthermore, the inhibition assay study demonstrates that SGI-1027 can inhibit the DNMT 1 activity with the IC50 values of 6 muM in the presence of 160 muM S-adenosylmethionine.	S-Adenosylmethionine	156-176	semenogelin 1	Homo sapiens	58-61
28870318-7	2017	Furthermore, the inhibition assay study demonstrates that SGI-1027 can inhibit the DNMT 1 activity with the IC50 values of 6 muM in the presence of 160 muM S-adenosylmethionine.	S-Adenosylmethionine	156-176	DNA methyltransferase 1	Homo sapiens	83-89
29037129-1	2017	Cystathionine beta-synthase (CBS) domains discovered 20 years ago can bind different adenosine derivatives (AMP, ADP, ATP, S-adenosylmethionine, NAD, diadenosine polyphosphates) and thus regulate the activities of numerous proteins.	S-Adenosylmethionine	123-143	cystathionine beta-synthase	Homo sapiens	0-27
28747433-3	2017	TsrM is a member of the radical S-adenosylmethionine (SAM) superfamily of enzymes, but it does not catalyze the formation of 5"-deoxyadenosin-5"-yl or any other SAM-derived radical.	S-Adenosylmethionine	54-57	TSRM	Homo sapiens	0-4
27232191-1	2017	A group of homologous nucleic acid modification enzymes called Dnmt2, Trdmt1, Pmt1, DnmA, and Ehmet in different model organisms catalyze the transfer of a methyl group from the cofactor S-adenosyl-methionine (SAM) to the carbon-5 of cytosine residues.	S-Adenosylmethionine	187-208	tRNA aspartic acid methyltransferase 1	Homo sapiens	63-68
27232191-1	2017	A group of homologous nucleic acid modification enzymes called Dnmt2, Trdmt1, Pmt1, DnmA, and Ehmet in different model organisms catalyze the transfer of a methyl group from the cofactor S-adenosyl-methionine (SAM) to the carbon-5 of cytosine residues.	S-Adenosylmethionine	187-208	tRNA aspartic acid methyltransferase 1	Homo sapiens	70-76
30023734-5	2017	Furthermore, the contributions of the cofactor S-adenosylmethionine (SAM) to the thermodynamic stability of TPMT were investigated, but only a modest stabilizing effect was observed.	S-Adenosylmethionine	47-67	thiopurine S-methyltransferase	Homo sapiens	108-112
28876240-2	2017	The NS5 methyltransferase contains a bound S-adenosyl-L-methionine (SAM) co-substrate.	S-Adenosylmethionine	45-66	Raf-1 proto-oncogene, serine/threonine kinase	Homo sapiens	4-7
28876240-2	2017	The NS5 methyltransferase contains a bound S-adenosyl-L-methionine (SAM) co-substrate.	S-Adenosylmethionine	68-71	Raf-1 proto-oncogene, serine/threonine kinase	Homo sapiens	4-7
28835163-2	2017	While DNA sequence variation explains some of the observed variability in response, epigenetic patterns present another promising avenue of inquiry due to the biological links between the PPAR-alpha pathway, homocysteine and S-adenosylmethionine - a source of methyl groups for the DNA methylation reaction.	S-Adenosylmethionine	225-245	peroxisome proliferator activated receptor alpha	Homo sapiens	188-198
30023734-5	2017	Furthermore, the contributions of the cofactor S-adenosylmethionine (SAM) to the thermodynamic stability of TPMT were investigated, but only a modest stabilizing effect was observed.	S-Adenosylmethionine	69-72	thiopurine S-methyltransferase	Homo sapiens	108-112
29707653-6	2017	With respect to 1-carbon metabolism, down-regulation of Chka, Chkb, Pcty1a, Gnmt and Ahcy with concurrent upregulation of Mat2a suggests a drive to maintain S-adenosylmethionine levels.	S-Adenosylmethionine	159-177	methionine adenosyltransferase 2A	Homo sapiens	122-127
28553945-0	2017	Targeting S-adenosylmethionine biosynthesis with a novel allosteric inhibitor of Mat2A.	S-Adenosylmethionine	12-30	methionine adenosyltransferase 2A	Homo sapiens	81-86
28656194-9	2017	In addition, we found that treatment with NaHS (a H2S donor) or S-adenosyl-L-methionine (SAM, a CBS agonist) mitigated OGD-induced ER stress, as well as the NO level, nNOS activity and AMPK phosphorylation in PC12 cells.	S-Adenosylmethionine	64-87	cystathionine beta-synthase	Homo sapiens	96-99
28656194-9	2017	In addition, we found that treatment with NaHS (a H2S donor) or S-adenosyl-L-methionine (SAM, a CBS agonist) mitigated OGD-induced ER stress, as well as the NO level, nNOS activity and AMPK phosphorylation in PC12 cells.	S-Adenosylmethionine	89-92	cystathionine beta-synthase	Homo sapiens	96-99
28656194-9	2017	In addition, we found that treatment with NaHS (a H2S donor) or S-adenosyl-L-methionine (SAM, a CBS agonist) mitigated OGD-induced ER stress, as well as the NO level, nNOS activity and AMPK phosphorylation in PC12 cells.	S-Adenosylmethionine	89-92	nitric oxide synthase 1	Homo sapiens	167-171
28821266-6	2017	Administration of S-adenosyl-L-methionine (SAM), a CBS-specific agonist, or sodium hydrosulfide (NaHS), a classical exogenous H2S donor, not only restored brain and plasma H2S content but also attenuated brain oedema, microglial accumulation and neurological deficits at 1 day post-ICH by inhibiting the P2X7R/NLRP3 inflammasome cascade.	S-Adenosylmethionine	18-41	NLR family pyrin domain containing 3	Homo sapiens	310-315
28821266-6	2017	Administration of S-adenosyl-L-methionine (SAM), a CBS-specific agonist, or sodium hydrosulfide (NaHS), a classical exogenous H2S donor, not only restored brain and plasma H2S content but also attenuated brain oedema, microglial accumulation and neurological deficits at 1 day post-ICH by inhibiting the P2X7R/NLRP3 inflammasome cascade.	S-Adenosylmethionine	43-46	NLR family pyrin domain containing 3	Homo sapiens	310-315
29108270-0	2017	S-adenosylmethionine and methylthioadenosine inhibit cancer metastasis by targeting microRNA 34a/b-methionine adenosyltransferase 2A/2B axis.	S-Adenosylmethionine	0-20	methionine adenosyltransferase 2A	Homo sapiens	99-132
29108270-3	2017	In the same model, S-adenosylmethionine (SAMe) and methylthioadenosine (MTA) inhibited IL-6/STAT3 and lowered tumor burden.	S-Adenosylmethionine	19-39	interleukin 6	Homo sapiens	87-91
29108270-3	2017	In the same model, S-adenosylmethionine (SAMe) and methylthioadenosine (MTA) inhibited IL-6/STAT3 and lowered tumor burden.	S-Adenosylmethionine	19-39	signal transducer and activator of transcription 3	Homo sapiens	92-97
28634235-6	2017	Using a combination of MS, isotope labeling, and 1H and 13C NMR techniques, we established that the major product, MftA*, is a tyramine-valine-cross-linked peptide formed by MftC through two S-adenosylmethionine-dependent turnovers.	S-Adenosylmethionine	193-211	solute carrier family 25 member 32	Homo sapiens	174-178
28708394-2	2017	Viperin is a member of the radical S-adenosyl-l-methionine (SAM) superfamily of enzymes, which typically employ a 4Fe-4S cluster to reductively cleave SAM to initiate chemistry.	S-Adenosylmethionine	37-58	radical S-adenosyl methionine domain containing 2	Homo sapiens	0-7
28708394-2	2017	Viperin is a member of the radical S-adenosyl-l-methionine (SAM) superfamily of enzymes, which typically employ a 4Fe-4S cluster to reductively cleave SAM to initiate chemistry.	S-Adenosylmethionine	60-63	radical S-adenosyl methionine domain containing 2	Homo sapiens	0-7
28748147-1	2017	Methionine adenosyltransferase (MAT) I/III deficiency is an inborn error of metabolism caused by mutations in MAT1A, encoding the catalytic subunit of MAT responsible for the synthesis of S-adenosylmethionine, and is characterized by persistent hypermethioninemia.	S-Adenosylmethionine	188-208	methionine adenosyltransferase 1A	Homo sapiens	110-115
28470989-3	2017	The formation of these newly discovered methylated metabolites from reactions involving trivalent phenylarsonous acid substrates, S-adenosylmethionine, and the arsenic (+3 oxidation state) methyltransferase enzyme As3MT suggests that these compounds are formed by addition of a methyl group to a trivalent phenylarsenical substrate in an enzymatic process.	S-Adenosylmethionine	130-150	arsenite methyltransferase	Gallus gallus	160-206
28470989-3	2017	The formation of these newly discovered methylated metabolites from reactions involving trivalent phenylarsonous acid substrates, S-adenosylmethionine, and the arsenic (+3 oxidation state) methyltransferase enzyme As3MT suggests that these compounds are formed by addition of a methyl group to a trivalent phenylarsenical substrate in an enzymatic process.	S-Adenosylmethionine	130-150	arsenite methyltransferase	Gallus gallus	214-219
28515364-4	2017	NNMT depletes S-adenosyl methionine (SAM), a methyl donor generated from methionine.	S-Adenosylmethionine	14-35	nicotinamide N-methyltransferase	Homo sapiens	0-4
27678102-5	2017	We postulate that alterations in the micronutrient metabolism may affect the regulation of enzymes, methionine adenosyltransferase ( MAT2A), and SAH-hydrolase ( AHCY), involved in the production of methyl donor S-adenosylmethionine (SAM), thereby influencing the methylation potential (MP) in the placenta of women delivering preterm.	S-Adenosylmethionine	211-231	methionine adenosyltransferase 2A	Homo sapiens	133-138
27678102-5	2017	We postulate that alterations in the micronutrient metabolism may affect the regulation of enzymes, methionine adenosyltransferase ( MAT2A), and SAH-hydrolase ( AHCY), involved in the production of methyl donor S-adenosylmethionine (SAM), thereby influencing the methylation potential (MP) in the placenta of women delivering preterm.	S-Adenosylmethionine	211-231	adenosylhomocysteinase	Homo sapiens	161-165
27678102-5	2017	We postulate that alterations in the micronutrient metabolism may affect the regulation of enzymes, methionine adenosyltransferase ( MAT2A), and SAH-hydrolase ( AHCY), involved in the production of methyl donor S-adenosylmethionine (SAM), thereby influencing the methylation potential (MP) in the placenta of women delivering preterm.	S-Adenosylmethionine	233-236	methionine adenosyltransferase 2A	Homo sapiens	133-138
27678102-5	2017	We postulate that alterations in the micronutrient metabolism may affect the regulation of enzymes, methionine adenosyltransferase ( MAT2A), and SAH-hydrolase ( AHCY), involved in the production of methyl donor S-adenosylmethionine (SAM), thereby influencing the methylation potential (MP) in the placenta of women delivering preterm.	S-Adenosylmethionine	233-236	adenosylhomocysteinase	Homo sapiens	161-165
28515364-4	2017	NNMT depletes S-adenosyl methionine (SAM), a methyl donor generated from methionine.	S-Adenosylmethionine	37-40	nicotinamide N-methyltransferase	Homo sapiens	0-4
27939670-6	2017	The catfish Comt shared conserved putative structural regions important for S-adenosyl methionine (AdoMet)- and catechol-binding, transmembrane regions, two glycosylation sites (N-65 and N-91) at the N-terminus and two phosphorylation sites (Ser-235 and Thr-240) at the C-terminus.	S-Adenosylmethionine	99-105	catechol-O-methyltransferase	Homo sapiens	12-16
28468239-2	2017	Diet intake of choline can modulate methylation because, via betaine homocysteine methyltransferase (BHMT), this nutrient (and its metabolite, betaine) regulate the concentrations of S-adenosylhomocysteine and S-adenosylmethionine.	S-Adenosylmethionine	210-230	betaine--homocysteine S-methyltransferase	Homo sapiens	61-99
27717843-6	2017	The active site of LIAS protein was mapped and docked with S-Adenosyl Methionine (SAM) using GOLD software.	S-Adenosylmethionine	59-80	lipoic acid synthetase	Homo sapiens	19-23
28448141-0	2017	Correction to Design of Potent and Druglike Nonphenolic Inhibitors for Catechol O-Methyltransferase Derived from a Fragment Screening Approach Targeting the S-Adenosyl-l-methionine Pocket.	S-Adenosylmethionine	157-180	catechol-O-methyltransferase	Homo sapiens	71-99
28468239-2	2017	Diet intake of choline can modulate methylation because, via betaine homocysteine methyltransferase (BHMT), this nutrient (and its metabolite, betaine) regulate the concentrations of S-adenosylhomocysteine and S-adenosylmethionine.	S-Adenosylmethionine	210-230	betaine--homocysteine S-methyltransferase	Homo sapiens	101-105
28281193-7	2017	Co-treatment with antioxidants, tocopheryl acetate (TA) and S-adenosylmethionine (SAM) effectively attenuated expression of Nrf2 and 8-OHdG in H2O2-treated cells.	S-Adenosylmethionine	60-80	NFE2 like bZIP transcription factor 2	Homo sapiens	124-128
27981425-0	2017	1H, 15N, 13C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-L-methionine and 3,5-dinitrocatechol.	S-Adenosylmethionine	106-129	catechol-O-methyltransferase	Homo sapiens	61-89
27981425-4	2017	Here we report the backbone 1H, 15N and 13C chemical shift assignments of S-COMT in complex with S-adenosyl-L-methionine, 3,5-dinitrocatechol and Mg2+.	S-Adenosylmethionine	97-120	catechol-O-methyltransferase	Homo sapiens	76-80
28281193-7	2017	Co-treatment with antioxidants, tocopheryl acetate (TA) and S-adenosylmethionine (SAM) effectively attenuated expression of Nrf2 and 8-OHdG in H2O2-treated cells.	S-Adenosylmethionine	82-85	NFE2 like bZIP transcription factor 2	Homo sapiens	124-128
28238725-3	2017	A subset of these iterative PKSs (iPKSs) contains a C-methyltransferase (CMeT) domain that adds one or more S-adenosylmethionine (SAM)-derived methyl groups to the carbon framework.	S-Adenosylmethionine	108-128	MET proto-oncogene, receptor tyrosine kinase	Homo sapiens	73-77
28238725-3	2017	A subset of these iterative PKSs (iPKSs) contains a C-methyltransferase (CMeT) domain that adds one or more S-adenosylmethionine (SAM)-derived methyl groups to the carbon framework.	S-Adenosylmethionine	130-133	MET proto-oncogene, receptor tyrosine kinase	Homo sapiens	73-77
28126738-4	2017	PRDM9 automethylation is abolished by a single active-site mutation, C321P, also known to disrupt interactions with S-adenosylmethionine.	S-Adenosylmethionine	116-136	PR/SET domain 9	Homo sapiens	0-5
28165739-0	2017	Discovery of Novel Disruptor of Silencing Telomeric 1-Like (DOT1L) Inhibitors using a Target-Specific Scoring Function for the (S)-Adenosyl-l-methionine (SAM)-Dependent Methyltransferase Family.	S-Adenosylmethionine	127-152	DOT1 like histone lysine methyltransferase	Homo sapiens	60-65
28165739-3	2017	Here, we report the development and application of a target-specific scoring function, the SAM score, for (S)-adenosyl-l-methionine (SAM)-dependent methyltransferases, for the discovery of novel DOT1L inhibitors.	S-Adenosylmethionine	106-131	DOT1 like histone lysine methyltransferase	Homo sapiens	195-200
28303926-7	2017	Our results showed that MDR (P-gp overexpressing) cells have a different metabolic profile from their drug-sensitive counterparts, demonstrating decreases in the pentose phosphate pathway and oxidative phosphorylation rate; increases in glutathione metabolism and glycolysis; and alterations in the methionine/S-adenosylmethionine pathway.	S-Adenosylmethionine	312-330	ATP binding cassette subfamily B member 1	Homo sapiens	29-33
27986851-5	2017	We show that Trm112 is important for Trm11 enzymatic activity by influencing S-adenosyl-L-methionine binding and by contributing to tRNA binding.	S-Adenosylmethionine	79-100	tRNA methyltransferase activator subunit 11-2	Homo sapiens	13-19
28118529-2	2017	The SLC25A26 gene encodes the mitochondrial carrier that catalyzes the import of S-adenosylmethionine (SAM) into the mitochondrial matrix, required for mitochondrial methylation processes, and is down-regulated in cervical cancer cells.	S-Adenosylmethionine	81-101	solute carrier family 25 member 26	Homo sapiens	4-12
27169843-6	2017	The DNA-damaging agent S-adenosylmethionine suppresses BLM expression, leading to the inhibition of cell growth following accumulation of DNA damage.	S-Adenosylmethionine	25-43	BLM RecQ like helicase	Homo sapiens	55-58
27986851-5	2017	We show that Trm112 is important for Trm11 enzymatic activity by influencing S-adenosyl-L-methionine binding and by contributing to tRNA binding.	S-Adenosylmethionine	79-100	tRNA methyltransferase 11 homolog	Homo sapiens	13-18
27997103-1	2017	Phenylethanolamine N-methyltransferase (PNMT) catalyzes the S-adenosyl-l-methionine (SAM)-dependent conversion of norepinephrine to epinephrine.	S-Adenosylmethionine	60-83	phenylethanolamine N-methyltransferase	Homo sapiens	0-38
27997103-1	2017	Phenylethanolamine N-methyltransferase (PNMT) catalyzes the S-adenosyl-l-methionine (SAM)-dependent conversion of norepinephrine to epinephrine.	S-Adenosylmethionine	60-83	phenylethanolamine N-methyltransferase	Homo sapiens	40-44
27997103-1	2017	Phenylethanolamine N-methyltransferase (PNMT) catalyzes the S-adenosyl-l-methionine (SAM)-dependent conversion of norepinephrine to epinephrine.	S-Adenosylmethionine	85-88	phenylethanolamine N-methyltransferase	Homo sapiens	0-38
27997103-1	2017	Phenylethanolamine N-methyltransferase (PNMT) catalyzes the S-adenosyl-l-methionine (SAM)-dependent conversion of norepinephrine to epinephrine.	S-Adenosylmethionine	85-88	phenylethanolamine N-methyltransferase	Homo sapiens	40-44
27865712-2	2017	Here, a focused metabolomics approach was used to identify changes in folate catabolism as well as the S-adenosylmethionine (SAM) cycle following NAT1 knockdown with shRNA.	S-Adenosylmethionine	105-123	N-acetyltransferase 1	Homo sapiens	146-150
28028175-8	2017	Specifically, we observe that reduced expression of SIN3 leads to an increase in S-adenosylmethionine (SAM), which is the major cellular donor of methyl groups for protein modification.	S-Adenosylmethionine	81-101	SIN3 transcription regulator family member A	Homo sapiens	52-56
28028175-8	2017	Specifically, we observe that reduced expression of SIN3 leads to an increase in S-adenosylmethionine (SAM), which is the major cellular donor of methyl groups for protein modification.	S-Adenosylmethionine	103-106	SIN3 transcription regulator family member A	Homo sapiens	52-56
28050904-3	2017	A high specificity of the sensor chip to detect cortisol with a detection limit of 3 pg/mL was achieved by conjugating anticortisol antibody (anti-CAB) on top of gold (Au) microelectrodes using 3,3"-dithiodipropionic acid di(N-hydroxysuccinimide ester (DTSP) as a self-assembled monolayer (SAM) agent.	S-Adenosylmethionine	290-293	neural proliferation, differentiation and control 1	Homo sapiens	147-150
28191311-18	2017	It is noteworthy that DNMT3A, which utilizes S-adenosylmethionine generated in the methionine cycle, was greater in OVE and OVE + SM indicating higher-energy diets might enhance DNA methylation, thus, Met utilization.	S-Adenosylmethionine	45-65	DNA methyltransferase 3 alpha	Bos taurus	22-28
27826992-1	2017	Catechol-O-methyltransferase, COMT, is an important phase II enzyme catalyzing the transfer of a methyl-group from S-adenosylmethionine to a catechol-containing substrate molecule.	S-Adenosylmethionine	115-135	catechol-O-methyltransferase	Homo sapiens	0-28
27826992-1	2017	Catechol-O-methyltransferase, COMT, is an important phase II enzyme catalyzing the transfer of a methyl-group from S-adenosylmethionine to a catechol-containing substrate molecule.	S-Adenosylmethionine	115-135	catechol-O-methyltransferase	Homo sapiens	30-34
28293840-4	2017	The first is the biosynthesis of 1-aminocyclopropane-1-carboxylic acid (ACC) from S-Adenosyl-Methionine (SAM), a common precursor in many metabolic pathways, which is catalyzed by ACC synthase (ACS).	S-Adenosylmethionine	82-103	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	180-192
27940170-2	2017	As methionine can alter S-adenosylmethionine (SAM) and S-adenosylhomocysteine (SAH), the substrate and product of DNA methyltransferase-1 (DNMT1), we hypothesized that MR diet alters DNA methylation.	S-Adenosylmethionine	24-44	DNA methyltransferase (cytosine-5) 1	Mus musculus	139-144
27940170-2	2017	As methionine can alter S-adenosylmethionine (SAM) and S-adenosylhomocysteine (SAH), the substrate and product of DNA methyltransferase-1 (DNMT1), we hypothesized that MR diet alters DNA methylation.	S-Adenosylmethionine	46-49	DNA methyltransferase (cytosine-5) 1	Mus musculus	139-144
28220408-5	2017	METHODS: Stable-isotope-labeled 13C2-guanidinoacetate and 2H3-S-adenosylmethionine (SAM) were used, which are converted by GAMT present in lymphocyte extracts into 2H3-13C2-creatine.	S-Adenosylmethionine	84-87	guanidinoacetate N-methyltransferase	Homo sapiens	123-127
27899265-6	2017	Further binding mode analysis suggested these molecules inhibit DNMT3A activity through binding the S-adenosyl-l-methionine (SAM) pocket.	S-Adenosylmethionine	100-123	DNA methyltransferase 3 alpha	Homo sapiens	64-70
27899265-6	2017	Further binding mode analysis suggested these molecules inhibit DNMT3A activity through binding the S-adenosyl-l-methionine (SAM) pocket.	S-Adenosylmethionine	125-128	DNA methyltransferase 3 alpha	Homo sapiens	64-70
28420001-3	2017	Nicotinamide N-methyltransferase (NNMT) decreases histone methylation in several cancer cells by altering the cellular ratio of S-adenosylmethionine (SAM) to S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	128-148	nicotinamide N-methyltransferase	Homo sapiens	0-32
28420001-3	2017	Nicotinamide N-methyltransferase (NNMT) decreases histone methylation in several cancer cells by altering the cellular ratio of S-adenosylmethionine (SAM) to S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	128-148	nicotinamide N-methyltransferase	Homo sapiens	34-38
28420001-3	2017	Nicotinamide N-methyltransferase (NNMT) decreases histone methylation in several cancer cells by altering the cellular ratio of S-adenosylmethionine (SAM) to S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	150-153	nicotinamide N-methyltransferase	Homo sapiens	0-32
28420001-3	2017	Nicotinamide N-methyltransferase (NNMT) decreases histone methylation in several cancer cells by altering the cellular ratio of S-adenosylmethionine (SAM) to S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	150-153	nicotinamide N-methyltransferase	Homo sapiens	34-38
27567046-0	2017	Sake yeast YHR032W/ERC1 haplotype contributes to high S-adenosylmethionine accumulation in sake yeast strains.	S-Adenosylmethionine	54-74	Erc1p	Saccharomyces cerevisiae S288C	19-23
28293840-4	2017	The first is the biosynthesis of 1-aminocyclopropane-1-carboxylic acid (ACC) from S-Adenosyl-Methionine (SAM), a common precursor in many metabolic pathways, which is catalyzed by ACC synthase (ACS).	S-Adenosylmethionine	82-103	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	194-197
28293840-4	2017	The first is the biosynthesis of 1-aminocyclopropane-1-carboxylic acid (ACC) from S-Adenosyl-Methionine (SAM), a common precursor in many metabolic pathways, which is catalyzed by ACC synthase (ACS).	S-Adenosylmethionine	105-108	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	180-192
28293840-4	2017	The first is the biosynthesis of 1-aminocyclopropane-1-carboxylic acid (ACC) from S-Adenosyl-Methionine (SAM), a common precursor in many metabolic pathways, which is catalyzed by ACC synthase (ACS).	S-Adenosylmethionine	105-108	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	194-197
27934872-7	2016	Consistent with this interpretation, the bound SAH can be replaced by the methyl donor S-adenosyl-L-methionine without triggering the methylation reaction.	S-Adenosylmethionine	87-110	acyl-CoA synthetase medium chain family member 3	Homo sapiens	47-50
28271477-4	2017	The structure of the 453 kDa heterooctameric PRMT5:MEP50 complex bound to an S-adenosylmethionine analog and a substrate peptide provides valuable insights into this intriguing target.	S-Adenosylmethionine	79-97	protein arginine methyltransferase 5	Homo sapiens	45-50
28271477-4	2017	The structure of the 453 kDa heterooctameric PRMT5:MEP50 complex bound to an S-adenosylmethionine analog and a substrate peptide provides valuable insights into this intriguing target.	S-Adenosylmethionine	79-97	WD repeat domain 77	Homo sapiens	51-56
27940912-7	2016	We therefore implemented the MS-based method to measure KIEs and binding isotope effects (BIEs) of the cofactor S-adenosyl-l-methionine (SAM) for SET8-catalyzed H4K20 monomethylation.	S-Adenosylmethionine	112-135	lysine methyltransferase 5A	Homo sapiens	146-150
27940912-7	2016	We therefore implemented the MS-based method to measure KIEs and binding isotope effects (BIEs) of the cofactor S-adenosyl-l-methionine (SAM) for SET8-catalyzed H4K20 monomethylation.	S-Adenosylmethionine	137-140	lysine methyltransferase 5A	Homo sapiens	146-150
28066248-2	2016	One of the main enzymes to take into account in pharmacogenomics is catechol O-methyltransferase (COMT), which catalyzes the transfer of a methyl group from S-adenosylmethionine to catechols and catecholamines, like the neurotransmitters dopamine, epinephrine, and norepinephrine.	S-Adenosylmethionine	157-177	catechol-O-methyltransferase	Rattus norvegicus	68-96
28066248-2	2016	One of the main enzymes to take into account in pharmacogenomics is catechol O-methyltransferase (COMT), which catalyzes the transfer of a methyl group from S-adenosylmethionine to catechols and catecholamines, like the neurotransmitters dopamine, epinephrine, and norepinephrine.	S-Adenosylmethionine	157-177	catechol-O-methyltransferase	Rattus norvegicus	98-102
28421128-2	2017	CBS activity, contributing to cellular redox homeostasis, is positively regulated by S-adenosyl-L-methionine (AdoMet) but fully inhibited upon CO or NO  binding to a noncatalytic heme moiety.	S-Adenosylmethionine	85-108	cystathionine beta-synthase	Homo sapiens	0-3
28421128-2	2017	CBS activity, contributing to cellular redox homeostasis, is positively regulated by S-adenosyl-L-methionine (AdoMet) but fully inhibited upon CO or NO  binding to a noncatalytic heme moiety.	S-Adenosylmethionine	110-116	cystathionine beta-synthase	Homo sapiens	0-3
27799657-3	2016	By developing genetically engineered mouse models and primary pancreatic epithelial cells, and employing transcriptional, proteomics, and metabolic analyses, we find that oncogenic cooperation between LKB1 loss and KRAS activation is fuelled by pronounced mTOR-dependent induction of the serine-glycine-one-carbon pathway coupled to S-adenosylmethionine generation.	S-Adenosylmethionine	335-353	serine/threonine kinase 11	Mus musculus	201-205
27422871-7	2016	Using biophysical and biochemical approaches, we observe that RAM increases the recruitment of the methyl donor, AdoMet (S-adenosyl methionine), to RNMT.	S-Adenosylmethionine	113-119	RNA guanine-7 methyltransferase activating subunit	Homo sapiens	62-65
27422871-7	2016	Using biophysical and biochemical approaches, we observe that RAM increases the recruitment of the methyl donor, AdoMet (S-adenosyl methionine), to RNMT.	S-Adenosylmethionine	113-119	RNA guanine-7 methyltransferase	Homo sapiens	148-152
27422871-7	2016	Using biophysical and biochemical approaches, we observe that RAM increases the recruitment of the methyl donor, AdoMet (S-adenosyl methionine), to RNMT.	S-Adenosylmethionine	121-142	RNA guanine-7 methyltransferase activating subunit	Homo sapiens	62-65
27422871-7	2016	Using biophysical and biochemical approaches, we observe that RAM increases the recruitment of the methyl donor, AdoMet (S-adenosyl methionine), to RNMT.	S-Adenosylmethionine	121-142	RNA guanine-7 methyltransferase	Homo sapiens	148-152
27890035-2	2016	The TNFa gene is subject of epigenetic regulation in which folate and homocysteine are important molecules because they participate in the methionine cycle where the most important methyl group donor (S-adenosylmethionine) is formed.	S-Adenosylmethionine	201-221	tumor necrosis factor	Homo sapiens	4-8
27685665-0	2016	Design of Potent and Druglike Nonphenolic Inhibitors for Catechol O-Methyltransferase Derived from a Fragment Screening Approach Targeting the S-Adenosyl-l-methionine Pocket.	S-Adenosylmethionine	145-166	catechol-O-methyltransferase	Homo sapiens	57-85
27799657-3	2016	By developing genetically engineered mouse models and primary pancreatic epithelial cells, and employing transcriptional, proteomics, and metabolic analyses, we find that oncogenic cooperation between LKB1 loss and KRAS activation is fuelled by pronounced mTOR-dependent induction of the serine-glycine-one-carbon pathway coupled to S-adenosylmethionine generation.	S-Adenosylmethionine	335-353	Kirsten rat sarcoma viral oncogene homolog	Mus musculus	215-219
27799657-3	2016	By developing genetically engineered mouse models and primary pancreatic epithelial cells, and employing transcriptional, proteomics, and metabolic analyses, we find that oncogenic cooperation between LKB1 loss and KRAS activation is fuelled by pronounced mTOR-dependent induction of the serine-glycine-one-carbon pathway coupled to S-adenosylmethionine generation.	S-Adenosylmethionine	335-353	mechanistic target of rapamycin kinase	Mus musculus	256-260
27703015-1	2016	Human NSun6 is an RNA methyltransferase that catalyzes the transfer of the methyl group from S-adenosyl-l-methionine (SAM) to C72 of tRNAThr and tRNACys In the current study, we used mass spectrometry to demonstrate that human NSun6 indeed introduces 5-methylcytosine (m5C) into tRNA, as expected.	S-Adenosylmethionine	93-116	NOP2/Sun RNA methyltransferase 6	Homo sapiens	6-11
27703015-1	2016	Human NSun6 is an RNA methyltransferase that catalyzes the transfer of the methyl group from S-adenosyl-l-methionine (SAM) to C72 of tRNAThr and tRNACys In the current study, we used mass spectrometry to demonstrate that human NSun6 indeed introduces 5-methylcytosine (m5C) into tRNA, as expected.	S-Adenosylmethionine	93-116	NOP2/Sun RNA methyltransferase 6	Homo sapiens	227-232
27703015-1	2016	Human NSun6 is an RNA methyltransferase that catalyzes the transfer of the methyl group from S-adenosyl-l-methionine (SAM) to C72 of tRNAThr and tRNACys In the current study, we used mass spectrometry to demonstrate that human NSun6 indeed introduces 5-methylcytosine (m5C) into tRNA, as expected.	S-Adenosylmethionine	118-121	NOP2/Sun RNA methyltransferase 6	Homo sapiens	6-11
27703015-1	2016	Human NSun6 is an RNA methyltransferase that catalyzes the transfer of the methyl group from S-adenosyl-l-methionine (SAM) to C72 of tRNAThr and tRNACys In the current study, we used mass spectrometry to demonstrate that human NSun6 indeed introduces 5-methylcytosine (m5C) into tRNA, as expected.	S-Adenosylmethionine	118-121	NOP2/Sun RNA methyltransferase 6	Homo sapiens	227-232
27834868-7	2016	For six mutations near the ligand-binding site we observed in simulations steric clashes with neighboring side chains near the substrate S-Adenosyl methionine (SAM) binding site, which may disrupt the enzymatic activity of NSD1.	S-Adenosylmethionine	137-158	nuclear receptor binding SET domain protein 1	Homo sapiens	223-227
27992360-5	2016	CD40 and CD40 intermediate subsets were positively correlated with plasma/cellular homocysteine levels, S-adenosylhomocysteine and S-adenosylmethionine but negatively correlated with estimated glomerular filtration rate.	S-Adenosylmethionine	131-151	CD40 molecule	Homo sapiens	0-4
27992360-5	2016	CD40 and CD40 intermediate subsets were positively correlated with plasma/cellular homocysteine levels, S-adenosylhomocysteine and S-adenosylmethionine but negatively correlated with estimated glomerular filtration rate.	S-Adenosylmethionine	131-151	CD40 molecule	Homo sapiens	9-13
27992360-10	2016	DNA hypomethylation was found on nuclear factor-kappaB consensus element in CD40 promoter in white blood cells from patients with CKD with lower S-adenosylmethionine / S-adenosylhomocysteine ratios.	S-Adenosylmethionine	145-165	CD40 molecule	Homo sapiens	76-80
27834868-7	2016	For six mutations near the ligand-binding site we observed in simulations steric clashes with neighboring side chains near the substrate S-Adenosyl methionine (SAM) binding site, which may disrupt the enzymatic activity of NSD1.	S-Adenosylmethionine	160-163	nuclear receptor binding SET domain protein 1	Homo sapiens	223-227
27707701-8	2016	The methylenetetrahydrofolate reductase (MTHFR) protein and methylation potential [ratio of S-adenosylmethionine (major methyl donor):S-adenosylhomocysteine) were reduced in maternal liver.	S-Adenosylmethionine	92-112	methylenetetrahydrofolate reductase	Homo sapiens	4-39
27707701-8	2016	The methylenetetrahydrofolate reductase (MTHFR) protein and methylation potential [ratio of S-adenosylmethionine (major methyl donor):S-adenosylhomocysteine) were reduced in maternal liver.	S-Adenosylmethionine	92-112	methylenetetrahydrofolate reductase	Homo sapiens	41-46
26889605-9	2016	Clinical improvement among children treated with methyl B12 was positively correlated with increases in plasma methionine (p = 0.05), decreases in S-adenosyl-l-homocysteine (SAH) (p = 0.007) and improvements in the ratio of S-adenosylmethionine (SAM) to SAH (p = 0.007), indicating an improvement in cellular methylation capacity.	S-Adenosylmethionine	224-244	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	56-59
26889605-9	2016	Clinical improvement among children treated with methyl B12 was positively correlated with increases in plasma methionine (p = 0.05), decreases in S-adenosyl-l-homocysteine (SAH) (p = 0.007) and improvements in the ratio of S-adenosylmethionine (SAM) to SAH (p = 0.007), indicating an improvement in cellular methylation capacity.	S-Adenosylmethionine	246-249	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	56-59
27474977-8	2016	Expression of Met adenosyltransferase 1A (MAT1A), which catalyzes the first step of Met metabolism to generate S-adenosylmethionine (SAM), a primary methyl donor, was decreased with increasing dl-Met or HMB concentration.	S-Adenosylmethionine	111-131	methionine adenosyltransferase 1A	Homo sapiens	14-40
27545444-4	2016	Molecular dynamics (MD) simulations were carried out for WT PRMT1 and its M48F, H293A, H293S, and H293S-M48F mutants bound with S-adenosylmethionine (AdoMet) and the arginine substrate in an unmethylated or methylated form.	S-Adenosylmethionine	128-148	protein arginine methyltransferase 1	Homo sapiens	60-65
27545444-4	2016	Molecular dynamics (MD) simulations were carried out for WT PRMT1 and its M48F, H293A, H293S, and H293S-M48F mutants bound with S-adenosylmethionine (AdoMet) and the arginine substrate in an unmethylated or methylated form.	S-Adenosylmethionine	150-156	protein arginine methyltransferase 1	Homo sapiens	60-65
27435264-8	2016	Of interest, under MDD, the bone development effects of 1,25-dihydroxyvitamin D3 were ineffectual and these could be rescued by the addition of S-adenosylmethionine, which restored expression of arginine methyltransferase 1, PGC1alpha, adiponectin, and HSP90.	S-Adenosylmethionine	144-164	PPARG coactivator 1 alpha	Homo sapiens	225-234
27435264-8	2016	Of interest, under MDD, the bone development effects of 1,25-dihydroxyvitamin D3 were ineffectual and these could be rescued by the addition of S-adenosylmethionine, which restored expression of arginine methyltransferase 1, PGC1alpha, adiponectin, and HSP90.	S-Adenosylmethionine	144-164	adiponectin, C1Q and collagen domain containing	Homo sapiens	236-247
27435264-8	2016	Of interest, under MDD, the bone development effects of 1,25-dihydroxyvitamin D3 were ineffectual and these could be rescued by the addition of S-adenosylmethionine, which restored expression of arginine methyltransferase 1, PGC1alpha, adiponectin, and HSP90.	S-Adenosylmethionine	144-164	heat shock protein 90 alpha family class A member 1	Homo sapiens	253-258
27474977-8	2016	Expression of Met adenosyltransferase 1A (MAT1A), which catalyzes the first step of Met metabolism to generate S-adenosylmethionine (SAM), a primary methyl donor, was decreased with increasing dl-Met or HMB concentration.	S-Adenosylmethionine	111-131	methionine adenosyltransferase 1A	Homo sapiens	42-47
27474977-8	2016	Expression of Met adenosyltransferase 1A (MAT1A), which catalyzes the first step of Met metabolism to generate S-adenosylmethionine (SAM), a primary methyl donor, was decreased with increasing dl-Met or HMB concentration.	S-Adenosylmethionine	133-136	methionine adenosyltransferase 1A	Homo sapiens	14-40
27474977-8	2016	Expression of Met adenosyltransferase 1A (MAT1A), which catalyzes the first step of Met metabolism to generate S-adenosylmethionine (SAM), a primary methyl donor, was decreased with increasing dl-Met or HMB concentration.	S-Adenosylmethionine	133-136	methionine adenosyltransferase 1A	Homo sapiens	42-47
27464505-9	2016	The inhibition study showed that, in the presence of SAM as methyl donor, Lomeguatrib, 5-Azacytidine, and 5-Aza-2"-deoxycytidine could inhibit the DNA MTase activity with IC50 values of 40.57 nM, 2.26 muM, and 0.48 muM, respectively.	S-Adenosylmethionine	53-56	latexin	Homo sapiens	201-204
27681803-0	2016	Rescue of Early bace-1 and Global DNA Demethylation by S-Adenosylmethionine Reduces Amyloid Pathology and Improves Cognition in an Alzheimer"s Model.	S-Adenosylmethionine	55-75	beta-secretase 1	Homo sapiens	16-22
27570878-2	2016	Employing the cofactor S-adenosyl-l-methionine, NNMT transfers a methyl group to the pyridine nitrogen of nicotinamide to generate N-methylnicotinamide.	S-Adenosylmethionine	23-46	nicotinamide N-methyltransferase	Homo sapiens	48-52
27464505-9	2016	The inhibition study showed that, in the presence of SAM as methyl donor, Lomeguatrib, 5-Azacytidine, and 5-Aza-2"-deoxycytidine could inhibit the DNA MTase activity with IC50 values of 40.57 nM, 2.26 muM, and 0.48 muM, respectively.	S-Adenosylmethionine	53-56	latexin	Homo sapiens	215-218
27085704-3	2016	METHODS: Here, we employed molecular dynamics simulations on full length human Smyd3, performed to a total of 1.2 mu-second, in the presence (holo) and absence (apo) of the S-Adenosyl methionine (AdoMet) cofactor.	S-Adenosylmethionine	196-202	SET and MYND domain containing 3	Homo sapiens	79-84
27582183-3	2016	To understand the molecular mechanism that underlies the cooperation of TRM6 and TRM61 in the methyl transfer reaction, we determined the crystal structure of TRM6-TRM61 holoenzyme from Saccharomyces cerevisiae in the presence and absence of its methyl donor S-Adenosyl-L-methionine (SAM).	S-Adenosylmethionine	259-282	tRNA 1-methyladenosine methyltransferase subunit GCD10	Saccharomyces cerevisiae S288C	72-76
27582183-3	2016	To understand the molecular mechanism that underlies the cooperation of TRM6 and TRM61 in the methyl transfer reaction, we determined the crystal structure of TRM6-TRM61 holoenzyme from Saccharomyces cerevisiae in the presence and absence of its methyl donor S-Adenosyl-L-methionine (SAM).	S-Adenosylmethionine	259-282	tRNA 1-methyladenosine methyltransferase subunit GCD14	Saccharomyces cerevisiae S288C	81-86
27582183-3	2016	To understand the molecular mechanism that underlies the cooperation of TRM6 and TRM61 in the methyl transfer reaction, we determined the crystal structure of TRM6-TRM61 holoenzyme from Saccharomyces cerevisiae in the presence and absence of its methyl donor S-Adenosyl-L-methionine (SAM).	S-Adenosylmethionine	259-282	tRNA 1-methyladenosine methyltransferase subunit GCD10	Saccharomyces cerevisiae S288C	81-85
27582183-3	2016	To understand the molecular mechanism that underlies the cooperation of TRM6 and TRM61 in the methyl transfer reaction, we determined the crystal structure of TRM6-TRM61 holoenzyme from Saccharomyces cerevisiae in the presence and absence of its methyl donor S-Adenosyl-L-methionine (SAM).	S-Adenosylmethionine	259-282	tRNA 1-methyladenosine methyltransferase subunit GCD14	Saccharomyces cerevisiae S288C	164-169
27365395-6	2016	This metabolite switch from cystathionine to cysteine and/or homocysteine renders H2S synthesis by CSE responsive to the known modulators of CBS: S-adenosylmethionine, NO, and CO. Used acutely, it regulates H2S synthesis; used chronically, it might contribute to disease pathology.	S-Adenosylmethionine	148-166	cystathionine gamma-lyase	Homo sapiens	99-102
27648357-3	2016	A major class of EZH2 inhibitors are S-adenosyl-L-methionine (SAM)-competitive inhibitors, such as EPZ005687, EI1, GSK126, UNC1999 and GSK343.	S-Adenosylmethionine	37-60	enhancer of zeste 2 polycomb repressive complex 2 subunit	Homo sapiens	17-21
27648357-3	2016	A major class of EZH2 inhibitors are S-adenosyl-L-methionine (SAM)-competitive inhibitors, such as EPZ005687, EI1, GSK126, UNC1999 and GSK343.	S-Adenosylmethionine	62-65	enhancer of zeste 2 polycomb repressive complex 2 subunit	Homo sapiens	17-21
27373337-4	2016	We present crystal structures of the complex of Mettl3/Mettl14 methyltransferase domains in apo form as well as with bound S-adenosylmethionine (SAM) or S-adenosylhomocysteine (SAH) in the catalytic site.	S-Adenosylmethionine	123-143	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	48-54
27373337-4	2016	We present crystal structures of the complex of Mettl3/Mettl14 methyltransferase domains in apo form as well as with bound S-adenosylmethionine (SAM) or S-adenosylhomocysteine (SAH) in the catalytic site.	S-Adenosylmethionine	123-143	methyltransferase 14, N6-adenosine-methyltransferase subunit	Homo sapiens	55-62
26765812-2	2016	Regulation of TS pathway kinetics involves stimulation of cystathionine beta-synthase (CBS) by S-adenosylmethionine (SAM) and oxidants such as H2O2, and by Michaelis-Menten principles whereby substrate concentrations affect reaction rates.	S-Adenosylmethionine	95-115	cystathionine beta-synthase	Homo sapiens	58-85
27548429-1	2016	Methionine adenosyltransferases MAT I and MAT III (encoded by Mat1a) catalyze S-adenosylmethionine synthesis in normal liver.	S-Adenosylmethionine	78-98	methionine adenosyltransferase 1A	Homo sapiens	62-67
27365395-6	2016	This metabolite switch from cystathionine to cysteine and/or homocysteine renders H2S synthesis by CSE responsive to the known modulators of CBS: S-adenosylmethionine, NO, and CO. Used acutely, it regulates H2S synthesis; used chronically, it might contribute to disease pathology.	S-Adenosylmethionine	148-166	cystathionine beta-synthase	Homo sapiens	141-144
26803480-0	2016	Low sulfide levels and a high degree of cystathionine beta-synthase (CBS) activation by S-adenosylmethionine (SAM) in the long-lived naked mole-rat.	S-Adenosylmethionine	88-108	cystathionine beta-synthase	Heterocephalus glaber	40-67
26803480-0	2016	Low sulfide levels and a high degree of cystathionine beta-synthase (CBS) activation by S-adenosylmethionine (SAM) in the long-lived naked mole-rat.	S-Adenosylmethionine	88-108	cystathionine beta-synthase	Heterocephalus glaber	69-72
26803480-5	2016	In addition, we show that the naked mole-rat cystathionine beta-synthase (CBS), an enzyme whose activity in the liver significantly contributes to systemic sulfide levels, has lower activity in the liver and is activated to a higher degree by S-adenosylmethionine compared to other species.	S-Adenosylmethionine	243-263	cystathionine beta-synthase	Heterocephalus glaber	45-72
26803480-5	2016	In addition, we show that the naked mole-rat cystathionine beta-synthase (CBS), an enzyme whose activity in the liver significantly contributes to systemic sulfide levels, has lower activity in the liver and is activated to a higher degree by S-adenosylmethionine compared to other species.	S-Adenosylmethionine	243-263	cystathionine beta-synthase	Heterocephalus glaber	74-77
27355841-2	2016	Glycine N-methyltransferase (GNMT), a member of the family that acts on small metabolites as the substrate, catalyzes methyl transfer from S-adenosyl-l-methionine (AdoMet) to glycine to form S-adenosyl-l-homocysteine and sarcosine.	S-Adenosylmethionine	139-162	glycine N-methyltransferase	Homo sapiens	0-27
27355841-2	2016	Glycine N-methyltransferase (GNMT), a member of the family that acts on small metabolites as the substrate, catalyzes methyl transfer from S-adenosyl-l-methionine (AdoMet) to glycine to form S-adenosyl-l-homocysteine and sarcosine.	S-Adenosylmethionine	139-162	glycine N-methyltransferase	Homo sapiens	29-33
27355841-2	2016	Glycine N-methyltransferase (GNMT), a member of the family that acts on small metabolites as the substrate, catalyzes methyl transfer from S-adenosyl-l-methionine (AdoMet) to glycine to form S-adenosyl-l-homocysteine and sarcosine.	S-Adenosylmethionine	164-170	glycine N-methyltransferase	Homo sapiens	0-27
27355841-2	2016	Glycine N-methyltransferase (GNMT), a member of the family that acts on small metabolites as the substrate, catalyzes methyl transfer from S-adenosyl-l-methionine (AdoMet) to glycine to form S-adenosyl-l-homocysteine and sarcosine.	S-Adenosylmethionine	164-170	glycine N-methyltransferase	Homo sapiens	29-33
26805382-0	2016	Kinetic stability of cystathionine beta-synthase can be modulated by structural analogs of S-adenosylmethionine: Potential approach to pharmacological chaperone therapy for homocystinuria.	S-Adenosylmethionine	91-111	cystathionine beta-synthase	Homo sapiens	21-48
26805382-3	2016	CBS contains two sets of binding sites for S-adenosylmethionine (SAM) that independently regulate the enzyme activity and kinetically stabilize its regulatory domain.	S-Adenosylmethionine	43-63	cystathionine beta-synthase	Homo sapiens	0-3
26805382-3	2016	CBS contains two sets of binding sites for S-adenosylmethionine (SAM) that independently regulate the enzyme activity and kinetically stabilize its regulatory domain.	S-Adenosylmethionine	65-68	cystathionine beta-synthase	Homo sapiens	0-3
27547295-8	2016	The most potent resulting compound (5) inhibited hIcmt in vitro with low micromolar potency (IC50 = 1.5 +- 0.2 muM) and was kinetically characterized as a competitive inhibitor for prenylated substrates and a non-competitive inhibitor for the cofactor and methyl donor S-adenosylmethionine (SAM).	S-Adenosylmethionine	269-289	isoprenylcysteine carboxyl methyltransferase	Homo sapiens	49-54
27175774-9	2016	The ratios of SAM/SAH were increased by 1.67- and 2.75-fold in the in ApoE-/- control group and Meth group, respectively, compared with the normal control group.	S-Adenosylmethionine	14-17	apolipoprotein E	Mus musculus	70-74
27214402-4	2016	We demonstrate that biogenesis of f(5)C34 is initiated by S-adenosylmethionine (AdoMet)-dependent methylation catalyzed by NSUN3, a putative methyltransferase in mitochondria.	S-Adenosylmethionine	58-78	NOP2/Sun RNA methyltransferase 3	Homo sapiens	123-128
27214402-4	2016	We demonstrate that biogenesis of f(5)C34 is initiated by S-adenosylmethionine (AdoMet)-dependent methylation catalyzed by NSUN3, a putative methyltransferase in mitochondria.	S-Adenosylmethionine	80-86	NOP2/Sun RNA methyltransferase 3	Homo sapiens	123-128
27281194-5	2016	Here we report the crystal structures of the METTL3-METTL14 heterodimer with MTase domains in the ligand-free, S-adenosyl methionine (AdoMet)-bound and S-adenosyl homocysteine (AdoHcy)-bound states, with resolutions of 1.9, 1.71 and 1.61 A, respectively.	S-Adenosylmethionine	111-132	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	45-51
27281194-5	2016	Here we report the crystal structures of the METTL3-METTL14 heterodimer with MTase domains in the ligand-free, S-adenosyl methionine (AdoMet)-bound and S-adenosyl homocysteine (AdoHcy)-bound states, with resolutions of 1.9, 1.71 and 1.61 A, respectively.	S-Adenosylmethionine	111-132	methyltransferase 14, N6-adenosine-methyltransferase subunit	Homo sapiens	52-59
27281194-5	2016	Here we report the crystal structures of the METTL3-METTL14 heterodimer with MTase domains in the ligand-free, S-adenosyl methionine (AdoMet)-bound and S-adenosyl homocysteine (AdoHcy)-bound states, with resolutions of 1.9, 1.71 and 1.61 A, respectively.	S-Adenosylmethionine	134-140	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	45-51
27281194-5	2016	Here we report the crystal structures of the METTL3-METTL14 heterodimer with MTase domains in the ligand-free, S-adenosyl methionine (AdoMet)-bound and S-adenosyl homocysteine (AdoHcy)-bound states, with resolutions of 1.9, 1.71 and 1.61 A, respectively.	S-Adenosylmethionine	134-140	methyltransferase 14, N6-adenosine-methyltransferase subunit	Homo sapiens	52-59
27291711-7	2016	Our work highlights the sensitivity of epigenetic networks to one-carbon metabolism due to their common S-adenosylmethionine-dependent transmethylation and has implications for human MTHFD1-associated diseases.	S-Adenosylmethionine	106-124	methylenetetrahydrofolate dehydrogenase, cyclohydrolase and formyltetrahydrofolate synthetase 1	Homo sapiens	183-189
27183271-2	2016	NSD2 binds to S-adenosyl-l-methionine (SAM) and nucleosome substrates to catalyze the transfer of a methyl group from SAM to the epsilon-amino group of histone H3K36.	S-Adenosylmethionine	14-37	nuclear receptor binding SET domain protein 2	Homo sapiens	0-4
27183271-2	2016	NSD2 binds to S-adenosyl-l-methionine (SAM) and nucleosome substrates to catalyze the transfer of a methyl group from SAM to the epsilon-amino group of histone H3K36.	S-Adenosylmethionine	39-42	nuclear receptor binding SET domain protein 2	Homo sapiens	0-4
27177086-0	2016	GADD45beta induction by S-adenosylmethionine inhibits hepatocellular carcinoma cell proliferation during acute ischemia-hypoxia.	S-Adenosylmethionine	24-44	growth arrest and DNA damage inducible beta	Homo sapiens	0-10
27262903-9	2016	Furthermore, CTL2 may be the major site for the control of choline oxidation in mitochondria and hence for the supply of endogenous betaine and S-adenosyl methionine, which serves as a major methyl donor.	S-Adenosylmethionine	144-165	solute carrier family 44 member 2	Homo sapiens	13-17
26940012-2	2016	The MAT2B protein with MAT2alpha catalyzes the formation of methyl donor S- adenosylmethionine (SAMe) to mediate cell metabolism including proliferation and apoptosis.	S-Adenosylmethionine	73-94	methionine adenosyltransferase 2B	Homo sapiens	4-9
26940012-2	2016	The MAT2B protein with MAT2alpha catalyzes the formation of methyl donor S- adenosylmethionine (SAMe) to mediate cell metabolism including proliferation and apoptosis.	S-Adenosylmethionine	73-94	methionine adenosyltransferase 2A	Homo sapiens	23-32
27547295-8	2016	The most potent resulting compound (5) inhibited hIcmt in vitro with low micromolar potency (IC50 = 1.5 +- 0.2 muM) and was kinetically characterized as a competitive inhibitor for prenylated substrates and a non-competitive inhibitor for the cofactor and methyl donor S-adenosylmethionine (SAM).	S-Adenosylmethionine	291-294	isoprenylcysteine carboxyl methyltransferase	Homo sapiens	49-54
27092053-6	2016	Support for the contribution of altered epigenetic mechanisms in the down-regulation of RELN expression in corticolimbic structures of psychotic patients includes the concomitant increase of DNA-methyltransferases and the increased levels of the methyl donor S-adenosylmethionine (SAM).	S-Adenosylmethionine	259-279	reelin	Homo sapiens	88-92
26986629-0	2016	S-Adenosylmethionine suppresses the expression of Smad3/4 in activated human hepatic stellate cells via Rac1 promoter methylation.	S-Adenosylmethionine	0-20	SMAD family member 3	Homo sapiens	50-55
26986629-0	2016	S-Adenosylmethionine suppresses the expression of Smad3/4 in activated human hepatic stellate cells via Rac1 promoter methylation.	S-Adenosylmethionine	0-20	Rac family small GTPase 1	Homo sapiens	104-108
27040643-6	2016	Our results explained the role of the upregulated expression of BCAT1, PLOD3 and six other methyltransferase genes involved in carnitine biosynthesis and S-adenosylmethionine metabolism in the early and advanced HCC stages.	S-Adenosylmethionine	154-174	branched chain amino acid transaminase 1	Homo sapiens	64-69
27040643-6	2016	Our results explained the role of the upregulated expression of BCAT1, PLOD3 and six other methyltransferase genes involved in carnitine biosynthesis and S-adenosylmethionine metabolism in the early and advanced HCC stages.	S-Adenosylmethionine	154-174	procollagen-lysine,2-oxoglutarate 5-dioxygenase 3	Homo sapiens	71-76
27068473-7	2016	MAT2A produces the PRMT5 substrate S-adenosylmethionine (SAM), and MAT2A depletion reduces growth and PRMT5 methylation activity selectively in MTAP-deleted cells.	S-Adenosylmethionine	35-55	methionine adenosyltransferase 2A	Homo sapiens	0-5
27068473-7	2016	MAT2A produces the PRMT5 substrate S-adenosylmethionine (SAM), and MAT2A depletion reduces growth and PRMT5 methylation activity selectively in MTAP-deleted cells.	S-Adenosylmethionine	35-55	protein arginine methyltransferase 5	Homo sapiens	19-24
27068473-7	2016	MAT2A produces the PRMT5 substrate S-adenosylmethionine (SAM), and MAT2A depletion reduces growth and PRMT5 methylation activity selectively in MTAP-deleted cells.	S-Adenosylmethionine	35-55	methylthioadenosine phosphorylase	Homo sapiens	144-148
27068473-7	2016	MAT2A produces the PRMT5 substrate S-adenosylmethionine (SAM), and MAT2A depletion reduces growth and PRMT5 methylation activity selectively in MTAP-deleted cells.	S-Adenosylmethionine	57-60	methionine adenosyltransferase 2A	Homo sapiens	0-5
27068473-7	2016	MAT2A produces the PRMT5 substrate S-adenosylmethionine (SAM), and MAT2A depletion reduces growth and PRMT5 methylation activity selectively in MTAP-deleted cells.	S-Adenosylmethionine	57-60	protein arginine methyltransferase 5	Homo sapiens	19-24
27068473-7	2016	MAT2A produces the PRMT5 substrate S-adenosylmethionine (SAM), and MAT2A depletion reduces growth and PRMT5 methylation activity selectively in MTAP-deleted cells.	S-Adenosylmethionine	57-60	methylthioadenosine phosphorylase	Homo sapiens	144-148
27128904-0	2016	Protective Effect of Tyrosol and S-Adenosylmethionine against Ethanol-Induced Oxidative Stress of Hepg2 Cells Involves Sirtuin 1, P53 and Erk1/2 Signaling.	S-Adenosylmethionine	33-53	sirtuin 1	Homo sapiens	119-128
27128904-0	2016	Protective Effect of Tyrosol and S-Adenosylmethionine against Ethanol-Induced Oxidative Stress of Hepg2 Cells Involves Sirtuin 1, P53 and Erk1/2 Signaling.	S-Adenosylmethionine	33-53	tumor protein p53	Homo sapiens	130-133
27128904-0	2016	Protective Effect of Tyrosol and S-Adenosylmethionine against Ethanol-Induced Oxidative Stress of Hepg2 Cells Involves Sirtuin 1, P53 and Erk1/2 Signaling.	S-Adenosylmethionine	33-53	mitogen-activated protein kinase 3	Homo sapiens	138-144
27092053-6	2016	Support for the contribution of altered epigenetic mechanisms in the down-regulation of RELN expression in corticolimbic structures of psychotic patients includes the concomitant increase of DNA-methyltransferases and the increased levels of the methyl donor S-adenosylmethionine (SAM).	S-Adenosylmethionine	281-284	reelin	Homo sapiens	88-92
26551522-4	2016	Here, the crystal structures of human CARM1 with the S-adenosylmethione (SAM) mimic sinefungin and three different peptide sequences from histone H3 and PABP1 are presented, with both nonmethylated and singly methylated arginine residues exemplified.	S-Adenosylmethionine	53-71	coactivator associated arginine methyltransferase 1	Homo sapiens	38-43
26813693-2	2016	SETDB1 methylates lysine 9 of histone 3 (H3K9), utilizing S-adenosylmethionine (SAM) as the methyl donor and its catalytic activity, has been reported to be regulated by a partner protein ATF7IP.	S-Adenosylmethionine	58-78	SET domain bifurcated histone lysine methyltransferase 1	Homo sapiens	0-6
26813693-2	2016	SETDB1 methylates lysine 9 of histone 3 (H3K9), utilizing S-adenosylmethionine (SAM) as the methyl donor and its catalytic activity, has been reported to be regulated by a partner protein ATF7IP.	S-Adenosylmethionine	58-78	activating transcription factor 7 interacting protein	Homo sapiens	188-194
26813693-2	2016	SETDB1 methylates lysine 9 of histone 3 (H3K9), utilizing S-adenosylmethionine (SAM) as the methyl donor and its catalytic activity, has been reported to be regulated by a partner protein ATF7IP.	S-Adenosylmethionine	80-83	SET domain bifurcated histone lysine methyltransferase 1	Homo sapiens	0-6
26813693-2	2016	SETDB1 methylates lysine 9 of histone 3 (H3K9), utilizing S-adenosylmethionine (SAM) as the methyl donor and its catalytic activity, has been reported to be regulated by a partner protein ATF7IP.	S-Adenosylmethionine	80-83	activating transcription factor 7 interacting protein	Homo sapiens	188-194
26418898-1	2016	We previously showed that S-adenosylmethionine-mediated hypermethylation of the PTEN promoter was important for the growth of tamoxifen-resistant MCF-7 (TAMR-MCF-7) cancer cells.	S-Adenosylmethionine	26-46	phosphatase and tensin homolog	Homo sapiens	80-84
26418898-2	2016	Here, we found that the basal expression level of methionine adenosyltransferase 2A (MAT2A), a critical enzyme for the biosynthesis of S-adenosylmethionine, was up-regulated in TAMR-MCF-7 cells compared with control MCF-7 cells.	S-Adenosylmethionine	135-155	methionine adenosyltransferase 2A	Homo sapiens	50-83
26418898-2	2016	Here, we found that the basal expression level of methionine adenosyltransferase 2A (MAT2A), a critical enzyme for the biosynthesis of S-adenosylmethionine, was up-regulated in TAMR-MCF-7 cells compared with control MCF-7 cells.	S-Adenosylmethionine	135-155	methionine adenosyltransferase 2A	Homo sapiens	85-90
26551522-4	2016	Here, the crystal structures of human CARM1 with the S-adenosylmethione (SAM) mimic sinefungin and three different peptide sequences from histone H3 and PABP1 are presented, with both nonmethylated and singly methylated arginine residues exemplified.	S-Adenosylmethionine	73-76	coactivator associated arginine methyltransferase 1	Homo sapiens	38-43
26929335-2	2016	The proposed catalytic mechanism of DNMT1 involves nucleophilic attack of Cys(1226) to cytosine (Cyt) C6, methyl transfer from S-adenosyl-l-methionine (SAM) to Cyt C5, and proton abstraction from C5 to form methylated CpG in DNA.	S-Adenosylmethionine	127-150	DNA methyltransferase 1	Homo sapiens	36-41
26841310-1	2016	TsrM, an annotated radical S-adenosylmethionine (SAM) enzyme, catalyzes the methylation of carbon 2 of the indole ring of L-tryptophan.	S-Adenosylmethionine	49-52	TSRM	Homo sapiens	0-4
26929335-2	2016	The proposed catalytic mechanism of DNMT1 involves nucleophilic attack of Cys(1226) to cytosine (Cyt) C6, methyl transfer from S-adenosyl-l-methionine (SAM) to Cyt C5, and proton abstraction from C5 to form methylated CpG in DNA.	S-Adenosylmethionine	152-155	DNA methyltransferase 1	Homo sapiens	36-41
26974652-7	2016	The optimal concentrations of the cofactor S-adenosyl-L-methionine (SAM) and substrate 5-aminolevulinic acid (ALA) were also determined to be 200 muM and 5 mM, respectively, in a tandem-enzyme assay.	S-Adenosylmethionine	43-66	latexin	Homo sapiens	146-149
26974652-7	2016	The optimal concentrations of the cofactor S-adenosyl-L-methionine (SAM) and substrate 5-aminolevulinic acid (ALA) were also determined to be 200 muM and 5 mM, respectively, in a tandem-enzyme assay.	S-Adenosylmethionine	68-71	latexin	Homo sapiens	146-149
26582199-0	2016	S-Adenosyl-l-methionine Modulates CO and NO  Binding to the Human H2S-generating Enzyme Cystathionine beta-Synthase.	S-Adenosylmethionine	0-23	cystathionine beta-synthase	Homo sapiens	88-115
26943589-4	2016	The metabolic facet of BRCA1 one-hit might involve tissue-specific alterations in acetyl-CoA, alpha-ketoglutarate, NAD+, FAD, or S-adenosylmethionine, critical factors for de/methylation or de/acetylation dynamics in the nuclear epigenome.	S-Adenosylmethionine	129-149	BRCA1 DNA repair associated	Homo sapiens	23-28
26895662-2	2016	FPGS-induced polyglutamylated folates are better substrates for several enzymes involved in the generation of S-adenosylmethionine, the primary methyl group donor, and hence FPGS modulation may affect DNA methylation.	S-Adenosylmethionine	110-130	folylpolyglutamate synthase	Homo sapiens	174-178
26394163-0	2016	Methionine and S-adenosylmethionine levels are critical regulators of PP2A activity modulating lipophagy during steatosis.	S-Adenosylmethionine	15-35	protein phosphatase 2 phosphatase activator	Homo sapiens	70-74
26394163-2	2016	Gnmt deficiency in mice (Gnmt-KO) results in abnormally elevated serum levels of methionine and its metabolite S-adenosylmethionine (SAMe), and this leads to rapid liver steatosis development.	S-Adenosylmethionine	111-131	glycine N-methyltransferase	Mus musculus	0-4
26973856-3	2016	Our previous study has demonstrated that GSK343, an S-adenosyl-L-methionine (SAM)-competitive inhibitor of EZH2, induces autophagy and enhances drug sensitivity in cancer cells including HCC.	S-Adenosylmethionine	52-75	enhancer of zeste 2 polycomb repressive complex 2 subunit	Homo sapiens	107-111
26973856-3	2016	Our previous study has demonstrated that GSK343, an S-adenosyl-L-methionine (SAM)-competitive inhibitor of EZH2, induces autophagy and enhances drug sensitivity in cancer cells including HCC.	S-Adenosylmethionine	77-80	enhancer of zeste 2 polycomb repressive complex 2 subunit	Homo sapiens	107-111
26541578-0	2016	Design of a fluorescent ligand targeting the S-adenosylmethionine binding site of the histone methyltransferase MLL1.	S-Adenosylmethionine	45-65	lysine methyltransferase 2A	Homo sapiens	112-116
26541578-4	2016	We present here a small molecule fluorescent ligand (FL-NAH, 6) that is able to bind to the S-adenosylmethionine (SAM) binding site of MLL1 in a manner independent of the associated complex members.	S-Adenosylmethionine	92-112	lysine methyltransferase 2A	Homo sapiens	135-139
26541578-4	2016	We present here a small molecule fluorescent ligand (FL-NAH, 6) that is able to bind to the S-adenosylmethionine (SAM) binding site of MLL1 in a manner independent of the associated complex members.	S-Adenosylmethionine	114-117	lysine methyltransferase 2A	Homo sapiens	135-139
26895662-2	2016	FPGS-induced polyglutamylated folates are better substrates for several enzymes involved in the generation of S-adenosylmethionine, the primary methyl group donor, and hence FPGS modulation may affect DNA methylation.	S-Adenosylmethionine	110-130	folylpolyglutamate synthase	Homo sapiens	0-4
26759408-5	2016	CHLM catalyzes a methyl group transfer by using S-adenosylmethionine (SAM).	S-Adenosylmethionine	48-68	magnesium-protoporphyrin IX methyltransferase	Arabidopsis thaliana	0-4
26759408-5	2016	CHLM catalyzes a methyl group transfer by using S-adenosylmethionine (SAM).	S-Adenosylmethionine	70-73	magnesium-protoporphyrin IX methyltransferase	Arabidopsis thaliana	0-4
26174106-0	2016	S-Adenosylmethionine Affects ERK1/2 and Stat3 Pathways and Induces Apotosis in Osteosarcoma Cells.	S-Adenosylmethionine	0-20	mitogen-activated protein kinase 3	Homo sapiens	29-35
26174106-0	2016	S-Adenosylmethionine Affects ERK1/2 and Stat3 Pathways and Induces Apotosis in Osteosarcoma Cells.	S-Adenosylmethionine	0-20	signal transducer and activator of transcription 3	Homo sapiens	40-45
26174106-11	2016	We also report that AdoMet consistently causes an increase of p53 and p21 cell-cycle inhibitor, a decrease of cyclin A and cyclin E protein levels, and a marked increase of pro-apoptotic Bax/Bcl-2 ratio, with caspase-3 activation and PARP cleavage.	S-Adenosylmethionine	20-26	tumor protein p53	Homo sapiens	62-65
26174106-11	2016	We also report that AdoMet consistently causes an increase of p53 and p21 cell-cycle inhibitor, a decrease of cyclin A and cyclin E protein levels, and a marked increase of pro-apoptotic Bax/Bcl-2 ratio, with caspase-3 activation and PARP cleavage.	S-Adenosylmethionine	20-26	cyclin A2	Homo sapiens	110-118
26174106-11	2016	We also report that AdoMet consistently causes an increase of p53 and p21 cell-cycle inhibitor, a decrease of cyclin A and cyclin E protein levels, and a marked increase of pro-apoptotic Bax/Bcl-2 ratio, with caspase-3 activation and PARP cleavage.	S-Adenosylmethionine	20-26	BCL2 associated X, apoptosis regulator	Homo sapiens	187-190
26174106-11	2016	We also report that AdoMet consistently causes an increase of p53 and p21 cell-cycle inhibitor, a decrease of cyclin A and cyclin E protein levels, and a marked increase of pro-apoptotic Bax/Bcl-2 ratio, with caspase-3 activation and PARP cleavage.	S-Adenosylmethionine	20-26	BCL2 apoptosis regulator	Homo sapiens	191-196
26174106-11	2016	We also report that AdoMet consistently causes an increase of p53 and p21 cell-cycle inhibitor, a decrease of cyclin A and cyclin E protein levels, and a marked increase of pro-apoptotic Bax/Bcl-2 ratio, with caspase-3 activation and PARP cleavage.	S-Adenosylmethionine	20-26	caspase 3	Homo sapiens	209-218
26174106-11	2016	We also report that AdoMet consistently causes an increase of p53 and p21 cell-cycle inhibitor, a decrease of cyclin A and cyclin E protein levels, and a marked increase of pro-apoptotic Bax/Bcl-2 ratio, with caspase-3 activation and PARP cleavage.	S-Adenosylmethionine	20-26	collagen type XI alpha 2 chain	Homo sapiens	234-238
26174106-12	2016	Moreover, the AdoMet-induced antiproliferative effects were dynamically accompanied by profound changes in ERK1/2 and STAT3 protein and phosphorylation levels.	S-Adenosylmethionine	14-20	mitogen-activated protein kinase 3	Homo sapiens	107-113
26174106-12	2016	Moreover, the AdoMet-induced antiproliferative effects were dynamically accompanied by profound changes in ERK1/2 and STAT3 protein and phosphorylation levels.	S-Adenosylmethionine	14-20	signal transducer and activator of transcription 3	Homo sapiens	118-123
26494244-4	2016	Moreover, s-adenosyl methionine to s-adenosyl homocysteine ratio was elevated in the liver of betaine-exposed piglets, which was accompanied by DNA hypermethylation on FAS and SCD gene promoters and more enriched repression histone mark H3K27me3 on SCD gene promoter.	S-Adenosylmethionine	10-31	fatty acid synthase	Homo sapiens	168-171
26494244-4	2016	Moreover, s-adenosyl methionine to s-adenosyl homocysteine ratio was elevated in the liver of betaine-exposed piglets, which was accompanied by DNA hypermethylation on FAS and SCD gene promoters and more enriched repression histone mark H3K27me3 on SCD gene promoter.	S-Adenosylmethionine	10-31	stearoyl-CoA desaturase	Homo sapiens	176-179
26494244-4	2016	Moreover, s-adenosyl methionine to s-adenosyl homocysteine ratio was elevated in the liver of betaine-exposed piglets, which was accompanied by DNA hypermethylation on FAS and SCD gene promoters and more enriched repression histone mark H3K27me3 on SCD gene promoter.	S-Adenosylmethionine	10-31	stearoyl-CoA desaturase	Homo sapiens	249-252
26931358-5	2016	In this review, we summarize the complex nature of CBS, its multidomain architecture, the interplay between the three cofactors required for CBS function (heme, pyridoxal-5"-phosphate (PLP) and S-adenosyl-L-methionine) as well as the intricate allosteric regulatory mechanism only recently explained thanks to advances in CBS crystallography.	S-Adenosylmethionine	194-217	cystathionine beta-synthase	Homo sapiens	51-54
26989453-4	2016	MS activity was dependent upon methylcobalamin (MeCbl) or the combination of hydroxocobalamin (OHCbl) and S-adenosylmethionine (SAM).	S-Adenosylmethionine	106-126	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	0-2
26585478-13	2016	The upregulation of PPARalpha target genes indicates that supplemental Met, likely through the synthesis of S-adenosylmethionine, activated PPARA-regulated signaling pathways.	S-Adenosylmethionine	108-128	peroxisome proliferator activated receptor alpha	Bos taurus	20-29
26585478-13	2016	The upregulation of PPARalpha target genes indicates that supplemental Met, likely through the synthesis of S-adenosylmethionine, activated PPARA-regulated signaling pathways.	S-Adenosylmethionine	108-128	peroxisome proliferator activated receptor alpha	Bos taurus	140-145
26989453-4	2016	MS activity was dependent upon methylcobalamin (MeCbl) or the combination of hydroxocobalamin (OHCbl) and S-adenosylmethionine (SAM).	S-Adenosylmethionine	128-131	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	0-2
26562720-5	2015	The mutation of residues along the allosteric pathways markedly reduced the methylation activity of PRMT1, which may be attributable to the destruction of dimer formation and accordingly reduced S-adenosyl-L-methionine (SAM) binding.	S-Adenosylmethionine	195-218	protein arginine methyltransferase 1	Homo sapiens	100-105
26562720-5	2015	The mutation of residues along the allosteric pathways markedly reduced the methylation activity of PRMT1, which may be attributable to the destruction of dimer formation and accordingly reduced S-adenosyl-L-methionine (SAM) binding.	S-Adenosylmethionine	220-223	protein arginine methyltransferase 1	Homo sapiens	100-105
26697113-11	2015	Consistent with the transcript changes of C1-related genes, a significant reduction in S-adenosyl-l-methionine content was detected in the fpgs1 mutant.	S-Adenosylmethionine	87-110	DHFS-FPGS homolog B	Arabidopsis thaliana	139-144
26527160-7	2015	An asymptomatic 7-year old son of the proband is also homozygous for the AHCY-R49H mutation and has elevated serum aminotransferase levels, as well as markedly elevated serum levels of SAH, S-adenosylmethionine (SAM), and methionine, which are hallmarks of SAH hydrolase deficiency.	S-Adenosylmethionine	190-210	adenosylhomocysteinase	Homo sapiens	73-77
26527160-7	2015	An asymptomatic 7-year old son of the proband is also homozygous for the AHCY-R49H mutation and has elevated serum aminotransferase levels, as well as markedly elevated serum levels of SAH, S-adenosylmethionine (SAM), and methionine, which are hallmarks of SAH hydrolase deficiency.	S-Adenosylmethionine	212-215	adenosylhomocysteinase	Homo sapiens	73-77
26550452-1	2015	Methionine synthase reductase (MTRR) is involved in the DNA synthesis and production of S-adenosylmethionine (SAM) and plays an important role in the carcinogenesis.	S-Adenosylmethionine	88-108	5-methyltetrahydrofolate-homocysteine methyltransferase reductase	Homo sapiens	0-29
26571212-4	2015	Specifically, in naive hESCs, NNMT and its enzymatic product 1-methylnicotinamide are highly upregulated, and NNMT is required for low S-adenosyl methionine (SAM) levels and the H3K27me3 repressive state.	S-Adenosylmethionine	135-156	nicotinamide N-methyltransferase	Homo sapiens	110-114
26571212-4	2015	Specifically, in naive hESCs, NNMT and its enzymatic product 1-methylnicotinamide are highly upregulated, and NNMT is required for low S-adenosyl methionine (SAM) levels and the H3K27me3 repressive state.	S-Adenosylmethionine	158-161	nicotinamide N-methyltransferase	Homo sapiens	110-114
26253436-1	2015	Catechol-O-methyltransferase (COMT) is a methylation enzyme engaged in the degradation of dopamine and noradrenaline by catalyzing the transfer of a methyl group from S-adenosylmethionine.	S-Adenosylmethionine	167-187	catechol-O-methyltransferase	Homo sapiens	0-28
26253436-1	2015	Catechol-O-methyltransferase (COMT) is a methylation enzyme engaged in the degradation of dopamine and noradrenaline by catalyzing the transfer of a methyl group from S-adenosylmethionine.	S-Adenosylmethionine	167-187	catechol-O-methyltransferase	Homo sapiens	30-34
25988356-0	2015	FERONIA receptor kinase interacts with S-adenosylmethionine synthetase and suppresses S-adenosylmethionine production and ethylene biosynthesis in Arabidopsis.	S-Adenosylmethionine	39-59	Malectin/receptor-like protein kinase family protein	Arabidopsis thaliana	0-7
25988356-2	2015	We report here that FERONIA (FER), a plasma membrane receptor-like kinase, may negatively regulate the S-adenosylmethionine (SAM) synthesis by interacting with two S-adenosylmethionine synthases (SAM1 and SAM2).	S-Adenosylmethionine	103-123	Malectin/receptor-like protein kinase family protein	Arabidopsis thaliana	20-27
25988356-2	2015	We report here that FERONIA (FER), a plasma membrane receptor-like kinase, may negatively regulate the S-adenosylmethionine (SAM) synthesis by interacting with two S-adenosylmethionine synthases (SAM1 and SAM2).	S-Adenosylmethionine	103-123	Malectin/receptor-like protein kinase family protein	Arabidopsis thaliana	20-23
25988356-2	2015	We report here that FERONIA (FER), a plasma membrane receptor-like kinase, may negatively regulate the S-adenosylmethionine (SAM) synthesis by interacting with two S-adenosylmethionine synthases (SAM1 and SAM2).	S-Adenosylmethionine	103-123	S-adenosylmethionine synthetase 1	Arabidopsis thaliana	196-200
25988356-2	2015	We report here that FERONIA (FER), a plasma membrane receptor-like kinase, may negatively regulate the S-adenosylmethionine (SAM) synthesis by interacting with two S-adenosylmethionine synthases (SAM1 and SAM2).	S-Adenosylmethionine	103-123	S-adenosylmethionine synthetase 2	Arabidopsis thaliana	205-209
26416353-2	2015	Methionine adenosyltransferase 2A (MAT2A) encodes for MATalpha2, the catalytic subunit of the MATII isoenzyme that synthesizes S-adenosylmethionine (SAMe).	S-Adenosylmethionine	127-147	methionine adenosyltransferase 2A	Homo sapiens	0-33
26416353-2	2015	Methionine adenosyltransferase 2A (MAT2A) encodes for MATalpha2, the catalytic subunit of the MATII isoenzyme that synthesizes S-adenosylmethionine (SAMe).	S-Adenosylmethionine	127-147	methionine adenosyltransferase 2A	Homo sapiens	35-40
26307088-9	2015	Notably, DACOR1 induction resulted in down-regulation of Cystathionine beta-synthase, which is known to lead to increased levels of S-adenosyl methionine-the key methyl donor for DNA methylation.	S-Adenosylmethionine	132-153	DNMT1-associated colon cancer repressed lncRNA 1	Homo sapiens	9-15
26307088-9	2015	Notably, DACOR1 induction resulted in down-regulation of Cystathionine beta-synthase, which is known to lead to increased levels of S-adenosyl methionine-the key methyl donor for DNA methylation.	S-Adenosylmethionine	132-153	cystathionine beta-synthase	Homo sapiens	57-84
26206890-2	2015	The enzyme histamine N-methyltransferase (HNMT) inactivates HA by transferring a methyl group from S-adenosyl-l-methionine to HA, and is the only well-known pathway for termination of neurotransmission actions of HA in mammalian central nervous system.	S-Adenosylmethionine	99-122	histamine N-methyltransferase	Homo sapiens	11-40
26206890-2	2015	The enzyme histamine N-methyltransferase (HNMT) inactivates HA by transferring a methyl group from S-adenosyl-l-methionine to HA, and is the only well-known pathway for termination of neurotransmission actions of HA in mammalian central nervous system.	S-Adenosylmethionine	99-122	histamine N-methyltransferase	Homo sapiens	42-46
26238650-11	2015	We also observed that 5"-aza-induced COX-2 expression and PGE2 production were inhibited by S-adenosylmethionine (SAM), a methyl donor.	S-Adenosylmethionine	92-112	prostaglandin-endoperoxide synthase 2	Homo sapiens	37-42
26238650-11	2015	We also observed that 5"-aza-induced COX-2 expression and PGE2 production were inhibited by S-adenosylmethionine (SAM), a methyl donor.	S-Adenosylmethionine	114-117	prostaglandin-endoperoxide synthase 2	Homo sapiens	37-42
26059517-6	2015	5-Aza-2"-deoxycytidine (5-Aza-CdR), which enhances mucin-promoted probiotic effects through inducing production of Sadenosyl- L-methionine (SAMe), was used to up-regulate MUC2 expression in Caco-2 cells.	S-Adenosylmethionine	115-138	LOC100508689	Homo sapiens	51-56
26059517-6	2015	5-Aza-2"-deoxycytidine (5-Aza-CdR), which enhances mucin-promoted probiotic effects through inducing production of Sadenosyl- L-methionine (SAMe), was used to up-regulate MUC2 expression in Caco-2 cells.	S-Adenosylmethionine	115-138	mucin 2, oligomeric mucus/gel-forming	Homo sapiens	171-175
26550452-1	2015	Methionine synthase reductase (MTRR) is involved in the DNA synthesis and production of S-adenosylmethionine (SAM) and plays an important role in the carcinogenesis.	S-Adenosylmethionine	88-108	5-methyltetrahydrofolate-homocysteine methyltransferase reductase	Homo sapiens	31-35
25979827-2	2015	Met is the obligate precursor of S-adenosylmethionine (SAM), the methyl donor utilized by all methyltransferases including the polycomb repressor complex (PRC2)-specific EZH2.	S-Adenosylmethionine	33-53	enhancer of zeste 2 polycomb repressive complex 2 subunit	Homo sapiens	170-174
26289392-2	2015	MAT1A encodes the subunit that forms two methionine adenosyltransferase isoenzymes, tetrameric MAT I and dimeric MAT III, that catalyze the conversion of methionine and ATP to S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	176-196	methionine adenosyltransferase 1A	Homo sapiens	0-5
26289392-2	2015	MAT1A encodes the subunit that forms two methionine adenosyltransferase isoenzymes, tetrameric MAT I and dimeric MAT III, that catalyze the conversion of methionine and ATP to S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	176-196	methionine adenosyltransferase 1A	Homo sapiens	95-100
26289392-2	2015	MAT1A encodes the subunit that forms two methionine adenosyltransferase isoenzymes, tetrameric MAT I and dimeric MAT III, that catalyze the conversion of methionine and ATP to S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	176-196	methionine adenosyltransferase 1A	Homo sapiens	117-120
26289392-2	2015	MAT1A encodes the subunit that forms two methionine adenosyltransferase isoenzymes, tetrameric MAT I and dimeric MAT III, that catalyze the conversion of methionine and ATP to S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	198-204	methionine adenosyltransferase 1A	Homo sapiens	0-5
26289392-2	2015	MAT1A encodes the subunit that forms two methionine adenosyltransferase isoenzymes, tetrameric MAT I and dimeric MAT III, that catalyze the conversion of methionine and ATP to S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	198-204	methionine adenosyltransferase 1A	Homo sapiens	95-100
26289392-2	2015	MAT1A encodes the subunit that forms two methionine adenosyltransferase isoenzymes, tetrameric MAT I and dimeric MAT III, that catalyze the conversion of methionine and ATP to S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	198-204	methionine adenosyltransferase 1A	Homo sapiens	117-120
26041283-2	2015	This enzyme harbors methyltransferase (MTase) and nsP1 guanylylation (GT) activities catalyzing the transfer of the methyl group from S-adenosylmethionine (AdoMet) to the N7 position of a GTP molecule followed by the formation of an m(7)GMP-nsP1 adduct.	S-Adenosylmethionine	134-154	SH2 domain containing 3A	Homo sapiens	50-54
26041283-2	2015	This enzyme harbors methyltransferase (MTase) and nsP1 guanylylation (GT) activities catalyzing the transfer of the methyl group from S-adenosylmethionine (AdoMet) to the N7 position of a GTP molecule followed by the formation of an m(7)GMP-nsP1 adduct.	S-Adenosylmethionine	134-154	5'-nucleotidase, cytosolic II	Homo sapiens	237-240
26041283-2	2015	This enzyme harbors methyltransferase (MTase) and nsP1 guanylylation (GT) activities catalyzing the transfer of the methyl group from S-adenosylmethionine (AdoMet) to the N7 position of a GTP molecule followed by the formation of an m(7)GMP-nsP1 adduct.	S-Adenosylmethionine	134-154	SH2 domain containing 3A	Homo sapiens	241-245
26130251-0	2015	A Phase II Randomized, Controlled Trial of S-Adenosylmethionine in Reducing Serum alpha-Fetoprotein in Patients with Hepatitis C Cirrhosis and Elevated AFP.	S-Adenosylmethionine	43-63	alpha fetoprotein	Homo sapiens	82-99
26130251-0	2015	A Phase II Randomized, Controlled Trial of S-Adenosylmethionine in Reducing Serum alpha-Fetoprotein in Patients with Hepatitis C Cirrhosis and Elevated AFP.	S-Adenosylmethionine	43-63	alpha fetoprotein	Homo sapiens	152-155
26308914-9	2015	Conversely, the TRMT1 gene encodes a tRNA methyltransferase that dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl methionine as the methyl group donor.	S-Adenosylmethionine	138-159	tRNA methyltransferase 1	Homo sapiens	16-21
26037613-4	2015	To characterize and fully understand protein methylation, we describe here novel N-mustard analogs of S-adenosyl-l-methionine (SAM) as biochemical tools to better understand protein arginine methylation events using protein arginine methyltransferase 1 (PRMT1).	S-Adenosylmethionine	102-125	protein arginine methyltransferase 1	Homo sapiens	254-259
25979827-2	2015	Met is the obligate precursor of S-adenosylmethionine (SAM), the methyl donor utilized by all methyltransferases including the polycomb repressor complex (PRC2)-specific EZH2.	S-Adenosylmethionine	55-58	enhancer of zeste 2 polycomb repressive complex 2 subunit	Homo sapiens	170-174
25866076-6	2015	The second assay utilizes time-resolved fluorescence resonance energy transfer to directly measure the conversion of the AS3MT substrate, S-adenosylmethionine, to S-adenosylhomocysteine catalyzed by AS3MT.	S-Adenosylmethionine	138-158	arsenite methyltransferase	Homo sapiens	121-126
25866076-6	2015	The second assay utilizes time-resolved fluorescence resonance energy transfer to directly measure the conversion of the AS3MT substrate, S-adenosylmethionine, to S-adenosylhomocysteine catalyzed by AS3MT.	S-Adenosylmethionine	138-158	arsenite methyltransferase	Homo sapiens	199-204
25913073-5	2015	IL-1beta reduced the intracellular concentrations of overall primary metabolites especially those of amino acid, urea cycle, polyamine, S-adenosylmethione and glutathione synthetic pathways.	S-Adenosylmethionine	136-154	interleukin 1 beta	Homo sapiens	0-8
25903303-1	2015	Histone methyltransferase PRDM9 catalyzes the methylation of H3K4me2 (histone 3 dimethylated lysine 4) to H3K4me3 (histone 3 trimethylated lysine 4) by transferring the methyl group from S-adenosyl methionine (AdoMet).	S-Adenosylmethionine	187-208	PR/SET domain 9	Homo sapiens	26-31
26309647-1	2015	Cocktail method was used to evaluate the influence of ademetionine on the activities of CYP450 isoforms CYP1A2, CYP2D6, CYP3A4, CYP2C19, CYP2C9 and CYP2B6, which were reflected by the changes of pharmacokinetic parameters of six specific probe drugs phenacetin, metroprolol, midazolam, omeprazole, tolbutamide and bupropion, respectively.	S-Adenosylmethionine	54-66	cytochrome P450, family 1, subfamily a, polypeptide 2	Rattus norvegicus	104-110
26309647-1	2015	Cocktail method was used to evaluate the influence of ademetionine on the activities of CYP450 isoforms CYP1A2, CYP2D6, CYP3A4, CYP2C19, CYP2C9 and CYP2B6, which were reflected by the changes of pharmacokinetic parameters of six specific probe drugs phenacetin, metroprolol, midazolam, omeprazole, tolbutamide and bupropion, respectively.	S-Adenosylmethionine	54-66	cytochrome P450, family 2, subfamily d, polypeptide 4	Rattus norvegicus	112-118
26309647-1	2015	Cocktail method was used to evaluate the influence of ademetionine on the activities of CYP450 isoforms CYP1A2, CYP2D6, CYP3A4, CYP2C19, CYP2C9 and CYP2B6, which were reflected by the changes of pharmacokinetic parameters of six specific probe drugs phenacetin, metroprolol, midazolam, omeprazole, tolbutamide and bupropion, respectively.	S-Adenosylmethionine	54-66	cytochrome P450, family 2, subfamily b, polypeptide 3	Rattus norvegicus	148-154
25985628-8	2015	Met deprivation results in a rapid decrease in intracellular S-adenosyl-methionine (SAM), triggering the activation of p53 signaling, reducing pluripotent marker gene NANOG expression, and poising human ES/iPS cells for differentiation, follow by potentiated differentiation into all three germ layers.	S-Adenosylmethionine	84-87	tumor protein p53	Homo sapiens	119-122
25771539-1	2015	The protein N-terminal methyltransferase 1 (NTMT1) catalyzes the transfer of the methyl group from the S-adenosyl-l-methionine to the protein alpha-amine, resulting in formation of S-adenosyl-l-homocysteine and alpha-N-methylated proteins.	S-Adenosylmethionine	103-126	N-terminal Xaa-Pro-Lys N-methyltransferase 1	Homo sapiens	12-42
25771539-1	2015	The protein N-terminal methyltransferase 1 (NTMT1) catalyzes the transfer of the methyl group from the S-adenosyl-l-methionine to the protein alpha-amine, resulting in formation of S-adenosyl-l-homocysteine and alpha-N-methylated proteins.	S-Adenosylmethionine	103-126	N-terminal Xaa-Pro-Lys N-methyltransferase 1	Homo sapiens	44-49
25903303-1	2015	Histone methyltransferase PRDM9 catalyzes the methylation of H3K4me2 (histone 3 dimethylated lysine 4) to H3K4me3 (histone 3 trimethylated lysine 4) by transferring the methyl group from S-adenosyl methionine (AdoMet).	S-Adenosylmethionine	210-216	PR/SET domain 9	Homo sapiens	26-31
25903303-3	2015	In PRDM9, two conserved tyrosine residues Tyr357 and Tyr276 surrounding the amino group of the substrate lysine may influence the methylation activity through hydrogen bond interactions with AdoMet or the substrate lysine.	S-Adenosylmethionine	191-197	PR/SET domain 9	Homo sapiens	3-8
25712161-7	2015	Our results demonstrate the feasibility of using a triazole group to link an S-adenosyl-L-methionine analog with a peptide substrate to construct bisubstrate analogues as NTMT1 potent and selective inhibitors.	S-Adenosylmethionine	77-100	N-terminal Xaa-Pro-Lys N-methyltransferase 1	Homo sapiens	171-176
26121858-0	2015	[S-Adenosylmethionine Inhibits Expression of Vascular Endothelial Growth Factor-C Protein and Cellular Proliferation in Gastric Cancer].	S-Adenosylmethionine	0-21	vascular endothelial growth factor C	Mus musculus	45-81
26121858-1	2015	OBJECTIVE: To explore inhibitory effects of S-adenosylmethionine on vascular endothelial growth factor-C (VEGF-C) protein and cellular proliferation in gastric cancer by regulating methylation status of VEGF-C promoter.	S-Adenosylmethionine	44-64	vascular endothelial growth factor C	Mus musculus	68-104
26121858-1	2015	OBJECTIVE: To explore inhibitory effects of S-adenosylmethionine on vascular endothelial growth factor-C (VEGF-C) protein and cellular proliferation in gastric cancer by regulating methylation status of VEGF-C promoter.	S-Adenosylmethionine	44-64	vascular endothelial growth factor C	Mus musculus	106-112
26121858-1	2015	OBJECTIVE: To explore inhibitory effects of S-adenosylmethionine on vascular endothelial growth factor-C (VEGF-C) protein and cellular proliferation in gastric cancer by regulating methylation status of VEGF-C promoter.	S-Adenosylmethionine	44-64	vascular endothelial growth factor C	Mus musculus	203-209
26121858-6	2015	The treatment of S-adenosylmethionine resulted in a heavy hypermethylation of VEGF-C promoter, which consequently down regulated protein level of VEGF-C.	S-Adenosylmethionine	17-37	vascular endothelial growth factor C	Mus musculus	78-84
26121858-6	2015	The treatment of S-adenosylmethionine resulted in a heavy hypermethylation of VEGF-C promoter, which consequently down regulated protein level of VEGF-C.	S-Adenosylmethionine	17-37	vascular endothelial growth factor C	Mus musculus	146-152
26121858-9	2015	CONCLUSION: S-adenosylmethionine can effectively reverse DNA hypomethylation on VEGF-C promoter which down-regulates VEGF-C protein expression and inhibit gastric cancer growth.	S-Adenosylmethionine	12-32	vascular endothelial growth factor C	Mus musculus	80-86
26121858-9	2015	CONCLUSION: S-adenosylmethionine can effectively reverse DNA hypomethylation on VEGF-C promoter which down-regulates VEGF-C protein expression and inhibit gastric cancer growth.	S-Adenosylmethionine	12-32	vascular endothelial growth factor C	Mus musculus	117-123
25925782-3	2015	Methionine adenosyltransferase IIalpha (MAT IIalpha) is a key enzyme in the methionine cycle, catalysing the production of S-adenosylmethionine (SAM), a key methyl donor in cellular processes, and is associated with uncontrolled cell proliferation in cancer.	S-Adenosylmethionine	123-143	methionine adenosyltransferase 2A	Homo sapiens	0-51
25925782-3	2015	Methionine adenosyltransferase IIalpha (MAT IIalpha) is a key enzyme in the methionine cycle, catalysing the production of S-adenosylmethionine (SAM), a key methyl donor in cellular processes, and is associated with uncontrolled cell proliferation in cancer.	S-Adenosylmethionine	145-148	methionine adenosyltransferase 2A	Homo sapiens	0-51
31245442-5	2015	In contrast, Pkm2 knock-in induced synthesis of a methylation-donor, S-adenosylmethionine, and increased unsaturated eicosanoid groups, which contributed to the redox control and maintenance of ESC undifferentiated status.	S-Adenosylmethionine	71-89	pyruvate kinase M1/2	Homo sapiens	13-17
25887881-6	2015	The hyperhomocysteinemia of aging and dementia is attributed to decreased synthesis of adenosyl methionine by thioretinaco ozonide and ATP, causing decreased allosteric activation of cystathionine synthase and decreased allosteric inhibition of methylenetetrahydrofolate reductase and resulting in dysregulation of methionine metabolism.	S-Adenosylmethionine	87-106	methylenetetrahydrofolate reductase	Homo sapiens	245-280
25623240-7	2015	Interestingly, BmDNMT-1 formed a complex with DNA in the presence or absence of methyl group donor, S-Adenosylmethionine (AdoMet) and the AdoMet-dependent complex formation was facilitated by Zn(2+) and Mn(2+).	S-Adenosylmethionine	100-120	DNA cytosine-5 methyltransferase	Bombyx mori	15-23
25466894-2	2015	The methyl donor S-adenosylmethionine (SAM) is produced in most cells through the folate cycle, but only a few cell types generate SAM from betaine (N,N,N-trimethylglycine) via betaine-homocysteine methyltransferase (BHMT), which is expressed in the mouse ICM.	S-Adenosylmethionine	17-37	betaine--homocysteine S-methyltransferase	Homo sapiens	177-215
25466894-2	2015	The methyl donor S-adenosylmethionine (SAM) is produced in most cells through the folate cycle, but only a few cell types generate SAM from betaine (N,N,N-trimethylglycine) via betaine-homocysteine methyltransferase (BHMT), which is expressed in the mouse ICM.	S-Adenosylmethionine	17-37	betaine--homocysteine S-methyltransferase	Homo sapiens	217-221
25466894-2	2015	The methyl donor S-adenosylmethionine (SAM) is produced in most cells through the folate cycle, but only a few cell types generate SAM from betaine (N,N,N-trimethylglycine) via betaine-homocysteine methyltransferase (BHMT), which is expressed in the mouse ICM.	S-Adenosylmethionine	39-42	betaine--homocysteine S-methyltransferase	Homo sapiens	217-221
25733650-3	2015	Methylenetetrahydrofolate reductase (MTHFR) provides methyl donors for S-adenosylmethionine (SAM) synthesis and methylation reactions.	S-Adenosylmethionine	71-91	methylenetetrahydrofolate reductase	Mus musculus	0-35
25733650-3	2015	Methylenetetrahydrofolate reductase (MTHFR) provides methyl donors for S-adenosylmethionine (SAM) synthesis and methylation reactions.	S-Adenosylmethionine	71-91	methylenetetrahydrofolate reductase	Mus musculus	37-42
25733650-3	2015	Methylenetetrahydrofolate reductase (MTHFR) provides methyl donors for S-adenosylmethionine (SAM) synthesis and methylation reactions.	S-Adenosylmethionine	93-96	methylenetetrahydrofolate reductase	Mus musculus	0-35
25733650-3	2015	Methylenetetrahydrofolate reductase (MTHFR) provides methyl donors for S-adenosylmethionine (SAM) synthesis and methylation reactions.	S-Adenosylmethionine	93-96	methylenetetrahydrofolate reductase	Mus musculus	37-42
25623240-7	2015	Interestingly, BmDNMT-1 formed a complex with DNA in the presence or absence of methyl group donor, S-Adenosylmethionine (AdoMet) and the AdoMet-dependent complex formation was facilitated by Zn(2+) and Mn(2+).	S-Adenosylmethionine	122-128	DNA cytosine-5 methyltransferase	Bombyx mori	15-23
25689298-4	2015	DNA methyltransferase 3A (DNMT3A) and ratio of S-adenosylmethionine (SAM) to S-adenosylhomocysteine (SAH) brought a relative forward daily variation to global DNA methylation, and the temporary change in ratio of SAM to SAH had no influence on the DNA methylation level.	S-Adenosylmethionine	213-216	DNA methyltransferase 3A	Mus musculus	0-24
25457203-2	2015	Low levels of hepatic S-adenosylmethionine (SAMe) decrease triglyceride (TG) secretion in VLDLs, contributing to hepatosteatosis in methionine adenosyltransferase 1A knockout mice but nothing is known about the effect of SAMe on the circulating VLDL metabolism.	S-Adenosylmethionine	22-42	CD320 antigen	Mus musculus	90-94
25706873-0	2015	DNA methyltransferase 3a regulates osteoclast differentiation by coupling to an S-adenosylmethionine-producing metabolic pathway.	S-Adenosylmethionine	80-100	DNA methyltransferase 3A	Mus musculus	0-24
25706873-4	2015	We also found that receptor activator of nuclear factor-kappaB ligand (RANKL), an essential cytokine for osteoclastogenesis, induces this metabolic shift towards oxidative metabolism, which is accompanied by an increase in S-adenosylmethionine (SAM) production.	S-Adenosylmethionine	223-243	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	19-69
25706873-4	2015	We also found that receptor activator of nuclear factor-kappaB ligand (RANKL), an essential cytokine for osteoclastogenesis, induces this metabolic shift towards oxidative metabolism, which is accompanied by an increase in S-adenosylmethionine (SAM) production.	S-Adenosylmethionine	223-243	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	71-76
25706873-4	2015	We also found that receptor activator of nuclear factor-kappaB ligand (RANKL), an essential cytokine for osteoclastogenesis, induces this metabolic shift towards oxidative metabolism, which is accompanied by an increase in S-adenosylmethionine (SAM) production.	S-Adenosylmethionine	245-248	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	19-69
25706873-4	2015	We also found that receptor activator of nuclear factor-kappaB ligand (RANKL), an essential cytokine for osteoclastogenesis, induces this metabolic shift towards oxidative metabolism, which is accompanied by an increase in S-adenosylmethionine (SAM) production.	S-Adenosylmethionine	245-248	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	71-76
26937386-2	2015	Deficiencies in MTHFR result in increased levels of homocysteine, which leads to reduced levels of S-adenosylmethionine (SAM).	S-Adenosylmethionine	99-119	methylenetetrahydrofolate reductase	Mus musculus	16-21
26937386-2	2015	Deficiencies in MTHFR result in increased levels of homocysteine, which leads to reduced levels of S-adenosylmethionine (SAM).	S-Adenosylmethionine	121-124	methylenetetrahydrofolate reductase	Mus musculus	16-21
25689298-4	2015	DNA methyltransferase 3A (DNMT3A) and ratio of S-adenosylmethionine (SAM) to S-adenosylhomocysteine (SAH) brought a relative forward daily variation to global DNA methylation, and the temporary change in ratio of SAM to SAH had no influence on the DNA methylation level.	S-Adenosylmethionine	213-216	DNA methyltransferase 3A	Mus musculus	26-32
25477522-2	2015	SPL is a radical S-adenosylmethionine (SAM) enzyme, utilizing the 5"-deoxyadenosyl radical generated by SAM reductive cleavage reaction to revert SP to two thymine residues.	S-Adenosylmethionine	17-37	sphingosine-1-phosphate lyase 1	Homo sapiens	0-3
25477522-2	2015	SPL is a radical S-adenosylmethionine (SAM) enzyme, utilizing the 5"-deoxyadenosyl radical generated by SAM reductive cleavage reaction to revert SP to two thymine residues.	S-Adenosylmethionine	39-42	sphingosine-1-phosphate lyase 1	Homo sapiens	0-3
25388538-1	2015	The enzyme catechol O-methyltransferase (COMT) catalyzes the transfer of a methyl group from S-adenosylmethionine to dopamine and related catechols.	S-Adenosylmethionine	93-113	catechol-O-methyltransferase	Homo sapiens	11-39
25203626-0	2015	S-Adenosyl-L-methionine-competitive inhibitors of the histone methyltransferase EZH2 induce autophagy and enhance drug sensitivity in cancer cells.	S-Adenosylmethionine	0-23	enhancer of zeste 2 polycomb repressive complex 2 subunit	Homo sapiens	80-84
25374015-4	2015	The activator, S-adenosyl-L-methionine and the inhibitor, hydroxylamine of cystathionine-beta-synthase (CBS), aggravated and remitted the hypoxic damage in the cortex cells, respectively.	S-Adenosylmethionine	15-38	cystathionine beta synthase	Rattus norvegicus	75-102
25559387-1	2015	S-adenosyl-L-methionine (SAM) synthase (SAMS) catalyze the biosynthesis of SAM, which is a precursor for ethylene and polyamines, and a methyl donor for a number of biomolecules.	S-Adenosylmethionine	25-28	methionine adenosyltransferase 1A	Homo sapiens	40-44
25388538-1	2015	The enzyme catechol O-methyltransferase (COMT) catalyzes the transfer of a methyl group from S-adenosylmethionine to dopamine and related catechols.	S-Adenosylmethionine	93-113	catechol-O-methyltransferase	Homo sapiens	41-45
26598833-7	2015	GNMT affects transmethylation kinetics and S-adenosylmethionine (adoMet) synthesis, and facilitates the conservation of methyl groups by limiting homocysteine remethylation fluxes.	S-Adenosylmethionine	43-63	glycine N-methyltransferase	Homo sapiens	0-4
25159911-4	2015	The example analyzed here is the reaction catalyzed by catechol O-methyltransferase, a methyl transfer reaction from S-adenosylmethionine (SAM) to the nucleophilic oxygen atom of catecholate.	S-Adenosylmethionine	117-137	catechol-O-methyltransferase	Homo sapiens	55-83
25159911-4	2015	The example analyzed here is the reaction catalyzed by catechol O-methyltransferase, a methyl transfer reaction from S-adenosylmethionine (SAM) to the nucleophilic oxygen atom of catecholate.	S-Adenosylmethionine	139-142	catechol-O-methyltransferase	Homo sapiens	55-83
25511700-2	2015	S-adenosylmethionine decarboxylase (AdoMetDc) and spermidine synthase (SpdSyn) are enzymes of this pathway that catalyze successive steps, with the product of the former, decarboxylated S-adenosylmethionine (dcSAM), acting as an aminopropyl donor for the latter enzyme.	S-Adenosylmethionine	0-20	adenosylmethionine decarboxylase 1	Homo sapiens	36-44
25511700-2	2015	S-adenosylmethionine decarboxylase (AdoMetDc) and spermidine synthase (SpdSyn) are enzymes of this pathway that catalyze successive steps, with the product of the former, decarboxylated S-adenosylmethionine (dcSAM), acting as an aminopropyl donor for the latter enzyme.	S-Adenosylmethionine	0-20	spermidine synthase	Homo sapiens	50-69
26098813-3	2015	In situations of extremely low levels of S-adenosyl methionine (SAM), DNMT-3A and -3B might demethylate C-5 methyl cytosine (5mC) via deamination to thymine, which is subsequently replaced by an unmodified cytosine through the base excision repair (BER) pathway.	S-Adenosylmethionine	41-62	DNA methyltransferase 3 alpha	Homo sapiens	70-85
26098813-3	2015	In situations of extremely low levels of S-adenosyl methionine (SAM), DNMT-3A and -3B might demethylate C-5 methyl cytosine (5mC) via deamination to thymine, which is subsequently replaced by an unmodified cytosine through the base excision repair (BER) pathway.	S-Adenosylmethionine	64-67	DNA methyltransferase 3 alpha	Homo sapiens	70-85
25502219-2	2015	Polyglutamylated folates are better substrates for several enzymes involved in the generation of S-adenosylmethionine, the primary methyl group donor, and hence, GGH modulation may affect DNA methylation.	S-Adenosylmethionine	97-117	gamma-glutamyl hydrolase	Homo sapiens	162-165
26598833-7	2015	GNMT affects transmethylation kinetics and S-adenosylmethionine (adoMet) synthesis, and facilitates the conservation of methyl groups by limiting homocysteine remethylation fluxes.	S-Adenosylmethionine	65-71	glycine N-methyltransferase	Homo sapiens	0-4
25338671-0	2015	S-Adenosylmethionine and methylthioadenosine inhibit beta-catenin signaling by multiple mechanisms in liver and colon cancer.	S-Adenosylmethionine	0-20	catenin beta 1	Homo sapiens	53-65
25387667-0	2014	DNA methylation regulates expression of VEGF-C, and S-adenosylmethionine is effective for VEGF-C methylation and for inhibiting cancer growth.	S-Adenosylmethionine	52-72	vascular endothelial growth factor C	Homo sapiens	90-96
26411936-2	2015	Genetic polymorphisms such as single nucleotide polymorphisms (SNPs) in arsenic (+3 oxidation state) methyltransferase (AS3MT), which can methylate arsenic compounds using S-adenosyl-l-methionine (AdoMet), have been reported to modify arsenic methylation.	S-Adenosylmethionine	172-195	arsenite methyltransferase	Homo sapiens	72-118
26411936-2	2015	Genetic polymorphisms such as single nucleotide polymorphisms (SNPs) in arsenic (+3 oxidation state) methyltransferase (AS3MT), which can methylate arsenic compounds using S-adenosyl-l-methionine (AdoMet), have been reported to modify arsenic methylation.	S-Adenosylmethionine	172-195	arsenite methyltransferase	Homo sapiens	120-125
26411936-2	2015	Genetic polymorphisms such as single nucleotide polymorphisms (SNPs) in arsenic (+3 oxidation state) methyltransferase (AS3MT), which can methylate arsenic compounds using S-adenosyl-l-methionine (AdoMet), have been reported to modify arsenic methylation.	S-Adenosylmethionine	197-203	arsenite methyltransferase	Homo sapiens	72-118
26411936-2	2015	Genetic polymorphisms such as single nucleotide polymorphisms (SNPs) in arsenic (+3 oxidation state) methyltransferase (AS3MT), which can methylate arsenic compounds using S-adenosyl-l-methionine (AdoMet), have been reported to modify arsenic methylation.	S-Adenosylmethionine	197-203	arsenite methyltransferase	Homo sapiens	120-125
25336647-0	2014	Inter-domain communication of human cystathionine beta-synthase: structural basis of S-adenosyl-L-methionine activation.	S-Adenosylmethionine	87-108	cystathionine beta-synthase	Homo sapiens	36-63
25489090-3	2014	Here we report atomic resolution structures of Bud23-Trm112 in the apo and S-adenosyl-L-methionine (SAM)-bound forms.	S-Adenosylmethionine	75-98	tRNA methyltransferase activator subunit 11-2	Homo sapiens	53-59
25489090-3	2014	Here we report atomic resolution structures of Bud23-Trm112 in the apo and S-adenosyl-L-methionine (SAM)-bound forms.	S-Adenosylmethionine	100-103	tRNA methyltransferase activator subunit 11-2	Homo sapiens	53-59
25515537-5	2014	Unlike wild-type yeast, which accumulated glutamine, Npr2-deficient yeast metabolized glutamine into nitrogen-containing metabolites and maintained a high concentration of S-adenosyl methionine (SAM).	S-Adenosylmethionine	172-193	nitrogen permease regulating protein NPR2	Saccharomyces cerevisiae S288C	53-57
25515537-5	2014	Unlike wild-type yeast, which accumulated glutamine, Npr2-deficient yeast metabolized glutamine into nitrogen-containing metabolites and maintained a high concentration of S-adenosyl methionine (SAM).	S-Adenosylmethionine	195-198	nitrogen permease regulating protein NPR2	Saccharomyces cerevisiae S288C	53-57
25447140-0	2014	Mutational analysis of residues in human arsenic (III)  methyltransferase (hAS3MT) belonging to 5 A around  S-adenosylmethionine (SAM).	S-Adenosylmethionine	108-128	arsenite methyltransferase	Homo sapiens	75-81
25447140-0	2014	Mutational analysis of residues in human arsenic (III)  methyltransferase (hAS3MT) belonging to 5 A around  S-adenosylmethionine (SAM).	S-Adenosylmethionine	130-133	arsenite methyltransferase	Homo sapiens	75-81
25271158-3	2014	We hypothesized that the GCs enhance IFN signaling by inducing S-adenosylmethionine (AdoMet) when hepatitis B virus (HBV) replication was effectively suppressed by IFN-alpha.	S-Adenosylmethionine	63-83	interferon alpha 1	Homo sapiens	164-173
25289094-1	2014	DNA methyltransferases (including DNMT1, DNMT3A and DNMT3B), catalyze the transfer of methyl groups from S-adenosyl-l-methionine to cytosine position 5; this methylation in promoter regions silences gene expression.	S-Adenosylmethionine	105-128	DNA methyltransferase 1	Homo sapiens	34-39
25271158-3	2014	We hypothesized that the GCs enhance IFN signaling by inducing S-adenosylmethionine (AdoMet) when hepatitis B virus (HBV) replication was effectively suppressed by IFN-alpha.	S-Adenosylmethionine	85-91	interferon alpha 1	Homo sapiens	164-173
25192721-3	2014	Keeping this fact in mind, the recent work is designed to reveal the role of CAV1 in inhibiting cancer cell progression in presence of epigenetic modulators like 5-aza-2"-deoxycytidine (AZA), trichostatin A (TSA), S-adenosyl methionine (SAM) and sulforaphane (SFN).	S-Adenosylmethionine	214-235	caveolin 1	Homo sapiens	77-81
25192721-3	2014	Keeping this fact in mind, the recent work is designed to reveal the role of CAV1 in inhibiting cancer cell progression in presence of epigenetic modulators like 5-aza-2"-deoxycytidine (AZA), trichostatin A (TSA), S-adenosyl methionine (SAM) and sulforaphane (SFN).	S-Adenosylmethionine	237-240	caveolin 1	Homo sapiens	77-81
25289094-1	2014	DNA methyltransferases (including DNMT1, DNMT3A and DNMT3B), catalyze the transfer of methyl groups from S-adenosyl-l-methionine to cytosine position 5; this methylation in promoter regions silences gene expression.	S-Adenosylmethionine	105-128	DNA methyltransferase 3 alpha	Homo sapiens	41-47
25289094-1	2014	DNA methyltransferases (including DNMT1, DNMT3A and DNMT3B), catalyze the transfer of methyl groups from S-adenosyl-l-methionine to cytosine position 5; this methylation in promoter regions silences gene expression.	S-Adenosylmethionine	105-128	DNA methyltransferase 3 beta	Homo sapiens	52-58
25044645-2	2014	CBS is allosterically activated by S-adenosylmethionine (SAM), which binds to its C-terminal regulatory domain.	S-Adenosylmethionine	35-55	cystathionine beta-synthase	Homo sapiens	0-3
26461333-5	2014	Pioneer works showed how oxidized GSH inhibits the activity of S-adenosyl methionine synthetase, MAT1A, a key enzyme involved in the synthesis of S-adenosyl methionine (SAM), which is used by DNA methyltransferases (DNMTs) and histone methyltransferases (HMTs).	S-Adenosylmethionine	63-84	methionine adenosyltransferase 1A	Homo sapiens	97-102
26461333-5	2014	Pioneer works showed how oxidized GSH inhibits the activity of S-adenosyl methionine synthetase, MAT1A, a key enzyme involved in the synthesis of S-adenosyl methionine (SAM), which is used by DNA methyltransferases (DNMTs) and histone methyltransferases (HMTs).	S-Adenosylmethionine	169-172	methionine adenosyltransferase 1A	Homo sapiens	97-102
25044645-2	2014	CBS is allosterically activated by S-adenosylmethionine (SAM), which binds to its C-terminal regulatory domain.	S-Adenosylmethionine	57-60	cystathionine beta-synthase	Homo sapiens	0-3
24667534-2	2014	The purpose of the current study was to investigate the effect of the allosteric CBS activator S-adenosyl-L-methionine (SAM) on the proliferation and bioenergetics of the CBS-expressing colon cancer cell line HCT116.	S-Adenosylmethionine	95-118	cystathionine beta-synthase	Homo sapiens	81-84
25197074-0	2014	Structural insight into the molecular mechanism of allosteric activation of human cystathionine beta-synthase by S-adenosylmethionine.	S-Adenosylmethionine	113-133	cystathionine beta-synthase	Homo sapiens	82-109
24667534-0	2014	Effect of S-adenosyl-L-methionine (SAM), an allosteric activator of cystathionine-beta-synthase (CBS) on colorectal cancer cell proliferation and bioenergetics in vitro.	S-Adenosylmethionine	10-33	cystathionine beta-synthase	Homo sapiens	68-95
24667534-2	2014	The purpose of the current study was to investigate the effect of the allosteric CBS activator S-adenosyl-L-methionine (SAM) on the proliferation and bioenergetics of the CBS-expressing colon cancer cell line HCT116.	S-Adenosylmethionine	95-118	cystathionine beta-synthase	Homo sapiens	171-174
24667534-0	2014	Effect of S-adenosyl-L-methionine (SAM), an allosteric activator of cystathionine-beta-synthase (CBS) on colorectal cancer cell proliferation and bioenergetics in vitro.	S-Adenosylmethionine	10-33	cystathionine beta-synthase	Homo sapiens	97-100
24667534-0	2014	Effect of S-adenosyl-L-methionine (SAM), an allosteric activator of cystathionine-beta-synthase (CBS) on colorectal cancer cell proliferation and bioenergetics in vitro.	S-Adenosylmethionine	35-38	cystathionine beta-synthase	Homo sapiens	68-95
24578214-1	2014	OBJECTIVE: Changes in polyamine-modulated factor 1 (PMF-1) promoter methylation might favor the expression of spermidine/spermine N1-acetyltransferase 1 (SSAT-1), causing excessive consumption of S-adenosyl methionine (SAM).	S-Adenosylmethionine	196-217	polyamine modulated factor 1	Homo sapiens	22-50
24667534-0	2014	Effect of S-adenosyl-L-methionine (SAM), an allosteric activator of cystathionine-beta-synthase (CBS) on colorectal cancer cell proliferation and bioenergetics in vitro.	S-Adenosylmethionine	35-38	cystathionine beta-synthase	Homo sapiens	97-100
25180283-1	2014	S-adenosylmethionine (SAM), the unique methyl donor in DNA methylation, has been shown to lower lipopolysaccharide (LPS)-induced expression of the proinflammatory cytokine TNF-alpha and increase the expression of the anti-inflammatory cytokine IL-10 in macrophages.	S-Adenosylmethionine	0-20	tumor necrosis factor	Homo sapiens	172-181
25180283-1	2014	S-adenosylmethionine (SAM), the unique methyl donor in DNA methylation, has been shown to lower lipopolysaccharide (LPS)-induced expression of the proinflammatory cytokine TNF-alpha and increase the expression of the anti-inflammatory cytokine IL-10 in macrophages.	S-Adenosylmethionine	0-20	interleukin 10	Homo sapiens	244-249
25180283-1	2014	S-adenosylmethionine (SAM), the unique methyl donor in DNA methylation, has been shown to lower lipopolysaccharide (LPS)-induced expression of the proinflammatory cytokine TNF-alpha and increase the expression of the anti-inflammatory cytokine IL-10 in macrophages.	S-Adenosylmethionine	22-25	tumor necrosis factor	Homo sapiens	172-181
25180283-1	2014	S-adenosylmethionine (SAM), the unique methyl donor in DNA methylation, has been shown to lower lipopolysaccharide (LPS)-induced expression of the proinflammatory cytokine TNF-alpha and increase the expression of the anti-inflammatory cytokine IL-10 in macrophages.	S-Adenosylmethionine	22-25	interleukin 10	Homo sapiens	244-249
24950428-1	2014	Spore photoproduct lyase (SPL) catalyzes the repair of the UV lesion spore photoproduct (SP) in a reaction dependent on S-adenosyl-L-methionine (SAM).	S-Adenosylmethionine	120-143	sphingosine-1-phosphate lyase 1	Homo sapiens	0-24
24950428-1	2014	Spore photoproduct lyase (SPL) catalyzes the repair of the UV lesion spore photoproduct (SP) in a reaction dependent on S-adenosyl-L-methionine (SAM).	S-Adenosylmethionine	120-143	sphingosine-1-phosphate lyase 1	Homo sapiens	26-29
24950428-1	2014	Spore photoproduct lyase (SPL) catalyzes the repair of the UV lesion spore photoproduct (SP) in a reaction dependent on S-adenosyl-L-methionine (SAM).	S-Adenosylmethionine	145-148	sphingosine-1-phosphate lyase 1	Homo sapiens	0-24
24950428-1	2014	Spore photoproduct lyase (SPL) catalyzes the repair of the UV lesion spore photoproduct (SP) in a reaction dependent on S-adenosyl-L-methionine (SAM).	S-Adenosylmethionine	145-148	sphingosine-1-phosphate lyase 1	Homo sapiens	26-29
25144183-0	2014	Selenium-based S-adenosylmethionine analog reveals the mammalian seven-beta-strand methyltransferase METTL10 to be an EF1A1 lysine methyltransferase.	S-Adenosylmethionine	15-35	EEF1A lysine methyltransferase 2	Homo sapiens	101-108
24726863-2	2014	AS3MT activity requires the presence of the methyl donor S-adenosylmethionine, a product of folate-dependent one-carbon metabolism, and a reductant.	S-Adenosylmethionine	57-77	arsenite methyltransferase	Homo sapiens	0-5
24879441-6	2014	In addition, a C. elegans gene, termed samt-1, coding for a candidate membrane transport protein for the presumptive donor substrate of glycan methylation, S-adenosyl-methionine, from the cytoplasm to the Golgi was identified.	S-Adenosylmethionine	156-177	Major facilitator superfamily domain-containing protein 5	Caenorhabditis elegans	39-45
24780582-3	2014	hCBS is a complex multidomain and oligomeric protein whose activity and stability are independently regulated by the binding of S-adenosyl-methionine (SAM) to two different types of sites at its C-terminal regulatory domain.	S-Adenosylmethionine	128-149	cystathionine beta-synthase	Homo sapiens	0-4
24780582-3	2014	hCBS is a complex multidomain and oligomeric protein whose activity and stability are independently regulated by the binding of S-adenosyl-methionine (SAM) to two different types of sites at its C-terminal regulatory domain.	S-Adenosylmethionine	151-154	cystathionine beta-synthase	Homo sapiens	0-4
24649856-1	2014	UNLABELLED: Methionine adenosyltransferase (MAT) is a family of enzymes that utilizes ATP and methionine to produce S-adenosylmethionine (AdoMet), the most crucial methyl donor in the biological methylation of biomolecules and bioactive natural products.	S-Adenosylmethionine	116-136	methionine adenosyltransferase 1A	Homo sapiens	12-42
24649856-1	2014	UNLABELLED: Methionine adenosyltransferase (MAT) is a family of enzymes that utilizes ATP and methionine to produce S-adenosylmethionine (AdoMet), the most crucial methyl donor in the biological methylation of biomolecules and bioactive natural products.	S-Adenosylmethionine	116-136	methionine adenosyltransferase 1A	Homo sapiens	44-47
24649856-1	2014	UNLABELLED: Methionine adenosyltransferase (MAT) is a family of enzymes that utilizes ATP and methionine to produce S-adenosylmethionine (AdoMet), the most crucial methyl donor in the biological methylation of biomolecules and bioactive natural products.	S-Adenosylmethionine	138-144	methionine adenosyltransferase 1A	Homo sapiens	12-42
24649856-1	2014	UNLABELLED: Methionine adenosyltransferase (MAT) is a family of enzymes that utilizes ATP and methionine to produce S-adenosylmethionine (AdoMet), the most crucial methyl donor in the biological methylation of biomolecules and bioactive natural products.	S-Adenosylmethionine	138-144	methionine adenosyltransferase 1A	Homo sapiens	44-47
24943396-0	2014	Striatal adenosine A2A receptor expression is controlled by S-adenosyl-L-methionine-mediated methylation.	S-Adenosylmethionine	60-83	adenosine A2a receptor	Homo sapiens	9-31
24943396-2	2014	Interestingly, previous in vitro studies demonstrated that A2AR expression levels are reduced after treatment with S-adenosyl-L-methionine (SAM), a methyl donor molecule involved in the methylation of important biological structures such as DNA, proteins, and lipids.	S-Adenosylmethionine	115-138	adenosine A2a receptor	Homo sapiens	59-63
24943396-2	2014	Interestingly, previous in vitro studies demonstrated that A2AR expression levels are reduced after treatment with S-adenosyl-L-methionine (SAM), a methyl donor molecule involved in the methylation of important biological structures such as DNA, proteins, and lipids.	S-Adenosylmethionine	140-143	adenosine A2a receptor	Homo sapiens	59-63
25062268-3	2014	Genome comparisons, knockouts, and in vitro enzyme studies identified a new S-adenosyl-l-methionine-dependent S-MT (TmtA) that is, surprisingly, encoded outside the gli gene cluster.	S-Adenosylmethionine	78-99	GLI family zinc finger 1	Homo sapiens	165-168
24899176-8	2014	Our analyses permitted putative identification of rotavirus VP3 active-site residues, including those that form the ribose-2"-O-methyltransferase catalytic tetrad, interact with S-adenosyl-l-methionine, and contribute to autoguanylation.	S-Adenosylmethionine	178-201	VP3	Rotavirus A	60-63
25063302-5	2014	Recombinant TrmO employs S-adenosyl-L-methionine (AdoMet) as a methyl donor to methylate t(6)A to form m(6)t(6)A in tRNA(Thr).	S-Adenosylmethionine	25-48	tRNA methyltransferase O	Homo sapiens	12-16
25063302-5	2014	Recombinant TrmO employs S-adenosyl-L-methionine (AdoMet) as a methyl donor to methylate t(6)A to form m(6)t(6)A in tRNA(Thr).	S-Adenosylmethionine	50-56	tRNA methyltransferase O	Homo sapiens	12-16
24578214-1	2014	OBJECTIVE: Changes in polyamine-modulated factor 1 (PMF-1) promoter methylation might favor the expression of spermidine/spermine N1-acetyltransferase 1 (SSAT-1), causing excessive consumption of S-adenosyl methionine (SAM).	S-Adenosylmethionine	196-217	polyamine modulated factor 1	Homo sapiens	52-57
24578214-1	2014	OBJECTIVE: Changes in polyamine-modulated factor 1 (PMF-1) promoter methylation might favor the expression of spermidine/spermine N1-acetyltransferase 1 (SSAT-1), causing excessive consumption of S-adenosyl methionine (SAM).	S-Adenosylmethionine	196-217	spermidine/spermine N1-acetyltransferase 1	Homo sapiens	110-152
24578214-1	2014	OBJECTIVE: Changes in polyamine-modulated factor 1 (PMF-1) promoter methylation might favor the expression of spermidine/spermine N1-acetyltransferase 1 (SSAT-1), causing excessive consumption of S-adenosyl methionine (SAM).	S-Adenosylmethionine	196-217	spermidine/spermine N1-acetyltransferase 1	Homo sapiens	154-160
24578214-1	2014	OBJECTIVE: Changes in polyamine-modulated factor 1 (PMF-1) promoter methylation might favor the expression of spermidine/spermine N1-acetyltransferase 1 (SSAT-1), causing excessive consumption of S-adenosyl methionine (SAM).	S-Adenosylmethionine	219-222	polyamine modulated factor 1	Homo sapiens	22-50
24578214-1	2014	OBJECTIVE: Changes in polyamine-modulated factor 1 (PMF-1) promoter methylation might favor the expression of spermidine/spermine N1-acetyltransferase 1 (SSAT-1), causing excessive consumption of S-adenosyl methionine (SAM).	S-Adenosylmethionine	219-222	polyamine modulated factor 1	Homo sapiens	52-57
24578214-1	2014	OBJECTIVE: Changes in polyamine-modulated factor 1 (PMF-1) promoter methylation might favor the expression of spermidine/spermine N1-acetyltransferase 1 (SSAT-1), causing excessive consumption of S-adenosyl methionine (SAM).	S-Adenosylmethionine	219-222	spermidine/spermine N1-acetyltransferase 1	Homo sapiens	110-152
24578214-1	2014	OBJECTIVE: Changes in polyamine-modulated factor 1 (PMF-1) promoter methylation might favor the expression of spermidine/spermine N1-acetyltransferase 1 (SSAT-1), causing excessive consumption of S-adenosyl methionine (SAM).	S-Adenosylmethionine	219-222	spermidine/spermine N1-acetyltransferase 1	Homo sapiens	154-160
27508177-4	2014	Alterations in the methylation of the promoter of methyl adenosyltransferase MAT1A and MAT2A genes in HCC result in decreased S-adenosylmethionine levels, global DNA hypomethylation, and deregulation of signal transduction pathways linked to methionine metabolism and methyl adenosyltransferases activity.	S-Adenosylmethionine	126-146	methionine adenosyltransferase 1A	Homo sapiens	77-82
24847974-0	2014	A fragment-based approach to identifying S-adenosyl-l-methionine -competitive inhibitors of catechol O-methyl transferase (COMT).	S-Adenosylmethionine	41-64	catechol-O-methyltransferase	Homo sapiens	92-121
24847974-0	2014	A fragment-based approach to identifying S-adenosyl-l-methionine -competitive inhibitors of catechol O-methyl transferase (COMT).	S-Adenosylmethionine	41-64	catechol-O-methyltransferase	Homo sapiens	123-127
24955845-6	2014	We show here that (1) the specific activity of CKB is significantly reduced in the brains of PIMT-deficient mice, (2) that in vitro aging of recombinant CKB results in significant accumulation of isoAsp sites with concomitant loss of enzymatic activity, and (3) that incubation of in vitro aged CKB with PIMT and its methyl donor S-adenosyl-L-methionine substantially repairs the aged CKB with regard to both its isoAsp content and its enzymatic activity.	S-Adenosylmethionine	330-353	creatine kinase, brain	Mus musculus	47-50
24955845-6	2014	We show here that (1) the specific activity of CKB is significantly reduced in the brains of PIMT-deficient mice, (2) that in vitro aging of recombinant CKB results in significant accumulation of isoAsp sites with concomitant loss of enzymatic activity, and (3) that incubation of in vitro aged CKB with PIMT and its methyl donor S-adenosyl-L-methionine substantially repairs the aged CKB with regard to both its isoAsp content and its enzymatic activity.	S-Adenosylmethionine	330-353	creatine kinase, brain	Mus musculus	153-156
24955845-6	2014	We show here that (1) the specific activity of CKB is significantly reduced in the brains of PIMT-deficient mice, (2) that in vitro aging of recombinant CKB results in significant accumulation of isoAsp sites with concomitant loss of enzymatic activity, and (3) that incubation of in vitro aged CKB with PIMT and its methyl donor S-adenosyl-L-methionine substantially repairs the aged CKB with regard to both its isoAsp content and its enzymatic activity.	S-Adenosylmethionine	330-353	creatine kinase, brain	Mus musculus	153-156
24955845-6	2014	We show here that (1) the specific activity of CKB is significantly reduced in the brains of PIMT-deficient mice, (2) that in vitro aging of recombinant CKB results in significant accumulation of isoAsp sites with concomitant loss of enzymatic activity, and (3) that incubation of in vitro aged CKB with PIMT and its methyl donor S-adenosyl-L-methionine substantially repairs the aged CKB with regard to both its isoAsp content and its enzymatic activity.	S-Adenosylmethionine	330-353	creatine kinase B	Homo sapiens	153-156
27508177-4	2014	Alterations in the methylation of the promoter of methyl adenosyltransferase MAT1A and MAT2A genes in HCC result in decreased S-adenosylmethionine levels, global DNA hypomethylation, and deregulation of signal transduction pathways linked to methionine metabolism and methyl adenosyltransferases activity.	S-Adenosylmethionine	126-146	methionine adenosyltransferase 2A	Homo sapiens	87-92
27508177-5	2014	Changes in S-adenosylmethionine levels may also depend on MAT1A mRNA destabilization associated with MAT2A mRNA stabilization by specific proteins.	S-Adenosylmethionine	11-31	methionine adenosyltransferase 1A	Homo sapiens	58-63
27508177-5	2014	Changes in S-adenosylmethionine levels may also depend on MAT1A mRNA destabilization associated with MAT2A mRNA stabilization by specific proteins.	S-Adenosylmethionine	11-31	methionine adenosyltransferase 2A	Homo sapiens	101-106
24927133-5	2014	Here, we report the development and validation of a highly sensitive and robust luminescence-based assay for NSD1 and other methyltransferases that use S-adenosylmethionine (SAM) as a methyl donor.	S-Adenosylmethionine	152-172	nuclear receptor binding SET domain protein 1	Homo sapiens	109-113
24927133-5	2014	Here, we report the development and validation of a highly sensitive and robust luminescence-based assay for NSD1 and other methyltransferases that use S-adenosylmethionine (SAM) as a methyl donor.	S-Adenosylmethionine	174-177	nuclear receptor binding SET domain protein 1	Homo sapiens	109-113
24767850-6	2014	Based on enzyme kinetics and docking studies, we propose that tanshindiol-mediated inhibition of EZH2 activity is competitive for the substrate S-adenosylmethionine.	S-Adenosylmethionine	146-164	enhancer of zeste 2 polycomb repressive complex 2 subunit	Homo sapiens	97-101
24598884-3	2014	Both reactions are catalyzed by arsenic (+3 oxidation state) methyltransferase (AS3MT) using S-adenosylmethionine (SAM) as the methyl donor, yielding the methylated product and S-adenosylhomocysteine (SAH), a potent product-inhibitor of AS3MT.	S-Adenosylmethionine	93-113	arsenite methyltransferase	Homo sapiens	80-85
24726727-1	2014	Protein arginine methyltransferase 7 (PRMT7) is a member of a family of enzymes that catalyze the transfer of methyl groups from S-adenosyl-l-methionine to nitrogen atoms on arginine residues.	S-Adenosylmethionine	129-152	Protein arginine N-methyltransferase 7	Caenorhabditis elegans	0-36
24726727-1	2014	Protein arginine methyltransferase 7 (PRMT7) is a member of a family of enzymes that catalyze the transfer of methyl groups from S-adenosyl-l-methionine to nitrogen atoms on arginine residues.	S-Adenosylmethionine	129-152	Protein arginine N-methyltransferase 7	Caenorhabditis elegans	38-43
24800880-1	2014	PURPOSE: Glycine N-methyltransferase (GNMT) affects genetic stability by regulating the ratio of S-adenosylmethionine to S-adenosylhomocysteine, by binding to folate, and by interacting with environmental carcinogens.	S-Adenosylmethionine	97-117	glycine N-methyltransferase	Homo sapiens	9-36
24800880-1	2014	PURPOSE: Glycine N-methyltransferase (GNMT) affects genetic stability by regulating the ratio of S-adenosylmethionine to S-adenosylhomocysteine, by binding to folate, and by interacting with environmental carcinogens.	S-Adenosylmethionine	97-117	glycine N-methyltransferase	Homo sapiens	38-42
24730580-2	2014	DMT is produced via the action of INMT on the endogenous substrates tryptamine and S-adenosyl-l-methionine (SAM).	S-Adenosylmethionine	83-106	indolethylamine N-methyltransferase	Homo sapiens	34-38
24730580-2	2014	DMT is produced via the action of INMT on the endogenous substrates tryptamine and S-adenosyl-l-methionine (SAM).	S-Adenosylmethionine	108-111	indolethylamine N-methyltransferase	Homo sapiens	34-38
24746817-3	2014	Metabolomic analysis of hemolymph from apoptosis-deficient mutants revealed increased sarcosine and reduced S-adenosyl-methionine (SAM) levels due to glycine N-methyltransferase (Gnmt) upregulation.	S-Adenosylmethionine	108-129	Glycine N-methyltransferase	Drosophila melanogaster	179-183
24746817-3	2014	Metabolomic analysis of hemolymph from apoptosis-deficient mutants revealed increased sarcosine and reduced S-adenosyl-methionine (SAM) levels due to glycine N-methyltransferase (Gnmt) upregulation.	S-Adenosylmethionine	131-134	Glycine N-methyltransferase	Drosophila melanogaster	150-177
24746804-4	2014	Met deprivation results in a rapid decrease in intracellular S-adenosylmethionine (SAM), triggering the activation of p53-p38 signaling, reducing NANOG expression, and poising human iPSC/ESCs for differentiation, follow by potentiated differentiation into all three germ layers.	S-Adenosylmethionine	83-86	tumor protein p53	Homo sapiens	118-121
24746804-4	2014	Met deprivation results in a rapid decrease in intracellular S-adenosylmethionine (SAM), triggering the activation of p53-p38 signaling, reducing NANOG expression, and poising human iPSC/ESCs for differentiation, follow by potentiated differentiation into all three germ layers.	S-Adenosylmethionine	83-86	mitogen-activated protein kinase 14	Homo sapiens	122-125
24598884-3	2014	Both reactions are catalyzed by arsenic (+3 oxidation state) methyltransferase (AS3MT) using S-adenosylmethionine (SAM) as the methyl donor, yielding the methylated product and S-adenosylhomocysteine (SAH), a potent product-inhibitor of AS3MT.	S-Adenosylmethionine	93-113	arsenite methyltransferase	Homo sapiens	237-242
24598884-3	2014	Both reactions are catalyzed by arsenic (+3 oxidation state) methyltransferase (AS3MT) using S-adenosylmethionine (SAM) as the methyl donor, yielding the methylated product and S-adenosylhomocysteine (SAH), a potent product-inhibitor of AS3MT.	S-Adenosylmethionine	115-118	arsenite methyltransferase	Homo sapiens	80-85
24598884-3	2014	Both reactions are catalyzed by arsenic (+3 oxidation state) methyltransferase (AS3MT) using S-adenosylmethionine (SAM) as the methyl donor, yielding the methylated product and S-adenosylhomocysteine (SAH), a potent product-inhibitor of AS3MT.	S-Adenosylmethionine	115-118	arsenite methyltransferase	Homo sapiens	237-242
24224954-3	2014	Recently, we reported that the decrease in the ratio of S-adenosylmethionine (SAM) to S-adenosylhomocysteine (SAH) that occurs with alcoholic liver injury renders hepatocytes sensitive to TNF cytotoxicity.	S-Adenosylmethionine	56-76	tumor necrosis factor	Homo sapiens	188-191
24717514-4	2014	NNMT methylates nicotinamide (vitamin B3) using S-adenosylmethionine (SAM) as a methyl donor.	S-Adenosylmethionine	48-68	nicotinamide N-methyltransferase	Homo sapiens	0-4
24717514-4	2014	NNMT methylates nicotinamide (vitamin B3) using S-adenosylmethionine (SAM) as a methyl donor.	S-Adenosylmethionine	70-73	nicotinamide N-methyltransferase	Homo sapiens	0-4
24224954-3	2014	Recently, we reported that the decrease in the ratio of S-adenosylmethionine (SAM) to S-adenosylhomocysteine (SAH) that occurs with alcoholic liver injury renders hepatocytes sensitive to TNF cytotoxicity.	S-Adenosylmethionine	78-81	tumor necrosis factor	Homo sapiens	188-191
26202509-0	2014	S-Adenosylmethionine attenuates lipopolysaccharide-induced liver injury by downregulating the Toll-like receptor 4 signal in Kupffer cells.	S-Adenosylmethionine	0-20	toll-like receptor 4	Mus musculus	94-114
24563539-3	2014	We have previously reported the discovery of EPZ005678 and EPZ-6438, potent and selective S-adenosyl-methionine-competitive small molecule inhibitors of EZH2.	S-Adenosylmethionine	90-111	enhancer of zeste 2 polycomb repressive complex 2 subunit	Homo sapiens	153-157
24495518-0	2014	S-adenosylmethionine inhibits the activated phenotype of human hepatic stellate cells via Rac1 and matrix metalloproteinases.	S-Adenosylmethionine	0-20	Rac family small GTPase 1	Homo sapiens	90-94
24422557-3	2014	The first step is the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-l-methionine (SAM) to the histidine residue of EF2, forming a C-C bond.	S-Adenosylmethionine	98-101	eukaryotic translation elongation factor 2	Homo sapiens	131-134
24412677-1	2014	Methylenetetrahydrofolate reductase (MTHFR) is necessary for the synthesis of methionine and S-adenosylmethionine, which is necessary for CNS (re-)myelination.	S-Adenosylmethionine	93-113	methylenetetrahydrofolate reductase	Homo sapiens	0-35
24412677-1	2014	Methylenetetrahydrofolate reductase (MTHFR) is necessary for the synthesis of methionine and S-adenosylmethionine, which is necessary for CNS (re-)myelination.	S-Adenosylmethionine	93-113	methylenetetrahydrofolate reductase	Homo sapiens	37-42
24532333-1	2014	Spore photoproduct lyase (SPL), a member of the radical S-adenosyl-L-methionine (SAM) superfamily, catalyzes the direct reversal of the spore photoproduct, a thymine dimer specific to bacterial spores, to two thymines.	S-Adenosylmethionine	58-79	sphingosine-1-phosphate lyase 1	Homo sapiens	0-24
24532333-1	2014	Spore photoproduct lyase (SPL), a member of the radical S-adenosyl-L-methionine (SAM) superfamily, catalyzes the direct reversal of the spore photoproduct, a thymine dimer specific to bacterial spores, to two thymines.	S-Adenosylmethionine	58-79	sphingosine-1-phosphate lyase 1	Homo sapiens	26-29
23974653-0	2014	Reduced response of Cystathionine Beta-Synthase (CBS) to S-Adenosylmethionine (SAM): Identification and functional analysis of CBS gene mutations in Homocystinuria patients.	S-Adenosylmethionine	57-77	cystathionine beta-synthase	Homo sapiens	20-47
23974653-0	2014	Reduced response of Cystathionine Beta-Synthase (CBS) to S-Adenosylmethionine (SAM): Identification and functional analysis of CBS gene mutations in Homocystinuria patients.	S-Adenosylmethionine	57-77	cystathionine beta-synthase	Homo sapiens	49-52
23974653-0	2014	Reduced response of Cystathionine Beta-Synthase (CBS) to S-Adenosylmethionine (SAM): Identification and functional analysis of CBS gene mutations in Homocystinuria patients.	S-Adenosylmethionine	79-82	cystathionine beta-synthase	Homo sapiens	20-47
23974653-0	2014	Reduced response of Cystathionine Beta-Synthase (CBS) to S-Adenosylmethionine (SAM): Identification and functional analysis of CBS gene mutations in Homocystinuria patients.	S-Adenosylmethionine	79-82	cystathionine beta-synthase	Homo sapiens	49-52
23974653-0	2014	Reduced response of Cystathionine Beta-Synthase (CBS) to S-Adenosylmethionine (SAM): Identification and functional analysis of CBS gene mutations in Homocystinuria patients.	S-Adenosylmethionine	79-82	cystathionine beta-synthase	Homo sapiens	127-130
24320160-0	2014	Profiling substrates of protein arginine N-methyltransferase 3 with S-adenosyl-L-methionine analogues.	S-Adenosylmethionine	68-91	protein arginine methyltransferase 3	Homo sapiens	24-62
24320160-1	2014	Protein arginine N-methyltransferase 3 (PRMT3) belongs to the family of type I PRMTs and harbors the activity to use S-adenosyl-l-methionine (SAM) as a methyl-donor cofactor for protein arginine labeling.	S-Adenosylmethionine	117-140	protein arginine methyltransferase 3	Homo sapiens	0-38
24320160-1	2014	Protein arginine N-methyltransferase 3 (PRMT3) belongs to the family of type I PRMTs and harbors the activity to use S-adenosyl-l-methionine (SAM) as a methyl-donor cofactor for protein arginine labeling.	S-Adenosylmethionine	117-140	protein arginine methyltransferase 3	Homo sapiens	40-45
24320160-1	2014	Protein arginine N-methyltransferase 3 (PRMT3) belongs to the family of type I PRMTs and harbors the activity to use S-adenosyl-l-methionine (SAM) as a methyl-donor cofactor for protein arginine labeling.	S-Adenosylmethionine	142-145	protein arginine methyltransferase 3	Homo sapiens	0-38
24320160-1	2014	Protein arginine N-methyltransferase 3 (PRMT3) belongs to the family of type I PRMTs and harbors the activity to use S-adenosyl-l-methionine (SAM) as a methyl-donor cofactor for protein arginine labeling.	S-Adenosylmethionine	142-145	protein arginine methyltransferase 3	Homo sapiens	40-45
24636201-1	2014	BACKGROUND: Methionine adenosyltransferase 2A (MAT2A) is an enzyme that catalyzes the formation of S-adenosylmethionine (SAMe) by joining methionine and ATP.	S-Adenosylmethionine	99-119	methionine adenosyltransferase 2A	Homo sapiens	12-45
24636201-1	2014	BACKGROUND: Methionine adenosyltransferase 2A (MAT2A) is an enzyme that catalyzes the formation of S-adenosylmethionine (SAMe) by joining methionine and ATP.	S-Adenosylmethionine	99-119	methionine adenosyltransferase 2A	Homo sapiens	47-52
24422557-3	2014	The first step is the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-l-methionine (SAM) to the histidine residue of EF2, forming a C-C bond.	S-Adenosylmethionine	73-96	eukaryotic translation elongation factor 2	Homo sapiens	131-134
24126418-7	2014	Down-regulation of MAT1A could lead to decreases in S-adenosylmethionine (SAMe), which is known to protect against APAP toxicity.	S-Adenosylmethionine	52-72	methionine adenosyltransferase I, alpha	Mus musculus	19-24
24286468-7	2014	Alteration of MTHFR function is expected to influence accumulation of the methyl donor S-adenosyl-L-methionine (SAM).	S-Adenosylmethionine	87-110	methylenetetrahydrofolate reductase	Homo sapiens	14-19
24155332-0	2014	S-adenosylmethionine limitation induces p38 mitogen-activated protein kinase and triggers cell cycle arrest in G1.	S-Adenosylmethionine	2-20	mitogen-activated protein kinase 14	Homo sapiens	40-43
24696348-6	2014	The N-terminal domain of NS5 has distinct GTP and S-adenosylmethionine (SAM) binding sites.	S-Adenosylmethionine	50-70	Raf-1 proto-oncogene, serine/threonine kinase	Homo sapiens	25-28
24696348-6	2014	The N-terminal domain of NS5 has distinct GTP and S-adenosylmethionine (SAM) binding sites.	S-Adenosylmethionine	72-75	Raf-1 proto-oncogene, serine/threonine kinase	Homo sapiens	25-28
24352086-1	2013	Vitamin B12 is a cofactor of methionine synthase in the synthesis of methionine, the precursor of the universal methyl donor S-Adenosylmethionine (SAMe), which is involved in different epigenomic regulatory mechanisms and especially in brain development.	S-Adenosylmethionine	125-145	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	29-48
23896663-0	2013	S-adenosylmethionine-induced adipogenesis is accompanied by suppression of Wnt/beta-catenin and Hedgehog signaling pathways.	S-Adenosylmethionine	2-20	catenin (cadherin associated protein), beta 1	Mus musculus	79-91
24148083-1	2013	Human 5"-methylthioadenosine phosphorylase (MTAP) is solely responsible for 5"-methylthioadenosine (MTA) metabolism to permit S-adenosylmethionine salvage.	S-Adenosylmethionine	126-146	methylthioadenosine phosphorylase	Homo sapiens	6-42
24148083-1	2013	Human 5"-methylthioadenosine phosphorylase (MTAP) is solely responsible for 5"-methylthioadenosine (MTA) metabolism to permit S-adenosylmethionine salvage.	S-Adenosylmethionine	126-146	methylthioadenosine phosphorylase	Homo sapiens	44-48
24101362-2	2013	Genes encoding enzymes for methylenetetrahydrofolate reductase (MTHFR) and methionine synthase (MTR) may determine biomarkers of the cycle including homocysteine (HCY), S-adenosylmethionine (SAM) and S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	169-189	methylenetetrahydrofolate reductase	Homo sapiens	27-62
24101362-2	2013	Genes encoding enzymes for methylenetetrahydrofolate reductase (MTHFR) and methionine synthase (MTR) may determine biomarkers of the cycle including homocysteine (HCY), S-adenosylmethionine (SAM) and S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	169-189	methylenetetrahydrofolate reductase	Homo sapiens	64-69
24101362-2	2013	Genes encoding enzymes for methylenetetrahydrofolate reductase (MTHFR) and methionine synthase (MTR) may determine biomarkers of the cycle including homocysteine (HCY), S-adenosylmethionine (SAM) and S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	169-189	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	75-94
24101362-2	2013	Genes encoding enzymes for methylenetetrahydrofolate reductase (MTHFR) and methionine synthase (MTR) may determine biomarkers of the cycle including homocysteine (HCY), S-adenosylmethionine (SAM) and S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	191-194	methylenetetrahydrofolate reductase	Homo sapiens	27-62
24101362-2	2013	Genes encoding enzymes for methylenetetrahydrofolate reductase (MTHFR) and methionine synthase (MTR) may determine biomarkers of the cycle including homocysteine (HCY), S-adenosylmethionine (SAM) and S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	191-194	methylenetetrahydrofolate reductase	Homo sapiens	64-69
24101362-2	2013	Genes encoding enzymes for methylenetetrahydrofolate reductase (MTHFR) and methionine synthase (MTR) may determine biomarkers of the cycle including homocysteine (HCY), S-adenosylmethionine (SAM) and S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	191-194	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	75-94
24124590-0	2013	Residues in human arsenic (+3 oxidation state) methyltransferase forming potential hydrogen bond network around S-adenosylmethionine.	S-Adenosylmethionine	112-132	arsenite methyltransferase	Homo sapiens	18-64
24124590-1	2013	Residues Tyr59, Gly78, Ser79, Met103, Gln107, Ile136 and Glu137 in human arsenic (+3 oxidation state) methyltransferase (hAS3MT) were deduced to form a potential hydrogen bond network around S-adenosylmethionine (SAM) from the sequence alignment between Cyanidioschyzon merolae arsenite S-adenosylmethyltransferase (CmArsM) and hAS3MT.	S-Adenosylmethionine	191-211	arsenite methyltransferase	Homo sapiens	73-119
24124590-1	2013	Residues Tyr59, Gly78, Ser79, Met103, Gln107, Ile136 and Glu137 in human arsenic (+3 oxidation state) methyltransferase (hAS3MT) were deduced to form a potential hydrogen bond network around S-adenosylmethionine (SAM) from the sequence alignment between Cyanidioschyzon merolae arsenite S-adenosylmethyltransferase (CmArsM) and hAS3MT.	S-Adenosylmethionine	191-211	arsenite methyltransferase	Homo sapiens	121-127
23505042-1	2013	UNLABELLED: Methionine adenosyltransferase 1A (MAT1A) and glycine N-methyltransferase (GNMT) are the primary genes involved in hepatic S-adenosylmethionine (SAMe) synthesis and degradation, respectively.	S-Adenosylmethionine	135-155	methionine adenosyltransferase I, alpha	Mus musculus	12-45
23505042-1	2013	UNLABELLED: Methionine adenosyltransferase 1A (MAT1A) and glycine N-methyltransferase (GNMT) are the primary genes involved in hepatic S-adenosylmethionine (SAMe) synthesis and degradation, respectively.	S-Adenosylmethionine	135-155	methionine adenosyltransferase I, alpha	Mus musculus	47-52
23505042-1	2013	UNLABELLED: Methionine adenosyltransferase 1A (MAT1A) and glycine N-methyltransferase (GNMT) are the primary genes involved in hepatic S-adenosylmethionine (SAMe) synthesis and degradation, respectively.	S-Adenosylmethionine	135-155	glycine N-methyltransferase	Mus musculus	58-85
23505042-1	2013	UNLABELLED: Methionine adenosyltransferase 1A (MAT1A) and glycine N-methyltransferase (GNMT) are the primary genes involved in hepatic S-adenosylmethionine (SAMe) synthesis and degradation, respectively.	S-Adenosylmethionine	135-155	glycine N-methyltransferase	Mus musculus	87-91
23665184-1	2013	Downregulation of liver-specific MAT1A gene, encoding S-adenosylmethionine (SAM) synthesizing isozymes MATI/III, and upregulation of widely expressed MAT2A, encoding MATII isozyme, known as MAT1A:MAT2A switch, occurs in hepatocellular carcinoma (HCC).	S-Adenosylmethionine	54-74	methionine adenosyltransferase 1A	Homo sapiens	33-38
23665184-1	2013	Downregulation of liver-specific MAT1A gene, encoding S-adenosylmethionine (SAM) synthesizing isozymes MATI/III, and upregulation of widely expressed MAT2A, encoding MATII isozyme, known as MAT1A:MAT2A switch, occurs in hepatocellular carcinoma (HCC).	S-Adenosylmethionine	76-79	methionine adenosyltransferase 1A	Homo sapiens	33-38
24385849-2	2013	The enzyme methylenetetrahydrofolate reductase (MTHFR) catalyzes the reduction of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate in the rate-limiting step of the cycle involving the methyl donor S-adenosyl-L-methionine (SAM).	S-Adenosylmethionine	207-230	methylenetetrahydrofolate reductase	Homo sapiens	11-46
24385849-2	2013	The enzyme methylenetetrahydrofolate reductase (MTHFR) catalyzes the reduction of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate in the rate-limiting step of the cycle involving the methyl donor S-adenosyl-L-methionine (SAM).	S-Adenosylmethionine	207-230	methylenetetrahydrofolate reductase	Homo sapiens	48-53
24385849-2	2013	The enzyme methylenetetrahydrofolate reductase (MTHFR) catalyzes the reduction of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate in the rate-limiting step of the cycle involving the methyl donor S-adenosyl-L-methionine (SAM).	S-Adenosylmethionine	232-235	methylenetetrahydrofolate reductase	Homo sapiens	11-46
24385849-2	2013	The enzyme methylenetetrahydrofolate reductase (MTHFR) catalyzes the reduction of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate in the rate-limiting step of the cycle involving the methyl donor S-adenosyl-L-methionine (SAM).	S-Adenosylmethionine	232-235	methylenetetrahydrofolate reductase	Homo sapiens	48-53
24018397-1	2013	Phenylethanolamine N-methyltransferase (PNMT) catalyzes the conversion of norepinephrine (noradrenaline) to epinephrine (adrenaline) while, concomitantly, S-adenosyl-L-methionine (AdoMet) is converted to S-adenosyl-L-homocysteine.	S-Adenosylmethionine	155-178	phenylethanolamine N-methyltransferase	Homo sapiens	0-38
24018397-1	2013	Phenylethanolamine N-methyltransferase (PNMT) catalyzes the conversion of norepinephrine (noradrenaline) to epinephrine (adrenaline) while, concomitantly, S-adenosyl-L-methionine (AdoMet) is converted to S-adenosyl-L-homocysteine.	S-Adenosylmethionine	155-178	phenylethanolamine N-methyltransferase	Homo sapiens	40-44
24018397-1	2013	Phenylethanolamine N-methyltransferase (PNMT) catalyzes the conversion of norepinephrine (noradrenaline) to epinephrine (adrenaline) while, concomitantly, S-adenosyl-L-methionine (AdoMet) is converted to S-adenosyl-L-homocysteine.	S-Adenosylmethionine	180-186	phenylethanolamine N-methyltransferase	Homo sapiens	0-38
24018397-1	2013	Phenylethanolamine N-methyltransferase (PNMT) catalyzes the conversion of norepinephrine (noradrenaline) to epinephrine (adrenaline) while, concomitantly, S-adenosyl-L-methionine (AdoMet) is converted to S-adenosyl-L-homocysteine.	S-Adenosylmethionine	180-186	phenylethanolamine N-methyltransferase	Homo sapiens	40-44
24046187-0	2013	S-adenosyl methionine prevents endothelial dysfunction by inducing heme oxygenase-1 in vascular endothelial cells.	S-Adenosylmethionine	2-21	heme oxygenase 1	Homo sapiens	67-83
24043838-2	2013	CBS condenses serine and homocysteine to cystathionine with the help of three cofactors, heme, pyridoxal-5"-phosphate, and S-adenosyl-l-methionine.	S-Adenosylmethionine	123-146	cystathionine beta-synthase	Homo sapiens	0-3
24043838-6	2013	The absence of large conformational changes and the crystal structure of the partially activated pathogenic D444N mutant suggest that the rotation of CBS motifs and relaxation of loops delineating the entrance to the catalytic site represent the most likely molecular mechanism of CBS activation by S-adenosyl-l-methionine.	S-Adenosylmethionine	299-322	cystathionine beta-synthase	Homo sapiens	150-153
23946480-0	2013	Automethylation of protein arginine methyltransferase 8 (PRMT8) regulates activity by impeding S-adenosylmethionine sensitivity.	S-Adenosylmethionine	95-115	protein arginine methyltransferase 8	Homo sapiens	19-55
23946480-0	2013	Automethylation of protein arginine methyltransferase 8 (PRMT8) regulates activity by impeding S-adenosylmethionine sensitivity.	S-Adenosylmethionine	95-115	protein arginine methyltransferase 8	Homo sapiens	57-62
23453262-2	2013	The methyl donor, S-adenosylmethionine (SAM), is biosynthesized from methionine and adenosine triphosphate by methionine adenosyltransferase 2a (Mat2a) in the one-carbon (C1) metabolism pathway.	S-Adenosylmethionine	18-38	methionine adenosyltransferase 2A	Homo sapiens	110-143
23654281-0	2013	Synthetic gene circuit-mediated monitoring of endogenous metabolites: identification of GAL11 as a novel multicopy enhancer of s-adenosylmethionine level in yeast.	S-Adenosylmethionine	127-147	Gal11p	Saccharomyces cerevisiae S288C	88-93
23804760-6	2013	We have solved two X-ray crystallographic structures of TFB1M with (2.1 A) and without (2.0 A) its cofactor S-adenosyl-L-methionine.	S-Adenosylmethionine	110-131	transcription factor B1, mitochondrial	Homo sapiens	56-61
23887145-1	2013	Enzymes of the Trm5 family catalyze methyl transfer from S-adenosyl methionine (AdoMet) to the N1 of G37 to synthesize m1 G37-tRNA as a critical determinant to prevent ribosome frameshift errors.	S-Adenosylmethionine	57-78	tRNA methyltransferase 5	Homo sapiens	15-19
23887145-1	2013	Enzymes of the Trm5 family catalyze methyl transfer from S-adenosyl methionine (AdoMet) to the N1 of G37 to synthesize m1 G37-tRNA as a critical determinant to prevent ribosome frameshift errors.	S-Adenosylmethionine	80-86	tRNA methyltransferase 5	Homo sapiens	15-19
23957506-3	2013	We tested the hypothesis that plasma S-adenosylmethionine (SAM) level alone or in combination with genetic variation in DNA methyltransferases (DNMT1, DNMT3A and DNMT3B) was associated with global DNA methylation extent at long interspersed nucleotide element-1 (LINE-1) sequences.	S-Adenosylmethionine	37-57	DNA methyltransferase 1	Homo sapiens	144-149
23957506-3	2013	We tested the hypothesis that plasma S-adenosylmethionine (SAM) level alone or in combination with genetic variation in DNA methyltransferases (DNMT1, DNMT3A and DNMT3B) was associated with global DNA methylation extent at long interspersed nucleotide element-1 (LINE-1) sequences.	S-Adenosylmethionine	37-57	DNA methyltransferase 3 alpha	Homo sapiens	151-157
23957506-3	2013	We tested the hypothesis that plasma S-adenosylmethionine (SAM) level alone or in combination with genetic variation in DNA methyltransferases (DNMT1, DNMT3A and DNMT3B) was associated with global DNA methylation extent at long interspersed nucleotide element-1 (LINE-1) sequences.	S-Adenosylmethionine	37-57	DNA methyltransferase 3 beta	Homo sapiens	162-168
23957506-3	2013	We tested the hypothesis that plasma S-adenosylmethionine (SAM) level alone or in combination with genetic variation in DNA methyltransferases (DNMT1, DNMT3A and DNMT3B) was associated with global DNA methylation extent at long interspersed nucleotide element-1 (LINE-1) sequences.	S-Adenosylmethionine	59-62	DNA methyltransferase 3 alpha	Homo sapiens	151-157
23957506-3	2013	We tested the hypothesis that plasma S-adenosylmethionine (SAM) level alone or in combination with genetic variation in DNA methyltransferases (DNMT1, DNMT3A and DNMT3B) was associated with global DNA methylation extent at long interspersed nucleotide element-1 (LINE-1) sequences.	S-Adenosylmethionine	59-62	DNA methyltransferase 3 beta	Homo sapiens	162-168
23689031-5	2013	The major effect of BHMT inhibition was a 50% decrease in S-adenosylmethionine levels.	S-Adenosylmethionine	58-78	betaine--homocysteine S-methyltransferase	Homo sapiens	20-24
23475283-3	2013	SAMe levels depend on the glycine-N-methyltransferase (GNMT), a one-carbon group methyltransferase, which catalyzes the conversion of SAMe to S-adenosylhomocysteine in hepatic cells.	S-Adenosylmethionine	0-4	glycine N-methyltransferase	Homo sapiens	26-53
23475283-3	2013	SAMe levels depend on the glycine-N-methyltransferase (GNMT), a one-carbon group methyltransferase, which catalyzes the conversion of SAMe to S-adenosylhomocysteine in hepatic cells.	S-Adenosylmethionine	0-4	glycine N-methyltransferase	Homo sapiens	55-59
23453262-2	2013	The methyl donor, S-adenosylmethionine (SAM), is biosynthesized from methionine and adenosine triphosphate by methionine adenosyltransferase 2a (Mat2a) in the one-carbon (C1) metabolism pathway.	S-Adenosylmethionine	18-38	methionine adenosyltransferase 2A	Homo sapiens	145-150
23453262-2	2013	The methyl donor, S-adenosylmethionine (SAM), is biosynthesized from methionine and adenosine triphosphate by methionine adenosyltransferase 2a (Mat2a) in the one-carbon (C1) metabolism pathway.	S-Adenosylmethionine	40-43	methionine adenosyltransferase 2A	Homo sapiens	110-143
23453262-2	2013	The methyl donor, S-adenosylmethionine (SAM), is biosynthesized from methionine and adenosine triphosphate by methionine adenosyltransferase 2a (Mat2a) in the one-carbon (C1) metabolism pathway.	S-Adenosylmethionine	40-43	methionine adenosyltransferase 2A	Homo sapiens	145-150
23936142-1	2013	Glycine N-methyltransferase (GNMT), an abundant cytosolic enzyme, catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to glycine generating S-adenosylhomocysteine and sarcosine (N-methylglycine).	S-Adenosylmethionine	112-132	glycine N-methyltransferase	Homo sapiens	0-27
23936142-1	2013	Glycine N-methyltransferase (GNMT), an abundant cytosolic enzyme, catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to glycine generating S-adenosylhomocysteine and sarcosine (N-methylglycine).	S-Adenosylmethionine	112-132	glycine N-methyltransferase	Homo sapiens	29-33
23936142-1	2013	Glycine N-methyltransferase (GNMT), an abundant cytosolic enzyme, catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to glycine generating S-adenosylhomocysteine and sarcosine (N-methylglycine).	S-Adenosylmethionine	134-137	glycine N-methyltransferase	Homo sapiens	0-27
23936142-1	2013	Glycine N-methyltransferase (GNMT), an abundant cytosolic enzyme, catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to glycine generating S-adenosylhomocysteine and sarcosine (N-methylglycine).	S-Adenosylmethionine	134-137	glycine N-methyltransferase	Homo sapiens	29-33
23435098-3	2013	In this study, we identified the methyltransferase encoded by umaA in Mycobacterium tuberculosis H37Rv as a novel S-adenosyl-l-methionine (SAM)-dependent methyltransferase capable of catalyzing the conversion of olefinic double bond of phospholipid-linked oleic acid to biologically essential TSA.	S-Adenosylmethionine	139-142	mycolic acid synthase UmaA	Mycobacterium tuberculosis H37Rv	62-66
23856002-7	2013	Furthermore, we demonstrate that both the histone acetyltransferase and radical S-adenosylmethionine domains of AtELP3 are essential for its function in plant immunity.	S-Adenosylmethionine	82-100	radical SAM domain-containing protein / GCN5-related N-acetyltransferase (GNAT) family protein	Arabidopsis thaliana	112-118
23665415-9	2013	Inhibition of hepatic methionine adenosyltransferase activity in Goto-Kakizaki rats was associated with a decrease in hepatic S-adenosylmethionine, which serves as an allosteric activator of cystathionine beta-synthase.	S-Adenosylmethionine	126-146	cystathionine beta synthase	Rattus norvegicus	191-218
23870128-7	2013	Thus, methionine and SAM levels represent a critical gauge of amino acid availability that is sensed via the methylation of PP2A to reciprocally regulate cell growth and autophagy.	S-Adenosylmethionine	21-24	protein phosphatase 2 phosphatase activator	Homo sapiens	124-128
23742935-0	2013	Functional evaluation of Asp76, 84, 102 and 150 in human arsenic(III) methyltransferase (hAS3MT) interacting with S-adenosylmethionine.	S-Adenosylmethionine	114-134	arsenite methyltransferase	Homo sapiens	89-95
23881414-8	2013	The competitive inhibitor of methyltransferases, S-adenosylhomocysteine, is markedly upregulated in fpgs1, by which fpgs1 reduces S-adenosylmethionine accessibility to methyltransferases and accordingly affects DNA and histone methylation.	S-Adenosylmethionine	132-150	DHFS-FPGS homolog B	Arabidopsis thaliana	100-105
23881414-8	2013	The competitive inhibitor of methyltransferases, S-adenosylhomocysteine, is markedly upregulated in fpgs1, by which fpgs1 reduces S-adenosylmethionine accessibility to methyltransferases and accordingly affects DNA and histone methylation.	S-Adenosylmethionine	132-150	DHFS-FPGS homolog B	Arabidopsis thaliana	116-121
23363077-1	2013	Methionine S-adenosyltransferase 2A (MAT2A) is the catalytic subunit for synthesis of S-adenosylmethionine (SAM), the principal methyl donor in many biological processes.	S-Adenosylmethionine	86-106	methionine adenosyltransferase 2A	Homo sapiens	0-35
23799365-8	2013	The H atom donor is suggested to be a conserved cysteine141 in B. subtilis SPL; the resulting thiyl radical likely interacts with a neighboring tyrosine99 before oxidizing the 5"-dA to 5"-dA radical and, subsequently, regenerating SAM.	S-Adenosylmethionine	231-234	sphingosine-1-phosphate lyase 1	Homo sapiens	75-78
23474979-5	2013	In addition, mutations in glycine-N-methyltransferase (GNMT) could be associated with a higher risk of hepatocellular carcinoma and liver disease due to an unbalanced S-adenosylmethionine (SAM)/S-adenosylhomocysteine (SAH) ratio, which leads to aberrant methylation reactions.	S-Adenosylmethionine	169-187	glycine N-methyltransferase	Homo sapiens	26-53
23474979-5	2013	In addition, mutations in glycine-N-methyltransferase (GNMT) could be associated with a higher risk of hepatocellular carcinoma and liver disease due to an unbalanced S-adenosylmethionine (SAM)/S-adenosylhomocysteine (SAH) ratio, which leads to aberrant methylation reactions.	S-Adenosylmethionine	169-187	glycine N-methyltransferase	Homo sapiens	55-59
23474979-5	2013	In addition, mutations in glycine-N-methyltransferase (GNMT) could be associated with a higher risk of hepatocellular carcinoma and liver disease due to an unbalanced S-adenosylmethionine (SAM)/S-adenosylhomocysteine (SAH) ratio, which leads to aberrant methylation reactions.	S-Adenosylmethionine	189-192	glycine N-methyltransferase	Homo sapiens	26-53
23474979-5	2013	In addition, mutations in glycine-N-methyltransferase (GNMT) could be associated with a higher risk of hepatocellular carcinoma and liver disease due to an unbalanced S-adenosylmethionine (SAM)/S-adenosylhomocysteine (SAH) ratio, which leads to aberrant methylation reactions.	S-Adenosylmethionine	189-192	glycine N-methyltransferase	Homo sapiens	55-59
23455543-2	2013	Here we show using metabolomics that NNMT impairs the methylation potential of cancer cells by consuming methyl units from S-adenosyl methionine to create the stable metabolic product 1-methylnicotinamide.	S-Adenosylmethionine	123-144	nicotinamide N-methyltransferase	Homo sapiens	37-41
23425511-0	2013	Insight into S-adenosylmethionine biosynthesis from the crystal structures of the human methionine adenosyltransferase catalytic and regulatory subunits.	S-Adenosylmethionine	15-33	methionine adenosyltransferase 1A	Homo sapiens	88-118
23425511-1	2013	MAT (methionine adenosyltransferase) utilizes L-methionine and ATP to form SAM (S-adenosylmethionine), the principal methyl donor in biological methylation.	S-Adenosylmethionine	75-78	methionine adenosyltransferase 1A	Homo sapiens	5-35
23425511-1	2013	MAT (methionine adenosyltransferase) utilizes L-methionine and ATP to form SAM (S-adenosylmethionine), the principal methyl donor in biological methylation.	S-Adenosylmethionine	80-100	methionine adenosyltransferase 1A	Homo sapiens	5-35
23415654-1	2013	Vitamin B12 (cobalamin, cbl) is a cofactor of methionine synthase (MTR) in the synthesis of methionine, the precursor of the universal methyl donor S-Adenosylmethionine (SAM), which is involved in epigenomic regulatory mechanisms.	S-Adenosylmethionine	148-168	Cbl proto-oncogene	Homo sapiens	24-27
23363077-1	2013	Methionine S-adenosyltransferase 2A (MAT2A) is the catalytic subunit for synthesis of S-adenosylmethionine (SAM), the principal methyl donor in many biological processes.	S-Adenosylmethionine	86-106	methionine adenosyltransferase 2A	Homo sapiens	37-42
23363077-1	2013	Methionine S-adenosyltransferase 2A (MAT2A) is the catalytic subunit for synthesis of S-adenosylmethionine (SAM), the principal methyl donor in many biological processes.	S-Adenosylmethionine	108-111	methionine adenosyltransferase 2A	Homo sapiens	0-35
23363077-1	2013	Methionine S-adenosyltransferase 2A (MAT2A) is the catalytic subunit for synthesis of S-adenosylmethionine (SAM), the principal methyl donor in many biological processes.	S-Adenosylmethionine	108-111	methionine adenosyltransferase 2A	Homo sapiens	37-42
23032700-2	2013	Cobalamin is the cofactor of methionine synthase, a key enzyme of the methionine cycle which synthesizes methionine, the precursor of cell S-adenosyl-methionine synthesis.	S-Adenosylmethionine	141-160	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	29-48
23519668-0	2013	Structures of histone methyltransferase SET7/9 in complexes with adenosylmethionine derivatives.	S-Adenosylmethionine	65-83	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	40-46
23519668-2	2013	In previous work, novel inhibitors of SET7/9 that are amine analogues of the coenzyme S-(5"-adenosyl)-L-methionine (AdoMet) have been developed.	S-Adenosylmethionine	116-122	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	38-44
23103529-5	2013	In this study, we have set up a robust in vitro bacterial M.SssI DNMT activity assay to systematically screen a collection of 26 240 compounds that were predicted to compete with the S-adenosyl-L-methionine (SAM) substrate of DNMT.	S-Adenosylmethionine	183-206	DNA methyltransferase 1	Homo sapiens	65-69
23103529-5	2013	In this study, we have set up a robust in vitro bacterial M.SssI DNMT activity assay to systematically screen a collection of 26 240 compounds that were predicted to compete with the S-adenosyl-L-methionine (SAM) substrate of DNMT.	S-Adenosylmethionine	183-206	DNA methyltransferase 1	Homo sapiens	226-230
22850906-3	2013	The enzyme glycine-N-methyltransferase (GNMT) contributes to S-adenosylmethionine level regulation and, by affecting DNA methylation, influences gene expression.	S-Adenosylmethionine	61-81	glycine N-methyltransferase	Homo sapiens	11-38
22850906-3	2013	The enzyme glycine-N-methyltransferase (GNMT) contributes to S-adenosylmethionine level regulation and, by affecting DNA methylation, influences gene expression.	S-Adenosylmethionine	61-81	glycine N-methyltransferase	Homo sapiens	40-44
22790542-0	2013	Adenosine kinase-deficient mutant of Saccharomyces cerevisiae accumulates S-adenosylmethionine because of an enhanced methionine biosynthesis pathway.	S-Adenosylmethionine	74-94	adenosine kinase	Saccharomyces cerevisiae S288C	0-16
23661436-0	2013	S-adenosylmethionine, a methyl donor, up regulates tissue inhibitor of metalloproteinase-2 in colorectal cancer.	S-Adenosylmethionine	0-20	TIMP metallopeptidase inhibitor 2	Homo sapiens	51-90
23446897-1	2013	BACKGROUND: Phosphatidylcholine (PC) produced via the S-adenosylmethionine-dependent phosphatidylethanolamine (PE) N-methyltransferase (PEMT) pathway is enriched with docosahexaenoic acid (DHA).	S-Adenosylmethionine	56-74	phosphatidylethanolamine N-methyltransferase	Homo sapiens	136-140
23079506-2	2013	In mammals, the rate-limiting step of the S-adenosylmethionine-dependent methylation process is exclusively controlled by S-adenosylhomocysteine (S-AdoHcy) hydrolase (SAHH).	S-Adenosylmethionine	44-62	adenosylhomocysteinase	Homo sapiens	167-171
23032700-9	2013	These data indicate that cobalamin mediates down-regulation of Multidrug Resistance-1 gene expression through increased S-adenosyl-methionine and phosphatidylcholine productions and phospholipase D activation.	S-Adenosylmethionine	120-141	ATP binding cassette subfamily B member 1	Homo sapiens	63-85
23002992-2	2013	CBS uses coenzyme pyridoxal 5"-phosphate (PLP) for catalysis, and S-adenosylmethionine regulates the activity of human CBS, but not yeast CBS.	S-Adenosylmethionine	66-86	cystathionine beta-synthase	Homo sapiens	119-122
23002992-2	2013	CBS uses coenzyme pyridoxal 5"-phosphate (PLP) for catalysis, and S-adenosylmethionine regulates the activity of human CBS, but not yeast CBS.	S-Adenosylmethionine	66-86	cystathionine beta-synthase	Homo sapiens	119-122
22985361-0	2013	Human cystathionine beta-synthase (CBS) contains two classes of binding sites for S-adenosylmethionine (SAM): complex regulation of CBS activity and stability by SAM.	S-Adenosylmethionine	82-102	cystathionine beta-synthase	Homo sapiens	6-33
22577887-5	2013	Two therapeutic modalities, betaine and S-adenosylmethionine, can correct methylation defects to attenuate many EtOH-induced liver changes, as well as improve IFN signaling pathways, thereby overcoming viral treatment resistance.	S-Adenosylmethionine	40-60	interferon alpha 1	Homo sapiens	159-162
24377546-9	2013	Our observations suggest that 5-Aza- CdR exerts its anti-tumor effects in Huh7 cells through an epigenetic change involving increased expression of the methionine adenosyltransferase 1A gene and induction of S-adenosylmethionine production.	S-Adenosylmethionine	208-228	MIR7-3 host gene	Homo sapiens	74-78
23178192-4	2013	Thus, in search of other similar Msr-inducing molecules, we examined the effects of pergolide, pergolide sulfoxide, and S-adenosyl-methionine on Msr activity in neuronal cells.	S-Adenosylmethionine	120-141	5-methyltetrahydrofolate-homocysteine methyltransferase reductase	Homo sapiens	145-148
23178192-7	2013	Similarly, treatment of cells with S-adenosyl methionine also increased cellular Msr activity, which was milder compared to increases induced by pergolide and pergolide sulfoxide.	S-Adenosylmethionine	35-56	5-methyltetrahydrofolate-homocysteine methyltransferase reductase	Homo sapiens	81-84
22985361-0	2013	Human cystathionine beta-synthase (CBS) contains two classes of binding sites for S-adenosylmethionine (SAM): complex regulation of CBS activity and stability by SAM.	S-Adenosylmethionine	82-102	cystathionine beta-synthase	Homo sapiens	35-38
22985361-0	2013	Human cystathionine beta-synthase (CBS) contains two classes of binding sites for S-adenosylmethionine (SAM): complex regulation of CBS activity and stability by SAM.	S-Adenosylmethionine	82-102	cystathionine beta-synthase	Homo sapiens	132-135
22985361-1	2013	CBS (cystathionine beta-synthase) is a multidomain tetrameric enzyme essential in the regulation of homocysteine metabolism, whose activity is enhanced by the allosteric regulator SAM (S-adenosylmethionine).	S-Adenosylmethionine	185-205	cystathionine beta-synthase	Homo sapiens	0-3
22985361-1	2013	CBS (cystathionine beta-synthase) is a multidomain tetrameric enzyme essential in the regulation of homocysteine metabolism, whose activity is enhanced by the allosteric regulator SAM (S-adenosylmethionine).	S-Adenosylmethionine	185-205	cystathionine beta-synthase	Homo sapiens	5-32
24450388-1	2013	Catechol-O-methyltransferase (COMT) is the enzyme which catalyzes the transfer of a methyl group from S-adenosylmethionine to catechols and catecholamines, like the neurotransmitters dopamine, epinephrine and norepinephrine.	S-Adenosylmethionine	102-122	catechol-O-methyltransferase	Homo sapiens	0-28
24450388-1	2013	Catechol-O-methyltransferase (COMT) is the enzyme which catalyzes the transfer of a methyl group from S-adenosylmethionine to catechols and catecholamines, like the neurotransmitters dopamine, epinephrine and norepinephrine.	S-Adenosylmethionine	102-122	catechol-O-methyltransferase	Homo sapiens	30-34
23370193-5	2013	We also developed a series of HMT inhibitors based on the structure of adenosylmethionine (AdoMet), a cofactor in the methylation reaction, by introducing various alkylamino groups onto the nitrogen atom in place of the sulfur atom of AdoMet.	S-Adenosylmethionine	71-89	PR/SET domain 9	Homo sapiens	30-33
23370193-5	2013	We also developed a series of HMT inhibitors based on the structure of adenosylmethionine (AdoMet), a cofactor in the methylation reaction, by introducing various alkylamino groups onto the nitrogen atom in place of the sulfur atom of AdoMet.	S-Adenosylmethionine	91-97	PR/SET domain 9	Homo sapiens	30-33
24463527-0	2013	A halt in poly(A) shortening during S-adenosyl-L-methionine-induced translation arrest in CGS1 mRNA of Arabidopsis thaliana.	S-Adenosylmethionine	38-59	Pyridoxal phosphate (PLP)-dependent transferases superfamily protein	Arabidopsis thaliana	90-94
23221482-1	2013	DNA methylation is linked to homocysteine metabolism through the generation of S-adenosylmethionine (AdoMet) and S-Adenosylhomocysteine (AdoHcy).	S-Adenosylmethionine	79-99	methionine adenosyltransferase I, alpha	Mus musculus	101-107
24463527-2	2013	Expression of the Arabidopsis thaliana CGS1 gene is negatively feedback-regulated in response to the direct Met metabolite S-adenosyl-L-methionine (AdoMet).	S-Adenosylmethionine	123-146	Pyridoxal phosphate (PLP)-dependent transferases superfamily protein	Arabidopsis thaliana	39-43
24463527-2	2013	Expression of the Arabidopsis thaliana CGS1 gene is negatively feedback-regulated in response to the direct Met metabolite S-adenosyl-L-methionine (AdoMet).	S-Adenosylmethionine	148-154	Pyridoxal phosphate (PLP)-dependent transferases superfamily protein	Arabidopsis thaliana	39-43
23180764-9	2013	In addition, we were able to identify specific point mutations in Rrp8, which show that a reduced S-adenosyl-methionine binding influences the quality of the 60S subunit.	S-Adenosylmethionine	98-119	25S rRNA (adenine645-N1)-methyltransferase	Saccharomyces cerevisiae S288C	66-70
23579332-6	2013	The ratio of the methyl donor S-adenosylmethionine to the methylation inhibitor S-adenosylhomocysteine was decreased, in association with an increase in HCY and a global decrease in DNA methylation, indicative of decreased activity of the redox-sensitive enzyme methionine synthase.	S-Adenosylmethionine	30-50	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	262-281
23051747-8	2012	Here we demonstrate that GSK126, a potent, highly selective, S-adenosyl-methionine-competitive, small-molecule inhibitor of EZH2 methyltransferase activity, decreases global H3K27me3 levels and reactivates silenced PRC2 target genes.	S-Adenosylmethionine	63-82	enhancer of zeste 2 polycomb repressive complex 2 subunit	Mus musculus	124-128
24065059-1	2013	1-aminocyclopropane-1-carboxylic acid (ACC) synthase (ACS) is the key enzyme in ethylene biosynthesis, catalyzing the conversion of S-adenosylmethionine (AdoMet) to ACC, which is the immediate precursor of ethylene.	S-Adenosylmethionine	132-152	acetyl-CoA synthetase	Arabidopsis thaliana	54-57
24065059-1	2013	1-aminocyclopropane-1-carboxylic acid (ACC) synthase (ACS) is the key enzyme in ethylene biosynthesis, catalyzing the conversion of S-adenosylmethionine (AdoMet) to ACC, which is the immediate precursor of ethylene.	S-Adenosylmethionine	154-160	acetyl-CoA synthetase	Arabidopsis thaliana	54-57
23469257-2	2013	Set1 catalyzes mono-, di- and trimethylation of the fourth residue, lysine 4, of histone H3 using methyl groups from S-adenosylmethionine, and requires a subset of COMPASS proteins for this activity.	S-Adenosylmethionine	117-137	histone methyltransferase SET1	Saccharomyces cerevisiae S288C	0-4
23418509-4	2013	It has been shown that changes in intracellular polyamine concentrations affect activities of -adenosyl-L-methionine-decaroboxylase, and, as a result, affect concentrations of the methyl group donor, S-adenosylmethionine (SAM), and of the competitive Dnmt inhibitor, decarboxylated SAM.	S-Adenosylmethionine	200-220	DNA methyltransferase 1	Homo sapiens	251-255
23236167-3	2012	To investigate if tumor growth is dependent on the enzymatic activity of Ezh2, we developed a potent and selective small molecule inhibitor, EI1, which inhibits the enzymatic activity of Ezh2 through direct binding to the enzyme and competing with the methyl group donor S-Adenosyl methionine.	S-Adenosylmethionine	271-292	enhancer of zeste 2 polycomb repressive complex 2 subunit	Homo sapiens	73-77
23236167-3	2012	To investigate if tumor growth is dependent on the enzymatic activity of Ezh2, we developed a potent and selective small molecule inhibitor, EI1, which inhibits the enzymatic activity of Ezh2 through direct binding to the enzyme and competing with the methyl group donor S-Adenosyl methionine.	S-Adenosylmethionine	271-292	enhancer of zeste 2 polycomb repressive complex 2 subunit	Homo sapiens	187-191
23030620-6	2012	Furthermore, the inhibition investigation demonstrated that, in the presence of 160 muM S-adenosyl-L-methionine as methyl donor, 5-aza-2"-deoxycytidine, procaine, epicatechin, and caffeic acid could inhibit the M. SssI MTase activity with the IC(50) values of 45.77, 410.3, 129.03, and 124.2 muM, respectively.	S-Adenosylmethionine	88-111	latexin	Homo sapiens	84-87
22955273-6	2012	S-Adenosyl-l-methionine (AdoMet) is the first-order reactant, which modulates the conformation of hAS3MT to a best matched state by hydrophobic interaction.	S-Adenosylmethionine	0-23	PDS5 cohesin associated factor B	Homo sapiens	98-102
22955273-6	2012	S-Adenosyl-l-methionine (AdoMet) is the first-order reactant, which modulates the conformation of hAS3MT to a best matched state by hydrophobic interaction.	S-Adenosylmethionine	25-31	PDS5 cohesin associated factor B	Homo sapiens	98-102
23022348-3	2012	In this article, we characterize the interaction between both proteins, demonstrate that MTERF4 strongly stimulates the specificity of NSUN4 during in vitro methylation experiments, and present the 2.0 A resolution crystal structure of the MTERF4:NSUN4 protein complex, lacking 48 residues of the MTERF4 C-terminal acidic tail, bound to S-adenosyl-L-methionine, thus revealing the nature of the interaction between both proteins and the structural conservation of the most divergent of the human MTERF family members.	S-Adenosylmethionine	337-360	mitochondrial transcription termination factor 4	Homo sapiens	89-95
23022348-3	2012	In this article, we characterize the interaction between both proteins, demonstrate that MTERF4 strongly stimulates the specificity of NSUN4 during in vitro methylation experiments, and present the 2.0 A resolution crystal structure of the MTERF4:NSUN4 protein complex, lacking 48 residues of the MTERF4 C-terminal acidic tail, bound to S-adenosyl-L-methionine, thus revealing the nature of the interaction between both proteins and the structural conservation of the most divergent of the human MTERF family members.	S-Adenosylmethionine	337-360	mitochondrial transcription termination factor 4	Homo sapiens	240-246
23022348-3	2012	In this article, we characterize the interaction between both proteins, demonstrate that MTERF4 strongly stimulates the specificity of NSUN4 during in vitro methylation experiments, and present the 2.0 A resolution crystal structure of the MTERF4:NSUN4 protein complex, lacking 48 residues of the MTERF4 C-terminal acidic tail, bound to S-adenosyl-L-methionine, thus revealing the nature of the interaction between both proteins and the structural conservation of the most divergent of the human MTERF family members.	S-Adenosylmethionine	337-360	NOP2/Sun RNA methyltransferase 4	Homo sapiens	247-252
23022348-3	2012	In this article, we characterize the interaction between both proteins, demonstrate that MTERF4 strongly stimulates the specificity of NSUN4 during in vitro methylation experiments, and present the 2.0 A resolution crystal structure of the MTERF4:NSUN4 protein complex, lacking 48 residues of the MTERF4 C-terminal acidic tail, bound to S-adenosyl-L-methionine, thus revealing the nature of the interaction between both proteins and the structural conservation of the most divergent of the human MTERF family members.	S-Adenosylmethionine	337-360	mitochondrial transcription termination factor 4	Homo sapiens	240-246
23022348-3	2012	In this article, we characterize the interaction between both proteins, demonstrate that MTERF4 strongly stimulates the specificity of NSUN4 during in vitro methylation experiments, and present the 2.0 A resolution crystal structure of the MTERF4:NSUN4 protein complex, lacking 48 residues of the MTERF4 C-terminal acidic tail, bound to S-adenosyl-L-methionine, thus revealing the nature of the interaction between both proteins and the structural conservation of the most divergent of the human MTERF family members.	S-Adenosylmethionine	337-360	mitochondrial transcription termination factor 1	Homo sapiens	89-94
23097428-5	2012	m1A58 formation in human mitochondrial tRNA(Leu(UUR)) could be reconstituted in vitro using recombinant Trmt61B in the presence of Ado-Met as a methyl donor.	S-Adenosylmethionine	131-138	mitochondrially encoded tRNA glycine	Homo sapiens	39-52
23097428-5	2012	m1A58 formation in human mitochondrial tRNA(Leu(UUR)) could be reconstituted in vitro using recombinant Trmt61B in the presence of Ado-Met as a methyl donor.	S-Adenosylmethionine	131-138	tRNA methyltransferase 61B	Homo sapiens	104-111
23030620-6	2012	Furthermore, the inhibition investigation demonstrated that, in the presence of 160 muM S-adenosyl-L-methionine as methyl donor, 5-aza-2"-deoxycytidine, procaine, epicatechin, and caffeic acid could inhibit the M. SssI MTase activity with the IC(50) values of 45.77, 410.3, 129.03, and 124.2 muM, respectively.	S-Adenosylmethionine	88-111	latexin	Homo sapiens	292-295
22995836-2	2012	Misu catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to carbon 5 of cytosines in tRNAs.	S-Adenosylmethionine	51-74	NOP2/Sun RNA methyltransferase 2	Homo sapiens	0-4
23143240-1	2012	Human cystathionine beta-synthase (CBS) is a pyridoxal-5"-phosphate-dependent hemeprotein, whose catalytic activity is regulated by S-adenosylmethionine.	S-Adenosylmethionine	132-152	cystathionine beta-synthase	Homo sapiens	6-33
23143240-1	2012	Human cystathionine beta-synthase (CBS) is a pyridoxal-5"-phosphate-dependent hemeprotein, whose catalytic activity is regulated by S-adenosylmethionine.	S-Adenosylmethionine	132-152	cystathionine beta-synthase	Homo sapiens	35-38
22879628-0	2012	The amyloid precursor protein (APP) family members are key players in S-adenosylmethionine formation by MAT2A and modify BACE1 and PSEN1 gene expression-relevance for Alzheimer"s disease.	S-Adenosylmethionine	70-90	amyloid beta precursor protein	Homo sapiens	4-29
22879628-0	2012	The amyloid precursor protein (APP) family members are key players in S-adenosylmethionine formation by MAT2A and modify BACE1 and PSEN1 gene expression-relevance for Alzheimer"s disease.	S-Adenosylmethionine	70-90	methionine adenosyltransferase 2A	Homo sapiens	104-109
22879628-0	2012	The amyloid precursor protein (APP) family members are key players in S-adenosylmethionine formation by MAT2A and modify BACE1 and PSEN1 gene expression-relevance for Alzheimer"s disease.	S-Adenosylmethionine	70-90	beta-secretase 1	Homo sapiens	121-126
22879628-0	2012	The amyloid precursor protein (APP) family members are key players in S-adenosylmethionine formation by MAT2A and modify BACE1 and PSEN1 gene expression-relevance for Alzheimer"s disease.	S-Adenosylmethionine	70-90	presenilin 1	Homo sapiens	131-136
22879628-7	2012	MAT2A catalyzes the production of S-adenosylmethionine from methionine and ATP, which plays a pivotal role in the methylation of neurotransmitters, DNA, proteins, and lipids.	S-Adenosylmethionine	34-54	methionine adenosyltransferase 2A	Homo sapiens	0-5
22879628-8	2012	MAT2A-dependent significant up-regulation of S-adenosylmethionine was also detectable in the knockdown cells compared with controls.	S-Adenosylmethionine	45-65	methionine adenosyltransferase 2A	Homo sapiens	0-5
23014492-7	2012	Bhmt(-/-) mice had higher plasma Hcy and hepatic S-adenosylhomocysteine (AdoHcy) concentrations and had lower hepatic S-adenosylmethionine (AdoMet) concentrations compared with Bhmt(+/+) mice for all diets.	S-Adenosylmethionine	118-138	betaine-homocysteine methyltransferase	Mus musculus	0-4
22942279-10	2012	Ursodeoxycholic acid and S-adenosylmethionine are anti-fibrotic in bile duct ligation, but this effect was nearly lost if GCLC induction was blocked.	S-Adenosylmethionine	25-45	glutamate-cysteine ligase, catalytic subunit	Rattus norvegicus	122-126
23071334-5	2012	We have determined the crystal structure of human PRMT5 in complex with MEP50 (methylosome protein 50), bound to an S-adenosylmethionine analog and a peptide substrate derived from histone H4.	S-Adenosylmethionine	116-136	protein arginine methyltransferase 5	Homo sapiens	50-55
23071334-5	2012	We have determined the crystal structure of human PRMT5 in complex with MEP50 (methylosome protein 50), bound to an S-adenosylmethionine analog and a peptide substrate derived from histone H4.	S-Adenosylmethionine	116-136	WD repeat domain 77	Homo sapiens	72-77
23071334-5	2012	We have determined the crystal structure of human PRMT5 in complex with MEP50 (methylosome protein 50), bound to an S-adenosylmethionine analog and a peptide substrate derived from histone H4.	S-Adenosylmethionine	116-136	WD repeat domain 77	Homo sapiens	79-101
22932905-5	2012	We sought to determine whether expression of SEPP1 and the aforementioned glucoconeogenic enzymes are regulated by protein methylation, the levels of which are reliant upon adequate S-adenosylmethionine (SAM) and inhibited by S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	182-202	selenoprotein P	Homo sapiens	45-50
22932905-5	2012	We sought to determine whether expression of SEPP1 and the aforementioned glucoconeogenic enzymes are regulated by protein methylation, the levels of which are reliant upon adequate S-adenosylmethionine (SAM) and inhibited by S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	204-207	selenoprotein P	Homo sapiens	45-50
22264868-1	2012	Glycine N-methyltransferase (GNMT) affects cellular methylation capacity through regulating the ratio between S-adenosylmethionine (SAM) and S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	110-130	glycine N-methyltransferase	Mus musculus	0-27
23073625-1	2012	S-adenosylmethionine (AdoMet, also known as SAM and SAMe) is the principal biological methyl donor synthesized in all mammalian cells but most abundantly in the liver.	S-Adenosylmethionine	0-20	methionine adenosyltransferase I, alpha	Mus musculus	22-28
22708516-1	2012	PRMT5 (protein arginine methyltransferase 5) is an enzyme that catalyses transfer of methyl groups from S-adenosyl methionine to the arginine residues of histones or non-histone proteins and is involved in a variety of cellular processes.	S-Adenosylmethionine	104-125	protein arginine methyltransferase 5	Homo sapiens	0-5
22708516-1	2012	PRMT5 (protein arginine methyltransferase 5) is an enzyme that catalyses transfer of methyl groups from S-adenosyl methionine to the arginine residues of histones or non-histone proteins and is involved in a variety of cellular processes.	S-Adenosylmethionine	104-125	protein arginine methyltransferase 5	Homo sapiens	7-43
22717137-7	2012	S-adenosylmethionine (SAM), xyloglucan endotransglucosylase/hydrolases (XTHs) and caffeoyl-CoA-O-methyl transferase (CCoAOMT) could promote cell wall formation in perfect flower buds of Japanese apricot, greatly contributing to pistil development.	S-Adenosylmethionine	0-20	caffeoyl-CoA O-methyltransferase	Prunus mume	117-124
22924785-6	2012	Isothermal titration calorimetry studies showed that two representative inhibitors bind with a high affinity to the DOT1L:nucleosome complex and only compete with the enzyme cofactor SAM (S-adenosyl-L-methionine) but not the substrate nucleosome.	S-Adenosylmethionine	188-211	DOT1 like histone lysine methyltransferase	Homo sapiens	116-121
22906093-2	2012	It is repaired by a radical SAM (S-adenosylmethionine) enzyme, the spore photoproduct lyase (SPL), at the bacterial early germination phase.	S-Adenosylmethionine	33-53	sphingosine-1-phosphate lyase 1	Homo sapiens	67-91
22906093-2	2012	It is repaired by a radical SAM (S-adenosylmethionine) enzyme, the spore photoproduct lyase (SPL), at the bacterial early germination phase.	S-Adenosylmethionine	33-53	sphingosine-1-phosphate lyase 1	Homo sapiens	93-96
22893684-4	2012	AtGXMT1, which was previously classified as a domain of unknown function (DUF) 579 protein, specifically transfers the methyl group from S-adenosyl-L-methionine to O-4 of alpha-D-glucopyranosyluronic acid residues that are linked to O-2 of the xylan backbone.	S-Adenosylmethionine	137-160	glucuronoxylan 4-O-methyltransferase-like protein (DUF579)	Arabidopsis thaliana	0-7
22264868-1	2012	Glycine N-methyltransferase (GNMT) affects cellular methylation capacity through regulating the ratio between S-adenosylmethionine (SAM) and S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	110-130	glycine N-methyltransferase	Mus musculus	29-33
22264868-1	2012	Glycine N-methyltransferase (GNMT) affects cellular methylation capacity through regulating the ratio between S-adenosylmethionine (SAM) and S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	132-135	glycine N-methyltransferase	Mus musculus	0-27
22264868-1	2012	Glycine N-methyltransferase (GNMT) affects cellular methylation capacity through regulating the ratio between S-adenosylmethionine (SAM) and S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	132-135	glycine N-methyltransferase	Mus musculus	29-33
23034269-0	2012	Inhibition of P-glycoprotein-mediated transport by S-adenosylmethionine and cynarin in multidrug-resistant human uterine sarcoma MES-SA/Dx5 cells.	S-Adenosylmethionine	51-71	ATP binding cassette subfamily B member 1	Homo sapiens	14-28
22392635-1	2012	UNLABELLED: Glycine N-methyltransferase (GNMT) catabolizes S-adenosylmethionine (SAMe), the main methyl donor of the body.	S-Adenosylmethionine	59-79	glycine N-methyltransferase	Homo sapiens	12-39
22392635-1	2012	UNLABELLED: Glycine N-methyltransferase (GNMT) catabolizes S-adenosylmethionine (SAMe), the main methyl donor of the body.	S-Adenosylmethionine	59-79	glycine N-methyltransferase	Homo sapiens	41-45
22514352-7	2012	This function of nsP2 depends on the integrity of the helicase and S-adenosylmethionine (SAM)-dependent methyltransferase-like domains, and point mutations in either of these domains abolish Rpb1 degradation.	S-Adenosylmethionine	69-87	reticulon 2	Homo sapiens	17-21
22318685-1	2012	UNLABELLED: Down-regulation of the liver-specific MAT1A gene, encoding S-adenosylmethionine (SAM) synthesizing isozymes MATI/III, and up-regulation of widely expressed MAT2A, encoding MATII isozyme, known as MAT1A:MAT2A switch, occurs in hepatocellular carcinoma (HCC).	S-Adenosylmethionine	71-91	methionine adenosyltransferase 1A	Homo sapiens	50-55
22514352-7	2012	This function of nsP2 depends on the integrity of the helicase and S-adenosylmethionine (SAM)-dependent methyltransferase-like domains, and point mutations in either of these domains abolish Rpb1 degradation.	S-Adenosylmethionine	89-92	reticulon 2	Homo sapiens	17-21
22612060-7	2012	Interestingly, the presence of the CBS allosteric activator, S-adenosylmethionine (AdoMet), increased the rate of cleavage of the wild type and the AdoMet-responsive mutants, while the proteolytic rate of the AdoMet-unresponsive mutants was not significantly changed.	S-Adenosylmethionine	61-81	cystathionine beta-synthase	Homo sapiens	35-38
22591353-5	2012	This cleft is located next to the binding pocket for the cofactor S-adenosyl-L-methionine, and the catalytic residues of DNMT2 are positioned at its walls or bottom.	S-Adenosylmethionine	66-89	tRNA aspartic acid methyltransferase 1	Homo sapiens	121-126
22221883-5	2012	We found that S-adenosylmethionine reduced amyloid production, increased spatial memory in TgCRND8 mice and inhibited the upregulation of B vitamin deficiency-induced PSEN1 and BACE1 expression and Tau phosphorylation in TgCRND8 and wild-type mice.	S-Adenosylmethionine	14-34	presenilin 1	Mus musculus	167-172
22221883-5	2012	We found that S-adenosylmethionine reduced amyloid production, increased spatial memory in TgCRND8 mice and inhibited the upregulation of B vitamin deficiency-induced PSEN1 and BACE1 expression and Tau phosphorylation in TgCRND8 and wild-type mice.	S-Adenosylmethionine	14-34	beta-site APP cleaving enzyme 1	Mus musculus	177-182
22270009-0	2012	Proteomic analysis of human hepatoma cells expressing methionine adenosyltransferase I/III: Characterization of DDX3X as a target of S-adenosylmethionine.	S-Adenosylmethionine	133-153	methionine adenosyltransferase 1A	Homo sapiens	54-90
22270009-0	2012	Proteomic analysis of human hepatoma cells expressing methionine adenosyltransferase I/III: Characterization of DDX3X as a target of S-adenosylmethionine.	S-Adenosylmethionine	133-153	DEAD-box helicase 3 X-linked	Homo sapiens	112-117
22270009-1	2012	Methionine adenosyltransferase I/III (MATI/III) synthesizes S-adenosylmethionine (SAM) in quiescent hepatocytes.	S-Adenosylmethionine	60-80	methionine adenosyltransferase 1A	Homo sapiens	0-36
22270009-1	2012	Methionine adenosyltransferase I/III (MATI/III) synthesizes S-adenosylmethionine (SAM) in quiescent hepatocytes.	S-Adenosylmethionine	60-80	methionine adenosyltransferase 1A	Homo sapiens	38-46
22270009-1	2012	Methionine adenosyltransferase I/III (MATI/III) synthesizes S-adenosylmethionine (SAM) in quiescent hepatocytes.	S-Adenosylmethionine	82-85	methionine adenosyltransferase 1A	Homo sapiens	0-36
22270009-1	2012	Methionine adenosyltransferase I/III (MATI/III) synthesizes S-adenosylmethionine (SAM) in quiescent hepatocytes.	S-Adenosylmethionine	82-85	methionine adenosyltransferase 1A	Homo sapiens	38-46
22612060-7	2012	Interestingly, the presence of the CBS allosteric activator, S-adenosylmethionine (AdoMet), increased the rate of cleavage of the wild type and the AdoMet-responsive mutants, while the proteolytic rate of the AdoMet-unresponsive mutants was not significantly changed.	S-Adenosylmethionine	83-89	cystathionine beta-synthase	Homo sapiens	35-38
22093367-2	2012	This activity is compromised when vitamin B12 concentration is low because methionine synthase activity is reduced, lowering the concentration of S-adenosyl methionine (SAM) which in turn may diminish DNA methylation and cause folate to become unavailable for the conversion of dUMP to dTMP.	S-Adenosylmethionine	146-167	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	75-94
22093367-2	2012	This activity is compromised when vitamin B12 concentration is low because methionine synthase activity is reduced, lowering the concentration of S-adenosyl methionine (SAM) which in turn may diminish DNA methylation and cause folate to become unavailable for the conversion of dUMP to dTMP.	S-Adenosylmethionine	169-172	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	75-94
22240119-5	2012	In contrast with other metazoan enzymes, CBS-1 lacks the haem and regulatory Bateman domain essential for activation by AdoMet (S-adenosylmethionine) and only forms monomers.	S-Adenosylmethionine	120-126	PALP domain-containing protein	Caenorhabditis elegans	41-46
22240119-5	2012	In contrast with other metazoan enzymes, CBS-1 lacks the haem and regulatory Bateman domain essential for activation by AdoMet (S-adenosylmethionine) and only forms monomers.	S-Adenosylmethionine	128-148	PALP domain-containing protein	Caenorhabditis elegans	41-46
22349227-2	2012	Catechol-O-methyltransferase (COMT; EC 2.1.1.6) inactivates neurotransmitters by catalyzing the transfer of a methyl group from S-adenosylmethionine to catechols in the presence of Mg2+.	S-Adenosylmethionine	128-148	catechol-O-methyltransferase	Homo sapiens	0-28
22274639-0	2012	Post-translational stabilization of thiopurine S-methyltransferase by S-adenosyl-L-methionine reveals regulation of TPMT*1 and *3C allozymes.	S-Adenosylmethionine	70-93	thiopurine S-methyltransferase	Homo sapiens	36-66
22274639-0	2012	Post-translational stabilization of thiopurine S-methyltransferase by S-adenosyl-L-methionine reveals regulation of TPMT*1 and *3C allozymes.	S-Adenosylmethionine	70-93	thiopurine S-methyltransferase	Homo sapiens	116-120
22274639-3	2012	Here, we describe the effect of fluctuations in physiological levels of S-adenosyl-L-methionine (SAM) and related metabolites on TPMT activity levels in cell lines and erythrocytes from healthy donors.	S-Adenosylmethionine	72-95	thiopurine S-methyltransferase	Homo sapiens	129-133
22274639-3	2012	Here, we describe the effect of fluctuations in physiological levels of S-adenosyl-L-methionine (SAM) and related metabolites on TPMT activity levels in cell lines and erythrocytes from healthy donors.	S-Adenosylmethionine	97-100	thiopurine S-methyltransferase	Homo sapiens	129-133
22262097-5	2012	Gene fusion experiments in which the metE transcriptional region was fused to an assayable reporter showed that addition of a GroE-independent MetK homologue [MetK synthesizes S-adenosylmethionine (SAM), the metJ corepressor] to the system (E. coli MetK depends on GroE for folding) almost fully suppressed the increased expression.	S-Adenosylmethionine	178-196	chaperonin GroES	Escherichia coli	126-130
21185701-2	2012	The S-adenosylmethionine synthetase type-1 (MAT1A), an essential enzyme in the conversion of methionine to S-adenosylmethionine, plays a key role in homocysteine metabolism.	S-Adenosylmethionine	4-24	methionine adenosyltransferase 1A	Homo sapiens	44-49
22100631-8	2012	Studies using liver cells have demonstrated that S-adenosyl methionine (SAM), which is a product of folate metabolism, regulates the expression and catalytic activity of CYP2E1.	S-Adenosylmethionine	49-70	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	170-176
22159228-3	2012	S-adenosylmethionine (SAMe) and its metabolite methylthioadenosine (MTA) can inhibit lipopolysaccharide-induced TNF-alpha expression in macrophages.	S-Adenosylmethionine	0-20	tumor necrosis factor	Mus musculus	112-121
22100631-8	2012	Studies using liver cells have demonstrated that S-adenosyl methionine (SAM), which is a product of folate metabolism, regulates the expression and catalytic activity of CYP2E1.	S-Adenosylmethionine	72-75	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	170-176
22761755-5	2012	Structure-guided analysis identified several conserved residues in hTYW2 that interact with S-adenosyl-methionine (AdoMet), and mutation studies revealed that K225 and E265 are critical residues for the enzymatic activity.	S-Adenosylmethionine	92-113	tRNA methyltransferase 12 homolog	Homo sapiens	67-72
22678405-3	2012	METHODS: Following our published data from S-adenosylmethionine (SAMe), oxaliplatin and sorafenib were further used to stimulate GADD45beta expression in cultured HepG2 (p53 wild type) and Hep3B (p53 null) hepatoma cells in vitro.	S-Adenosylmethionine	43-63	growth arrest and DNA damage inducible beta	Homo sapiens	129-139
22045486-0	2012	Dietary supplementation with S-adenosyl methionine delayed amyloid-beta and tau pathology in 3xTg-AD mice.	S-Adenosylmethionine	29-50	microtubule associated protein tau	Homo sapiens	76-79
23250418-3	2012	Here we report the three-dimensional structure of the protein methyltransferase DOT1L bound to EPZ004777, the first S-adenosylmethionine-competitive inhibitor of a protein methyltransferase with in vivo efficacy.	S-Adenosylmethionine	118-136	DOT1 like histone lysine methyltransferase	Homo sapiens	80-85
23250418-6	2012	These data provide important new insight into mechanisms of cell-active S-adenosylmethionine-competitive protein methyltransferase inhibitors, and establish a foundation for the further development of drug-like inhibitors of DOT1L for cancer therapy.	S-Adenosylmethionine	74-92	DOT1 like histone lysine methyltransferase	Homo sapiens	225-230
23189196-1	2012	Mammalian methionine adenosyltransferase II (MAT II) is the only hetero-oligomer in this family of enzymes that synthesize S-adenosylmethionine using methionine and ATP as substrates.	S-Adenosylmethionine	123-143	methionine adenosyltransferase 2B	Homo sapiens	10-43
23189196-1	2012	Mammalian methionine adenosyltransferase II (MAT II) is the only hetero-oligomer in this family of enzymes that synthesize S-adenosylmethionine using methionine and ATP as substrates.	S-Adenosylmethionine	123-143	methionine adenosyltransferase 2B	Homo sapiens	45-51
22033378-6	2012	L-Ornithine is substrate of ornithine decarboxylase (ODC) - one of the key enzymes of polyamine biosynthesis and a validated target for therapeutic intervention - producing putrescine, which in turn is converted to spermidine by condensing with an aminopropyl group from decarboxylated S-adenosylmethionine.	S-Adenosylmethionine	286-306	ornithine decarboxylase 1	Homo sapiens	28-51
22033378-6	2012	L-Ornithine is substrate of ornithine decarboxylase (ODC) - one of the key enzymes of polyamine biosynthesis and a validated target for therapeutic intervention - producing putrescine, which in turn is converted to spermidine by condensing with an aminopropyl group from decarboxylated S-adenosylmethionine.	S-Adenosylmethionine	286-306	ornithine decarboxylase 1	Homo sapiens	53-56
21989639-1	2012	S-adenosylmethionine synthetase (SAM-s) catalyzes the synthesis of S-adenosylmethionine (SAM), which is essential for methylation, transcription, proliferation, and production of secondary metabolites.	S-Adenosylmethionine	0-20	BN7_5082	Wickerhamomyces ciferrii	33-38
23056605-1	2012	Catechol-O-methyltransferase (COMT) degrades catecholamines, such as dopamine and epinephrine, by methylating them in the presence of a divalent metal cation (usually Mg(II)), and S-adenosyl-L-methionine.	S-Adenosylmethionine	180-203	catechol-O-methyltransferase	Homo sapiens	0-28
23056605-1	2012	Catechol-O-methyltransferase (COMT) degrades catecholamines, such as dopamine and epinephrine, by methylating them in the presence of a divalent metal cation (usually Mg(II)), and S-adenosyl-L-methionine.	S-Adenosylmethionine	180-203	catechol-O-methyltransferase	Homo sapiens	30-34
22761755-5	2012	Structure-guided analysis identified several conserved residues in hTYW2 that interact with S-adenosyl-methionine (AdoMet), and mutation studies revealed that K225 and E265 are critical residues for the enzymatic activity.	S-Adenosylmethionine	115-121	tRNA methyltransferase 12 homolog	Homo sapiens	67-72
22363738-1	2012	Viperin, an antiviral protein, has been shown to contain a CX(3)CX(2)C motif, which is conserved in the radical S-adenosyl-methionine (SAM) enzyme family.	S-Adenosylmethionine	112-133	radical S-adenosyl methionine domain containing 2	Homo sapiens	0-7
22558281-8	2012	A methyl donor, S-adenosylmethionine (SAM), reduces the degree of arsenic trioxide-induced re-expression of ERalpha and demethylation.	S-Adenosylmethionine	16-36	estrogen receptor 1	Homo sapiens	108-115
22558281-8	2012	A methyl donor, S-adenosylmethionine (SAM), reduces the degree of arsenic trioxide-induced re-expression of ERalpha and demethylation.	S-Adenosylmethionine	38-41	estrogen receptor 1	Homo sapiens	108-115
22077332-5	2011	Energetic analysis of Abeta adsorption on the SAMs reveals that Abeta adsorption on the SAMs is a net outcome of different competitions between dominant hydrophobic Abeta-CH(3)-SAM interactions and weak CH(3)-SAM-water interactions, between dominant electrostatic Abeta-COOH-SAM interactions and strong COOH-SAM-water interactions, and between comparable hydrophobic and electrostatic Abeta-OH-SAM interactions and strong OH-SAM-water interactions.	S-Adenosylmethionine	46-49	amyloid beta precursor protein	Homo sapiens	22-27
22195972-3	2011	We have determined the crystal structure of a prokaryotic ICMT ortholog, revealing a markedly different architecture from conventional methyltransferases that utilize S-adenosyl-L-methionine (SAM) as a cofactor.	S-Adenosylmethionine	167-190	isoprenylcysteine carboxyl methyltransferase	Homo sapiens	58-62
22195972-3	2011	We have determined the crystal structure of a prokaryotic ICMT ortholog, revealing a markedly different architecture from conventional methyltransferases that utilize S-adenosyl-L-methionine (SAM) as a cofactor.	S-Adenosylmethionine	192-195	isoprenylcysteine carboxyl methyltransferase	Homo sapiens	58-62
22077332-5	2011	Energetic analysis of Abeta adsorption on the SAMs reveals that Abeta adsorption on the SAMs is a net outcome of different competitions between dominant hydrophobic Abeta-CH(3)-SAM interactions and weak CH(3)-SAM-water interactions, between dominant electrostatic Abeta-COOH-SAM interactions and strong COOH-SAM-water interactions, and between comparable hydrophobic and electrostatic Abeta-OH-SAM interactions and strong OH-SAM-water interactions.	S-Adenosylmethionine	46-49	amyloid beta precursor protein	Homo sapiens	64-69
22077332-5	2011	Energetic analysis of Abeta adsorption on the SAMs reveals that Abeta adsorption on the SAMs is a net outcome of different competitions between dominant hydrophobic Abeta-CH(3)-SAM interactions and weak CH(3)-SAM-water interactions, between dominant electrostatic Abeta-COOH-SAM interactions and strong COOH-SAM-water interactions, and between comparable hydrophobic and electrostatic Abeta-OH-SAM interactions and strong OH-SAM-water interactions.	S-Adenosylmethionine	46-49	amyloid beta precursor protein	Homo sapiens	64-69
22077332-5	2011	Energetic analysis of Abeta adsorption on the SAMs reveals that Abeta adsorption on the SAMs is a net outcome of different competitions between dominant hydrophobic Abeta-CH(3)-SAM interactions and weak CH(3)-SAM-water interactions, between dominant electrostatic Abeta-COOH-SAM interactions and strong COOH-SAM-water interactions, and between comparable hydrophobic and electrostatic Abeta-OH-SAM interactions and strong OH-SAM-water interactions.	S-Adenosylmethionine	46-49	amyloid beta precursor protein	Homo sapiens	64-69
22077332-5	2011	Energetic analysis of Abeta adsorption on the SAMs reveals that Abeta adsorption on the SAMs is a net outcome of different competitions between dominant hydrophobic Abeta-CH(3)-SAM interactions and weak CH(3)-SAM-water interactions, between dominant electrostatic Abeta-COOH-SAM interactions and strong COOH-SAM-water interactions, and between comparable hydrophobic and electrostatic Abeta-OH-SAM interactions and strong OH-SAM-water interactions.	S-Adenosylmethionine	88-91	amyloid beta precursor protein	Homo sapiens	22-27
22077332-5	2011	Energetic analysis of Abeta adsorption on the SAMs reveals that Abeta adsorption on the SAMs is a net outcome of different competitions between dominant hydrophobic Abeta-CH(3)-SAM interactions and weak CH(3)-SAM-water interactions, between dominant electrostatic Abeta-COOH-SAM interactions and strong COOH-SAM-water interactions, and between comparable hydrophobic and electrostatic Abeta-OH-SAM interactions and strong OH-SAM-water interactions.	S-Adenosylmethionine	88-91	amyloid beta precursor protein	Homo sapiens	64-69
22077332-5	2011	Energetic analysis of Abeta adsorption on the SAMs reveals that Abeta adsorption on the SAMs is a net outcome of different competitions between dominant hydrophobic Abeta-CH(3)-SAM interactions and weak CH(3)-SAM-water interactions, between dominant electrostatic Abeta-COOH-SAM interactions and strong COOH-SAM-water interactions, and between comparable hydrophobic and electrostatic Abeta-OH-SAM interactions and strong OH-SAM-water interactions.	S-Adenosylmethionine	88-91	amyloid beta precursor protein	Homo sapiens	64-69
22077332-5	2011	Energetic analysis of Abeta adsorption on the SAMs reveals that Abeta adsorption on the SAMs is a net outcome of different competitions between dominant hydrophobic Abeta-CH(3)-SAM interactions and weak CH(3)-SAM-water interactions, between dominant electrostatic Abeta-COOH-SAM interactions and strong COOH-SAM-water interactions, and between comparable hydrophobic and electrostatic Abeta-OH-SAM interactions and strong OH-SAM-water interactions.	S-Adenosylmethionine	88-91	amyloid beta precursor protein	Homo sapiens	64-69
21985704-1	2011	Human 5"-methylthioadenosine phosphorylase (MTAP) links the polyamine biosynthetic and S-adenosyl-l-methionine salvage pathways and is a target for anticancer drugs.	S-Adenosylmethionine	87-110	methylthioadenosine phosphorylase	Homo sapiens	6-42
21985704-1	2011	Human 5"-methylthioadenosine phosphorylase (MTAP) links the polyamine biosynthetic and S-adenosyl-l-methionine salvage pathways and is a target for anticancer drugs.	S-Adenosylmethionine	87-110	methylthioadenosine phosphorylase	Homo sapiens	44-48
22005461-8	2011	The lack of methyltransferase activity of Delta4,5 As3MT seems to be related to the deletion of an S-adenosylmethionine-binding site and a critical cysteine residue.	S-Adenosylmethionine	99-119	arsenite methyltransferase	Homo sapiens	51-56
21994249-9	2011	Examples include two hypothesized auto-regulatory feedback mechanisms: one involving six long hairpins in the 3"-UTR of MAT2A, a key metabolic gene that produces the primary human methyl donor S-adenosylmethionine; the other involving a tRNA-like structure in the intron of the tRNA maturation gene POP1.	S-Adenosylmethionine	193-213	methionine adenosyltransferase 2A	Homo sapiens	120-125
21919174-0	2011	Dual role of S-adenosylmethionine (SAM+) in the methylation of sp2-hybridized electrophilic carbons.	S-Adenosylmethionine	13-33	Sp2 transcription factor	Homo sapiens	63-66
22102254-2	2011	TRM61 is the subunit that binds S-adenosyl-L-methionine and both subunits contribute to target tRNA binding.	S-Adenosylmethionine	32-55	tRNA 1-methyladenosine methyltransferase subunit GCD14	Saccharomyces cerevisiae S288C	0-5
22035958-3	2011	Our studies identify a conserved regulatory circuit in which SREBP-1 controls genes in the one-carbon cycle, which produces the methyl donor S-adenosylmethionine (SAMe).	S-Adenosylmethionine	141-161	sterol regulatory element binding transcription factor 1	Homo sapiens	61-68
21880715-4	2011	We have solved the high resolution crystal structures of the full-length SMYD2 protein in binary complex with its cofactor S-adenosylmethionine and in ternary complex with cofactor product S-adenosylhomocysteine and p53 substrate peptide (residues 368-375), respectively.	S-Adenosylmethionine	125-143	SET and MYND domain containing 2	Homo sapiens	73-78
21958159-1	2011	Human catechol-O-methyltransferase (COMT) catalyzes a methyl transfer from S-adenosylmethionine (AdoMet) to dopamine.	S-Adenosylmethionine	75-95	catechol-O-methyltransferase	Homo sapiens	6-34
21958159-1	2011	Human catechol-O-methyltransferase (COMT) catalyzes a methyl transfer from S-adenosylmethionine (AdoMet) to dopamine.	S-Adenosylmethionine	75-95	catechol-O-methyltransferase	Homo sapiens	36-40
21958159-1	2011	Human catechol-O-methyltransferase (COMT) catalyzes a methyl transfer from S-adenosylmethionine (AdoMet) to dopamine.	S-Adenosylmethionine	97-103	catechol-O-methyltransferase	Homo sapiens	6-34
21958159-1	2011	Human catechol-O-methyltransferase (COMT) catalyzes a methyl transfer from S-adenosylmethionine (AdoMet) to dopamine.	S-Adenosylmethionine	97-103	catechol-O-methyltransferase	Homo sapiens	36-40
21994249-9	2011	Examples include two hypothesized auto-regulatory feedback mechanisms: one involving six long hairpins in the 3"-UTR of MAT2A, a key metabolic gene that produces the primary human methyl donor S-adenosylmethionine; the other involving a tRNA-like structure in the intron of the tRNA maturation gene POP1.	S-Adenosylmethionine	193-213	POP1 homolog, ribonuclease P/MRP subunit	Homo sapiens	299-303
21741329-4	2011	PIMT catalyzes transmethylation of S-adenosylmethionine to L-beta-Asp and D-alpha-Asp residues in proteins and peptides.	S-Adenosylmethionine	35-55	protein-L-isoaspartate (D-aspartate) O-methyltransferase	Homo sapiens	0-4
21823666-1	2011	Nicotinamide N-methyltransferase (NNMT) catalyzes the N-methylation of nicotinamide, pyridines, and other analogues using S-adenosyl-l-methionine as donor.	S-Adenosylmethionine	122-145	nicotinamide N-methyltransferase	Homo sapiens	0-32
21723961-5	2011	The hypoxia-induced up-regulation of c-fos mRNA could be markedly antagonized by S-adenosyl-l-methionine (SAM, activator of CBS), but greatly increased by NH(2)OH.	S-Adenosylmethionine	81-104	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	37-42
21723961-5	2011	The hypoxia-induced up-regulation of c-fos mRNA could be markedly antagonized by S-adenosyl-l-methionine (SAM, activator of CBS), but greatly increased by NH(2)OH.	S-Adenosylmethionine	81-104	cystathionine beta synthase	Rattus norvegicus	124-127
21723961-5	2011	The hypoxia-induced up-regulation of c-fos mRNA could be markedly antagonized by S-adenosyl-l-methionine (SAM, activator of CBS), but greatly increased by NH(2)OH.	S-Adenosylmethionine	106-109	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	37-42
21723961-5	2011	The hypoxia-induced up-regulation of c-fos mRNA could be markedly antagonized by S-adenosyl-l-methionine (SAM, activator of CBS), but greatly increased by NH(2)OH.	S-Adenosylmethionine	106-109	cystathionine beta synthase	Rattus norvegicus	124-127
21839172-4	2011	Herein we report long (>100ns) molecular dynamics simulations for human DNMT3B bound to nanaomycin A with and without the presence of the cofactor S-adenosyl-L-methionine (SAM).	S-Adenosylmethionine	150-173	DNA methyltransferase 3 beta	Homo sapiens	75-81
21839172-4	2011	Herein we report long (>100ns) molecular dynamics simulations for human DNMT3B bound to nanaomycin A with and without the presence of the cofactor S-adenosyl-L-methionine (SAM).	S-Adenosylmethionine	175-178	DNA methyltransferase 3 beta	Homo sapiens	75-81
21900497-7	2011	Experiments using this system with and without Opi1p showed that Met4 activates and Opi1p represses genes that maintain levels of S-adenosylmethionine (SAM), the substrate for most methyltransferase reactions.	S-Adenosylmethionine	130-150	transcriptional regulator OPI1	Saccharomyces cerevisiae S288C	47-52
21900497-7	2011	Experiments using this system with and without Opi1p showed that Met4 activates and Opi1p represses genes that maintain levels of S-adenosylmethionine (SAM), the substrate for most methyltransferase reactions.	S-Adenosylmethionine	130-150	Met4p	Saccharomyces cerevisiae S288C	65-69
21900497-7	2011	Experiments using this system with and without Opi1p showed that Met4 activates and Opi1p represses genes that maintain levels of S-adenosylmethionine (SAM), the substrate for most methyltransferase reactions.	S-Adenosylmethionine	130-150	transcriptional regulator OPI1	Saccharomyces cerevisiae S288C	84-89
21878621-5	2011	Deletion of Bhmt resulted in a 43% reduction in hepatic S-adenosylmethionine (AdoMet) (p < 0.01) and a 3-fold increase in hepatic S-adenosylhomocysteine (AdoHcy) (p < 0.01) concentrations, resulting in a 75% reduction in methylation potential (AdoMet:AdoHcy) (p < 0.01).	S-Adenosylmethionine	56-76	betaine-homocysteine methyltransferase	Mus musculus	12-16
21878621-5	2011	Deletion of Bhmt resulted in a 43% reduction in hepatic S-adenosylmethionine (AdoMet) (p < 0.01) and a 3-fold increase in hepatic S-adenosylhomocysteine (AdoHcy) (p < 0.01) concentrations, resulting in a 75% reduction in methylation potential (AdoMet:AdoHcy) (p < 0.01).	S-Adenosylmethionine	78-84	betaine-homocysteine methyltransferase	Mus musculus	12-16
21823666-1	2011	Nicotinamide N-methyltransferase (NNMT) catalyzes the N-methylation of nicotinamide, pyridines, and other analogues using S-adenosyl-l-methionine as donor.	S-Adenosylmethionine	122-145	nicotinamide N-methyltransferase	Homo sapiens	34-38
21104457-5	2011	S-Adenosylmethionine, an activator of CBS, not only prevents homocysteine-induced inhibition of endogenous H(2)S production but also attenuates homocysteine-triggered cytotoxicity and accumulation of ROS.	S-Adenosylmethionine	0-20	cystathionine beta synthase	Rattus norvegicus	38-41
21780197-2	2011	In spore DNA, due to an unusual packing of the genetic material, a special spore photoproduct lesion (SP lesion) is formed, which is repaired by the enzyme spore photoproduct lyase (Spl), a radical S-adenosylmethionine (SAM) enzyme.	S-Adenosylmethionine	198-218	sphingosine-1-phosphate lyase 1	Homo sapiens	156-180
22276430-6	2011	The null gsh1/met1 mutant showed total growth restoration on minimal media supplemented with cysteine or glutathione as a sole sulfur source, but not with inorganic (sulfate, sulfite) or organic (methionine, S-adenosylmethionine) sources of sulfur.	S-Adenosylmethionine	208-228	uroporphyrinogen-III C-methyltransferase	Saccharomyces cerevisiae S288C	14-18
21780197-2	2011	In spore DNA, due to an unusual packing of the genetic material, a special spore photoproduct lesion (SP lesion) is formed, which is repaired by the enzyme spore photoproduct lyase (Spl), a radical S-adenosylmethionine (SAM) enzyme.	S-Adenosylmethionine	198-218	sphingosine-1-phosphate lyase 1	Homo sapiens	182-185
21780197-2	2011	In spore DNA, due to an unusual packing of the genetic material, a special spore photoproduct lesion (SP lesion) is formed, which is repaired by the enzyme spore photoproduct lyase (Spl), a radical S-adenosylmethionine (SAM) enzyme.	S-Adenosylmethionine	220-223	sphingosine-1-phosphate lyase 1	Homo sapiens	156-180
21780197-2	2011	In spore DNA, due to an unusual packing of the genetic material, a special spore photoproduct lesion (SP lesion) is formed, which is repaired by the enzyme spore photoproduct lyase (Spl), a radical S-adenosylmethionine (SAM) enzyme.	S-Adenosylmethionine	220-223	sphingosine-1-phosphate lyase 1	Homo sapiens	182-185
21678921-1	2011	SET and MYND domain-containing protein 2 (SMYD2) is a protein lysine methyltransferase that catalyzes the transfer of methyl groups from S-adenosylmethionine (AdoMet) to acceptor lysine residues on histones and other proteins.	S-Adenosylmethionine	137-157	SET and MYND domain containing 2	Homo sapiens	0-40
21515635-5	2011	The structure of SETD6 in complex with RelA peptide containing the methylation site, in the presence of S-adenosyl-L-methionine, reveals a V-like protein structure and suggests a model for NF-kappaB binding to SETD6.	S-Adenosylmethionine	104-127	SET domain containing 6, protein lysine methyltransferase	Homo sapiens	17-22
21515635-5	2011	The structure of SETD6 in complex with RelA peptide containing the methylation site, in the presence of S-adenosyl-L-methionine, reveals a V-like protein structure and suggests a model for NF-kappaB binding to SETD6.	S-Adenosylmethionine	104-127	RELA proto-oncogene, NF-kB subunit	Homo sapiens	39-43
21515635-5	2011	The structure of SETD6 in complex with RelA peptide containing the methylation site, in the presence of S-adenosyl-L-methionine, reveals a V-like protein structure and suggests a model for NF-kappaB binding to SETD6.	S-Adenosylmethionine	104-127	SET domain containing 6, protein lysine methyltransferase	Homo sapiens	210-215
21678921-1	2011	SET and MYND domain-containing protein 2 (SMYD2) is a protein lysine methyltransferase that catalyzes the transfer of methyl groups from S-adenosylmethionine (AdoMet) to acceptor lysine residues on histones and other proteins.	S-Adenosylmethionine	137-157	SET and MYND domain containing 2	Homo sapiens	42-47
21678921-1	2011	SET and MYND domain-containing protein 2 (SMYD2) is a protein lysine methyltransferase that catalyzes the transfer of methyl groups from S-adenosylmethionine (AdoMet) to acceptor lysine residues on histones and other proteins.	S-Adenosylmethionine	159-165	SET and MYND domain containing 2	Homo sapiens	0-40
21678921-1	2011	SET and MYND domain-containing protein 2 (SMYD2) is a protein lysine methyltransferase that catalyzes the transfer of methyl groups from S-adenosylmethionine (AdoMet) to acceptor lysine residues on histones and other proteins.	S-Adenosylmethionine	159-165	SET and MYND domain containing 2	Homo sapiens	42-47
21410432-1	2011	CARM1 (co-activator-associated arginine methyltransferase 1) is a PRMT (protein arginine N-methyltransferase) family member that catalyses the transfer of methyl groups from SAM (S-adenosylmethionine) to the side chain of specific arginine residues of substrate proteins.	S-Adenosylmethionine	179-199	coactivator associated arginine methyltransferase 1	Homo sapiens	0-5
21677046-8	2011	AtCGS1 codes for cystathionine gamma-synthase (CGS) that catalyzes the first committed step of methionine and S-adenosyl-l-methionine (AdoMet) biosynthesis in plants, and is feedback regulated by mRNA degradation coupled with translation elongation arrest.	S-Adenosylmethionine	110-133	Pyridoxal phosphate (PLP)-dependent transferases superfamily protein	Arabidopsis thaliana	0-6
21677046-8	2011	AtCGS1 codes for cystathionine gamma-synthase (CGS) that catalyzes the first committed step of methionine and S-adenosyl-l-methionine (AdoMet) biosynthesis in plants, and is feedback regulated by mRNA degradation coupled with translation elongation arrest.	S-Adenosylmethionine	110-133	Pyridoxal phosphate (PLP)-dependent transferases superfamily protein	Arabidopsis thaliana	17-45
21677046-8	2011	AtCGS1 codes for cystathionine gamma-synthase (CGS) that catalyzes the first committed step of methionine and S-adenosyl-l-methionine (AdoMet) biosynthesis in plants, and is feedback regulated by mRNA degradation coupled with translation elongation arrest.	S-Adenosylmethionine	135-141	Pyridoxal phosphate (PLP)-dependent transferases superfamily protein	Arabidopsis thaliana	0-6
21677046-8	2011	AtCGS1 codes for cystathionine gamma-synthase (CGS) that catalyzes the first committed step of methionine and S-adenosyl-l-methionine (AdoMet) biosynthesis in plants, and is feedback regulated by mRNA degradation coupled with translation elongation arrest.	S-Adenosylmethionine	135-141	Pyridoxal phosphate (PLP)-dependent transferases superfamily protein	Arabidopsis thaliana	17-45
21549127-4	2011	First, DNMT3B, unlike DNMT3A, requires a DNA cofactor in order to stably bind to S-adenosyl-l-methionine (SAM), suggesting that it proceeds according to an ordered catalytic scheme.	S-Adenosylmethionine	81-104	DNA methyltransferase 3 beta	Homo sapiens	7-13
21840473-1	2011	Methylation of homocysteine (Hcy) by betaine-Hcy S-methyltransferase (BHMT) produces methionine, which is required for S-adenosylmethionine (SAM) synthesis.	S-Adenosylmethionine	119-139	betaine-homocysteine S-methyltransferase	Rattus norvegicus	37-68
21840473-1	2011	Methylation of homocysteine (Hcy) by betaine-Hcy S-methyltransferase (BHMT) produces methionine, which is required for S-adenosylmethionine (SAM) synthesis.	S-Adenosylmethionine	119-139	betaine-homocysteine S-methyltransferase	Rattus norvegicus	70-74
21840473-1	2011	Methylation of homocysteine (Hcy) by betaine-Hcy S-methyltransferase (BHMT) produces methionine, which is required for S-adenosylmethionine (SAM) synthesis.	S-Adenosylmethionine	141-144	betaine-homocysteine S-methyltransferase	Rattus norvegicus	37-68
21840473-1	2011	Methylation of homocysteine (Hcy) by betaine-Hcy S-methyltransferase (BHMT) produces methionine, which is required for S-adenosylmethionine (SAM) synthesis.	S-Adenosylmethionine	141-144	betaine-homocysteine S-methyltransferase	Rattus norvegicus	70-74
21602303-1	2011	Bacterial TrmD and eukaryotic-archaeal Trm5 form a pair of analogous tRNA methyltransferase that catalyze methyl transfer from S-adenosyl methionine (AdoMet) to N(1) of G37, using catalytic motifs that share no sequence or structural homology.	S-Adenosylmethionine	127-148	tRNA methyltransferase 5	Homo sapiens	39-43
21602303-3	2011	Instead, fragments of AdoMet, adenosine and methionine, are selectively inhibitory of TrmD rather than Trm5.	S-Adenosylmethionine	22-28	tRNA methyltransferase 5	Homo sapiens	103-107
21410432-1	2011	CARM1 (co-activator-associated arginine methyltransferase 1) is a PRMT (protein arginine N-methyltransferase) family member that catalyses the transfer of methyl groups from SAM (S-adenosylmethionine) to the side chain of specific arginine residues of substrate proteins.	S-Adenosylmethionine	179-199	coactivator associated arginine methyltransferase 1	Homo sapiens	7-59
21406397-3	2011	Cytoplasmic serine hydroxymethyltransferase (SHMT1) regulates the partitioning of folate-activated one-carbons between thymidylate and S-adenosylmethionine biosynthesis.	S-Adenosylmethionine	137-155	serine hydroxymethyltransferase 1 (soluble)	Mus musculus	45-50
21460102-3	2011	Methionine adenosyltransferase 2A (MAT2A) maintains the homeostasis of S-adenosylmethionine (SAM), a critical marker of genomic methylation status.	S-Adenosylmethionine	71-91	methionine adenosyltransferase 2A	Homo sapiens	0-33
21460102-3	2011	Methionine adenosyltransferase 2A (MAT2A) maintains the homeostasis of S-adenosylmethionine (SAM), a critical marker of genomic methylation status.	S-Adenosylmethionine	71-91	methionine adenosyltransferase 2A	Homo sapiens	35-40
21310715-3	2011	Purified recombinant hMTr2 protein transfers a methyl group from S-adenosylmethionine to the 2"-O-ribose of the second nucleotide of messenger RNA and small nuclear RNA.	S-Adenosylmethionine	65-85	cap methyltransferase 2	Homo sapiens	21-26
21518804-4	2011	Curiously, Abp140p is composed of a poorly conserved N-terminal ORF fused by a programed +1 frameshift in budding yeasts to a C-terminal ORF containing an S-adenosylmethionine (SAM) domain that is highly conserved among eukaryotes.	S-Adenosylmethionine	155-175	tRNA(Thr) (cytosine(32)-N(3))-methyltransferase	Saccharomyces cerevisiae S288C	11-18
21518804-4	2011	Curiously, Abp140p is composed of a poorly conserved N-terminal ORF fused by a programed +1 frameshift in budding yeasts to a C-terminal ORF containing an S-adenosylmethionine (SAM) domain that is highly conserved among eukaryotes.	S-Adenosylmethionine	177-180	tRNA(Thr) (cytosine(32)-N(3))-methyltransferase	Saccharomyces cerevisiae S288C	11-18
21518805-4	2011	ABP140 consists of an N-terminal actin-binding sequence and a C-terminal S-adenosylmethionine (Ado-Met) binding motif.	S-Adenosylmethionine	73-93	tRNA(Thr) (cytosine(32)-N(3))-methyltransferase	Saccharomyces cerevisiae S288C	0-6
21518805-4	2011	ABP140 consists of an N-terminal actin-binding sequence and a C-terminal S-adenosylmethionine (Ado-Met) binding motif.	S-Adenosylmethionine	95-102	tRNA(Thr) (cytosine(32)-N(3))-methyltransferase	Saccharomyces cerevisiae S288C	0-6
21518897-3	2011	Here we report the crystal structure of the large fragment (291-1620) of mouse Dnmt1 and its complexes with cofactor S-adenosyl-L-methionine and its product S-adenosyl-L-homocystein.	S-Adenosylmethionine	117-140	DNA methyltransferase (cytosine-5) 1	Mus musculus	79-84
21538606-2	2011	COMT catalyzes the transfer of an activated methyl group from S-adenosylmethionine (SAM) to its catechol substrates, such as L-dopa, in the presence of magnesium ions.	S-Adenosylmethionine	62-82	catechol-O-methyltransferase	Homo sapiens	0-4
21538606-2	2011	COMT catalyzes the transfer of an activated methyl group from S-adenosylmethionine (SAM) to its catechol substrates, such as L-dopa, in the presence of magnesium ions.	S-Adenosylmethionine	84-87	catechol-O-methyltransferase	Homo sapiens	0-4
21538606-3	2011	The molecular recognition properties of the SAM-binding site of COMT have been investigated only sparsely.	S-Adenosylmethionine	44-47	catechol-O-methyltransferase	Homo sapiens	64-68
21210071-1	2011	Glycine N-methyltransferase (GNMT) is a major hepatic enzyme that converts S-adenosylmethionine to S-adenosylhomocysteine while generating sarcosine from glycine, hence it can regulate mediating methyl group availability in mammalian cells.	S-Adenosylmethionine	75-95	glycine N-methyltransferase	Homo sapiens	0-27
21210071-1	2011	Glycine N-methyltransferase (GNMT) is a major hepatic enzyme that converts S-adenosylmethionine to S-adenosylhomocysteine while generating sarcosine from glycine, hence it can regulate mediating methyl group availability in mammalian cells.	S-Adenosylmethionine	75-95	glycine N-methyltransferase	Homo sapiens	29-33
21335553-0	2011	S-adenosyl-L-methionine induces compaction of nascent peptide chain inside the ribosomal exit tunnel upon translation arrest in the Arabidopsis CGS1 gene.	S-Adenosylmethionine	0-23	Pyridoxal phosphate (PLP)-dependent transferases superfamily protein	Arabidopsis thaliana	144-148
21335553-1	2011	Expression of the Arabidopsis CGS1 gene, encoding the first committed enzyme of methionine biosynthesis, is feedback-regulated in response to S-adenosyl-L-methionine (AdoMet) at the mRNA level.	S-Adenosylmethionine	142-165	Pyridoxal phosphate (PLP)-dependent transferases superfamily protein	Arabidopsis thaliana	30-34
21335553-1	2011	Expression of the Arabidopsis CGS1 gene, encoding the first committed enzyme of methionine biosynthesis, is feedback-regulated in response to S-adenosyl-L-methionine (AdoMet) at the mRNA level.	S-Adenosylmethionine	167-173	Pyridoxal phosphate (PLP)-dependent transferases superfamily protein	Arabidopsis thaliana	30-34
21481189-2	2011	We show here that the mouse Dnmt3a DNA methyltransferase is able to transfer the methyl group from S-adenosyl-l-methionine (AdoMet) to a cysteine residue in its catalytic center.	S-Adenosylmethionine	124-130	DNA methyltransferase 3A	Mus musculus	28-34
21481189-2	2011	We show here that the mouse Dnmt3a DNA methyltransferase is able to transfer the methyl group from S-adenosyl-l-methionine (AdoMet) to a cysteine residue in its catalytic center.	S-Adenosylmethionine	124-130	methionine adenosyltransferase I, alpha	Mus musculus	99-122
21247894-1	2011	The X protein (HBx) of hepatitis B virus (HBV) is involved in the development of hepatocellular carcinoma (HCC), and methionine adenosyltransferase 2A (MAT2A) promotes the growth of liver cancer cells through altering S-adenosylmethionine homeostasis.	S-Adenosylmethionine	220-238	X protein	Hepatitis B virus	15-18
21247894-1	2011	The X protein (HBx) of hepatitis B virus (HBV) is involved in the development of hepatocellular carcinoma (HCC), and methionine adenosyltransferase 2A (MAT2A) promotes the growth of liver cancer cells through altering S-adenosylmethionine homeostasis.	S-Adenosylmethionine	220-238	methionine adenosyltransferase 2A	Homo sapiens	152-157
21247894-9	2011	Thus, we proposed that HBx activates MAT2A expression through NF-kappaB and CREB signaling pathways to reduce AdoMet production, inhibit hepatoma cell apoptosis, and perhaps enhance HCC development.	S-Adenosylmethionine	110-116	X protein	Hepatitis B virus	23-26
21247894-9	2011	Thus, we proposed that HBx activates MAT2A expression through NF-kappaB and CREB signaling pathways to reduce AdoMet production, inhibit hepatoma cell apoptosis, and perhaps enhance HCC development.	S-Adenosylmethionine	110-116	methionine adenosyltransferase 2A	Homo sapiens	37-42
21247894-9	2011	Thus, we proposed that HBx activates MAT2A expression through NF-kappaB and CREB signaling pathways to reduce AdoMet production, inhibit hepatoma cell apoptosis, and perhaps enhance HCC development.	S-Adenosylmethionine	110-116	cAMP responsive element binding protein 1	Homo sapiens	76-80
21339507-3	2011	Here we show that two lipid hydrolytic genes, pancreatic-related protein 2 (mPlrp2) and procolipase (mClps), expressed specifically in the mouse pancreas, are associated with the ratio of S-adenosylmethionine (AdoMet) to S-adenosylhomocysteine (AdoHcy).	S-Adenosylmethionine	188-208	pancreatic lipase-related protein 2	Mus musculus	76-82
21339507-3	2011	Here we show that two lipid hydrolytic genes, pancreatic-related protein 2 (mPlrp2) and procolipase (mClps), expressed specifically in the mouse pancreas, are associated with the ratio of S-adenosylmethionine (AdoMet) to S-adenosylhomocysteine (AdoHcy).	S-Adenosylmethionine	210-216	pancreatic lipase-related protein 2	Mus musculus	76-82
21275900-4	2011	In fact, the CBS enzyme contains a heme cofactor that functions as a redox sensor and utilizes S-adenosylmethionine (SAM) as an allosteric activator.	S-Adenosylmethionine	95-115	cystathionine beta-synthase	Homo sapiens	13-16
24212770-4	2011	Methionine adenosyltransferase (MAT) is an essential enzyme required for the biosynthesis of S-adenosylmethionine (AdoMet), an important methyl donor in the cell.	S-Adenosylmethionine	93-113	methionine adenosyltransferase 1A	Homo sapiens	0-30
24212770-4	2011	Methionine adenosyltransferase (MAT) is an essential enzyme required for the biosynthesis of S-adenosylmethionine (AdoMet), an important methyl donor in the cell.	S-Adenosylmethionine	93-113	methionine adenosyltransferase 1A	Homo sapiens	32-35
24212770-4	2011	Methionine adenosyltransferase (MAT) is an essential enzyme required for the biosynthesis of S-adenosylmethionine (AdoMet), an important methyl donor in the cell.	S-Adenosylmethionine	115-121	methionine adenosyltransferase 1A	Homo sapiens	0-30
24212770-4	2011	Methionine adenosyltransferase (MAT) is an essential enzyme required for the biosynthesis of S-adenosylmethionine (AdoMet), an important methyl donor in the cell.	S-Adenosylmethionine	115-121	methionine adenosyltransferase 1A	Homo sapiens	32-35
21196496-3	2011	The 1.7 A structure of the catalytic domain of NSD1 presented here shows that a regulatory loop adopts a conformation that prevents free access of H3K36 to the bound S-adenosyl-L-methionine.	S-Adenosylmethionine	166-189	nuclear receptor binding SET domain protein 1	Homo sapiens	47-51
21362551-1	2011	Protein methylation pathways comprise methionine adenosyltransferase (MAT), which produces S-adenosylmethionine (SAM) and SAM-dependent substrate-specific methyltransferases.	S-Adenosylmethionine	91-111	methionine adenosyltransferase I, alpha	Mus musculus	38-68
21362551-1	2011	Protein methylation pathways comprise methionine adenosyltransferase (MAT), which produces S-adenosylmethionine (SAM) and SAM-dependent substrate-specific methyltransferases.	S-Adenosylmethionine	91-111	methionine adenosyltransferase I, alpha	Mus musculus	70-73
21362551-1	2011	Protein methylation pathways comprise methionine adenosyltransferase (MAT), which produces S-adenosylmethionine (SAM) and SAM-dependent substrate-specific methyltransferases.	S-Adenosylmethionine	113-116	methionine adenosyltransferase I, alpha	Mus musculus	38-68
21362551-1	2011	Protein methylation pathways comprise methionine adenosyltransferase (MAT), which produces S-adenosylmethionine (SAM) and SAM-dependent substrate-specific methyltransferases.	S-Adenosylmethionine	113-116	methionine adenosyltransferase I, alpha	Mus musculus	70-73
21406397-4	2011	Therefore, changes in SHMT1 expression enable the determination of the specific contributions made by thymidylate and S-adenosylmethionine biosynthesis to CRC risk.	S-Adenosylmethionine	120-138	serine hydroxymethyltransferase 1 (soluble)	Mus musculus	22-27
20821054-7	2011	The presence of CBS in human plasma was confirmed by an in silico search of the proteome database, and was further evidenced by the activation of CBS by S-adenosyl-L-methionine and pyridoxal 5"-phosphate, and by configuration of the detected reaction product, 3,3-(2)H-cystathionine, which was in agreement with the previously observed CBS reaction mechanism.	S-Adenosylmethionine	153-176	cystathionine beta-synthase	Homo sapiens	16-19
21273441-4	2011	Set9 methylated the nuclear and cytoplasmic AR utilizing the cofactor S-adenosyl-methionine.	S-Adenosylmethionine	72-91	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	0-4
21273441-4	2011	Set9 methylated the nuclear and cytoplasmic AR utilizing the cofactor S-adenosyl-methionine.	S-Adenosylmethionine	72-91	androgen receptor	Homo sapiens	44-46
21273441-13	2011	Because the cellular metabolic state determines the level of S-adenosylmethionine and consequently the activity of Set9, the enhanced activity of methylated AR may have special significance in certain metabolic contexts.	S-Adenosylmethionine	61-81	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	115-119
21273441-13	2011	Because the cellular metabolic state determines the level of S-adenosylmethionine and consequently the activity of Set9, the enhanced activity of methylated AR may have special significance in certain metabolic contexts.	S-Adenosylmethionine	61-81	androgen receptor	Homo sapiens	157-159
20972225-6	2011	Remarkably, the restored growth of a nep1-1(ts) mutant upon addition of S-adenosylmethionine was even observed after preventing U1191 methylation in a Deltasnr35 mutant.	S-Adenosylmethionine	72-92	18S rRNA pseudouridine methyltransferase	Saccharomyces cerevisiae S288C	37-41
21135097-1	2011	The S-adenosylmethionine (AdoMet) salvage enzyme 5"-methylthioadenosine phosphorylase (MTAP) has been implicated as both a cancer target and a tumor suppressor.	S-Adenosylmethionine	4-24	methylthioadenosine phosphorylase	Mus musculus	49-85
21135097-1	2011	The S-adenosylmethionine (AdoMet) salvage enzyme 5"-methylthioadenosine phosphorylase (MTAP) has been implicated as both a cancer target and a tumor suppressor.	S-Adenosylmethionine	4-24	methylthioadenosine phosphorylase	Mus musculus	87-91
21135097-1	2011	The S-adenosylmethionine (AdoMet) salvage enzyme 5"-methylthioadenosine phosphorylase (MTAP) has been implicated as both a cancer target and a tumor suppressor.	S-Adenosylmethionine	26-32	methylthioadenosine phosphorylase	Mus musculus	49-85
21135097-1	2011	The S-adenosylmethionine (AdoMet) salvage enzyme 5"-methylthioadenosine phosphorylase (MTAP) has been implicated as both a cancer target and a tumor suppressor.	S-Adenosylmethionine	26-32	methylthioadenosine phosphorylase	Mus musculus	87-91
20512387-3	2011	The S-adenosylmethionine decarboxylase (AdoMetDC) catalyzes the irreversible decarboxylation of S-adenosylmethionine (AdoMet), generating the decarboxylated S-adenosylmethionine (dAdoMet), which is a substrate, together with putrescine, for spermidine synthase (SpdS).	S-Adenosylmethionine	4-24	adenosylmethionine decarboxylase 1	Homo sapiens	40-48
20512387-3	2011	The S-adenosylmethionine decarboxylase (AdoMetDC) catalyzes the irreversible decarboxylation of S-adenosylmethionine (AdoMet), generating the decarboxylated S-adenosylmethionine (dAdoMet), which is a substrate, together with putrescine, for spermidine synthase (SpdS).	S-Adenosylmethionine	4-24	spermidine synthase	Homo sapiens	241-260
20512387-3	2011	The S-adenosylmethionine decarboxylase (AdoMetDC) catalyzes the irreversible decarboxylation of S-adenosylmethionine (AdoMet), generating the decarboxylated S-adenosylmethionine (dAdoMet), which is a substrate, together with putrescine, for spermidine synthase (SpdS).	S-Adenosylmethionine	4-24	spermidine synthase	Homo sapiens	262-266
20512387-3	2011	The S-adenosylmethionine decarboxylase (AdoMetDC) catalyzes the irreversible decarboxylation of S-adenosylmethionine (AdoMet), generating the decarboxylated S-adenosylmethionine (dAdoMet), which is a substrate, together with putrescine, for spermidine synthase (SpdS).	S-Adenosylmethionine	40-46	adenosylmethionine decarboxylase 1	Homo sapiens	4-38
20512387-3	2011	The S-adenosylmethionine decarboxylase (AdoMetDC) catalyzes the irreversible decarboxylation of S-adenosylmethionine (AdoMet), generating the decarboxylated S-adenosylmethionine (dAdoMet), which is a substrate, together with putrescine, for spermidine synthase (SpdS).	S-Adenosylmethionine	40-46	spermidine synthase	Homo sapiens	241-260
20512387-3	2011	The S-adenosylmethionine decarboxylase (AdoMetDC) catalyzes the irreversible decarboxylation of S-adenosylmethionine (AdoMet), generating the decarboxylated S-adenosylmethionine (dAdoMet), which is a substrate, together with putrescine, for spermidine synthase (SpdS).	S-Adenosylmethionine	40-46	spermidine synthase	Homo sapiens	262-266
20512387-3	2011	The S-adenosylmethionine decarboxylase (AdoMetDC) catalyzes the irreversible decarboxylation of S-adenosylmethionine (AdoMet), generating the decarboxylated S-adenosylmethionine (dAdoMet), which is a substrate, together with putrescine, for spermidine synthase (SpdS).	S-Adenosylmethionine	96-116	adenosylmethionine decarboxylase 1	Homo sapiens	4-38
20512387-3	2011	The S-adenosylmethionine decarboxylase (AdoMetDC) catalyzes the irreversible decarboxylation of S-adenosylmethionine (AdoMet), generating the decarboxylated S-adenosylmethionine (dAdoMet), which is a substrate, together with putrescine, for spermidine synthase (SpdS).	S-Adenosylmethionine	96-116	adenosylmethionine decarboxylase 1	Homo sapiens	40-48
20512387-3	2011	The S-adenosylmethionine decarboxylase (AdoMetDC) catalyzes the irreversible decarboxylation of S-adenosylmethionine (AdoMet), generating the decarboxylated S-adenosylmethionine (dAdoMet), which is a substrate, together with putrescine, for spermidine synthase (SpdS).	S-Adenosylmethionine	96-116	spermidine synthase	Homo sapiens	241-260
20512387-3	2011	The S-adenosylmethionine decarboxylase (AdoMetDC) catalyzes the irreversible decarboxylation of S-adenosylmethionine (AdoMet), generating the decarboxylated S-adenosylmethionine (dAdoMet), which is a substrate, together with putrescine, for spermidine synthase (SpdS).	S-Adenosylmethionine	96-116	spermidine synthase	Homo sapiens	262-266
21068006-6	2011	Finally, we present a multiple isotopomer distribution analysis approach, based on transfer of deuterated methyl groups to S-adenosylmethionine and subsequent sequential methylations of PE, to quantify absolute flux rates through the PEMT pathway that are applicable to studies of liver dysfunction in clinical studies.	S-Adenosylmethionine	123-143	phosphatidylethanolamine N-methyltransferase	Homo sapiens	234-238
20821054-7	2011	The presence of CBS in human plasma was confirmed by an in silico search of the proteome database, and was further evidenced by the activation of CBS by S-adenosyl-L-methionine and pyridoxal 5"-phosphate, and by configuration of the detected reaction product, 3,3-(2)H-cystathionine, which was in agreement with the previously observed CBS reaction mechanism.	S-Adenosylmethionine	153-176	cystathionine beta-synthase	Homo sapiens	146-149
20821054-7	2011	The presence of CBS in human plasma was confirmed by an in silico search of the proteome database, and was further evidenced by the activation of CBS by S-adenosyl-L-methionine and pyridoxal 5"-phosphate, and by configuration of the detected reaction product, 3,3-(2)H-cystathionine, which was in agreement with the previously observed CBS reaction mechanism.	S-Adenosylmethionine	153-176	cystathionine beta-synthase	Homo sapiens	146-149
21093336-4	2011	Understanding the relationship between BHMT genetic polymorphisms and function might increase our understanding of the role of this reaction in homocysteine remethylation and in S-adenosylmethionine-dependent methylation.	S-Adenosylmethionine	178-198	betaine--homocysteine S-methyltransferase	Homo sapiens	39-43
21304959-6	2011	COMT has been shown to interact with methylenetetrahydrofolate reductase (MTHFR), which modulates the availability of S-adenosylmethionine (SAM), a COMT cofactor.	S-Adenosylmethionine	118-138	catechol-O-methyltransferase	Homo sapiens	0-4
21304959-6	2011	COMT has been shown to interact with methylenetetrahydrofolate reductase (MTHFR), which modulates the availability of S-adenosylmethionine (SAM), a COMT cofactor.	S-Adenosylmethionine	118-138	methylenetetrahydrofolate reductase	Homo sapiens	37-72
21619845-10	2011	The TBIL level dropped at 7 d 5 patients showed an increase in ALT at 7 d and 3 patients showed a decrease in AST at 7 d. CONCLUSION: Transmetil may play an important role in reducing the mortality of Amanita verna poisoning.	S-Adenosylmethionine	134-144	solute carrier family 17 member 5	Homo sapiens	110-113
21304959-6	2011	COMT has been shown to interact with methylenetetrahydrofolate reductase (MTHFR), which modulates the availability of S-adenosylmethionine (SAM), a COMT cofactor.	S-Adenosylmethionine	118-138	methylenetetrahydrofolate reductase	Homo sapiens	74-79
21304959-6	2011	COMT has been shown to interact with methylenetetrahydrofolate reductase (MTHFR), which modulates the availability of S-adenosylmethionine (SAM), a COMT cofactor.	S-Adenosylmethionine	118-138	catechol-O-methyltransferase	Homo sapiens	148-152
21304959-6	2011	COMT has been shown to interact with methylenetetrahydrofolate reductase (MTHFR), which modulates the availability of S-adenosylmethionine (SAM), a COMT cofactor.	S-Adenosylmethionine	140-143	catechol-O-methyltransferase	Homo sapiens	0-4
21304959-6	2011	COMT has been shown to interact with methylenetetrahydrofolate reductase (MTHFR), which modulates the availability of S-adenosylmethionine (SAM), a COMT cofactor.	S-Adenosylmethionine	140-143	methylenetetrahydrofolate reductase	Homo sapiens	37-72
21304959-6	2011	COMT has been shown to interact with methylenetetrahydrofolate reductase (MTHFR), which modulates the availability of S-adenosylmethionine (SAM), a COMT cofactor.	S-Adenosylmethionine	140-143	methylenetetrahydrofolate reductase	Homo sapiens	74-79
21304959-6	2011	COMT has been shown to interact with methylenetetrahydrofolate reductase (MTHFR), which modulates the availability of S-adenosylmethionine (SAM), a COMT cofactor.	S-Adenosylmethionine	140-143	catechol-O-methyltransferase	Homo sapiens	148-152
21206058-4	2011	An X-ray crystal structure of human LCMT1 protein in complex with the cofactor S-adenosylmethionine (AdoMet) has been solved to a resolution of 2 A.	S-Adenosylmethionine	81-99	leucine carboxyl methyltransferase 1	Homo sapiens	36-41
21243721-5	2011	Our strategy makes use of an alkyne-bearing S-adenosylmethionine (SAM) analogue, which is accepted by the PKMT, SETDB1, as a cofactor, resulting in the enzymatic attachment of a terminal alkyne to its substrate.	S-Adenosylmethionine	44-64	SET domain bifurcated histone lysine methyltransferase 1	Homo sapiens	112-118
21243721-5	2011	Our strategy makes use of an alkyne-bearing S-adenosylmethionine (SAM) analogue, which is accepted by the PKMT, SETDB1, as a cofactor, resulting in the enzymatic attachment of a terminal alkyne to its substrate.	S-Adenosylmethionine	66-69	SET domain bifurcated histone lysine methyltransferase 1	Homo sapiens	112-118
20955694-5	2011	CBS enzyme activity is allosterically regulated by the endogenous activator S-adenosyl methionine.	S-Adenosylmethionine	78-97	cystathionine beta-synthase	Mus musculus	0-3
20955694-9	2011	We demonstrate that CBS enzyme from endogenous sources can be activated by S-adenosyl methionine to a greater extent compared to recombinant enzyme, suggesting greater potential for activation than previously anticipated.	S-Adenosylmethionine	75-96	cystathionine beta-synthase	Mus musculus	20-23
21036620-2	2010	To obtain novel inhibitors as tools for investigating the physiological function of members of the HMT family, we designed and synthesized novel inhibitors, which are amine analogues of adenosylmethionine (AdoMet; the cofactor utilized in the methylation reaction) bearing various alkylamino groups coupled via an ethylene linker.	S-Adenosylmethionine	186-204	histamine N-methyltransferase	Homo sapiens	99-102
21731446-2	2011	Arsenic (+3 oxidation state) methyltransferase (AS3MT) that can catalyze the transfer of a methyl group from S-adenosyl-l-methionine (AdoMet) to trivalent arsenical, may play a role in arsenic metabolism in humans.	S-Adenosylmethionine	109-132	arsenite methyltransferase	Homo sapiens	0-46
21731446-2	2011	Arsenic (+3 oxidation state) methyltransferase (AS3MT) that can catalyze the transfer of a methyl group from S-adenosyl-l-methionine (AdoMet) to trivalent arsenical, may play a role in arsenic metabolism in humans.	S-Adenosylmethionine	109-132	arsenite methyltransferase	Homo sapiens	48-53
21731446-2	2011	Arsenic (+3 oxidation state) methyltransferase (AS3MT) that can catalyze the transfer of a methyl group from S-adenosyl-l-methionine (AdoMet) to trivalent arsenical, may play a role in arsenic metabolism in humans.	S-Adenosylmethionine	134-140	arsenite methyltransferase	Homo sapiens	0-46
21731446-2	2011	Arsenic (+3 oxidation state) methyltransferase (AS3MT) that can catalyze the transfer of a methyl group from S-adenosyl-l-methionine (AdoMet) to trivalent arsenical, may play a role in arsenic metabolism in humans.	S-Adenosylmethionine	134-140	arsenite methyltransferase	Homo sapiens	48-53
21858212-11	2011	CONCLUSIONS/SIGNIFICANCE: The different intersubunit interfaces and rearrangement of subunits of Thermus MTHFR may be related to human enzyme properties, such as the allosteric regulation by S-adenosylmethionine and the enhanced instability of the Ala222Val mutant upon loss of FAD.	S-Adenosylmethionine	191-211	methylenetetrahydrofolate reductase	Homo sapiens	105-110
21779408-2	2011	Here we report an analysis of the crystal structure of the full length human SMYD3 in a complex with an analog of the S-adenosyl methionine (SAM) methyl donor cofactor.	S-Adenosylmethionine	118-139	SET and MYND domain containing 3	Homo sapiens	77-82
21779408-2	2011	Here we report an analysis of the crystal structure of the full length human SMYD3 in a complex with an analog of the S-adenosyl methionine (SAM) methyl donor cofactor.	S-Adenosylmethionine	141-144	SET and MYND domain containing 3	Homo sapiens	77-82
21625555-6	2011	In addition, the results of molecular docking and MD simulations indicate that the new water channel continues to remain open when S-adenosyl-L-methionine (AdoMet) or S-adenosyl-L-homocysteine (AdoHcy) is bound to SET9.	S-Adenosylmethionine	131-154	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	214-218
21625555-6	2011	In addition, the results of molecular docking and MD simulations indicate that the new water channel continues to remain open when S-adenosyl-L-methionine (AdoMet) or S-adenosyl-L-homocysteine (AdoHcy) is bound to SET9.	S-Adenosylmethionine	156-162	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	214-218
21081698-6	2010	Furthermore, the structure of the regulatory "energy-sensing" CBS domains, named after this protein, suggests a mechanism for allosteric activation by S-adenosylmethionine.	S-Adenosylmethionine	151-171	Cystathionine beta-synthase	Drosophila melanogaster	62-65
21904625-0	2011	Structural mechanism of S-adenosyl methionine binding to catechol O-methyltransferase.	S-Adenosylmethionine	24-45	catechol-O-methyltransferase	Homo sapiens	57-85
20608698-2	2010	The reaction requires the cofactors S-adenosyl-L-methionine (SAM), pyridoxal-5"-phosphate (PLP), and a [4Fe-4S] cluster.	S-Adenosylmethionine	38-59	pyridoxal phosphatase	Homo sapiens	91-94
21152119-0	2010	S-adenosylmethionine inhibits the growth of cancer cells by reversing the hypomethylation status of c-myc and H-ras in human gastric cancer and colon cancer.	S-Adenosylmethionine	0-20	MYC proto-oncogene, bHLH transcription factor	Homo sapiens	100-105
21152119-0	2010	S-adenosylmethionine inhibits the growth of cancer cells by reversing the hypomethylation status of c-myc and H-ras in human gastric cancer and colon cancer.	S-Adenosylmethionine	0-20	HRas proto-oncogene, GTPase	Homo sapiens	110-115
21036620-2	2010	To obtain novel inhibitors as tools for investigating the physiological function of members of the HMT family, we designed and synthesized novel inhibitors, which are amine analogues of adenosylmethionine (AdoMet; the cofactor utilized in the methylation reaction) bearing various alkylamino groups coupled via an ethylene linker.	S-Adenosylmethionine	206-212	histamine N-methyltransferase	Homo sapiens	99-102
20036517-8	2010	CONCLUSION: Our results imply that methionine deprivation induces a metabolic state in which methionine is effectively conserved in tissue by shutdown of the transsulfuration pathway by an S-adenosylmethionine-independent mechanism that signals a rapid downregulation of CBS protein.	S-Adenosylmethionine	189-209	cystathionine beta-synthase	Mus musculus	271-274
20980671-1	2010	Trm5 is a eukaryal and archaeal tRNA methyltransferase that catalyzes methyl transfer from S-adenosylmethionine (AdoMet) to the N(1) position of G37 directly 3" to the anticodon.	S-Adenosylmethionine	91-111	tRNA methyltransferase 5	Homo sapiens	0-4
20980671-1	2010	Trm5 is a eukaryal and archaeal tRNA methyltransferase that catalyzes methyl transfer from S-adenosylmethionine (AdoMet) to the N(1) position of G37 directly 3" to the anticodon.	S-Adenosylmethionine	113-119	tRNA methyltransferase 5	Homo sapiens	0-4
21154325-1	2010	The enzyme catechol-O-methyltransferase (COMT) transfers a methyl group from S-adenosylmethionine to the benzene ring of catecholamines including the neurotransmitters dopamine, epinephrine and norepinephrine.	S-Adenosylmethionine	77-97	catechol-O-methyltransferase	Homo sapiens	11-39
21154325-1	2010	The enzyme catechol-O-methyltransferase (COMT) transfers a methyl group from S-adenosylmethionine to the benzene ring of catecholamines including the neurotransmitters dopamine, epinephrine and norepinephrine.	S-Adenosylmethionine	77-97	catechol-O-methyltransferase	Homo sapiens	41-45
21079746-3	2010	S-adenosyl-L-methionine (SAMe) and betaine potentiate IFNalpha signaling in cultured cells that express hepatitis C virus (HCV) proteins, and enhance the inhibitory effect of IFNalpha on HCV replicons.	S-Adenosylmethionine	0-23	interferon alpha 1	Homo sapiens	54-62
21079746-3	2010	S-adenosyl-L-methionine (SAMe) and betaine potentiate IFNalpha signaling in cultured cells that express hepatitis C virus (HCV) proteins, and enhance the inhibitory effect of IFNalpha on HCV replicons.	S-Adenosylmethionine	0-23	interferon alpha 1	Homo sapiens	175-183
20815019-2	2010	Mice lacking the methionine adenosyltransferase (MAT) gene MAT1A exhibit a chronic reduction in hepatic S-adenosylmethionine (SAMe) levels, basal activation of LKB1, and spontaneous development of nonalcoholic steatohepatitis (NASH) and hepatocellular carcinoma (HCC).	S-Adenosylmethionine	104-124	methionine adenosyltransferase I, alpha	Mus musculus	17-47
20815019-2	2010	Mice lacking the methionine adenosyltransferase (MAT) gene MAT1A exhibit a chronic reduction in hepatic S-adenosylmethionine (SAMe) levels, basal activation of LKB1, and spontaneous development of nonalcoholic steatohepatitis (NASH) and hepatocellular carcinoma (HCC).	S-Adenosylmethionine	104-124	methionine adenosyltransferase I, alpha	Mus musculus	59-64
20647003-1	2010	Protein arginine N-methyltransferase 3 (PRMT3) is a cytoplasmic enzyme that utilizes S-adenosyl-L-methionine (AdoMet) to methylate specific proteins, most of which contain GAR (glycine-arginine rich) motifs.	S-Adenosylmethionine	85-108	protein arginine methyltransferase 3	Rattus norvegicus	0-38
20864509-1	2010	S-adenosyl-(L)-homocysteine (SAH) riboswitches are regulatory elements found in bacterial mRNAs that up-regulate genes involved in the S-adenosyl-(L)-methionine (SAM) regeneration cycle.	S-Adenosylmethionine	137-160	acyl-CoA synthetase medium chain family member 3	Homo sapiens	29-32
19826910-1	2010	Evidence indicates that both S-adenosylmethionine (SAMe) metabolism and intramuscular fat are associated with insulin resistance and type II diabetes.	S-Adenosylmethionine	29-49	insulin	Sus scrofa	110-117
20675163-2	2010	In the liver, MAT I and III, tetrameric and dimeric isoforms of the same catalytic subunit encoded by the gene MAT1A, account for the predominant portion of total body synthesis of S-adenosylmethionine (SAM), a versatile sulfonium ion-containing molecule involved in a variety of vital metabolic reactions and in the control of hepatocyte proliferation and differentiation.	S-Adenosylmethionine	181-201	methionine adenosyltransferase 1A	Homo sapiens	111-116
20675163-2	2010	In the liver, MAT I and III, tetrameric and dimeric isoforms of the same catalytic subunit encoded by the gene MAT1A, account for the predominant portion of total body synthesis of S-adenosylmethionine (SAM), a versatile sulfonium ion-containing molecule involved in a variety of vital metabolic reactions and in the control of hepatocyte proliferation and differentiation.	S-Adenosylmethionine	203-206	methionine adenosyltransferase 1A	Homo sapiens	111-116
20647003-1	2010	Protein arginine N-methyltransferase 3 (PRMT3) is a cytoplasmic enzyme that utilizes S-adenosyl-L-methionine (AdoMet) to methylate specific proteins, most of which contain GAR (glycine-arginine rich) motifs.	S-Adenosylmethionine	85-108	protein arginine methyltransferase 3	Rattus norvegicus	40-45
20647003-1	2010	Protein arginine N-methyltransferase 3 (PRMT3) is a cytoplasmic enzyme that utilizes S-adenosyl-L-methionine (AdoMet) to methylate specific proteins, most of which contain GAR (glycine-arginine rich) motifs.	S-Adenosylmethionine	110-116	protein arginine methyltransferase 3	Rattus norvegicus	0-38
20647003-1	2010	Protein arginine N-methyltransferase 3 (PRMT3) is a cytoplasmic enzyme that utilizes S-adenosyl-L-methionine (AdoMet) to methylate specific proteins, most of which contain GAR (glycine-arginine rich) motifs.	S-Adenosylmethionine	110-116	protein arginine methyltransferase 3	Rattus norvegicus	40-45
20677792-3	2010	S-Adenosyl-l-methionine (SAM), the primary methyl group donor for enzyme-mediated methylation of proteins and other biological targets, activates RyR2 via an unknown mechanism.	S-Adenosylmethionine	0-23	ryanodine receptor 2	Homo sapiens	146-150
20677792-3	2010	S-Adenosyl-l-methionine (SAM), the primary methyl group donor for enzyme-mediated methylation of proteins and other biological targets, activates RyR2 via an unknown mechanism.	S-Adenosylmethionine	25-28	ryanodine receptor 2	Homo sapiens	146-150
20600111-1	2010	tRNA:m(5)C methyltransferase Trm4 generates the modified nucleotide 5-methylcytidine in archaeal and eukaryotic tRNA molecules, using S-adenosyl-l-methionine (AdoMet) as methyl donor.	S-Adenosylmethionine	134-157	NOP2/Sun RNA methyltransferase 2	Homo sapiens	29-33
20499380-8	2010	Additionally, downregulation of SM22alpha, either by siRNA or by a methyl group donor (S-adenosyl methionine), resulted in overexpression of Cbfa1.	S-Adenosylmethionine	87-108	transgelin	Homo sapiens	32-41
20499380-8	2010	Additionally, downregulation of SM22alpha, either by siRNA or by a methyl group donor (S-adenosyl methionine), resulted in overexpression of Cbfa1.	S-Adenosylmethionine	87-108	RUNX family transcription factor 2	Homo sapiens	141-146
20838441-2	2010	Inhibition of polyamine synthesis by ornithine decarboxylase antizyme-1 (OAZ) in human oral cancer cell line resulted in accumulation of decarboxylated S-adenosylmethionine (dcSAM), which acts as a competitive inhibitor of methylation reactions.	S-Adenosylmethionine	152-172	ornithine decarboxylase antizyme 1	Homo sapiens	37-71
20838441-2	2010	Inhibition of polyamine synthesis by ornithine decarboxylase antizyme-1 (OAZ) in human oral cancer cell line resulted in accumulation of decarboxylated S-adenosylmethionine (dcSAM), which acts as a competitive inhibitor of methylation reactions.	S-Adenosylmethionine	152-172	ornithine decarboxylase antizyme 1	Homo sapiens	73-76
20600111-1	2010	tRNA:m(5)C methyltransferase Trm4 generates the modified nucleotide 5-methylcytidine in archaeal and eukaryotic tRNA molecules, using S-adenosyl-l-methionine (AdoMet) as methyl donor.	S-Adenosylmethionine	159-165	NOP2/Sun RNA methyltransferase 2	Homo sapiens	29-33
20452364-5	2010	TrmD and Trm5 catalyze methyl transfer to synthesize the m1G37 base at the 3" position adjacent to the tRNA anticodon, using S-adenosyl methionine (AdoMet) as the methyl donor.	S-Adenosylmethionine	125-146	tRNA methyltransferase 5	Homo sapiens	9-13
20433827-11	2010	Previous studies indicate that S-adenosylmethionine or betaine prevented IFNg induced UbD and MDB formations.	S-Adenosylmethionine	31-51	interferon gamma	Mus musculus	73-77
20452364-5	2010	TrmD and Trm5 catalyze methyl transfer to synthesize the m1G37 base at the 3" position adjacent to the tRNA anticodon, using S-adenosyl methionine (AdoMet) as the methyl donor.	S-Adenosylmethionine	148-154	tRNA methyltransferase 5	Homo sapiens	9-13
20421295-10	2010	We show that yeast cells can take up (R,S)-AdoMet from the medium using the same transporter (Sam3) used to import (S,S)-AdoMet.	S-Adenosylmethionine	115-127	bifunctional polyamine/amino acid permease SAM3	Saccharomyces cerevisiae S288C	94-98
20444942-1	2010	Methylenetetrahydrofolate reductase (MTHFR) is a crucial folate pathway enzyme that contributes to the maintenance of cellular pools of S-adenosylmethionine, the universal methyl donor for several reactions including DNA methylation.	S-Adenosylmethionine	136-156	methylenetetrahydrofolate reductase	Homo sapiens	0-35
20444942-1	2010	Methylenetetrahydrofolate reductase (MTHFR) is a crucial folate pathway enzyme that contributes to the maintenance of cellular pools of S-adenosylmethionine, the universal methyl donor for several reactions including DNA methylation.	S-Adenosylmethionine	136-156	methylenetetrahydrofolate reductase	Homo sapiens	37-42
20578266-1	2010	UNLABELLED: Deletion of glycine N-methyltransferase (GNMT), the main gene involved in liver S-adenosylmethionine (SAM) catabolism, leads to the hepatic accumulation of this molecule and the development of fatty liver and fibrosis in mice.	S-Adenosylmethionine	94-112	glycine N-methyltransferase	Mus musculus	24-51
20578266-1	2010	UNLABELLED: Deletion of glycine N-methyltransferase (GNMT), the main gene involved in liver S-adenosylmethionine (SAM) catabolism, leads to the hepatic accumulation of this molecule and the development of fatty liver and fibrosis in mice.	S-Adenosylmethionine	94-112	glycine N-methyltransferase	Mus musculus	53-57
20578266-1	2010	UNLABELLED: Deletion of glycine N-methyltransferase (GNMT), the main gene involved in liver S-adenosylmethionine (SAM) catabolism, leads to the hepatic accumulation of this molecule and the development of fatty liver and fibrosis in mice.	S-Adenosylmethionine	114-117	glycine N-methyltransferase	Mus musculus	24-51
20578266-1	2010	UNLABELLED: Deletion of glycine N-methyltransferase (GNMT), the main gene involved in liver S-adenosylmethionine (SAM) catabolism, leads to the hepatic accumulation of this molecule and the development of fatty liver and fibrosis in mice.	S-Adenosylmethionine	114-117	glycine N-methyltransferase	Mus musculus	53-57
20146260-9	2010	Ursodeoxycholic acid (UDCA) or S-adenosylmethionine (SAMe) prevented the LCA-induced decrease in expression of GSH synthetic enzymes and promoter activity and prevented the increase in MafG and c-Maf levels.	S-Adenosylmethionine	31-51	v-maf musculoaponeurotic fibrosarcoma oncogene family, protein G (avian)	Mus musculus	185-189
20381365-1	2010	Aminopropyl transferases like spermidine synthase (SPDS; EC 2.5.1.16), spermine synthase and thermospermine synthase (SPMS, tSPMS; EC 2.5.1.22) belong to a class of widely distributed enzymes that use decarboxylated S-adenosylmethionine as an aminopropyl donor and putrescine or spermidine as an amino acceptor to form in that order spermidine, spermine or thermospermine.	S-Adenosylmethionine	218-236	spermidine synthase 3	Arabidopsis thaliana	118-122
20185185-3	2010	GNMT is a mediator in the methionine and folate cycles, and the homotetrameric form enzymatically transfers a methyl group from S-adenosylmethionine (SAM) to glycine forming S-adenosylhomocysteine (SAH) and sarcosine.	S-Adenosylmethionine	128-148	glycine N-methyltransferase	Fundulus heteroclitus	0-4
20185185-3	2010	GNMT is a mediator in the methionine and folate cycles, and the homotetrameric form enzymatically transfers a methyl group from S-adenosylmethionine (SAM) to glycine forming S-adenosylhomocysteine (SAH) and sarcosine.	S-Adenosylmethionine	150-153	glycine N-methyltransferase	Fundulus heteroclitus	0-4
20689184-2	2010	MA-ACS1 catalyses the conversion of S-adenosyl-L-methionine (SAM) to ACC, the key regulatory step in ethylene biosynthesis.	S-Adenosylmethionine	36-59	1-aminocyclopropane-1-carboxylate synthase	Musa acuminata	0-7
20689184-2	2010	MA-ACS1 catalyses the conversion of S-adenosyl-L-methionine (SAM) to ACC, the key regulatory step in ethylene biosynthesis.	S-Adenosylmethionine	61-64	1-aminocyclopropane-1-carboxylate synthase	Musa acuminata	0-7
20208423-0	2010	S-Adenosyl-L-methionine ameliorates TNFalpha-induced insulin resistance in 3T3-L1 adipocytes.	S-Adenosylmethionine	2-23	tumor necrosis factor	Homo sapiens	36-44
20208423-0	2010	S-Adenosyl-L-methionine ameliorates TNFalpha-induced insulin resistance in 3T3-L1 adipocytes.	S-Adenosylmethionine	2-23	insulin	Homo sapiens	53-60
20363925-1	2010	Methionine adenosyltransferase (MAT) catalyzes the synthesis of S-adenosylmethionine, the principal methyl donor, and is encoded by MAT1A and MAT2A in mammals.	S-Adenosylmethionine	64-84	methionine adenosyltransferase 1A	Homo sapiens	132-137
20363925-1	2010	Methionine adenosyltransferase (MAT) catalyzes the synthesis of S-adenosylmethionine, the principal methyl donor, and is encoded by MAT1A and MAT2A in mammals.	S-Adenosylmethionine	64-84	methionine adenosyltransferase 2A	Homo sapiens	142-147
20363925-7	2010	Huh7 cells overexpressing MAT1A had higher S-adenosylmethionine levels but lower bromodeoxyuridine incorporation than control cells.	S-Adenosylmethionine	43-63	methionine adenosyltransferase 1A	Homo sapiens	26-31
20102719-1	2010	BACKGROUND & AIMS: Hepatic de-differentiation, liver development, and malignant transformation are processes in which the levels of hepatic S-adenosylmethionine are tightly regulated by 2 genes: methionine adenosyltransferase 1A (MAT1A) and methionine adenosyltransferase 2A (MAT2A).	S-Adenosylmethionine	144-164	methionine adenosyltransferase 1A	Homo sapiens	199-232
20102719-1	2010	BACKGROUND & AIMS: Hepatic de-differentiation, liver development, and malignant transformation are processes in which the levels of hepatic S-adenosylmethionine are tightly regulated by 2 genes: methionine adenosyltransferase 1A (MAT1A) and methionine adenosyltransferase 2A (MAT2A).	S-Adenosylmethionine	144-164	methionine adenosyltransferase 1A	Homo sapiens	234-239
20102719-1	2010	BACKGROUND & AIMS: Hepatic de-differentiation, liver development, and malignant transformation are processes in which the levels of hepatic S-adenosylmethionine are tightly regulated by 2 genes: methionine adenosyltransferase 1A (MAT1A) and methionine adenosyltransferase 2A (MAT2A).	S-Adenosylmethionine	144-164	methionine adenosyltransferase 2A	Homo sapiens	245-278
20102719-1	2010	BACKGROUND & AIMS: Hepatic de-differentiation, liver development, and malignant transformation are processes in which the levels of hepatic S-adenosylmethionine are tightly regulated by 2 genes: methionine adenosyltransferase 1A (MAT1A) and methionine adenosyltransferase 2A (MAT2A).	S-Adenosylmethionine	144-164	methionine adenosyltransferase 2A	Homo sapiens	280-285
20102719-7	2010	S-adenosylmethionine treatment altered this homeostasis by shifting the balance of AUF1 and methyl-HuR/HuR, which was identified as an inhibitor of MAT2A messenger RNA (mRNA) stability.	S-Adenosylmethionine	0-20	heterogeneous nuclear ribonucleoprotein D	Homo sapiens	83-87
20102719-7	2010	S-adenosylmethionine treatment altered this homeostasis by shifting the balance of AUF1 and methyl-HuR/HuR, which was identified as an inhibitor of MAT2A messenger RNA (mRNA) stability.	S-Adenosylmethionine	0-20	ELAV like RNA binding protein 1	Homo sapiens	99-102
20102719-7	2010	S-adenosylmethionine treatment altered this homeostasis by shifting the balance of AUF1 and methyl-HuR/HuR, which was identified as an inhibitor of MAT2A messenger RNA (mRNA) stability.	S-Adenosylmethionine	0-20	ELAV like RNA binding protein 1	Homo sapiens	103-106
20102719-7	2010	S-adenosylmethionine treatment altered this homeostasis by shifting the balance of AUF1 and methyl-HuR/HuR, which was identified as an inhibitor of MAT2A messenger RNA (mRNA) stability.	S-Adenosylmethionine	0-20	methionine adenosyltransferase 2A	Homo sapiens	148-153
20380929-10	2010	Preliminary results of S-adenosylmethionine (SAM) supplementation in two Arts syndrome patients show improvement of their condition, indicating that SAM supplementation in the diet could alleviate some of the symptoms of patients with PRPS1 spectrum diseases by replenishing purine nucleotides (J.C., unpublished data).	S-Adenosylmethionine	23-43	phosphoribosyl pyrophosphate synthetase 1	Homo sapiens	235-240
20080087-1	2010	Regeneration of the liver is inhibited as a result of a sustained increase in S-adenosylmethionine levels in glycine N-methyltransferase (GNMT)-/- mice.	S-Adenosylmethionine	78-98	glycine N-methyltransferase	Mus musculus	109-136
20080087-1	2010	Regeneration of the liver is inhibited as a result of a sustained increase in S-adenosylmethionine levels in glycine N-methyltransferase (GNMT)-/- mice.	S-Adenosylmethionine	78-98	glycine N-methyltransferase	Mus musculus	138-142
19701798-2	2010	Two genes (MAT1A and MAT2A) encode for the catalytic subunit of MAT, while a third gene (MAT2beta) encodes for a regulatory subunit (MAT II beta) that regulates the activity of the MAT2A-encoded isoenzyme and intracellular S-adenosylmethionine levels.	S-Adenosylmethionine	223-243	methionine adenosyltransferase 1A	Sus scrofa	11-16
19701798-2	2010	Two genes (MAT1A and MAT2A) encode for the catalytic subunit of MAT, while a third gene (MAT2beta) encodes for a regulatory subunit (MAT II beta) that regulates the activity of the MAT2A-encoded isoenzyme and intracellular S-adenosylmethionine levels.	S-Adenosylmethionine	223-243	methionine adenosyltransferase 2A	Sus scrofa	21-26
19701798-2	2010	Two genes (MAT1A and MAT2A) encode for the catalytic subunit of MAT, while a third gene (MAT2beta) encodes for a regulatory subunit (MAT II beta) that regulates the activity of the MAT2A-encoded isoenzyme and intracellular S-adenosylmethionine levels.	S-Adenosylmethionine	223-243	methionine adenosyltransferase 2B	Sus scrofa	89-97
19701798-2	2010	Two genes (MAT1A and MAT2A) encode for the catalytic subunit of MAT, while a third gene (MAT2beta) encodes for a regulatory subunit (MAT II beta) that regulates the activity of the MAT2A-encoded isoenzyme and intracellular S-adenosylmethionine levels.	S-Adenosylmethionine	223-243	methionine adenosyltransferase 2A	Sus scrofa	181-186
20146260-9	2010	Ursodeoxycholic acid (UDCA) or S-adenosylmethionine (SAMe) prevented the LCA-induced decrease in expression of GSH synthetic enzymes and promoter activity and prevented the increase in MafG and c-Maf levels.	S-Adenosylmethionine	31-51	avian musculoaponeurotic fibrosarcoma oncogene homolog	Mus musculus	194-199
19857525-5	2010	The potential improvement of S-adenosylmethionine (SAM) in the antiviral effect of IFN-alpha was also investigated.	S-Adenosylmethionine	29-49	interferon alpha 1	Homo sapiens	83-92
20238404-0	2010	Hepatoprotective effects of S-adenosyl-L-methionine against alcohol- and cytochrome P450 2E1-induced liver injury.	S-Adenosylmethionine	28-51	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	73-92
19857525-5	2010	The potential improvement of S-adenosylmethionine (SAM) in the antiviral effect of IFN-alpha was also investigated.	S-Adenosylmethionine	51-54	interferon alpha 1	Homo sapiens	83-92
20356199-1	2010	In this paper, we report on n-alkyl phosphonic acid (PA) self-assembled monolayer (SAM)/hafnium oxide (HfO(2)) hybrid dielectrics utilizing the advantages of SAMs for control over the dielectric/semiconductor interface with those of high-k metal oxides for low-voltage organic thin film transistors (OTFTs).	S-Adenosylmethionine	83-86	methionine adenosyltransferase 1A	Homo sapiens	158-162
20026078-0	2010	Binding of S-methyl-5"-thioadenosine and S-adenosyl-L-methionine to protein MJ0100 triggers an open-to-closed conformational change in its CBS motif pair.	S-Adenosylmethionine	41-64	cystathionine beta-synthase	Homo sapiens	139-142
20026078-4	2010	This work presents the crystallographic analysis of four different states of the CBS motif pair of MJ0100 in complex with different numbers of S-adenosyl-L-methionine (SAM) and S-methyl-5"-thioadenosine (MTA) ligands, providing evidence that ligand-induced conformational reorganization of Bateman domain dimers could be an important regulatory mechanism.	S-Adenosylmethionine	143-166	cystathionine beta-synthase	Homo sapiens	81-84
20026078-4	2010	This work presents the crystallographic analysis of four different states of the CBS motif pair of MJ0100 in complex with different numbers of S-adenosyl-L-methionine (SAM) and S-methyl-5"-thioadenosine (MTA) ligands, providing evidence that ligand-induced conformational reorganization of Bateman domain dimers could be an important regulatory mechanism.	S-Adenosylmethionine	168-171	cystathionine beta-synthase	Homo sapiens	81-84
20043323-2	2010	Methionine adenosyltransferase (MAT) catalyzes biosynthesis of S-adenosylmethionine (SAMe), the principle methyl donor.	S-Adenosylmethionine	63-83	methionine adenosyltransferase 1A	Homo sapiens	0-30
20026257-2	2010	Both human NAT1 and its murine equivalent NAT2 have previously been shown to play roles in the catabolism of folate, which is required for the synthesis of S-adenosylmethionine, the methyl donor for cellular methylation reactions.	S-Adenosylmethionine	156-176	N-acetyltransferase 1	Homo sapiens	11-15
20026257-2	2010	Both human NAT1 and its murine equivalent NAT2 have previously been shown to play roles in the catabolism of folate, which is required for the synthesis of S-adenosylmethionine, the methyl donor for cellular methylation reactions.	S-Adenosylmethionine	156-176	N-acetyltransferase 2 (arylamine N-acetyltransferase)	Mus musculus	42-46
20413874-4	2010	S-adenosylmethionine potentiated superoxide dismutase and glutathione S-transferase activity and restored altered brain glutathione and erythrocytes lipid peroxidation.	S-Adenosylmethionine	0-20	hematopoietic prostaglandin D synthase	Mus musculus	58-83
19892394-1	2010	Glycine N-methyltransferase (GNMT) is a mediator in the methionine and folate cycles, and is responsible for the transfer of a methyl group from S-adenosylmethionine (SAM) to glycine forming S-adenosylhomocysteine (SAH) and sarcosine.	S-Adenosylmethionine	145-165	glycine N-methyltransferase	Fundulus heteroclitus	0-27
19892394-1	2010	Glycine N-methyltransferase (GNMT) is a mediator in the methionine and folate cycles, and is responsible for the transfer of a methyl group from S-adenosylmethionine (SAM) to glycine forming S-adenosylhomocysteine (SAH) and sarcosine.	S-Adenosylmethionine	145-165	glycine N-methyltransferase	Fundulus heteroclitus	29-33
19892394-1	2010	Glycine N-methyltransferase (GNMT) is a mediator in the methionine and folate cycles, and is responsible for the transfer of a methyl group from S-adenosylmethionine (SAM) to glycine forming S-adenosylhomocysteine (SAH) and sarcosine.	S-Adenosylmethionine	167-170	glycine N-methyltransferase	Fundulus heteroclitus	0-27
19892394-1	2010	Glycine N-methyltransferase (GNMT) is a mediator in the methionine and folate cycles, and is responsible for the transfer of a methyl group from S-adenosylmethionine (SAM) to glycine forming S-adenosylhomocysteine (SAH) and sarcosine.	S-Adenosylmethionine	167-170	glycine N-methyltransferase	Fundulus heteroclitus	29-33
20027219-4	2009	To cause deprivation of vitamin B12, we have recently developed a cell model that produces decreased synthesis of S-adenosylmethionine by anchoring transcobalamin (TCII) to the reticulum through its fusion with Oleosin (OLEO).	S-Adenosylmethionine	114-134	transcobalamin 2	Rattus norvegicus	164-168
19843527-4	2009	Comparative analysis of the published CARM1 crystal structures reveals that the hydroxyl group of Ser(217) forms a strong hydrogen bond with the carbonyl oxygen atom of Tyr(154) to lock the cofactor S-adenosylmethionine inside the binding cavity.	S-Adenosylmethionine	201-219	coactivator associated arginine methyltransferase 1	Homo sapiens	38-43
19924280-3	2009	Here, we investigated whether periconceptional maternal folic acid use and markers of global DNA methylation potential (S-adenosylmethionine and S-adenosylhomocysteine blood levels) in mothers and children affect methylation of the insulin-like growth factor 2 gene differentially methylation region (IGF2 DMR) in the child.	S-Adenosylmethionine	120-140	insulin like growth factor 2	Homo sapiens	232-260
19924280-8	2009	IGF2 DMR methylation of the children also was associated with the S-adenosylmethionine blood level of the mother but not of the child (+1.7% methylation per SD S-adenosylmethionine; p = 0.037).	S-Adenosylmethionine	66-86	insulin like growth factor 2	Homo sapiens	0-4
19924280-8	2009	IGF2 DMR methylation of the children also was associated with the S-adenosylmethionine blood level of the mother but not of the child (+1.7% methylation per SD S-adenosylmethionine; p = 0.037).	S-Adenosylmethionine	66-86	WD repeat domain 20	Homo sapiens	5-8
19924280-8	2009	IGF2 DMR methylation of the children also was associated with the S-adenosylmethionine blood level of the mother but not of the child (+1.7% methylation per SD S-adenosylmethionine; p = 0.037).	S-Adenosylmethionine	160-180	insulin like growth factor 2	Homo sapiens	0-4
19924280-8	2009	IGF2 DMR methylation of the children also was associated with the S-adenosylmethionine blood level of the mother but not of the child (+1.7% methylation per SD S-adenosylmethionine; p = 0.037).	S-Adenosylmethionine	160-180	WD repeat domain 20	Homo sapiens	5-8
19082889-2	2009	MTHFR plays a central role in biotransformation of folate to form S-adenosylmethionine, the universal methyl donor in cells and affects DNA methylation status.	S-Adenosylmethionine	66-86	methylenetetrahydrofolate reductase	Homo sapiens	0-5
19620624-7	2009	The enzymatic function of MRDI was required for methionine salvage from S-adenosylmethionine but distinct from its function in cell invasion.	S-Adenosylmethionine	72-92	methylthioribose-1-phosphate isomerase 1	Homo sapiens	26-30
19497982-8	2009	Nuclear accumulation of the active enzyme only correlated with histone H3K27 trimethylation among the epigenetic modifications evaluated, therefore pointing to the necessity of methionine adenosyltransferase I/III to guarantee the supply of S-adenosylmethionine for specific methylations.	S-Adenosylmethionine	241-261	methionine adenosyltransferase 1A	Homo sapiens	177-213
19538983-3	2009	AS3MT catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to trivalent arsenicals, resulting in the production of methylated (MAs) and dimethylated arsenicals (DMAs).	S-Adenosylmethionine	52-75	arsenite methyltransferase	Homo sapiens	0-5
19565184-0	2009	S-adenosylmethionine and S-adenosylhomocysteine levels in the aging brain of APP/PS1 Alzheimer mice.	S-Adenosylmethionine	0-20	presenilin 1	Mus musculus	81-84
19565184-1	2009	Hyperhomocysteinemia and factors of homocysteine metabolism, S-adenosylhomocysteine (AdoHcy) and S-adenosylmethionine (AdoMet), may play a role in Alzheimer"s disease (AD).	S-Adenosylmethionine	97-117	methionine adenosyltransferase I, alpha	Mus musculus	119-125
19651420-1	2009	Putrescine N-methyltransferase (PMT) catalyses S-adenosylmethionine (SAM) dependent methylation of the diamine putrescine.	S-Adenosylmethionine	49-67	putrescine N-methyltransferase 3	Nicotiana tabacum	32-35
19651420-7	2009	PMT and spermidine synthase proteins share the same overall protein structure; they bind the same substrate putrescine and similar co-substrates, SAM and decarboxylated S-adenosylmethionine.	S-Adenosylmethionine	169-189	putrescine N-methyltransferase 3	Nicotiana tabacum	0-3
20198169-2	2009	To understand the pharmacogenetics of TPMT and 6MP, X-ray co-crystal structures of TPMT complexes with S-adenosyl-L-methionine (AdoMet) and 6MP are required.	S-Adenosylmethionine	103-126	thiopurine S-methyltransferase	Homo sapiens	83-87
20198169-2	2009	To understand the pharmacogenetics of TPMT and 6MP, X-ray co-crystal structures of TPMT complexes with S-adenosyl-L-methionine (AdoMet) and 6MP are required.	S-Adenosylmethionine	128-134	thiopurine S-methyltransferase	Homo sapiens	83-87
19483083-4	2009	It seems that the level of S-adenosylmethionine must be regulated in response to developmental stages and metabolic changes, and the enzyme glycine N-methyltransferase has been shown to play a major role in such regulation in mammals.	S-Adenosylmethionine	27-47	glycine N-methyltransferase	Homo sapiens	140-167
19344311-7	2009	Whereas the kinetic parameters of recombinant PfPRMT1 on an H4 peptide and S-adenosylmethionine were similar to those of mammalian PRMT1s, PfPRMT1 had much higher substrate-turnover rates.	S-Adenosylmethionine	75-95	protein arginine methyltransferase 1	Homo sapiens	48-53
19531479-6	2009	At equimolar concentrations of CBS and CSE, the simulations predict that H2S production by CBS would account for approximately 25-70% of the total H2S generated via the trans-sulfuration pathway depending on the extent of allosteric activation of CBS by S-adenosylmethionine.	S-Adenosylmethionine	254-274	cystathionine beta-synthase	Homo sapiens	31-34
19531479-6	2009	At equimolar concentrations of CBS and CSE, the simulations predict that H2S production by CBS would account for approximately 25-70% of the total H2S generated via the trans-sulfuration pathway depending on the extent of allosteric activation of CBS by S-adenosylmethionine.	S-Adenosylmethionine	254-274	cystathionine gamma-lyase	Homo sapiens	39-42
19531479-6	2009	At equimolar concentrations of CBS and CSE, the simulations predict that H2S production by CBS would account for approximately 25-70% of the total H2S generated via the trans-sulfuration pathway depending on the extent of allosteric activation of CBS by S-adenosylmethionine.	S-Adenosylmethionine	254-274	cystathionine beta-synthase	Homo sapiens	91-94
19531479-6	2009	At equimolar concentrations of CBS and CSE, the simulations predict that H2S production by CBS would account for approximately 25-70% of the total H2S generated via the trans-sulfuration pathway depending on the extent of allosteric activation of CBS by S-adenosylmethionine.	S-Adenosylmethionine	254-274	cystathionine beta-synthase	Homo sapiens	91-94
19582817-1	2009	UNLABELLED: Hepatic S-adenosylmethionine (SAMe) is maintained constant by the action of methionine adenosyltransferase I/III (MATI/III), which converts methionine into SAMe and glycine N-methyltransferase (GNMT), which eliminates excess SAMe to avoid aberrant methylation reactions.	S-Adenosylmethionine	20-40	glycine N-methyltransferase	Mus musculus	177-204
19582817-1	2009	UNLABELLED: Hepatic S-adenosylmethionine (SAMe) is maintained constant by the action of methionine adenosyltransferase I/III (MATI/III), which converts methionine into SAMe and glycine N-methyltransferase (GNMT), which eliminates excess SAMe to avoid aberrant methylation reactions.	S-Adenosylmethionine	20-40	glycine N-methyltransferase	Mus musculus	206-210
19636072-6	2009	The high dose of PCB and Mix reduced the abundance of the universal methyl donor S-adenosylmethionine, and Mix also reduced global genome DNA methylation (5-methyl-deoxycytidine/5-methyl-deoxycytidine + deoxycytidine).	S-Adenosylmethionine	81-101	pyruvate carboxylase	Homo sapiens	17-20
19372210-0	2009	S-Adenosylmethionine and methylthioadenosine inhibit cellular FLICE inhibitory protein expression and induce apoptosis in colon cancer cells.	S-Adenosylmethionine	0-20	caspase 8	Homo sapiens	62-67
19428339-0	2009	S-adenosylmethionine regulates thiopurine methyltransferase activity and decreases 6-mercaptopurine cytotoxicity in MOLT lymphoblasts.	S-Adenosylmethionine	0-20	thiopurine S-methyltransferase	Homo sapiens	31-59
19428339-3	2009	We propose a novel TPMT-mediated mechanism of S-adenosylmethionine (SAM)-specific effects on 6-mercaptopurine (6-MP) induced cytotoxicity in a model cell line for acute lymphoblastic leukemia (MOLT).	S-Adenosylmethionine	46-66	thiopurine S-methyltransferase	Homo sapiens	19-23
19428339-3	2009	We propose a novel TPMT-mediated mechanism of S-adenosylmethionine (SAM)-specific effects on 6-mercaptopurine (6-MP) induced cytotoxicity in a model cell line for acute lymphoblastic leukemia (MOLT).	S-Adenosylmethionine	68-71	thiopurine S-methyltransferase	Homo sapiens	19-23
19428339-7	2009	We further show that the addition of exogenous SAM to 6-MP treated cells maintains intracellular SAM levels, TPMT activity and protein levels, all of which are diminished in cells incubated with 6-MP.	S-Adenosylmethionine	47-50	thiopurine S-methyltransferase	Homo sapiens	109-113
19366698-1	2009	Phospholipid N-methyltransferase (PLMT) enzymes catalyze the S-adenosylmethionine-dependent methylation of ethanolamine-containing phospholipids to produce the abundant membrane lipid phosphatidylcholine (PtdCho).	S-Adenosylmethionine	63-81	phospholipid N-methyltransferase	Glycine max	0-32
19366698-1	2009	Phospholipid N-methyltransferase (PLMT) enzymes catalyze the S-adenosylmethionine-dependent methylation of ethanolamine-containing phospholipids to produce the abundant membrane lipid phosphatidylcholine (PtdCho).	S-Adenosylmethionine	63-81	phospholipid N-methyltransferase	Glycine max	34-38
19417133-4	2009	Here, we report that a quinoline-based compound, designated SGI-1027, inhibits the activity of DNMT1, DNMT3A, and DNMT3B as well M. SssI with comparable IC(50) (6-13 micromol/L) by competing with S-adenosylmethionine in the methylation reaction.	S-Adenosylmethionine	196-216	chromogranin B	Rattus norvegicus	60-63
19349371-6	2009	Interestingly, specific glutathione (GSH) up-regulation in hepatocytes by S-adenosylmethionine increased Mn-SOD expression and protected against I/R-mediated liver injury despite TNF/IL-1beta induction.	S-Adenosylmethionine	74-94	superoxide dismutase 2, mitochondrial	Mus musculus	105-111
19349371-6	2009	Interestingly, specific glutathione (GSH) up-regulation in hepatocytes by S-adenosylmethionine increased Mn-SOD expression and protected against I/R-mediated liver injury despite TNF/IL-1beta induction.	S-Adenosylmethionine	74-94	tumor necrosis factor	Mus musculus	179-182
19349371-6	2009	Interestingly, specific glutathione (GSH) up-regulation in hepatocytes by S-adenosylmethionine increased Mn-SOD expression and protected against I/R-mediated liver injury despite TNF/IL-1beta induction.	S-Adenosylmethionine	74-94	interleukin 1 beta	Mus musculus	183-191
19175412-1	2009	The DNA adenine methyltransferase (Dam methylase) of Gammaproteobacteria and the cell cycle-regulated methyltransferase (CcrM) methylase of Alphaproteobacteria catalyze an identical reaction (methylation of adenosine moieties using S-adenosyl-methionine as a methyl donor) at similar DNA targets (GATC and GANTC, respectively).	S-Adenosylmethionine	232-253	glutamyl-tRNA amidotransferase subunit C	Homo sapiens	297-301
19170661-4	2009	METHODS: In this study we estimated the flux of fatty acids (FA) through the stearoyl-CoA desaturase (SCD), phosphatidylethanolamine-N-methyltransferase (PEMT), and FA elongation pathways in relation to liver triacylglycerol (TG) content in Yucatan micropigs fed a 40% ethanol folate-deficient diet with or without supplementation with S-adenosyl methionine (SAM) compared with controls.	S-Adenosylmethionine	336-357	stearoyl-CoA desaturase	Sus scrofa	77-100
19159958-0	2009	Effects of selenium on the structure and function of recombinant human S-adenosyl-L-methionine dependent arsenic (+3 oxidation state) methyltransferase in E. coli.	S-Adenosylmethionine	73-94	arsenite methyltransferase	Homo sapiens	105-151
19287006-3	2009	TYW4 is an S-adenosylmethionine (SAM)-dependent enzyme that catalyzes the final step of yW biosynthesis, methylation and methoxycarbonylation.	S-Adenosylmethionine	11-31	tRNA methyltransferase PPM2	Saccharomyces cerevisiae S288C	0-4
19287006-3	2009	TYW4 is an S-adenosylmethionine (SAM)-dependent enzyme that catalyzes the final step of yW biosynthesis, methylation and methoxycarbonylation.	S-Adenosylmethionine	33-36	tRNA methyltransferase PPM2	Saccharomyces cerevisiae S288C	0-4
19279102-4	2009	AL2 and L2 interact with and inactivate adenosine kinase (ADK), which is required for efficient production of S-adenosyl methionine, an essential methyltransferase cofactor.	S-Adenosylmethionine	110-131	alfin-like 2	Arabidopsis thaliana	0-3
19279102-4	2009	AL2 and L2 interact with and inactivate adenosine kinase (ADK), which is required for efficient production of S-adenosyl methionine, an essential methyltransferase cofactor.	S-Adenosylmethionine	110-131	adenosine kinase	Homo sapiens	40-56
19279102-4	2009	AL2 and L2 interact with and inactivate adenosine kinase (ADK), which is required for efficient production of S-adenosyl methionine, an essential methyltransferase cofactor.	S-Adenosylmethionine	110-131	adenosine kinase	Homo sapiens	58-61
19170661-4	2009	METHODS: In this study we estimated the flux of fatty acids (FA) through the stearoyl-CoA desaturase (SCD), phosphatidylethanolamine-N-methyltransferase (PEMT), and FA elongation pathways in relation to liver triacylglycerol (TG) content in Yucatan micropigs fed a 40% ethanol folate-deficient diet with or without supplementation with S-adenosyl methionine (SAM) compared with controls.	S-Adenosylmethionine	336-357	stearoyl-CoA desaturase	Sus scrofa	102-105
19170661-4	2009	METHODS: In this study we estimated the flux of fatty acids (FA) through the stearoyl-CoA desaturase (SCD), phosphatidylethanolamine-N-methyltransferase (PEMT), and FA elongation pathways in relation to liver triacylglycerol (TG) content in Yucatan micropigs fed a 40% ethanol folate-deficient diet with or without supplementation with S-adenosyl methionine (SAM) compared with controls.	S-Adenosylmethionine	336-357	phosphatidylethanolamine N-methyltransferase	Sus scrofa	154-158
19170661-4	2009	METHODS: In this study we estimated the flux of fatty acids (FA) through the stearoyl-CoA desaturase (SCD), phosphatidylethanolamine-N-methyltransferase (PEMT), and FA elongation pathways in relation to liver triacylglycerol (TG) content in Yucatan micropigs fed a 40% ethanol folate-deficient diet with or without supplementation with S-adenosyl methionine (SAM) compared with controls.	S-Adenosylmethionine	359-362	stearoyl-CoA desaturase	Sus scrofa	77-100
19170661-4	2009	METHODS: In this study we estimated the flux of fatty acids (FA) through the stearoyl-CoA desaturase (SCD), phosphatidylethanolamine-N-methyltransferase (PEMT), and FA elongation pathways in relation to liver triacylglycerol (TG) content in Yucatan micropigs fed a 40% ethanol folate-deficient diet with or without supplementation with S-adenosyl methionine (SAM) compared with controls.	S-Adenosylmethionine	359-362	stearoyl-CoA desaturase	Sus scrofa	102-105
19170661-4	2009	METHODS: In this study we estimated the flux of fatty acids (FA) through the stearoyl-CoA desaturase (SCD), phosphatidylethanolamine-N-methyltransferase (PEMT), and FA elongation pathways in relation to liver triacylglycerol (TG) content in Yucatan micropigs fed a 40% ethanol folate-deficient diet with or without supplementation with S-adenosyl methionine (SAM) compared with controls.	S-Adenosylmethionine	359-362	phosphatidylethanolamine N-methyltransferase	Sus scrofa	154-158
19088160-0	2009	Effects of insulin and glucose on cellular metabolic fluxes in homocysteine transsulfuration, remethylation, S-adenosylmethionine synthesis, and global deoxyribonucleic acid methylation.	S-Adenosylmethionine	109-129	insulin	Homo sapiens	11-18
19270382-8	2009	In addition, a recessive mutant gene, sah1-1, that is known to overproduce S-adenosylmethionine, was introduced into the diploid sake strain by the replacement of one wild-type allele and subsequent disruption of the other.	S-Adenosylmethionine	75-95	adenosylhomocysteinase	Saccharomyces cerevisiae S288C	38-44
19270382-9	2009	The resulting sah1-1/sah1Delta::URA3 strain produced higher amounts of S-adenosylmethionine than the wild type.	S-Adenosylmethionine	71-91	adenosylhomocysteinase	Saccharomyces cerevisiae S288C	14-20
19270382-9	2009	The resulting sah1-1/sah1Delta::URA3 strain produced higher amounts of S-adenosylmethionine than the wild type.	S-Adenosylmethionine	71-91	orotidine-5'-phosphate decarboxylase	Saccharomyces cerevisiae S288C	32-36
19146867-10	2009	Automated docking experiments showed that AFB(1) binds to the S-adenosylmethionine binding domain of GNMT.	S-Adenosylmethionine	62-82	glycine N-methyltransferase	Mus musculus	101-105
19048023-1	2009	Methionine adenosyltransferase II (MAT II) is a key enzyme in cellular metabolism and catalyzes the formation of S-adenosylmethionine (SAMe) from L-methionine and ATP.	S-Adenosylmethionine	113-133	methionine adenosyltransferase 2A	Homo sapiens	0-33
19048023-1	2009	Methionine adenosyltransferase II (MAT II) is a key enzyme in cellular metabolism and catalyzes the formation of S-adenosylmethionine (SAMe) from L-methionine and ATP.	S-Adenosylmethionine	113-133	methionine adenosyltransferase 2A	Homo sapiens	35-41
18983843-0	2009	S-adenosylmethionine regulates apurinic/apyrimidinic endonuclease 1 stability: implication in hepatocarcinogenesis.	S-Adenosylmethionine	0-20	apurinic/apyrimidinic endonuclease 1	Mus musculus	31-67
18983843-3	2009	Mice deficient in methionine adenosyltransferase 1a (Mat1a KO) have chronic hepatic deficiency of S-adenosylmethionine (SAMe) and increased oxidative stress, and develop HCC.	S-Adenosylmethionine	98-118	methionine adenosyltransferase I, alpha	Mus musculus	53-58
19201949-3	2009	Reduced Ahcy activity in dtp mutants led to elevated levels of S-adenosylhomocysteine (SAH) and, to a lesser degree, of its metabolic precursor S-adenosylmethionine (SAM).	S-Adenosylmethionine	144-164	adenosylhomocysteinase	Homo sapiens	8-12
19201949-3	2009	Reduced Ahcy activity in dtp mutants led to elevated levels of S-adenosylhomocysteine (SAH) and, to a lesser degree, of its metabolic precursor S-adenosylmethionine (SAM).	S-Adenosylmethionine	166-169	adenosylhomocysteinase	Homo sapiens	8-12
19177591-0	2009	Evidence for LKB1/AMP-activated protein kinase/ endothelial nitric oxide synthase cascade regulated by hepatocyte growth factor, S-adenosylmethionine, and nitric oxide in hepatocyte proliferation.	S-Adenosylmethionine	129-149	serine/threonine kinase 11	Mus musculus	13-17
19111934-1	2009	Catechol-O-methyltransferase (COMT, EC 2.1.1.6) is a monomeric enzyme that catalyzes the transfer of a methyl group from S-adenosyl-l-methionine (AdoMet) to the phenolic oxygen of substituted catechols.	S-Adenosylmethionine	146-152	catechol-O-methyltransferase	Rattus norvegicus	0-28
19111934-1	2009	Catechol-O-methyltransferase (COMT, EC 2.1.1.6) is a monomeric enzyme that catalyzes the transfer of a methyl group from S-adenosyl-l-methionine (AdoMet) to the phenolic oxygen of substituted catechols.	S-Adenosylmethionine	146-152	catechol-O-methyltransferase	Rattus norvegicus	30-34
19111934-1	2009	Catechol-O-methyltransferase (COMT, EC 2.1.1.6) is a monomeric enzyme that catalyzes the transfer of a methyl group from S-adenosyl-l-methionine (AdoMet) to the phenolic oxygen of substituted catechols.	S-Adenosylmethionine	146-152	methionine adenosyltransferase 1A	Rattus norvegicus	121-144
19035462-2	2009	Glycine N-methyltransferase (GNMT) participates in one-carbon metabolism and affects DNA methylation by regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine.	S-Adenosylmethionine	128-148	glycine N-methyltransferase	Mus musculus	0-27
19035462-2	2009	Glycine N-methyltransferase (GNMT) participates in one-carbon metabolism and affects DNA methylation by regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine.	S-Adenosylmethionine	128-148	glycine N-methyltransferase	Mus musculus	29-33
21475826-2	2009	Methylenetetrahydrofolate reductase (MTHFR) regulates DNA methylation by affecting synthesis of S-adenosylmethionine, which is a universal methyl donor for methylation reactions.	S-Adenosylmethionine	96-116	methylenetetrahydrofolate reductase	Homo sapiens	0-35
21475826-2	2009	Methylenetetrahydrofolate reductase (MTHFR) regulates DNA methylation by affecting synthesis of S-adenosylmethionine, which is a universal methyl donor for methylation reactions.	S-Adenosylmethionine	96-116	methylenetetrahydrofolate reductase	Homo sapiens	37-42
19178276-3	2009	SPL is a member of the radical AdoMet superfamily of enzymes, and utilizes an iron-sulfur cluster and S-adenosylmethionine to repair SP by a direct reversal mechanism initiated by H atom abstraction from C-6 of the thymine dimer.	S-Adenosylmethionine	102-122	sphingosine-1-phosphate lyase 1	Homo sapiens	0-3
19177591-0	2009	Evidence for LKB1/AMP-activated protein kinase/ endothelial nitric oxide synthase cascade regulated by hepatocyte growth factor, S-adenosylmethionine, and nitric oxide in hepatocyte proliferation.	S-Adenosylmethionine	129-149	nitric oxide synthase 3, endothelial cell	Mus musculus	48-81
19098360-0	2008	Folate and S-adenosylmethionine modulate synaptic activity in cultured cortical neurons: acute differential impact on normal and apolipoprotein-deficient mice.	S-Adenosylmethionine	11-31	apolipoprotein E	Mus musculus	129-143
18824331-4	2009	We have therefore investigated the efficacy of SAM-e in managing schizophrenia symptomatology in patients with the low activity COMT polymorphism.	S-Adenosylmethionine	47-52	catechol-O-methyltransferase	Homo sapiens	128-132
19077667-1	2009	Human catechol-O-methyltransferase (COMT; EC 2.1.1.6) catalyzes the transfer of the methyl group to a variety of endogenous and exogenous catechol substrates using S-adenosyl-L-methionine as the methyl donor.	S-Adenosylmethionine	164-187	catechol-O-methyltransferase	Homo sapiens	6-34
19077667-1	2009	Human catechol-O-methyltransferase (COMT; EC 2.1.1.6) catalyzes the transfer of the methyl group to a variety of endogenous and exogenous catechol substrates using S-adenosyl-L-methionine as the methyl donor.	S-Adenosylmethionine	164-187	catechol-O-methyltransferase	Homo sapiens	36-40
19033438-4	2009	Mthfd1gt/+ mice demonstrated lower hepatic adenosylmethionine levels, which is consistent with formate serving as a source of 1Cs for cellular methylation reactions.	S-Adenosylmethionine	43-61	methylenetetrahydrofolate dehydrogenase (NADP+ dependent), methenyltetrahydrofolate cyclohydrolase, formyltetrahydrofolate synthase	Mus musculus	0-6
19276539-1	2009	Very recent findings confirmed that S-adenosylmethionine (SAM) can exert a direct effect on glutathione S-transferase (GST) activity.	S-Adenosylmethionine	36-56	glutathione S-transferase kappa 1	Homo sapiens	92-117
19276539-1	2009	Very recent findings confirmed that S-adenosylmethionine (SAM) can exert a direct effect on glutathione S-transferase (GST) activity.	S-Adenosylmethionine	36-56	glutathione S-transferase kappa 1	Homo sapiens	119-122
19276539-1	2009	Very recent findings confirmed that S-adenosylmethionine (SAM) can exert a direct effect on glutathione S-transferase (GST) activity.	S-Adenosylmethionine	58-61	glutathione S-transferase kappa 1	Homo sapiens	92-117
19276539-1	2009	Very recent findings confirmed that S-adenosylmethionine (SAM) can exert a direct effect on glutathione S-transferase (GST) activity.	S-Adenosylmethionine	58-61	glutathione S-transferase kappa 1	Homo sapiens	119-122
19020775-1	2008	Human catechol-O-methyltransferase (COMT, EC 2.1.1.6) catalyzes the transfer of the methyl group to a variety of endogenous and exogenous catechol substrates using S-adenosyl-L-methionine as the methyl donor.	S-Adenosylmethionine	164-187	catechol-O-methyltransferase	Homo sapiens	6-34
18849566-5	2008	Purification of recombinant CBS enzyme expressed in the presence of various metalloporphyrins confirmed that Mn(III) and Co(III) had 30-60% of the specific activity of Fe(III)-CBS, and still responded to allosteric activation by S-adenosyl-L-methionine.	S-Adenosylmethionine	229-252	cystathionine beta-synthase	Homo sapiens	28-31
18849566-5	2008	Purification of recombinant CBS enzyme expressed in the presence of various metalloporphyrins confirmed that Mn(III) and Co(III) had 30-60% of the specific activity of Fe(III)-CBS, and still responded to allosteric activation by S-adenosyl-L-methionine.	S-Adenosylmethionine	229-252	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	112-115
18849566-5	2008	Purification of recombinant CBS enzyme expressed in the presence of various metalloporphyrins confirmed that Mn(III) and Co(III) had 30-60% of the specific activity of Fe(III)-CBS, and still responded to allosteric activation by S-adenosyl-L-methionine.	S-Adenosylmethionine	229-252	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	121-128
18849566-5	2008	Purification of recombinant CBS enzyme expressed in the presence of various metalloporphyrins confirmed that Mn(III) and Co(III) had 30-60% of the specific activity of Fe(III)-CBS, and still responded to allosteric activation by S-adenosyl-L-methionine.	S-Adenosylmethionine	229-252	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	124-127
19020775-1	2008	Human catechol-O-methyltransferase (COMT, EC 2.1.1.6) catalyzes the transfer of the methyl group to a variety of endogenous and exogenous catechol substrates using S-adenosyl-L-methionine as the methyl donor.	S-Adenosylmethionine	164-187	catechol-O-methyltransferase	Homo sapiens	36-40
19020775-5	2008	Kinetic analysis showed that these new COMT variants had essentially the same kinetic characteristics and catalytic activity as the wild-type COMTs for the O-methylation of 2-hydroxyestradiol and 4-hydroxyestradiol in vitro, but they have asignificantly reduced thermostability at 37 degrees C. In addition, the mutant enzymes have different binding affinities for S-adenosyl-L-methionine compared with the wild-type COMTs.	S-Adenosylmethionine	365-388	catechol-O-methyltransferase	Homo sapiens	39-43
19017745-5	2008	The expansion defect in fei1 fei2 roots was suppressed by inhibition of 1-aminocyclopropane-1-carboxylic acid (ACC) synthase, an enzyme that converts Ado-Met to ACC in ethylene biosynthesis, but not by disruption of the ethylene response pathway.	S-Adenosylmethionine	150-157	Leucine-rich repeat protein kinase family protein	Arabidopsis thaliana	24-28
18815415-1	2008	S-adenosylhomocysteine hydrolase (SAHH) is a ubiquitous enzyme that plays a central role in methylation-based processes by maintaining the intracellular balance between S-adenosylhomocysteine (SAH) and S-adenosylmethionine.	S-Adenosylmethionine	202-222	adenosylhomocysteinase	Homo sapiens	34-38
19017745-5	2008	The expansion defect in fei1 fei2 roots was suppressed by inhibition of 1-aminocyclopropane-1-carboxylic acid (ACC) synthase, an enzyme that converts Ado-Met to ACC in ethylene biosynthesis, but not by disruption of the ethylene response pathway.	S-Adenosylmethionine	150-157	Leucine-rich repeat protein kinase family protein	Arabidopsis thaliana	29-33
18708030-3	2008	TPMT, like DNA methyltransferases (DNMTs), transfers methyl groups from S-adenosylmethionine (SAM) and generates S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	72-92	thiopurine S-methyltransferase	Homo sapiens	0-4
18721845-7	2008	Treatment with antioxidants such as vitamin C or S-adenosyl-l-methionine (SAM) or an inhibitor of iNOS prevented the pyrazole-induced oxidative liver damage, thus validating the role of oxidative/nitrosative stress in the pyrazole induced liver injury to the Nrf2 knockout mice.	S-Adenosylmethionine	49-72	nuclear factor, erythroid derived 2, like 2	Mus musculus	259-263
18708030-3	2008	TPMT, like DNA methyltransferases (DNMTs), transfers methyl groups from S-adenosylmethionine (SAM) and generates S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	94-97	thiopurine S-methyltransferase	Homo sapiens	0-4
18755835-8	2008	Phylogenetically, ybeA and its homologs are grouped with other putative S-adenosylmethionine-dependent, SPOUT methyltransferase genes in the Cluster of Orthologous Genes COG1576; ybeA is the first member to be functionally characterized.	S-Adenosylmethionine	74-92	hypothetical protein	Escherichia coli	18-22
18695670-2	2008	Lipopolysaccharide (LPS) was shown to inactivate hepatic methionine adenosyltransferase (MAT), the enzyme responsible for S-adenosylmethionine (SAMe) biosynthesis.	S-Adenosylmethionine	122-142	methionine adenosyltransferase I, alpha	Mus musculus	57-87
18695670-2	2008	Lipopolysaccharide (LPS) was shown to inactivate hepatic methionine adenosyltransferase (MAT), the enzyme responsible for S-adenosylmethionine (SAMe) biosynthesis.	S-Adenosylmethionine	122-142	methionine adenosyltransferase I, alpha	Mus musculus	89-92
18755835-8	2008	Phylogenetically, ybeA and its homologs are grouped with other putative S-adenosylmethionine-dependent, SPOUT methyltransferase genes in the Cluster of Orthologous Genes COG1576; ybeA is the first member to be functionally characterized.	S-Adenosylmethionine	74-92	hypothetical protein	Escherichia coli	179-183
18803868-5	2008	This is important, since it is now well recognized that LuxS also holds a central role as a metabolic enzyme in the activated methyl cycle which is responsible for the generation of S-adenosyl-L-methionine, the major methyl donor in the cell.	S-Adenosylmethionine	182-205	Lutheran suppressor, X-linked	Homo sapiens	56-60
18698489-4	2008	In the present study, we determined that EWS was physically associated with PRMT8, the novel eighth member of the PRMT family, through the COOH-terminal region of EWS including RGG3 with the NH2-terminal region of PRMT8 encompassing the S-adenosyl-L-methionine binding domain, and that arginine residues in EWS were asymmetrically dimethylated by PRMT8 using amino acid analysis with thin-layer chromatography.	S-Adenosylmethionine	239-260	EWS RNA binding protein 1	Homo sapiens	41-44
18698489-4	2008	In the present study, we determined that EWS was physically associated with PRMT8, the novel eighth member of the PRMT family, through the COOH-terminal region of EWS including RGG3 with the NH2-terminal region of PRMT8 encompassing the S-adenosyl-L-methionine binding domain, and that arginine residues in EWS were asymmetrically dimethylated by PRMT8 using amino acid analysis with thin-layer chromatography.	S-Adenosylmethionine	239-260	protein arginine methyltransferase 8	Homo sapiens	76-81
18698489-4	2008	In the present study, we determined that EWS was physically associated with PRMT8, the novel eighth member of the PRMT family, through the COOH-terminal region of EWS including RGG3 with the NH2-terminal region of PRMT8 encompassing the S-adenosyl-L-methionine binding domain, and that arginine residues in EWS were asymmetrically dimethylated by PRMT8 using amino acid analysis with thin-layer chromatography.	S-Adenosylmethionine	239-260	EWS RNA binding protein 1	Homo sapiens	163-166
18698489-4	2008	In the present study, we determined that EWS was physically associated with PRMT8, the novel eighth member of the PRMT family, through the COOH-terminal region of EWS including RGG3 with the NH2-terminal region of PRMT8 encompassing the S-adenosyl-L-methionine binding domain, and that arginine residues in EWS were asymmetrically dimethylated by PRMT8 using amino acid analysis with thin-layer chromatography.	S-Adenosylmethionine	239-260	protein arginine methyltransferase 8	Homo sapiens	214-219
18698489-4	2008	In the present study, we determined that EWS was physically associated with PRMT8, the novel eighth member of the PRMT family, through the COOH-terminal region of EWS including RGG3 with the NH2-terminal region of PRMT8 encompassing the S-adenosyl-L-methionine binding domain, and that arginine residues in EWS were asymmetrically dimethylated by PRMT8 using amino acid analysis with thin-layer chromatography.	S-Adenosylmethionine	239-260	EWS RNA binding protein 1	Homo sapiens	163-166
18698489-4	2008	In the present study, we determined that EWS was physically associated with PRMT8, the novel eighth member of the PRMT family, through the COOH-terminal region of EWS including RGG3 with the NH2-terminal region of PRMT8 encompassing the S-adenosyl-L-methionine binding domain, and that arginine residues in EWS were asymmetrically dimethylated by PRMT8 using amino acid analysis with thin-layer chromatography.	S-Adenosylmethionine	239-260	protein arginine methyltransferase 8	Homo sapiens	214-219
19017057-1	2008	S-adenosylmethionine is one of the most important metabolites in living cells and is synthesized in a single reaction catalyzed by methionine adenosyltransferase (MAT).	S-Adenosylmethionine	0-20	methionine adenosyltransferase 1A	Homo sapiens	131-161
19017057-1	2008	S-adenosylmethionine is one of the most important metabolites in living cells and is synthesized in a single reaction catalyzed by methionine adenosyltransferase (MAT).	S-Adenosylmethionine	0-20	methionine adenosyltransferase 1A	Homo sapiens	163-166
18591246-1	2008	In eukaryotes, S-adenosyl-L-homocysteine hydrolase (Sah1) offers a single way for degradation of S-adenosyl-L-homocysteine, a product and potent competitive inhibitor of S-adenosyl-L-methionine (AdoMet)-dependent methyltransferases.	S-Adenosylmethionine	170-193	adenosylhomocysteinase	Saccharomyces cerevisiae S288C	52-56
18596098-3	2008	These related proteins can suppress silencing by multiple mechanisms, one of which involves interacting with and inhibiting adenosine kinase (ADK), a cellular enzyme associated with the methyl cycle that generates S-adenosyl-methionine, an essential methyltransferase cofactor.	S-Adenosylmethionine	214-235	adenosine kinase	Homo sapiens	142-145
18596098-3	2008	These related proteins can suppress silencing by multiple mechanisms, one of which involves interacting with and inhibiting adenosine kinase (ADK), a cellular enzyme associated with the methyl cycle that generates S-adenosyl-methionine, an essential methyltransferase cofactor.	S-Adenosylmethionine	214-235	adenosine kinase	Homo sapiens	124-140
18591246-1	2008	In eukaryotes, S-adenosyl-L-homocysteine hydrolase (Sah1) offers a single way for degradation of S-adenosyl-L-homocysteine, a product and potent competitive inhibitor of S-adenosyl-L-methionine (AdoMet)-dependent methyltransferases.	S-Adenosylmethionine	195-201	adenosylhomocysteinase	Saccharomyces cerevisiae S288C	52-56
18678947-1	2008	Transfer RNA (tRNA) (m(7)G46) methyltransferase (TrmB) belongs to the Rossmann-fold methyltransferase (RFM) family and uses S-adenosyl-L-methionine (SAM) as the methyl-group donor to catalyze the formation of N(7)-methylguanosine (m(7)G) at position 46 in the variable loop of tRNAs.	S-Adenosylmethionine	124-147	methyltransferase 1, tRNA methylguanosine	Homo sapiens	0-47
18655704-1	2008	The yeast SCFMet30 ubiquitin ligase plays a critical role in cell division by regulating the Met4 transcriptional activator of genes that control the uptake and assimilation of sulfur into methionine and S-adenosyl-methionine.	S-Adenosylmethionine	204-225	Met4p	Saccharomyces cerevisiae S288C	93-97
18474266-4	2008	COMT contains two tryptophan residues, W143 and W38Y, which are located in loops that border the S-adenosylmethionine (SAM) and catechol binding sites.	S-Adenosylmethionine	97-117	catechol-O-methyltransferase	Homo sapiens	0-4
18469001-2	2008	Seventeen mutations were introduced into the dengue virus type 2 NS5 methyltransferase domain, targeting amino acids either predicted to be directly involved in S-adenosyl-l-methionine binding or important for NS5 conformation and/or charged interactions.	S-Adenosylmethionine	163-184	Raf-1 proto-oncogene, serine/threonine kinase	Homo sapiens	65-68
18487201-4	2008	A marked suppression of S-adenosylmethionine (SAM) levels occurred with decreased methionine adenosyltransferase 2A (converts methionine to SAM) expression and increased negative regulator methionine adenosyltransferase B, suggesting reduced conversion of Hcy to SAM.	S-Adenosylmethionine	24-44	methionine adenosyltransferase 2A	Homo sapiens	82-115
18487201-4	2008	A marked suppression of S-adenosylmethionine (SAM) levels occurred with decreased methionine adenosyltransferase 2A (converts methionine to SAM) expression and increased negative regulator methionine adenosyltransferase B, suggesting reduced conversion of Hcy to SAM.	S-Adenosylmethionine	46-49	methionine adenosyltransferase 2A	Homo sapiens	82-115
18474266-4	2008	COMT contains two tryptophan residues, W143 and W38Y, which are located in loops that border the S-adenosylmethionine (SAM) and catechol binding sites.	S-Adenosylmethionine	119-122	catechol-O-methyltransferase	Homo sapiens	0-4
18435763-2	2008	As a final step of juvenile hormone biosynthesis, juvenile hormone acid O-methyltransferase (JHAMT) transfers the methyl group from S-adenosyl-l-methionine to the carboxyl group of farnesoic acid and juvenile hormone acid.	S-Adenosylmethionine	132-155	Juvenile hormone acid O-methyltransferase-like	Tribolium castaneum	50-91
18599958-0	2008	S-adenosylmethionine mediates glutathione efficacy by increasing glutathione S-transferase activity: implications for S-adenosyl methionine as a neuroprotective dietary supplement.	S-Adenosylmethionine	0-20	hematopoietic prostaglandin D synthase	Mus musculus	65-90
18599958-0	2008	S-adenosylmethionine mediates glutathione efficacy by increasing glutathione S-transferase activity: implications for S-adenosyl methionine as a neuroprotective dietary supplement.	S-Adenosylmethionine	118-139	hematopoietic prostaglandin D synthase	Mus musculus	65-90
18414994-0	2008	A decrease in S-adenosyl-L-methionine potentiates arachidonic acid cytotoxicity in primary rat hepatocytes enriched in CYP2E1.	S-Adenosylmethionine	14-37	cytochrome P450, family 2, subfamily e, polypeptide 1	Rattus norvegicus	119-125
18484748-1	2008	Thiopurine S-methyltransferase (TPMT) modulates the cytotoxic effects of thiopurine prodrugs such as 6-mercaptopurine by methylating them in a reaction using S-adenosyl- l-methionine as the donor.	S-Adenosylmethionine	158-182	thiopurine S-methyltransferase	Homo sapiens	0-30
18484748-1	2008	Thiopurine S-methyltransferase (TPMT) modulates the cytotoxic effects of thiopurine prodrugs such as 6-mercaptopurine by methylating them in a reaction using S-adenosyl- l-methionine as the donor.	S-Adenosylmethionine	158-182	thiopurine S-methyltransferase	Homo sapiens	32-36
18484748-8	2008	Substitution of Arg152 (Arg147 in murine TPMT) with glutamic acid decreases V max and increases K m for 6-mercaptopurine but not K m for S-adenosyl- l-methionine.	S-Adenosylmethionine	137-161	thiopurine methyltransferase	Mus musculus	41-45
18549957-1	2008	Juvenile hormone (JH) acid O-methyltransferase (JHAMT) is the enzyme that transfers a methyl group from S-adenosyl-l-methionine (SAM) to the carboxyl group of JH acids to produce active JHs in the corpora allata.	S-Adenosylmethionine	104-127	juvenile hormone acid methyltransferase	Drosophila melanogaster	48-53
18486144-6	2008	Here we describe the crystal structures of the 108V and 108M variants of the soluble form of human COMT bound with S-adenosylmethionine (SAM) and a substrate analog, 3,5-dinitrocatechol.	S-Adenosylmethionine	115-135	catechol-O-methyltransferase	Homo sapiens	99-103
18486144-6	2008	Here we describe the crystal structures of the 108V and 108M variants of the soluble form of human COMT bound with S-adenosylmethionine (SAM) and a substrate analog, 3,5-dinitrocatechol.	S-Adenosylmethionine	137-140	catechol-O-methyltransferase	Homo sapiens	99-103
18435763-2	2008	As a final step of juvenile hormone biosynthesis, juvenile hormone acid O-methyltransferase (JHAMT) transfers the methyl group from S-adenosyl-l-methionine to the carboxyl group of farnesoic acid and juvenile hormone acid.	S-Adenosylmethionine	132-155	Juvenile hormone acid O-methyltransferase-like	Tribolium castaneum	93-98
19787085-1	2008	S-adenosylmethionine decarboxylase (SAMDC) is an enzyme which converts S-adenosylmethione (SAM), a methyl donor, to decarboxylated SAM (dcSAM), an aminopropyl donor for polyamine biosynthesis.	S-Adenosylmethionine	71-89	adenosylmethionine decarboxylase 1	Homo sapiens	0-34
17869084-3	2008	It has been demonstrated that the formation of S-adenosylmethionine (SAMe) catalyzed by methionine adenosyltransferase (MAT) II is essential for CD4(+) T-cell activation and proliferation.	S-Adenosylmethionine	47-67	methionine adenosyltransferase 2A	Homo sapiens	88-127
17869084-3	2008	It has been demonstrated that the formation of S-adenosylmethionine (SAMe) catalyzed by methionine adenosyltransferase (MAT) II is essential for CD4(+) T-cell activation and proliferation.	S-Adenosylmethionine	47-67	CD4 molecule	Homo sapiens	145-148
19787085-1	2008	S-adenosylmethionine decarboxylase (SAMDC) is an enzyme which converts S-adenosylmethione (SAM), a methyl donor, to decarboxylated SAM (dcSAM), an aminopropyl donor for polyamine biosynthesis.	S-Adenosylmethionine	71-89	adenosylmethionine decarboxylase 1	Homo sapiens	36-41
19787085-1	2008	S-adenosylmethionine decarboxylase (SAMDC) is an enzyme which converts S-adenosylmethione (SAM), a methyl donor, to decarboxylated SAM (dcSAM), an aminopropyl donor for polyamine biosynthesis.	S-Adenosylmethionine	36-39	adenosylmethionine decarboxylase 1	Homo sapiens	0-34
18393372-1	2008	UNLABELLED: We previously showed that S-adenosylmethionine (SAMe) and its metabolite methylthioadenosine (MTA) blocked lipopolysaccharide (LPS)-induced tumor necrosis factor alpha (TNFalpha) expression in RAW (murine macrophage cell line) and Kupffer cells at the transcriptional level without affecting nuclear factor kappa B nuclear binding.	S-Adenosylmethionine	38-58	tumor necrosis factor	Mus musculus	181-189
18452426-2	2008	The QS molecules C4-HSL and C12-oxo-HSL are synthesized from the universal precursor S-adenosyl methionine, which is also a precursor of polyamines in human cells.	S-Adenosylmethionine	85-106	lipase E, hormone sensitive type	Homo sapiens	20-23
18452426-2	2008	The QS molecules C4-HSL and C12-oxo-HSL are synthesized from the universal precursor S-adenosyl methionine, which is also a precursor of polyamines in human cells.	S-Adenosylmethionine	85-106	lipase E, hormone sensitive type	Homo sapiens	36-39
18393372-1	2008	UNLABELLED: We previously showed that S-adenosylmethionine (SAMe) and its metabolite methylthioadenosine (MTA) blocked lipopolysaccharide (LPS)-induced tumor necrosis factor alpha (TNFalpha) expression in RAW (murine macrophage cell line) and Kupffer cells at the transcriptional level without affecting nuclear factor kappa B nuclear binding.	S-Adenosylmethionine	38-58	tumor necrosis factor	Mus musculus	152-179
18275848-0	2008	Heme oxygenase-1 is a novel target and antioxidant mediator of S-adenosylmethionine.	S-Adenosylmethionine	63-83	heme oxygenase 1	Homo sapiens	0-16
18318442-1	2008	UNLABELLED: Glycine N-methyltransferase (GNMT) is the main enzyme responsible for catabolism of excess hepatic S-adenosylmethionine (SAMe).	S-Adenosylmethionine	111-131	glycine N-methyltransferase	Mus musculus	12-39
18230605-6	2008	Methionine is a stronger inhibitor of BHMT-2 than BHMT, and S-adenosylmethionine does not inhibit BHMT but is a weak inhibitor of BHMT-2.	S-Adenosylmethionine	60-80	betaine--homocysteine S-methyltransferase 2	Homo sapiens	130-136
18404532-0	2008	The differential NF-kB modulation by S-adenosyl-L-methionine, N-acetylcysteine and quercetin on the promotion stage of chemical hepatocarcinogenesis.	S-Adenosylmethionine	37-60	RELA proto-oncogene, NF-kB subunit	Rattus norvegicus	17-22
18263580-1	2008	Human protein arginine N-methyltransferase 6 (PRMT6) transfers methyl groups from the co-substrate S-adenosyl-L-methionine to arginine residues within proteins, forming S-adenosyl-L-homocysteine as well as omega-N(G)-monomethylarginine (MMA) and asymmetric dimethylarginine (aDMA) residues in the process.	S-Adenosylmethionine	99-122	protein arginine methyltransferase 6	Homo sapiens	6-44
18263580-1	2008	Human protein arginine N-methyltransferase 6 (PRMT6) transfers methyl groups from the co-substrate S-adenosyl-L-methionine to arginine residues within proteins, forming S-adenosyl-L-homocysteine as well as omega-N(G)-monomethylarginine (MMA) and asymmetric dimethylarginine (aDMA) residues in the process.	S-Adenosylmethionine	99-122	protein arginine methyltransferase 6	Homo sapiens	46-51
18263580-3	2008	We find that PRMT6 follows an ordered sequential mechanism in which S-adenosyl-L-methionine binds to the enzyme first and the methylated product is the first to dissociate.	S-Adenosylmethionine	68-91	protein arginine methyltransferase 6	Homo sapiens	13-18
18318442-1	2008	UNLABELLED: Glycine N-methyltransferase (GNMT) is the main enzyme responsible for catabolism of excess hepatic S-adenosylmethionine (SAMe).	S-Adenosylmethionine	111-131	glycine N-methyltransferase	Mus musculus	41-45
18184691-1	2008	Expression of the Arabidopsis CGS1 gene that codes for cystathionine gamma-synthase is feedback-regulated at the step of mRNA degradation in response to S-adenosyl-L-methionine (AdoMet).	S-Adenosylmethionine	153-176	Pyridoxal phosphate (PLP)-dependent transferases superfamily protein	Arabidopsis thaliana	30-34
18285355-2	2008	Expression of CGS1 is feedback-regulated at the step of mRNA degradation in response to S-adenosyl-L-methionine (AdoMet).	S-Adenosylmethionine	88-111	Pyridoxal phosphate (PLP)-dependent transferases superfamily protein	Arabidopsis thaliana	14-18
18285355-2	2008	Expression of CGS1 is feedback-regulated at the step of mRNA degradation in response to S-adenosyl-L-methionine (AdoMet).	S-Adenosylmethionine	113-119	Pyridoxal phosphate (PLP)-dependent transferases superfamily protein	Arabidopsis thaliana	14-18
18201837-10	2008	Infusion of the CBS activator, s-adenosyl-L-methionine (0.1 mM and 1 mM), likewise decreased MAP.	S-Adenosylmethionine	31-54	cystathionine beta synthase	Rattus norvegicus	16-19
18208838-3	2008	In Saccharomyces cerevisiae the malfunction of a temperature-sensitive Nep1 protein (nep1-1(ts)) was suppressed by the addition of S-adenosylmethionine (SAM).	S-Adenosylmethionine	131-151	18S rRNA pseudouridine methyltransferase	Saccharomyces cerevisiae S288C	71-75
18208838-3	2008	In Saccharomyces cerevisiae the malfunction of a temperature-sensitive Nep1 protein (nep1-1(ts)) was suppressed by the addition of S-adenosylmethionine (SAM).	S-Adenosylmethionine	131-151	18S rRNA pseudouridine methyltransferase	Saccharomyces cerevisiae S288C	85-89
18208838-3	2008	In Saccharomyces cerevisiae the malfunction of a temperature-sensitive Nep1 protein (nep1-1(ts)) was suppressed by the addition of S-adenosylmethionine (SAM).	S-Adenosylmethionine	153-156	18S rRNA pseudouridine methyltransferase	Saccharomyces cerevisiae S288C	71-75
18208838-3	2008	In Saccharomyces cerevisiae the malfunction of a temperature-sensitive Nep1 protein (nep1-1(ts)) was suppressed by the addition of S-adenosylmethionine (SAM).	S-Adenosylmethionine	153-156	18S rRNA pseudouridine methyltransferase	Saccharomyces cerevisiae S288C	85-89
18208838-6	2008	Here, we present the X-ray structure of the Nep1 homolog from the archaebacterium Methanocaldococcus jannaschii in its free form (2.2 A resolution) and bound to the S-adenosylmethionine analog S-adenosylhomocysteine (SAH, 2.15 A resolution) and the antibiotic and general methyltransferase inhibitor sinefungin (2.25 A resolution).	S-Adenosylmethionine	167-185	18S rRNA pseudouridine methyltransferase	Saccharomyces cerevisiae S288C	44-48
18208517-1	2008	In the S-methylmethionine cycle of plants, homocysteine methyltransferase (HMT) catalyzes the formation of two molecules of methionine from homocysteine and S-methylmethionine, and methionine methyltransferase (MMT) catalyzes the formation of methionine from S-methylmethionine using S-adenosylmethionine as a methyl group donor.	S-Adenosylmethionine	284-304	histamine N-methyltransferase	Homo sapiens	43-73
18208517-1	2008	In the S-methylmethionine cycle of plants, homocysteine methyltransferase (HMT) catalyzes the formation of two molecules of methionine from homocysteine and S-methylmethionine, and methionine methyltransferase (MMT) catalyzes the formation of methionine from S-methylmethionine using S-adenosylmethionine as a methyl group donor.	S-Adenosylmethionine	284-304	histamine N-methyltransferase	Homo sapiens	75-78
18326758-12	2008	The mechanism of AICAR inhibition may be attributed to the interference of adenosylmethionine-dependent methylation.	S-Adenosylmethionine	75-93	5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase	Homo sapiens	17-22
18317335-1	2008	PURPOSE: The C677T polymorphism of methylene tetrahydrofolate reductase (MTHFR) lowers the activity of this enzyme, producing moderate elevation of blood levels of homocysteine (Hcy) and lowering the levels of 5-methyl-tetrahydro-folic acid (5-MeTHFA), methionine (Meth), and S-adenosylmethionine (SAM).	S-Adenosylmethionine	276-296	methylenetetrahydrofolate reductase	Homo sapiens	35-71
18317335-1	2008	PURPOSE: The C677T polymorphism of methylene tetrahydrofolate reductase (MTHFR) lowers the activity of this enzyme, producing moderate elevation of blood levels of homocysteine (Hcy) and lowering the levels of 5-methyl-tetrahydro-folic acid (5-MeTHFA), methionine (Meth), and S-adenosylmethionine (SAM).	S-Adenosylmethionine	276-296	methylenetetrahydrofolate reductase	Homo sapiens	73-78
18317335-1	2008	PURPOSE: The C677T polymorphism of methylene tetrahydrofolate reductase (MTHFR) lowers the activity of this enzyme, producing moderate elevation of blood levels of homocysteine (Hcy) and lowering the levels of 5-methyl-tetrahydro-folic acid (5-MeTHFA), methionine (Meth), and S-adenosylmethionine (SAM).	S-Adenosylmethionine	298-301	methylenetetrahydrofolate reductase	Homo sapiens	35-71
18317335-1	2008	PURPOSE: The C677T polymorphism of methylene tetrahydrofolate reductase (MTHFR) lowers the activity of this enzyme, producing moderate elevation of blood levels of homocysteine (Hcy) and lowering the levels of 5-methyl-tetrahydro-folic acid (5-MeTHFA), methionine (Meth), and S-adenosylmethionine (SAM).	S-Adenosylmethionine	298-301	methylenetetrahydrofolate reductase	Homo sapiens	73-78
18184691-1	2008	Expression of the Arabidopsis CGS1 gene that codes for cystathionine gamma-synthase is feedback-regulated at the step of mRNA degradation in response to S-adenosyl-L-methionine (AdoMet).	S-Adenosylmethionine	153-176	Pyridoxal phosphate (PLP)-dependent transferases superfamily protein	Arabidopsis thaliana	55-83
18184691-1	2008	Expression of the Arabidopsis CGS1 gene that codes for cystathionine gamma-synthase is feedback-regulated at the step of mRNA degradation in response to S-adenosyl-L-methionine (AdoMet).	S-Adenosylmethionine	178-184	Pyridoxal phosphate (PLP)-dependent transferases superfamily protein	Arabidopsis thaliana	30-34
18184691-1	2008	Expression of the Arabidopsis CGS1 gene that codes for cystathionine gamma-synthase is feedback-regulated at the step of mRNA degradation in response to S-adenosyl-L-methionine (AdoMet).	S-Adenosylmethionine	178-184	Pyridoxal phosphate (PLP)-dependent transferases superfamily protein	Arabidopsis thaliana	55-83
18769049-1	2008	BACKGROUND/AIMS: S-Adenosylhomocysteine hydrolase (AdoHcyase) catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy), which is a potent product inhibitor of S-adenosylmethionine (AdoMet)-dependent methyltransferases.	S-Adenosylmethionine	173-193	adenosylhomocysteinase	Homo sapiens	17-49
18060852-10	2008	Finally, we show that CBS is stimulated by S-adenosyl- l-methionine but not its analogs.	S-Adenosylmethionine	43-67	cystathionine beta-synthase	Homo sapiens	22-25
18041713-4	2008	Methionine adenosyltransferase (MAT) is an essential enzyme that catalyzes the formation of S-adenosylmethionine (SAMe), the principal methyl donor and precursor of polyamines.	S-Adenosylmethionine	92-112	methionine adenosyltransferase 1A	Homo sapiens	0-30
18041713-4	2008	Methionine adenosyltransferase (MAT) is an essential enzyme that catalyzes the formation of S-adenosylmethionine (SAMe), the principal methyl donor and precursor of polyamines.	S-Adenosylmethionine	92-112	methionine adenosyltransferase 1A	Homo sapiens	32-35
18077728-6	2008	Moreover, our work, for the first time, provides strong evidence suggesting that viperin is a putative radical S-adenosyl-l-methionine (SAM) enzyme.	S-Adenosylmethionine	136-139	radical S-adenosyl methionine domain containing 2	Homo sapiens	81-88
18184782-6	2008	Furthermore, adding excess substrate for DNA methylation (S-adenosyl-L-methionine) rescues the suppression of mEPSCs by DNMT inhibitors in wild-type neurons, as well as the defect seen in MeCP2-deficient neurons.	S-Adenosylmethionine	58-81	DNA methyltransferase 1	Homo sapiens	120-124
18078345-2	2008	To develop a simple and effective way to enzymatically synthesize and produce SAM, a soluble form of SAM synthetase encoded by SAM2 from Saccharomyces cerevisiae was successfully produced at high level ( approximately 200 mg/L) by the recombinant methylotrophic yeast Pichia pastoris.	S-Adenosylmethionine	78-81	methionine adenosyltransferase SAM2	Saccharomyces cerevisiae S288C	127-131
18063569-2	2008	Here we report the determination of the crystal structure of Emg1 at 2 A resolution in complex with the methyl donor, S-adenosyl-methionine (SAM).	S-Adenosylmethionine	118-139	EMG1 N1-specific pseudouridine methyltransferase	Homo sapiens	61-65
18063569-2	2008	Here we report the determination of the crystal structure of Emg1 at 2 A resolution in complex with the methyl donor, S-adenosyl-methionine (SAM).	S-Adenosylmethionine	141-144	EMG1 N1-specific pseudouridine methyltransferase	Homo sapiens	61-65
18092814-1	2008	The Saccharomyces cerevisiae methyltransferase encoded by TMT1 catalyzes the AdoMet-dependent monomethylation of 3-isopropylmalate, an intermediate of the leucine biosynthetic pathway.	S-Adenosylmethionine	77-83	trans-aconitate 3-methyltransferase	Saccharomyces cerevisiae S288C	58-62
18769049-1	2008	BACKGROUND/AIMS: S-Adenosylhomocysteine hydrolase (AdoHcyase) catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy), which is a potent product inhibitor of S-adenosylmethionine (AdoMet)-dependent methyltransferases.	S-Adenosylmethionine	173-193	adenosylhomocysteinase	Homo sapiens	51-60
18769049-1	2008	BACKGROUND/AIMS: S-Adenosylhomocysteine hydrolase (AdoHcyase) catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy), which is a potent product inhibitor of S-adenosylmethionine (AdoMet)-dependent methyltransferases.	S-Adenosylmethionine	195-201	adenosylhomocysteinase	Homo sapiens	17-49
18769049-1	2008	BACKGROUND/AIMS: S-Adenosylhomocysteine hydrolase (AdoHcyase) catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy), which is a potent product inhibitor of S-adenosylmethionine (AdoMet)-dependent methyltransferases.	S-Adenosylmethionine	195-201	adenosylhomocysteinase	Homo sapiens	51-60
18044969-2	2007	Proton dissociation (SET7/9.Lys4-NH3+.AdoMet --> SET7/9.Lys4-NH2.AdoMet + H+) must be prior to the methylation by S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	117-137	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	21-27
17629356-4	2008	In addition, it is also regulated by S-adenosylmethionine which acts as an allosteric activator of CBS.	S-Adenosylmethionine	37-57	cystathionine beta-synthase	Homo sapiens	99-102
18804700-6	2008	GNMT is one of the key enzymes in methionine and S-adenosylmethionine (AdoMet) metabolism.	S-Adenosylmethionine	49-69	glycine N-methyltransferase	Homo sapiens	0-4
18044969-2	2007	Proton dissociation (SET7/9.Lys4-NH3+.AdoMet --> SET7/9.Lys4-NH2.AdoMet + H+) must be prior to the methylation by S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	117-137	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	52-58
18044969-2	2007	Proton dissociation (SET7/9.Lys4-NH3+.AdoMet --> SET7/9.Lys4-NH2.AdoMet + H+) must be prior to the methylation by S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	38-44	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	21-27
18044969-2	2007	Proton dissociation (SET7/9.Lys4-NH3+.AdoMet --> SET7/9.Lys4-NH2.AdoMet + H+) must be prior to the methylation by S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	38-44	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	52-58
18064318-2	2007	Catechol-O-methyltransferase (COMT) is involved in the S-adenosylmethionine-dependent methylation of catecholamines and catecholestrogens and in this way contributes to homocysteine synthesis.	S-Adenosylmethionine	57-75	catechol-O-methyltransferase	Homo sapiens	0-28
17928413-3	2007	This is a two-step process in which l-arginine:glycine amidinotransferase (AGAT) catalyzes the conversion of glycine and arginine to ornithine and guanidinoacetate (GAA); guanidinoacetate methyltransferase (GAMT) then catalyzes the S-adenosylmethionine-dependent methylation of GAA to creatine.	S-Adenosylmethionine	234-252	glycine amidinotransferase	Rattus norvegicus	36-73
17928413-3	2007	This is a two-step process in which l-arginine:glycine amidinotransferase (AGAT) catalyzes the conversion of glycine and arginine to ornithine and guanidinoacetate (GAA); guanidinoacetate methyltransferase (GAMT) then catalyzes the S-adenosylmethionine-dependent methylation of GAA to creatine.	S-Adenosylmethionine	234-252	glycine amidinotransferase	Rattus norvegicus	75-79
17928413-3	2007	This is a two-step process in which l-arginine:glycine amidinotransferase (AGAT) catalyzes the conversion of glycine and arginine to ornithine and guanidinoacetate (GAA); guanidinoacetate methyltransferase (GAMT) then catalyzes the S-adenosylmethionine-dependent methylation of GAA to creatine.	S-Adenosylmethionine	234-252	guanidinoacetate N-methyltransferase	Rattus norvegicus	171-205
17928413-3	2007	This is a two-step process in which l-arginine:glycine amidinotransferase (AGAT) catalyzes the conversion of glycine and arginine to ornithine and guanidinoacetate (GAA); guanidinoacetate methyltransferase (GAMT) then catalyzes the S-adenosylmethionine-dependent methylation of GAA to creatine.	S-Adenosylmethionine	234-252	guanidinoacetate N-methyltransferase	Rattus norvegicus	207-211
18064318-2	2007	Catechol-O-methyltransferase (COMT) is involved in the S-adenosylmethionine-dependent methylation of catecholamines and catecholestrogens and in this way contributes to homocysteine synthesis.	S-Adenosylmethionine	57-75	catechol-O-methyltransferase	Homo sapiens	30-34
17907785-12	2007	Inclusion of the catechol-O-methyltransferase cofactor S-adenosylmethionine (SAM) in S-9 incubations also dramatically reduced the covalent binding of [(3)H]paroxetine, a finding that was consistent with O-methylation of the paroxetine-catechol metabolite to the corresponding guaiacol regioisomers in S-9 incubations.	S-Adenosylmethionine	55-75	catechol-O-methyltransferase	Homo sapiens	17-45
17976013-1	2007	Prokaryote DNA methyltransferases (MTases) of the Dam family (including those of bacteriophages T2 and T4) catalyze methyl group transfer from S-adenosyl-L-methionine (AdoMet), producing S-adenosyl-L-homocysteine (AdoHcy) and methylated adenine residues in palindromic GATC sequences.	S-Adenosylmethionine	145-166	glutamyl-tRNA amidotransferase subunit C	Homo sapiens	269-273
17976013-1	2007	Prokaryote DNA methyltransferases (MTases) of the Dam family (including those of bacteriophages T2 and T4) catalyze methyl group transfer from S-adenosyl-L-methionine (AdoMet), producing S-adenosyl-L-homocysteine (AdoHcy) and methylated adenine residues in palindromic GATC sequences.	S-Adenosylmethionine	168-174	glutamyl-tRNA amidotransferase subunit C	Homo sapiens	269-273
18057781-4	2007	PIMT catalyzes the transfer of the methyl group of S-adenosyl-L-methionine onto the alpha-carboxyl group of an L-isoaspartyl (or the beta-carboxyl group of an D-aspartyl) residue, which initiates the conversion of this residue to an L-aspartyl residue.	S-Adenosylmethionine	51-74	protein-L-isoaspartate (D-aspartate) O-methyltransferase 1	Mus musculus	0-4
17907785-12	2007	Inclusion of the catechol-O-methyltransferase cofactor S-adenosylmethionine (SAM) in S-9 incubations also dramatically reduced the covalent binding of [(3)H]paroxetine, a finding that was consistent with O-methylation of the paroxetine-catechol metabolite to the corresponding guaiacol regioisomers in S-9 incubations.	S-Adenosylmethionine	55-75	ribosomal protein S9	Homo sapiens	85-88
17907785-12	2007	Inclusion of the catechol-O-methyltransferase cofactor S-adenosylmethionine (SAM) in S-9 incubations also dramatically reduced the covalent binding of [(3)H]paroxetine, a finding that was consistent with O-methylation of the paroxetine-catechol metabolite to the corresponding guaiacol regioisomers in S-9 incubations.	S-Adenosylmethionine	55-75	ribosomal protein S9	Homo sapiens	302-305
17907785-12	2007	Inclusion of the catechol-O-methyltransferase cofactor S-adenosylmethionine (SAM) in S-9 incubations also dramatically reduced the covalent binding of [(3)H]paroxetine, a finding that was consistent with O-methylation of the paroxetine-catechol metabolite to the corresponding guaiacol regioisomers in S-9 incubations.	S-Adenosylmethionine	77-80	catechol-O-methyltransferase	Homo sapiens	17-45
17907785-12	2007	Inclusion of the catechol-O-methyltransferase cofactor S-adenosylmethionine (SAM) in S-9 incubations also dramatically reduced the covalent binding of [(3)H]paroxetine, a finding that was consistent with O-methylation of the paroxetine-catechol metabolite to the corresponding guaiacol regioisomers in S-9 incubations.	S-Adenosylmethionine	77-80	ribosomal protein S9	Homo sapiens	85-88
17907785-12	2007	Inclusion of the catechol-O-methyltransferase cofactor S-adenosylmethionine (SAM) in S-9 incubations also dramatically reduced the covalent binding of [(3)H]paroxetine, a finding that was consistent with O-methylation of the paroxetine-catechol metabolite to the corresponding guaiacol regioisomers in S-9 incubations.	S-Adenosylmethionine	77-80	ribosomal protein S9	Homo sapiens	302-305
17724020-7	2007	Inhibition of catechol-O-methyltransferase activity with tyrphostin AG1288 prevents both base-volatile product formation and protein labeling from methyl-labeled S-adenosylmethionine in heart, kidney, and liver, but not in testes or brain extracts.	S-Adenosylmethionine	162-182	catechol-O-methyltransferase	Homo sapiens	14-42
17868690-1	2007	TrmD and Trm5 are, respectively, the bacterial and eukarya/archaea methyl transferases that catalyze transfer of the methyl group from S-adenosyl methionine (AdoMet) to the N1 position of G37 in tRNA to synthesize m1G37-tRNA.	S-Adenosylmethionine	135-156	tRNA methyltransferase 5	Homo sapiens	9-13
17446309-2	2007	The present study investigated the effects of S-adenosyl-l-methionine (SAM) on the CYP2E1-dependent liver injury in ob/ob mice.	S-Adenosylmethionine	46-69	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	83-89
17880176-1	2007	Catechol-O-methyltransferase (COMT, EC 2.1.1.6) catalyzes the O-methylation of a wide array of catechol-containing substrates using s-adenosyl-L-methionine as the methyl donor.	S-Adenosylmethionine	132-155	catechol-O-methyltransferase	Homo sapiens	0-28
17880176-1	2007	Catechol-O-methyltransferase (COMT, EC 2.1.1.6) catalyzes the O-methylation of a wide array of catechol-containing substrates using s-adenosyl-L-methionine as the methyl donor.	S-Adenosylmethionine	132-155	catechol-O-methyltransferase	Homo sapiens	30-34
17548352-2	2007	The sole function of MTAP is to recycle 5"-methylthioadenosine (MTA) to S-adenosylmethionine.	S-Adenosylmethionine	72-92	methylthioadenosine phosphorylase	Homo sapiens	21-25
17640612-0	2007	Depletion of S-adenosyl-l-methionine with cycloleucine potentiates cytochrome P450 2E1 toxicity in primary rat hepatocytes.	S-Adenosylmethionine	13-36	cytochrome P450, family 2, subfamily e, polypeptide 1	Rattus norvegicus	67-86
17640894-4	2007	When the serine residue is mutated to glutamic acid, which mimics the phosphorylated serine residue, the mutant CARM1 exhibits diminished ability to bind the methyl donor adenosylmethionine and diminished histone methylation activity.	S-Adenosylmethionine	171-189	coactivator associated arginine methyltransferase 1	Homo sapiens	112-117
17446309-2	2007	The present study investigated the effects of S-adenosyl-l-methionine (SAM) on the CYP2E1-dependent liver injury in ob/ob mice.	S-Adenosylmethionine	71-74	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	83-89
17446309-4	2007	Administration of SAM (50 mg/kg body wt ip every 12 h for 3 days) prevented the observed pathological changes as well as the increase of apoptotic hepatocytes, caspase 3 activity, and serum TNF-alpha levels.	S-Adenosylmethionine	18-21	caspase 3	Mus musculus	160-169
17446309-4	2007	Administration of SAM (50 mg/kg body wt ip every 12 h for 3 days) prevented the observed pathological changes as well as the increase of apoptotic hepatocytes, caspase 3 activity, and serum TNF-alpha levels.	S-Adenosylmethionine	18-21	tumor necrosis factor	Mus musculus	190-199
17446309-5	2007	SAM administration inhibited CYP2E1 activity but not CYP2E1 content.	S-Adenosylmethionine	0-3	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	29-35
17477549-3	2007	On the basis of sequence similarity with Escherichia coli cobalamin-dependent MS (MetH), human MS comprises four discrete functional modules that bind from the N- to C-terminus, respectively, homocysteine, methyltetrahydrofolate, cobalamin, and S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	245-265	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	78-80
17591973-3	2007	As a methyl donor for biological transmethylation reactions, S-adenosylmethionine (SAMe) could restore GADD45beta expression in HepG2 in Northern blot analyses and quantitative real-time polymerase chain reaction.	S-Adenosylmethionine	61-81	growth arrest and DNA damage inducible beta	Homo sapiens	103-113
17631143-1	2007	BACKGROUND & AIMS: Two genes (MAT1A and MAT2A) encode for methionine adenosyltransferase, an essential enzyme responsible for S-adenosylmethionine (SAMe) biosynthesis.	S-Adenosylmethionine	130-150	methionine adenosyltransferase 1A	Homo sapiens	34-39
17631143-1	2007	BACKGROUND & AIMS: Two genes (MAT1A and MAT2A) encode for methionine adenosyltransferase, an essential enzyme responsible for S-adenosylmethionine (SAMe) biosynthesis.	S-Adenosylmethionine	130-150	methionine adenosyltransferase 2A	Homo sapiens	44-49
17477549-3	2007	On the basis of sequence similarity with Escherichia coli cobalamin-dependent MS (MetH), human MS comprises four discrete functional modules that bind from the N- to C-terminus, respectively, homocysteine, methyltetrahydrofolate, cobalamin, and S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	267-273	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	78-80
17457696-6	2007	Moderately decreased fibroblast MTHFR activity was associated with severely reduced affinity for NADPH and increased sensitivity to inhibition by S-adenosylmethionine (AdoMet) in case 2, and with mild FAD responsiveness in case 3.	S-Adenosylmethionine	146-166	methylenetetrahydrofolate reductase	Homo sapiens	32-37
17457696-6	2007	Moderately decreased fibroblast MTHFR activity was associated with severely reduced affinity for NADPH and increased sensitivity to inhibition by S-adenosylmethionine (AdoMet) in case 2, and with mild FAD responsiveness in case 3.	S-Adenosylmethionine	168-174	methylenetetrahydrofolate reductase	Homo sapiens	32-37
17213385-10	2007	HPLC analysis consistently revealed that ANGPTL4 could significantly restore the augmented S-adenosylmethionine levels and S-adenosylmethionine/S-adenosylhomocysteine ratios in livers of db/db mice.	S-Adenosylmethionine	91-111	angiopoietin-like 4	Mus musculus	41-48
17483780-13	2007	Results from in vitro studies have shown that the normalisation of STAT 1 methylation by bringing betaine and S Adenosyl Methionine (which belongs to homocysteine cycle) restores the antiviral activity of interferon.	S-Adenosylmethionine	112-131	signal transducer and activator of transcription 1	Homo sapiens	67-73
17426150-4	2007	sam1(-) sam2(-) mutants, in which the conversion of methionine to S-adenosylmethionine is blocked, exhibit reduced selenomethionine toxicity compared with wild-type yeast, increased production of protein during growth in selenomethionine, and efficient replacement of methionine by selenomethionine, based on quantitative mass spectrometry and x-ray crystallography.	S-Adenosylmethionine	66-86	methionine adenosyltransferase SAM1	Saccharomyces cerevisiae S288C	0-4
17426150-4	2007	sam1(-) sam2(-) mutants, in which the conversion of methionine to S-adenosylmethionine is blocked, exhibit reduced selenomethionine toxicity compared with wild-type yeast, increased production of protein during growth in selenomethionine, and efficient replacement of methionine by selenomethionine, based on quantitative mass spectrometry and x-ray crystallography.	S-Adenosylmethionine	66-86	methionine adenosyltransferase SAM2	Saccharomyces cerevisiae S288C	8-12
17301815-0	2007	Folate restriction and methylenetetrahydrofolate reductase 677T polymorphism decreases adoMet synthesis via folate-dependent remethylation in human-transformed lymphoblasts.	S-Adenosylmethionine	87-93	methylenetetrahydrofolate reductase	Homo sapiens	23-58
17213385-10	2007	HPLC analysis consistently revealed that ANGPTL4 could significantly restore the augmented S-adenosylmethionine levels and S-adenosylmethionine/S-adenosylhomocysteine ratios in livers of db/db mice.	S-Adenosylmethionine	123-143	angiopoietin-like 4	Mus musculus	41-48
17218313-3	2007	DUR3 catalyzed the uptake of polyamines together with urea, and SAM3 was found to catalyze the uptake of polyamines together with S-adenosylmethionine, glutamic acid, and lysine.	S-Adenosylmethionine	130-150	bifunctional polyamine/amino acid permease SAM3	Saccharomyces cerevisiae S288C	64-68
17360897-8	2007	Conversely, incubation of N2a cells with S-adenosylmethionine and expression of PPMT enhance PP2A methylation.	S-Adenosylmethionine	41-61	protein phosphatase 2 (formerly 2A), catalytic subunit, alpha isoform	Mus musculus	93-97
17264075-6	2007	These enzymes are the products of the SAM4 and MHT1 genes, identified previously as homocysteine methyltransferases dependent upon AdoMet and S-methylmethionine, respectively.	S-Adenosylmethionine	131-137	S-adenosylmethionine-homocysteine S-methyltransferase SAM4	Saccharomyces cerevisiae S288C	38-42
17264075-6	2007	These enzymes are the products of the SAM4 and MHT1 genes, identified previously as homocysteine methyltransferases dependent upon AdoMet and S-methylmethionine, respectively.	S-Adenosylmethionine	131-137	S-adenosylmethionine-homocysteine S-methyltransferase MHT1	Saccharomyces cerevisiae S288C	47-51
17283123-5	2007	Furthermore, treatment with demethylation inhibitor S-adenosylmethionine or stable expression of uPA short hairpin RNA significantly inhibits uPA expression and tumor cell invasion in vitro and tumor growth and incidence of lung metastasis in vivo.	S-Adenosylmethionine	52-72	plasminogen activator, urokinase	Homo sapiens	142-145
17158459-2	2007	It is abundant in the liver, where it uses excess S-adenosylmethionine (AdoMet) to methylate glycine to N-methylglycine (sarcosine) and produces S-adenosylhomocysteine (AdoHcy), thereby controlling the methylating potential of the cell.	S-Adenosylmethionine	50-70	methionine adenosyltransferase 1A	Rattus norvegicus	72-78
17156888-1	2007	BACKGROUND/AIMS: Previous studies in our laboratory implicated ethanol-induced decreases in hepatocellular S-adenosylmethionine to S-adenosylhomocysteine (SAM:SAH) ratios in lowering the activity of phosphatidylethanolamine methyltransferase (PEMT), which is associated with the generation of steatosis.	S-Adenosylmethionine	107-127	phosphatidylethanolamine N-methyltransferase	Rattus norvegicus	243-247
17317269-11	2007	In summary, the present work shows that the molecular mechanism of MAT2A expression is different during G0-G1 or G1-S transition and this may be related to the distinct requirements of S-adenosylmethionine during liver regeneration.	S-Adenosylmethionine	185-205	methionine adenosyltransferase 2A	Homo sapiens	67-72
17191129-2	2007	Here we report the study of in vitro methylation of heterogeneous nuclear ribonucleoprotein K (hnRNP K) with protein arginine methyltransferase 1 (PRMT1), as an enzyme, and S-adenosyl-L-methionine (SAM), as a methyl donor.	S-Adenosylmethionine	198-201	heterogeneous nuclear ribonucleoprotein K	Homo sapiens	52-93
17191129-2	2007	Here we report the study of in vitro methylation of heterogeneous nuclear ribonucleoprotein K (hnRNP K) with protein arginine methyltransferase 1 (PRMT1), as an enzyme, and S-adenosyl-L-methionine (SAM), as a methyl donor.	S-Adenosylmethionine	198-201	heterogeneous nuclear ribonucleoprotein K	Homo sapiens	95-102
16953798-0	2007	Inhibition of human betaine-homocysteine methyltransferase expression by S-adenosylmethionine and methylthioadenosine.	S-Adenosylmethionine	73-93	betaine--homocysteine S-methyltransferase	Homo sapiens	20-58
17237308-0	2007	S-adenosyl-L-methionine increases skeletal muscle mitochondrial DNA density and whole body insulin sensitivity in OLETF rats.	S-Adenosylmethionine	0-23	insulin	Homo sapiens	91-98
17237308-2	2007	Evidence also suggests that metabolism of S-adenosyl-L-methionine (SAM), the universal methyl donor for biological methylation, is associated with mitochondrial dysfunction and insulin resistance.	S-Adenosylmethionine	42-65	insulin	Homo sapiens	177-184
17237308-2	2007	Evidence also suggests that metabolism of S-adenosyl-L-methionine (SAM), the universal methyl donor for biological methylation, is associated with mitochondrial dysfunction and insulin resistance.	S-Adenosylmethionine	67-70	insulin	Homo sapiens	177-184
17259861-3	2007	In schizophrenia and bipolar disorder patients, the increase of S-adenosyl methionine is associated with an overexpression of DNA methyltransferase-1 mRNA in Brodmann"s area 9 GABAergic neurons.	S-Adenosylmethionine	64-85	DNA methyltransferase 1	Homo sapiens	126-149
17259861-4	2007	Hence, the increased expression of S-adenosyl methionine and DNA methyltransferase-1 may contribute to promoter cytosine 5-methylation and to downregulation of the expression of mRNAs encoding for reelin and GAD67 in cortical GABAergic neurons of schizhophrenia and bipolar disorder patients.	S-Adenosylmethionine	35-56	reelin	Homo sapiens	197-203
17259861-4	2007	Hence, the increased expression of S-adenosyl methionine and DNA methyltransferase-1 may contribute to promoter cytosine 5-methylation and to downregulation of the expression of mRNAs encoding for reelin and GAD67 in cortical GABAergic neurons of schizhophrenia and bipolar disorder patients.	S-Adenosylmethionine	35-56	glutamate decarboxylase 1	Homo sapiens	208-213
17982279-2	2007	Alterations of DNA methylation of the mdr-1 gene promoter are known to be linked to mdr-1 gene expression and are probably related to intracellular S-adenosyl-methionine.	S-Adenosylmethionine	148-169	ATP binding cassette subfamily B member 1	Homo sapiens	38-43
17182830-5	2007	Catechol polyphenols may indirectly inhibit DNMT by generating S-adenosyl-L-homocysteine on their methylation by S-adenosyl-L-methionine.	S-Adenosylmethionine	113-136	DNA methyltransferase 1	Homo sapiens	44-48
17272833-2	2007	A detailed study of the expression and activities of two enzymes, adenosine kinase (ADK) and S-adenosylhomocysteine hydrolase (SAHH), which are both required for the maintenance and recycling of S-adenosylmethionine-dependent methylation in plants, was carried out.	S-Adenosylmethionine	197-215	adenosine kinase	Arabidopsis thaliana	66-82
17272833-2	2007	A detailed study of the expression and activities of two enzymes, adenosine kinase (ADK) and S-adenosylhomocysteine hydrolase (SAHH), which are both required for the maintenance and recycling of S-adenosylmethionine-dependent methylation in plants, was carried out.	S-Adenosylmethionine	197-215	adenosine kinase	Arabidopsis thaliana	84-87
17720483-5	2007	HEN1 recognizes 21 to 24 nt small RNA duplexes, which are the products of Dicer-like enzymes, and transfers a methyl group from S-adenosylmethionine (SAM) to the 2" OH of the last nucleotides of the small RNA duplexes.	S-Adenosylmethionine	128-148	double-stranded RNA binding protein-related / DsRBD protein-like protein	Arabidopsis thaliana	0-4
17634574-5	2007	DNA methyltransferase 1 (DNMT1) is thought to play an important role in maintaining already established methylation patterns during DNA replication and catalyzes the transfer of a methyl moiety from S-adenosyl-L-methionine (SAM) to the 5-position of cytosines in the CpG dinucleotide.	S-Adenosylmethionine	199-222	DNA methyltransferase 1	Homo sapiens	0-23
17634574-5	2007	DNA methyltransferase 1 (DNMT1) is thought to play an important role in maintaining already established methylation patterns during DNA replication and catalyzes the transfer of a methyl moiety from S-adenosyl-L-methionine (SAM) to the 5-position of cytosines in the CpG dinucleotide.	S-Adenosylmethionine	199-222	DNA methyltransferase 1	Homo sapiens	25-30
17720483-5	2007	HEN1 recognizes 21 to 24 nt small RNA duplexes, which are the products of Dicer-like enzymes, and transfers a methyl group from S-adenosylmethionine (SAM) to the 2" OH of the last nucleotides of the small RNA duplexes.	S-Adenosylmethionine	150-153	double-stranded RNA binding protein-related / DsRBD protein-like protein	Arabidopsis thaliana	0-4
17020760-9	2006	Stimulation with SAM (S-adenosyl methionine) and homocysteine led to an increase in Herp promoter methylation, which correlated to an acute decrease in luciferase expression in SAM, but not in homocysteine stimulated cells.	S-Adenosylmethionine	22-43	homocysteine inducible ER protein with ubiquitin like domain 1	Homo sapiens	84-88
17032644-1	2006	Methylenetetrahydrofolate reductase (MTHFR; EC 1.5.1.20) is the sole enzyme responsible for generation of 5-methyltetrahydrofolate, which is required for methionine synthesis and provision of methyl groups via S-adenosylmethionine.	S-Adenosylmethionine	210-230	methylenetetrahydrofolate reductase	Mus musculus	37-42
17183144-8	2006	Prior studies demonstrate that impaired DNA methylation resulting from a deficiency in S-adenosylmethionine (SAM, which is rapidly depleted following folate deprivation) leads to PS-1 overexpression, and that direct supplementation with SAM attenuates PS-1 overexpression.	S-Adenosylmethionine	87-107	presenilin 1	Mus musculus	179-183
17132109-0	2006	Suppression of TNF-alpha production by S-adenosylmethionine in human mononuclear leukocytes is not mediated by polyamines.	S-Adenosylmethionine	39-59	tumor necrosis factor	Homo sapiens	15-24
17132109-3	2006	The aim of this study was to investigate whether methionine, its precursors or metabolites [phosphatidylcholine, choline, betaine, S-adenosylmethionine (SAM)] have a modulating effect on tumor necrosis factor alpha (TNF-alpha) production by endotoxin-stimulated human mononuclear leukocytes and whether SAM-dependent polyamines (spermidine, spermine) are mediators of SAM-induced inhibition of TNF-alpha synthesis.	S-Adenosylmethionine	133-151	tumor necrosis factor	Homo sapiens	187-214
17132109-3	2006	The aim of this study was to investigate whether methionine, its precursors or metabolites [phosphatidylcholine, choline, betaine, S-adenosylmethionine (SAM)] have a modulating effect on tumor necrosis factor alpha (TNF-alpha) production by endotoxin-stimulated human mononuclear leukocytes and whether SAM-dependent polyamines (spermidine, spermine) are mediators of SAM-induced inhibition of TNF-alpha synthesis.	S-Adenosylmethionine	153-156	tumor necrosis factor	Homo sapiens	187-214
17132109-3	2006	The aim of this study was to investigate whether methionine, its precursors or metabolites [phosphatidylcholine, choline, betaine, S-adenosylmethionine (SAM)] have a modulating effect on tumor necrosis factor alpha (TNF-alpha) production by endotoxin-stimulated human mononuclear leukocytes and whether SAM-dependent polyamines (spermidine, spermine) are mediators of SAM-induced inhibition of TNF-alpha synthesis.	S-Adenosylmethionine	153-156	tumor necrosis factor	Homo sapiens	216-225
17132109-3	2006	The aim of this study was to investigate whether methionine, its precursors or metabolites [phosphatidylcholine, choline, betaine, S-adenosylmethionine (SAM)] have a modulating effect on tumor necrosis factor alpha (TNF-alpha) production by endotoxin-stimulated human mononuclear leukocytes and whether SAM-dependent polyamines (spermidine, spermine) are mediators of SAM-induced inhibition of TNF-alpha synthesis.	S-Adenosylmethionine	153-156	tumor necrosis factor	Homo sapiens	394-403
17183144-8	2006	Prior studies demonstrate that impaired DNA methylation resulting from a deficiency in S-adenosylmethionine (SAM, which is rapidly depleted following folate deprivation) leads to PS-1 overexpression, and that direct supplementation with SAM attenuates PS-1 overexpression.	S-Adenosylmethionine	109-112	presenilin 1	Mus musculus	179-183
17183144-8	2006	Prior studies demonstrate that impaired DNA methylation resulting from a deficiency in S-adenosylmethionine (SAM, which is rapidly depleted following folate deprivation) leads to PS-1 overexpression, and that direct supplementation with SAM attenuates PS-1 overexpression.	S-Adenosylmethionine	109-112	presenilin 1	Mus musculus	252-256
17116711-2	2006	Recent studies have suggested that PEMT is an important consumer of methyl groups from S-adenosylmethionine (SAM) and is a major determinant of homocysteine pools.	S-Adenosylmethionine	87-107	phosphatidylethanolamine N-methyltransferase	Rattus norvegicus	35-39
17116711-2	2006	Recent studies have suggested that PEMT is an important consumer of methyl groups from S-adenosylmethionine (SAM) and is a major determinant of homocysteine pools.	S-Adenosylmethionine	109-112	phosphatidylethanolamine N-methyltransferase	Rattus norvegicus	35-39
17183426-3	2006	We demonstrate herein that these mice were depleted in the methyl donor S-adenosyl methionine (SAM), which inhibited glutathione S-transferase, since this enzyme requires methylation of oxidative species prior to glutathione-dependent reduction.	S-Adenosylmethionine	72-93	hematopoietic prostaglandin D synthase	Mus musculus	117-142
17080400-6	2006	S-adenosylmethionine (SAM) and methylthioadenosine (MTA), an intermediate metabolite in SAM metabolism, are hepatoprotective by modulating TNFalpha expression and increasing reduced glutathione (GSH) levels.	S-Adenosylmethionine	0-20	tumor necrosis factor	Mus musculus	139-147
17080400-6	2006	S-adenosylmethionine (SAM) and methylthioadenosine (MTA), an intermediate metabolite in SAM metabolism, are hepatoprotective by modulating TNFalpha expression and increasing reduced glutathione (GSH) levels.	S-Adenosylmethionine	22-25	tumor necrosis factor	Mus musculus	139-147
17183426-3	2006	We demonstrate herein that these mice were depleted in the methyl donor S-adenosyl methionine (SAM), which inhibited glutathione S-transferase, since this enzyme requires methylation of oxidative species prior to glutathione-dependent reduction.	S-Adenosylmethionine	95-98	hematopoietic prostaglandin D synthase	Mus musculus	117-142
16988141-7	2006	With regard to polymorphisms in 5,10-methylenetetrahydrofolate reductase (MTHFR), the modeling predicts that decrease MTHFR activity reduces concentrations of S-adenosylmethionine and 5-methyltetrahydrofolate, as well as DNA methylation, while modestly increasing S-adenosylhomocysteine and homocysteine concentrations and thymidine or purine synthesis.	S-Adenosylmethionine	159-179	methylenetetrahydrofolate reductase	Homo sapiens	32-72
17056803-6	2006	GAA supplementation dose-dependently decreased the hepatic S-adenosylmethionine (SAM) concentration and the activity of cystathionine beta-synthase (CBS) and increased the hepatic S-adenosylhomocysteine (SAH) and homocysteine concentrations.	S-Adenosylmethionine	59-79	alpha glucosidase	Rattus norvegicus	0-3
16988141-7	2006	With regard to polymorphisms in 5,10-methylenetetrahydrofolate reductase (MTHFR), the modeling predicts that decrease MTHFR activity reduces concentrations of S-adenosylmethionine and 5-methyltetrahydrofolate, as well as DNA methylation, while modestly increasing S-adenosylhomocysteine and homocysteine concentrations and thymidine or purine synthesis.	S-Adenosylmethionine	159-179	methylenetetrahydrofolate reductase	Homo sapiens	74-79
16988141-7	2006	With regard to polymorphisms in 5,10-methylenetetrahydrofolate reductase (MTHFR), the modeling predicts that decrease MTHFR activity reduces concentrations of S-adenosylmethionine and 5-methyltetrahydrofolate, as well as DNA methylation, while modestly increasing S-adenosylhomocysteine and homocysteine concentrations and thymidine or purine synthesis.	S-Adenosylmethionine	159-179	methylenetetrahydrofolate reductase	Homo sapiens	118-123
17004132-1	2006	Homocysteine is a sulfur-containing, nonproteinogenic, neurotoxic amino acid biosynthesized during methyl cycles after demethylation of S-adenosylmethionine (SAM) to S-adenosylhomocysteine (SAH) and subsequent hydrolysis of SAH into homocysteine and adenosine.	S-Adenosylmethionine	158-161	acyl-CoA synthetase medium chain family member 3	Homo sapiens	190-193
17004132-1	2006	Homocysteine is a sulfur-containing, nonproteinogenic, neurotoxic amino acid biosynthesized during methyl cycles after demethylation of S-adenosylmethionine (SAM) to S-adenosylhomocysteine (SAH) and subsequent hydrolysis of SAH into homocysteine and adenosine.	S-Adenosylmethionine	158-161	acyl-CoA synthetase medium chain family member 3	Homo sapiens	224-227
16830232-4	2006	Autoradiographic and vapor-phase equilibration analyses suggested that the nuclear PP4c undergoes OKA-sensitive carboxylmethylation (CML) when S-adenosyl-L-((3)H-methyl) methionine (SAM) was used as the methyl donor.	S-Adenosylmethionine	182-185	protein phosphatase 4 catalytic subunit	Homo sapiens	83-87
16953589-0	2006	Solvent-accessible cysteines in human cystathionine beta-synthase: crucial role of cysteine 431 in S-adenosyl-L-methionine binding.	S-Adenosylmethionine	99-122	cystathionine beta-synthase	Homo sapiens	38-65
16958675-1	2006	Methionine adenosyltransferase (MAT) is an essential enzyme that catalyzes the formation of the principal methyl donor S-adenosylmethionine (SAMe).	S-Adenosylmethionine	119-139	methionine adenosyltransferase 1A	Homo sapiens	0-30
16958675-1	2006	Methionine adenosyltransferase (MAT) is an essential enzyme that catalyzes the formation of the principal methyl donor S-adenosylmethionine (SAMe).	S-Adenosylmethionine	119-139	methionine adenosyltransferase 1A	Homo sapiens	32-35
16953589-4	2006	In this report, we demonstrate that in both the presence and absence of the CBS allosteric regulator S-adenosyl-l-methionine (AdoMet), only C15 and C431 of human CBS are solvent accessible.	S-Adenosylmethionine	101-124	cystathionine beta-synthase	Homo sapiens	76-79
16953589-4	2006	In this report, we demonstrate that in both the presence and absence of the CBS allosteric regulator S-adenosyl-l-methionine (AdoMet), only C15 and C431 of human CBS are solvent accessible.	S-Adenosylmethionine	101-124	placenta associated 8	Homo sapiens	140-143
16953589-4	2006	In this report, we demonstrate that in both the presence and absence of the CBS allosteric regulator S-adenosyl-l-methionine (AdoMet), only C15 and C431 of human CBS are solvent accessible.	S-Adenosylmethionine	101-124	cystathionine beta-synthase	Homo sapiens	162-165
16953589-4	2006	In this report, we demonstrate that in both the presence and absence of the CBS allosteric regulator S-adenosyl-l-methionine (AdoMet), only C15 and C431 of human CBS are solvent accessible.	S-Adenosylmethionine	126-132	cystathionine beta-synthase	Homo sapiens	76-79
16953589-4	2006	In this report, we demonstrate that in both the presence and absence of the CBS allosteric regulator S-adenosyl-l-methionine (AdoMet), only C15 and C431 of human CBS are solvent accessible.	S-Adenosylmethionine	126-132	placenta associated 8	Homo sapiens	140-143
16953589-4	2006	In this report, we demonstrate that in both the presence and absence of the CBS allosteric regulator S-adenosyl-l-methionine (AdoMet), only C15 and C431 of human CBS are solvent accessible.	S-Adenosylmethionine	126-132	cystathionine beta-synthase	Homo sapiens	162-165
16912287-4	2006	We show that a recombinant full-length and a truncated NS5 protein containing the methyltransferase (MTase) domain methylates GpppA-capped and m(7)GpppA-capped RNAs to m(7)GpppAm-RNA, using S-adenosylmethionine as a methyl donor.	S-Adenosylmethionine	190-210	Raf-1 proto-oncogene, serine/threonine kinase	Homo sapiens	55-58
16831604-0	2006	S-adenosylmethionine regulates cytoplasmic HuR via AMP-activated kinase.	S-Adenosylmethionine	0-20	ELAV (embryonic lethal, abnormal vision)-like 1 (Hu antigen R)	Mus musculus	43-46
16627483-5	2006	Both low and high FDH expression reduced total cellular folate concentrations by 60%, elevated rates of folate catabolism, and depleted cellular 5-methyl-THF and S-adenosylmethionine levels.	S-Adenosylmethionine	162-182	aldehyde dehydrogenase 1 family member L1	Homo sapiens	18-21
16627483-10	2006	FDH expression does deplete cellular 5-methyl-THF and S-adenosylmethionine levels indicating that FDH impairs the folate-dependent homocysteine remethylation cycle.	S-Adenosylmethionine	54-74	aldehyde dehydrogenase 1 family member L1	Homo sapiens	0-3
16614071-0	2006	S-adenosylmethionine stabilizes cystathionine beta-synthase and modulates redox capacity.	S-Adenosylmethionine	0-20	cystathionine beta-synthase	Homo sapiens	32-59
16469827-0	2006	Differential regulation of the JNK/AP-1 pathway by S-adenosylmethionine and methylthioadenosine in primary rat hepatocytes versus HuH7 hepatoma cells.	S-Adenosylmethionine	51-71	mitogen-activated protein kinase 8	Homo sapiens	31-34
16642040-7	2006	Multistep enzymatic formation of yW from yW-187 could be reconstituted in vitro using recombinant TYW2, TYW3 and TYW4 with S-adenosylmethionine, suggesting that yW synthesis might proceed through sequential reactions in a complex formed by multiple components assembled with the precursor tRNA.	S-Adenosylmethionine	123-143	tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase	Saccharomyces cerevisiae S288C	98-102
16642040-7	2006	Multistep enzymatic formation of yW from yW-187 could be reconstituted in vitro using recombinant TYW2, TYW3 and TYW4 with S-adenosylmethionine, suggesting that yW synthesis might proceed through sequential reactions in a complex formed by multiple components assembled with the precursor tRNA.	S-Adenosylmethionine	123-143	tRNA methyltransferase PPM2	Saccharomyces cerevisiae S288C	113-117
16648481-5	2006	The highly conserved S-adenosylmethionine-binding domain of PRMT2 mediated this effect.	S-Adenosylmethionine	23-41	protein arginine N-methyltransferase 2	Mus musculus	60-65
16618795-6	2006	The major structural and chemical factors that determine the enzyme regioselectivity of O-methylation were identified, and the X-ray structure of the complex of COMT with S-adenosyl-l-methionine and BIA 8-176 is herein disclosed.	S-Adenosylmethionine	171-194	catechol-O-methyltransferase	Homo sapiens	161-165
16497670-4	2006	Here, we have demonstrated that intracellular cysteine levels dictate the degradation of Met4 in vivo, as shown by the ability of cysteine, but not methionine or S-adenosylmethionine (AdoMet), to trigger Met4 degradation in an str4Delta strain, which lacks the ability to produce cysteine from methionine or AdoMet.	S-Adenosylmethionine	308-314	Met4p	Saccharomyces cerevisiae S288C	89-93
16614071-2	2006	The first and committing step in this pathway is catalyzed by cystathionine beta-synthase (CBS), which is subject to complex regulation, including allosteric activation by the methyl donor, S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	190-210	cystathionine beta-synthase	Homo sapiens	62-89
16614071-2	2006	The first and committing step in this pathway is catalyzed by cystathionine beta-synthase (CBS), which is subject to complex regulation, including allosteric activation by the methyl donor, S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	190-210	cystathionine beta-synthase	Homo sapiens	91-94
16614071-2	2006	The first and committing step in this pathway is catalyzed by cystathionine beta-synthase (CBS), which is subject to complex regulation, including allosteric activation by the methyl donor, S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	212-218	cystathionine beta-synthase	Homo sapiens	62-89
16614071-2	2006	The first and committing step in this pathway is catalyzed by cystathionine beta-synthase (CBS), which is subject to complex regulation, including allosteric activation by the methyl donor, S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	212-218	cystathionine beta-synthase	Homo sapiens	91-94
16581789-3	2006	In support of this model, we provide evidence that Mediator serves in vivo as a coactivator for the yeast activator Met4, which controls the gene network responsible for the biosynthesis of sulfur-containing amino acids and S-adenosylmethionine.	S-Adenosylmethionine	224-244	Met4p	Saccharomyces cerevisiae S288C	116-120
16472757-1	2006	Spermidine synthase (SPDS) catalyzes transfer of the propylamine group from decarboxylated S-adenosylmethionine (dcSAM) to putrescine to yield methylthioadenosine (MTA) and spermidine.	S-Adenosylmethionine	91-111	spermidine synthase	Homo sapiens	0-19
16472757-1	2006	Spermidine synthase (SPDS) catalyzes transfer of the propylamine group from decarboxylated S-adenosylmethionine (dcSAM) to putrescine to yield methylthioadenosine (MTA) and spermidine.	S-Adenosylmethionine	91-111	spermidine synthase	Homo sapiens	21-25
16557551-6	2006	We show that treating cells with S-adenosyl-L-methionine (AdoMet) and betaine could restore STAT1 methylation and improve IFNalpha signaling.	S-Adenosylmethionine	33-56	signal transducer and activator of transcription 1	Homo sapiens	92-97
16557551-6	2006	We show that treating cells with S-adenosyl-L-methionine (AdoMet) and betaine could restore STAT1 methylation and improve IFNalpha signaling.	S-Adenosylmethionine	33-56	interferon alpha 1	Homo sapiens	122-130
16557551-6	2006	We show that treating cells with S-adenosyl-L-methionine (AdoMet) and betaine could restore STAT1 methylation and improve IFNalpha signaling.	S-Adenosylmethionine	58-64	signal transducer and activator of transcription 1	Homo sapiens	92-97
16557551-6	2006	We show that treating cells with S-adenosyl-L-methionine (AdoMet) and betaine could restore STAT1 methylation and improve IFNalpha signaling.	S-Adenosylmethionine	58-64	interferon alpha 1	Homo sapiens	122-130
16557551-7	2006	Furthermore, the antiviral effect of IFNalpha in cell culture could be significantly enhanced by the addition of AdoMet and betaine.	S-Adenosylmethionine	113-119	interferon alpha 1	Homo sapiens	37-45
16373529-0	2006	S-adenosyl-L-methionine attenuates hepatotoxicity induced by agonistic Jo2 Fas antibody following CYP2E1 induction in mice.	S-Adenosylmethionine	0-23	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	98-104
16472822-6	2006	D96A (motif III) showed reduced AdoMet binding but increased activity under conditions of saturation with S-adenosyl-L-methionine (AdoMet), indicating that the contact of Asp96 to AdoMet is not required for catalysis.	S-Adenosylmethionine	106-129	methionine adenosyltransferase I, alpha	Mus musculus	131-137
16472822-6	2006	D96A (motif III) showed reduced AdoMet binding but increased activity under conditions of saturation with S-adenosyl-L-methionine (AdoMet), indicating that the contact of Asp96 to AdoMet is not required for catalysis.	S-Adenosylmethionine	106-129	methionine adenosyltransferase I, alpha	Mus musculus	131-137
16609996-0	2006	S-adenosyl-methionine decreases ethanol-induced apoptosis in primary hepatocyte cultures by a c-Jun N-terminal kinase activity-independent mechanism.	S-Adenosylmethionine	0-21	mitogen-activated protein kinase 8	Homo sapiens	94-117
16433904-2	2006	HEN1 transfers a methyl group from S-adenosylmethionine to the 2"-OH or 3"-OH group of the last nucleotide of miRNA/miRNA* duplexes produced by the nuclease Dicer.	S-Adenosylmethionine	35-55	double-stranded RNA binding protein-related / DsRBD protein-like protein	Arabidopsis thaliana	0-4
16632891-5	2006	The activity of hepatic glycine N-methyltransferase (GNMT), an enzyme involved in the regulation of tissue S-adenosylmethionine (SAM) and S-adenosylhomocysteine (SAH), was increased by folate deficiency (p < 0.006) and decreased by selenium deprivation (p < 0.0003).	S-Adenosylmethionine	107-127	glycine N-methyltransferase	Rattus norvegicus	24-51
16632891-5	2006	The activity of hepatic glycine N-methyltransferase (GNMT), an enzyme involved in the regulation of tissue S-adenosylmethionine (SAM) and S-adenosylhomocysteine (SAH), was increased by folate deficiency (p < 0.006) and decreased by selenium deprivation (p < 0.0003).	S-Adenosylmethionine	107-127	glycine N-methyltransferase	Rattus norvegicus	53-57
16420352-0	2006	The Elongator subunit Elp3 contains a Fe4S4 cluster and binds S-adenosylmethionine.	S-Adenosylmethionine	62-82	elongator acetyltransferase complex subunit 3	Homo sapiens	22-26
16519522-6	2006	Product inhibition studies with SUV39H1 showed that S-adenosyl-l-homocysteine is a competitive inhibitor of S-adenosyl-l-methionine and a mixed inhibitor of substrate peptide.	S-Adenosylmethionine	108-131	SUV39H1 histone lysine methyltransferase	Homo sapiens	32-39
16475806-2	2006	While the two proteins have similar kinetic properties, 108M COMT loses activity more rapidly than 108V COMT at 37 degrees C. The cosubstrate S-adenosylmethionine (SAM) stabilizes the activity of 108M COMT at 40 degrees C. The 108M allele has been associated with increased risk for breast cancer, obsessive-compulsive disorder, and aggressive and highly antisocial manifestations of schizophrenia.	S-Adenosylmethionine	142-162	catechol-O-methyltransferase	Homo sapiens	61-65
16475806-2	2006	While the two proteins have similar kinetic properties, 108M COMT loses activity more rapidly than 108V COMT at 37 degrees C. The cosubstrate S-adenosylmethionine (SAM) stabilizes the activity of 108M COMT at 40 degrees C. The 108M allele has been associated with increased risk for breast cancer, obsessive-compulsive disorder, and aggressive and highly antisocial manifestations of schizophrenia.	S-Adenosylmethionine	142-162	catechol-O-methyltransferase	Homo sapiens	104-108
16475806-2	2006	While the two proteins have similar kinetic properties, 108M COMT loses activity more rapidly than 108V COMT at 37 degrees C. The cosubstrate S-adenosylmethionine (SAM) stabilizes the activity of 108M COMT at 40 degrees C. The 108M allele has been associated with increased risk for breast cancer, obsessive-compulsive disorder, and aggressive and highly antisocial manifestations of schizophrenia.	S-Adenosylmethionine	142-162	catechol-O-methyltransferase	Homo sapiens	104-108
16475806-2	2006	While the two proteins have similar kinetic properties, 108M COMT loses activity more rapidly than 108V COMT at 37 degrees C. The cosubstrate S-adenosylmethionine (SAM) stabilizes the activity of 108M COMT at 40 degrees C. The 108M allele has been associated with increased risk for breast cancer, obsessive-compulsive disorder, and aggressive and highly antisocial manifestations of schizophrenia.	S-Adenosylmethionine	164-167	catechol-O-methyltransferase	Homo sapiens	61-65
16475806-2	2006	While the two proteins have similar kinetic properties, 108M COMT loses activity more rapidly than 108V COMT at 37 degrees C. The cosubstrate S-adenosylmethionine (SAM) stabilizes the activity of 108M COMT at 40 degrees C. The 108M allele has been associated with increased risk for breast cancer, obsessive-compulsive disorder, and aggressive and highly antisocial manifestations of schizophrenia.	S-Adenosylmethionine	164-167	catechol-O-methyltransferase	Homo sapiens	104-108
16475806-2	2006	While the two proteins have similar kinetic properties, 108M COMT loses activity more rapidly than 108V COMT at 37 degrees C. The cosubstrate S-adenosylmethionine (SAM) stabilizes the activity of 108M COMT at 40 degrees C. The 108M allele has been associated with increased risk for breast cancer, obsessive-compulsive disorder, and aggressive and highly antisocial manifestations of schizophrenia.	S-Adenosylmethionine	164-167	catechol-O-methyltransferase	Homo sapiens	104-108
16614482-3	2006	The evidence indicates that the critical site of B12 function in nerve tissue is in the enzyme, methionine synthase, in a system which requires S-adenosylmethionine.	S-Adenosylmethionine	144-164	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	49-52
16471489-2	2006	GAMT catalyzes the S-adenosyl-L-methionine (SAM)-dependent methylation of guanidinoacetate (GAA) to form creatine.	S-Adenosylmethionine	19-42	guanidinoacetate N-methyltransferase	Homo sapiens	0-4
16471489-2	2006	GAMT catalyzes the S-adenosyl-L-methionine (SAM)-dependent methylation of guanidinoacetate (GAA) to form creatine.	S-Adenosylmethionine	44-47	guanidinoacetate N-methyltransferase	Homo sapiens	0-4
16614482-3	2006	The evidence indicates that the critical site of B12 function in nerve tissue is in the enzyme, methionine synthase, in a system which requires S-adenosylmethionine.	S-Adenosylmethionine	144-164	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	96-115
16614482-5	2006	Evidence is reviewed which suggests that there is an analogy between the two systems and that S-adenosyl methionine may catalyze a rearrangement of homocysteine on methionine synthase giving rise to iso- or beta-methionine.	S-Adenosylmethionine	96-115	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	164-183
16230360-4	2005	At micromolar concentrations, procainamide was found to be a partial competitive inhibitor of DNMT1, reducing the affinity of the enzyme for its two substrates, hemimethylated DNA and S-adenosyl-l-methionine.	S-Adenosylmethionine	186-207	DNA methyltransferase 1	Homo sapiens	94-99
16515461-3	2006	AdoMetDC catalyzes decarboxylation of S-adenosylmethionine (AdoMet) which provides aminopropyl groups for spermidine and spermine synthesis.	S-Adenosylmethionine	38-58	adenosylmethionine decarboxylase 1	Homo sapiens	0-8
15614425-2	2005	Levodopa is metabolised via O-methylation by catechol-O-methyltransferase (COMT) using S-adenosyl-L-methionine (SAM) as the methyl donor, this leading to the subsequent formation of homocysteine.	S-Adenosylmethionine	87-110	catechol-O-methyltransferase	Homo sapiens	45-73
16226262-2	2005	Biochemical characterisation of the recombinantly expressed protein revealed a high degree of similarity to other eukaryotic SPDS with the exception of a low affinity towards the substrate decarboxylated S-adenosylmethionine (Km = 110 microM) and a less pronounced feedback inhibition by the second reaction product 5"-methylthioadenosine (IC50 = 430 microM).	S-Adenosylmethionine	204-224	PABS domain-containing protein	Caenorhabditis elegans	125-129
16340382-1	2005	Metabolism of levodopa via the enzyme catechol-O-methyltransferase requires S-adenosylmethionine (SAM) as a methyl donor.	S-Adenosylmethionine	76-96	catechol-O-methyltransferase	Homo sapiens	38-66
16340382-1	2005	Metabolism of levodopa via the enzyme catechol-O-methyltransferase requires S-adenosylmethionine (SAM) as a methyl donor.	S-Adenosylmethionine	98-101	catechol-O-methyltransferase	Homo sapiens	38-66
16225687-5	2005	RESULTS: Two widespread folds, Rossmann fold and TIM barrel, have been repeatedly used in evolution for diverse types of S-adenosylmethionine conversion.	S-Adenosylmethionine	121-141	Rho guanine nucleotide exchange factor 5	Homo sapiens	49-52
16275737-8	2005	However, recent experiments revealing that CBS domains can bind adenosine-containing ligands such ATP, AMP, or S-adenosylmethionine have led to the hypothesis that CBS domains function as sensors of intracellular metabolites.	S-Adenosylmethionine	111-131	cystathionine beta-synthase	Homo sapiens	43-46
16275737-8	2005	However, recent experiments revealing that CBS domains can bind adenosine-containing ligands such ATP, AMP, or S-adenosylmethionine have led to the hypothesis that CBS domains function as sensors of intracellular metabolites.	S-Adenosylmethionine	111-131	cystathionine beta-synthase	Homo sapiens	164-167
15983038-0	2005	S-adenosylmethionine blocks collagen I production by preventing transforming growth factor-beta induction of the COL1A2 promoter.	S-Adenosylmethionine	0-20	collagen, type I, alpha 2	Mus musculus	113-119
15614425-2	2005	Levodopa is metabolised via O-methylation by catechol-O-methyltransferase (COMT) using S-adenosyl-L-methionine (SAM) as the methyl donor, this leading to the subsequent formation of homocysteine.	S-Adenosylmethionine	87-110	catechol-O-methyltransferase	Homo sapiens	75-79
16115544-1	2005	Protein L-isoaspartyl (D-aspartyl) O-methyltransferase (PCMT1) is a protein-repair enzyme, and mice lacking this enzyme accumulate damaged proteins in multiple tissues, die at an early age from progressive epilepsy and have an increased S-adenosylmethionine (AdoMet) to S-adenosylhomocysteine (AdoHcy) ratio in brain tissue.	S-Adenosylmethionine	237-257	protein-L-isoaspartate (D-aspartate) O-methyltransferase 1	Mus musculus	56-61
15614425-2	2005	Levodopa is metabolised via O-methylation by catechol-O-methyltransferase (COMT) using S-adenosyl-L-methionine (SAM) as the methyl donor, this leading to the subsequent formation of homocysteine.	S-Adenosylmethionine	112-115	catechol-O-methyltransferase	Homo sapiens	45-73
15614425-2	2005	Levodopa is metabolised via O-methylation by catechol-O-methyltransferase (COMT) using S-adenosyl-L-methionine (SAM) as the methyl donor, this leading to the subsequent formation of homocysteine.	S-Adenosylmethionine	112-115	catechol-O-methyltransferase	Homo sapiens	75-79
15958390-9	2005	Liver activity of betaine:homocysteine methyltransferase and methionine adenosyltransferase are elevated in the knockout mice as a mechanism for maintaining normal hepatic S-adenosylmethionine and S-adenosylhomocysteine levels.	S-Adenosylmethionine	172-192	betaine-homocysteine methyltransferase	Mus musculus	18-56
15964170-1	2005	Folate, methionine, betaine, choline, zinc and Vitamins B(12), B(6) and B(2) are involved in one-carbon metabolism, which includes S-adenosylmethionine (SAM) substrated methylation.	S-Adenosylmethionine	131-151	immunoglobulin kappa variable 5-2	Homo sapiens	72-76
16045352-4	2005	In this article we are reporting static and dynamic aspects of the enzyme catalysis in a bimolecular reaction, namely a methyl transfer from S-adenosylmethionine to the hydroxylate oxygen of a substituted catechol catalyzed by catechol O-methyltransferase.	S-Adenosylmethionine	141-161	catechol-O-methyltransferase	Homo sapiens	227-255
16027170-1	2005	Expression of the Arabidopsis CGS1 gene that codes for cystathionine gamma-synthase is feedback regulated at the step of mRNA stability in response to S-adenosyl-L-methionine (AdoMet).	S-Adenosylmethionine	151-174	Pyridoxal phosphate (PLP)-dependent transferases superfamily protein	Arabidopsis thaliana	30-34
16027170-1	2005	Expression of the Arabidopsis CGS1 gene that codes for cystathionine gamma-synthase is feedback regulated at the step of mRNA stability in response to S-adenosyl-L-methionine (AdoMet).	S-Adenosylmethionine	151-174	Pyridoxal phosphate (PLP)-dependent transferases superfamily protein	Arabidopsis thaliana	55-83
16027170-1	2005	Expression of the Arabidopsis CGS1 gene that codes for cystathionine gamma-synthase is feedback regulated at the step of mRNA stability in response to S-adenosyl-L-methionine (AdoMet).	S-Adenosylmethionine	176-182	Pyridoxal phosphate (PLP)-dependent transferases superfamily protein	Arabidopsis thaliana	30-34
16027170-1	2005	Expression of the Arabidopsis CGS1 gene that codes for cystathionine gamma-synthase is feedback regulated at the step of mRNA stability in response to S-adenosyl-L-methionine (AdoMet).	S-Adenosylmethionine	176-182	Pyridoxal phosphate (PLP)-dependent transferases superfamily protein	Arabidopsis thaliana	55-83
16024724-2	2005	Regulation of MTHFR activity is crucial for maintaining cellular concentrations of methionine and S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	98-118	methylenetetrahydrofolate reductase	Homo sapiens	14-19
15979267-2	2005	MTHFR is a critical enzyme in folate metabolism; the product of the MTHFR reaction, 5-methyltetrahydrofolate, is required for homocysteine remethylation to methionine and synthesis of S-adenosylmethionine (SAM).	S-Adenosylmethionine	184-204	methylenetetrahydrofolate reductase	Mus musculus	0-5
15979267-2	2005	MTHFR is a critical enzyme in folate metabolism; the product of the MTHFR reaction, 5-methyltetrahydrofolate, is required for homocysteine remethylation to methionine and synthesis of S-adenosylmethionine (SAM).	S-Adenosylmethionine	184-204	methylenetetrahydrofolate reductase	Mus musculus	68-73
15979267-2	2005	MTHFR is a critical enzyme in folate metabolism; the product of the MTHFR reaction, 5-methyltetrahydrofolate, is required for homocysteine remethylation to methionine and synthesis of S-adenosylmethionine (SAM).	S-Adenosylmethionine	206-209	methylenetetrahydrofolate reductase	Mus musculus	0-5
15979267-2	2005	MTHFR is a critical enzyme in folate metabolism; the product of the MTHFR reaction, 5-methyltetrahydrofolate, is required for homocysteine remethylation to methionine and synthesis of S-adenosylmethionine (SAM).	S-Adenosylmethionine	206-209	methylenetetrahydrofolate reductase	Mus musculus	68-73
16024724-2	2005	Regulation of MTHFR activity is crucial for maintaining cellular concentrations of methionine and S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	120-126	methylenetetrahydrofolate reductase	Homo sapiens	14-19
15964937-8	2005	Their characterization of this S-adenosylmethionine analog suggests that it inhibits mRNA cap methyltransferases and exhibits approximately 5- to 10-fold specificity for the yeast ABD1 and fungal CCM1 enzymes over the human Hcm1 enzyme expressed in yeast cells.	S-Adenosylmethionine	33-51	mRNA (guanine-N7)-methyltransferase	Saccharomyces cerevisiae S288C	180-184
16000004-4	2005	Products of the MTAP reaction (adenine and 5-methylthio-alpha-D-ribose-1-phosphate) are recycled to S-adenosylmethionine, the precursor for polyamine synthesis.	S-Adenosylmethionine	100-120	methylthioadenosine phosphorylase	Homo sapiens	16-20
16000004-5	2005	Potent inhibitors of MTAP might allow the build-up of sufficient levels of MTA to generate feedback inhibition of polyamine biosynthesis and/or reduce S-adenosylmethionine levels.	S-Adenosylmethionine	151-171	methylthioadenosine phosphorylase	Homo sapiens	21-25
15897017-5	2005	We therefore, established an optimized and fast isocratic HPLC linked TPMT assay based on the enzymatic methylation of mercaptopurine or thioguanine in RBC lysates with S-adenosyl-l-methionine as methyl donor.	S-Adenosylmethionine	169-192	thiopurine S-methyltransferase	Homo sapiens	70-74
15973722-4	2005	Furthermore, common genetic polymorphisms in the gene encoding methylenetetrahydrofolate reductase (MTHFR) may have an indirect impact on thiopurine drug methylation by influencing levels of the methyl donor S-adenosylmethionine (SAM).	S-Adenosylmethionine	208-228	methylenetetrahydrofolate reductase	Homo sapiens	63-98
15973722-4	2005	Furthermore, common genetic polymorphisms in the gene encoding methylenetetrahydrofolate reductase (MTHFR) may have an indirect impact on thiopurine drug methylation by influencing levels of the methyl donor S-adenosylmethionine (SAM).	S-Adenosylmethionine	208-228	methylenetetrahydrofolate reductase	Homo sapiens	100-105
15964937-8	2005	Their characterization of this S-adenosylmethionine analog suggests that it inhibits mRNA cap methyltransferases and exhibits approximately 5- to 10-fold specificity for the yeast ABD1 and fungal CCM1 enzymes over the human Hcm1 enzyme expressed in yeast cells.	S-Adenosylmethionine	33-51	Ccm1p	Saccharomyces cerevisiae S288C	196-200
15843034-0	2005	S-adenosylmethionine (SAMe) modulates interleukin-10 and interleukin-6, but not TNF, production via the adenosine (A2) receptor.	S-Adenosylmethionine	0-20	interleukin 10	Mus musculus	38-52
15760890-0	2005	Encephalitozoon cuniculi mRNA cap (guanine N-7) methyltransferase: methyl acceptor specificity, inhibition BY S-adenosylmethionine analogs, and structure-guided mutational analysis.	S-Adenosylmethionine	110-130	RNA (guanine-7-) methyltransferase	Mus musculus	25-65
15789416-1	2005	The Escherichia coli TrmB protein and its Saccharomyces cerevisiae ortholog Trm8p catalyze the S-adenosyl-L-methionine-dependent formation of 7-methylguanosine at position 46 (m7G46) in tRNA.	S-Adenosylmethionine	95-118	tRNA (guanine46-N7)-methyltransferase	Saccharomyces cerevisiae S288C	76-81
15940873-1	2005	S-adenosylmethionine decarboxylase activity (SAMDC; EC 4.1.1.21) leads to spermidine and spermine synthesis through specific synthases which use putrescine, spermidine and decarboxylated S-adenosylmethionine as substrates.	S-Adenosylmethionine	0-20	S-adenosylmethionine decarboxylase proenzyme	Nicotiana tabacum	45-50
16047261-4	2005	In particular, S-adenosylmethionine acts as a switch between remethylation and transsulfuration through its allosteric inhibition of methylenetetrahydrofolate reductase and activation of cystathionine beta-synthase.	S-Adenosylmethionine	15-35	methylenetetrahydrofolate reductase	Homo sapiens	133-168
16047261-4	2005	In particular, S-adenosylmethionine acts as a switch between remethylation and transsulfuration through its allosteric inhibition of methylenetetrahydrofolate reductase and activation of cystathionine beta-synthase.	S-Adenosylmethionine	15-35	cystathionine beta-synthase	Homo sapiens	187-214
15835908-1	2005	Saturation transfer difference NMR measurements were performed to investigate the interaction of S-adenosyl-l-methionine (AdoMet) with SU(VAR)3-9 from Drosophila melanogaster.	S-Adenosylmethionine	97-120	Suppressor of variegation 3-9	Drosophila melanogaster	135-145
15835908-1	2005	Saturation transfer difference NMR measurements were performed to investigate the interaction of S-adenosyl-l-methionine (AdoMet) with SU(VAR)3-9 from Drosophila melanogaster.	S-Adenosylmethionine	122-128	Suppressor of variegation 3-9	Drosophila melanogaster	135-145
15843034-0	2005	S-adenosylmethionine (SAMe) modulates interleukin-10 and interleukin-6, but not TNF, production via the adenosine (A2) receptor.	S-Adenosylmethionine	0-20	interleukin 6	Mus musculus	57-70
15695433-1	2005	The betaine biosynthesis pathway of betaine-accumulating plants involves choline monooxygenase (CMO) as the key enzyme and phosphoethanolamine N-methyltransferase (PEAMT), which require S-adenosyl-L-methionine (SAM) as a methyl donor.	S-Adenosylmethionine	186-209	phosphatidylethanolamine N-methyltransferase	Homo sapiens	123-162
16054984-1	2005	Two genes (MAT1A and MAT2A) encode for the essential enzyme methionine adenosyltransferase (MAT), which catalyzes the biosynthesis of S-adenosylmethionine (SAMe), the principal methyl donor and, in the liver, a precursor of glutathione.	S-Adenosylmethionine	134-154	methionine adenosyltransferase 1A	Homo sapiens	11-16
16054984-1	2005	Two genes (MAT1A and MAT2A) encode for the essential enzyme methionine adenosyltransferase (MAT), which catalyzes the biosynthesis of S-adenosylmethionine (SAMe), the principal methyl donor and, in the liver, a precursor of glutathione.	S-Adenosylmethionine	134-154	methionine adenosyltransferase 2A	Homo sapiens	21-26
15763544-0	2005	Inhibition of CYP2E1 catalytic activity in vitro by S-adenosyl-L-methionine.	S-Adenosylmethionine	52-75	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	14-20
15763544-1	2005	The objective of this work was to evaluate the possible in vitro interactions of S-adenosyl-l-methionine (SAM) and its metabolites S-(5"-Adenosyl)-l-homocysteine (SAH), 5"-Deoxy-5"-(methylthio)adenosine (MTA) and methionine with cytochrome P450 enzymes, in particular CYP2E1.	S-Adenosylmethionine	81-104	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	268-274
15763544-1	2005	The objective of this work was to evaluate the possible in vitro interactions of S-adenosyl-l-methionine (SAM) and its metabolites S-(5"-Adenosyl)-l-homocysteine (SAH), 5"-Deoxy-5"-(methylthio)adenosine (MTA) and methionine with cytochrome P450 enzymes, in particular CYP2E1.	S-Adenosylmethionine	106-109	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	268-274
15763544-5	2005	However, SAM inhibited the catalytic activity of CYP2E1 with typical substrates such as p-nitrophenol, ethanol, and dimethylnitrosamine, with an IC(50) around 1.5-5mM.	S-Adenosylmethionine	9-12	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	49-55
15763544-9	2005	SAM also inhibited CYP2E1 catalytic activity in intact HepG2 cells engineered to express CYP2E1.	S-Adenosylmethionine	0-3	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	19-25
15763544-9	2005	SAM also inhibited CYP2E1 catalytic activity in intact HepG2 cells engineered to express CYP2E1.	S-Adenosylmethionine	0-3	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	89-95
15548731-2	2005	Within the folate pathway, methylenetetrahydrofolate reductase (MTHFR) reduces 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate, a methyl donor for remethylation of homocysteine to methionine, the precursor of S-adenosylmethionine.	S-Adenosylmethionine	220-240	methylenetetrahydrofolate reductase	Homo sapiens	27-62
15548731-2	2005	Within the folate pathway, methylenetetrahydrofolate reductase (MTHFR) reduces 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate, a methyl donor for remethylation of homocysteine to methionine, the precursor of S-adenosylmethionine.	S-Adenosylmethionine	220-240	methylenetetrahydrofolate reductase	Homo sapiens	64-69
15526190-6	2005	Human recombinant Cyt19 catalyzed transfer of a methyl group from S-adenosyl-L-methionine to arsenic and produced monomethyl and dimethyl arsenicals.	S-Adenosylmethionine	66-89	arsenite methyltransferase	Homo sapiens	18-23
15695433-1	2005	The betaine biosynthesis pathway of betaine-accumulating plants involves choline monooxygenase (CMO) as the key enzyme and phosphoethanolamine N-methyltransferase (PEAMT), which require S-adenosyl-L-methionine (SAM) as a methyl donor.	S-Adenosylmethionine	186-209	phosphatidylethanolamine N-methyltransferase	Homo sapiens	164-169
15695433-1	2005	The betaine biosynthesis pathway of betaine-accumulating plants involves choline monooxygenase (CMO) as the key enzyme and phosphoethanolamine N-methyltransferase (PEAMT), which require S-adenosyl-L-methionine (SAM) as a methyl donor.	S-Adenosylmethionine	211-214	phosphatidylethanolamine N-methyltransferase	Homo sapiens	164-169
15590684-5	2005	Here we show that purified recombinant fission yeast Tgs1 catalyzes methyl transfer from S-adenosylmethionine (AdoMet) to m7GTP and m7GDP.	S-Adenosylmethionine	89-109	RNA methyltransferase	Saccharomyces cerevisiae S288C	53-57
15728403-2	2005	N-methylated pyridines (e.g. MPP+) are well-established dopaminergic toxins, and the xenobiotic enzyme nicotinamide N-methyltransferase (NNMT) can convert pyridines such as 4-phenylpyridine into MPP+, using S-adenosyl methionine (SAM) as the methyl donor.	S-Adenosylmethionine	207-228	nicotinamide N-methyltransferase	Homo sapiens	103-135
15728403-2	2005	N-methylated pyridines (e.g. MPP+) are well-established dopaminergic toxins, and the xenobiotic enzyme nicotinamide N-methyltransferase (NNMT) can convert pyridines such as 4-phenylpyridine into MPP+, using S-adenosyl methionine (SAM) as the methyl donor.	S-Adenosylmethionine	207-228	nicotinamide N-methyltransferase	Homo sapiens	137-141
15728403-2	2005	N-methylated pyridines (e.g. MPP+) are well-established dopaminergic toxins, and the xenobiotic enzyme nicotinamide N-methyltransferase (NNMT) can convert pyridines such as 4-phenylpyridine into MPP+, using S-adenosyl methionine (SAM) as the methyl donor.	S-Adenosylmethionine	230-233	nicotinamide N-methyltransferase	Homo sapiens	103-135
15728403-2	2005	N-methylated pyridines (e.g. MPP+) are well-established dopaminergic toxins, and the xenobiotic enzyme nicotinamide N-methyltransferase (NNMT) can convert pyridines such as 4-phenylpyridine into MPP+, using S-adenosyl methionine (SAM) as the methyl donor.	S-Adenosylmethionine	230-233	nicotinamide N-methyltransferase	Homo sapiens	137-141
15590684-5	2005	Here we show that purified recombinant fission yeast Tgs1 catalyzes methyl transfer from S-adenosylmethionine (AdoMet) to m7GTP and m7GDP.	S-Adenosylmethionine	111-117	RNA methyltransferase	Saccharomyces cerevisiae S288C	53-57
15670956-3	2005	Methionine S-adenosyltransferase (MAT) is an enzyme involved in the synthesis of S-adenosylmethionine (SAM), a methyl donor essential for mycolipid biosynthesis.	S-Adenosylmethionine	81-101	methionine adenosyltransferase 1A	Homo sapiens	0-32
15548527-1	2005	Aclacinomycin 10-hydroxylase is a methyltransferase homologue that catalyzes a S-adenosyl-L-methionine (AdoMet)-dependent hydroxylation of the C-10 carbon atom of 15-demethoxy-epsilon-rhodomycin, a step in the biosynthesis of the polyketide antibiotic beta-rhodomycin.	S-Adenosylmethionine	81-102	homeobox C10	Homo sapiens	143-147
15548527-1	2005	Aclacinomycin 10-hydroxylase is a methyltransferase homologue that catalyzes a S-adenosyl-L-methionine (AdoMet)-dependent hydroxylation of the C-10 carbon atom of 15-demethoxy-epsilon-rhodomycin, a step in the biosynthesis of the polyketide antibiotic beta-rhodomycin.	S-Adenosylmethionine	104-110	homeobox C10	Homo sapiens	143-147
15498786-6	2005	These lesions also showed low expression of Mat1A and low activity of methionine adenosyltransferase I/III, whose reaction product, S-adenosyl-l-methionine, enhances IkappaB-alpha expression.	S-Adenosylmethionine	132-155	methionine adenosyltransferase 1A	Rattus norvegicus	70-106
15498786-6	2005	These lesions also showed low expression of Mat1A and low activity of methionine adenosyltransferase I/III, whose reaction product, S-adenosyl-l-methionine, enhances IkappaB-alpha expression.	S-Adenosylmethionine	132-155	NFKB inhibitor alpha	Rattus norvegicus	166-179
15504733-1	2005	(S)-adenosylmethionine (SAM) is a critical element of melatonin synthesis as the methyl donor in the last step of the pathway, the O-methylation of N-acetyl 5-hydroxytryptamine by hydroxyindole-O-methyltransferase.	S-Adenosylmethionine	0-22	acetylserotonin O-methyltransferase	Homo sapiens	180-213
15504733-1	2005	(S)-adenosylmethionine (SAM) is a critical element of melatonin synthesis as the methyl donor in the last step of the pathway, the O-methylation of N-acetyl 5-hydroxytryptamine by hydroxyindole-O-methyltransferase.	S-Adenosylmethionine	24-27	acetylserotonin O-methyltransferase	Homo sapiens	180-213
15670956-3	2005	Methionine S-adenosyltransferase (MAT) is an enzyme involved in the synthesis of S-adenosylmethionine (SAM), a methyl donor essential for mycolipid biosynthesis.	S-Adenosylmethionine	81-101	methionine adenosyltransferase 1A	Homo sapiens	34-37
15670956-3	2005	Methionine S-adenosyltransferase (MAT) is an enzyme involved in the synthesis of S-adenosylmethionine (SAM), a methyl donor essential for mycolipid biosynthesis.	S-Adenosylmethionine	103-106	methionine adenosyltransferase 1A	Homo sapiens	0-32
15670956-3	2005	Methionine S-adenosyltransferase (MAT) is an enzyme involved in the synthesis of S-adenosylmethionine (SAM), a methyl donor essential for mycolipid biosynthesis.	S-Adenosylmethionine	103-106	methionine adenosyltransferase 1A	Homo sapiens	34-37
17150753-1	2005	Transfer RNA (Gm18) methyltransferase (TrmH, EC 2.1.1.34) catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to the 2"-OH of the ribose of guanosine at position 18 in the D-loop of tRNA.	S-Adenosylmethionine	104-127	mitochondrially encoded tRNA glycine	Homo sapiens	209-213
15671130-9	2005	Folate and vitamin B12 are major determinants of one-carbon metabolism, in which S-adenosylmethionine (SAM) is formed.	S-Adenosylmethionine	81-101	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	19-22
15671130-9	2005	Folate and vitamin B12 are major determinants of one-carbon metabolism, in which S-adenosylmethionine (SAM) is formed.	S-Adenosylmethionine	103-106	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	19-22
15607954-0	2005	S-adenosylmethionine/homocysteine cycle alterations modify DNA methylation status with consequent deregulation of PS1 and BACE and beta-amyloid production.	S-Adenosylmethionine	0-20	presenilin 1	Homo sapiens	114-117
15607954-0	2005	S-adenosylmethionine/homocysteine cycle alterations modify DNA methylation status with consequent deregulation of PS1 and BACE and beta-amyloid production.	S-Adenosylmethionine	0-20	beta-secretase 1	Homo sapiens	122-126
15607954-3	2005	It has already been shown that DNA methylation is involved in amyloid precursor protein (APP) processing and beta-amyloid (A beta) production through the regulation of Presenilin1 (PS1) expression and that exogenous S-adenosylmethionine (SAM) can silence the gene reducing A beta production.	S-Adenosylmethionine	216-236	amyloid beta precursor protein	Homo sapiens	273-279
15607954-3	2005	It has already been shown that DNA methylation is involved in amyloid precursor protein (APP) processing and beta-amyloid (A beta) production through the regulation of Presenilin1 (PS1) expression and that exogenous S-adenosylmethionine (SAM) can silence the gene reducing A beta production.	S-Adenosylmethionine	238-241	amyloid beta precursor protein	Homo sapiens	62-87
17150753-1	2005	Transfer RNA (Gm18) methyltransferase (TrmH, EC 2.1.1.34) catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to the 2"-OH of the ribose of guanosine at position 18 in the D-loop of tRNA.	S-Adenosylmethionine	129-135	mitochondrially encoded tRNA glycine	Homo sapiens	209-213
15124004-1	2004	The enzyme catechol-o-methyltransferase (COMT) transfers a methyl group from adenosylmethionine to catecholamines including the neurotransmitters dopamine, epinephrine and norepinephrine.	S-Adenosylmethionine	77-95	catechol-O-methyltransferase	Homo sapiens	11-39
15625008-5	2004	In the reaction catalyzed by Icmt, S-adenosyl-L-methionine (AdoMet) provides the methyl group that is transferred to the second substrate, the C-terminal isoprenylated cysteine residue of a CaaX protein, thereby generating a C-terminal prenylcysteine methyl ester on the protein.	S-Adenosylmethionine	35-58	isoprenylcysteine carboxyl methyltransferase	Homo sapiens	29-33
15625008-5	2004	In the reaction catalyzed by Icmt, S-adenosyl-L-methionine (AdoMet) provides the methyl group that is transferred to the second substrate, the C-terminal isoprenylated cysteine residue of a CaaX protein, thereby generating a C-terminal prenylcysteine methyl ester on the protein.	S-Adenosylmethionine	60-66	isoprenylcysteine carboxyl methyltransferase	Homo sapiens	29-33
15334060-4	2004	PRMT3 catalyses the post-translational transfer of methyl groups from S-adenosyl-L-methionine to arginine residues of proteins.	S-Adenosylmethionine	70-93	protein arginine methyltransferase 3	Homo sapiens	0-5
15566950-0	2004	Modulation of endotoxin stimulated interleukin-6 production in monocytes and Kupffer cells by S-adenosylmethionine (SAMe).	S-Adenosylmethionine	94-114	interleukin 6	Mus musculus	35-48
15642325-8	2004	The catalytic activity for CBS, which was assayed by measuring the production of C14-cystathionine from C14-serine in the presence of homocysteine, S-adenosyl-methionine and pyridoxal phosphate, was detectable in the HLE cells and transiently activated with H2O2.	S-Adenosylmethionine	148-169	cystathionine beta-synthase	Homo sapiens	27-30
15514261-1	2004	Methylenetetrahydrofolate reductase (MTHFR) catalyzes the synthesis of 5-methyltetrahydrofolate (5-methylTHF), which is used for homocysteine remethylation to methionine, the precursor of S-adenosylmethionine (SAM).	S-Adenosylmethionine	188-208	methylenetetrahydrofolate reductase	Mus musculus	0-35
15514261-1	2004	Methylenetetrahydrofolate reductase (MTHFR) catalyzes the synthesis of 5-methyltetrahydrofolate (5-methylTHF), which is used for homocysteine remethylation to methionine, the precursor of S-adenosylmethionine (SAM).	S-Adenosylmethionine	188-208	methylenetetrahydrofolate reductase	Mus musculus	37-42
15514261-1	2004	Methylenetetrahydrofolate reductase (MTHFR) catalyzes the synthesis of 5-methyltetrahydrofolate (5-methylTHF), which is used for homocysteine remethylation to methionine, the precursor of S-adenosylmethionine (SAM).	S-Adenosylmethionine	210-213	methylenetetrahydrofolate reductase	Mus musculus	0-35
15514261-1	2004	Methylenetetrahydrofolate reductase (MTHFR) catalyzes the synthesis of 5-methyltetrahydrofolate (5-methylTHF), which is used for homocysteine remethylation to methionine, the precursor of S-adenosylmethionine (SAM).	S-Adenosylmethionine	210-213	methylenetetrahydrofolate reductase	Mus musculus	37-42
15124004-1	2004	The enzyme catechol-o-methyltransferase (COMT) transfers a methyl group from adenosylmethionine to catecholamines including the neurotransmitters dopamine, epinephrine and norepinephrine.	S-Adenosylmethionine	77-95	catechol-O-methyltransferase	Homo sapiens	41-45
15252047-10	2004	The latter led to heightened metabolic flux through the polyamine pathway and an associated approximately 70% reduction in the SSAT cofactor acetyl-CoA and a approximately 40% reduction in the polyamine aminopropyl donor S-adenosylmethionine in TRAMP/SSAT compared with TRAMP prostatic tissue.	S-Adenosylmethionine	223-241	TNF receptor superfamily member 25	Homo sapiens	245-250
15379558-0	2004	Consequences of binding an S-adenosylmethionine analogue on the structure and dynamics of the thiopurine methyltransferase protein backbone.	S-Adenosylmethionine	27-47	thiopurine S-methyltransferase	Homo sapiens	94-122
15379558-4	2004	Addition of the cosubstrate, S-adenosylmethionine (SAM), prevents degradation of the TPMT polymorphs in experimental assays, presumably by stabilizing the native structure.	S-Adenosylmethionine	29-49	thiopurine S-methyltransferase	Homo sapiens	85-89
15252047-10	2004	The latter led to heightened metabolic flux through the polyamine pathway and an associated approximately 70% reduction in the SSAT cofactor acetyl-CoA and a approximately 40% reduction in the polyamine aminopropyl donor S-adenosylmethionine in TRAMP/SSAT compared with TRAMP prostatic tissue.	S-Adenosylmethionine	223-241	spermidine/spermine N1-acetyltransferase 1	Homo sapiens	251-255
15252047-10	2004	The latter led to heightened metabolic flux through the polyamine pathway and an associated approximately 70% reduction in the SSAT cofactor acetyl-CoA and a approximately 40% reduction in the polyamine aminopropyl donor S-adenosylmethionine in TRAMP/SSAT compared with TRAMP prostatic tissue.	S-Adenosylmethionine	223-241	TNF receptor superfamily member 25	Homo sapiens	270-275
15219714-2	2004	Previous studies have shown that mice deficient in the gene encoding this enzyme (Pcmt1-/-) accumulate damaged proteins, have altered levels of brain S-adenosylmethionine (AdoMet) and S-adenosylhomocysteine (AdoHcy), and suffer from epileptic seizures that result in death at an average age of about 42 days.	S-Adenosylmethionine	150-170	protein-L-isoaspartate (D-aspartate) O-methyltransferase 1	Mus musculus	82-87
15064230-0	2004	Inhibition of lipopolysaccharide-stimulated TNF-alpha promoter activity by S-adenosylmethionine and 5"-methylthioadenosine.	S-Adenosylmethionine	75-95	tumor necrosis factor	Homo sapiens	44-53
15250699-1	2004	Secondary alpha-D3 kinetic isotope effects calculated by the hybrid AM1/TIP3P/CHARMM method for the reaction of S-adenosylmethionine with catecholate anion in aqueous solution and catalyzed by rat liver catechol O-methyltransferase at 298 K are 0.94 and 0.85, respectively, in good accord with experiment.	S-Adenosylmethionine	112-132	catechol-O-methyltransferase	Rattus norvegicus	203-231
15270685-0	2004	Autoregulation of the gene for cystathionine gamma-synthase in Arabidopsis: post-transcriptional regulation induced by S-adenosylmethionine.	S-Adenosylmethionine	119-139	Pyridoxal phosphate (PLP)-dependent transferases superfamily protein	Arabidopsis thaliana	31-59
15150277-5	2004	Treatment of MDA-231 cells with AdoMet, but not its unmethylated analogue S-adenosylhomocysteine, significantly inhibits uPA expression and tumor cell invasion in vitro and tumor growth and metastasis in vivo.	S-Adenosylmethionine	32-38	proline rich acidic protein 1	Homo sapiens	121-124
15239106-0	2004	S-adenosylmethionine and its metabolite induce apoptosis in HepG2 cells: Role of protein phosphatase 1 and Bcl-x(S).	S-Adenosylmethionine	0-20	inorganic pyrophosphatase 1	Homo sapiens	81-102
15225602-8	2004	The identification of an additional methyltransferase domain at the C-terminus of one of the Lsm12 proteins also led to the recognition of three new groups of methyltransferases, presumably dependent on S-adenosyl-l-methionine.	S-Adenosylmethionine	205-226	Lsm12p	Saccharomyces cerevisiae S288C	93-98
15239106-0	2004	S-adenosylmethionine and its metabolite induce apoptosis in HepG2 cells: Role of protein phosphatase 1 and Bcl-x(S).	S-Adenosylmethionine	0-20	BCL2 like 1	Homo sapiens	107-112
15181470-4	2004	Glycine N-methyltransferase exhibits Michaelis-Menten kinetics for its substrates, S-adenosylmethionine and glycine, respectively.	S-Adenosylmethionine	83-103	glycine N-methyltransferase	Oryctolagus cuniculus	0-27
15205391-6	2004	Incubation of MLB, M1, M2, or M4 in rat hepatic cytosol in the presence of S-adenosyl-l-methionine demonstrated the formation of all four metabolites, which indicated that the enzyme responsible for the biotransformation is catechol O-methyltransferase.	S-Adenosylmethionine	75-98	catechol-O-methyltransferase	Rattus norvegicus	224-252
15181470-9	2004	Based on the kinetic data glycine N-methyltransferase from rabbit liver exhibits appreciable activity at physiological S-adenosylmethionine and S-adenosylhomocysteine levels.	S-Adenosylmethionine	119-139	glycine N-methyltransferase	Oryctolagus cuniculus	26-53
14630804-5	2004	With the control diet, the S-adenosylmethionine (SAM) to S-adenosylhomocysteine (SAH) ratio was lower in the liver and brain of Mthfr(+/-) mice than Mthfr(+/+) mice (P<.05).	S-Adenosylmethionine	27-47	methylenetetrahydrofolate reductase	Mus musculus	128-133
15150120-1	2004	Glycine N-methyltransferase (GNMT) affects genetic stability by (a) regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine and (b) binding to folate.	S-Adenosylmethionine	92-112	glycine N-methyltransferase	Homo sapiens	0-27
15150120-1	2004	Glycine N-methyltransferase (GNMT) affects genetic stability by (a) regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine and (b) binding to folate.	S-Adenosylmethionine	92-112	glycine N-methyltransferase	Homo sapiens	29-33
15150120-7	2004	Automated BaP docking using a Lamarckian genetic algorithm with GNMT X-ray crystallography revealed a BaP preference for the S-adenosylmethionine-binding domain of the dimeric form of GNMT, a novel finding of a cellular defense against potentially damaging exposures.	S-Adenosylmethionine	127-145	glycine N-methyltransferase	Homo sapiens	64-68
15150120-7	2004	Automated BaP docking using a Lamarckian genetic algorithm with GNMT X-ray crystallography revealed a BaP preference for the S-adenosylmethionine-binding domain of the dimeric form of GNMT, a novel finding of a cellular defense against potentially damaging exposures.	S-Adenosylmethionine	127-145	glycine N-methyltransferase	Homo sapiens	184-188
15063092-10	2004	The concentrations of S-adenosylmethionine (up 21%; p<0.05) and methylation of DNA (up 46%) and proteins (up 12%; p<0.01) in hippocampus were significantly increased in Pemt-/- mice, suggesting that increased S-adenosylmethionine availability may mediate the observed developmental changes.	S-Adenosylmethionine	22-42	phosphatidylethanolamine N-methyltransferase	Mus musculus	175-179
15033934-1	2004	Methionine adenosyltransferase (MAT) is an essential enzyme because it catalyzes the formation of S-adenosylmethionine (SAMe), the principal biological methyl donor.	S-Adenosylmethionine	98-118	methionine adenosyltransferase 1A	Homo sapiens	32-35
14630804-5	2004	With the control diet, the S-adenosylmethionine (SAM) to S-adenosylhomocysteine (SAH) ratio was lower in the liver and brain of Mthfr(+/-) mice than Mthfr(+/+) mice (P<.05).	S-Adenosylmethionine	49-52	methylenetetrahydrofolate reductase	Mus musculus	128-133
14630804-5	2004	With the control diet, the S-adenosylmethionine (SAM) to S-adenosylhomocysteine (SAH) ratio was lower in the liver and brain of Mthfr(+/-) mice than Mthfr(+/+) mice (P<.05).	S-Adenosylmethionine	49-52	methylenetetrahydrofolate reductase	Mus musculus	149-154
14660564-5	2004	The complexes with the S-adenosyl-l-methionine methyl donor and the S-adenosyl-l-homocysteine product and inhibitor unambiguously revealed the co-substrate binding site and provided a convincing hypothesis for the PP2A C-terminal peptide binding site.	S-Adenosylmethionine	23-46	neuropeptide Y receptor Y6 (pseudogene)	Homo sapiens	214-217
14983000-10	2004	We propose that functional heterodimerization enhances the isozyme diversity of the ACS gene family and provides physiological versatility by being able to operate in a broad gradient of S-adenosylmethionine concentration in various cells/tissues during plant growth and development.	S-Adenosylmethionine	187-207	1-amino-cyclopropane-1-carboxylate synthase 2	Arabidopsis thaliana	84-87
14967023-1	2004	S-Adenosylmethionine synthetase (MAT) catalyzes formation of S-adenosylmethionine (SAM) from ATP and l-methionine (Met) and hydrolysis of tripolyphosphate to PP(i) and P(i).	S-Adenosylmethionine	61-81	methionine adenosyltransferase 1A	Rattus norvegicus	0-31
14596598-1	2003	Protein L-isoaspartyl methyltransferases (PIMT; EC 2.1.1.77) catalyze the S-adenosylmethionine-dependent methylation of L-isoaspartyl residues that arise spontaneously in proteins with age, thereby initiating a repair process that restores the normal backbone configuration to the damaged polypeptide.	S-Adenosylmethionine	76-94	Protein-L-isoaspartate (D-aspartate) O-methyltransferase	Drosophila melanogaster	0-40
14652353-1	2003	Glycine N-methyltransferase (GNMT) regulates the methyl group supply for S-adenosylmethionine-dependent transmethylation reactions.	S-Adenosylmethionine	75-93	glycine N-methyltransferase	Rattus norvegicus	0-27
14652353-1	2003	Glycine N-methyltransferase (GNMT) regulates the methyl group supply for S-adenosylmethionine-dependent transmethylation reactions.	S-Adenosylmethionine	75-93	glycine N-methyltransferase	Rattus norvegicus	29-33
14609944-2	2003	Here the identification of the mitochondrial carrier for S-adenosylmethionine (SAM) Sam5p is described.	S-Adenosylmethionine	57-77	Pet8p	Saccharomyces cerevisiae S288C	84-89
14709722-1	2004	The expression of genes for S-adenosylmethionine synthetase (SAMS), which catalyzes the synthesis of S-adenosylmethionine (AdoMet), a major methyl donor in cells, was studied in symbiont-free (D) and symbiont-bearing (xD) amoeba strains to determine the effect of bacterial endosymbionts.	S-Adenosylmethionine	28-48	methionine adenosyltransferase 1A	Homo sapiens	61-65
14709722-1	2004	The expression of genes for S-adenosylmethionine synthetase (SAMS), which catalyzes the synthesis of S-adenosylmethionine (AdoMet), a major methyl donor in cells, was studied in symbiont-free (D) and symbiont-bearing (xD) amoeba strains to determine the effect of bacterial endosymbionts.	S-Adenosylmethionine	123-129	methionine adenosyltransferase 1A	Homo sapiens	28-59
14709722-1	2004	The expression of genes for S-adenosylmethionine synthetase (SAMS), which catalyzes the synthesis of S-adenosylmethionine (AdoMet), a major methyl donor in cells, was studied in symbiont-free (D) and symbiont-bearing (xD) amoeba strains to determine the effect of bacterial endosymbionts.	S-Adenosylmethionine	123-129	methionine adenosyltransferase 1A	Homo sapiens	61-65
14530285-2	2003	Two genes (MAT1A and MAT2A) encode for methionine adenosyltransferase (MAT), an essential cellular enzyme responsible for S-adenosylmethionine biosynthesis.	S-Adenosylmethionine	122-142	methionine adenosyltransferase 1A	Homo sapiens	11-16
14530285-2	2003	Two genes (MAT1A and MAT2A) encode for methionine adenosyltransferase (MAT), an essential cellular enzyme responsible for S-adenosylmethionine biosynthesis.	S-Adenosylmethionine	122-142	methionine adenosyltransferase 2A	Homo sapiens	21-26
14611810-8	2003	Compared with wild-type mice, hepatocyte RXRalpha-deficient mice have significant lower levels of S-adenosylmethionine and glutathione, which is further reduced after alcohol treatment, and that may account for severe liver injury induced by alcohol.	S-Adenosylmethionine	98-118	retinoid X receptor alpha	Mus musculus	41-49
14609944-2	2003	Here the identification of the mitochondrial carrier for S-adenosylmethionine (SAM) Sam5p is described.	S-Adenosylmethionine	79-82	Pet8p	Saccharomyces cerevisiae S288C	84-89
14596598-1	2003	Protein L-isoaspartyl methyltransferases (PIMT; EC 2.1.1.77) catalyze the S-adenosylmethionine-dependent methylation of L-isoaspartyl residues that arise spontaneously in proteins with age, thereby initiating a repair process that restores the normal backbone configuration to the damaged polypeptide.	S-Adenosylmethionine	76-94	Protein-L-isoaspartate (D-aspartate) O-methyltransferase	Drosophila melanogaster	42-46
12964806-3	2003	Vitamin B12 and folate also play important roles in DNA methylation since these two coenzymes are required for the synthesis of methionine and S-adenosyl methionine, the common methyl donor required for the maintenance of methylation patterns in DNA.	S-Adenosylmethionine	143-164	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	8-11
14556746-6	2003	Bacterial TPMT similarly catalyzes the S-adenosylmethionine (SAM)-dependent transmethylation of 6-TPs and shares 45% similarity (33% identity) with the human enzyme.	S-Adenosylmethionine	39-59	thiopurine S-methyltransferase	Homo sapiens	10-14
14556746-6	2003	Bacterial TPMT similarly catalyzes the S-adenosylmethionine (SAM)-dependent transmethylation of 6-TPs and shares 45% similarity (33% identity) with the human enzyme.	S-Adenosylmethionine	61-64	thiopurine S-methyltransferase	Homo sapiens	10-14
12910461-1	2003	S-adenosylhomocysteine hydrolase (SAHH) is a key regulator of S-adenosylmethionine-dependent methylation reactions and an interesting pharmacologic target.	S-Adenosylmethionine	64-82	adenosylhomocysteinase	Homo sapiens	34-38
14981985-6	2003	RESULTS: AST, ALT and LDH levels recorded at the moment of the recognition of liver toxicity were significantly reduced after one week of AdoMet therapy (respectively p: 0.009, 0.0005 and 0.012).	S-Adenosylmethionine	138-144	solute carrier family 17 member 5	Homo sapiens	9-12
14608049-2	2003	Glycine N-methyltransferase (GNMT) is a key protein that functions to regulate the supply and utilization of methyl groups for S-adenosylmethionine (SAM)-dependent transmethylation reactions.	S-Adenosylmethionine	127-147	glycine N-methyltransferase	Rattus norvegicus	0-27
14608049-2	2003	Glycine N-methyltransferase (GNMT) is a key protein that functions to regulate the supply and utilization of methyl groups for S-adenosylmethionine (SAM)-dependent transmethylation reactions.	S-Adenosylmethionine	127-147	glycine N-methyltransferase	Rattus norvegicus	29-33
14608049-2	2003	Glycine N-methyltransferase (GNMT) is a key protein that functions to regulate the supply and utilization of methyl groups for S-adenosylmethionine (SAM)-dependent transmethylation reactions.	S-Adenosylmethionine	149-152	glycine N-methyltransferase	Rattus norvegicus	0-27
14608049-2	2003	Glycine N-methyltransferase (GNMT) is a key protein that functions to regulate the supply and utilization of methyl groups for S-adenosylmethionine (SAM)-dependent transmethylation reactions.	S-Adenosylmethionine	149-152	glycine N-methyltransferase	Rattus norvegicus	29-33
14508388-2	2003	This paper describe a new simple, nonradioactive HPLC method for determination of TPMT activity in isolated erythrocytes (Ery), based on the conversion of 6-mercaptopurine (pH 7.5, 37 degrees C) to 6-methylmercaptopurine (6-MMP) using S-adenosyl-l-methionine as methyl donor.	S-Adenosylmethionine	235-258	thiopurine S-methyltransferase	Homo sapiens	82-86
12842883-0	2003	Molecular dissection of the S-adenosylmethionine-binding site of phosphatidylethanolamine N-methyltransferase.	S-Adenosylmethionine	28-48	phosphatidylethanolamine N-methyltransferase	Homo sapiens	65-109
12842883-4	2003	To gain insight into the PEMT transmethylation reaction and the mechanism by which PEMT regulates homocysteine levels, we sought to define residues that are required for binding of the methyl group donor, S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	205-225	phosphatidylethanolamine N-methyltransferase	Homo sapiens	25-29
12842883-4	2003	To gain insight into the PEMT transmethylation reaction and the mechanism by which PEMT regulates homocysteine levels, we sought to define residues that are required for binding of the methyl group donor, S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	205-225	phosphatidylethanolamine N-methyltransferase	Homo sapiens	83-87
12842883-4	2003	To gain insight into the PEMT transmethylation reaction and the mechanism by which PEMT regulates homocysteine levels, we sought to define residues that are required for binding of the methyl group donor, S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	227-233	phosphatidylethanolamine N-methyltransferase	Homo sapiens	25-29
12842883-4	2003	To gain insight into the PEMT transmethylation reaction and the mechanism by which PEMT regulates homocysteine levels, we sought to define residues that are required for binding of the methyl group donor, S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	227-233	phosphatidylethanolamine N-methyltransferase	Homo sapiens	83-87
12842102-2	2003	In this method, the methyl group of S-adenosyl-L-methionine was enzymatically transferred to esculetin with the aid of catechol-O-methyltransferase and then the resulting scopoletin was extracted with n-hexane:ethyl acetate (7:3, v/v) and measured by high-performance liquid chromatography with Si 60 column and fluorometric detection with excitation and emission wavelengths at 347 and 415 nm, respectively.	S-Adenosylmethionine	36-59	catechol-O-methyltransferase	Homo sapiens	119-147
12897151-5	2003	In addition, point mutations in conserved methyltransferase motifs of h-mtTFB1 revealed that it stimulates transcription in vitro independently of S-adenosylmethionine binding and rRNA methyltransferase activity.	S-Adenosylmethionine	147-167	transcription factor B1, mitochondrial	Homo sapiens	70-78
12736147-0	2003	S-adenosylmethionine (AdoMet) modulates endotoxin stimulated interleukin-10 production in monocytes.	S-Adenosylmethionine	0-20	methionine adenosyltransferase I, alpha	Mus musculus	22-28
12859184-2	2003	Glycine N-methyltransferase (GNMT) catalyzes the S-adenosyl-l-methionine- (SAM-) dependent methylation of glycine to form sarcosine.	S-Adenosylmethionine	51-72	glycine N-methyltransferase	Homo sapiens	0-27
12859184-2	2003	Glycine N-methyltransferase (GNMT) catalyzes the S-adenosyl-l-methionine- (SAM-) dependent methylation of glycine to form sarcosine.	S-Adenosylmethionine	51-72	glycine N-methyltransferase	Homo sapiens	29-33
12697024-1	2003	Glycine N-methyltransferase (GNMT) is an abundant cytosolic enzyme that catalyses the methylation of glycine into sarcosine, coupled with conversion of the methyl donor, S -adenosylmethionine (AdoMet), into S -adenosylhomocysteine (AdoHcy).	S-Adenosylmethionine	170-191	glycine N-methyltransferase	Homo sapiens	0-27
12697024-1	2003	Glycine N-methyltransferase (GNMT) is an abundant cytosolic enzyme that catalyses the methylation of glycine into sarcosine, coupled with conversion of the methyl donor, S -adenosylmethionine (AdoMet), into S -adenosylhomocysteine (AdoHcy).	S-Adenosylmethionine	170-191	glycine N-methyltransferase	Homo sapiens	29-33
12697024-1	2003	Glycine N-methyltransferase (GNMT) is an abundant cytosolic enzyme that catalyses the methylation of glycine into sarcosine, coupled with conversion of the methyl donor, S -adenosylmethionine (AdoMet), into S -adenosylhomocysteine (AdoHcy).	S-Adenosylmethionine	193-199	glycine N-methyltransferase	Homo sapiens	0-27
12697024-1	2003	Glycine N-methyltransferase (GNMT) is an abundant cytosolic enzyme that catalyses the methylation of glycine into sarcosine, coupled with conversion of the methyl donor, S -adenosylmethionine (AdoMet), into S -adenosylhomocysteine (AdoHcy).	S-Adenosylmethionine	193-199	glycine N-methyltransferase	Homo sapiens	29-33
12736147-0	2003	S-adenosylmethionine (AdoMet) modulates endotoxin stimulated interleukin-10 production in monocytes.	S-Adenosylmethionine	0-20	interleukin 10	Mus musculus	61-75
12736147-3	2003	Intracellular deficiency of S-adenosylmethionine (AdoMet) is a hallmark of toxin-induced liver injury.	S-Adenosylmethionine	28-48	methionine adenosyltransferase I, alpha	Mus musculus	50-56
12671891-1	2003	BACKGROUND & AIMS: Of the 2 genes (MAT1A, MAT2A) encoding methionine adenosyltransferase, the enzyme that synthesizes S-adenosylmethionine, MAT1A, is expressed in liver, whereas MAT2A is expressed in extrahepatic tissues.	S-Adenosylmethionine	122-142	methionine adenosyltransferase 1A	Homo sapiens	39-44
12756332-5	2003	This assay is based on the fact that the Hmt1 enzyme utilizes S-Adenosyl-L-methionine as the methyl donor for protein arginine methylation.	S-Adenosylmethionine	62-85	ALG1 chitobiosyldiphosphodolichol beta-mannosyltransferase	Homo sapiens	41-45
12660248-1	2003	In mammals, methionine adenosyltransferase (MAT), the enzyme responsible for S-adenosylmethionine (AdoMet) synthesis, is encoded by two genes, MAT1A and MAT2A.	S-Adenosylmethionine	77-97	methionine adenosyltransferase 1A	Homo sapiens	12-42
12660248-1	2003	In mammals, methionine adenosyltransferase (MAT), the enzyme responsible for S-adenosylmethionine (AdoMet) synthesis, is encoded by two genes, MAT1A and MAT2A.	S-Adenosylmethionine	77-97	methionine adenosyltransferase 1A	Homo sapiens	44-47
12660248-1	2003	In mammals, methionine adenosyltransferase (MAT), the enzyme responsible for S-adenosylmethionine (AdoMet) synthesis, is encoded by two genes, MAT1A and MAT2A.	S-Adenosylmethionine	77-97	methionine adenosyltransferase 1A	Homo sapiens	143-148
12660248-1	2003	In mammals, methionine adenosyltransferase (MAT), the enzyme responsible for S-adenosylmethionine (AdoMet) synthesis, is encoded by two genes, MAT1A and MAT2A.	S-Adenosylmethionine	77-97	methionine adenosyltransferase 2A	Homo sapiens	153-158
12660248-1	2003	In mammals, methionine adenosyltransferase (MAT), the enzyme responsible for S-adenosylmethionine (AdoMet) synthesis, is encoded by two genes, MAT1A and MAT2A.	S-Adenosylmethionine	99-105	methionine adenosyltransferase 1A	Homo sapiens	12-42
12660248-1	2003	In mammals, methionine adenosyltransferase (MAT), the enzyme responsible for S-adenosylmethionine (AdoMet) synthesis, is encoded by two genes, MAT1A and MAT2A.	S-Adenosylmethionine	99-105	methionine adenosyltransferase 1A	Homo sapiens	44-47
12660248-1	2003	In mammals, methionine adenosyltransferase (MAT), the enzyme responsible for S-adenosylmethionine (AdoMet) synthesis, is encoded by two genes, MAT1A and MAT2A.	S-Adenosylmethionine	99-105	methionine adenosyltransferase 1A	Homo sapiens	143-148
12660248-1	2003	In mammals, methionine adenosyltransferase (MAT), the enzyme responsible for S-adenosylmethionine (AdoMet) synthesis, is encoded by two genes, MAT1A and MAT2A.	S-Adenosylmethionine	99-105	methionine adenosyltransferase 2A	Homo sapiens	153-158
12660248-5	2003	Restoration of l-methionine rapidly down-regulates MAT2A mRNA levels; for this effect, l-methionine needs to be converted into AdoMet.	S-Adenosylmethionine	127-133	methionine adenosyltransferase 2A	Homo sapiens	51-56
12706835-0	2003	Presenilin 1 gene silencing by S-adenosylmethionine: a treatment for Alzheimer disease?	S-Adenosylmethionine	31-51	presenilin 1	Homo sapiens	0-12
12706835-4	2003	Here we report that SAM administration, in human neuroblastoma SK-N-SH cell cultures, downregulates PS1 gene expression and Ab production.	S-Adenosylmethionine	20-23	presenilin 1	Homo sapiens	100-103
12702816-6	2003	Yeast Trm10p purified from E. coli quantitatively modifies the G(9) position of tRNA(Gly) in an S-adenosylmethionine-dependent fashion.	S-Adenosylmethionine	96-116	tRNA (guanine(9)-N(1))-methyltransferase	Saccharomyces cerevisiae S288C	6-12
12671891-1	2003	BACKGROUND & AIMS: Of the 2 genes (MAT1A, MAT2A) encoding methionine adenosyltransferase, the enzyme that synthesizes S-adenosylmethionine, MAT1A, is expressed in liver, whereas MAT2A is expressed in extrahepatic tissues.	S-Adenosylmethionine	122-142	methionine adenosyltransferase 2A	Homo sapiens	182-187
12671891-1	2003	BACKGROUND & AIMS: Of the 2 genes (MAT1A, MAT2A) encoding methionine adenosyltransferase, the enzyme that synthesizes S-adenosylmethionine, MAT1A, is expressed in liver, whereas MAT2A is expressed in extrahepatic tissues.	S-Adenosylmethionine	122-142	methionine adenosyltransferase 2A	Homo sapiens	46-51
12671891-1	2003	BACKGROUND & AIMS: Of the 2 genes (MAT1A, MAT2A) encoding methionine adenosyltransferase, the enzyme that synthesizes S-adenosylmethionine, MAT1A, is expressed in liver, whereas MAT2A is expressed in extrahepatic tissues.	S-Adenosylmethionine	122-142	methionine adenosyltransferase 1A	Homo sapiens	144-149
12641227-8	2003	SAM molecules can also be removed from the tip apex by application of a negative sample bias (-2.0 V for 0.5-10 min) making it possible to alternate between conventional STM images and STM images with chemically enhanced contrasts.	S-Adenosylmethionine	0-3	sulfotransferase family 1A member 3	Homo sapiens	170-173
12628190-3	2003	We have solved a 2.5 A resolution structure of the catalytic domain of human Dot1, hDOT1L, in complex with S-adenosyl-L-methionine (SAM).	S-Adenosylmethionine	107-130	DOT1 like histone lysine methyltransferase	Homo sapiens	77-81
12628190-3	2003	We have solved a 2.5 A resolution structure of the catalytic domain of human Dot1, hDOT1L, in complex with S-adenosyl-L-methionine (SAM).	S-Adenosylmethionine	107-130	DOT1 like histone lysine methyltransferase	Homo sapiens	83-89
12641227-8	2003	SAM molecules can also be removed from the tip apex by application of a negative sample bias (-2.0 V for 0.5-10 min) making it possible to alternate between conventional STM images and STM images with chemically enhanced contrasts.	S-Adenosylmethionine	0-3	sulfotransferase family 1A member 3	Homo sapiens	185-188
12466265-3	2003	One of gene products (ORF1) catalyzed the methylation reactions of glycine and sarcosine with S-adenosylmethionine acting as the methyl donor.	S-Adenosylmethionine	94-114	ORF1	Homo sapiens	22-26
12801808-5	2003	The two pathways are coordinated by S-adenosylmethionine which acts as an allosteric inhibitor of the methylenetetrahydrofolate reductase (MTHFR) and as an activator of cystathionine beta-synthase (CBS).	S-Adenosylmethionine	36-56	methylenetetrahydrofolate reductase	Homo sapiens	102-137
12801808-5	2003	The two pathways are coordinated by S-adenosylmethionine which acts as an allosteric inhibitor of the methylenetetrahydrofolate reductase (MTHFR) and as an activator of cystathionine beta-synthase (CBS).	S-Adenosylmethionine	36-56	methylenetetrahydrofolate reductase	Homo sapiens	139-144
12801808-5	2003	The two pathways are coordinated by S-adenosylmethionine which acts as an allosteric inhibitor of the methylenetetrahydrofolate reductase (MTHFR) and as an activator of cystathionine beta-synthase (CBS).	S-Adenosylmethionine	36-56	cystathionine beta-synthase	Homo sapiens	169-196
12466265-10	2003	The changes of amino acids Arg-169 to Lys or Glu in ORF1 and Pro-171 to Gln and/or Met-172 to Arg in ORF2 significantly decreased V(max) and increased K(m) for methyl acceptors (glycine, sarcosine, and dimethylglycine) but modestly affected K(m) for S-adenosylmethionine, indicating the importance of these amino acids for the binding of methyl acceptors.	S-Adenosylmethionine	250-270	ORF1	Homo sapiens	52-56
12431977-2	2003	Phosphatidylethanolamine N-methyltransferase (PEMT) catalyzes each transmethylation reaction, and S-adenosylmethionine is the methyl group donor.	S-Adenosylmethionine	98-118	phosphatidylethanolamine N-methyltransferase	Homo sapiens	0-44
12431977-2	2003	Phosphatidylethanolamine N-methyltransferase (PEMT) catalyzes each transmethylation reaction, and S-adenosylmethionine is the methyl group donor.	S-Adenosylmethionine	98-118	phosphatidylethanolamine N-methyltransferase	Homo sapiens	46-50
12514135-2	2003	Here, we report two crystal structures of SET7/9, a histone methyltransferase (HMTase) that transfers methyl groups to Lys4 of histone H3, in complex with S-adenosyl-L-methionine (AdoMet) determined at 1.7 and 2.3 A resolution.	S-Adenosylmethionine	155-178	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	42-48
12514135-2	2003	Here, we report two crystal structures of SET7/9, a histone methyltransferase (HMTase) that transfers methyl groups to Lys4 of histone H3, in complex with S-adenosyl-L-methionine (AdoMet) determined at 1.7 and 2.3 A resolution.	S-Adenosylmethionine	180-186	SET domain containing 7, histone lysine methyltransferase	Homo sapiens	42-48
12533089-3	2003	However, patients with Parkinson disease (PD) may have elevated homocysteine levels resulting from methylation of levodopa and dopamine by catechol O-methyltransferase, an enzyme that uses S-adenosylmethionine as a methyl donor and yields S-adenosylhomocysteine.	S-Adenosylmethionine	189-209	catechol-O-methyltransferase	Homo sapiens	139-167
12674502-1	2003	S-Adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme of the polyamine synthetic pathway providing decarboxylated S-adenosylmethionine for the formation of spermidine and spermine, respectively.	S-Adenosylmethionine	122-142	adenosylmethionine decarboxylase 1	Homo sapiens	36-44
12205086-5	2002	The resulting increased activity of AdoMetDC caused disruption to polyamine levels with depletion of putrescine, reduction of spermine levels, and a more than 400-fold increase in the level of decarboxylated S-adenosylmethionine.	S-Adenosylmethionine	208-228	S-adenosylmethionine decarboxylase proenzyme	Nicotiana tabacum	36-44
12450669-1	2002	Catechol O-methyltransferase (COMT) transfers a methyl group from S-adenosyl-L-methionine to the catechol substrate in the presence of magnesium.	S-Adenosylmethionine	66-89	catechol-O-methyltransferase	Homo sapiens	0-28
12450669-1	2002	Catechol O-methyltransferase (COMT) transfers a methyl group from S-adenosyl-L-methionine to the catechol substrate in the presence of magnesium.	S-Adenosylmethionine	66-89	catechol-O-methyltransferase	Homo sapiens	30-34
14564626-2	2003	DNA (cytosine-5)-methyltransferase (DNMT) catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (SAM) to C5 of cytosine within CpG dinucleotide sequences in the genomic DNA of higher eukaryotes.	S-Adenosylmethionine	88-111	DNA methyltransferase 1	Homo sapiens	36-40
12355263-1	2002	MT-A70 is the S-adenosylmethionine-binding subunit of human mRNA:m(6)A methyl-transferase (MTase), an enzyme that sequence-specifically methylates adenines in pre-mRNAs.	S-Adenosylmethionine	16-34	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	0-6
12228189-7	2002	MTD was a substrate for TPMT-catalyzed S-methylation, with an apparent K(m) value of 63 micro M. Recombinant TPMT, with [(14)C-methyl]S-adenosyl-L-methionine as a cosubstrate, was then used to radioactively label a methyl acceptor substrate present in liver and kidney cytosol preparations from patients who had been treated preoperatively with cefazolin.	S-Adenosylmethionine	136-157	thiopurine S-methyltransferase	Homo sapiens	24-28
12228189-7	2002	MTD was a substrate for TPMT-catalyzed S-methylation, with an apparent K(m) value of 63 micro M. Recombinant TPMT, with [(14)C-methyl]S-adenosyl-L-methionine as a cosubstrate, was then used to radioactively label a methyl acceptor substrate present in liver and kidney cytosol preparations from patients who had been treated preoperatively with cefazolin.	S-Adenosylmethionine	136-157	thiopurine S-methyltransferase	Homo sapiens	109-113
12161434-0	2002	Cytoplasmic serine hydroxymethyltransferase mediates competition between folate-dependent deoxyribonucleotide and S-adenosylmethionine biosyntheses.	S-Adenosylmethionine	114-134	serine hydroxymethyltransferase 1	Homo sapiens	0-43
12237326-6	2002	BIA 3-335 was found to act as a potent, reversible, tight-binding inhibitor of COMT with a K(i) of 6.0 +/- 1.6 nM and displaying a competitive inhibition toward the substrate binding site and uncompetitive inhibition toward the S-adenosyl-L-methionine (SAM) binding site.	S-Adenosylmethionine	228-251	catechol-O-methyltransferase	Rattus norvegicus	79-83
12215523-6	2002	We show that purified snoRNPs are able to reproduce the site-specific methylation pattern on target RNA and that the predicted S-adenosyl-L-methionine-binding region of Nop1p is responsible for the catalytic activity.	S-Adenosylmethionine	129-150	rRNA methyltransferase NOP1	Saccharomyces cerevisiae S288C	169-174
12237326-6	2002	BIA 3-335 was found to act as a potent, reversible, tight-binding inhibitor of COMT with a K(i) of 6.0 +/- 1.6 nM and displaying a competitive inhibition toward the substrate binding site and uncompetitive inhibition toward the S-adenosyl-L-methionine (SAM) binding site.	S-Adenosylmethionine	253-256	catechol-O-methyltransferase	Rattus norvegicus	79-83
12023972-2	2002	In the course of this reaction, PCMT1 converts the methyl donor S-adenosylmethionine (AdoMet) to S-adenosylhomocysteine (AdoHcy).	S-Adenosylmethionine	64-84	protein-L-isoaspartate (D-aspartate) O-methyltransferase	Homo sapiens	32-37
12403464-3	2002	ORF YDL201w encodes Trm8, a protein that is highly conserved in prokaryotes and eukaryotes and that contains an S-adenosylmethionine binding domain.	S-Adenosylmethionine	112-132	tRNA (guanine46-N7)-methyltransferase	Saccharomyces cerevisiae S288C	20-24
12221207-1	2002	Glycine N-methyltransferase (GNMT) regulates S-adenosylmethionine (SAM) levels and the ratio of SAM:S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	45-65	glycine N-methyltransferase	Rattus norvegicus	0-27
12221207-1	2002	Glycine N-methyltransferase (GNMT) regulates S-adenosylmethionine (SAM) levels and the ratio of SAM:S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	45-65	glycine N-methyltransferase	Rattus norvegicus	29-33
12221207-1	2002	Glycine N-methyltransferase (GNMT) regulates S-adenosylmethionine (SAM) levels and the ratio of SAM:S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	67-70	glycine N-methyltransferase	Rattus norvegicus	0-27
12221207-1	2002	Glycine N-methyltransferase (GNMT) regulates S-adenosylmethionine (SAM) levels and the ratio of SAM:S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	67-70	glycine N-methyltransferase	Rattus norvegicus	29-33
12023972-2	2002	In the course of this reaction, PCMT1 converts the methyl donor S-adenosylmethionine (AdoMet) to S-adenosylhomocysteine (AdoHcy).	S-Adenosylmethionine	86-92	protein-L-isoaspartate (D-aspartate) O-methyltransferase	Homo sapiens	32-37
12060674-3	2002	Mice lacking MAT1A have reduced hepatic S-adenosylmethionine content and hyperplasia and spontaneously develop nonalcoholic steatohepatitis.	S-Adenosylmethionine	42-60	methionine adenosyltransferase I, alpha	Mus musculus	13-18
12163711-6	2002	FA-induced hypomethylation is most likely due to its ability to inhibit the enzyme glycine hydroxymethyltransferase, thereby inhibiting the homocysteine remethylation cycle necessary to regenerate S-adenosylmethionine, the methyl donor for DNA methyltransferases.	S-Adenosylmethionine	197-217	serine hydroxymethyltransferase 2	Homo sapiens	83-115
12163655-0	2002	In the cystathionine beta-synthase knockout mouse, elevations in total plasma homocysteine increase tissue S-adenosylhomocysteine, but responses of S-adenosylmethionine and DNA methylation are tissue specific.	S-Adenosylmethionine	148-168	cystathionine beta-synthase	Mus musculus	7-34
12115739-8	2002	The intracellular level of the CBS regulator compound, S-adenosylmethionine, was found to reflect the proliferation status of both yeast and human cells, and as such, constitutes an additional mechanism for proliferation-specific regulation of human CBS.	S-Adenosylmethionine	55-75	cystathionine beta-synthase	Homo sapiens	31-34
12163143-12	2002	If SAM levels also decrease in these cells, this may contribute to the induction of tumor necrosis factor (TNF) expression and release.	S-Adenosylmethionine	3-6	tumor necrosis factor	Homo sapiens	84-105
12163143-12	2002	If SAM levels also decrease in these cells, this may contribute to the induction of tumor necrosis factor (TNF) expression and release.	S-Adenosylmethionine	3-6	tumor necrosis factor	Homo sapiens	107-110
12163148-1	2002	Hepatic deficiency of S-adenosylmethionine (AdoMet) is a critical acquired metabolic abnormality in alcoholic liver disease (ALD) and in many experimental models of hepatotoxicity.	S-Adenosylmethionine	22-42	methionine adenosyltransferase 1A	Rattus norvegicus	44-50
12115739-8	2002	The intracellular level of the CBS regulator compound, S-adenosylmethionine, was found to reflect the proliferation status of both yeast and human cells, and as such, constitutes an additional mechanism for proliferation-specific regulation of human CBS.	S-Adenosylmethionine	55-75	cystathionine beta-synthase	Homo sapiens	250-253
12007221-5	2002	We describe a novel class of missense mutations consisting of I435T, P422L, and S466L that are located in the non-catalytic C-terminal region of CBS that yield enzymes that are catalytically active but deficient in their response to S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	233-253	cystathionine beta-synthase	Homo sapiens	145-148
12150908-4	2002	In the latter growth condition, oligo-ubiquitylated Met4 is not recruited to MET gene promoters, but is recruited to the SAM genes, which are required for production of S-adenosylmethionine, an unstable metabolite that is not present in rich medium.	S-Adenosylmethionine	169-189	Met4p	Saccharomyces cerevisiae S288C	52-56
12007221-5	2002	We describe a novel class of missense mutations consisting of I435T, P422L, and S466L that are located in the non-catalytic C-terminal region of CBS that yield enzymes that are catalytically active but deficient in their response to S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	255-261	cystathionine beta-synthase	Homo sapiens	145-148
12042458-2	2002	The enzyme protein-L-isoaspartyl methyltransferase (PIMT) catalyzes the transfer of the methyl group of S-adenosyl-L-methionine (SAM) to these L-isoaspartyl sites, thereby allowing reisomerization and restoration of the original alpha peptide linkage.	S-Adenosylmethionine	104-127	protein-L-isoaspartate (D-aspartate) O-methyltransferase 1	Rattus norvegicus	11-50
12042458-2	2002	The enzyme protein-L-isoaspartyl methyltransferase (PIMT) catalyzes the transfer of the methyl group of S-adenosyl-L-methionine (SAM) to these L-isoaspartyl sites, thereby allowing reisomerization and restoration of the original alpha peptide linkage.	S-Adenosylmethionine	104-127	protein-L-isoaspartate (D-aspartate) O-methyltransferase 1	Rattus norvegicus	52-56
12054683-5	2002	Previous findings, which showed that S-adenosyl-l-methionine (SAM), a CBS activator, is much reduced in AD brain and that homocysteine accumulates in the serum of AD patients, were confirmed.	S-Adenosylmethionine	37-60	cystathionine beta-synthase	Homo sapiens	70-73
11912212-1	2002	PIMT (PRIP-interacting protein with methyltransferase domain), an RNA-binding protein with a methyltransferase domain capable of binding S-adenosylmethionine, has been shown previously to interact with nuclear receptor coactivator PRIP (peroxisome proliferator-activated receptor (PPAR)-interacting protein) and enhance its coactivator function.	S-Adenosylmethionine	137-157	nuclear receptor coactivator 6	Homo sapiens	6-10
11912212-1	2002	PIMT (PRIP-interacting protein with methyltransferase domain), an RNA-binding protein with a methyltransferase domain capable of binding S-adenosylmethionine, has been shown previously to interact with nuclear receptor coactivator PRIP (peroxisome proliferator-activated receptor (PPAR)-interacting protein) and enhance its coactivator function.	S-Adenosylmethionine	137-157	nuclear receptor coactivator 6	Homo sapiens	231-235
11912212-1	2002	PIMT (PRIP-interacting protein with methyltransferase domain), an RNA-binding protein with a methyltransferase domain capable of binding S-adenosylmethionine, has been shown previously to interact with nuclear receptor coactivator PRIP (peroxisome proliferator-activated receptor (PPAR)-interacting protein) and enhance its coactivator function.	S-Adenosylmethionine	137-157	nuclear receptor coactivator 6	Homo sapiens	237-307
12071701-0	2002	Expression of recombinant human betaine: homocysteine S-methyltransferase for x-ray crystallographic studies and further characterization of interaction with S-adenosylmethionine.	S-Adenosylmethionine	158-178	betaine--homocysteine S-methyltransferase	Homo sapiens	32-73
12054683-5	2002	Previous findings, which showed that S-adenosyl-l-methionine (SAM), a CBS activator, is much reduced in AD brain and that homocysteine accumulates in the serum of AD patients, were confirmed.	S-Adenosylmethionine	62-65	cystathionine beta-synthase	Homo sapiens	70-73
11856739-3	2002	Using S-adenosyl-l-methionine as co-substrate, RMT2 methylated a protein in the ribosome salt wash fraction.	S-Adenosylmethionine	6-29	protein-arginine N5-methyltransferase	Saccharomyces cerevisiae S288C	47-51
11997462-4	2002	ADK not only ensures normal adenine nucleotide levels but also is essential for maintaining S-adenosylmethionine-dependent transmethylation processes, where adenosine, an obligatory product, has to be constantly removed.	S-Adenosylmethionine	94-112	adenosine kinase	Homo sapiens	0-3
12192860-1	2002	To utilize Pichia pastoris to produce S-adenosyl-L-methionine (SAM), an intracellular expression vector harboring S. cerevisiae SAM2 was transformed into GS115.	S-Adenosylmethionine	38-61	methionine adenosyltransferase SAM2	Saccharomyces cerevisiae S288C	128-132
11997007-3	2002	S-Adenosylmethionine-dependent carboxyl methylation is essential for the assembly of PP2A heterotrimers.	S-Adenosylmethionine	0-20	protein phosphatase 2 phosphatase activator	Homo sapiens	85-89
11984522-7	2002	We have studied the modulation of hepatocyte growth factor-induced proliferation by NO through the regulation of S-adenosylmethionine levels.	S-Adenosylmethionine	113-133	hepatocyte growth factor	Homo sapiens	34-58
11984522-11	2002	Accordingly, we found that S-adenosylmethionine inhibits hepatocyte growth factor-induced cyclin D1 and D2 expression, activator protein 1 induction, and hepatocyte proliferation.	S-Adenosylmethionine	27-47	hepatocyte growth factor	Homo sapiens	57-81
11984522-11	2002	Accordingly, we found that S-adenosylmethionine inhibits hepatocyte growth factor-induced cyclin D1 and D2 expression, activator protein 1 induction, and hepatocyte proliferation.	S-Adenosylmethionine	27-47	cyclin D1	Rattus norvegicus	90-99
11984522-11	2002	Accordingly, we found that S-adenosylmethionine inhibits hepatocyte growth factor-induced cyclin D1 and D2 expression, activator protein 1 induction, and hepatocyte proliferation.	S-Adenosylmethionine	27-47	Jun proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	119-138
11984522-12	2002	CONCLUSIONS: Together our findings indicate that NO may switch hepatocytes into a hepatocyte growth factor-responsive state through the down-regulation of S-adenosylmethionine levels.	S-Adenosylmethionine	155-175	hepatocyte growth factor	Homo sapiens	82-106
12054489-1	2002	Glycine N-methyltransferase (GNMT) is a key protein in the liver that functions to regulate S-adenosylmethionine (SAM) and the SAM/S-adenosylhomocysteine ratio.	S-Adenosylmethionine	92-112	glycine N-methyltransferase	Rattus norvegicus	0-27
12054489-1	2002	Glycine N-methyltransferase (GNMT) is a key protein in the liver that functions to regulate S-adenosylmethionine (SAM) and the SAM/S-adenosylhomocysteine ratio.	S-Adenosylmethionine	92-112	glycine N-methyltransferase	Rattus norvegicus	29-33
12054489-1	2002	Glycine N-methyltransferase (GNMT) is a key protein in the liver that functions to regulate S-adenosylmethionine (SAM) and the SAM/S-adenosylhomocysteine ratio.	S-Adenosylmethionine	114-117	glycine N-methyltransferase	Rattus norvegicus	0-27
12054489-1	2002	Glycine N-methyltransferase (GNMT) is a key protein in the liver that functions to regulate S-adenosylmethionine (SAM) and the SAM/S-adenosylhomocysteine ratio.	S-Adenosylmethionine	114-117	glycine N-methyltransferase	Rattus norvegicus	29-33
12192860-1	2002	To utilize Pichia pastoris to produce S-adenosyl-L-methionine (SAM), an intracellular expression vector harboring S. cerevisiae SAM2 was transformed into GS115.	S-Adenosylmethionine	63-66	methionine adenosyltransferase SAM2	Saccharomyces cerevisiae S288C	128-132
11929966-2	2002	Methylenetetrahydrofolate reductase (MTHFR) catalyzes the synthesis of 5-methyltetrahydrofolate (5-methylTHF), the methyl donor for synthesis of methionine from homocysteine and precursor of S-adenosyl-l-methionine.	S-Adenosylmethionine	191-214	methylenetetrahydrofolate reductase	Homo sapiens	0-35
11929966-2	2002	Methylenetetrahydrofolate reductase (MTHFR) catalyzes the synthesis of 5-methyltetrahydrofolate (5-methylTHF), the methyl donor for synthesis of methionine from homocysteine and precursor of S-adenosyl-l-methionine.	S-Adenosylmethionine	191-214	methylenetetrahydrofolate reductase	Homo sapiens	37-42
11821381-9	2002	Kinetic analysis supports an Ordered Bi Bi mechanism for Dnmt3a, where DNA binds first, followed by S-adenosyl-l-methionine.	S-Adenosylmethionine	100-123	DNA methyltransferase 3 alpha	Homo sapiens	57-63
11807261-1	2002	Phenylethanolamine N-methyltransferase, PNMT, utilizes the methylating cofactor S-adenosyl-L-methionine to catalyse the synthesis of adrenaline.	S-Adenosylmethionine	80-103	phenylethanolamine N-methyltransferase	Homo sapiens	0-38
11880556-1	2002	Regulation of S-adenosylmethionine (SAM) and the SAM/S-adenosylhomocysteine (SAH) ratio by the key cytosolic enzyme glycine N-methyltransferase (GNMT) is essential in optimizing methyl group supply and subsequent functioning of methyltransferase enzymes.	S-Adenosylmethionine	14-34	glycine N-methyltransferase	Rattus norvegicus	116-143
11880556-1	2002	Regulation of S-adenosylmethionine (SAM) and the SAM/S-adenosylhomocysteine (SAH) ratio by the key cytosolic enzyme glycine N-methyltransferase (GNMT) is essential in optimizing methyl group supply and subsequent functioning of methyltransferase enzymes.	S-Adenosylmethionine	14-34	glycine N-methyltransferase	Rattus norvegicus	145-149
11880556-1	2002	Regulation of S-adenosylmethionine (SAM) and the SAM/S-adenosylhomocysteine (SAH) ratio by the key cytosolic enzyme glycine N-methyltransferase (GNMT) is essential in optimizing methyl group supply and subsequent functioning of methyltransferase enzymes.	S-Adenosylmethionine	36-39	glycine N-methyltransferase	Rattus norvegicus	116-143
11807261-1	2002	Phenylethanolamine N-methyltransferase, PNMT, utilizes the methylating cofactor S-adenosyl-L-methionine to catalyse the synthesis of adrenaline.	S-Adenosylmethionine	80-103	phenylethanolamine N-methyltransferase	Homo sapiens	40-44
12622183-0	2002	Native state, energetic interaction of chlorophyll precursors and intraplastid location of S-adenosyl-L-methionine: Mg-protoporphyrin IX methyltransferase in etiolated leaves.	S-Adenosylmethionine	91-114	xantha-g	Hordeum vulgare	116-136
12075857-2	2002	Since COMT requires Mg2+ and S-adenosylmethionine as methyl donor for this transmethylating process, COMT converts S-adenosylmethionine to S-adenosylhomocysteine and subsequent homocysteine.	S-Adenosylmethionine	29-49	catechol-O-methyltransferase	Homo sapiens	6-10
12075857-2	2002	Since COMT requires Mg2+ and S-adenosylmethionine as methyl donor for this transmethylating process, COMT converts S-adenosylmethionine to S-adenosylhomocysteine and subsequent homocysteine.	S-Adenosylmethionine	29-49	catechol-O-methyltransferase	Homo sapiens	101-105
12075857-2	2002	Since COMT requires Mg2+ and S-adenosylmethionine as methyl donor for this transmethylating process, COMT converts S-adenosylmethionine to S-adenosylhomocysteine and subsequent homocysteine.	S-Adenosylmethionine	115-135	catechol-O-methyltransferase	Homo sapiens	6-10
12075857-2	2002	Since COMT requires Mg2+ and S-adenosylmethionine as methyl donor for this transmethylating process, COMT converts S-adenosylmethionine to S-adenosylhomocysteine and subsequent homocysteine.	S-Adenosylmethionine	115-135	catechol-O-methyltransferase	Homo sapiens	101-105
11844113-7	2002	SAMS3 gene expression and total SAMS protein were not changed in mto3; however, both total SAMS activity and S-adenosylmethionine (SAM) concentration were decreased in mto3 compared with wild type.	S-Adenosylmethionine	109-129	S-adenosylmethionine synthetase family protein	Arabidopsis thaliana	168-172
11809803-7	2002	This observation, coupled with the ability of recombinant h-mtTFB to bind S-adenosylmethionine in vitro, suggests that a structural, and perhaps functional, relationship exists between this class of transcription factors and this family of RNA modification enzymes and that h-mtTFB may perform dual functions during mitochondrial gene expression.	S-Adenosylmethionine	74-94	transcription factor B2, mitochondrial	Homo sapiens	58-65
11809803-7	2002	This observation, coupled with the ability of recombinant h-mtTFB to bind S-adenosylmethionine in vitro, suggests that a structural, and perhaps functional, relationship exists between this class of transcription factors and this family of RNA modification enzymes and that h-mtTFB may perform dual functions during mitochondrial gene expression.	S-Adenosylmethionine	74-94	transcription factor B2, mitochondrial	Homo sapiens	274-281
11784318-2	2002	Here, we report the first plant S-adenosyl-l-methionine:Mg-protoporphyrin IX methyltransferase (MgP(IX)MT) sequence identified in the Arabidopsis genome owing to its similarity with the Synechocystis sp.	S-Adenosylmethionine	34-55	magnesium-protoporphyrin IX methyltransferase	Arabidopsis thaliana	96-105
11756224-5	2002	In folate-adequate Min mice, we identified positive linear correlations between SAM or SAH and tumor numbers (R(2) = 0.38, P < 0.005; R(2) = 0.26, P = 0.025, respectively).	S-Adenosylmethionine	80-83	APC, WNT signaling pathway regulator	Mus musculus	19-22
11810299-6	2002	The function of GNMT has been hypothesized to provide an alternative route for the conversion of excess AdoMet to AdoHcy in order to preserve the AdoMet/AdoHcy ratio.	S-Adenosylmethionine	104-110	glycine N-methyltransferase	Homo sapiens	16-20
11738094-5	2001	This notion led us to study the effect of S-adenosylmethionine administration on hepatic nitric oxide synthase-2 induction in response to bacterial lipopolysaccharide and proinflammatory cytokines.	S-Adenosylmethionine	42-62	nitric oxide synthase 2	Rattus norvegicus	89-112
11742092-5	2001	The Ala222Val MTHFR, however, has an enhanced propensity to dissociate into monomers and to lose its FAD cofactor on dilution; the resulting loss of activity is slowed in the presence of methyltetrahydrofolate or adenosylmethionine.	S-Adenosylmethionine	213-231	methylenetetrahydrofolate reductase	Homo sapiens	14-19
11738094-6	2001	METHODS: The effect of S-adenosylmethionine on nitric oxide synthase-2 expression was assessed in rats challenged with bacterial lipopolysaccharide and in isolated rat hepatocytes treated with proinflammatory cytokines.	S-Adenosylmethionine	23-43	nitric oxide synthase 2	Rattus norvegicus	47-70
11738094-8	2001	RESULTS: S-Adenosylmethionine attenuated the induction of nitric oxide synthase-2 in the liver of lipopolysaccharide-treated rats and in cytokine-treated hepatocytes.	S-Adenosylmethionine	9-29	nitric oxide synthase 2	Rattus norvegicus	58-81
11738094-9	2001	S-Adenosylmethionine accelerated the resynthesis of inhibitor kappa B alpha, blunted the activation of nuclear factor kappa B and reduced the transactivation of nitric oxide synthase-2 promoter.	S-Adenosylmethionine	0-20	nitric oxide synthase 2	Rattus norvegicus	161-184
11728447-3	2001	Here we demonstrate that S-adenosylmethionine-sulphate-p-toluenesulphonate (SAM) inhibits myogenin expression and myoblast differentiation by delaying the demethylation of specific CpG in differentiating myoblasts.	S-Adenosylmethionine	76-79	myogenin	Mus musculus	90-98
11559709-10	2001	Hepatic concentrations of S-adenosylmethionine and S-adenosylhomocysteine, allosteric activators of cystathionine beta-synthase, were also increased following glucagon treatment.	S-Adenosylmethionine	26-46	cystathionine beta synthase	Rattus norvegicus	100-127
11577006-1	2001	Catechol-O-methyltransferase (COMT) catalyzes the O-methylation of catechol estrogens (CEs), using S-adenosylmethionine (SAM) as a methyl donor.	S-Adenosylmethionine	99-119	catechol-O-methyltransferase	Homo sapiens	0-28
11551827-4	2001	The two splice-variant mRNAs produced from the MT-A70 gene are transcribed at different rates depending on the level of S-adenosyl-L-methionine inhibition.	S-Adenosylmethionine	122-143	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	47-53
11551827-7	2001	This result indicates that the control of MT-A70 gene expression is directly related to methionine availability and the subsequent synthesis of S-adenosyl-L-methionine.	S-Adenosylmethionine	144-167	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	42-48
11706201-7	2001	Biotin synthase in this heterologous system obeyed Michaelis-Menten kinetics with respect to dethiobiotin (K(m) = 30 microM) and exhibited a kinetic cooperativity with respect to S-adenosyl-methionine (Hill coefficient = 1.9; K(0.5) = 39 microM), an obligatory cofactor of the reaction.	S-Adenosylmethionine	179-200	Radical SAM superfamily protein	Arabidopsis thaliana	0-15
11577006-1	2001	Catechol-O-methyltransferase (COMT) catalyzes the O-methylation of catechol estrogens (CEs), using S-adenosylmethionine (SAM) as a methyl donor.	S-Adenosylmethionine	99-119	catechol-O-methyltransferase	Homo sapiens	30-34
11577006-1	2001	Catechol-O-methyltransferase (COMT) catalyzes the O-methylation of catechol estrogens (CEs), using S-adenosylmethionine (SAM) as a methyl donor.	S-Adenosylmethionine	121-124	catechol-O-methyltransferase	Homo sapiens	0-28
11577006-1	2001	Catechol-O-methyltransferase (COMT) catalyzes the O-methylation of catechol estrogens (CEs), using S-adenosylmethionine (SAM) as a methyl donor.	S-Adenosylmethionine	121-124	catechol-O-methyltransferase	Homo sapiens	30-34
11577006-3	2001	Folate, whose intake levels have also been associated with breast cancer risk, and other micronutrients in the folate metabolic pathway influence levels of SAM and S-adenosylhomocysteine (SAH), a COMT inhibitor generated by the demethylation of SAM.	S-Adenosylmethionine	156-159	catechol-O-methyltransferase	Homo sapiens	196-200
11570851-4	2001	Recombinant catechol-O-methyltransferase, in the bacterial soluble fraction, exhibited the same affinity for adrenaline as rat liver soluble catechol-O-methyltransferase (K(m) 428 [246, 609] microM and 531 [330, 732] microM, respectively), as well as the same affinity for the methyl donor, S-adenosyl-l-methionine (K(m) 27 [9, 45] microM and 38 [21, 55] microM, respectively).	S-Adenosylmethionine	291-314	catechol-O-methyltransferase	Rattus norvegicus	12-40
11413150-8	2001	A mutation introduced into the S-adenosyl-l-methionine-binding motif I of a myc-tagged PRMT5 construct in COS-1 cells led to a near complete loss of observed enzymatic activity.	S-Adenosylmethionine	33-54	protein arginine methyltransferase 5	Homo sapiens	87-92
11554794-2	2001	The crystal structure of Rv2118c in complex with S-adenosyl-l-methionine (AdoMet) has been determined at 1.98 A resolution.	S-Adenosylmethionine	49-72	tRNA (adenine(58)-N(1))-methyltransferase	Mycobacterium tuberculosis H37Rv	25-32
11554794-2	2001	The crystal structure of Rv2118c in complex with S-adenosyl-l-methionine (AdoMet) has been determined at 1.98 A resolution.	S-Adenosylmethionine	74-80	tRNA (adenine(58)-N(1))-methyltransferase	Mycobacterium tuberculosis H37Rv	25-32
11524006-0	2001	Regulation of human cystathionine beta-synthase by S-adenosyl-L-methionine: evidence for two catalytically active conformations involving an autoinhibitory domain in the C-terminal region.	S-Adenosylmethionine	51-74	cystathionine beta-synthase	Homo sapiens	20-47
11524006-3	2001	CBS is activated by S-adenosyl-L-methionine (AdoMet) by inducing a conformational change involving a noncatalytic C-terminal region spanning residues 414-551.	S-Adenosylmethionine	20-43	cystathionine beta-synthase	Homo sapiens	0-3
11524006-3	2001	CBS is activated by S-adenosyl-L-methionine (AdoMet) by inducing a conformational change involving a noncatalytic C-terminal region spanning residues 414-551.	S-Adenosylmethionine	45-51	cystathionine beta-synthase	Homo sapiens	0-3
11520127-4	2001	In this study we investigated whether L-dopa increases the transmethylation process by inducing methionine adenosyl transferase (MAT), the enzyme that produces SAM, and catechol-O-methyl transferase (COMT), the enzyme that transfers the methyl group from SAM to L-dopa and DA.	S-Adenosylmethionine	160-163	methionine adenosyltransferase 1A	Homo sapiens	129-132
11566133-8	2001	CONCLUSIONS: HNMT has a 2 domain structure including a consensus AdoMet binding domain, where the residue 105 is located on the surface, consistent with the kinetic data that the polymorphism does not affect overall protein stability at physiological temperatures but lowers K(M) values for AdoMet and histamine.	S-Adenosylmethionine	65-71	histamine N-methyltransferase	Homo sapiens	13-17
11387442-7	2001	Most important, a mutation in the S-adenosyl-l-methionine-binding site of PRMT1 substantially crippled its nuclear receptor coactivator activity.	S-Adenosylmethionine	36-57	protein arginine methyltransferase 1	Homo sapiens	74-79
11445284-3	2001	S-adenosylmethionine (SAM), which is synthesized from adenosine triphosphate and methionine (MET), serves as methyl donor for this O-metabolisation of levodopa with resulting conversion of SAM to total homocysteine (tHcy) via S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	0-20	SAFB like transcription modulator	Homo sapiens	93-96
16256695-5	2001	The first enzyme, lysine 2,3-aminomutase, is a PLP-dependent enzyme that catalyzes the interconversion of L-lysine to L-beta-lysine using a one-electron-based mechanism utilizing a [4Fe-4S] cluster and S-adenosylmethionine.	S-Adenosylmethionine	202-222	pyridoxal phosphatase	Homo sapiens	47-50
11445284-3	2001	S-adenosylmethionine (SAM), which is synthesized from adenosine triphosphate and methionine (MET), serves as methyl donor for this O-metabolisation of levodopa with resulting conversion of SAM to total homocysteine (tHcy) via S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	22-25	SAFB like transcription modulator	Homo sapiens	93-96
11406421-1	2001	Because polymorphisms in the methyl group metabolism genes methylene-tetrahydrofolate reductase (MTHFR), methionine synthase (MS), and cystathione beta-synthetase (CBS) affect plasma homocysteine levels and intracellular concentrations of S-adenosylmethionine (SAM), they modify the susceptibility to cardiovascular diseases and cancer.	S-Adenosylmethionine	239-259	methylenetetrahydrofolate reductase	Homo sapiens	59-95
11470512-2	2001	ACC synthase (ACS) catalyzes the formation of ACC from S-adenosyl-L-methionine.	S-Adenosylmethionine	55-78	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	0-12
11470512-2	2001	ACC synthase (ACS) catalyzes the formation of ACC from S-adenosyl-L-methionine.	S-Adenosylmethionine	55-78	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	14-17
11435507-1	2001	Glycine N-methyltransferase (GNMT) functions to regulate S-adenosylmethionine (SAM) levels and the ratio of SAM/S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	57-77	glycine N-methyltransferase	Rattus norvegicus	0-27
11435507-1	2001	Glycine N-methyltransferase (GNMT) functions to regulate S-adenosylmethionine (SAM) levels and the ratio of SAM/S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	57-77	glycine N-methyltransferase	Rattus norvegicus	29-33
11435507-1	2001	Glycine N-methyltransferase (GNMT) functions to regulate S-adenosylmethionine (SAM) levels and the ratio of SAM/S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	79-82	glycine N-methyltransferase	Rattus norvegicus	0-27
11435507-1	2001	Glycine N-methyltransferase (GNMT) functions to regulate S-adenosylmethionine (SAM) levels and the ratio of SAM/S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	79-82	glycine N-methyltransferase	Rattus norvegicus	29-33
11413290-4	2001	Immunopurified P110 catalyzed transfer of a methyl group from S-adenosylmethionine (AdoMet) to GTP and GDP to yield m(7)GTP or m(7)GDP.	S-Adenosylmethionine	62-82	endogenous retrovirus group K member 15	Homo sapiens	15-19
11413290-4	2001	Immunopurified P110 catalyzed transfer of a methyl group from S-adenosylmethionine (AdoMet) to GTP and GDP to yield m(7)GTP or m(7)GDP.	S-Adenosylmethionine	84-90	endogenous retrovirus group K member 15	Homo sapiens	15-19
11475331-7	2001	Mouse HNMT was expressed in COS-1 cells, and its apparent Km values for histamine and S-adenosyl-L-methionine (Ado-Met), the two cosubstrates for the reaction, were 5.3 and 5.8 microM, respectively.	S-Adenosylmethionine	86-109	histamine N-methyltransferase	Mus musculus	6-10
11475331-7	2001	Mouse HNMT was expressed in COS-1 cells, and its apparent Km values for histamine and S-adenosyl-L-methionine (Ado-Met), the two cosubstrates for the reaction, were 5.3 and 5.8 microM, respectively.	S-Adenosylmethionine	111-118	histamine N-methyltransferase	Mus musculus	6-10
11406421-1	2001	Because polymorphisms in the methyl group metabolism genes methylene-tetrahydrofolate reductase (MTHFR), methionine synthase (MS), and cystathione beta-synthetase (CBS) affect plasma homocysteine levels and intracellular concentrations of S-adenosylmethionine (SAM), they modify the susceptibility to cardiovascular diseases and cancer.	S-Adenosylmethionine	239-259	methylenetetrahydrofolate reductase	Homo sapiens	97-102
11406421-1	2001	Because polymorphisms in the methyl group metabolism genes methylene-tetrahydrofolate reductase (MTHFR), methionine synthase (MS), and cystathione beta-synthetase (CBS) affect plasma homocysteine levels and intracellular concentrations of S-adenosylmethionine (SAM), they modify the susceptibility to cardiovascular diseases and cancer.	S-Adenosylmethionine	239-259	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	105-124
11406421-1	2001	Because polymorphisms in the methyl group metabolism genes methylene-tetrahydrofolate reductase (MTHFR), methionine synthase (MS), and cystathione beta-synthetase (CBS) affect plasma homocysteine levels and intracellular concentrations of S-adenosylmethionine (SAM), they modify the susceptibility to cardiovascular diseases and cancer.	S-Adenosylmethionine	261-264	methylenetetrahydrofolate reductase	Homo sapiens	59-95
11406421-1	2001	Because polymorphisms in the methyl group metabolism genes methylene-tetrahydrofolate reductase (MTHFR), methionine synthase (MS), and cystathione beta-synthetase (CBS) affect plasma homocysteine levels and intracellular concentrations of S-adenosylmethionine (SAM), they modify the susceptibility to cardiovascular diseases and cancer.	S-Adenosylmethionine	261-264	methylenetetrahydrofolate reductase	Homo sapiens	97-102
11406421-1	2001	Because polymorphisms in the methyl group metabolism genes methylene-tetrahydrofolate reductase (MTHFR), methionine synthase (MS), and cystathione beta-synthetase (CBS) affect plasma homocysteine levels and intracellular concentrations of S-adenosylmethionine (SAM), they modify the susceptibility to cardiovascular diseases and cancer.	S-Adenosylmethionine	261-264	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	105-124
11320206-1	2001	Liver-specific and nonliver-specific methionine adenosyltransferases (MATs) are products of two genes, MAT1A and MAT2A, respectively, that catalyze the formation of S-adenosylmethionine (AdoMet), the principal biological methyl donor.	S-Adenosylmethionine	165-185	methionine adenosyltransferase I, alpha	Mus musculus	187-193
11223943-2	2001	Disruption of this gene (renamed ADO1) affected utilization of S-adenosyl methionine (AdoMet) as a purine source and resulted in a severe reduction of adenosine kinase activity in crude extracts.	S-Adenosylmethionine	86-92	adenosine kinase	Saccharomyces cerevisiae S288C	33-37
11320206-1	2001	Liver-specific and nonliver-specific methionine adenosyltransferases (MATs) are products of two genes, MAT1A and MAT2A, respectively, that catalyze the formation of S-adenosylmethionine (AdoMet), the principal biological methyl donor.	S-Adenosylmethionine	165-185	methionine adenosyltransferase 1A	Homo sapiens	103-108
11320206-1	2001	Liver-specific and nonliver-specific methionine adenosyltransferases (MATs) are products of two genes, MAT1A and MAT2A, respectively, that catalyze the formation of S-adenosylmethionine (AdoMet), the principal biological methyl donor.	S-Adenosylmethionine	165-185	methionine adenosyltransferase 2A	Homo sapiens	113-118
11388769-6	2001	S-Adenosylmethionine (SAMe), an effective antidepressant, may owe its effects in the latter disorders in part to variations in the strength of interferon-alpha signaling impacting RNA processing.	S-Adenosylmethionine	0-20	interferon alpha	Mus musculus	143-159
11295154-2	2001	This activity is compromised when Vitamin B12 (B12) concentration is low because methionine synthase activity is reduced, lowering the concentration of S-adenosyl methionine (SAM) which in turn may diminish DNA methylation and cause folate to become unavailable for the conversion of dUMP to dTMP.	S-Adenosylmethionine	152-173	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	81-100
11223943-2	2001	Disruption of this gene (renamed ADO1) affected utilization of S-adenosyl methionine (AdoMet) as a purine source and resulted in a severe reduction of adenosine kinase activity in crude extracts.	S-Adenosylmethionine	63-84	adenosine kinase	Saccharomyces cerevisiae S288C	33-37
11223943-2	2001	Disruption of this gene (renamed ADO1) affected utilization of S-adenosyl methionine (AdoMet) as a purine source and resulted in a severe reduction of adenosine kinase activity in crude extracts.	S-Adenosylmethionine	63-84	adenosine kinase	Saccharomyces cerevisiae S288C	151-167
11372589-9	2001	TPMT activity in the RBC hemolysate was determined using a radioactive assay with tritiated S-adenosyl methionine as a methyl donor.	S-Adenosylmethionine	92-113	thiopurine S-methyltransferase	Homo sapiens	0-4
11244502-5	2001	Ectopic expression of ODC-Az gene in hamster malignant oral keratinocytes led to reduce ODC activity and the subsequent demethylation of 5-methyl cytosines, presumably via the ODC/ polyamines/ decarboxylated S-adenosylmethionine (dc-AdoMet) pathways.	S-Adenosylmethionine	208-228	ornithine decarboxylase, structural 1	Mus musculus	22-25
11309147-1	2001	Angiosperms synthesize S-methylmethionine (SMM) from methionine (Met) and S-adenosylmethionine (AdoMet) in a unique reaction catalyzed by Met S-methyltransferase (MMT).	S-Adenosylmethionine	74-94	methionine S-methyltransferase	Arabidopsis thaliana	138-161
11309147-1	2001	Angiosperms synthesize S-methylmethionine (SMM) from methionine (Met) and S-adenosylmethionine (AdoMet) in a unique reaction catalyzed by Met S-methyltransferase (MMT).	S-Adenosylmethionine	74-94	methionine S-methyltransferase	Arabidopsis thaliana	163-166
11309147-1	2001	Angiosperms synthesize S-methylmethionine (SMM) from methionine (Met) and S-adenosylmethionine (AdoMet) in a unique reaction catalyzed by Met S-methyltransferase (MMT).	S-Adenosylmethionine	96-102	methionine S-methyltransferase	Arabidopsis thaliana	138-161
11309147-1	2001	Angiosperms synthesize S-methylmethionine (SMM) from methionine (Met) and S-adenosylmethionine (AdoMet) in a unique reaction catalyzed by Met S-methyltransferase (MMT).	S-Adenosylmethionine	96-102	methionine S-methyltransferase	Arabidopsis thaliana	163-166
11042162-1	2001	Human cystathionine beta-synthase is a pyridoxal 5"-phosphate enzyme containing a heme binding domain and an S-adenosyl-l-methionine regulatory site.	S-Adenosylmethionine	111-132	cystathionine beta-synthase	Homo sapiens	6-33
11223018-0	2001	COMT-dependent protection of dopaminergic neurons by methionine, dimethionine and S-adenosylmethionine (SAM) against L-dopa toxicity in vitro.	S-Adenosylmethionine	82-102	catechol-O-methyltransferase	Homo sapiens	0-4
11344332-2	2001	In plants, the methionine pathway shares the same substrate, O-phospho-L-homoserine (OPH), and TS is activated by S-adenosyl-methionine (SAM), a downstream product of methionine synthesis.	S-Adenosylmethionine	114-135	Pyridoxal-5'-phosphate-dependent enzyme family protein	Arabidopsis thaliana	95-97
11344332-2	2001	In plants, the methionine pathway shares the same substrate, O-phospho-L-homoserine (OPH), and TS is activated by S-adenosyl-methionine (SAM), a downstream product of methionine synthesis.	S-Adenosylmethionine	137-140	Pyridoxal-5'-phosphate-dependent enzyme family protein	Arabidopsis thaliana	95-97
11208539-1	2001	Methionine adenosyltransferase (MAT), an essential enzyme that catalyzes the formation of S-adenosylmethionine (SAM), is encoded by two genes, MAT1A (liver-specific) and MAT2A (non-liver-specific).	S-Adenosylmethionine	90-110	methionine adenosyltransferase 1A	Homo sapiens	143-148
11208539-1	2001	Methionine adenosyltransferase (MAT), an essential enzyme that catalyzes the formation of S-adenosylmethionine (SAM), is encoded by two genes, MAT1A (liver-specific) and MAT2A (non-liver-specific).	S-Adenosylmethionine	90-110	methionine adenosyltransferase 2A	Homo sapiens	170-175
11139614-2	2001	DNMT2 contains all 10 sequence motifs that are conserved among m(5)C MTases, including the consensus S:-adenosyl-L-methionine-binding motifs and the active site ProCys dipeptide.	S-Adenosylmethionine	104-125	tRNA aspartic acid methyltransferase 1	Homo sapiens	0-5
11103808-2	2000	The cystathionine-beta-synthase (CBS) gene (localized to chromosome 21q22.3) may have downstream effects on reduced folate and S-adenosylmethionine pathways; ara-C metabolism and folate pools are linked by the known synergistic effect of sequential methotrexate and ara-C therapy.	S-Adenosylmethionine	127-147	cystathionine beta-synthase	Homo sapiens	4-31
11713417-6	2001	This amino acid substitution alters the amino acid composition of a conserved methylating enzyme motif shown to be involved in S-adenosylmethionine binding in M.HhaI, a bacterial methyltransferase that is almost identical to DNMT2 in size and structure.	S-Adenosylmethionine	127-147	tRNA aspartic acid methyltransferase 1	Homo sapiens	225-230
11346894-9	2000	Plasma ALT concentrations were significantly lower (p < 0.01) in mice treated with 2.5 mmol/kg of S-adenosyl-L-methionine than in those given N-acetylcysteine.	S-Adenosylmethionine	101-124	glutamic pyruvic transaminase, soluble	Mus musculus	7-10
11508552-2	2000	Decreased activity of MTHFR leads to reduction of 5-methyltetrahydrofolate, the main methyl donor for methionine synthesis necessary for synthesis of S-adenosyl-methionine (SAM).	S-Adenosylmethionine	150-171	methylenetetrahydrofolate reductase	Homo sapiens	22-27
11508552-2	2000	Decreased activity of MTHFR leads to reduction of 5-methyltetrahydrofolate, the main methyl donor for methionine synthesis necessary for synthesis of S-adenosyl-methionine (SAM).	S-Adenosylmethionine	173-176	methylenetetrahydrofolate reductase	Homo sapiens	22-27
11103808-2	2000	The cystathionine-beta-synthase (CBS) gene (localized to chromosome 21q22.3) may have downstream effects on reduced folate and S-adenosylmethionine pathways; ara-C metabolism and folate pools are linked by the known synergistic effect of sequential methotrexate and ara-C therapy.	S-Adenosylmethionine	127-147	cystathionine beta-synthase	Homo sapiens	33-36
11074524-2	2000	A possible cause underlying altered DNA methylation could be an insufficient level of S-adenosylmethionine as a consequence of nutritional imbalances or of weaker alleles of genes for its synthesis, i.e., encoding methylene-tetrahydrofolate reductase (MTHFR), methionine synthase (MS), and beta-cystathione synthetase (CBS).	S-Adenosylmethionine	86-106	methylenetetrahydrofolate reductase	Homo sapiens	214-250
11074524-2	2000	A possible cause underlying altered DNA methylation could be an insufficient level of S-adenosylmethionine as a consequence of nutritional imbalances or of weaker alleles of genes for its synthesis, i.e., encoding methylene-tetrahydrofolate reductase (MTHFR), methionine synthase (MS), and beta-cystathione synthetase (CBS).	S-Adenosylmethionine	86-106	methylenetetrahydrofolate reductase	Homo sapiens	252-257
11074524-2	2000	A possible cause underlying altered DNA methylation could be an insufficient level of S-adenosylmethionine as a consequence of nutritional imbalances or of weaker alleles of genes for its synthesis, i.e., encoding methylene-tetrahydrofolate reductase (MTHFR), methionine synthase (MS), and beta-cystathione synthetase (CBS).	S-Adenosylmethionine	86-106	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	260-279
11084378-13	2000	Administration of bilirubin (5 micromol kg(-1) body weight) or S-adenosyl L-methionine (46 micromol kg(-1) body weight) 2 h before APAP treatment entirely prevented the increase in malondialdehyde (MDA) content, the decrease in GSH levels as well as HO and ALA-S induction.	S-Adenosylmethionine	63-86	5'-aminolevulinate synthase 1	Rattus norvegicus	257-262
10950844-3	2000	When (-)-epicatechin was used as substrate, its O-methylation by human placental COMT showed dependence on incubation time, cytosolic protein concentration, incubation pH, and concentration of S-adenosyl-L-methionine (the methyl donor).	S-Adenosylmethionine	193-216	catechol-O-methyltransferase	Homo sapiens	81-85
10950844-5	2000	Additional analysis revealed that COMT-catalyzed O-methylation of (-)-epicatechin and (-)-epigallocatechin was strongly inhibited in a concentration-dependent manner by S-adenosyl-L-homocysteine (IC(50) = 3.2-5.7 microM), a demethylated product of S-adenosyl-L-methionine.	S-Adenosylmethionine	248-271	catechol-O-methyltransferase	Homo sapiens	34-38
10952104-2	2000	Methylenetetrahydrofolate reductase (MTHFR) catalyzes the synthesis of 5-methyltetrahydrofolate, the methyl donor for methionine synthesis and the precursor of S-adenosylmethionine.	S-Adenosylmethionine	160-180	methylenetetrahydrofolate reductase	Homo sapiens	0-35
10952104-2	2000	Methylenetetrahydrofolate reductase (MTHFR) catalyzes the synthesis of 5-methyltetrahydrofolate, the methyl donor for methionine synthesis and the precursor of S-adenosylmethionine.	S-Adenosylmethionine	160-180	methylenetetrahydrofolate reductase	Homo sapiens	37-42
10903903-5	2000	We demonstrated that JBP1 can complement Saccharomyces cerevisiae with a disrupted HSL7 gene as judged by a reduction of the elongated bud phenotype, and a point mutation in the JBP1 S-adenosylmethionine consensus binding sequence eliminated all complementation by JBP1.	S-Adenosylmethionine	185-203	protein arginine methyltransferase 5	Homo sapiens	21-25
11032186-6	2000	Since the level of S-adenosylmethionine (SAM) is greatly reduced in SAMDC-overexpressing embryos and this induces inhibition of protein synthesis accompanied by the inhibition of DNA and RNA syntheses, we conclude that deficiency in SAM induced by SAMDC overexpression activates the maternal program of apoptosis in Xenopus embryos at the late blastula stage, but not before.	S-Adenosylmethionine	19-39	adenosylmethionine decarboxylase 1 S homeolog	Xenopus laevis	68-73
10903903-5	2000	We demonstrated that JBP1 can complement Saccharomyces cerevisiae with a disrupted HSL7 gene as judged by a reduction of the elongated bud phenotype, and a point mutation in the JBP1 S-adenosylmethionine consensus binding sequence eliminated all complementation by JBP1.	S-Adenosylmethionine	185-203	protein arginine methyltransferase 5	Homo sapiens	178-182
10903903-5	2000	We demonstrated that JBP1 can complement Saccharomyces cerevisiae with a disrupted HSL7 gene as judged by a reduction of the elongated bud phenotype, and a point mutation in the JBP1 S-adenosylmethionine consensus binding sequence eliminated all complementation by JBP1.	S-Adenosylmethionine	185-203	protein arginine methyltransferase 5	Homo sapiens	178-182
10898761-1	2000	Liver-specific and non-liver-specific methionine adenosyltransferase (MAT) are products of two genes, MAT1A and MAT2A, respectively, that catalyze the formation of S-adenosylmethionine (SAM).	S-Adenosylmethionine	164-184	methionine adenosyltransferase 1A	Rattus norvegicus	102-107
10898761-1	2000	Liver-specific and non-liver-specific methionine adenosyltransferase (MAT) are products of two genes, MAT1A and MAT2A, respectively, that catalyze the formation of S-adenosylmethionine (SAM).	S-Adenosylmethionine	164-184	methionine adenosyltransferase 2A	Rattus norvegicus	112-117
10756111-1	2000	Glycine N-methyltransferase (S-adenosyl-l-methionine: glycine methyltransferase, EC 2.1.1.20; GNMT) catalyzes the AdoMet-dependent methylation of glycine to form sarcosine (N-methylglycine).	S-Adenosylmethionine	114-120	glycine N-methyltransferase	Homo sapiens	0-27
10874162-1	2000	When we studied polyamine metabolism in Xenopus embryos, we cloned the cDNA for Xenopus S-adenosylmethionine decarboxylase (SAMDC), which converts SAM (S-adenosylmethionine), the methyl donor, into decarboxylated SAM (dcSAM), the aminopropyl donor, and microinjected its in vitro transcribed mRNA into Xenopus fertilized eggs.	S-Adenosylmethionine	124-127	adenosylmethionine decarboxylase 1 S homeolog	Xenopus laevis	88-122
10874162-1	2000	When we studied polyamine metabolism in Xenopus embryos, we cloned the cDNA for Xenopus S-adenosylmethionine decarboxylase (SAMDC), which converts SAM (S-adenosylmethionine), the methyl donor, into decarboxylated SAM (dcSAM), the aminopropyl donor, and microinjected its in vitro transcribed mRNA into Xenopus fertilized eggs.	S-Adenosylmethionine	88-108	adenosylmethionine decarboxylase 1 S homeolog	Xenopus laevis	124-129
10809741-1	2000	We previously reported that S-adenosylmethionine (AdoMet), a key molecule in methylation reactions and polyamine biosynthesis, enhances axenic culture of the AIDS-associated opportunistic fungal pathogen Pneumocystis carinii.	S-Adenosylmethionine	28-48	methionine adenosyltransferase 1A	Rattus norvegicus	50-56
10843803-1	2000	The glycine N-methyltransferase (GNMT) gene encodes a protein that not only acts as an enzyme to regulate the ratio of S-adenosylmethionine to S-adenosylhomocysteine, but also participates in the detoxification pathway in liver cells.	S-Adenosylmethionine	119-139	glycine N-methyltransferase	Homo sapiens	4-31
10843803-1	2000	The glycine N-methyltransferase (GNMT) gene encodes a protein that not only acts as an enzyme to regulate the ratio of S-adenosylmethionine to S-adenosylhomocysteine, but also participates in the detoxification pathway in liver cells.	S-Adenosylmethionine	119-139	glycine N-methyltransferase	Homo sapiens	33-37
10779558-3	2000	Gcd10p is found in a complex with Gcd14p, which contains conserved motifs for binding S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	86-106	tRNA 1-methyladenosine methyltransferase subunit GCD10	Saccharomyces cerevisiae S288C	0-6
10779558-3	2000	Gcd10p is found in a complex with Gcd14p, which contains conserved motifs for binding S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	86-106	tRNA 1-methyladenosine methyltransferase subunit GCD14	Saccharomyces cerevisiae S288C	34-40
10779558-3	2000	Gcd10p is found in a complex with Gcd14p, which contains conserved motifs for binding S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	108-114	tRNA 1-methyladenosine methyltransferase subunit GCD10	Saccharomyces cerevisiae S288C	0-6
10779558-3	2000	Gcd10p is found in a complex with Gcd14p, which contains conserved motifs for binding S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	108-114	tRNA 1-methyladenosine methyltransferase subunit GCD14	Saccharomyces cerevisiae S288C	34-40
10766755-1	2000	Calmodulin is trimethylated at lysine 115 by a highly specific methyltransferase that utilizes S-adenosylmethionine as a co-substrate.	S-Adenosylmethionine	95-115	calmodulin 1	Homo sapiens	0-10
10747987-7	2000	AtHMT-1 and -2 both utilize l-SMM or (S,S)-AdoMet as a methyl donor in vitro and have higher affinities for SMM.	S-Adenosylmethionine	37-49	Homocysteine S-methyltransferase family protein	Arabidopsis thaliana	0-14
10756111-1	2000	Glycine N-methyltransferase (S-adenosyl-l-methionine: glycine methyltransferase, EC 2.1.1.20; GNMT) catalyzes the AdoMet-dependent methylation of glycine to form sarcosine (N-methylglycine).	S-Adenosylmethionine	114-120	glycine N-methyltransferase	Homo sapiens	94-98
10753866-13	2000	Dnmt1b protein purified from a baculovirus expression system was demonstrated to be a functional DNA methyltransferase, and to have Michaelis constants for both DNA and S-adenosyl-L-methionine similar to baculovirus-expressed Dnmt1.	S-Adenosylmethionine	169-192	DNA methyltransferase 1	Homo sapiens	0-5
10785817-1	2000	The enzyme catechol O-methyltransferase (COMT) catalyzes the Me group transfer from the cofactor S-adenosylmethionine (SAM) to the hydroxy group of catechol substrates.	S-Adenosylmethionine	97-117	catechol-O-methyltransferase	Rattus norvegicus	11-39
10713084-8	2000	Recombinant glutathione S-transferase-PRMT1, but not purified FDH, can be cross-linked to the methyl-donor substrate S-adenosyl-L-methionine.	S-Adenosylmethionine	117-140	protein arginine methyltransferase 1	Homo sapiens	38-43
10785817-1	2000	The enzyme catechol O-methyltransferase (COMT) catalyzes the Me group transfer from the cofactor S-adenosylmethionine (SAM) to the hydroxy group of catechol substrates.	S-Adenosylmethionine	97-117	catechol-O-methyltransferase	Rattus norvegicus	41-45
10785817-1	2000	The enzyme catechol O-methyltransferase (COMT) catalyzes the Me group transfer from the cofactor S-adenosylmethionine (SAM) to the hydroxy group of catechol substrates.	S-Adenosylmethionine	119-122	catechol-O-methyltransferase	Rattus norvegicus	11-39
10785817-1	2000	The enzyme catechol O-methyltransferase (COMT) catalyzes the Me group transfer from the cofactor S-adenosylmethionine (SAM) to the hydroxy group of catechol substrates.	S-Adenosylmethionine	119-122	catechol-O-methyltransferase	Rattus norvegicus	41-45
10692500-8	2000	Furthermore, the primary metabolite of L-dopa formed by COMT, 3-O-methyldopa, and the methyl group donor S-adenosyl-L-methionine used by COMT did not alter THir neuron survival and L-dopa-induced toxicity, respectively, with concentrations up to 100 microM.	S-Adenosylmethionine	107-128	catechol-O-methyltransferase	Homo sapiens	137-141
10652296-6	2000	Amino acid changes in the putative Hmt1p S-adenosyl-L-methionine-binding site were generated and shown to be unable to catalyze methylation of Npl3p in vitro and in vivo or to restore growth to strains that require HMT1.	S-Adenosylmethionine	43-64	protein-arginine omega-N methyltransferase HMT1	Saccharomyces cerevisiae S288C	35-40
11268392-4	2000	Indeed, increases in hydrogen sulfide levels within the hypothalamus, either obtained with hydrogen sulfide-enriched media or by the addition of the hydrogen sulfide precursor S-adenosyl-methionine, are associated with the inhibition of the stimulated release of corticotropin-releasing hormone from rat hypothalamic explants.	S-Adenosylmethionine	176-197	corticotropin releasing hormone	Rattus norvegicus	263-294
10648622-0	2000	Spb1p is a yeast nucleolar protein associated with Nop1p and Nop58p that is able to bind S-adenosyl-L-methionine in vitro.	S-Adenosylmethionine	89-112	27S pre-rRNA (guanosine2922-2'-O)-methyltransferase	Saccharomyces cerevisiae S288C	0-5
10648622-0	2000	Spb1p is a yeast nucleolar protein associated with Nop1p and Nop58p that is able to bind S-adenosyl-L-methionine in vitro.	S-Adenosylmethionine	89-112	RNA-processing protein NOP58	Saccharomyces cerevisiae S288C	61-67
10648622-7	2000	Protein sequence analysis reveals that Spb1p possesses a putative S-adenosyl-L-methionine (AdoMet)-binding domain, which is common to the AdoMet-dependent methyltransferases.	S-Adenosylmethionine	68-89	27S pre-rRNA (guanosine2922-2'-O)-methyltransferase	Saccharomyces cerevisiae S288C	39-44
10648622-7	2000	Protein sequence analysis reveals that Spb1p possesses a putative S-adenosyl-L-methionine (AdoMet)-binding domain, which is common to the AdoMet-dependent methyltransferases.	S-Adenosylmethionine	91-97	27S pre-rRNA (guanosine2922-2'-O)-methyltransferase	Saccharomyces cerevisiae S288C	39-44
10637232-2	2000	We report here that the SCF(Met30 )complex mediates the transcriptional repression of the MET gene network by triggering degradation of the transcriptional activator Met4p when intracellular S-adenosylmethionine (AdoMet) increases.	S-Adenosylmethionine	191-211	ubiquitin-binding SDF ubiquitin ligase complex subunit MET30	Saccharomyces cerevisiae S288C	28-33
10637232-2	2000	We report here that the SCF(Met30 )complex mediates the transcriptional repression of the MET gene network by triggering degradation of the transcriptional activator Met4p when intracellular S-adenosylmethionine (AdoMet) increases.	S-Adenosylmethionine	191-211	Met4p	Saccharomyces cerevisiae S288C	166-171
10637232-2	2000	We report here that the SCF(Met30 )complex mediates the transcriptional repression of the MET gene network by triggering degradation of the transcriptional activator Met4p when intracellular S-adenosylmethionine (AdoMet) increases.	S-Adenosylmethionine	213-219	ubiquitin-binding SDF ubiquitin ligase complex subunit MET30	Saccharomyces cerevisiae S288C	28-33
10637232-2	2000	We report here that the SCF(Met30 )complex mediates the transcriptional repression of the MET gene network by triggering degradation of the transcriptional activator Met4p when intracellular S-adenosylmethionine (AdoMet) increases.	S-Adenosylmethionine	213-219	Met4p	Saccharomyces cerevisiae S288C	166-171
11996106-13	2000	Nucleotide synthesis from SAM involves the formation of adenine as an intermediate with its subsequent incorporation by adenine phosphoribosyltransferase.	S-Adenosylmethionine	26-29	adenine phosphoribosyl transferase	Rattus norvegicus	120-153
10737174-5	2000	ERG6 encodes S-adenosylmethionine: delta 24-sterol-C-methyltransferase (EC 2.1.1.41) in the ergosterol synthetic pathway.	S-Adenosylmethionine	15-33	sterol 24-C-methyltransferase	Saccharomyces cerevisiae S288C	0-4
10531356-6	1999	JBP1 can be cross-linked to radiolabeled S-adenosylmethionine (AdoMet) and methylates histones (H2A and H4) and myelin basic protein.	S-Adenosylmethionine	41-61	protein arginine methyltransferase 5	Homo sapiens	0-4
10608809-1	1999	Glycine N-methyltransferase (EC 2.1.1.20) catalyzes the methylation of glycine by S-adenosylmethionine to form sarcosine and S-adenosylhomocysteine.	S-Adenosylmethionine	82-102	glycine N-methyltransferase	Rattus norvegicus	0-27
10608809-3	1999	We now report that the inhibition of glycine N-methyltransferase by (6S)-5-CH(3)-H(4)PteGlu(5) is noncompetitive with regard to both S-adenosylmethionine and glycine.	S-Adenosylmethionine	133-153	glycine N-methyltransferase	Rattus norvegicus	37-64
10674710-1	2000	Hepatic methionine adenosyltransferase (MAT) deficiency is caused by mutations in the human MAT1A gene that abolish or reduce hepatic MAT activity that catalyzes the synthesis of S-adenosylmethionine from methionine and ATP.	S-Adenosylmethionine	179-199	methionine adenosyltransferase 1A	Homo sapiens	92-97
10955733-1	2000	Methionine adenosyltransferase (MAT) catalyzes the synthesis of S-adenosylmethionine (AdoMet) from ATP and L-methionine.	S-Adenosylmethionine	64-84	methionine adenosyltransferase 1A	Homo sapiens	0-30
10955733-1	2000	Methionine adenosyltransferase (MAT) catalyzes the synthesis of S-adenosylmethionine (AdoMet) from ATP and L-methionine.	S-Adenosylmethionine	64-84	methionine adenosyltransferase 1A	Homo sapiens	32-35
10955733-1	2000	Methionine adenosyltransferase (MAT) catalyzes the synthesis of S-adenosylmethionine (AdoMet) from ATP and L-methionine.	S-Adenosylmethionine	86-92	methionine adenosyltransferase 1A	Homo sapiens	0-30
10955733-1	2000	Methionine adenosyltransferase (MAT) catalyzes the synthesis of S-adenosylmethionine (AdoMet) from ATP and L-methionine.	S-Adenosylmethionine	86-92	methionine adenosyltransferase 1A	Homo sapiens	32-35
10593891-11	1999	A reversible MTHFR reaction would obviate the need for inhibition by S-adenosylmethionine to prevent excessive conversion of methylene- to methyltetrahydrofolate.	S-Adenosylmethionine	69-89	methylenetetrahydrofolate reductase	Homo sapiens	13-18
10567242-1	1999	S-Adenosylmethionine (AdoMet) synthetase (SAMS: EC 2.5.1.6) catalyses the formation of AdoMet from methionine and ATP.	S-Adenosylmethionine	22-28	methionine adenosyltransferase 1A	Homo sapiens	42-46
10561698-10	1999	CDP-choline may act by increasing PtdCho synthesis via two pathways: (1) conversion of 1, 2-diacylglycerol to PtdCho, and (2) biosynthesis of S-adenosyl-L-methionine, thus stabilizing the membrane and reducing AA release and metabolism to leukotriene C(4).	S-Adenosylmethionine	142-165	cut like homeobox 1	Homo sapiens	0-3
10588658-4	1999	SAHH is the only enzyme that cleaves S-adenosylhomocysteine, a reaction product and an inhibitor of all S-adenosylmethionine-dependent methylation reactions.	S-Adenosylmethionine	104-124	adenosylhomocysteinase S homeolog	Xenopus laevis	0-4
10580153-1	1999	Protein L-isoaspartyl methyltransferase (Pimt) is a highly conserved enzyme utilising S-adenosylmethionine (AdoMet) to methylate aspartate residues of proteins damaged by age-related isomerisation and deamidation.	S-Adenosylmethionine	86-106	protein-L-isoaspartate (D-aspartate) O-methyltransferase 1	Rattus norvegicus	0-39
10580153-1	1999	Protein L-isoaspartyl methyltransferase (Pimt) is a highly conserved enzyme utilising S-adenosylmethionine (AdoMet) to methylate aspartate residues of proteins damaged by age-related isomerisation and deamidation.	S-Adenosylmethionine	86-106	protein-L-isoaspartate (D-aspartate) O-methyltransferase 1	Rattus norvegicus	41-45
10580153-1	1999	Protein L-isoaspartyl methyltransferase (Pimt) is a highly conserved enzyme utilising S-adenosylmethionine (AdoMet) to methylate aspartate residues of proteins damaged by age-related isomerisation and deamidation.	S-Adenosylmethionine	86-106	methionine adenosyltransferase 1A	Rattus norvegicus	108-114
10531356-6	1999	JBP1 can be cross-linked to radiolabeled S-adenosylmethionine (AdoMet) and methylates histones (H2A and H4) and myelin basic protein.	S-Adenosylmethionine	63-69	protein arginine methyltransferase 5	Homo sapiens	0-4
10415148-2	1999	The activity of L-methionine S-adenosyltransferase (MAT), a regulatory enzyme of S-adenosylmethionine biosynthesis, was investigated in erythrocytes of 21 patients with ALS, spinal cord specimens of 7 ALS patients, and matched controls.	S-Adenosylmethionine	81-101	methionine adenosyltransferase 1A	Homo sapiens	16-50
10468559-6	1999	To further test this model, recombinant F5H was incubated together with ferulic acid, coniferaldehyde, or coniferyl alcohol in the presence of native or recombinant Arabidopsis caffeic acid/5-hydroxyferulic acid O-methyltransferase and [(14)C]S-adenosylmethionine.	S-Adenosylmethionine	245-263	ferulic acid 5-hydroxylase 1	Arabidopsis thaliana	40-43
10432295-1	1999	Intracellular deficiency of S-adenosylmethionine (AdoMet) and elevated serum concentrations of tumour necrosis factor alpha (TNF) are hallmarks of toxin-induced liver injury.	S-Adenosylmethionine	28-48	methionine adenosyltransferase 1A	Rattus norvegicus	50-56
10415148-2	1999	The activity of L-methionine S-adenosyltransferase (MAT), a regulatory enzyme of S-adenosylmethionine biosynthesis, was investigated in erythrocytes of 21 patients with ALS, spinal cord specimens of 7 ALS patients, and matched controls.	S-Adenosylmethionine	81-101	methionine adenosyltransferase 1A	Homo sapiens	52-55
10381882-4	1999	CARM1 can methylate histone H3 in vitro, and a mutation in the putative S-adenosylmethionine binding domain of CARM1 substantially reduced both methyltransferase and coactivator activities.	S-Adenosylmethionine	74-92	coactivator associated arginine methyltransferase 1	Homo sapiens	111-116
10424321-4	1999	Furthermore, we studied the influence of different 6-TG compounds on the affinity of the methyl donor S-adenosyl-L-methionine (SAM) to the TPMT enzyme.	S-Adenosylmethionine	102-125	thiopurine S-methyltransferase	Homo sapiens	139-143
10347220-5	1999	Recombinant Hcm1p catalyzed quantitative S-adenosylmethionine-dependent conversion of GpppA-capped poly(A) to m7GpppA-capped poly(A).	S-Adenosylmethionine	43-61	RNA guanine-7 methyltransferase	Homo sapiens	12-17
10456560-1	1999	Beneficial effects of S-adenosyl-L-methionine (SAM) in preventing inhibition of blood delta-aminolevulinic acid dehydratase (ALAD), alterations in blood and hepatic glutathione (GSH), hepatic and brain malondialdehyde (MDA) formation, and uptake of lead following acute lead plus ethanol coexposure were investigated in mice.	S-Adenosylmethionine	22-45	aminolevulinate, delta-, dehydratase	Mus musculus	86-123
10456560-1	1999	Beneficial effects of S-adenosyl-L-methionine (SAM) in preventing inhibition of blood delta-aminolevulinic acid dehydratase (ALAD), alterations in blood and hepatic glutathione (GSH), hepatic and brain malondialdehyde (MDA) formation, and uptake of lead following acute lead plus ethanol coexposure were investigated in mice.	S-Adenosylmethionine	22-45	aminolevulinate, delta-, dehydratase	Mus musculus	125-129
10456560-1	1999	Beneficial effects of S-adenosyl-L-methionine (SAM) in preventing inhibition of blood delta-aminolevulinic acid dehydratase (ALAD), alterations in blood and hepatic glutathione (GSH), hepatic and brain malondialdehyde (MDA) formation, and uptake of lead following acute lead plus ethanol coexposure were investigated in mice.	S-Adenosylmethionine	47-50	aminolevulinate, delta-, dehydratase	Mus musculus	86-123
10456560-1	1999	Beneficial effects of S-adenosyl-L-methionine (SAM) in preventing inhibition of blood delta-aminolevulinic acid dehydratase (ALAD), alterations in blood and hepatic glutathione (GSH), hepatic and brain malondialdehyde (MDA) formation, and uptake of lead following acute lead plus ethanol coexposure were investigated in mice.	S-Adenosylmethionine	47-50	aminolevulinate, delta-, dehydratase	Mus musculus	125-129
10216131-1	1999	Liver-specific and non-liver-specific methionine adenosyltransferase (MAT) are products of two genes, MAT1A and MAT2A, respectively, that catalyze the formation of S-adenosylmethionine (SAM), the principal methyl donor.	S-Adenosylmethionine	164-184	methionine adenosyltransferase 1A	Homo sapiens	38-68
10330157-3	1999	Here we show that Gcd14p is an essential protein with predicted binding motifs for S-adenosylmethionine, consistent with a direct function in tRNA methylation.	S-Adenosylmethionine	83-103	tRNA 1-methyladenosine methyltransferase subunit GCD14	Saccharomyces cerevisiae S288C	18-24
10371420-2	1999	S-adenosylmethionine was reported to oppose CCl4-induced fibrosis in the rat, to attenuate the consequences of the ethanol-induced oxidative stress, and to decrease mortality in cirrhotics.	S-Adenosylmethionine	0-20	C-C motif chemokine ligand 4	Rattus norvegicus	44-48
10224081-6	1999	Poly(A)-binding protein II and deletion mutants expressed in Escherichia coli were in vitro substrates for two mammalian protein arginine methyltransferases, PRMT1 and PRMT3, with S-adenosyl-L-methionine as the methyl group donor.	S-Adenosylmethionine	180-203	poly(A) binding protein nuclear 1	Bos taurus	0-26
10224081-6	1999	Poly(A)-binding protein II and deletion mutants expressed in Escherichia coli were in vitro substrates for two mammalian protein arginine methyltransferases, PRMT1 and PRMT3, with S-adenosyl-L-methionine as the methyl group donor.	S-Adenosylmethionine	180-203	protein arginine methyltransferase 1	Homo sapiens	158-163
10224081-6	1999	Poly(A)-binding protein II and deletion mutants expressed in Escherichia coli were in vitro substrates for two mammalian protein arginine methyltransferases, PRMT1 and PRMT3, with S-adenosyl-L-methionine as the methyl group donor.	S-Adenosylmethionine	180-203	protein arginine methyltransferase 3	Homo sapiens	168-173
10216131-1	1999	Liver-specific and non-liver-specific methionine adenosyltransferase (MAT) are products of two genes, MAT1A and MAT2A, respectively, that catalyze the formation of S-adenosylmethionine (SAM), the principal methyl donor.	S-Adenosylmethionine	164-184	methionine adenosyltransferase 1A	Homo sapiens	70-73
10216131-1	1999	Liver-specific and non-liver-specific methionine adenosyltransferase (MAT) are products of two genes, MAT1A and MAT2A, respectively, that catalyze the formation of S-adenosylmethionine (SAM), the principal methyl donor.	S-Adenosylmethionine	164-184	methionine adenosyltransferase 1A	Homo sapiens	102-107
10216131-1	1999	Liver-specific and non-liver-specific methionine adenosyltransferase (MAT) are products of two genes, MAT1A and MAT2A, respectively, that catalyze the formation of S-adenosylmethionine (SAM), the principal methyl donor.	S-Adenosylmethionine	164-184	methionine adenosyltransferase 2A	Homo sapiens	112-117
10216131-1	1999	Liver-specific and non-liver-specific methionine adenosyltransferase (MAT) are products of two genes, MAT1A and MAT2A, respectively, that catalyze the formation of S-adenosylmethionine (SAM), the principal methyl donor.	S-Adenosylmethionine	186-189	methionine adenosyltransferase 1A	Homo sapiens	38-68
10216131-1	1999	Liver-specific and non-liver-specific methionine adenosyltransferase (MAT) are products of two genes, MAT1A and MAT2A, respectively, that catalyze the formation of S-adenosylmethionine (SAM), the principal methyl donor.	S-Adenosylmethionine	186-189	methionine adenosyltransferase 1A	Homo sapiens	70-73
10216131-1	1999	Liver-specific and non-liver-specific methionine adenosyltransferase (MAT) are products of two genes, MAT1A and MAT2A, respectively, that catalyze the formation of S-adenosylmethionine (SAM), the principal methyl donor.	S-Adenosylmethionine	186-189	methionine adenosyltransferase 1A	Homo sapiens	102-107
10216131-1	1999	Liver-specific and non-liver-specific methionine adenosyltransferase (MAT) are products of two genes, MAT1A and MAT2A, respectively, that catalyze the formation of S-adenosylmethionine (SAM), the principal methyl donor.	S-Adenosylmethionine	186-189	methionine adenosyltransferase 2A	Homo sapiens	112-117
10448523-2	1999	The two pathways are coordinated by S-adenosylmethionine, which acts as an allosteric inhibitor of the methylenetetrahydrofolate reductase reaction and as an activator of cystathionine beta-synthase.	S-Adenosylmethionine	36-56	methylenetetrahydrofolate reductase	Homo sapiens	103-138
9920939-5	1999	Increased SAH catabolism was associated with a concomitant increase in S-adenosylmethionine catabolism.	S-Adenosylmethionine	71-91	acyl-CoA synthetase medium chain family member 3	Homo sapiens	10-13
10064789-2	1999	COMT activity was evaluated by the ability to methylate adrenaline (0.1 to 2000 microM) to metanephrine in the presence of a saturating concentration of the methyl donor (S-adenosyl-l-methionine).	S-Adenosylmethionine	171-194	catechol-O-methyltransferase	Homo sapiens	0-4
10448523-2	1999	The two pathways are coordinated by S-adenosylmethionine, which acts as an allosteric inhibitor of the methylenetetrahydrofolate reductase reaction and as an activator of cystathionine beta-synthase.	S-Adenosylmethionine	36-56	cystathionine beta-synthase	Homo sapiens	171-198
9606964-1	1998	The ERG6 gene that encodes (S)-adenosyl-L-methionine: delta 24(25)-to delta 24(28)-sterol methyl transferase (SMT) enzyme from Saccharomyces cerevisiae was introduced into plasmid pET23a(+) and the resulting native protein was overexpressed in BL21 (DE3) host cells under control of a T7 promoter.	S-Adenosylmethionine	27-52	sterol 24-C-methyltransferase	Saccharomyces cerevisiae S288C	4-8
9655679-1	1998	Liver-specific and non-liver-specific methionine adenosyltransferase (MAT) are products of two genes (MAT1A and MAT2A, respectively) that catalyze the formation of S-adenosylmethionine (SAM), the principal methyl donor.	S-Adenosylmethionine	164-184	methionine adenosyltransferase 1A	Homo sapiens	102-107
9655679-1	1998	Liver-specific and non-liver-specific methionine adenosyltransferase (MAT) are products of two genes (MAT1A and MAT2A, respectively) that catalyze the formation of S-adenosylmethionine (SAM), the principal methyl donor.	S-Adenosylmethionine	164-184	methionine adenosyltransferase 2A	Homo sapiens	112-117
9655679-1	1998	Liver-specific and non-liver-specific methionine adenosyltransferase (MAT) are products of two genes (MAT1A and MAT2A, respectively) that catalyze the formation of S-adenosylmethionine (SAM), the principal methyl donor.	S-Adenosylmethionine	186-189	methionine adenosyltransferase 1A	Homo sapiens	102-107
9655679-1	1998	Liver-specific and non-liver-specific methionine adenosyltransferase (MAT) are products of two genes (MAT1A and MAT2A, respectively) that catalyze the formation of S-adenosylmethionine (SAM), the principal methyl donor.	S-Adenosylmethionine	186-189	methionine adenosyltransferase 2A	Homo sapiens	112-117
9972236-7	1998	All the fingerprint sequences, forming parts of the cobalamin- and S-adenosylmethionine-binding sites, were completely conserved in the rat methionine synthase.	S-Adenosylmethionine	67-87	5-methyltetrahydrofolate-homocysteine methyltransferase	Rattus norvegicus	140-159
9755242-2	1998	Hepatic MAT plays an essential role in the metabolism of methionine, converting this amino acid into S-adenosylmethionine.	S-Adenosylmethionine	101-121	methionine adenosyltransferase 1A	Homo sapiens	8-11
9712709-1	1998	Phenylethanolamine N-methyltransferase (PNMT) catalyzes the production of epinephrine from norepinephrine using S-adenosyl-L-methionine as a methyl donor.	S-Adenosylmethionine	112-135	phenylethanolamine N-methyltransferase	Homo sapiens	0-38
9712709-1	1998	Phenylethanolamine N-methyltransferase (PNMT) catalyzes the production of epinephrine from norepinephrine using S-adenosyl-L-methionine as a methyl donor.	S-Adenosylmethionine	112-135	phenylethanolamine N-methyltransferase	Homo sapiens	40-44
9746350-10	1998	In the presence of AdoMet, delipidated microsomes from erg6 Ntsm1-1 efficiently converted cycloartenol into 24-methylene cycloartanol, but did not produce any 24-ethylidene lophenol upon incubation with 24-methylene lophenol.	S-Adenosylmethionine	19-25	sterol 24-C-methyltransferase	Saccharomyces cerevisiae S288C	55-59
9655336-2	1998	GNMT is a tetrameric enzyme (monomer Mr = 32,423Da, 292 amino acids) that catalyzes the transfer of a methyl group from S-adenosylmethionine (AdoMet) to glycine with the formation of S-adenosylhomocysteine (AdoHcy) and sarcosine (N-methylglycine).	S-Adenosylmethionine	120-140	glycine N-methyltransferase	Homo sapiens	0-4
9655336-2	1998	GNMT is a tetrameric enzyme (monomer Mr = 32,423Da, 292 amino acids) that catalyzes the transfer of a methyl group from S-adenosylmethionine (AdoMet) to glycine with the formation of S-adenosylhomocysteine (AdoHcy) and sarcosine (N-methylglycine).	S-Adenosylmethionine	142-148	glycine N-methyltransferase	Homo sapiens	0-4
9597750-1	1998	Glycine N-methyltransferase (EC 2.1.1.20) catalyzes the transfer of the methyl group of S-adenosylmethionine (AdoMet) to glycine to form S-adenosylhomocysteine and sarcosine.	S-Adenosylmethionine	110-116	glycine N-methyltransferase	Rattus norvegicus	0-27
9537246-8	1998	SAM level and SAM:S-adenosylhomocysteine (SAH) ratio increased by 50-75% after MAT1A transfection and by an additional 60-80% after MAT2A antisense treatment.	S-Adenosylmethionine	0-3	methionine adenosyltransferase 1A	Homo sapiens	79-84
9537246-8	1998	SAM level and SAM:S-adenosylhomocysteine (SAH) ratio increased by 50-75% after MAT1A transfection and by an additional 60-80% after MAT2A antisense treatment.	S-Adenosylmethionine	0-3	methionine adenosyltransferase 2A	Homo sapiens	132-137
9681662-3	1998	RESULTS: The activity of COMT was measured with 3,4-dihydroxybenzoic acid (242 micromol x l(-1)), the methyl acceptor substrate, and adenosyl-L-methionine (44 micromol x l(-1)), the methyl donor substrate.	S-Adenosylmethionine	133-154	catechol-O-methyltransferase	Homo sapiens	25-29
18429662-2	1998	This study showed that starfish MIS activity was present in a reactant derived from S-adenosylmethionine (SAM) by heat treatment.	S-Adenosylmethionine	84-104	anti-Mullerian hormone	Homo sapiens	32-35
9517003-1	1998	Four cDNAs for spermidine synthase (SPDS), which converts the diamine putrescine to the higher polyamine spermidine using decarboxylated S-adenosylmethionine as the co-factor, were isolated from Nicotiana sylvestris, Hyoscyamus niger, and Arabidopsis thaliana.	S-Adenosylmethionine	137-157	spermidine synthase	Nicotiana sylvestris	15-34
9517003-1	1998	Four cDNAs for spermidine synthase (SPDS), which converts the diamine putrescine to the higher polyamine spermidine using decarboxylated S-adenosylmethionine as the co-factor, were isolated from Nicotiana sylvestris, Hyoscyamus niger, and Arabidopsis thaliana.	S-Adenosylmethionine	137-157	spermidine synthase	Nicotiana sylvestris	36-40
9875556-7	1998	Restoration of mitochondrial GSH by the in vivo administration of S-adenosyl-L-methionine or the in vitro use of GSH ethyl ester prevents the susceptibility of hepatocytes to TNF.	S-Adenosylmethionine	66-89	tumor necrosis factor	Homo sapiens	175-178
18429662-2	1998	This study showed that starfish MIS activity was present in a reactant derived from S-adenosylmethionine (SAM) by heat treatment.	S-Adenosylmethionine	106-109	anti-Mullerian hormone	Homo sapiens	32-35
9337154-1	1997	Liver methionine adenosyltransferase (MAT) plays a critical role in the metabolism of methionine converting this amino acid, in the presence of ATP, into S-adenosylmethionine.	S-Adenosylmethionine	154-174	methionine adenosyltransferase 1A	Homo sapiens	38-41
9359408-0	1997	Recombinant expression of rat glycine N-methyltransferase and evidence for contribution of N-terminal acetylation to co-operative binding of S-adenosylmethionine.	S-Adenosylmethionine	141-161	glycine N-methyltransferase	Rattus norvegicus	30-57
21528287-4	1997	Treatment of human ovarian cancer cells 2008 and the cisplatin-resistant subline 2008/C13*5.25 with the S-adenosylhomocysteine hydrolase inhibitor adenosine-dialdehyde, an indirect inhibitor of transmethylation, resulted in a significant elevation (16-fold in 2008, 6-fold in 2008/C13*5.25) in the cellular content of S-adenosylhomocysteine without changing S-adenosylmethionine.	S-Adenosylmethionine	358-378	adenosylhomocysteinase	Homo sapiens	104-136
9201956-0	1997	Cobalamin-dependent methionine synthase is a modular protein with distinct regions for binding homocysteine, methyltetrahydrofolate, cobalamin, and adenosylmethionine.	S-Adenosylmethionine	148-166	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	0-39
9370326-8	1997	The activity of PEMT is regulated by supply of the substrates, phosphatidylethanolamine and S-adenosylmethionine, and by the product S-adenosylhomocysteine.	S-Adenosylmethionine	92-112	phosphatidylethanolamine N-methyltransferase	Rattus norvegicus	16-20
9207015-9	1997	The AdoMet binding site is located at the C-terminal ends of strands beta1 and beta2 and the active site is at the C-terminal ends of strands beta4 and beta5 and the N-terminal end of strand beta7.	S-Adenosylmethionine	4-10	UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2	Homo sapiens	69-74
9207015-9	1997	The AdoMet binding site is located at the C-terminal ends of strands beta1 and beta2 and the active site is at the C-terminal ends of strands beta4 and beta5 and the N-terminal end of strand beta7.	S-Adenosylmethionine	4-10	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	79-84
9188065-2	1997	This trapped cohort of PIMT is able to utilize radiolabeled S-adenosyl-L-methionine (AdoMet) introduced into the circulation to methylate blood vessel proteins containing altered aspartyl residues.	S-Adenosylmethionine	60-83	protein-L-isoaspartate (D-aspartate) O-methyltransferase 1	Rattus norvegicus	23-27
9225849-1	1997	S-adenosylmethionine decarboxylase (SAMDC; EC 4.1.4.50) is one of the key enzymes in polyamine biosynthesis, and the product of its catalytic reaction, decarboxylated S-adenosylmethionine (dcSAM), serves as an aminopropyl donor in the biosynthesis of spermidine and spermine.	S-Adenosylmethionine	0-20	adenosylmethionine decarboxylase 1	Homo sapiens	36-41
11902725-4	1997	Sporulation experiments performed in a series of supplemented media indicated that the role of SHMT in the KinB pathway is to feed the pool of C1 units recruited for the biosynthesis of key metabolites, which include the methyl donor S-adenosyl-methionine (SAM).	S-Adenosylmethionine	234-255	serine hydroxymethyltransferase 1	Homo sapiens	95-99
11902725-4	1997	Sporulation experiments performed in a series of supplemented media indicated that the role of SHMT in the KinB pathway is to feed the pool of C1 units recruited for the biosynthesis of key metabolites, which include the methyl donor S-adenosyl-methionine (SAM).	S-Adenosylmethionine	257-260	serine hydroxymethyltransferase 1	Homo sapiens	95-99
9139683-6	1997	The predicted amino acid sequence of ORF-2 (234 amino acids) contains a methyltransferase consensus sequence and shows a 22% identity with UbiG of Escherichia coli, which catalyzes S-adenosyl-L-methionine-dependent methylation of 2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone.	S-Adenosylmethionine	181-204	hypothetical protein	Escherichia coli	37-42
9139683-8	1997	The cell-free homogenate of the transformant of E. coli with an expression vector of ORF-2 catalyzed the incorporation of S-adenosyl-L-methionine into menaquinone-8, indicating that ORF-2 encodes 2-heptaprenyl-1,4-naphthoquinone methyltransferase, which participates in the terminal step of the menaquinone biosynthesis.	S-Adenosylmethionine	122-145	hypothetical protein	Escherichia coli	85-90
9139683-8	1997	The cell-free homogenate of the transformant of E. coli with an expression vector of ORF-2 catalyzed the incorporation of S-adenosyl-L-methionine into menaquinone-8, indicating that ORF-2 encodes 2-heptaprenyl-1,4-naphthoquinone methyltransferase, which participates in the terminal step of the menaquinone biosynthesis.	S-Adenosylmethionine	122-145	hypothetical protein	Escherichia coli	182-187
9188065-2	1997	This trapped cohort of PIMT is able to utilize radiolabeled S-adenosyl-L-methionine (AdoMet) introduced into the circulation to methylate blood vessel proteins containing altered aspartyl residues.	S-Adenosylmethionine	85-91	protein-L-isoaspartate (D-aspartate) O-methyltransferase 1	Rattus norvegicus	23-27
9101129-8	1997	S-Adenosylmethionine opposes CCl4-induced fibrosis and can affect some of the consequences of the ethanol-induced oxidative stress in experimental animals and in man.	S-Adenosylmethionine	0-20	C-C motif chemokine ligand 4	Rattus norvegicus	29-33
9006913-7	1997	Recombinant UPM1 protein was found to catalyze S-adenosyl-L-methionine-dependent transmethylation by UPM1 in a multistep process involving the formation of a covalently linked complex with S-adenosyl-L-methionine.	S-Adenosylmethionine	47-70	urophorphyrin methylase 1	Arabidopsis thaliana	12-16
9006913-7	1997	Recombinant UPM1 protein was found to catalyze S-adenosyl-L-methionine-dependent transmethylation by UPM1 in a multistep process involving the formation of a covalently linked complex with S-adenosyl-L-methionine.	S-Adenosylmethionine	47-70	urophorphyrin methylase 1	Arabidopsis thaliana	101-105
9006913-7	1997	Recombinant UPM1 protein was found to catalyze S-adenosyl-L-methionine-dependent transmethylation by UPM1 in a multistep process involving the formation of a covalently linked complex with S-adenosyl-L-methionine.	S-Adenosylmethionine	189-212	urophorphyrin methylase 1	Arabidopsis thaliana	12-16
9006913-7	1997	Recombinant UPM1 protein was found to catalyze S-adenosyl-L-methionine-dependent transmethylation by UPM1 in a multistep process involving the formation of a covalently linked complex with S-adenosyl-L-methionine.	S-Adenosylmethionine	189-212	urophorphyrin methylase 1	Arabidopsis thaliana	101-105
9187403-0	1997	Hydroxyindole-O-methyltransferase activity assay using high-performance liquid chromatography with fluorometric detection: determination of melatonin enzymatically formed from N-acetylserotonin and S-adenosyl-L-methionine.	S-Adenosylmethionine	198-221	acetylserotonin O-methyltransferase	Rattus norvegicus	0-33
8920979-2	1996	As a result, S-adenosylmethionine synthetase activity increased 2.3-fold, an effect that was accompanied by increased S-adenosylmethionine, a depletion of ATP and NAD levels, elevation of the S-adenosylmethionine/S-adenosylhomocysteine ratio (the methylation ratio), increased DNA methylation and polyamine levels (spermidine and spermine), and normal GSH levels.	S-Adenosylmethionine	118-138	methionine adenosyltransferase 1A	Rattus norvegicus	13-44
8985362-2	1997	MT catalyzes the transfer of the methyl group from S-adenosylmethionine (AdoMet) to position 7 of GTP, and this reaction is followed by GT-catalyzed formation of the covalent complex m7GMP-nsP1.	S-Adenosylmethionine	51-71	SH2 domain containing 3A	Homo sapiens	189-193
8985362-2	1997	MT catalyzes the transfer of the methyl group from S-adenosylmethionine (AdoMet) to position 7 of GTP, and this reaction is followed by GT-catalyzed formation of the covalent complex m7GMP-nsP1.	S-Adenosylmethionine	73-79	SH2 domain containing 3A	Homo sapiens	189-193
9247319-0	1997	Depletion of nigrostriatal and forebrain tyrosine hydroxylase by S-adenosylmethionine: a model that may explain the occurrence of depression in Parkinson"s disease.	S-Adenosylmethionine	65-85	tyrosine hydroxylase	Rattus norvegicus	41-61
9155210-1	1996	Folate and vitamin B12 are required both in the methylation of homocysteine to methionine and in the synthesis of S-adenosylmethionine.	S-Adenosylmethionine	114-134	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	19-22
8903381-1	1996	S-adenosylmethionine synthetase (SAMS) catalyzes the formation of S-adenosylmethionine (SAM) and is essential to normal cell function.	S-Adenosylmethionine	0-20	methionine adenosyltransferase 1A	Homo sapiens	33-37
8939751-0	1996	The structure of the C-terminal domain of methionine synthase: presenting S-adenosylmethionine for reductive methylation of B12.	S-Adenosylmethionine	76-94	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	42-61
8939751-0	1996	The structure of the C-terminal domain of methionine synthase: presenting S-adenosylmethionine for reductive methylation of B12.	S-Adenosylmethionine	76-94	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	124-127
8939751-7	1996	The structures of the AdoMet binding site and the cobalamin-binding domains (previously determined) provide a starting point for understanding the methyl transfer reactions of methionine synthase.	S-Adenosylmethionine	22-28	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	176-195
8903381-1	1996	S-adenosylmethionine synthetase (SAMS) catalyzes the formation of S-adenosylmethionine (SAM) and is essential to normal cell function.	S-Adenosylmethionine	33-36	methionine adenosyltransferase 1A	Homo sapiens	0-31
8755636-0	1996	Defective cystathionine beta-synthase regulation by S-adenosylmethionine in a partially pyridoxine responsive homocystinuria patient.	S-Adenosylmethionine	52-72	cystathionine beta-synthase	Homo sapiens	10-37
8703953-4	1996	In eukaryotes, the first O-methylation step is carried out by the Coq3 polypeptide, which catalyzes the transfer of a methyl group from S-adenosylmethionine to 3,4-dihydroxy-5-polyprenylbenzoate.	S-Adenosylmethionine	136-156	hexaprenyldihydroxybenzoate methyltransferase	Saccharomyces cerevisiae S288C	66-70
8706836-4	1996	The recombinant protein is activated by S-adenosylmethionine in the same range as the plant threonine synthase and evidence is presented for an involvement of the N-terminal part of the mature enzyme in the sensitivity to S-adenosylmethionine.	S-Adenosylmethionine	40-60	Pyridoxal-5'-phosphate-dependent enzyme family protein	Arabidopsis thaliana	92-110
8706836-4	1996	The recombinant protein is activated by S-adenosylmethionine in the same range as the plant threonine synthase and evidence is presented for an involvement of the N-terminal part of the mature enzyme in the sensitivity to S-adenosylmethionine.	S-Adenosylmethionine	222-242	Pyridoxal-5'-phosphate-dependent enzyme family protein	Arabidopsis thaliana	92-110
8810903-1	1996	Glycine N-methyltransferase (GNMT) from rat liver is a tetrameric enzyme with 292 amino acid residues in each identical subunit and catalyzes the S-adenosylmethionine (AdoMet) dependent methylation of glycine to form sarcosine.	S-Adenosylmethionine	146-166	glycine N-methyltransferase	Rattus norvegicus	0-27
8810903-1	1996	Glycine N-methyltransferase (GNMT) from rat liver is a tetrameric enzyme with 292 amino acid residues in each identical subunit and catalyzes the S-adenosylmethionine (AdoMet) dependent methylation of glycine to form sarcosine.	S-Adenosylmethionine	146-166	glycine N-methyltransferase	Rattus norvegicus	29-33
8810903-1	1996	Glycine N-methyltransferase (GNMT) from rat liver is a tetrameric enzyme with 292 amino acid residues in each identical subunit and catalyzes the S-adenosylmethionine (AdoMet) dependent methylation of glycine to form sarcosine.	S-Adenosylmethionine	146-166	methionine adenosyltransferase 1A	Rattus norvegicus	168-174
8755636-6	1996	The mutation was introduced in an E. coli expression system and CBS activities were measured after addition of different S-adenosylmethionine concentrations (0-200 microM).	S-Adenosylmethionine	121-141	cystathionine beta-synthase	Homo sapiens	64-67
8755636-7	1996	Again, we observed a defective stimulation of CBS activity by S-adenosylmethionine in the mutated construct, whereas the normal construct showed a threefold stimulation in activity.	S-Adenosylmethionine	62-82	cystathionine beta-synthase	Homo sapiens	46-49
8755636-8	1996	These data suggest that this D444N mutation interferes in S-adenosylmethionine regulation of CBS.	S-Adenosylmethionine	60-78	cystathionine beta-synthase	Homo sapiens	93-96
8606515-10	1996	Incubation in the presence of S-adenosyl-L-methionine also increased hepatocyte glutathione content (7.1 +/- 0.7, after 24 hr, vs 3.6 +/- 0.3 nmole/mg protein, P < 0.01), and prevented the decrease in glutathione induced by tumor necrosis factor (5.4 +/- 0.2 vs 2.1 +/- 0.1 nmole/mg protein, 100 ng/ml TNF alpha at 24 hr, P < 0.01).	S-Adenosylmethionine	30-53	tumor necrosis factor	Rattus norvegicus	305-314
8674545-4	1996	The enhanced transcription was dependent on the CBF1 gene, but did not compete with an excess of wild-type Met4p, suggesting that some changes in the affinity of Met4p to other factors might be involved in S-adenosylmethionine-mediated transcriptional regulation.	S-Adenosylmethionine	208-226	Cbf1p	Saccharomyces cerevisiae S288C	48-52
8674545-4	1996	The enhanced transcription was dependent on the CBF1 gene, but did not compete with an excess of wild-type Met4p, suggesting that some changes in the affinity of Met4p to other factors might be involved in S-adenosylmethionine-mediated transcriptional regulation.	S-Adenosylmethionine	208-226	Met4p	Saccharomyces cerevisiae S288C	162-167
8687414-1	1996	Vitamin B12-dependent methionine synthase is an important enzyme for sulphur amino acid, folate polyamine metabolism, S-adenosylmethionine metabolism and also in the methylation pathway of DNA, RNA, proteins and lipids.	S-Adenosylmethionine	118-138	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	0-41
8694756-0	1996	Probing the S-adenosylmethionine-binding site of rat guanidinoacetate methyltransferase.	S-Adenosylmethionine	12-32	guanidinoacetate N-methyltransferase	Rattus norvegicus	53-87
8694756-3	1996	To gain insight into the S-adenosyl-methionine (AdoMet)-binding site of guanidinoacetate methyltransferase, we mutated several conserved residues that are found in or near motifs I and II.	S-Adenosylmethionine	25-46	guanidinoacetate N-methyltransferase	Rattus norvegicus	72-106
8694756-3	1996	To gain insight into the S-adenosyl-methionine (AdoMet)-binding site of guanidinoacetate methyltransferase, we mutated several conserved residues that are found in or near motifs I and II.	S-Adenosylmethionine	48-54	guanidinoacetate N-methyltransferase	Rattus norvegicus	72-106
8757959-2	1996	Here we show that L929 cells, expressing human APO-1 treated with agonistic antibodies (anti-APO-1), elicit an early and transient increase of S-adenosylhomocysteine (AdoHcy), a potent inhibitor of S-adenosylmethionine (AdoMet)-dependent methylation reactions.	S-Adenosylmethionine	198-218	Fas cell surface death receptor	Homo sapiens	47-52
8757959-2	1996	Here we show that L929 cells, expressing human APO-1 treated with agonistic antibodies (anti-APO-1), elicit an early and transient increase of S-adenosylhomocysteine (AdoHcy), a potent inhibitor of S-adenosylmethionine (AdoMet)-dependent methylation reactions.	S-Adenosylmethionine	198-218	Fas cell surface death receptor	Homo sapiens	93-98
8757959-2	1996	Here we show that L929 cells, expressing human APO-1 treated with agonistic antibodies (anti-APO-1), elicit an early and transient increase of S-adenosylhomocysteine (AdoHcy), a potent inhibitor of S-adenosylmethionine (AdoMet)-dependent methylation reactions.	S-Adenosylmethionine	220-226	Fas cell surface death receptor	Homo sapiens	47-52
8757959-2	1996	Here we show that L929 cells, expressing human APO-1 treated with agonistic antibodies (anti-APO-1), elicit an early and transient increase of S-adenosylhomocysteine (AdoHcy), a potent inhibitor of S-adenosylmethionine (AdoMet)-dependent methylation reactions.	S-Adenosylmethionine	220-226	Fas cell surface death receptor	Homo sapiens	93-98
8662690-3	1996	Partially purified CLNMT isolated from rat testes had a Vmax of 540 pmol/min/mg and Km values for mushroom demethylcalmodulin and S-adenosyl-L-methionine of 230 nM and 2.0 microM, respectively.	S-Adenosylmethionine	130-153	calmodulin-lysine N-methyltransferase	Rattus norvegicus	19-24
8662690-4	1996	Kinetic analysis indicated a complex Bi Bi sequential kinetic mechanism for CLNMT where S-adenosyl-L-methionine binds initially and is followed by demethylcalmodulin binding.	S-Adenosylmethionine	88-111	calmodulin-lysine N-methyltransferase	Rattus norvegicus	76-81
8845860-4	1996	Mouse liver NNMT was a cytoplasmic enzyme with a pH optimum of 7.4 and apparent Km values for nicotinamide and S-adenosyl-L-methionine, cosubstrates for the reaction, of 370 and 6.5 microM, respectively.	S-Adenosylmethionine	111-134	nicotinamide N-methyltransferase	Mus musculus	12-16
8743048-1	1996	The ERG6 gene from Saccharomyces cerevisiae has been functionally expressed in Escherichia coli, for the first time, yielding a protein that catalyzes the bisubstrate transfer reaction whereby the reactive methyl group from (S)-adenosyl-L-methionine is transferred stereoselectively to C-24 of the sterol side chain.	S-Adenosylmethionine	224-249	sterol 24-C-methyltransferase	Saccharomyces cerevisiae S288C	4-8
8617442-3	1996	TAM-induced changes in albumin and beta-actin mRNA levels were prevented by cotreatment with S-adenosyl-L-methionine (SAM).	S-Adenosylmethionine	93-116	actin, beta	Rattus norvegicus	35-45
8617442-3	1996	TAM-induced changes in albumin and beta-actin mRNA levels were prevented by cotreatment with S-adenosyl-L-methionine (SAM).	S-Adenosylmethionine	118-121	actin, beta	Rattus norvegicus	35-45
8904527-4	1996	Methionine synthase converts cellular homocysteine to methionine and is a major enzyme in the biosynthetic pathways for folates, S-adenosylmethionine and biological methylations, sulphur amino acids and polyamines.	S-Adenosylmethionine	129-149	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	0-19
8821542-4	1996	COMT activity, evaluated by the ability to methylate adrenaline to metanephrine, was determined in liver and kidney homogenates prepared in 0.5 mM phosphate buffer (pH = 7.8) containing pargyline (0.1 mM), MgCl2 (0.1 mM), EGTA (1 mM) and S-adenosyl-L-methionine (0.1 mM).	S-Adenosylmethionine	238-261	catechol-O-methyltransferase	Rattus norvegicus	0-4
8558235-4	1996	In this work we show the following: (1) an H2S-producing enzyme, cystathionine beta-synthase (CBS), is highly expressed in the hippocampus; (2) CBS inhibitors hydroxylamine and amino-oxyacetate suppress the production of brain H2S; and (3) a CBS activator, S-adenosyl-L-methionine, enhances H2S production, indicating that CBS contributes to the production of endogenous H2S.	S-Adenosylmethionine	257-280	cystathionine beta-synthase	Homo sapiens	65-92
8558235-4	1996	In this work we show the following: (1) an H2S-producing enzyme, cystathionine beta-synthase (CBS), is highly expressed in the hippocampus; (2) CBS inhibitors hydroxylamine and amino-oxyacetate suppress the production of brain H2S; and (3) a CBS activator, S-adenosyl-L-methionine, enhances H2S production, indicating that CBS contributes to the production of endogenous H2S.	S-Adenosylmethionine	257-280	cystathionine beta-synthase	Homo sapiens	94-97
8558235-4	1996	In this work we show the following: (1) an H2S-producing enzyme, cystathionine beta-synthase (CBS), is highly expressed in the hippocampus; (2) CBS inhibitors hydroxylamine and amino-oxyacetate suppress the production of brain H2S; and (3) a CBS activator, S-adenosyl-L-methionine, enhances H2S production, indicating that CBS contributes to the production of endogenous H2S.	S-Adenosylmethionine	257-280	cystathionine beta-synthase	Homo sapiens	144-147
8558235-4	1996	In this work we show the following: (1) an H2S-producing enzyme, cystathionine beta-synthase (CBS), is highly expressed in the hippocampus; (2) CBS inhibitors hydroxylamine and amino-oxyacetate suppress the production of brain H2S; and (3) a CBS activator, S-adenosyl-L-methionine, enhances H2S production, indicating that CBS contributes to the production of endogenous H2S.	S-Adenosylmethionine	257-280	cystathionine beta-synthase	Homo sapiens	144-147
8558235-4	1996	In this work we show the following: (1) an H2S-producing enzyme, cystathionine beta-synthase (CBS), is highly expressed in the hippocampus; (2) CBS inhibitors hydroxylamine and amino-oxyacetate suppress the production of brain H2S; and (3) a CBS activator, S-adenosyl-L-methionine, enhances H2S production, indicating that CBS contributes to the production of endogenous H2S.	S-Adenosylmethionine	257-280	cystathionine beta-synthase	Homo sapiens	144-147
7586211-8	1995	The results indicate that specific 5-methyl cytosines within the hepatic p53 gene from methyl deficient rats are resistant to demethylation despite the diet-induced decrease in S-adenosylmethionine and the increase in cell proliferation associated with this dietary intervention.	S-Adenosylmethionine	177-197	Wistar clone pR53P1 p53 pseudogene	Rattus norvegicus	73-76
8524217-0	1995	Met30p, a yeast transcriptional inhibitor that responds to S-adenosylmethionine, is an essential protein with WD40 repeats.	S-Adenosylmethionine	59-79	ubiquitin-binding SDF ubiquitin ligase complex subunit MET30	Saccharomyces cerevisiae S288C	0-6
8550737-7	1996	Moreover, spermidine depletion and decarboxylated S-adenosylmethionine accumulation induced by DFMO required prior mitogenic stimulation by E2 and/or IGF-I.	S-Adenosylmethionine	50-70	insulin like growth factor 1	Homo sapiens	150-155
8748929-9	1995	S-adenosylmethionine (AdoMet), the limiting factor in the methylation process, was injected into the lateral ventricle of rats.	S-Adenosylmethionine	0-20	methionine adenosyltransferase 1A	Rattus norvegicus	22-28
7703232-7	1995	The distinctive difference between the enzyme forms was also the higher affinity of MB-COMT for the coenzyme S-adenosyl-L-methionine (AdoMet).	S-Adenosylmethionine	109-132	catechol-O-methyltransferase	Homo sapiens	87-91
7557886-1	1995	Carbon tetrachloride (CCl4) administration to rats produces hepatic cirrhosis and supplementation with S-adenosylmethionine (SAM) can partially prevent CCl4-induced liver injury.	S-Adenosylmethionine	103-123	C-C motif chemokine ligand 4	Rattus norvegicus	152-156
7557886-1	1995	Carbon tetrachloride (CCl4) administration to rats produces hepatic cirrhosis and supplementation with S-adenosylmethionine (SAM) can partially prevent CCl4-induced liver injury.	S-Adenosylmethionine	125-128	C-C motif chemokine ligand 4	Rattus norvegicus	152-156
7557886-8	1995	SAM treatment partially prevented (P < .05) the reduction of the ratio SAM/SAH induced by CCl4.	S-Adenosylmethionine	0-3	C-C motif chemokine ligand 4	Rattus norvegicus	93-97
11607550-2	1995	Because of the importance of SAHH in a number of S-adenosylmethionine-dependent transmethylation reactions, particularly the 5" capping of mRNA during viral replication, SAHH has been considered as a target of potential antiviral agents against animal viruses.	S-Adenosylmethionine	51-69	adenosylhomocysteinase	Nicotiana tabacum	29-33
11607550-2	1995	Because of the importance of SAHH in a number of S-adenosylmethionine-dependent transmethylation reactions, particularly the 5" capping of mRNA during viral replication, SAHH has been considered as a target of potential antiviral agents against animal viruses.	S-Adenosylmethionine	51-69	adenosylhomocysteinase	Nicotiana tabacum	170-174
7748194-1	1995	The S-adenosylmethionine (AdoMet) analogue AdoMac [S-(5"-deoxy-5"-adenosyl)-1-ammonio-4-methylsulfonio-2-cyclopen ten e], an enzyme-activated, irreversible inhibitor of the Escherchia coli form of S-adenosylmethionine decarboxylase (AdoMet-DC), also acts as a potent inhibitor of the human form of the enzyme.	S-Adenosylmethionine	4-24	adenosylmethionine decarboxylase 1	Homo sapiens	197-231
7748194-1	1995	The S-adenosylmethionine (AdoMet) analogue AdoMac [S-(5"-deoxy-5"-adenosyl)-1-ammonio-4-methylsulfonio-2-cyclopen ten e], an enzyme-activated, irreversible inhibitor of the Escherchia coli form of S-adenosylmethionine decarboxylase (AdoMet-DC), also acts as a potent inhibitor of the human form of the enzyme.	S-Adenosylmethionine	4-24	adenosylmethionine decarboxylase 1	Homo sapiens	233-242
7748194-1	1995	The S-adenosylmethionine (AdoMet) analogue AdoMac [S-(5"-deoxy-5"-adenosyl)-1-ammonio-4-methylsulfonio-2-cyclopen ten e], an enzyme-activated, irreversible inhibitor of the Escherchia coli form of S-adenosylmethionine decarboxylase (AdoMet-DC), also acts as a potent inhibitor of the human form of the enzyme.	S-Adenosylmethionine	26-32	adenosylmethionine decarboxylase 1	Homo sapiens	197-231
7748194-1	1995	The S-adenosylmethionine (AdoMet) analogue AdoMac [S-(5"-deoxy-5"-adenosyl)-1-ammonio-4-methylsulfonio-2-cyclopen ten e], an enzyme-activated, irreversible inhibitor of the Escherchia coli form of S-adenosylmethionine decarboxylase (AdoMet-DC), also acts as a potent inhibitor of the human form of the enzyme.	S-Adenosylmethionine	26-32	adenosylmethionine decarboxylase 1	Homo sapiens	233-242
11607550-1	1995	S-Adenosylhomocysteine hydrolase (SAHH) is a key enzyme in transmethylation reactions that use S-adenosylmethionine as the methyl donor.	S-Adenosylmethionine	95-115	adenosylhomocysteinase	Homo sapiens	0-32
11607550-1	1995	S-Adenosylhomocysteine hydrolase (SAHH) is a key enzyme in transmethylation reactions that use S-adenosylmethionine as the methyl donor.	S-Adenosylmethionine	95-115	adenosylhomocysteinase	Homo sapiens	34-38
7663167-1	1995	Protein L-isoaspartyl methyltransferase (PIMT) methylates isoaspartyl residues in peptides and proteins using S-adenosyl-L-methionine as the methyl donor.	S-Adenosylmethionine	110-133	protein-L-isoaspartate (D-aspartate) O-methyltransferase	Homo sapiens	0-39
7663167-1	1995	Protein L-isoaspartyl methyltransferase (PIMT) methylates isoaspartyl residues in peptides and proteins using S-adenosyl-L-methionine as the methyl donor.	S-Adenosylmethionine	110-133	protein-L-isoaspartate (D-aspartate) O-methyltransferase	Homo sapiens	41-45
7752200-9	1995	Thus, the S-adenosylmethionine analogue trans-1S,4S-AdoMao acts as an effective inhibitor of AdoMet-DC and appears to serve as a parasite-specific trypanocidal agent in vitro.	S-Adenosylmethionine	10-30	adenosylmethionine decarboxylase 1	Homo sapiens	93-102
7703232-7	1995	The distinctive difference between the enzyme forms was also the higher affinity of MB-COMT for the coenzyme S-adenosyl-L-methionine (AdoMet).	S-Adenosylmethionine	134-140	catechol-O-methyltransferase	Homo sapiens	87-91
7897657-1	1995	The DNA methyltransferases, M.HhaI and M.TaqI, and catechol O-methyl-transferase (COMT) catalyze the transfer of a methyl group from the cofactor S-adenosyl-L-methionine (AdoMet) to carbon-5 of cytosine, to nitrogen-6 of adenine, and to a hydroxyl group of catechol, respectively.	S-Adenosylmethionine	148-169	catechol-O-methyltransferase	Homo sapiens	51-80
7640156-5	1995	Kinetic studies demonstrated that the inhibition of TPMT by sulphasalazine and ASA isomers was non-competitive with regard to the thiopurine substrate, 6-MP, and was uncompetitive with regard to the methyl donor for the reaction, S-adenosyl-L-methionine.	S-Adenosylmethionine	230-253	thiopurine S-methyltransferase	Homo sapiens	52-56
7897657-1	1995	The DNA methyltransferases, M.HhaI and M.TaqI, and catechol O-methyl-transferase (COMT) catalyze the transfer of a methyl group from the cofactor S-adenosyl-L-methionine (AdoMet) to carbon-5 of cytosine, to nitrogen-6 of adenine, and to a hydroxyl group of catechol, respectively.	S-Adenosylmethionine	148-169	catechol-O-methyltransferase	Homo sapiens	82-86
7897657-1	1995	The DNA methyltransferases, M.HhaI and M.TaqI, and catechol O-methyl-transferase (COMT) catalyze the transfer of a methyl group from the cofactor S-adenosyl-L-methionine (AdoMet) to carbon-5 of cytosine, to nitrogen-6 of adenine, and to a hydroxyl group of catechol, respectively.	S-Adenosylmethionine	171-177	catechol-O-methyltransferase	Homo sapiens	51-80
7897657-1	1995	The DNA methyltransferases, M.HhaI and M.TaqI, and catechol O-methyl-transferase (COMT) catalyze the transfer of a methyl group from the cofactor S-adenosyl-L-methionine (AdoMet) to carbon-5 of cytosine, to nitrogen-6 of adenine, and to a hydroxyl group of catechol, respectively.	S-Adenosylmethionine	171-177	catechol-O-methyltransferase	Homo sapiens	82-86
7890685-10	1995	Importantly, the protein encoded by the intronless gene was functional, i.e. it catalyzed the decarboxylation of S-adenosylmethionine, and its specific activity was comparable with that of recombinant human AdoMetDC purified according to the same procedure.	S-Adenosylmethionine	113-133	adenosylmethionine decarboxylase 1	Homo sapiens	207-215
7773746-4	1995	Structural comparison of HhaI C5-cytosine methyltransferase, TaqI N6-adenine methyltransferase, and catechol O-methyltransferase reveals a common catalytic domain structure, which might be universal among S-adenosyl-L-methionine (SAM)-dependent methyltransferases.	S-Adenosylmethionine	207-228	catechol-O-methyltransferase	Homo sapiens	61-128
7773746-4	1995	Structural comparison of HhaI C5-cytosine methyltransferase, TaqI N6-adenine methyltransferase, and catechol O-methyltransferase reveals a common catalytic domain structure, which might be universal among S-adenosyl-L-methionine (SAM)-dependent methyltransferases.	S-Adenosylmethionine	230-233	catechol-O-methyltransferase	Homo sapiens	61-128
7998928-3	1994	6-MP is converted into tIMP, and thereafter it is methylated to Me-tIMP by thiopurine methyltransferase, an S-adenosylmethionine (S-Ado-Met)-dependent conversion.	S-Adenosylmethionine	108-128	TIMP metallopeptidase inhibitor 1	Homo sapiens	67-71
7819283-1	1995	Thioether S-methyltransferase catalyzes transfer of the methyl group from S-adenosylmethionine to X in compounds of the structure R-X-R", where X may be sulfur, selenium, or tellurium, and R and R" may be various organic groups.	S-Adenosylmethionine	74-94	indolethylamine N-methyltransferase	Mus musculus	0-29
7529961-3	1995	Glycine N-methyltransferase, an enzyme which regulates the ratio of S-adenosylmethionine to S-adenosylhomocysteine, is particularly abundant in the exocrine pancreas.	S-Adenosylmethionine	69-88	glycine N-methyltransferase	Rattus norvegicus	0-27
7799928-0	1995	Functional analysis of Met4, a yeast transcriptional activator responsive to S-adenosylmethionine.	S-Adenosylmethionine	77-97	Met4p	Saccharomyces cerevisiae S288C	23-27
7799928-2	1995	In this report, we show that one mechanism permitting the repression of the sulfur network by S-adenosylmethionine (AdoMet) involves inhibition of the transcriptional activation function of Met4.	S-Adenosylmethionine	94-114	Met4p	Saccharomyces cerevisiae S288C	190-194
7799928-2	1995	In this report, we show that one mechanism permitting the repression of the sulfur network by S-adenosylmethionine (AdoMet) involves inhibition of the transcriptional activation function of Met4.	S-Adenosylmethionine	116-122	Met4p	Saccharomyces cerevisiae S288C	190-194
7803479-4	1994	The Km value of the enzyme for S-adenosylmethionine was 16 microM, which is two times higher than that of previously reported S-adenosylmethionine decarboxylase (SAMDC I) (8.1 microM).	S-Adenosylmethionine	31-51	S-adenosylmethionine decarboxylase	Glycine max	126-160
7803479-4	1994	The Km value of the enzyme for S-adenosylmethionine was 16 microM, which is two times higher than that of previously reported S-adenosylmethionine decarboxylase (SAMDC I) (8.1 microM).	S-Adenosylmethionine	31-51	S-adenosylmethionine decarboxylase	Glycine max	162-167
7998928-3	1994	6-MP is converted into tIMP, and thereafter it is methylated to Me-tIMP by thiopurine methyltransferase, an S-adenosylmethionine (S-Ado-Met)-dependent conversion.	S-Adenosylmethionine	130-139	TIMP metallopeptidase inhibitor 1	Homo sapiens	23-27
7998928-3	1994	6-MP is converted into tIMP, and thereafter it is methylated to Me-tIMP by thiopurine methyltransferase, an S-adenosylmethionine (S-Ado-Met)-dependent conversion.	S-Adenosylmethionine	130-139	TIMP metallopeptidase inhibitor 1	Homo sapiens	67-71
7998928-8	1994	The effects of both 6-MP and Me-MPR can be ascribed to a decreased conversion of methionine into S-Ado-Met, due to the ATP depletion induced by the inhibition of purine synthesis de novo by Me-tIMP.	S-Adenosylmethionine	97-106	TIMP metallopeptidase inhibitor 1	Homo sapiens	193-197
7961628-5	1994	This enzyme, like the methionine synthase from Escherichia coli is dependent on S-adenosylmethionine for activity.	S-Adenosylmethionine	80-100	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	22-41
7866549-3	1994	The assay is based on the TPMT-catalysed conversion of 6-MP to 6-methylmercaptopurine (methyl-MP) with non-radioactive S-adenosyl-L-methionine as the methyl donor.	S-Adenosylmethionine	119-142	thiopurine S-methyltransferase	Homo sapiens	26-30
7994174-1	1994	S-Adenosyl-L-methionine synthetase (SAM-S) catalyzes the conversion of L-methionine and ATP into S-adenosyl-L-methionine.	S-Adenosylmethionine	97-120	S-adenosylmethionine synthase 1	Nicotiana tabacum	36-41
7933125-11	1994	The methyltransferase activities in the P15 fractions of SFV-infected BHK cells and AcNPV-nsP1-infected Sf9 cells and in E. coli catalyzed linear incorporation of the [3H]methyl group from S-adenosylmethionine to GTP for a 60-min period.	S-Adenosylmethionine	189-209	SH2 domain containing 3A	Homo sapiens	90-94
7929015-3	1994	Since spe1 delta SPE2 cells can synthesize decarboxylated adenosylmethionine (dcAdoMet), these data indicate that dcAdoMet may be toxic to amine-deficient cells.	S-Adenosylmethionine	58-76	ornithine decarboxylase SPE1	Saccharomyces cerevisiae S288C	6-10
7929015-3	1994	Since spe1 delta SPE2 cells can synthesize decarboxylated adenosylmethionine (dcAdoMet), these data indicate that dcAdoMet may be toxic to amine-deficient cells.	S-Adenosylmethionine	58-76	adenosylmethionine decarboxylase SPE2	Saccharomyces cerevisiae S288C	17-21
7929130-6	1994	When HPr-2 was incubated with S-adenosylmethionine and the methyltransferase, the bulk of the L-isoaspartyl residues at position 12 was converted to L-aspartyl residues.	S-Adenosylmethionine	30-50	heparanase 2 (inactive)	Homo sapiens	5-10
7994174-1	1994	S-Adenosyl-L-methionine synthetase (SAM-S) catalyzes the conversion of L-methionine and ATP into S-adenosyl-L-methionine.	S-Adenosylmethionine	97-120	S-adenosylmethionine synthase 1	Nicotiana tabacum	0-34
7996385-1	1994	Catechol-O-methyltransferase (COMT) catalyses the transfer of the methyl group from S-adenyl-L-methionine (SAM) to one of the hydroxy groups of a catechol, usually the hydroxy group in position 3.	S-Adenosylmethionine	107-110	catechol-O-methyltransferase	Rattus norvegicus	30-34
7996385-1	1994	Catechol-O-methyltransferase (COMT) catalyses the transfer of the methyl group from S-adenyl-L-methionine (SAM) to one of the hydroxy groups of a catechol, usually the hydroxy group in position 3.	S-Adenosylmethionine	107-110	catechol-O-methyltransferase	Rattus norvegicus	0-28
8280752-2	1994	S-Adenosylmethionine (AdoMet) is an important biologic methylating agent for nucleic acids, phospholipids, biologic amines, and proteins.	S-Adenosylmethionine	0-20	methionine adenosyltransferase 1A	Rattus norvegicus	22-28
7910516-0	1994	Correlation between S-adenosyl-L-methionine content and production of c-myc, c-Ha-ras, and c-Ki-ras mRNA transcripts in the early stages of rat liver carcinogenesis.	S-Adenosylmethionine	20-43	MYC proto-oncogene, bHLH transcription factor	Rattus norvegicus	70-75
7910516-0	1994	Correlation between S-adenosyl-L-methionine content and production of c-myc, c-Ha-ras, and c-Ki-ras mRNA transcripts in the early stages of rat liver carcinogenesis.	S-Adenosylmethionine	20-43	KRAS proto-oncogene, GTPase	Rattus norvegicus	91-99
7943660-4	1994	Phosphatidylethanolamine N-methyltransferase activity was measured in sequential percutaneous needle liver biopsies by the conversion of phosphatidylethanolamine to phosphatidylcholine, using radioactive S-adenosylmethionine as a methyl donor.	S-Adenosylmethionine	204-224	phosphatidylethanolamine N-methyltransferase	Homo sapiens	0-44
8196654-5	1994	Complementation studies in vitro revealed that both cytosol and S-adenosylmethionine are required for the hypermethylation of an m7G-capped U1 snRNP reconstituted in vitro, indicating that the U1 snRNA-(guanosine-N2)-methyltransferase is a trans-active non-snRNP protein.	S-Adenosylmethionine	64-84	glutamate receptor KA2 L homeolog	Xenopus laevis	140-148
8196654-5	1994	Complementation studies in vitro revealed that both cytosol and S-adenosylmethionine are required for the hypermethylation of an m7G-capped U1 snRNP reconstituted in vitro, indicating that the U1 snRNA-(guanosine-N2)-methyltransferase is a trans-active non-snRNP protein.	S-Adenosylmethionine	64-84	glutamate receptor KA2 L homeolog	Xenopus laevis	193-201
8195133-0	1994	Location of the S-adenosyl-L-methionine binding region of the vaccinia virus mRNA (guanine-7-)methyltransferase.	S-Adenosylmethionine	18-39	RNA (guanine-7-) methyltransferase	Mus musculus	77-111
8182091-12	1994	Human liver NNMT and transfected COS-1 cell NNMT had apparent Km values for the two cosubstrates for the reaction, nicotinamide and S-adenosyl-L-methionine, of 0.43 and 0.38 mM and of 1.8 and 2.2 microM, respectively.	S-Adenosylmethionine	132-155	nicotinamide N-methyltransferase	Homo sapiens	12-16
8182091-12	1994	Human liver NNMT and transfected COS-1 cell NNMT had apparent Km values for the two cosubstrates for the reaction, nicotinamide and S-adenosyl-L-methionine, of 0.43 and 0.38 mM and of 1.8 and 2.2 microM, respectively.	S-Adenosylmethionine	132-155	nicotinamide N-methyltransferase	Homo sapiens	44-48
8123667-4	1994	The enzyme formed a mixture of mono-, di-, and trimethyllysine residues at lysine 115 of calmodulin in vitro, had a Km for the methyl donor, S-adenosyl methionine (AdoMet), of about 1 microM and a pH optimum of about 7.5.	S-Adenosylmethionine	141-162	calmodulin 1	Homo sapiens	89-99
8123667-4	1994	The enzyme formed a mixture of mono-, di-, and trimethyllysine residues at lysine 115 of calmodulin in vitro, had a Km for the methyl donor, S-adenosyl methionine (AdoMet), of about 1 microM and a pH optimum of about 7.5.	S-Adenosylmethionine	164-170	calmodulin 1	Homo sapiens	89-99
8135750-4	1994	55, 131-138], we proposed that homocysteinaemia arises from an interruption in S-adenosylmethionine"s (AdoMet) coordinate regulation of homocysteine metabolism.	S-Adenosylmethionine	103-109	methionine adenosyltransferase 1A	Rattus norvegicus	79-101
8135750-12	1994	Like AdoMet, S-adenosylethionine is an activator of cystathionine beta-synthase and will effectively promote the catabolism of homocysteine through cystathionine synthesis.	S-Adenosylmethionine	5-11	cystathionine beta synthase	Rattus norvegicus	52-79
8312439-1	1994	Guanidinoacetate methyltransferase (GAMT) catalyzes the last step of the biosynthetic pathway to creatine (Cr), the transfer of a methyl group from S-adenosylmethionine to guanidinoactate.	S-Adenosylmethionine	148-168	guanidinoacetate methyltransferase	Mus musculus	0-34
8312439-1	1994	Guanidinoacetate methyltransferase (GAMT) catalyzes the last step of the biosynthetic pathway to creatine (Cr), the transfer of a methyl group from S-adenosylmethionine to guanidinoactate.	S-Adenosylmethionine	148-168	guanidinoacetate methyltransferase	Mus musculus	36-40
7967489-4	1994	CBS, a tetramer of these subunits, binds its two substrates, homocysteine and serine, and three additional ligands: pyridoxal 5"-phosphate, S-adenosylmethionine, and haem.	S-Adenosylmethionine	140-160	cystathionine beta-synthase	Homo sapiens	0-3
8278461-1	1993	Methionine adenosyltransferase (MAT), a key enzyme in metabolism, catalyzes the synthesis of one of the most important and pivotal biological molecules, S-adenosyl-methionine.	S-Adenosylmethionine	153-174	methionine adenosyltransferase 1A	Homo sapiens	0-30
8295845-4	1993	The high erythrocytic uroporphyrinogen synthetase (URO-S) activity noticed in Pb administered rats, was significantly (P < 0.001) reduced in animals treated either with zinc or with SAM.	S-Adenosylmethionine	185-188	uroporphyrinogen III synthase	Rattus norvegicus	51-56
8147263-12	1993	When the concentration of the cosubstrate for the reaction, S-adenosyl-L-methionine, was varied in the presence of variable concentrations of pargyline, inhibition of HNMT by pargyline was noncompetitive with regard to the methyl donor, with Kii and Kis values of 1.23 and 0.95 mM, respectively.	S-Adenosylmethionine	60-83	histamine N-methyltransferase	Homo sapiens	167-171
1460050-5	1992	The first is an activation of the reductase by dA1 and RT and requires S-adenosylmethionine, NADPH, dithiothreitol, and possibly K+ ions.	S-Adenosylmethionine	71-91	anon-A1	Drosophila melanogaster	47-50
8468468-1	1993	Defects in the enzymes involved in the pathway of S-adenosylmethionine (AdoMet) metabolism, or inhibition of those enzymes, results in profound immunodeficiency.	S-Adenosylmethionine	50-70	methionine adenosyltransferase I, alpha	Mus musculus	72-78
8458902-2	1993	This assay requires a partially purified PNMT preparation derived from bovine adrenals, with noradrenaline and S-adenosyl-L-methionine (SAM) as co-substrates.	S-Adenosylmethionine	111-134	phenylethanolamine N-methyltransferase	Bos taurus	41-45
8458902-2	1993	This assay requires a partially purified PNMT preparation derived from bovine adrenals, with noradrenaline and S-adenosyl-L-methionine (SAM) as co-substrates.	S-Adenosylmethionine	136-139	phenylethanolamine N-methyltransferase	Bos taurus	41-45
8333583-3	1993	The action of the ethanol results in an increase in the hepatic level of the substrate N5-methyltetrahydrofolate but as an adaptive mechanism, betaine homocysteine methyltransferase, is induced in order to maintain hepatic S-adenosylmethionine at normal levels.	S-Adenosylmethionine	223-243	betaine-homocysteine S-methyltransferase	Rattus norvegicus	143-181
1332963-1	1992	Glycine N-methyltransferase (GNMT) regulates the ratio of S-adenosylmethionine to S-adenosylhomocysteine.	S-Adenosylmethionine	58-78	glycine N-methyltransferase	Homo sapiens	0-27
1332963-1	1992	Glycine N-methyltransferase (GNMT) regulates the ratio of S-adenosylmethionine to S-adenosylhomocysteine.	S-Adenosylmethionine	58-78	glycine N-methyltransferase	Homo sapiens	29-33
1480164-8	1992	The specificity of labeling of AdoMetDC by this procedure was confirmed by the prevention of 35S-decarboxylated S-adenosylmethionine (AdoMet) binding in the presence of specific AdoMetDC inhibitors [either methylglyoxal bis(guanylhydrazone (MGBG), a reversible inhibitor, or 5"-deoxy-5"-[(2-hydrazinoethyl)methylamino]adenosine (MHZEA), an irreversible inactivator].	S-Adenosylmethionine	112-132	adenosylmethionine decarboxylase 1	Homo sapiens	31-39
1469689-4	1992	The assayed compounds showed a reversible inhibition of COMT, which was mixed for all the dihydroxynitro derivatives but noncompetitive for 3-hydroxy-4-methoxy-5-nitrobenzaldehyde when pyrocatechol was the variable substrate and uncompetitive in all the inhibitors with respect to S-adenosyl-L-methionine.	S-Adenosylmethionine	281-304	catechol-O-methyltransferase	Sus scrofa	56-60
1480164-8	1992	The specificity of labeling of AdoMetDC by this procedure was confirmed by the prevention of 35S-decarboxylated S-adenosylmethionine (AdoMet) binding in the presence of specific AdoMetDC inhibitors [either methylglyoxal bis(guanylhydrazone (MGBG), a reversible inhibitor, or 5"-deoxy-5"-[(2-hydrazinoethyl)methylamino]adenosine (MHZEA), an irreversible inactivator].	S-Adenosylmethionine	112-132	adenosylmethionine decarboxylase 1	Homo sapiens	178-186
1480164-8	1992	The specificity of labeling of AdoMetDC by this procedure was confirmed by the prevention of 35S-decarboxylated S-adenosylmethionine (AdoMet) binding in the presence of specific AdoMetDC inhibitors [either methylglyoxal bis(guanylhydrazone (MGBG), a reversible inhibitor, or 5"-deoxy-5"-[(2-hydrazinoethyl)methylamino]adenosine (MHZEA), an irreversible inactivator].	S-Adenosylmethionine	31-37	adenosylmethionine decarboxylase 1	Homo sapiens	178-186
1325535-2	1992	The formation of 2-methoxyestrone (2-OHE1 2-Me) from 2-hydroxyestrone (2-OHE1) by catechol-O-methyltransferase (COMT) was followed by measuring the transfer of the radiolabeled methyl group from S-adenosylmethionine.	S-Adenosylmethionine	195-215	catechol-O-methyltransferase	Rattus norvegicus	82-110
1417958-0	1992	The relationship between the activity of methionine synthase and the ratio of S-adenosylmethionine to S-adenosylhomocysteine in the brain and other tissues of the pig.	S-Adenosylmethionine	78-98	5-methyltetrahydrofolate-homocysteine methyltransferase	Sus scrofa	41-60
1417958-1	1992	Using nitrous oxide to inactivate methionine synthase in vivo, the relationship of the activity of methionine synthase to the S-adenosylmethionine (AdoMet)/S-adenosylhomocysteine (AdoHcy) ratio was examined in neural and other tissues of the pig.	S-Adenosylmethionine	126-146	5-methyltetrahydrofolate-homocysteine methyltransferase	Sus scrofa	99-118
1530666-4	1992	HNMT inhibition by harmaline was competitive with respect to both substrates, S-adenosylmethionine and histamine (Ki = 1.4 microM).	S-Adenosylmethionine	78-98	histamine N-methyltransferase	Rattus norvegicus	0-4
1306116-5	1992	Human liver TPMT is a cytoplasmic enzyme and the Km values for 6-MP and S-adenosyl-L-methionine, cosubstrates for the reaction, were 580 microM and 2.7 microM, respectively.	S-Adenosylmethionine	72-95	thiopurine S-methyltransferase	Homo sapiens	12-16
1631127-3	1992	Insertion mutants in ahcY lack detectable S-adenosyl-L-homocysteine hydrolase activity and, as a consequence, S-adenosyl-L-homocysteine accumulates in the cells, resulting in a 16-fold decrease in the intracellular ratio of S-adenosyl-L-methionine to S-adenosyl-L-homocysteine as compared to wild-type cells.	S-Adenosylmethionine	224-247	adenosylhomocysteinase	Homo sapiens	21-25
1631127-5	1992	The ahcY mutant, when grown in supplemented medium, synthesizes significantly reduced levels of bacteriochlorophyll, indicating that modulation of the intracellular ratio of S-adenosyl-L-methionine to S-adenosyl-L-homocysteine may be an important factor in regulating bacteriochlorophyll biosynthesis.	S-Adenosylmethionine	174-197	adenosylhomocysteinase	Homo sapiens	4-8
1466504-5	1992	S-Adenosyl-methionine decreased dose-dependently the synthesis of fibronectin, as well as the content of fibronectin and keratan sulfate.	S-Adenosylmethionine	0-21	fibronectin 1	Canis lupus familiaris	66-77
1466504-5	1992	S-Adenosyl-methionine decreased dose-dependently the synthesis of fibronectin, as well as the content of fibronectin and keratan sulfate.	S-Adenosylmethionine	0-21	fibronectin 1	Canis lupus familiaris	105-116
1415709-2	1992	SAMDC decarboxylates S-adenosylmethionine, which then donates aminopropyl groups for spermidine and spermine synthesis.	S-Adenosylmethionine	21-41	adenosylmethionine decarboxylase 1	Rattus norvegicus	0-5
1398482-0	1992	S-adenosylmethionine treatment prevents carbon tetrachloride-induced S-adenosylmethionine synthetase inactivation and attenuates liver injury.	S-Adenosylmethionine	0-20	methionine adenosyltransferase 1A	Rattus norvegicus	69-100
1510725-5	1992	Our experiments were performed to determine whether S-adenosyl-L-methionine (Ado-Met), the methyl donor for the TPMT reaction, could be used as a photoaffinity ligand for these isozymes as one step in the study of the molecular basis for the TPMT genetic polymorphism.	S-Adenosylmethionine	52-75	thiopurine S-methyltransferase	Homo sapiens	112-116
1510725-5	1992	Our experiments were performed to determine whether S-adenosyl-L-methionine (Ado-Met), the methyl donor for the TPMT reaction, could be used as a photoaffinity ligand for these isozymes as one step in the study of the molecular basis for the TPMT genetic polymorphism.	S-Adenosylmethionine	52-75	thiopurine S-methyltransferase	Homo sapiens	242-246
1510725-5	1992	Our experiments were performed to determine whether S-adenosyl-L-methionine (Ado-Met), the methyl donor for the TPMT reaction, could be used as a photoaffinity ligand for these isozymes as one step in the study of the molecular basis for the TPMT genetic polymorphism.	S-Adenosylmethionine	77-84	thiopurine S-methyltransferase	Homo sapiens	112-116
1510725-5	1992	Our experiments were performed to determine whether S-adenosyl-L-methionine (Ado-Met), the methyl donor for the TPMT reaction, could be used as a photoaffinity ligand for these isozymes as one step in the study of the molecular basis for the TPMT genetic polymorphism.	S-Adenosylmethionine	77-84	thiopurine S-methyltransferase	Homo sapiens	242-246
1325535-2	1992	The formation of 2-methoxyestrone (2-OHE1 2-Me) from 2-hydroxyestrone (2-OHE1) by catechol-O-methyltransferase (COMT) was followed by measuring the transfer of the radiolabeled methyl group from S-adenosylmethionine.	S-Adenosylmethionine	195-215	catechol-O-methyltransferase	Rattus norvegicus	112-116
1735533-4	1992	In both mouse models, S-adenosylmethionine reduced depletion of plasma (median = 20.8 mumol/L vs. 14.6 mumol/L) and liver glutathione (198% vs. 100%; p less than 0.05), liver damage and release of AST after acetaminophen administration.	S-Adenosylmethionine	22-42	solute carrier family 17 (anion/sugar transporter), member 5	Mus musculus	197-200
1567883-0	1992	Identification of a tyrosine residue in rat guanidinoacetate methyltransferase that is photolabeled with S-adenosyl-L-methionine.	S-Adenosylmethionine	105-128	guanidinoacetate N-methyltransferase	Rattus norvegicus	44-78
1549123-9	1992	Moreover, an 18-bp fragment of the MET25 5" upstream region was found to confer S-adenosylmethionine-dependent regulation of a fusion gene.	S-Adenosylmethionine	82-100	bifunctional cysteine synthase/O-acetylhomoserine aminocarboxypropyltransferase MET17	Saccharomyces cerevisiae S288C	35-40
1590912-5	1992	This hypothesis was tested by reacting SAM, MPP+, or MPTP with dopamine in the presence of catechol-O-methyltransferase and measuring the methylated product of dopamine produced.	S-Adenosylmethionine	39-42	catechol-O-methyltransferase	Homo sapiens	91-119
2019995-5	1991	Treatment of cells with A-4, A-5 and HC-3 resulted in an increase in the incorporation of S-adenosyl-methionine into phosphatidylcholine.	S-Adenosylmethionine	90-111	ATPase, H+ transporting, lysosomal V0 subunit A4	Mus musculus	24-27
1951678-9	1991	CSAD activity may be specifically regulated by sulfur amino acids metabolized by the S-adenosylmethionine-dependent pathway of methionine metabolism.	S-Adenosylmethionine	87-105	cysteine sulfinic acid decarboxylase	Rattus norvegicus	0-4
16668418-1	1991	S-Adenosyl-l-methionine:caffeic acid 3-O-methyltransferase (COMT, EC 2.1.1.6) catalyzes the conversion of caffeic acid to ferulic acid, a key step in the biosynthesis of lignin monomers.	S-Adenosylmethionine	0-23	catechol-O-methyltransferase	Homo sapiens	60-64
1886293-4	1991	The IC50 values for THA, 9-aminoacridine and physostigmine in the inhibition of HMT determined at fixed concentrations of histamine (20 microM) and S-adenosylmethionine (50 microM) were 0.2, 0.37 and 20 microM, respectively.	S-Adenosylmethionine	148-168	histamine N-methyltransferase	Mus musculus	80-83
2019995-5	1991	Treatment of cells with A-4, A-5 and HC-3 resulted in an increase in the incorporation of S-adenosyl-methionine into phosphatidylcholine.	S-Adenosylmethionine	90-111	laminin, alpha 5	Mus musculus	29-32
2260986-4	1990	The above data are consistent with the metabolism of SAM to ATP by a route recently identified by us whereby ATP is formed from deoxyadenosine: namely binding to the enzyme S-adenosylhomocysteine hydrolase with subsequent release of adenine and further conversion to ATP via APRT.	S-Adenosylmethionine	53-56	adenosylhomocysteinase	Homo sapiens	173-205
1990977-6	1991	An equilibrium binding study shows that guanidinoacetate methyltransferase in the free form binds AdoMet but not guanidinoacetate.	S-Adenosylmethionine	98-104	guanidinoacetate N-methyltransferase	Rattus norvegicus	40-74
16667960-7	1991	As with the tomato enzyme, apple ACC synthase was inactivated and radiolabeled by its substrate S-adenosyl-l-methionine.	S-Adenosylmethionine	96-119	1-aminocyclopropane-1-carboxylate synthase 7-like	Malus domestica	33-45
16667960-8	1991	Apple ACC synthase was identified to be a 48-kilodalton protein based on the observation that it was specifically bound to immunoaffinity column and it was specifically radiolabeled by its substrate S-adenosyl-l-methionine.	S-Adenosylmethionine	199-222	1-aminocyclopropane-1-carboxylate synthase 7-like	Malus domestica	6-18
2013278-2	1991	A potent irreversible inhibitor of S-adenosylmethionine (AdoMet) decarboxylase, S-(5"-adenosyl)-methylthio-2-aminooxyethane (AdoMeSaoe), was used to study the regulatory control of this key enzyme in the polyamine biosynthetic pathway.	S-Adenosylmethionine	35-55	methionine adenosyltransferase I, alpha	Mus musculus	57-63
1647344-2	1991	Some in vitro studies were performed to elucidate the action of S-adenosyl-L-methionine (SAM) and thiosulphate on liver rhodanese, delta-amino-levulinic acid dehydratase (Al A-D) and cytochrome oxidase affected by cyanide in the experimental conditions.	S-Adenosylmethionine	64-87	aminolevulinate dehydratase	Homo sapiens	131-169
1647344-2	1991	Some in vitro studies were performed to elucidate the action of S-adenosyl-L-methionine (SAM) and thiosulphate on liver rhodanese, delta-amino-levulinic acid dehydratase (Al A-D) and cytochrome oxidase affected by cyanide in the experimental conditions.	S-Adenosylmethionine	64-87	aminolevulinate dehydratase	Homo sapiens	171-177
2260986-4	1990	The above data are consistent with the metabolism of SAM to ATP by a route recently identified by us whereby ATP is formed from deoxyadenosine: namely binding to the enzyme S-adenosylhomocysteine hydrolase with subsequent release of adenine and further conversion to ATP via APRT.	S-Adenosylmethionine	53-56	adenine phosphoribosyltransferase	Homo sapiens	275-279
2313931-0	1990	Protective effect of S-adenosyl-L-methionine against CCl4-induced hepatotoxicity in cultured hepatocytes.	S-Adenosylmethionine	21-44	C-C motif chemokine ligand 4	Rattus norvegicus	53-57
2244927-0	1990	Influence of S-adenosylhomocysteine hydrolase inhibitors on S-adenosylhomocysteine and S-adenosylmethionine pool levels in L929 cells.	S-Adenosylmethionine	89-107	S-adenosylhomocysteine hydrolase	Mus musculus	13-45
1698095-1	1990	Although the physical and kinetic properties of S-adenosylmethionine (AdoMet) synthetases from different sources are quite different, it appears that these enzymes have structurally or antigenically conserved regions as demonstrated by studies with AdoMet synthetase specific antibodies.	S-Adenosylmethionine	48-68	methionine adenosyltransferase 1A	Rattus norvegicus	70-76
1698095-1	1990	Although the physical and kinetic properties of S-adenosylmethionine (AdoMet) synthetases from different sources are quite different, it appears that these enzymes have structurally or antigenically conserved regions as demonstrated by studies with AdoMet synthetase specific antibodies.	S-Adenosylmethionine	48-68	methionine adenosyltransferase 1A	Rattus norvegicus	249-255
2403387-3	1990	THA was found to be a potent competitive inhibitor of rat brain HNMT in vitro, with a Ki of 35 nM with respect to both histamine and S-adenosyl-L-methionine, the co-substrate.	S-Adenosylmethionine	133-156	histamine N-methyltransferase	Rattus norvegicus	64-68
2388614-2	1990	This modification arises by enzymatic transfer of a methyl group from S-adenosylmethionine to the central adenosine residue in the canonical sequence G/AAC.	S-Adenosylmethionine	70-90	glycine N-acyltransferase	Bos taurus	152-155
2311261-5	1990	Apparent Km values of human liver NNMT for nicotinamide and Ado-Met were 347 and 1.76 mumol/l, respectively.	S-Adenosylmethionine	60-67	nicotinamide N-methyltransferase	Homo sapiens	34-38
2131828-8	1990	Furthermore, the tris-OH-M becomes radiolabeled by [methyl-3H3]-S- adenosylmethionine (SAM) in a reaction catalyzed by catechol O-methyltransferase (COMT), indicating that tris-OH-M behaves like a catechol.	S-Adenosylmethionine	87-90	catechol-O-methyltransferase	Rattus norvegicus	119-147
2131828-8	1990	Furthermore, the tris-OH-M becomes radiolabeled by [methyl-3H3]-S- adenosylmethionine (SAM) in a reaction catalyzed by catechol O-methyltransferase (COMT), indicating that tris-OH-M behaves like a catechol.	S-Adenosylmethionine	87-90	catechol-O-methyltransferase	Rattus norvegicus	149-153
2128841-3	1990	However, the corresponding succinimide analogue shows a reversible inhibition of COMT, which is competitive with pyrocatecholphthalein and non-competitive with AdoMet.	S-Adenosylmethionine	160-166	catechol-O-methyltransferase	Homo sapiens	81-85
11543736-0	2001	Long-term treatment with S-adenosylmethionine induces changes in presynaptic CaM kinase II and synapsin I.	S-Adenosylmethionine	25-45	synapsin I	Homo sapiens	95-105
33807010-1	2021	Glycine N-methyltransferase (GNMT) regulates S-adenosylmethionine (SAMe), a methyl donor in methylation.	S-Adenosylmethionine	45-65	glycine N-methyltransferase	Mus musculus	0-27
33807010-1	2021	Glycine N-methyltransferase (GNMT) regulates S-adenosylmethionine (SAMe), a methyl donor in methylation.	S-Adenosylmethionine	45-65	glycine N-methyltransferase	Mus musculus	29-33
29332244-3	2018	Although the catalytic subunit of Elongator is Elp3, which contains a radical S-adenosyl-L-methionine (SAM) domain and a putative histone acetyltransferase domain, the Elp4/5/6 subcomplex also possesses ATP-modulated tRNA binding activity.	S-Adenosylmethionine	78-101	elongator acetyltransferase complex subunit 3	Homo sapiens	47-51
29332244-3	2018	Although the catalytic subunit of Elongator is Elp3, which contains a radical S-adenosyl-L-methionine (SAM) domain and a putative histone acetyltransferase domain, the Elp4/5/6 subcomplex also possesses ATP-modulated tRNA binding activity.	S-Adenosylmethionine	103-106	elongator acetyltransferase complex subunit 3	Homo sapiens	47-51
20382747-7	2010	Oxidant stress contributed to the ethanol-induced changes on the interstitial and alveolar cells, since maternal supplementation with the glutathione precursor S-adenosylmethionine during ethanol ingestion normalized CD32/CD11b (P < or = 0.05), phagocytosis (P < or = 0.05), and TGF-beta(1) in the bronchoalveolar lavage fluid and macrophages (P < or = 0.05).	S-Adenosylmethionine	160-180	Fc receptor, IgG, low affinity IIb	Mus musculus	217-221
20382747-7	2010	Oxidant stress contributed to the ethanol-induced changes on the interstitial and alveolar cells, since maternal supplementation with the glutathione precursor S-adenosylmethionine during ethanol ingestion normalized CD32/CD11b (P < or = 0.05), phagocytosis (P < or = 0.05), and TGF-beta(1) in the bronchoalveolar lavage fluid and macrophages (P < or = 0.05).	S-Adenosylmethionine	160-180	integrin alpha M	Mus musculus	222-227
20382747-7	2010	Oxidant stress contributed to the ethanol-induced changes on the interstitial and alveolar cells, since maternal supplementation with the glutathione precursor S-adenosylmethionine during ethanol ingestion normalized CD32/CD11b (P < or = 0.05), phagocytosis (P < or = 0.05), and TGF-beta(1) in the bronchoalveolar lavage fluid and macrophages (P < or = 0.05).	S-Adenosylmethionine	160-180	transforming growth factor, beta 1	Mus musculus	285-296
15295103-2	2004	The main step in PCho biosynthesis in Arabidopsis thaliana is the triple, sequential N-methylation of phosphoethanolamine, catalyzed by S-adenosyl-l-methionine:phosphoethanolamine N-methyltransferase (PEAMT).	S-Adenosylmethionine	136-159	S-adenosyl-L-methionine-dependent methyltransferases superfamily protein	Arabidopsis thaliana	201-206
33765609-5	2021	The administration of sodium hydrosulfide (NaHS, a H2S donor) or S-adenosylmethionine (SAMe, an allosteric activator of CBS) restored high glucose-induced downregulation of CBS and H2S levels.	S-Adenosylmethionine	65-85	cystathionine beta-synthase	Mus musculus	120-123
33765609-5	2021	The administration of sodium hydrosulfide (NaHS, a H2S donor) or S-adenosylmethionine (SAMe, an allosteric activator of CBS) restored high glucose-induced downregulation of CBS and H2S levels.	S-Adenosylmethionine	65-85	cystathionine beta-synthase	Mus musculus	173-176
33972509-2	2021	To investigate how the oncohistone mutation affects the function of SETD2 at the nucleosome level, we determined the cryo-EM structure of human SETD2 associated with an H3.3K36M nucleosome and cofactor S-adenosylmethionine (SAM), and revealed that SETD2 is attached to the N-terminal region of histone H3 and the nucleosome DNA at superhelix location 1, accompanied with the partial unwrapping of nucleosome DNA to expose the SETD2-binding site.	S-Adenosylmethionine	203-222	SET domain containing 2, histone lysine methyltransferase	Homo sapiens	144-149
33972509-2	2021	To investigate how the oncohistone mutation affects the function of SETD2 at the nucleosome level, we determined the cryo-EM structure of human SETD2 associated with an H3.3K36M nucleosome and cofactor S-adenosylmethionine (SAM), and revealed that SETD2 is attached to the N-terminal region of histone H3 and the nucleosome DNA at superhelix location 1, accompanied with the partial unwrapping of nucleosome DNA to expose the SETD2-binding site.	S-Adenosylmethionine	203-222	SET domain containing 2, histone lysine methyltransferase	Homo sapiens	144-149
33972509-2	2021	To investigate how the oncohistone mutation affects the function of SETD2 at the nucleosome level, we determined the cryo-EM structure of human SETD2 associated with an H3.3K36M nucleosome and cofactor S-adenosylmethionine (SAM), and revealed that SETD2 is attached to the N-terminal region of histone H3 and the nucleosome DNA at superhelix location 1, accompanied with the partial unwrapping of nucleosome DNA to expose the SETD2-binding site.	S-Adenosylmethionine	203-222	SET domain containing 2, histone lysine methyltransferase	Homo sapiens	144-149
33972509-2	2021	To investigate how the oncohistone mutation affects the function of SETD2 at the nucleosome level, we determined the cryo-EM structure of human SETD2 associated with an H3.3K36M nucleosome and cofactor S-adenosylmethionine (SAM), and revealed that SETD2 is attached to the N-terminal region of histone H3 and the nucleosome DNA at superhelix location 1, accompanied with the partial unwrapping of nucleosome DNA to expose the SETD2-binding site.	S-Adenosylmethionine	224-227	SET domain containing 2, histone lysine methyltransferase	Homo sapiens	144-149
33972509-2	2021	To investigate how the oncohistone mutation affects the function of SETD2 at the nucleosome level, we determined the cryo-EM structure of human SETD2 associated with an H3.3K36M nucleosome and cofactor S-adenosylmethionine (SAM), and revealed that SETD2 is attached to the N-terminal region of histone H3 and the nucleosome DNA at superhelix location 1, accompanied with the partial unwrapping of nucleosome DNA to expose the SETD2-binding site.	S-Adenosylmethionine	224-227	SET domain containing 2, histone lysine methyltransferase	Homo sapiens	144-149
33972509-2	2021	To investigate how the oncohistone mutation affects the function of SETD2 at the nucleosome level, we determined the cryo-EM structure of human SETD2 associated with an H3.3K36M nucleosome and cofactor S-adenosylmethionine (SAM), and revealed that SETD2 is attached to the N-terminal region of histone H3 and the nucleosome DNA at superhelix location 1, accompanied with the partial unwrapping of nucleosome DNA to expose the SETD2-binding site.	S-Adenosylmethionine	224-227	SET domain containing 2, histone lysine methyltransferase	Homo sapiens	144-149
33809964-7	2021	By contrast, the phosphatidylethanolamine N-methyl transferase (PEMT) pathway was restricted by low endogenous methionine and consequently low S-adenosylmethionine, which resulted in a concomitant decrease in phosphatidylcholine and accumulation of phosphatidylethanolamine.	S-Adenosylmethionine	143-163	phosphatidylethanolamine N-methyltransferase	Rattus norvegicus	17-62
33809964-7	2021	By contrast, the phosphatidylethanolamine N-methyl transferase (PEMT) pathway was restricted by low endogenous methionine and consequently low S-adenosylmethionine, which resulted in a concomitant decrease in phosphatidylcholine and accumulation of phosphatidylethanolamine.	S-Adenosylmethionine	143-163	phosphatidylethanolamine N-methyltransferase	Rattus norvegicus	64-68
28902392-1	2018	Protein arginine methyltransferase 7 (PRMT7) is a member of a family of enzymes that catalyze the transfer of methyl groups from S-adenosyl-l-methionine to nitrogen atoms on arginine residues.	S-Adenosylmethionine	129-152	protein arginine methyltransferase 7	Homo sapiens	0-36
28902392-1	2018	Protein arginine methyltransferase 7 (PRMT7) is a member of a family of enzymes that catalyze the transfer of methyl groups from S-adenosyl-l-methionine to nitrogen atoms on arginine residues.	S-Adenosylmethionine	129-152	protein arginine methyltransferase 7	Homo sapiens	38-43
11543736-4	2001	METHODS: We investigated the effect of S-adenosylmethionine (SAM), a compound with putative antidepressant activity, on presynaptic CaMKII and its synaptic vesicle substrate synapsin I.	S-Adenosylmethionine	39-59	calcium/calmodulin dependent protein kinase II gamma	Homo sapiens	132-138
11543736-4	2001	METHODS: We investigated the effect of S-adenosylmethionine (SAM), a compound with putative antidepressant activity, on presynaptic CaMKII and its synaptic vesicle substrate synapsin I.	S-Adenosylmethionine	39-59	synapsin I	Homo sapiens	174-184
11543736-4	2001	METHODS: We investigated the effect of S-adenosylmethionine (SAM), a compound with putative antidepressant activity, on presynaptic CaMKII and its synaptic vesicle substrate synapsin I.	S-Adenosylmethionine	61-64	calcium/calmodulin dependent protein kinase II gamma	Homo sapiens	132-138
11543736-4	2001	METHODS: We investigated the effect of S-adenosylmethionine (SAM), a compound with putative antidepressant activity, on presynaptic CaMKII and its synaptic vesicle substrate synapsin I.	S-Adenosylmethionine	61-64	synapsin I	Homo sapiens	174-184
34974065-9	2021	Mitochondrial STAT3 further facilitates adenosine triphosphate synthesis to fuel the methionine cycle and generation of S-adenosylmethionine, which supports the epigenetic reprogramming of type 2 cytokines in ILC2s.	S-Adenosylmethionine	120-140	signal transducer and activator of transcription 3	Mus musculus	14-19
1460049-13	1992	With dA3, dA1, RT, and potassium ions, CTP reduction shows absolute requirements for S-adenosylmethionine, NADPH (with NADH as a less active substitute), dithiothreitol, and magnesium ions, and is strongly stimulated by ATP, probably acting as an allosteric effector.	S-Adenosylmethionine	85-105	A3	Drosophila melanogaster	5-8
34922197-4	2022	We solved the structure of human METTL6 in the presence of S-adenosyl-L-methionine and found by enzyme assay that recombinant human METTL6 is active towards tRNASER(UGA).	S-Adenosylmethionine	59-82	methyltransferase 6, methylcytidine	Homo sapiens	33-39
34922197-4	2022	We solved the structure of human METTL6 in the presence of S-adenosyl-L-methionine and found by enzyme assay that recombinant human METTL6 is active towards tRNASER(UGA).	S-Adenosylmethionine	59-82	methyltransferase 6, methylcytidine	Homo sapiens	132-138
34922197-4	2022	We solved the structure of human METTL6 in the presence of S-adenosyl-L-methionine and found by enzyme assay that recombinant human METTL6 is active towards tRNASER(UGA).	S-Adenosylmethionine	59-82	tRNA-Ser (anticodon AGA) 2-3	Homo sapiens	157-164
34922197-5	2022	Structural analysis indicated the detailed interactions between S-adenosyl-L-methionine and METTL6, and suggested potential tRNA binding region on the surface of METTL6.	S-Adenosylmethionine	64-87	methyltransferase 6, methylcytidine	Homo sapiens	92-98
34922197-5	2022	Structural analysis indicated the detailed interactions between S-adenosyl-L-methionine and METTL6, and suggested potential tRNA binding region on the surface of METTL6.	S-Adenosylmethionine	64-87	methyltransferase 6, methylcytidine	Homo sapiens	162-168
34449924-0	2022	S-Adenosylmethionine Inhibits La Ribonucleoprotein Domain Family Member 1 in Murine Liver and Human Liver Cancer Cells.	S-Adenosylmethionine	0-20	La ribonucleoprotein domain family, member 1	Mus musculus	30-73
34449924-1	2022	BACKGROUND & AIMS: Methionine adenosyltransferase 1A (MAT1A) is responsible for S-adenosylmethionine (SAMe) biosynthesis in the liver.	S-Adenosylmethionine	80-100	methionine adenosyltransferase I, alpha	Mus musculus	19-52
34449924-1	2022	BACKGROUND & AIMS: Methionine adenosyltransferase 1A (MAT1A) is responsible for S-adenosylmethionine (SAMe) biosynthesis in the liver.	S-Adenosylmethionine	80-100	methionine adenosyltransferase I, alpha	Mus musculus	54-59
34517051-4	2022	Levels of methionine, S-adenosylmethionine (SAM), S-adenosylhomocysteine (SAH) and cystathionine were positively correlated with NFE2L2 expression, while homocysteine (HCY) was negatively correlated.	S-Adenosylmethionine	22-42	NFE2 like bZIP transcription factor 2	Homo sapiens	129-135
34517051-4	2022	Levels of methionine, S-adenosylmethionine (SAM), S-adenosylhomocysteine (SAH) and cystathionine were positively correlated with NFE2L2 expression, while homocysteine (HCY) was negatively correlated.	S-Adenosylmethionine	44-47	NFE2 like bZIP transcription factor 2	Homo sapiens	129-135
34737197-3	2022	Here we describe the discovery of potent and selective S-adenosylmethionine (SAM) competitive PRMT5 inhibitors, with in vitro and in vivo characterization of clinical candidate PF-06939999.	S-Adenosylmethionine	55-75	protein arginine N-methyltransferase 5	Mus musculus	94-99
34737197-3	2022	Here we describe the discovery of potent and selective S-adenosylmethionine (SAM) competitive PRMT5 inhibitors, with in vitro and in vivo characterization of clinical candidate PF-06939999.	S-Adenosylmethionine	77-80	protein arginine N-methyltransferase 5	Mus musculus	94-99
34863249-0	2021	Ethionine-mediated reduction of S-adenosylmethionine is responsible for the neural tube defects in the developing mouse embryo-mediated m6A modification and is involved in neural tube defects via modulating Wnt/beta-catenin signaling pathway.	S-Adenosylmethionine	32-52	catenin (cadherin associated protein), beta 1	Mus musculus	211-223
34375635-1	2021	BACKGROUND: Combined oxidative phosphorylation deficiency 28 (COXPD28) is associated with mitochondrial dysfunction caused by mutations in SLC25A26, the gene which encodes the mitochondrial S-adenosylmethionine carrier (SAMC) that responsible for the transport of S-adenosylmethionine (SAM) into the mitochondria.	S-Adenosylmethionine	190-210	solute carrier family 25 member 26	Homo sapiens	139-147
34375635-1	2021	BACKGROUND: Combined oxidative phosphorylation deficiency 28 (COXPD28) is associated with mitochondrial dysfunction caused by mutations in SLC25A26, the gene which encodes the mitochondrial S-adenosylmethionine carrier (SAMC) that responsible for the transport of S-adenosylmethionine (SAM) into the mitochondria.	S-Adenosylmethionine	190-210	solute carrier family 25 member 26	Homo sapiens	220-224
34375635-1	2021	BACKGROUND: Combined oxidative phosphorylation deficiency 28 (COXPD28) is associated with mitochondrial dysfunction caused by mutations in SLC25A26, the gene which encodes the mitochondrial S-adenosylmethionine carrier (SAMC) that responsible for the transport of S-adenosylmethionine (SAM) into the mitochondria.	S-Adenosylmethionine	264-284	solute carrier family 25 member 26	Homo sapiens	139-147
34375635-1	2021	BACKGROUND: Combined oxidative phosphorylation deficiency 28 (COXPD28) is associated with mitochondrial dysfunction caused by mutations in SLC25A26, the gene which encodes the mitochondrial S-adenosylmethionine carrier (SAMC) that responsible for the transport of S-adenosylmethionine (SAM) into the mitochondria.	S-Adenosylmethionine	264-284	solute carrier family 25 member 26	Homo sapiens	220-224
34375635-1	2021	BACKGROUND: Combined oxidative phosphorylation deficiency 28 (COXPD28) is associated with mitochondrial dysfunction caused by mutations in SLC25A26, the gene which encodes the mitochondrial S-adenosylmethionine carrier (SAMC) that responsible for the transport of S-adenosylmethionine (SAM) into the mitochondria.	S-Adenosylmethionine	286-289	solute carrier family 25 member 26	Homo sapiens	139-147
34375635-1	2021	BACKGROUND: Combined oxidative phosphorylation deficiency 28 (COXPD28) is associated with mitochondrial dysfunction caused by mutations in SLC25A26, the gene which encodes the mitochondrial S-adenosylmethionine carrier (SAMC) that responsible for the transport of S-adenosylmethionine (SAM) into the mitochondria.	S-Adenosylmethionine	286-289	solute carrier family 25 member 26	Homo sapiens	220-224
34780697-3	2021	The initial velocity pattern and results of product inhibition by SAM, phosphate, and pyrophosphate, and dead-end inhibition by the l-Met analog cycloleucine (l-cLeu) suggest that Mat2A follows a strictly ordered kinetic mechanism where ATP binds before l-Met and with SAM released prior to random release of phosphate and pyrophosphate.	S-Adenosylmethionine	66-69	methionine adenosyltransferase 2A	Homo sapiens	180-185
34794285-0	2021	Effects of S-adenosyl-L-Methionine Combined with Ursodesoxycholic Acid on Serum Endotoxin, MMP-9 and IL-18 in Neonates with Cholestasis.	S-Adenosylmethionine	11-34	matrix metallopeptidase 9	Homo sapiens	91-96
34794285-0	2021	Effects of S-adenosyl-L-Methionine Combined with Ursodesoxycholic Acid on Serum Endotoxin, MMP-9 and IL-18 in Neonates with Cholestasis.	S-Adenosylmethionine	11-34	interleukin 18	Homo sapiens	101-106
34655178-8	2021	We speculate that depletion of NNMT promotes histone methylation and leads to tumor suppression because NNMT consumes S-adenosyl methionine (SAM), which is an essential methylation cofactor.	S-Adenosylmethionine	118-139	nicotinamide N-methyltransferase	Homo sapiens	104-108
34655178-8	2021	We speculate that depletion of NNMT promotes histone methylation and leads to tumor suppression because NNMT consumes S-adenosyl methionine (SAM), which is an essential methylation cofactor.	S-Adenosylmethionine	141-144	nicotinamide N-methyltransferase	Homo sapiens	31-35
34655178-8	2021	We speculate that depletion of NNMT promotes histone methylation and leads to tumor suppression because NNMT consumes S-adenosyl methionine (SAM), which is an essential methylation cofactor.	S-Adenosylmethionine	141-144	nicotinamide N-methyltransferase	Homo sapiens	104-108
34357424-0	2021	Retraction Note to: S-Adenosylmethionine synergistically enhances the antitumor effect of gemcitabine against pancreatic cancer through JAK2/STAT3 pathway.	S-Adenosylmethionine	20-40	Janus kinase 2	Homo sapiens	136-140
34647332-8	2022	LINC00662 can reduce the promoter methylation level of s-adenosylmethionine (SAM)-dependent hepatocellular carcinoma (HCC)-promoting genes by regulating the MAT1A/SAM and AHCY/SAH axes, thereby promoting the activation of oncogenes.	S-Adenosylmethionine	55-75	long intergenic non-protein coding RNA 662	Homo sapiens	0-9
34647332-8	2022	LINC00662 can reduce the promoter methylation level of s-adenosylmethionine (SAM)-dependent hepatocellular carcinoma (HCC)-promoting genes by regulating the MAT1A/SAM and AHCY/SAH axes, thereby promoting the activation of oncogenes.	S-Adenosylmethionine	55-75	methionine adenosyltransferase 1A	Homo sapiens	157-166
34647332-8	2022	LINC00662 can reduce the promoter methylation level of s-adenosylmethionine (SAM)-dependent hepatocellular carcinoma (HCC)-promoting genes by regulating the MAT1A/SAM and AHCY/SAH axes, thereby promoting the activation of oncogenes.	S-Adenosylmethionine	55-75	adenosylhomocysteinase	Homo sapiens	171-175
34647332-8	2022	LINC00662 can reduce the promoter methylation level of s-adenosylmethionine (SAM)-dependent hepatocellular carcinoma (HCC)-promoting genes by regulating the MAT1A/SAM and AHCY/SAH axes, thereby promoting the activation of oncogenes.	S-Adenosylmethionine	77-80	long intergenic non-protein coding RNA 662	Homo sapiens	0-9
34647332-8	2022	LINC00662 can reduce the promoter methylation level of s-adenosylmethionine (SAM)-dependent hepatocellular carcinoma (HCC)-promoting genes by regulating the MAT1A/SAM and AHCY/SAH axes, thereby promoting the activation of oncogenes.	S-Adenosylmethionine	77-80	methionine adenosyltransferase 1A	Homo sapiens	157-166
34647332-8	2022	LINC00662 can reduce the promoter methylation level of s-adenosylmethionine (SAM)-dependent hepatocellular carcinoma (HCC)-promoting genes by regulating the MAT1A/SAM and AHCY/SAH axes, thereby promoting the activation of oncogenes.	S-Adenosylmethionine	77-80	adenosylhomocysteinase	Homo sapiens	171-175
34684735-3	2021	At first, a structural similarity study against the co-crystallized ligand, S-Adenosyl Methionine (SAM), of SARS-CoV-2 nonstructural protein (nsp10) (PDB ID: 6W4H) was carried out.	S-Adenosylmethionine	76-97	ORF1a polyprotein;ORF1ab polyprotein	Severe acute respiratory syndrome coronavirus 2	142-147
34684735-3	2021	At first, a structural similarity study against the co-crystallized ligand, S-Adenosyl Methionine (SAM), of SARS-CoV-2 nonstructural protein (nsp10) (PDB ID: 6W4H) was carried out.	S-Adenosylmethionine	99-102	ORF1a polyprotein;ORF1ab polyprotein	Severe acute respiratory syndrome coronavirus 2	142-147
34505434-13	2021	Thus, upregulated S-adenosylmethionine, S-adenosylhomocysteine, and N6,N6,N6-trimethyl-L-lysine indicated that LAMTOR1 may regulate the process of DNA or protein methylation.	S-Adenosylmethionine	18-38	late endosomal/lysosomal adaptor, MAPK and MTOR activator 1	Mus musculus	111-118
34505434-20	2021	MAT1A encodes methionine adenosyltransferase 1A, an essential enzyme that catalyzes the formation of S-adenosylmethionine.	S-Adenosylmethionine	101-121	methionine adenosyltransferase I, alpha	Mus musculus	0-5
34679357-3	2021	The catechol O-methyltransferase (COMT) gene is located within the 22q11.2 region, and its product is an enzyme involved in transferring a methyl group from S-adenosylmethionine to catecholamines, including dopamine.	S-Adenosylmethionine	157-177	catechol-O-methyltransferase	Homo sapiens	4-32
34679357-3	2021	The catechol O-methyltransferase (COMT) gene is located within the 22q11.2 region, and its product is an enzyme involved in transferring a methyl group from S-adenosylmethionine to catecholamines, including dopamine.	S-Adenosylmethionine	157-177	catechol-O-methyltransferase	Homo sapiens	34-38
34616406-0	2021	MAT2A-Mediated S-Adenosylmethionine Level in CD4+ T Cells Regulates HIV-1 Latent Infection.	S-Adenosylmethionine	15-35	methionine adenosyltransferase 2A	Homo sapiens	0-5
34616406-0	2021	MAT2A-Mediated S-Adenosylmethionine Level in CD4+ T Cells Regulates HIV-1 Latent Infection.	S-Adenosylmethionine	15-35	CD4 molecule	Homo sapiens	45-48
34616406-6	2021	Mechanistically, MAT2A modulates HIV-1 latency through S-Adenosylmethionine (SAM)-mediated one-carbon flux.	S-Adenosylmethionine	55-75	methionine adenosyltransferase 2A	Homo sapiens	17-22
34616406-6	2021	Mechanistically, MAT2A modulates HIV-1 latency through S-Adenosylmethionine (SAM)-mediated one-carbon flux.	S-Adenosylmethionine	77-80	methionine adenosyltransferase 2A	Homo sapiens	17-22
34424711-3	2021	The development of small-molecule NNMT inhibitors has gained interest in recent years, with the most potent inhibitors sharing structural features based on elements of the nicotinamide substrate and the S-adenosyl-l-methionine (SAM) cofactor.	S-Adenosylmethionine	203-226	nicotinamide N-methyltransferase	Homo sapiens	34-38
34424711-3	2021	The development of small-molecule NNMT inhibitors has gained interest in recent years, with the most potent inhibitors sharing structural features based on elements of the nicotinamide substrate and the S-adenosyl-l-methionine (SAM) cofactor.	S-Adenosylmethionine	228-231	nicotinamide N-methyltransferase	Homo sapiens	34-38
34668717-1	2021	Human methionine adenosyltransferase MAT2A provides S-adenosyl-l-methionine (AdoMet) for methyl-transfer reactions.	S-Adenosylmethionine	52-75	methionine adenosyltransferase 2A	Homo sapiens	37-42
34668717-1	2021	Human methionine adenosyltransferase MAT2A provides S-adenosyl-l-methionine (AdoMet) for methyl-transfer reactions.	S-Adenosylmethionine	77-83	methionine adenosyltransferase 2A	Homo sapiens	37-42
34668717-5	2021	Crystal structures of MAT2A with analogues of AdoMet and pyrophosphate were obtained in the presence of Mg2+, Al3+, and F-.	S-Adenosylmethionine	46-52	methionine adenosyltransferase 2A	Homo sapiens	22-27
34720086-0	2021	Cul4A-DDB1-mediated monoubiquitination of phosphoglycerate dehydrogenase promotes colorectal cancer metastasis via increased S-adenosylmethionine.	S-Adenosylmethionine	125-145	cullin 4A	Homo sapiens	0-5
34720086-0	2021	Cul4A-DDB1-mediated monoubiquitination of phosphoglycerate dehydrogenase promotes colorectal cancer metastasis via increased S-adenosylmethionine.	S-Adenosylmethionine	125-145	damage specific DNA binding protein 1	Homo sapiens	6-10
34720086-0	2021	Cul4A-DDB1-mediated monoubiquitination of phosphoglycerate dehydrogenase promotes colorectal cancer metastasis via increased S-adenosylmethionine.	S-Adenosylmethionine	125-145	phosphoglycerate dehydrogenase	Homo sapiens	42-72
34720086-3	2021	Here we show that PHGDH was monoubiquitinated by cullin 4A-based E3 ligase complex at lysine 146 in colorectal cancer (CRC) cells, which enhanced PHGDH activity by recruiting a chaperone protein, DnaJ homolog subfamily A member 1, to promote its tetrameric formation, thereby increasing the levels of serine, glycine, and S-adenosylmethionine (SAM).	S-Adenosylmethionine	322-342	phosphoglycerate dehydrogenase	Homo sapiens	18-23
34720086-3	2021	Here we show that PHGDH was monoubiquitinated by cullin 4A-based E3 ligase complex at lysine 146 in colorectal cancer (CRC) cells, which enhanced PHGDH activity by recruiting a chaperone protein, DnaJ homolog subfamily A member 1, to promote its tetrameric formation, thereby increasing the levels of serine, glycine, and S-adenosylmethionine (SAM).	S-Adenosylmethionine	322-342	cullin 4A	Homo sapiens	49-58
34720086-3	2021	Here we show that PHGDH was monoubiquitinated by cullin 4A-based E3 ligase complex at lysine 146 in colorectal cancer (CRC) cells, which enhanced PHGDH activity by recruiting a chaperone protein, DnaJ homolog subfamily A member 1, to promote its tetrameric formation, thereby increasing the levels of serine, glycine, and S-adenosylmethionine (SAM).	S-Adenosylmethionine	322-342	DnaJ heat shock protein family (Hsp40) member A1	Homo sapiens	196-229
34720086-3	2021	Here we show that PHGDH was monoubiquitinated by cullin 4A-based E3 ligase complex at lysine 146 in colorectal cancer (CRC) cells, which enhanced PHGDH activity by recruiting a chaperone protein, DnaJ homolog subfamily A member 1, to promote its tetrameric formation, thereby increasing the levels of serine, glycine, and S-adenosylmethionine (SAM).	S-Adenosylmethionine	344-347	phosphoglycerate dehydrogenase	Homo sapiens	18-23
34720086-3	2021	Here we show that PHGDH was monoubiquitinated by cullin 4A-based E3 ligase complex at lysine 146 in colorectal cancer (CRC) cells, which enhanced PHGDH activity by recruiting a chaperone protein, DnaJ homolog subfamily A member 1, to promote its tetrameric formation, thereby increasing the levels of serine, glycine, and S-adenosylmethionine (SAM).	S-Adenosylmethionine	344-347	cullin 4A	Homo sapiens	49-58
34720086-3	2021	Here we show that PHGDH was monoubiquitinated by cullin 4A-based E3 ligase complex at lysine 146 in colorectal cancer (CRC) cells, which enhanced PHGDH activity by recruiting a chaperone protein, DnaJ homolog subfamily A member 1, to promote its tetrameric formation, thereby increasing the levels of serine, glycine, and S-adenosylmethionine (SAM).	S-Adenosylmethionine	344-347	phosphoglycerate dehydrogenase	Homo sapiens	146-151
34720086-3	2021	Here we show that PHGDH was monoubiquitinated by cullin 4A-based E3 ligase complex at lysine 146 in colorectal cancer (CRC) cells, which enhanced PHGDH activity by recruiting a chaperone protein, DnaJ homolog subfamily A member 1, to promote its tetrameric formation, thereby increasing the levels of serine, glycine, and S-adenosylmethionine (SAM).	S-Adenosylmethionine	344-347	DnaJ heat shock protein family (Hsp40) member A1	Homo sapiens	196-229
34685411-3	2021	SETD3 consists of a catalytic SET domain responsible for transferring the methyl group from S-adenosyl-L-methionine (AdoMet) to a protein substrate and a RuBisCO LSMT domain that recognizes and binds the methyl-accepting protein(s).	S-Adenosylmethionine	92-115	SET domain containing 3, actin histidine methyltransferase	Homo sapiens	0-5
34679865-9	2021	Overall, the results indicate that salivary CgA is a potential candidate for SAM-mediated stress markers in dogs.	S-Adenosylmethionine	77-80	chromogranin-A	Canis lupus familiaris	44-47
34592146-0	2021	Vitamin B12 impacts amyloid beta-induced proteotoxicity by regulating the methionine/S-adenosylmethionine cycle.	S-Adenosylmethionine	85-105	amyloid beta precursor protein	Homo sapiens	20-32
34592146-7	2021	Vitamin B12 has this protective effect by acting as a cofactor for methionine synthase, impacting the methionine/S-adenosylmethionine (SAMe) cycle.	S-Adenosylmethionine	115-133	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	67-86
34357424-0	2021	Retraction Note to: S-Adenosylmethionine synergistically enhances the antitumor effect of gemcitabine against pancreatic cancer through JAK2/STAT3 pathway.	S-Adenosylmethionine	20-40	signal transducer and activator of transcription 3	Homo sapiens	141-146
34502219-0	2021	S-Adenosylmethionine Increases the Sensitivity of Human Colorectal Cancer Cells to 5-Fluorouracil by Inhibiting P-Glycoprotein Expression and NF-kappaB Activation.	S-Adenosylmethionine	0-20	ATP binding cassette subfamily B member 1	Homo sapiens	112-126
34502219-0	2021	S-Adenosylmethionine Increases the Sensitivity of Human Colorectal Cancer Cells to 5-Fluorouracil by Inhibiting P-Glycoprotein Expression and NF-kappaB Activation.	S-Adenosylmethionine	0-20	nuclear factor kappa B subunit 1	Homo sapiens	142-151
34439880-1	2021	Nicotinamide N-methyltransferase (NNMT) catalyzes the N-methylation reaction of nicotinamide, using S-adenosyl-L-methionine as the methyl donor.	S-Adenosylmethionine	100-123	nicotinamide N-methyltransferase	Homo sapiens	0-32
34704059-1	2021	Nicotinamide N-methyltransferase (NNMT) methylates nicotinamide to form 1-methylnicotinamide (MNA) using S-adenosyl-l-methionine (SAM) as the methyl donor.	S-Adenosylmethionine	105-128	nicotinamide N-methyltransferase	Homo sapiens	0-32
34704059-1	2021	Nicotinamide N-methyltransferase (NNMT) methylates nicotinamide to form 1-methylnicotinamide (MNA) using S-adenosyl-l-methionine (SAM) as the methyl donor.	S-Adenosylmethionine	105-128	nicotinamide N-methyltransferase	Homo sapiens	34-38
34704059-1	2021	Nicotinamide N-methyltransferase (NNMT) methylates nicotinamide to form 1-methylnicotinamide (MNA) using S-adenosyl-l-methionine (SAM) as the methyl donor.	S-Adenosylmethionine	130-133	nicotinamide N-methyltransferase	Homo sapiens	0-32
34704059-1	2021	Nicotinamide N-methyltransferase (NNMT) methylates nicotinamide to form 1-methylnicotinamide (MNA) using S-adenosyl-l-methionine (SAM) as the methyl donor.	S-Adenosylmethionine	130-133	nicotinamide N-methyltransferase	Homo sapiens	34-38
34704059-7	2021	Interestingly, substrate competition experiments reveal that these cyclic peptide inhibitors are noncompetitive with either SAM or NA indicating they may be the first allosteric inhibitors reported for NNMT.	S-Adenosylmethionine	124-127	nicotinamide N-methyltransferase	Homo sapiens	202-206
34439880-1	2021	Nicotinamide N-methyltransferase (NNMT) catalyzes the N-methylation reaction of nicotinamide, using S-adenosyl-L-methionine as the methyl donor.	S-Adenosylmethionine	100-123	nicotinamide N-methyltransferase	Homo sapiens	34-38
34184886-1	2021	TYW1 is a radical S-adenosyl-l-methionine (SAM) enzyme that catalyzes the condensation of pyruvate and N-methylguanosine-containing tRNAPhe, forming 4-demethylwyosine-containing tRNAPhe.	S-Adenosylmethionine	18-41	putative tRNA 4-demethylwyosine synthase	Saccharomyces cerevisiae S288C	0-4
34336098-0	2021	Methionine Protects Mammary Cells against Oxidative Stress through Producing S-Adenosylmethionine to Maintain mTORC1 Signaling Activity.	S-Adenosylmethionine	77-97	CREB regulated transcription coactivator 1	Mus musculus	110-116
34184886-1	2021	TYW1 is a radical S-adenosyl-l-methionine (SAM) enzyme that catalyzes the condensation of pyruvate and N-methylguanosine-containing tRNAPhe, forming 4-demethylwyosine-containing tRNAPhe.	S-Adenosylmethionine	43-46	putative tRNA 4-demethylwyosine synthase	Saccharomyces cerevisiae S288C	0-4
34253866-9	2021	To translate our results into a potential pharmacological therapeutic strategy, we tested the effect of systemic treatment with the global methyl donor S-adenosyl methionine (SAM), for supplementing DNA methylation, or retinoic acid, for activating RORA downstream pathways.	S-Adenosylmethionine	152-173	RAR related orphan receptor A	Homo sapiens	249-253
34253866-9	2021	To translate our results into a potential pharmacological therapeutic strategy, we tested the effect of systemic treatment with the global methyl donor S-adenosyl methionine (SAM), for supplementing DNA methylation, or retinoic acid, for activating RORA downstream pathways.	S-Adenosylmethionine	175-178	RAR related orphan receptor A	Homo sapiens	249-253
34156827-1	2021	Viperin is a member of the radical S-adenosylmethionine superfamily and has been shown to restrict the replication of a wide range of RNA and DNA viruses.	S-Adenosylmethionine	35-55	radical S-adenosyl methionine domain containing 2	Homo sapiens	0-7
34377057-1	2021	Nicotinamide N-methyltransferase (NNMT), a key cytoplasmic protein in the human body, is accountable to catalyze the nicotinamide (NCA) N1-methylation through S-adenosyl-L-methionine (SAM) as a methyl donor, which has been linked to many diseases.	S-Adenosylmethionine	159-182	nicotinamide N-methyltransferase	Homo sapiens	0-32
34227247-4	2022	METTL16"s methyltransferase domain contains the Rossmann-like fold of class I methyltransferases and uses S-adenosylmethionine (SAM) as the methyl donor.	S-Adenosylmethionine	106-126	methyltransferase 16, N6-methyladenosine	Homo sapiens	0-7
34227247-4	2022	METTL16"s methyltransferase domain contains the Rossmann-like fold of class I methyltransferases and uses S-adenosylmethionine (SAM) as the methyl donor.	S-Adenosylmethionine	128-131	methyltransferase 16, N6-methyladenosine	Homo sapiens	0-7
34154323-1	2021	All radical S-adenosylmethionine (radical-SAM) enzymes, including the noncanonical radical-SAM enzyme diphthamide biosynthetic enzyme Dph1-Dph2, require at least one (4Fe-4S)(Cys)3 cluster for activity.	S-Adenosylmethionine	12-32	2-(3-amino-3-carboxypropyl)histidine synthase	Saccharomyces cerevisiae S288C	134-138
34154323-1	2021	All radical S-adenosylmethionine (radical-SAM) enzymes, including the noncanonical radical-SAM enzyme diphthamide biosynthetic enzyme Dph1-Dph2, require at least one (4Fe-4S)(Cys)3 cluster for activity.	S-Adenosylmethionine	12-32	2-(3-amino-3-carboxypropyl)histidine synthase	Saccharomyces cerevisiae S288C	139-143
34131072-2	2021	The SARS-CoV-2 genome encodes the 2"-O-methyltransferase nsp16, which, when bound to the coactivator nsp10, uses S-adenosylmethionine (SAM) as a donor to transfer a methyl group to the first ribonucleotide of the mRNA in the final step of viral mRNA capping.	S-Adenosylmethionine	113-133	ORF1a polyprotein;ORF1ab polyprotein	Severe acute respiratory syndrome coronavirus 2	101-106
34131072-2	2021	The SARS-CoV-2 genome encodes the 2"-O-methyltransferase nsp16, which, when bound to the coactivator nsp10, uses S-adenosylmethionine (SAM) as a donor to transfer a methyl group to the first ribonucleotide of the mRNA in the final step of viral mRNA capping.	S-Adenosylmethionine	135-138	ORF1a polyprotein;ORF1ab polyprotein	Severe acute respiratory syndrome coronavirus 2	101-106
34163008-5	2021	B12 activated hepatic IGF-1 production via normalization of S-adenosylmethionine levels, DNA methyltransferase (DNMT)-1/3a/3b mRNA, and DNA methylation of promoters for suppressor of cytokine signaling (SOCS)-1/3.	S-Adenosylmethionine	60-80	insulin-like growth factor 1	Mus musculus	22-27
34377057-1	2021	Nicotinamide N-methyltransferase (NNMT), a key cytoplasmic protein in the human body, is accountable to catalyze the nicotinamide (NCA) N1-methylation through S-adenosyl-L-methionine (SAM) as a methyl donor, which has been linked to many diseases.	S-Adenosylmethionine	159-182	nicotinamide N-methyltransferase	Homo sapiens	34-38
34377057-1	2021	Nicotinamide N-methyltransferase (NNMT), a key cytoplasmic protein in the human body, is accountable to catalyze the nicotinamide (NCA) N1-methylation through S-adenosyl-L-methionine (SAM) as a methyl donor, which has been linked to many diseases.	S-Adenosylmethionine	184-187	nicotinamide N-methyltransferase	Homo sapiens	0-32
34377057-1	2021	Nicotinamide N-methyltransferase (NNMT), a key cytoplasmic protein in the human body, is accountable to catalyze the nicotinamide (NCA) N1-methylation through S-adenosyl-L-methionine (SAM) as a methyl donor, which has been linked to many diseases.	S-Adenosylmethionine	184-187	nicotinamide N-methyltransferase	Homo sapiens	34-38
34065390-2	2021	Hepatic and extrahepatic tissues methionine adenosyltransferases (MATs) are products of two genes, MAT1A and MAT2A that catalyze the formation of S-adenosylmethionine (SAM), the principal biological methyl donor.	S-Adenosylmethionine	146-166	methionine adenosyltransferase 1A	Homo sapiens	99-104
34065390-2	2021	Hepatic and extrahepatic tissues methionine adenosyltransferases (MATs) are products of two genes, MAT1A and MAT2A that catalyze the formation of S-adenosylmethionine (SAM), the principal biological methyl donor.	S-Adenosylmethionine	146-166	methionine adenosyltransferase 2A	Homo sapiens	109-114
34065390-2	2021	Hepatic and extrahepatic tissues methionine adenosyltransferases (MATs) are products of two genes, MAT1A and MAT2A that catalyze the formation of S-adenosylmethionine (SAM), the principal biological methyl donor.	S-Adenosylmethionine	168-171	methionine adenosyltransferase 1A	Homo sapiens	99-104
34065390-2	2021	Hepatic and extrahepatic tissues methionine adenosyltransferases (MATs) are products of two genes, MAT1A and MAT2A that catalyze the formation of S-adenosylmethionine (SAM), the principal biological methyl donor.	S-Adenosylmethionine	168-171	methionine adenosyltransferase 2A	Homo sapiens	109-114
34065390-3	2021	Glycine N-methyltransferase (GNMT) further utilizes SAM for sarcosine formation, thus it regulates the ratio of SAM:S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	112-115	glycine N-methyltransferase	Homo sapiens	0-27
34065390-3	2021	Glycine N-methyltransferase (GNMT) further utilizes SAM for sarcosine formation, thus it regulates the ratio of SAM:S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	112-115	glycine N-methyltransferase	Homo sapiens	29-33
34517946-1	2021	The RNA methyltransferase (MTase) complex METTL3-METTL14 transfers methyl groups from S-adenosyl-l-methionine (AdoMet) to the N6-position of adenosines within its consensus sequence, the DRACH motif (D=A, G, U; R=A, G; H=A, C, U).	S-Adenosylmethionine	86-109	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	42-48
34517946-1	2021	The RNA methyltransferase (MTase) complex METTL3-METTL14 transfers methyl groups from S-adenosyl-l-methionine (AdoMet) to the N6-position of adenosines within its consensus sequence, the DRACH motif (D=A, G, U; R=A, G; H=A, C, U).	S-Adenosylmethionine	86-109	methyltransferase 14, N6-adenosine-methyltransferase subunit	Homo sapiens	49-56
34517946-1	2021	The RNA methyltransferase (MTase) complex METTL3-METTL14 transfers methyl groups from S-adenosyl-l-methionine (AdoMet) to the N6-position of adenosines within its consensus sequence, the DRACH motif (D=A, G, U; R=A, G; H=A, C, U).	S-Adenosylmethionine	111-117	methyltransferase 14, N6-adenosine-methyltransferase subunit	Homo sapiens	49-56
34517946-1	2021	The RNA methyltransferase (MTase) complex METTL3-METTL14 transfers methyl groups from S-adenosyl-l-methionine (AdoMet) to the N6-position of adenosines within its consensus sequence, the DRACH motif (D=A, G, U; R=A, G; H=A, C, U).	S-Adenosylmethionine	111-117	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	42-48
35490796-3	2022	This study further investigated the ability of the methyl group donors, S-adenosyl methionine (SAM) and folic acid, to prevent promoter hypomethylation that results in decreased mRNA expression of inflammatory genes (COX2, EGR1, and SOCS3), and a reduction in arsenic-induced oxidative and nitrative DNA damage in human lymphoblast cells.	S-Adenosylmethionine	72-93	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	217-221
35490796-3	2022	This study further investigated the ability of the methyl group donors, S-adenosyl methionine (SAM) and folic acid, to prevent promoter hypomethylation that results in decreased mRNA expression of inflammatory genes (COX2, EGR1, and SOCS3), and a reduction in arsenic-induced oxidative and nitrative DNA damage in human lymphoblast cells.	S-Adenosylmethionine	72-93	early growth response 1	Homo sapiens	223-227
35490796-3	2022	This study further investigated the ability of the methyl group donors, S-adenosyl methionine (SAM) and folic acid, to prevent promoter hypomethylation that results in decreased mRNA expression of inflammatory genes (COX2, EGR1, and SOCS3), and a reduction in arsenic-induced oxidative and nitrative DNA damage in human lymphoblast cells.	S-Adenosylmethionine	72-93	suppressor of cytokine signaling 3	Homo sapiens	233-238
35490796-3	2022	This study further investigated the ability of the methyl group donors, S-adenosyl methionine (SAM) and folic acid, to prevent promoter hypomethylation that results in decreased mRNA expression of inflammatory genes (COX2, EGR1, and SOCS3), and a reduction in arsenic-induced oxidative and nitrative DNA damage in human lymphoblast cells.	S-Adenosylmethionine	95-98	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	217-221
35490796-3	2022	This study further investigated the ability of the methyl group donors, S-adenosyl methionine (SAM) and folic acid, to prevent promoter hypomethylation that results in decreased mRNA expression of inflammatory genes (COX2, EGR1, and SOCS3), and a reduction in arsenic-induced oxidative and nitrative DNA damage in human lymphoblast cells.	S-Adenosylmethionine	95-98	early growth response 1	Homo sapiens	223-227
35579944-2	2022	CARM1 catalyzes methyl group transfer from the cofactor S-adenosyl-l-methionine (AdoMet) to both histone and nonhistone protein substrates.	S-Adenosylmethionine	56-79	coactivator associated arginine methyltransferase 1	Homo sapiens	0-5
35636512-0	2022	mTORC1-independent translation control in mammalian cells by methionine adenosyltransferase 2A and S-adenosylmethionine.	S-Adenosylmethionine	99-119	CREB regulated transcription coactivator 1	Mus musculus	0-6
35316659-2	2022	Viperin, a member of the radical S-adenosyl methionine (SAM) superfamily of enzymes, is the product of one such ISG that restricts the replication of a broad spectrum of viruses.	S-Adenosylmethionine	33-54	radical S-adenosyl methionine domain containing 2	Homo sapiens	0-7
35626640-7	2022	Supplementation with S-adenosylmethionine (SAM), a methyl group donor that is produced during the metabolism of Met, caused the cell cycle progression to resume and lipid peroxidation and the subsequent induction of ferroptosis was also restored under conditions of Met/cystine double deprivation.	S-Adenosylmethionine	21-41	SAFB like transcription modulator	Homo sapiens	112-115
35626640-7	2022	Supplementation with S-adenosylmethionine (SAM), a methyl group donor that is produced during the metabolism of Met, caused the cell cycle progression to resume and lipid peroxidation and the subsequent induction of ferroptosis was also restored under conditions of Met/cystine double deprivation.	S-Adenosylmethionine	21-41	SAFB like transcription modulator	Homo sapiens	266-269
35626640-7	2022	Supplementation with S-adenosylmethionine (SAM), a methyl group donor that is produced during the metabolism of Met, caused the cell cycle progression to resume and lipid peroxidation and the subsequent induction of ferroptosis was also restored under conditions of Met/cystine double deprivation.	S-Adenosylmethionine	43-46	SAFB like transcription modulator	Homo sapiens	112-115
35626640-7	2022	Supplementation with S-adenosylmethionine (SAM), a methyl group donor that is produced during the metabolism of Met, caused the cell cycle progression to resume and lipid peroxidation and the subsequent induction of ferroptosis was also restored under conditions of Met/cystine double deprivation.	S-Adenosylmethionine	43-46	SAFB like transcription modulator	Homo sapiens	266-269
35486881-5	2022	The N-terminal domain of PCMTD1 contains l-isoaspartate and S-adenosylmethionine (AdoMet) binding motifs similar to those in PCMT1.	S-Adenosylmethionine	60-80	protein-L-isoaspartate (D-aspartate) O-methyltransferase domain containing 1	Homo sapiens	25-31
35486881-5	2022	The N-terminal domain of PCMTD1 contains l-isoaspartate and S-adenosylmethionine (AdoMet) binding motifs similar to those in PCMT1.	S-Adenosylmethionine	82-88	protein-L-isoaspartate (D-aspartate) O-methyltransferase domain containing 1	Homo sapiens	25-31
35486881-7	2022	We demonstrate specific PCMTD1 binding to the canonical methyltransferase cofactor S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	83-103	protein-L-isoaspartate (D-aspartate) O-methyltransferase domain containing 1	Homo sapiens	24-30
35486881-7	2022	We demonstrate specific PCMTD1 binding to the canonical methyltransferase cofactor S-adenosylmethionine (AdoMet).	S-Adenosylmethionine	105-111	protein-L-isoaspartate (D-aspartate) O-methyltransferase domain containing 1	Homo sapiens	24-30
35627245-2	2022	S-adenosylmethionine (SAM) is widely involved in the plant stress response and growth regulation; however, the role of the S-adenosylmethionine synthase (SAMS) gene family in this process is poorly understood.	S-Adenosylmethionine	0-20	S-adenosylmethionine synthase	Gossypium hirsutum	123-152
35627245-2	2022	S-adenosylmethionine (SAM) is widely involved in the plant stress response and growth regulation; however, the role of the S-adenosylmethionine synthase (SAMS) gene family in this process is poorly understood.	S-Adenosylmethionine	0-20	S-adenosylmethionine synthase	Gossypium hirsutum	154-158
35627245-2	2022	S-adenosylmethionine (SAM) is widely involved in the plant stress response and growth regulation; however, the role of the S-adenosylmethionine synthase (SAMS) gene family in this process is poorly understood.	S-Adenosylmethionine	22-25	S-adenosylmethionine synthase	Gossypium hirsutum	123-152
35627245-2	2022	S-adenosylmethionine (SAM) is widely involved in the plant stress response and growth regulation; however, the role of the S-adenosylmethionine synthase (SAMS) gene family in this process is poorly understood.	S-Adenosylmethionine	22-25	S-adenosylmethionine synthase	Gossypium hirsutum	154-158
35316659-2	2022	Viperin, a member of the radical S-adenosyl methionine (SAM) superfamily of enzymes, is the product of one such ISG that restricts the replication of a broad spectrum of viruses.	S-Adenosylmethionine	56-59	radical S-adenosyl methionine domain containing 2	Homo sapiens	0-7
35464759-2	2022	Slc25a26 is the gene encoding S-adenosylmethionine carrier (SAMC), a member of the mitochondrial carrier family.	S-Adenosylmethionine	30-50	solute carrier family 25 (mitochondrial carrier, phosphate carrier), member 26	Mus musculus	0-8
35244730-4	2022	The current model consists of AS3MT methylating iAs in the presence of the cofactor S-adenosyl-L-methionine (SAM), and the formation of intramolecular disulfide bonds following the reduction of MAsV to MAsIII.	S-Adenosylmethionine	84-107	arsenite methyltransferase	Mus musculus	30-35
35244730-4	2022	The current model consists of AS3MT methylating iAs in the presence of the cofactor S-adenosyl-L-methionine (SAM), and the formation of intramolecular disulfide bonds following the reduction of MAsV to MAsIII.	S-Adenosylmethionine	109-112	arsenite methyltransferase	Mus musculus	30-35
35244730-11	2022	In vitro experiments show that automethylated AS3MT can methylate iAs in the presence of SAM.	S-Adenosylmethionine	89-92	arsenite methyltransferase	Mus musculus	46-51
35462606-11	2022	Indeed, SAM treatment resulted to be effective in inducing hypermethylation of SCNN1B gene promoter and in lowering its expression.	S-Adenosylmethionine	8-11	sodium channel epithelial 1 subunit beta	Homo sapiens	79-85
35361955-7	2022	Mechanistically, AC-derived methionine is converted to S-adenosylmethionine, which is used by DNA methyltransferase-3A (DNMT3A) to methylate Dusp4.	S-Adenosylmethionine	55-75	DNA methyltransferase 3A	Mus musculus	94-118
35344653-0	2022	The Atypical Cobalamin-Dependent S-Adenosyl-l-Methionine Nonradical Methylase TsrM and Its Radical Counterparts.	S-Adenosylmethionine	33-56	TSRM	Homo sapiens	78-82
35121169-2	2022	This includes decreased glycine N-methyltransferase (GNMT), a critical regulator of s-adenosylmethionine (SAM).	S-Adenosylmethionine	84-104	glycine N-methyltransferase	Mus musculus	24-51
35121169-2	2022	This includes decreased glycine N-methyltransferase (GNMT), a critical regulator of s-adenosylmethionine (SAM).	S-Adenosylmethionine	84-104	glycine N-methyltransferase	Mus musculus	53-57
35121169-2	2022	This includes decreased glycine N-methyltransferase (GNMT), a critical regulator of s-adenosylmethionine (SAM).	S-Adenosylmethionine	106-109	glycine N-methyltransferase	Mus musculus	24-51
35121169-2	2022	This includes decreased glycine N-methyltransferase (GNMT), a critical regulator of s-adenosylmethionine (SAM).	S-Adenosylmethionine	106-109	glycine N-methyltransferase	Mus musculus	53-57
35432433-1	2022	In plants, the key enzyme in ethylene biosynthesis is 1-aminocyclopropane-1 carboxylic acid (ACC) synthase (ACS), which catalyzes S-adenosyl-L-methionine (SAM) to ACC, the precursor of ethylene.	S-Adenosylmethionine	130-153	acetyl-CoA synthetase	Arabidopsis thaliana	108-111
35432433-1	2022	In plants, the key enzyme in ethylene biosynthesis is 1-aminocyclopropane-1 carboxylic acid (ACC) synthase (ACS), which catalyzes S-adenosyl-L-methionine (SAM) to ACC, the precursor of ethylene.	S-Adenosylmethionine	155-158	acetyl-CoA synthetase	Arabidopsis thaliana	108-111
35361955-7	2022	Mechanistically, AC-derived methionine is converted to S-adenosylmethionine, which is used by DNA methyltransferase-3A (DNMT3A) to methylate Dusp4.	S-Adenosylmethionine	55-75	DNA methyltransferase 3A	Mus musculus	120-126
35361955-7	2022	Mechanistically, AC-derived methionine is converted to S-adenosylmethionine, which is used by DNA methyltransferase-3A (DNMT3A) to methylate Dusp4.	S-Adenosylmethionine	55-75	dual specificity phosphatase 4	Mus musculus	141-146
35293760-1	2022	Inhibition of the S-adenosyl methionine (SAM)-producing metabolic enzyme, methionine adenosyltransferase 2A (MAT2A), has received significant interest in the field of medicinal chemistry due to its implication as a synthetic lethal target in cancers with the deletion of the methylthioadenosine phosphorylase (MTAP) gene.	S-Adenosylmethionine	41-44	methionine adenosyltransferase 2A	Homo sapiens	74-107
35293760-1	2022	Inhibition of the S-adenosyl methionine (SAM)-producing metabolic enzyme, methionine adenosyltransferase 2A (MAT2A), has received significant interest in the field of medicinal chemistry due to its implication as a synthetic lethal target in cancers with the deletion of the methylthioadenosine phosphorylase (MTAP) gene.	S-Adenosylmethionine	41-44	methionine adenosyltransferase 2A	Homo sapiens	109-114
35293760-1	2022	Inhibition of the S-adenosyl methionine (SAM)-producing metabolic enzyme, methionine adenosyltransferase 2A (MAT2A), has received significant interest in the field of medicinal chemistry due to its implication as a synthetic lethal target in cancers with the deletion of the methylthioadenosine phosphorylase (MTAP) gene.	S-Adenosylmethionine	41-44	methylthioadenosine phosphorylase	Homo sapiens	275-308
35293760-1	2022	Inhibition of the S-adenosyl methionine (SAM)-producing metabolic enzyme, methionine adenosyltransferase 2A (MAT2A), has received significant interest in the field of medicinal chemistry due to its implication as a synthetic lethal target in cancers with the deletion of the methylthioadenosine phosphorylase (MTAP) gene.	S-Adenosylmethionine	41-44	methylthioadenosine phosphorylase	Homo sapiens	310-314
35113558-4	2022	The succinimide intermediate formed during reaction of l-isoAsp-containing peptides with PIMT and S-adenosyl methionine (SAM) is reactive with Tris base and results in a Tris-modified aspartic acid residue with a mass shift of +103 Da.	S-Adenosylmethionine	121-124	protein-L-isoaspartate (D-aspartate) O-methyltransferase	Homo sapiens	89-93
35303200-0	2022	S-Adenosylmethionine affects ERK1/2 and STAT3 pathway in androgen-independent prostate cancer cells.	S-Adenosylmethionine	0-20	mitogen-activated protein kinase 3	Homo sapiens	29-35
35303200-0	2022	S-Adenosylmethionine affects ERK1/2 and STAT3 pathway in androgen-independent prostate cancer cells.	S-Adenosylmethionine	0-20	signal transducer and activator of transcription 3	Homo sapiens	40-45
35182729-7	2022	Mechanistically, MAT2A mediates the production of S-adenosylmethionine (SAM), which upregulates ACSL3 by increasing the trimethylation of lysine-4 on histone H3 (H3K4me3) at the promoter area, resulting in ferroptosis resistance.	S-Adenosylmethionine	50-70	methionine adenosyltransferase 2A	Homo sapiens	17-22
35182729-7	2022	Mechanistically, MAT2A mediates the production of S-adenosylmethionine (SAM), which upregulates ACSL3 by increasing the trimethylation of lysine-4 on histone H3 (H3K4me3) at the promoter area, resulting in ferroptosis resistance.	S-Adenosylmethionine	50-70	acyl-CoA synthetase long chain family member 3	Homo sapiens	96-101
35182729-7	2022	Mechanistically, MAT2A mediates the production of S-adenosylmethionine (SAM), which upregulates ACSL3 by increasing the trimethylation of lysine-4 on histone H3 (H3K4me3) at the promoter area, resulting in ferroptosis resistance.	S-Adenosylmethionine	72-75	methionine adenosyltransferase 2A	Homo sapiens	17-22
35182729-7	2022	Mechanistically, MAT2A mediates the production of S-adenosylmethionine (SAM), which upregulates ACSL3 by increasing the trimethylation of lysine-4 on histone H3 (H3K4me3) at the promoter area, resulting in ferroptosis resistance.	S-Adenosylmethionine	72-75	acyl-CoA synthetase long chain family member 3	Homo sapiens	96-101
35064691-1	2022	Methionine adenosyltransferase II alpha (MAT2A) is the key enzyme to transform methionine and adenosine-triphosphate (ATP) to S-adenosylmethionine (SAM), a general methyl-group donor in vitro.	S-Adenosylmethionine	126-146	methionine adenosyltransferase 2A	Homo sapiens	0-39
35143475-7	2022	Finally, control over METTL3/METTL14 condensation is determined by its small molecule cofactor, S-adenosylmethionine (SAM), which regulates conformations of 2 gate loops, and some cancer-associated mutations near gate loops can impair METTL3 condensation.	S-Adenosylmethionine	96-116	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	22-28
35143475-7	2022	Finally, control over METTL3/METTL14 condensation is determined by its small molecule cofactor, S-adenosylmethionine (SAM), which regulates conformations of 2 gate loops, and some cancer-associated mutations near gate loops can impair METTL3 condensation.	S-Adenosylmethionine	96-116	methyltransferase 14, N6-adenosine-methyltransferase subunit	Homo sapiens	29-36
35143475-7	2022	Finally, control over METTL3/METTL14 condensation is determined by its small molecule cofactor, S-adenosylmethionine (SAM), which regulates conformations of 2 gate loops, and some cancer-associated mutations near gate loops can impair METTL3 condensation.	S-Adenosylmethionine	96-116	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	235-241
35143475-7	2022	Finally, control over METTL3/METTL14 condensation is determined by its small molecule cofactor, S-adenosylmethionine (SAM), which regulates conformations of 2 gate loops, and some cancer-associated mutations near gate loops can impair METTL3 condensation.	S-Adenosylmethionine	118-121	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	22-28
35143475-7	2022	Finally, control over METTL3/METTL14 condensation is determined by its small molecule cofactor, S-adenosylmethionine (SAM), which regulates conformations of 2 gate loops, and some cancer-associated mutations near gate loops can impair METTL3 condensation.	S-Adenosylmethionine	118-121	methyltransferase 14, N6-adenosine-methyltransferase subunit	Homo sapiens	29-36
35143475-7	2022	Finally, control over METTL3/METTL14 condensation is determined by its small molecule cofactor, S-adenosylmethionine (SAM), which regulates conformations of 2 gate loops, and some cancer-associated mutations near gate loops can impair METTL3 condensation.	S-Adenosylmethionine	118-121	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	235-241
35216315-9	2022	We did, however, detect increased expression of solute carrier family 25A26 (SLC25A26), encoding the importer of S-adenosylmethionine, together with enhanced mtDNA copy numbers in myopathy fibroblasts compared to healthy controls.	S-Adenosylmethionine	113-133	solute carrier family 25 member 26	Homo sapiens	48-75
35216315-9	2022	We did, however, detect increased expression of solute carrier family 25A26 (SLC25A26), encoding the importer of S-adenosylmethionine, together with enhanced mtDNA copy numbers in myopathy fibroblasts compared to healthy controls.	S-Adenosylmethionine	113-133	solute carrier family 25 member 26	Homo sapiens	77-85
35216100-8	2022	We found that a reduction of GNMT leads to a significant increase in S-adenosylmethionine (AdoMet), an essential metabolite for transmethylation reactions and a substrate for polyamine synthesis.	S-Adenosylmethionine	69-89	glycine N-methyltransferase	Homo sapiens	29-33
35216100-8	2022	We found that a reduction of GNMT leads to a significant increase in S-adenosylmethionine (AdoMet), an essential metabolite for transmethylation reactions and a substrate for polyamine synthesis.	S-Adenosylmethionine	91-97	glycine N-methyltransferase	Homo sapiens	29-33
35064691-1	2022	Methionine adenosyltransferase II alpha (MAT2A) is the key enzyme to transform methionine and adenosine-triphosphate (ATP) to S-adenosylmethionine (SAM), a general methyl-group donor in vitro.	S-Adenosylmethionine	126-146	methionine adenosyltransferase 2A	Homo sapiens	41-46
35064691-1	2022	Methionine adenosyltransferase II alpha (MAT2A) is the key enzyme to transform methionine and adenosine-triphosphate (ATP) to S-adenosylmethionine (SAM), a general methyl-group donor in vitro.	S-Adenosylmethionine	148-151	methionine adenosyltransferase 2A	Homo sapiens	0-39
35064691-1	2022	Methionine adenosyltransferase II alpha (MAT2A) is the key enzyme to transform methionine and adenosine-triphosphate (ATP) to S-adenosylmethionine (SAM), a general methyl-group donor in vitro.	S-Adenosylmethionine	148-151	methionine adenosyltransferase 2A	Homo sapiens	41-46
35091576-1	2022	MATalpha1 catalyzes the synthesis of S-adenosylmethionine, the principal biological methyl donor.	S-Adenosylmethionine	37-57	methionine adenosyltransferase 1A	Homo sapiens	0-9
35159219-1	2022	Alterations of methionine cycle in steatohepatitis, cirrhosis, and hepatocellular carcinoma induce MAT1A decrease and MAT2A increase expressions with the consequent decrease of S-adenosyl-L-methionine (SAM).	S-Adenosylmethionine	177-200	methionine adenosyltransferase 2A	Homo sapiens	118-123
35159219-1	2022	Alterations of methionine cycle in steatohepatitis, cirrhosis, and hepatocellular carcinoma induce MAT1A decrease and MAT2A increase expressions with the consequent decrease of S-adenosyl-L-methionine (SAM).	S-Adenosylmethionine	202-205	methionine adenosyltransferase 2A	Homo sapiens	118-123
34523682-0	2022	Electrical polarity-dependent gating and a unique subconductance of RyR2 induced by S-adenosyl methionine via the ATP binding site.	S-Adenosylmethionine	84-105	ryanodine receptor 2	Homo sapiens	68-72
34523682-1	2022	S-Adenosyl-l-methionine (SAM) was used to probe the functional effects exerted via the RyR2 adenine nucleotide binding site.	S-Adenosylmethionine	0-23	ryanodine receptor 2	Homo sapiens	87-91
34523682-1	2022	S-Adenosyl-l-methionine (SAM) was used to probe the functional effects exerted via the RyR2 adenine nucleotide binding site.	S-Adenosylmethionine	25-28	ryanodine receptor 2	Homo sapiens	87-91
35060905-1	2022	Methyltransferase like-3 (METTL3) and METTL14 complex transfers a methyl group from S-adenosyl-L-methionine to N6 amino group of adenosine bases in RNA (m6A) and DNA (m6dA).	S-Adenosylmethionine	84-107	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	0-24
35060905-1	2022	Methyltransferase like-3 (METTL3) and METTL14 complex transfers a methyl group from S-adenosyl-L-methionine to N6 amino group of adenosine bases in RNA (m6A) and DNA (m6dA).	S-Adenosylmethionine	84-107	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	26-32
35060905-1	2022	Methyltransferase like-3 (METTL3) and METTL14 complex transfers a methyl group from S-adenosyl-L-methionine to N6 amino group of adenosine bases in RNA (m6A) and DNA (m6dA).	S-Adenosylmethionine	84-107	methyltransferase 14, N6-adenosine-methyltransferase subunit	Homo sapiens	38-45
35024855-1	2022	The SLC25A26 gene encodes a mitochondrial inner membrane carrier that transports S-adenosylmethionine (SAM) into the mitochondrial matrix in exchange for S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	81-101	solute carrier family 25 member 26	Homo sapiens	4-12
35024855-1	2022	The SLC25A26 gene encodes a mitochondrial inner membrane carrier that transports S-adenosylmethionine (SAM) into the mitochondrial matrix in exchange for S-adenosylhomocysteine (SAH).	S-Adenosylmethionine	103-106	solute carrier family 25 member 26	Homo sapiens	4-12