PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
12837111-3	2003	On dense SAMs, hydroxyl ions are highly mobile.	Hydroxyl Radical	15-23	methionine adenosyltransferase 1A	Homo sapiens	9-13
12409306-3	2003	It has a putative Akt phosphorylation motif at amino acids 595-600, and Ser(600) was found to be phosphorylated by active Akt resulting in the activation of kinase activity toward the SAMS peptide, a consensus AMPK substrate.	Serine	72-75	methionine adenosyltransferase 1A	Homo sapiens	184-188
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.	Adenosine Monophosphate	12-15	methionine adenosyltransferase 1A	Homo sapiens	39-44
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.	Adenosine Monophosphate	12-15	methionine adenosyltransferase 1A	Homo sapiens	144-149
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
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
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	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
12660248-4	2003	In l-methionine-deficient cells, MAT2A gene expression is rapidly induced, and methionine adenosyltransferase activity is increased.	Methionine	3-15	methionine adenosyltransferase 1A	Homo sapiens	79-109
11467525-9	2001	The as-prepared Au films on substrates are reproducible and stable, which allows them to be used as electrodes for electrochemical experiments and as platforms for studying SAMs.	Gold	16-18	methionine adenosyltransferase 1A	Homo sapiens	173-177
12145770-1	2002	Abnormal elevation of plasma methionine may result from several different genetic abnormalities, including deficiency of cystathionine beta-synthase (CBS) or of the isoenzymes of methionine adenosyltransferase (MAT) I and III expressed solely in nonfetal liver (MAT I/III deficiency).	Methionine	29-39	methionine adenosyltransferase 1A	Homo sapiens	222-225
11890768-0	2002	SERS detection of the vibrational Stark effect from nitrile-terminated SAMs to probe electric fields in the diffuse double-layer.	Nitriles	52-59	methionine adenosyltransferase 1A	Homo sapiens	71-75
11853422-5	2002	The Pd/S interfacial layer formed by the reaction of palladium films with sulfur-containing compounds provides good resistance to etches independently of the barrier to access the surface provided by the film of (CH2)n groups in the long-chain SAMs.	Palladium	4-6	methionine adenosyltransferase 1A	Homo sapiens	244-248
11853422-5	2002	The Pd/S interfacial layer formed by the reaction of palladium films with sulfur-containing compounds provides good resistance to etches independently of the barrier to access the surface provided by the film of (CH2)n groups in the long-chain SAMs.	Sulfur	7-8	methionine adenosyltransferase 1A	Homo sapiens	244-248
11853422-5	2002	The Pd/S interfacial layer formed by the reaction of palladium films with sulfur-containing compounds provides good resistance to etches independently of the barrier to access the surface provided by the film of (CH2)n groups in the long-chain SAMs.	Sulfur	74-80	methionine adenosyltransferase 1A	Homo sapiens	244-248
11745541-3	2002	Cell growth on patterned SAMs demonstrated preferences for one pattern region in all combinations of alkylthiols, with the hierarchical preference COOH > OH > CH(3).	Carbonic Acid	147-151	methionine adenosyltransferase 1A	Homo sapiens	25-29
11745541-8	2002	Attachment was maximal on COOH-terminated SAMs precoated with fibronectin.	Carbonic Acid	26-30	methionine adenosyltransferase 1A	Homo sapiens	42-46
12387320-5	2002	The data suggest that neutralization of methyl cation with hydrocarbon and fluorocarbon SAMs occurs by concerted chemical reactions, i.e., that neutralization of the projectile occurs not only by a direct electron transfer from the surface but also by formation of a neutral molecule.	Fluorocarbons	75-87	methionine adenosyltransferase 1A	Homo sapiens	88-92
12240390-0	2001	The structure dependent electrochemical-response of novel 1-(4-mercaptobutyl)-4-(2-ferrocenylvinyl)pyridinium bromide SAMs on an au electrode.	1-(4-mercaptobutyl)-4-(2-ferrocenylvinyl)pyridinium bromide	58-117	methionine adenosyltransferase 1A	Homo sapiens	118-122
12240390-0	2001	The structure dependent electrochemical-response of novel 1-(4-mercaptobutyl)-4-(2-ferrocenylvinyl)pyridinium bromide SAMs on an au electrode.	Gold	129-131	methionine adenosyltransferase 1A	Homo sapiens	118-122
11520127-0	2001	L-dopa upregulates the expression and activities of methionine adenosyl transferase and catechol-O-methyltransferase.	Levodopa	0-6	methionine adenosyltransferase 1A	Homo sapiens	52-83
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.	Levodopa	38-44	methionine adenosyltransferase 1A	Homo sapiens	96-127
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.	Levodopa	38-44	methionine adenosyltransferase 1A	Homo sapiens	129-132
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
11520127-11	2001	Western blot analysis showed that MAT is more clearly characterized in 10% mercaptoethanol reducing buffer in which 31.5-, 38- (beta), and 48-kDa (alpha1/alpha2) subunits were distinctly revealed.	Mercaptoethanol	75-90	methionine adenosyltransferase 1A	Homo sapiens	34-37
11520127-16	2001	The highlight of the study is the fact that L-dopa induces the enzymes MAT and COMT.	Levodopa	44-50	methionine adenosyltransferase 1A	Homo sapiens	71-74
11520127-18	2001	Thus, during PD treatment with L-dopa the induction of MAT and COMT is likely to occur and in turn increase the methylation and reduction of L-dopa and DA that may help cause the tolerance or the wearing-off effect developed to L-dopa.	Levodopa	31-37	methionine adenosyltransferase 1A	Homo sapiens	55-58
11520127-18	2001	Thus, during PD treatment with L-dopa the induction of MAT and COMT is likely to occur and in turn increase the methylation and reduction of L-dopa and DA that may help cause the tolerance or the wearing-off effect developed to L-dopa.	Levodopa	141-147	methionine adenosyltransferase 1A	Homo sapiens	55-58
11520127-18	2001	Thus, during PD treatment with L-dopa the induction of MAT and COMT is likely to occur and in turn increase the methylation and reduction of L-dopa and DA that may help cause the tolerance or the wearing-off effect developed to L-dopa.	Dopamine	152-154	methionine adenosyltransferase 1A	Homo sapiens	55-58
11520127-18	2001	Thus, during PD treatment with L-dopa the induction of MAT and COMT is likely to occur and in turn increase the methylation and reduction of L-dopa and DA that may help cause the tolerance or the wearing-off effect developed to L-dopa.	Levodopa	141-147	methionine adenosyltransferase 1A	Homo sapiens	55-58
11288084-2	2001	In this study two laboratory-synthesized long-chain alkanethiols, HS(CH(2))(10)PO(3)-(C(2)H(5))(2) and HS(CH(2))(10)PO(3)H(2), were employed for the direct preparation of SAMs with nonionic and ionic functional groups.	alkanethiols	52-64	methionine adenosyltransferase 1A	Homo sapiens	171-175
11374919-4	2001	According to this model, the ionic and/or other binding interactions between the surface Au(2)O(3) and the alkanethiol hydrophilic terminal end as well as the interactions between the terminal SAM functionalities could cause the packing disorder found on these three SAMs formed on Au substrates containing Au(2)O(3) surface species.	au(2)o	89-95	methionine adenosyltransferase 1A	Homo sapiens	267-271
11374919-4	2001	According to this model, the ionic and/or other binding interactions between the surface Au(2)O(3) and the alkanethiol hydrophilic terminal end as well as the interactions between the terminal SAM functionalities could cause the packing disorder found on these three SAMs formed on Au substrates containing Au(2)O(3) surface species.	alkanethiol	107-118	methionine adenosyltransferase 1A	Homo sapiens	267-271
11374919-4	2001	According to this model, the ionic and/or other binding interactions between the surface Au(2)O(3) and the alkanethiol hydrophilic terminal end as well as the interactions between the terminal SAM functionalities could cause the packing disorder found on these three SAMs formed on Au substrates containing Au(2)O(3) surface species.	Gold	89-91	methionine adenosyltransferase 1A	Homo sapiens	267-271
11374919-4	2001	According to this model, the ionic and/or other binding interactions between the surface Au(2)O(3) and the alkanethiol hydrophilic terminal end as well as the interactions between the terminal SAM functionalities could cause the packing disorder found on these three SAMs formed on Au substrates containing Au(2)O(3) surface species.	au(2)o	307-313	methionine adenosyltransferase 1A	Homo sapiens	267-271
11145114-6	2000	A low plasma AdoMet concentration in the presence of an elevated methionine provides a useful diagnostic tool that pinpoints the cause of a case of hypermethioninemia as defective MAT I/III activity.	Methionine	65-75	methionine adenosyltransferase 1A	Homo sapiens	180-189
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
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
10834300-3	2000	Chronic L-dopa induces catechol-O-methyltransferase (COMT) and methionine adenosyl transferase (MAT), enzymes involved in the methylation of catecholamines (CA).	Levodopa	8-14	methionine adenosyltransferase 1A	Homo sapiens	63-94
10952521-3	2000	Experiments using model probes coated with -CH3 and -COOH terminated SAMs have been performed on the two aspirin crystal planes (001) and (100).	Carbonic Acid	53-57	methionine adenosyltransferase 1A	Homo sapiens	69-73
10952521-3	2000	Experiments using model probes coated with -CH3 and -COOH terminated SAMs have been performed on the two aspirin crystal planes (001) and (100).	Aspirin	105-112	methionine adenosyltransferase 1A	Homo sapiens	69-73
10834300-3	2000	Chronic L-dopa induces catechol-O-methyltransferase (COMT) and methionine adenosyl transferase (MAT), enzymes involved in the methylation of catecholamines (CA).	Levodopa	8-14	methionine adenosyltransferase 1A	Homo sapiens	96-99
10834300-3	2000	Chronic L-dopa induces catechol-O-methyltransferase (COMT) and methionine adenosyl transferase (MAT), enzymes involved in the methylation of catecholamines (CA).	Catecholamines	141-155	methionine adenosyltransferase 1A	Homo sapiens	63-94
10834300-3	2000	Chronic L-dopa induces catechol-O-methyltransferase (COMT) and methionine adenosyl transferase (MAT), enzymes involved in the methylation of catecholamines (CA).	Catecholamines	141-155	methionine adenosyltransferase 1A	Homo sapiens	96-99
10834300-11	2000	L-dopa produces high levels of DA and induces MAT and COMT.	Levodopa	0-6	methionine adenosyltransferase 1A	Homo sapiens	46-49
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
10620770-7	2000	We assume that methionine reduces the level of one or several adenine nucleotides by a SAMS-mediated mechanism.	Methionine	15-25	methionine adenosyltransferase 1A	Homo sapiens	87-91
10620770-7	2000	We assume that methionine reduces the level of one or several adenine nucleotides by a SAMS-mediated mechanism.	Adenine Nucleotides	62-81	methionine adenosyltransferase 1A	Homo sapiens	87-91
10627284-10	2000	Finally we demonstrate that MAT1A expression is reactivated in the human hepatoma cell line HepG2 treated with 5-aza-2"-deoxycytidine or the histone deacetylase inhibitor trichostatin, suggesting a role for DNA hypermethylation and histone deacetylation in MAT1A silencing.	Decitabine	111-133	methionine adenosyltransferase 1A	Homo sapiens	28-33
10627284-10	2000	Finally we demonstrate that MAT1A expression is reactivated in the human hepatoma cell line HepG2 treated with 5-aza-2"-deoxycytidine or the histone deacetylase inhibitor trichostatin, suggesting a role for DNA hypermethylation and histone deacetylation in MAT1A silencing.	Decitabine	111-133	methionine adenosyltransferase 1A	Homo sapiens	257-262
10627284-10	2000	Finally we demonstrate that MAT1A expression is reactivated in the human hepatoma cell line HepG2 treated with 5-aza-2"-deoxycytidine or the histone deacetylase inhibitor trichostatin, suggesting a role for DNA hypermethylation and histone deacetylation in MAT1A silencing.	trichostatin A	171-183	methionine adenosyltransferase 1A	Homo sapiens	28-33
10627284-10	2000	Finally we demonstrate that MAT1A expression is reactivated in the human hepatoma cell line HepG2 treated with 5-aza-2"-deoxycytidine or the histone deacetylase inhibitor trichostatin, suggesting a role for DNA hypermethylation and histone deacetylation in MAT1A silencing.	trichostatin A	171-183	methionine adenosyltransferase 1A	Homo sapiens	257-262
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
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.	Methionine	8-18	methionine adenosyltransferase 1A	Homo sapiens	92-97
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.	Adenosine Triphosphate	220-223	methionine adenosyltransferase 1A	Homo sapiens	92-97
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
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
10415148-4	1999	In comparison with controls, the male group presented a 33% higher V(max) (P < 0.05) and a 41% decrease in the affinity of MAT for methionine (K(m), P < 0.05).	Methionine	131-141	methionine adenosyltransferase 1A	Homo sapiens	123-126
10328895-2	1999	The structure and surface properties of the SAMs of MDQ were characterized by ellipsometry, reflection absorption FTIR (RA-IR), and contact angle titration.	mdq	52-55	methionine adenosyltransferase 1A	Homo sapiens	44-48
10328895-4	1999	The molecular orientation of MDQ in SAMs was evaluated by RA-IR spectroscopy which indicates that the alkyl chain exhibits a tilting angle of 24 +/- 4 degrees with respect to the surface normal and a twisting angle of 50 +/- 5 degrees around its axis.	mdq	29-32	methionine adenosyltransferase 1A	Homo sapiens	36-40
10328895-5	1999	Contact angle titration in the pH range between 2 and 12 illustrates that the surface of SAM of MDQ is less hydrophilic for acidic solution than for basic solution, which is in contrast with the previous reports on SAMs that basic groups are located at the ends of the molecules.	mdq	96-99	methionine adenosyltransferase 1A	Homo sapiens	215-219
10216131-0	1999	Differential effect of thioacetamide on hepatic methionine adenosyltransferase expression in the rat.	Thioacetamide	23-36	methionine adenosyltransferase 1A	Homo sapiens	48-78
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
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	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
10216131-4	1999	To gain a better understanding of the chronology and significance of the change in MAT expression, we examined changes in hepatic MAT expression after acute treatment of rats with a hepatocarcinogen, thioacetamide (TAA).	Thioacetamide	200-213	methionine adenosyltransferase 1A	Homo sapiens	130-133
10216131-8	1999	Because liver-specific MAT exhibits a much higher Km for methionine (mmol/L) than non-liver-specific MAT ( approximately 10 micromol/L), MAT activity was decreased at 5 mmol/L but increased at 20 micromol/L methionine concentration.	Methionine	57-67	methionine adenosyltransferase 1A	Homo sapiens	23-26
10216131-8	1999	Because liver-specific MAT exhibits a much higher Km for methionine (mmol/L) than non-liver-specific MAT ( approximately 10 micromol/L), MAT activity was decreased at 5 mmol/L but increased at 20 micromol/L methionine concentration.	Methionine	207-217	methionine adenosyltransferase 1A	Homo sapiens	23-26
9755242-1	1998	We investigated the mechanism of nitric oxide (NO) action on hepatic methionine adenosyltransferase (MAT) activity using S-nitrosoglutathione (GSNO) as NO donor.	Nitric Oxide	33-45	methionine adenosyltransferase 1A	Homo sapiens	101-104
9755242-2	1998	Hepatic MAT plays an essential role in the metabolism of methionine, converting this amino acid into S-adenosylmethionine.	Methionine	57-67	methionine adenosyltransferase 1A	Homo sapiens	8-11
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
9755242-5	1998	In MAT I, S-nitrosylation of 1 thiol residue per subunit was associated with a marked inactivation of the enzyme (about 70%) that was reversed by glutathione (GSH).	Sulfhydryl Compounds	31-36	methionine adenosyltransferase 1A	Homo sapiens	3-6
9755242-5	1998	In MAT I, S-nitrosylation of 1 thiol residue per subunit was associated with a marked inactivation of the enzyme (about 70%) that was reversed by glutathione (GSH).	Glutathione	146-157	methionine adenosyltransferase 1A	Homo sapiens	3-6
9755242-5	1998	In MAT I, S-nitrosylation of 1 thiol residue per subunit was associated with a marked inactivation of the enzyme (about 70%) that was reversed by glutathione (GSH).	Glutathione	159-162	methionine adenosyltransferase 1A	Homo sapiens	3-6
9755242-6	1998	In MAT III, S-nitrosylation of 3 thiol residues per subunit led to a similar inactivation of the enzyme, which was also reversed by GSH.	Sulfhydryl Compounds	33-38	methionine adenosyltransferase 1A	Homo sapiens	3-6
9755242-6	1998	In MAT III, S-nitrosylation of 3 thiol residues per subunit led to a similar inactivation of the enzyme, which was also reversed by GSH.	Glutathione	132-135	methionine adenosyltransferase 1A	Homo sapiens	3-6
9755242-7	1998	Incubation of isolated rat hepatocytes with S-nitrosoglutathione monoethyl ester (EGSNO), a NO donor permeable through the cellular membrane, induced a dose-dependent inactivation of MAT that was reversed by removing the NO donor from the cell suspension.	s-nitrosoglutathione monoethyl ester	44-80	methionine adenosyltransferase 1A	Homo sapiens	183-186
9755242-7	1998	Incubation of isolated rat hepatocytes with S-nitrosoglutathione monoethyl ester (EGSNO), a NO donor permeable through the cellular membrane, induced a dose-dependent inactivation of MAT that was reversed by removing the NO donor from the cell suspension.	egsno	82-87	methionine adenosyltransferase 1A	Homo sapiens	183-186
9755242-8	1998	MAT, purified from isolated rat hepatocytes, contained S-nitrosothiol groups and the addition of increasing concentrations of EGSNO to the hepatocyte suspension led to a progressive S-nitrosylation of the enzyme.	S-Nitrosothiols	55-69	methionine adenosyltransferase 1A	Homo sapiens	0-3
9755242-8	1998	MAT, purified from isolated rat hepatocytes, contained S-nitrosothiol groups and the addition of increasing concentrations of EGSNO to the hepatocyte suspension led to a progressive S-nitrosylation of the enzyme.	egsno	126-131	methionine adenosyltransferase 1A	Homo sapiens	0-3
10677294-5	2000	Two patients-a compound heterozygote for truncating and severely inactivating missense mutations and a homozygote for an aberrant splicing MAT1A mutation-have plasma methionine in the 1,226-1,870 microM range (normal 5-35 microM) and manifest abnormalities of the brain gray matter or signs of brain demyelination.	Methionine	166-176	methionine adenosyltransferase 1A	Homo sapiens	139-144
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
10955733-1	2000	Methionine adenosyltransferase (MAT) catalyzes the synthesis of S-adenosylmethionine (AdoMet) from ATP and L-methionine.	Adenosine Triphosphate	99-102	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.	Adenosine Triphosphate	99-102	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.	Methionine	107-119	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.	Methionine	107-119	methionine adenosyltransferase 1A	Homo sapiens	32-35
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
10567242-1	1999	S-Adenosylmethionine (AdoMet) synthetase (SAMS: EC 2.5.1.6) catalyses the formation of AdoMet from methionine and ATP.	Methionine	10-20	methionine adenosyltransferase 1A	Homo sapiens	42-46
10567242-1	1999	S-Adenosylmethionine (AdoMet) synthetase (SAMS: EC 2.5.1.6) catalyses the formation of AdoMet from methionine and ATP.	Adenosine Triphosphate	114-117	methionine adenosyltransferase 1A	Homo sapiens	42-46
10567242-6	1999	The PfSAMS protein is highly homologous to all other SAMS, including a conserved motif for the phosphate-binding P-loop, HGGGAFSGKD, and the signature hexapeptide, GAGDQG.	Phosphates	95-104	methionine adenosyltransferase 1A	Homo sapiens	6-10
10567242-7	1999	All the active-site amino acids for the binding of ADP, P(i) and metal ions are similarly preserved, matching entirely those of human hepatic SAMS and Escherichia coli SAMS.	Adenosine Diphosphate	51-54	methionine adenosyltransferase 1A	Homo sapiens	142-146
10567242-7	1999	All the active-site amino acids for the binding of ADP, P(i) and metal ions are similarly preserved, matching entirely those of human hepatic SAMS and Escherichia coli SAMS.	Adenosine Diphosphate	51-54	methionine adenosyltransferase 1A	Homo sapiens	168-172
10567242-8	1999	Molecular modelling of PfSAMS guided by the X-ray crystal structure of E. coli SAMS indicates that PfSAMS binds ATP/Mg(2+) in a manner similar to that seen in the E. coli SAMS structure.	Adenosine Triphosphate	112-115	methionine adenosyltransferase 1A	Homo sapiens	25-29
10567242-8	1999	Molecular modelling of PfSAMS guided by the X-ray crystal structure of E. coli SAMS indicates that PfSAMS binds ATP/Mg(2+) in a manner similar to that seen in the E. coli SAMS structure.	Adenosine Triphosphate	112-115	methionine adenosyltransferase 1A	Homo sapiens	79-83
10567242-8	1999	Molecular modelling of PfSAMS guided by the X-ray crystal structure of E. coli SAMS indicates that PfSAMS binds ATP/Mg(2+) in a manner similar to that seen in the E. coli SAMS structure.	Magnesium	116-118	methionine adenosyltransferase 1A	Homo sapiens	25-29
10567242-8	1999	Molecular modelling of PfSAMS guided by the X-ray crystal structure of E. coli SAMS indicates that PfSAMS binds ATP/Mg(2+) in a manner similar to that seen in the E. coli SAMS structure.	Magnesium	116-118	methionine adenosyltransferase 1A	Homo sapiens	79-83
10567242-10	1999	There was a differential sensitivity towards the inhibition by cycloleucine between the expressed PfSAMS and the human hepatic SAMS with K(i) values of 17 and 10 mM, respectively.	Cycloleucine	63-75	methionine adenosyltransferase 1A	Homo sapiens	100-104
10502391-3	1999	Ellipsometry proved that the self-assembled monolayers and multilayers (SAMs) of Ge6 exhibited a tilted orientation to the substrate surface.	UNII-F0JG9C0OQD	81-84	methionine adenosyltransferase 1A	Homo sapiens	72-76
10502391-4	1999	The multilayer film of Ge6 on silicon substrate was obtained by reducing the monolayer SAMs to alcohol hydroxylated surface with LiAlH(4) and repeating the self-assembly process.	UNII-F0JG9C0OQD	23-26	methionine adenosyltransferase 1A	Homo sapiens	87-91
10502391-4	1999	The multilayer film of Ge6 on silicon substrate was obtained by reducing the monolayer SAMs to alcohol hydroxylated surface with LiAlH(4) and repeating the self-assembly process.	Silicon	30-37	methionine adenosyltransferase 1A	Homo sapiens	87-91
18967651-1	1999	The covalent immobilization of DNA onto self-assembled monolayer (SAM) modified gold electrodes (SAM/Au) was studied by X-ray photoelectron spectrometry and electrochemical method so as to optimize its covalent immobilization on SAMs.	Gold	101-103	methionine adenosyltransferase 1A	Homo sapiens	229-233
18967651-4	1999	The ratio of amount of dsDNA immobilized on hydroxyl-terminated SAMs to that on carboxyl-terminated SAMs and to that on amino-terminated SAMs is (3-3.5): (1-1.5): 1.	Hydroxyl Radical	44-52	methionine adenosyltransferase 1A	Homo sapiens	64-68
18967651-5	1999	The dsDNA immobilized covalently on hydroxyl-terminated SAMs accounts for 82.8-87.6% of its total surface amount (including small amount of dsDNA adsorbed).	Hydroxyl Radical	36-44	methionine adenosyltransferase 1A	Homo sapiens	56-60
31416111-1	1998	The formation of three-dimensional self-assembled monolayers (3-D SAMs) generated by the adsorption of n-octadecyl disulfide onto colloidal gold and silver nanoparticles is described.	Disulfide, dioctadecyl	103-124	methionine adenosyltransferase 1A	Homo sapiens	66-70
31416111-3	1998	On gold nanoparticles, this new functionalization method affords crystalline 3-D SAMs that are indistinct from those prepared by the analogous adsorption of n-octadecanethiol.	n-octadecyl mercaptan	157-174	methionine adenosyltransferase 1A	Homo sapiens	81-85
18967358-3	1998	The concentration range of linear response and detection limit were 0.1-10 and 0.05 mM, the interference of ascorbic acid and uric acid were eliminated by the presence of SAMs and the enzyme electrodes were stable over 3 weeks.	Ascorbic Acid	108-121	methionine adenosyltransferase 1A	Homo sapiens	171-175
18967358-3	1998	The concentration range of linear response and detection limit were 0.1-10 and 0.05 mM, the interference of ascorbic acid and uric acid were eliminated by the presence of SAMs and the enzyme electrodes were stable over 3 weeks.	Uric Acid	126-135	methionine adenosyltransferase 1A	Homo sapiens	171-175
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
9699005-3	1998	In order to assess the role of free radicals in cell signaling, we have studies the modulator effect of oxygen and nitrogen active species on liver methionine adenosyltransferase (MAT), a key metabolic enzyme.	Free Radicals	31-44	methionine adenosyltransferase 1A	Homo sapiens	180-183
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
9699005-3	1998	In order to assess the role of free radicals in cell signaling, we have studies the modulator effect of oxygen and nitrogen active species on liver methionine adenosyltransferase (MAT), a key metabolic enzyme.	Oxygen	104-110	methionine adenosyltransferase 1A	Homo sapiens	180-183
9699005-3	1998	In order to assess the role of free radicals in cell signaling, we have studies the modulator effect of oxygen and nitrogen active species on liver methionine adenosyltransferase (MAT), a key metabolic enzyme.	Nitrogen	115-123	methionine adenosyltransferase 1A	Homo sapiens	180-183
9699005-4	1998	The presence of 10 cysteine residues per subunit, makes liver MAT a sensitive target for oxidation/nitrosylation.	Cysteine	19-27	methionine adenosyltransferase 1A	Homo sapiens	62-65
9699005-6	1998	Incubation with H202 or the NO donor S-nitrosylated GSH (GSNO), diminish MAT activity in a dose-and time-dependent manner.	h202	16-20	methionine adenosyltransferase 1A	Homo sapiens	73-76
9699005-6	1998	Incubation with H202 or the NO donor S-nitrosylated GSH (GSNO), diminish MAT activity in a dose-and time-dependent manner.	Glutathione	52-55	methionine adenosyltransferase 1A	Homo sapiens	73-76
9699005-6	1998	Incubation with H202 or the NO donor S-nitrosylated GSH (GSNO), diminish MAT activity in a dose-and time-dependent manner.	S-Nitrosoglutathione	57-61	methionine adenosyltransferase 1A	Homo sapiens	73-76
9699005-8	1998	MAT inactivation originates on the specific and covalent modification of the sulphydryl group of cysteine residue 121.	Cysteine	97-105	methionine adenosyltransferase 1A	Homo sapiens	0-3
9699005-10	1998	It was previously shown that MAT activity is strongly dependent on cellular GSH levels.	Glutathione	76-79	methionine adenosyltransferase 1A	Homo sapiens	29-32
9699005-14	1998	Oxidation also controls liver MAT activity in a cell environment as shown in CHO cells stably transfected with rat liver MAT cDNA upon addition of H2O2 to the culture medium.	Hydrogen Peroxide	147-151	methionine adenosyltransferase 1A	Homo sapiens	30-33
9699005-14	1998	Oxidation also controls liver MAT activity in a cell environment as shown in CHO cells stably transfected with rat liver MAT cDNA upon addition of H2O2 to the culture medium.	Hydrogen Peroxide	147-151	methionine adenosyltransferase 1A	Homo sapiens	121-124
9699005-16	1998	On the basis of the metabolic implications of liver MAT, together with the structural features accounting for the sensitivity of this enzyme to active oxygen and nitrogen species, we propose that modulation of MAT by these agents could be a mechanism to regulate the consumption of ATP in the liver, and thus preserve cellular viability under different stress conditions.	Oxygen	151-157	methionine adenosyltransferase 1A	Homo sapiens	210-213
9699005-16	1998	On the basis of the metabolic implications of liver MAT, together with the structural features accounting for the sensitivity of this enzyme to active oxygen and nitrogen species, we propose that modulation of MAT by these agents could be a mechanism to regulate the consumption of ATP in the liver, and thus preserve cellular viability under different stress conditions.	Nitrogen	162-170	methionine adenosyltransferase 1A	Homo sapiens	210-213
9699005-16	1998	On the basis of the metabolic implications of liver MAT, together with the structural features accounting for the sensitivity of this enzyme to active oxygen and nitrogen species, we propose that modulation of MAT by these agents could be a mechanism to regulate the consumption of ATP in the liver, and thus preserve cellular viability under different stress conditions.	Adenosine Triphosphate	282-285	methionine adenosyltransferase 1A	Homo sapiens	52-55
9699005-16	1998	On the basis of the metabolic implications of liver MAT, together with the structural features accounting for the sensitivity of this enzyme to active oxygen and nitrogen species, we propose that modulation of MAT by these agents could be a mechanism to regulate the consumption of ATP in the liver, and thus preserve cellular viability under different stress conditions.	Adenosine Triphosphate	282-285	methionine adenosyltransferase 1A	Homo sapiens	210-213
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.	Methionine	6-16	methionine adenosyltransferase 1A	Homo sapiens	38-41
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.	Adenosine Triphosphate	144-147	methionine adenosyltransferase 1A	Homo sapiens	38-41
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
9337154-2	1997	Here we report that hydrogen peroxide (H2O2), via generation of hydroxyl radical, inactivates liver MAT by reversibly and covalently oxidizing an enzyme site.	Hydrogen Peroxide	20-37	methionine adenosyltransferase 1A	Homo sapiens	100-103
9337154-2	1997	Here we report that hydrogen peroxide (H2O2), via generation of hydroxyl radical, inactivates liver MAT by reversibly and covalently oxidizing an enzyme site.	Hydrogen Peroxide	39-43	methionine adenosyltransferase 1A	Homo sapiens	100-103
9337154-2	1997	Here we report that hydrogen peroxide (H2O2), via generation of hydroxyl radical, inactivates liver MAT by reversibly and covalently oxidizing an enzyme site.	Hydroxyl Radical	64-80	methionine adenosyltransferase 1A	Homo sapiens	100-103
9337154-3	1997	In vitro studies using pure liver recombinant enzyme and mutants of MAT, where each of the 10 cysteine residues of the enzyme subunit were individually changed to serine by site-directed mutagenesis, identified cysteine 121 as the site of molecular interaction between H2O2 and liver MAT.	Cysteine	94-102	methionine adenosyltransferase 1A	Homo sapiens	68-71
7573050-2	1995	Biopsies to confirm the presumptive diagnosis of partially deficient activity of ATP: L-methionine S-adenosyltransferase (MAT; E.C.2.5.1.6) in liver were not performed on most of these patients.	Adenosine Triphosphate	81-84	methionine adenosyltransferase 1A	Homo sapiens	86-120
9337154-3	1997	In vitro studies using pure liver recombinant enzyme and mutants of MAT, where each of the 10 cysteine residues of the enzyme subunit were individually changed to serine by site-directed mutagenesis, identified cysteine 121 as the site of molecular interaction between H2O2 and liver MAT.	Serine	163-169	methionine adenosyltransferase 1A	Homo sapiens	68-71
9337154-3	1997	In vitro studies using pure liver recombinant enzyme and mutants of MAT, where each of the 10 cysteine residues of the enzyme subunit were individually changed to serine by site-directed mutagenesis, identified cysteine 121 as the site of molecular interaction between H2O2 and liver MAT.	Cysteine	211-219	methionine adenosyltransferase 1A	Homo sapiens	68-71
9337154-3	1997	In vitro studies using pure liver recombinant enzyme and mutants of MAT, where each of the 10 cysteine residues of the enzyme subunit were individually changed to serine by site-directed mutagenesis, identified cysteine 121 as the site of molecular interaction between H2O2 and liver MAT.	Cysteine	211-219	methionine adenosyltransferase 1A	Homo sapiens	284-287
9337154-3	1997	In vitro studies using pure liver recombinant enzyme and mutants of MAT, where each of the 10 cysteine residues of the enzyme subunit were individually changed to serine by site-directed mutagenesis, identified cysteine 121 as the site of molecular interaction between H2O2 and liver MAT.	Hydrogen Peroxide	269-273	methionine adenosyltransferase 1A	Homo sapiens	68-71
9337154-4	1997	Cysteine 121 is specific to the hepatic enzyme and is localized at a "flexible loop" over the active site cleft of MAT.	Cysteine	0-8	methionine adenosyltransferase 1A	Homo sapiens	115-118
9337154-5	1997	In vivo studies, using wild-type Chinese hamster ovary (CHO) cells and CHO cells stably expressing liver MAT, demonstrate that the inactivation of MAT by H2O2 is specific to the hepatic enzyme, resulting from the modification of the cysteine residue 121, and that this effect is mediated by the generation of the hydroxyl radical.	Hydrogen Peroxide	154-158	methionine adenosyltransferase 1A	Homo sapiens	105-108
9337154-5	1997	In vivo studies, using wild-type Chinese hamster ovary (CHO) cells and CHO cells stably expressing liver MAT, demonstrate that the inactivation of MAT by H2O2 is specific to the hepatic enzyme, resulting from the modification of the cysteine residue 121, and that this effect is mediated by the generation of the hydroxyl radical.	Hydrogen Peroxide	154-158	methionine adenosyltransferase 1A	Homo sapiens	147-150
9337154-5	1997	In vivo studies, using wild-type Chinese hamster ovary (CHO) cells and CHO cells stably expressing liver MAT, demonstrate that the inactivation of MAT by H2O2 is specific to the hepatic enzyme, resulting from the modification of the cysteine residue 121, and that this effect is mediated by the generation of the hydroxyl radical.	Cysteine	233-241	methionine adenosyltransferase 1A	Homo sapiens	105-108
9337154-5	1997	In vivo studies, using wild-type Chinese hamster ovary (CHO) cells and CHO cells stably expressing liver MAT, demonstrate that the inactivation of MAT by H2O2 is specific to the hepatic enzyme, resulting from the modification of the cysteine residue 121, and that this effect is mediated by the generation of the hydroxyl radical.	Cysteine	233-241	methionine adenosyltransferase 1A	Homo sapiens	147-150
9337154-5	1997	In vivo studies, using wild-type Chinese hamster ovary (CHO) cells and CHO cells stably expressing liver MAT, demonstrate that the inactivation of MAT by H2O2 is specific to the hepatic enzyme, resulting from the modification of the cysteine residue 121, and that this effect is mediated by the generation of the hydroxyl radical.	Hydroxyl Radical	313-329	methionine adenosyltransferase 1A	Homo sapiens	105-108
9337154-5	1997	In vivo studies, using wild-type Chinese hamster ovary (CHO) cells and CHO cells stably expressing liver MAT, demonstrate that the inactivation of MAT by H2O2 is specific to the hepatic enzyme, resulting from the modification of the cysteine residue 121, and that this effect is mediated by the generation of the hydroxyl radical.	Hydroxyl Radical	313-329	methionine adenosyltransferase 1A	Homo sapiens	147-150
9337154-6	1997	Our results suggest that H2O2-induced MAT inactivation might be the cause of reduced MAT activity and abnormal methionine metabolism observed in patients with alcoholic liver disease.	Hydrogen Peroxide	25-29	methionine adenosyltransferase 1A	Homo sapiens	38-41
9337154-6	1997	Our results suggest that H2O2-induced MAT inactivation might be the cause of reduced MAT activity and abnormal methionine metabolism observed in patients with alcoholic liver disease.	Hydrogen Peroxide	25-29	methionine adenosyltransferase 1A	Homo sapiens	85-88
9337154-6	1997	Our results suggest that H2O2-induced MAT inactivation might be the cause of reduced MAT activity and abnormal methionine metabolism observed in patients with alcoholic liver disease.	Methionine	111-121	methionine adenosyltransferase 1A	Homo sapiens	38-41
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
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
8903381-3	1996	SAMS isoenzymes differ greatly in kinetic parameters and sensitivity to inhibition by methionine analogs.	Methionine	86-96	methionine adenosyltransferase 1A	Homo sapiens	0-4
8903381-9	1996	As a result of the change in SAMS expression, SAMS activity was higher in HepG2 and HuH-7 cells at physiologically relevant methionine concentrations but lower at high (mmol/L) methionine concentrations than rat hepatocytes.	Methionine	124-134	methionine adenosyltransferase 1A	Homo sapiens	29-33
8903381-9	1996	As a result of the change in SAMS expression, SAMS activity was higher in HepG2 and HuH-7 cells at physiologically relevant methionine concentrations but lower at high (mmol/L) methionine concentrations than rat hepatocytes.	Methionine	124-134	methionine adenosyltransferase 1A	Homo sapiens	46-50
8903381-9	1996	As a result of the change in SAMS expression, SAMS activity was higher in HepG2 and HuH-7 cells at physiologically relevant methionine concentrations but lower at high (mmol/L) methionine concentrations than rat hepatocytes.	Methionine	177-187	methionine adenosyltransferase 1A	Homo sapiens	29-33
8903381-9	1996	As a result of the change in SAMS expression, SAMS activity was higher in HepG2 and HuH-7 cells at physiologically relevant methionine concentrations but lower at high (mmol/L) methionine concentrations than rat hepatocytes.	Methionine	177-187	methionine adenosyltransferase 1A	Homo sapiens	46-50
8903381-10	1996	Treatment with ethionine and seleno-D,L-ethionine, two inhibitors known to have I50 values 50 to 60 times lower against SAMS purified from Novikoff hepatoma cells as compared with SAMS purified from normal rat liver, resulted in increased cell lysis in HepG2 and HuH-7 cells but not cultured rat hepatocytes.	Ethionine	15-24	methionine adenosyltransferase 1A	Homo sapiens	120-124
8903381-10	1996	Treatment with ethionine and seleno-D,L-ethionine, two inhibitors known to have I50 values 50 to 60 times lower against SAMS purified from Novikoff hepatoma cells as compared with SAMS purified from normal rat liver, resulted in increased cell lysis in HepG2 and HuH-7 cells but not cultured rat hepatocytes.	Seleno-D,L-ethionine	29-49	methionine adenosyltransferase 1A	Homo sapiens	120-124
8903381-10	1996	Treatment with ethionine and seleno-D,L-ethionine, two inhibitors known to have I50 values 50 to 60 times lower against SAMS purified from Novikoff hepatoma cells as compared with SAMS purified from normal rat liver, resulted in increased cell lysis in HepG2 and HuH-7 cells but not cultured rat hepatocytes.	Seleno-D,L-ethionine	29-49	methionine adenosyltransferase 1A	Homo sapiens	180-184
8857669-0	1996	Monoclonal antibody MAT-1 against human tyrosinase can detect melanogenic cells on formalin-fixed paraffin-embedded sections.	Formaldehyde	83-91	methionine adenosyltransferase 1A	Homo sapiens	20-25
8857669-0	1996	Monoclonal antibody MAT-1 against human tyrosinase can detect melanogenic cells on formalin-fixed paraffin-embedded sections.	Paraffin	98-106	methionine adenosyltransferase 1A	Homo sapiens	20-25
8624412-1	1996	Two cDNA clones coding for S-adenosyl-L-methionine synthase (SAMs, EC 2.5.1.6) have been isolated from a cDNA library of gibberellic acid-treated unpollinated pea ovaries.	gibberellic acid	121-137	methionine adenosyltransferase 1A	Homo sapiens	27-59
8624412-1	1996	Two cDNA clones coding for S-adenosyl-L-methionine synthase (SAMs, EC 2.5.1.6) have been isolated from a cDNA library of gibberellic acid-treated unpollinated pea ovaries.	gibberellic acid	121-137	methionine adenosyltransferase 1A	Homo sapiens	61-65
9217094-4	1997	The catalytic activity of MAT was increased by 30% in patients compared to controls, with the Vmax for methionine being 17.9 +/- 3.7 and 13.9 +/- 2.2 pmol/mg/h, respectively.	Methionine	103-113	methionine adenosyltransferase 1A	Homo sapiens	26-29
8857669-5	1996	Thus, MoAb MAT-1 could recognize the cells with melanogenic activity on routine formalin-fixed paraffin-embedded sections.	Formaldehyde	80-88	methionine adenosyltransferase 1A	Homo sapiens	11-16
8857669-5	1996	Thus, MoAb MAT-1 could recognize the cells with melanogenic activity on routine formalin-fixed paraffin-embedded sections.	Paraffin	95-103	methionine adenosyltransferase 1A	Homo sapiens	11-16
8857669-7	1996	Nevertheless, MoAb MAT-1 can be expected to be very useful for identifying melanogenic cells on paraffin-embedded sections, because we have to date no other antibody available for it.	Paraffin	96-104	methionine adenosyltransferase 1A	Homo sapiens	19-24
7803470-1	1994	Two peaks of methionine adenosyltransferase (MAT) activity from human erythrocytes were partially purified on a DEAE-cellulose column.	DEAE-Cellulose	112-126	methionine adenosyltransferase 1A	Homo sapiens	13-43
7803470-1	1994	Two peaks of methionine adenosyltransferase (MAT) activity from human erythrocytes were partially purified on a DEAE-cellulose column.	DEAE-Cellulose	112-126	methionine adenosyltransferase 1A	Homo sapiens	45-48
33778193-7	2021	SAMs-NH2 and SAMs-COOH could adsorb Fn efficiently via vdW interactions, electrostatic interactions, hydrogen bonds and salt bridges.	Hydrogen	101-109	methionine adenosyltransferase 1A	Homo sapiens	0-4
8479601-2	1993	Since SAM causes PD-like symptoms in rodents, the decreased efficacy of chronic L-dopa administered to PD patients may result from a rebound increase in SAM via methionine adenosyl transferase (MAT), which produces SAM from methionine and ATP.	Levodopa	80-86	methionine adenosyltransferase 1A	Homo sapiens	161-192
8479601-2	1993	Since SAM causes PD-like symptoms in rodents, the decreased efficacy of chronic L-dopa administered to PD patients may result from a rebound increase in SAM via methionine adenosyl transferase (MAT), which produces SAM from methionine and ATP.	Levodopa	80-86	methionine adenosyltransferase 1A	Homo sapiens	194-197
8479601-2	1993	Since SAM causes PD-like symptoms in rodents, the decreased efficacy of chronic L-dopa administered to PD patients may result from a rebound increase in SAM via methionine adenosyl transferase (MAT), which produces SAM from methionine and ATP.	Methionine	161-171	methionine adenosyltransferase 1A	Homo sapiens	194-197
8479601-2	1993	Since SAM causes PD-like symptoms in rodents, the decreased efficacy of chronic L-dopa administered to PD patients may result from a rebound increase in SAM via methionine adenosyl transferase (MAT), which produces SAM from methionine and ATP.	Adenosine Triphosphate	239-242	methionine adenosyltransferase 1A	Homo sapiens	161-192
8479601-2	1993	Since SAM causes PD-like symptoms in rodents, the decreased efficacy of chronic L-dopa administered to PD patients may result from a rebound increase in SAM via methionine adenosyl transferase (MAT), which produces SAM from methionine and ATP.	Adenosine Triphosphate	239-242	methionine adenosyltransferase 1A	Homo sapiens	194-197
1587846-8	1992	The Km for L-methionine for enzyme from resting peripheral blood mononuclear cells was 19-23 microM, which is 3-8-fold higher than purified MAT from fresh leukemic cells or enzyme from Jurkat cells, both of which have a Km of 3.5-3.8 microM.	Methionine	11-23	methionine adenosyltransferase 1A	Homo sapiens	140-143
7894257-4	1994	The apparent values of MAT Km and Vmax in the parietal cortex were 11.41 +/- 3.51 microM methionine and 25.72 +/- 3.90 nmol/mg protein/h, respectively.	Methionine	89-99	methionine adenosyltransferase 1A	Homo sapiens	23-26
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
33778193-7	2021	SAMs-NH2 and SAMs-COOH could adsorb Fn efficiently via vdW interactions, electrostatic interactions, hydrogen bonds and salt bridges.	Hydrogen	101-109	methionine adenosyltransferase 1A	Homo sapiens	13-17
33778193-9	2021	SAMs-OH showed poor Fn adsorption as the water film.	Water	41-46	methionine adenosyltransferase 1A	Homo sapiens	0-4
3356043-4	1988	SAMs are generated by subjecting attached cells to a shearing force by rinsing with phosphate-buffered saline (PBS).	Phosphate-Buffered Saline	84-109	methionine adenosyltransferase 1A	Homo sapiens	0-4
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	77-80	methionine adenosyltransferase 1A	Homo sapiens	157-166
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	168-171	methionine adenosyltransferase 1A	Homo sapiens	99-104
35612423-16	2022	Our results indicate that the ADH1C/MAT1A axis possibly increases cisplatin resistance in LUAD cells.	Cisplatin	66-75	methionine adenosyltransferase 1A	Homo sapiens	36-41
35483011-0	2022	Liquid Metal Fiber Mat as a Highly Stable Solid-State Junction for Inkjet-Printed Flexible Reference Electrodes.	Metals	7-12	methionine adenosyltransferase 1A	Homo sapiens	19-22
35483011-1	2022	An all-solid liquid-metal-fiber-mat-based membrane flexible reference electrode (LMFM-FRE) was developed by combining liquid metal eutectic gallium indium (EGaIn) and poly(styrene-block-butadiene-block-styrene) (SBS) as a liquid junction layer.	Metals	125-130	methionine adenosyltransferase 1A	Homo sapiens	32-35
35483011-1	2022	An all-solid liquid-metal-fiber-mat-based membrane flexible reference electrode (LMFM-FRE) was developed by combining liquid metal eutectic gallium indium (EGaIn) and poly(styrene-block-butadiene-block-styrene) (SBS) as a liquid junction layer.	gallium indium	140-154	methionine adenosyltransferase 1A	Homo sapiens	32-35
35483011-1	2022	An all-solid liquid-metal-fiber-mat-based membrane flexible reference electrode (LMFM-FRE) was developed by combining liquid metal eutectic gallium indium (EGaIn) and poly(styrene-block-butadiene-block-styrene) (SBS) as a liquid junction layer.	Polystyrenes	167-179	methionine adenosyltransferase 1A	Homo sapiens	32-35
35483011-1	2022	An all-solid liquid-metal-fiber-mat-based membrane flexible reference electrode (LMFM-FRE) was developed by combining liquid metal eutectic gallium indium (EGaIn) and poly(styrene-block-butadiene-block-styrene) (SBS) as a liquid junction layer.	Styrene	202-209	methionine adenosyltransferase 1A	Homo sapiens	32-35
34813297-0	2021	Improved Thermal Stability and Homogeneity of Low Probe Density DNA SAMs Using Potential-Assisted Thiol-Exchange Assembly Methods.	Sulfhydryl Compounds	98-103	methionine adenosyltransferase 1A	Homo sapiens	68-72
34813297-10	2021	The potential-assisted thiol-exchange approach to preparing low-coverage DNA SAMs was shown to quickly create modified surfaces that were consistent, had mobility characteristics which should yield superior DNA hybridization efficiencies, and having greater thermal stability which will translate into a longer shelf-life.	Sulfhydryl Compounds	23-28	methionine adenosyltransferase 1A	Homo sapiens	77-81
35385253-7	2022	Density functional theory predicts that para- and ortho-substituted position SAMs might form a well-ordered structure by improving the SAM"s arrangement and in consequence enhancing its stability on the metal oxide surface.	metal oxide	203-214	methionine adenosyltransferase 1A	Homo sapiens	135-140
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
35091576-2	2022	Lower MATalpha1 activity and mitochondrial dysfunction occur in alcohol-associated liver disease.	Alcohols	64-71	methionine adenosyltransferase 1A	Homo sapiens	6-15
35091576-4	2022	Here, we show that mitochondrial MATalpha1 is selectively depleted in alcohol-associated liver disease through a mechanism that involves the isomerase PIN1 and the kinase CK2.	Alcohols	70-77	methionine adenosyltransferase 1A	Homo sapiens	33-42
35091576-5	2022	Alcohol activates CK2, which phosphorylates MATalpha1 at Ser114 facilitating interaction with PIN1, thereby inhibiting its mitochondrial localization.	Alcohols	0-7	methionine adenosyltransferase 1A	Homo sapiens	44-53
35091576-7	2022	Normally, MATalpha1 interacts with mitochondrial proteins involved in TCA cycle, oxidative phosphorylation, and fatty acid beta-oxidation.	Trichloroacetic Acid	70-73	methionine adenosyltransferase 1A	Homo sapiens	10-19
35091576-7	2022	Normally, MATalpha1 interacts with mitochondrial proteins involved in TCA cycle, oxidative phosphorylation, and fatty acid beta-oxidation.	Fatty Acids	112-122	methionine adenosyltransferase 1A	Homo sapiens	10-19
35091576-9	2022	Our study demonstrates a role of CK2 and PIN1 in reducing mitochondrial MATalpha1 content leading to mitochondrial dysfunction in alcohol-associated liver disease.	Alcohols	130-137	methionine adenosyltransferase 1A	Homo sapiens	72-81
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).	Methionine	15-25	methionine adenosyltransferase 1A	Homo sapiens	99-104
35008908-0	2022	Downregulation of Methionine Cycle Genes MAT1A and GNMT Enriches Protein-Associated Translation Process and Worsens Hepatocellular Carcinoma Prognosis.	Methionine	18-28	methionine adenosyltransferase 1A	Homo sapiens	41-46
35008908-11	2022	This is the first study demonstrated that MAT1A and GNMT, the 2 key enzymes involved in methionine cycle, could attenuate the function of ribosome translation.	Methionine	88-98	methionine adenosyltransferase 1A	Homo sapiens	42-47
3339126-8	1988	This abnormally low rate is due not to a decreased flux through the primarily defective enzyme, MAT, since SAM is produced at an essentially normal rate of 18 mmol/d, but rather to a rate of homocysteine methylation which is abnormally high in the face of the very elevated methionine concentrations demonstrated in this patient.	Homocysteine	191-203	methionine adenosyltransferase 1A	Homo sapiens	96-99
3339126-8	1988	This abnormally low rate is due not to a decreased flux through the primarily defective enzyme, MAT, since SAM is produced at an essentially normal rate of 18 mmol/d, but rather to a rate of homocysteine methylation which is abnormally high in the face of the very elevated methionine concentrations demonstrated in this patient.	Methionine	274-284	methionine adenosyltransferase 1A	Homo sapiens	96-99
3356043-4	1988	SAMs are generated by subjecting attached cells to a shearing force by rinsing with phosphate-buffered saline (PBS).	pbs	111-114	methionine adenosyltransferase 1A	Homo sapiens	0-4
3919220-5	1985	In contrast, full-thickness skin fibroblasts from an elderly patient (AG2261) generate GAG distributions in their L-SAMs (with greatly elevated levels of hyaluronate and chondroitin sulfate) that are very different from those of the cell fractions and from those of AG4449; furthermore, these distributions in AG2261 fractions do not change when shifted from asc- to asc+ medium.	Glycosaminoglycans	87-90	methionine adenosyltransferase 1A	Homo sapiens	116-120
33670854-3	2021	In order to further improve the device characteristics, we have developed a stand alone type of mesa structures (SAMs) of Bi2212 crystals.	bi2212	122-128	methionine adenosyltransferase 1A	Homo sapiens	113-117
33621073-4	2021	The performances of the as-prepared Ru SAMs and HBMs toward H2O2 oxidation were investigated using electrochemical means, kinetic isotope effect (KIE) studies, and Tafel analyses.	Hydrogen Peroxide	60-64	methionine adenosyltransferase 1A	Homo sapiens	39-43
33922430-4	2021	Instead of a complex doping process, the electrical performance can be enhanced by anchoring silane-based SAMs on the IGZO surface.	Silanes	93-99	methionine adenosyltransferase 1A	Homo sapiens	106-110
6689276-3	1983	The mean excretion of SAM sulphate (SAMS) and SAM glucuronide (SAMG) in the urine following oral and rectal administration was 71.3 per cent and 45.6 per cent respectively.	salicylamide	22-25	methionine adenosyltransferase 1A	Homo sapiens	36-40
1150631-1	1975	The proteins precipitated with ammonium sulfate from the urine of a patient (Mat) with multiple myeloma were separated into three components by ion-exchange and gel chromatographies.	Ammonium Sulfate	31-47	methionine adenosyltransferase 1A	Homo sapiens	77-80
1150631-5	1975	This indicates that the monomer of Mat protein contains a cysteinyl residue in the variable region in addition to a cysteinyl residue at the COOH terminus.	lysyl-cysteinyl-cysteinyl-arginyl-cysteinyl-lysine	58-67	methionine adenosyltransferase 1A	Homo sapiens	35-38
1150631-5	1975	This indicates that the monomer of Mat protein contains a cysteinyl residue in the variable region in addition to a cysteinyl residue at the COOH terminus.	lysyl-cysteinyl-cysteinyl-arginyl-cysteinyl-lysine	116-125	methionine adenosyltransferase 1A	Homo sapiens	35-38
1150631-5	1975	This indicates that the monomer of Mat protein contains a cysteinyl residue in the variable region in addition to a cysteinyl residue at the COOH terminus.	Carbonic Acid	141-145	methionine adenosyltransferase 1A	Homo sapiens	35-38
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
32702115-3	2021	RESULTS: Patients with stages III-V CKD stages have significantly decreased urine levels and SAM/S-adenosylhomocysteine ratio and also cysteine/homocysteine ratio in blood plasma (P <.05), compared with patients with stage II CKD.	S-Adenosylhomocysteine	99-119	methionine adenosyltransferase 1A	Homo sapiens	93-98
33231463-1	2020	The thermal stability of thiol based DNA SAMs prepared on gold surfaces is an important parameter that is correlated to sensor lifetime.	Sulfhydryl Compounds	25-30	methionine adenosyltransferase 1A	Homo sapiens	41-45
33273451-6	2020	The conversion of key enzymes of methionine metabolism methionine adenosyltransferase (MAT) 1 A and MAT2A/MAT2B is closely related to fibrosis and hepatocellular carcinoma.	Methionine	33-43	methionine adenosyltransferase 1A	Homo sapiens	55-95
33000151-1	2020	Metabolism of excess methionine (Met) to homocysteine (Hcy) by transmethylation is facilitated by the expression of methionine adenosyltransferase (MAT) I/III and glycine N-methyltransferase (GNMT) in liver, and a lack of either enzyme results in hypermethioninemia despite normal concentrations of MATII and methyltransferases other than GNMT.	Methionine	21-31	methionine adenosyltransferase 1A	Homo sapiens	116-158
33000151-1	2020	Metabolism of excess methionine (Met) to homocysteine (Hcy) by transmethylation is facilitated by the expression of methionine adenosyltransferase (MAT) I/III and glycine N-methyltransferase (GNMT) in liver, and a lack of either enzyme results in hypermethioninemia despite normal concentrations of MATII and methyltransferases other than GNMT.	Homocysteine	41-53	methionine adenosyltransferase 1A	Homo sapiens	116-158
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-Adenosylhomocysteine	90-93	methionine adenosyltransferase 1A	Homo sapiens	145-150
33000151-1	2020	Metabolism of excess methionine (Met) to homocysteine (Hcy) by transmethylation is facilitated by the expression of methionine adenosyltransferase (MAT) I/III and glycine N-methyltransferase (GNMT) in liver, and a lack of either enzyme results in hypermethioninemia despite normal concentrations of MATII and methyltransferases other than GNMT.	Homocysteine	55-58	methionine adenosyltransferase 1A	Homo sapiens	116-158
32649833-3	2020	The corresponding experiments were then carried out to verify the simulation results (The simulations of DhaA on SAMs provided parallel insights into DhaA adsorption in carriers.	Dehydroascorbic Acid	105-109	methionine adenosyltransferase 1A	Homo sapiens	113-117
32649833-3	2020	The corresponding experiments were then carried out to verify the simulation results (The simulations of DhaA on SAMs provided parallel insights into DhaA adsorption in carriers.	Dehydroascorbic Acid	150-154	methionine adenosyltransferase 1A	Homo sapiens	113-117
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
31959915-7	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
31959915-8	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-Adenosylhomocysteine	90-93	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-Adenosylhomocysteine	212-215	methionine adenosyltransferase 1A	Homo sapiens	193-198
31909973-4	2020	p-i-n-type perovskite devices employing these SAMs exhibited power conversion efficiencies surpassing 21%.	perovskite	11-21	methionine adenosyltransferase 1A	Homo sapiens	46-50
32134238-4	2020	The FET devices were systematically functionalized using mixtures of benzenethiol derivatives (4-mercaptobenzoic acid and benzenethiol), which changed the nanostructure of the SAMs formed on gold sensing electrodes.	thiophenol	69-81	methionine adenosyltransferase 1A	Homo sapiens	176-180
32134238-4	2020	The FET devices were systematically functionalized using mixtures of benzenethiol derivatives (4-mercaptobenzoic acid and benzenethiol), which changed the nanostructure of the SAMs formed on gold sensing electrodes.	4-mercaptobenzoate	95-117	methionine adenosyltransferase 1A	Homo sapiens	176-180
32134238-4	2020	The FET devices were systematically functionalized using mixtures of benzenethiol derivatives (4-mercaptobenzoic acid and benzenethiol), which changed the nanostructure of the SAMs formed on gold sensing electrodes.	thiophenol	122-134	methionine adenosyltransferase 1A	Homo sapiens	176-180
32141286-6	2020	Infusing another polymer into the voids between these fibers and subsequently removing the nanofiber template should yield an inverse porous membrane, complementary in pore structure to the original nanofiber mat membrane.	Polymers	17-24	methionine adenosyltransferase 1A	Homo sapiens	209-212
31893227-4	2019	As a proof-of-concept, SAMs composed of n-alkanethiolates and oligophenylenethiolates of different lengths are focused.	esterbut-3	40-57	methionine adenosyltransferase 1A	Homo sapiens	23-27
31851615-2	2020	Among these, the disease caused by methionine adenosyltransferase (MAT) I/III deficiency is the most common, and is characterized by persistent, isolated hypermethioninemia as well as slightly elevated homocysteine.	Homocysteine	202-214	methionine adenosyltransferase 1A	Homo sapiens	35-77
31851615-7	2020	Results and conclusions MAT I/III deficiency is a common reason for Met elevation in neonatal screening by tandem mass spectrometry (MS/MS), which needs long-term follow-up except for these patients with explicitly benign mutations.	Methionine	68-71	methionine adenosyltransferase 1A	Homo sapiens	24-33
31951129-4	2020	Junctions made of SAMs of n-alkanethiolates supported by Au were characterized with both DC and AC techniques, revealing that carbon-paint protective layers provide a solution to three well-know challenges in molecular junctions: series resistance of the leads, poor interface conductance and low effective contact area related to the roughness of the interfaces.	esterbut-3	26-43	methionine adenosyltransferase 1A	Homo sapiens	18-22
31951129-4	2020	Junctions made of SAMs of n-alkanethiolates supported by Au were characterized with both DC and AC techniques, revealing that carbon-paint protective layers provide a solution to three well-know challenges in molecular junctions: series resistance of the leads, poor interface conductance and low effective contact area related to the roughness of the interfaces.	Gold	57-59	methionine adenosyltransferase 1A	Homo sapiens	18-22
31951129-4	2020	Junctions made of SAMs of n-alkanethiolates supported by Au were characterized with both DC and AC techniques, revealing that carbon-paint protective layers provide a solution to three well-know challenges in molecular junctions: series resistance of the leads, poor interface conductance and low effective contact area related to the roughness of the interfaces.	Carbon	126-132	methionine adenosyltransferase 1A	Homo sapiens	18-22
32019203-9	2020	The linear relationships between cathodic and anodic current vs. san rate were obtained for both symmetric and asymmetric SAMs incorporating Co2+ and Cu2+, indicating that oxidized and reduced redox sites are adsorbed on the electrode surface.	Carbon Dioxide	141-145	methionine adenosyltransferase 1A	Homo sapiens	122-126
32019203-9	2020	The linear relationships between cathodic and anodic current vs. san rate were obtained for both symmetric and asymmetric SAMs incorporating Co2+ and Cu2+, indicating that oxidized and reduced redox sites are adsorbed on the electrode surface.	cupric ion	150-154	methionine adenosyltransferase 1A	Homo sapiens	122-126
32019203-13	2020	The detection limits obtained for SAMs incorporating Cu2+, both symmetric and asymmetric, were better in comparison to SAMs incorporating Co2+.	cupric ion	53-57	methionine adenosyltransferase 1A	Homo sapiens	34-38
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
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.	Methionine	10-20	methionine adenosyltransferase 1A	Homo sapiens	204-209
31893227-4	2019	As a proof-of-concept, SAMs composed of n-alkanethiolates and oligophenylenethiolates of different lengths are focused.	oligophenylenethiolates	62-85	methionine adenosyltransferase 1A	Homo sapiens	23-27
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
31077594-11	2019	Mat1a KO hepatocytes had reduced mitochondrial membrane potential and higher mitochondrial reactive oxygen species, both of which were normalized when MAT1A was overexpressed.	Reactive Oxygen Species	91-114	methionine adenosyltransferase 1A	Homo sapiens	0-5
31582217-0	2019	SAHH and SAMS form a methyl donor complex with CCoAOMT7 for methylation of phenolic compounds.	3-O-methyl-alpha-methyldopamine	21-27	methionine adenosyltransferase 1A	Homo sapiens	9-13
31582217-0	2019	SAHH and SAMS form a methyl donor complex with CCoAOMT7 for methylation of phenolic compounds.	phenolic acid	75-83	methionine adenosyltransferase 1A	Homo sapiens	9-13
30861507-6	2019	The alkylsilane SAMs are combined with the silicon oxide substrate to make them hydrophilic, using poly (3, 4-ethylenedioxythiophene)-poly (PEDOT: PSS) as the conductive polymer material.	alkylsilane	4-15	methionine adenosyltransferase 1A	Homo sapiens	16-20
31641591-2	2019	Newborn screening by MS/MS on dried blood spot samples (DBS) has one of its items in methionine levels: the knowledge of this parameter allows the identification of infant affected by homocystinuria (cystathionine beta-synthase, CBS, deficiency) but can also lead, as side effect, to identify cases of methionine adenosyltransferase (MAT) type I/III deficiency.	Methionine	85-95	methionine adenosyltransferase 1A	Homo sapiens	334-337
31600961-4	2019	Transcriptomic profiling of bladder cancer xenograft tumors by RNA-sequencing analysis, before and after relapse, following a 21-day cisplatin/gemcitabine drug treatment regimen identified methionine adenosyltransferase 1a (MAT1A) as one of the significantly upregulated genes following drug treatment.	Cisplatin	133-142	methionine adenosyltransferase 1A	Homo sapiens	189-222
31600961-4	2019	Transcriptomic profiling of bladder cancer xenograft tumors by RNA-sequencing analysis, before and after relapse, following a 21-day cisplatin/gemcitabine drug treatment regimen identified methionine adenosyltransferase 1a (MAT1A) as one of the significantly upregulated genes following drug treatment.	gemcitabine	143-154	methionine adenosyltransferase 1A	Homo sapiens	189-222
31600961-6	2019	Overexpression of MAT1A in 5637 bladder cancer cells increased tolerance to gemcitabine and stalled cell proliferation rates, suggesting MAT1A upregulation as a potential mechanism by which bladder cancer cells persist in a quiescent state to evade chemotherapy.	gemcitabine	76-87	methionine adenosyltransferase 1A	Homo sapiens	18-23
30861507-6	2019	The alkylsilane SAMs are combined with the silicon oxide substrate to make them hydrophilic, using poly (3, 4-ethylenedioxythiophene)-poly (PEDOT: PSS) as the conductive polymer material.	poly (3, 4-ethylenedioxythiophene)-poly	99-138	methionine adenosyltransferase 1A	Homo sapiens	16-20
30861507-6	2019	The alkylsilane SAMs are combined with the silicon oxide substrate to make them hydrophilic, using poly (3, 4-ethylenedioxythiophene)-poly (PEDOT: PSS) as the conductive polymer material.	Polymers	170-177	methionine adenosyltransferase 1A	Homo sapiens	16-20
30300060-0	2019	The Acute Effects of Mat Pilates on Hemodynamic and Salivary Nitrite Responses After Exercise in Postmenopausal Women.	Nitrites	61-68	methionine adenosyltransferase 1A	Homo sapiens	21-24
30189138-0	2018	Application of FRET Microscopy to the Study of the Local Environment and Dynamics of DNA SAMs on Au Electrodes.	Gold	97-99	methionine adenosyltransferase 1A	Homo sapiens	89-93
30785562-7	2019	MAT1-1 idiomorph was identified in CE0311, CE0411 and CE2813 isolates; MAT1-2 idiomorph was found in CE0511 and CE2513 isolates.	ce2813	54-60	methionine adenosyltransferase 1A	Homo sapiens	0-4
30687859-1	2019	Electrochemically driven interfacial halogen bonding between redox-active SAMs and halide anions was quantitatively studied for the first time.	Halogens	37-44	methionine adenosyltransferase 1A	Homo sapiens	74-78
30687859-1	2019	Electrochemically driven interfacial halogen bonding between redox-active SAMs and halide anions was quantitatively studied for the first time.	halide	83-89	methionine adenosyltransferase 1A	Homo sapiens	74-78
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
30189138-5	2018	The DNA SAMs that were studied were composed of a series of mole fraction ratios of alkylthiol-modified DNA which was labeled with either AlexaFluor488 or AlexaFluor647, a FRET donor and acceptor, respectively.	alkylthiol	84-94	methionine adenosyltransferase 1A	Homo sapiens	8-12
31458905-3	2018	The lignin-anchored SAMs were prepared for the first time by click chemistry based on an azide-alkyne Huisgen cycloaddition: mixed SAMs are fabricated on gold thin film using a mixture of alkynyl and methyl thioalkyloligo(ethylene oxide) disulfides and then reacted with azidated milled wood lignins to furnish the functional SAMs anchoring lignins covalently.	Lignin	4-10	methionine adenosyltransferase 1A	Homo sapiens	20-24
30226369-7	2018	Proteomics analysis of Nnmt-interacting proteins in the liver identified Bhmt, Mat1a, and Ahcy, all components of the methionine cycle, and functional experiments showed that mutant Nnmt increased the level of remethylation of homocysteine to SAM.	Methionine	118-128	methionine adenosyltransferase 1A	Homo sapiens	79-84
30226369-7	2018	Proteomics analysis of Nnmt-interacting proteins in the liver identified Bhmt, Mat1a, and Ahcy, all components of the methionine cycle, and functional experiments showed that mutant Nnmt increased the level of remethylation of homocysteine to SAM.	Homocysteine	227-239	methionine adenosyltransferase 1A	Homo sapiens	79-84
30007019-4	2018	In this work, the authors studied the efficiency of the liposome deposition method to form hybrid membranes on octanethiol and hexadecanethiol SAMs in aqueous environment.	hexadecanethiol	127-142	methionine adenosyltransferase 1A	Homo sapiens	143-147
30277764-1	2018	We explore the redox-dependent electronic and structural changes of ferrocene-terminated self-assembled monolayers (Fc SAMs) immersed in aqueous solution.	ferrocene	68-77	methionine adenosyltransferase 1A	Homo sapiens	119-123
30277764-2	2018	By exploiting X-ray and ultraviolet photoelectron spectroscopy combined with an electrochemical cell (EC-XPS/UPS), we can electrochemically control the Fc SAMs and spectroscopically probe the induced changes with the ferrocene/ferrocenium (Fc/Fc+) redox center (Fe oxidation state), formation of 1:1 Fc+-ClO4- ion pairs, molecular orientation, and monolayer thickness.	ferrocene	217-226	methionine adenosyltransferase 1A	Homo sapiens	155-159
30277764-2	2018	By exploiting X-ray and ultraviolet photoelectron spectroscopy combined with an electrochemical cell (EC-XPS/UPS), we can electrochemically control the Fc SAMs and spectroscopically probe the induced changes with the ferrocene/ferrocenium (Fc/Fc+) redox center (Fe oxidation state), formation of 1:1 Fc+-ClO4- ion pairs, molecular orientation, and monolayer thickness.	ferrocenium	227-238	methionine adenosyltransferase 1A	Homo sapiens	155-159
30277764-2	2018	By exploiting X-ray and ultraviolet photoelectron spectroscopy combined with an electrochemical cell (EC-XPS/UPS), we can electrochemically control the Fc SAMs and spectroscopically probe the induced changes with the ferrocene/ferrocenium (Fc/Fc+) redox center (Fe oxidation state), formation of 1:1 Fc+-ClO4- ion pairs, molecular orientation, and monolayer thickness.	Iron	262-264	methionine adenosyltransferase 1A	Homo sapiens	155-159
30277764-2	2018	By exploiting X-ray and ultraviolet photoelectron spectroscopy combined with an electrochemical cell (EC-XPS/UPS), we can electrochemically control the Fc SAMs and spectroscopically probe the induced changes with the ferrocene/ferrocenium (Fc/Fc+) redox center (Fe oxidation state), formation of 1:1 Fc+-ClO4- ion pairs, molecular orientation, and monolayer thickness.	perchlorate	304-308	methionine adenosyltransferase 1A	Homo sapiens	155-159
30277764-4	2018	Electrolyte dependencies could be identified with 0.1 M NaClO4 and HClO4 when probing partially oxidized Fc/Fc+ SAMs.	sodium perchlorate	56-62	methionine adenosyltransferase 1A	Homo sapiens	112-116
30277764-4	2018	Electrolyte dependencies could be identified with 0.1 M NaClO4 and HClO4 when probing partially oxidized Fc/Fc+ SAMs.	Perchloric Acid	67-72	methionine adenosyltransferase 1A	Homo sapiens	112-116
30277764-6	2018	The oxidation to Fc+ is also met with an increase in work function ascribed to the induced negative interfacial dipole caused by the presence of Fc+-ClO4- ion pairs along with a contribution from the reorientation of the Fc+ SAMs.	fc+	17-20	methionine adenosyltransferase 1A	Homo sapiens	225-229
30277764-6	2018	The oxidation to Fc+ is also met with an increase in work function ascribed to the induced negative interfacial dipole caused by the presence of Fc+-ClO4- ion pairs along with a contribution from the reorientation of the Fc+ SAMs.	dipole	112-118	methionine adenosyltransferase 1A	Homo sapiens	225-229
30277764-6	2018	The oxidation to Fc+ is also met with an increase in work function ascribed to the induced negative interfacial dipole caused by the presence of Fc+-ClO4- ion pairs along with a contribution from the reorientation of the Fc+ SAMs.	fc+	145-148	methionine adenosyltransferase 1A	Homo sapiens	225-229
30277764-6	2018	The oxidation to Fc+ is also met with an increase in work function ascribed to the induced negative interfacial dipole caused by the presence of Fc+-ClO4- ion pairs along with a contribution from the reorientation of the Fc+ SAMs.	perchlorate	149-153	methionine adenosyltransferase 1A	Homo sapiens	225-229
31458905-3	2018	The lignin-anchored SAMs were prepared for the first time by click chemistry based on an azide-alkyne Huisgen cycloaddition: mixed SAMs are fabricated on gold thin film using a mixture of alkynyl and methyl thioalkyloligo(ethylene oxide) disulfides and then reacted with azidated milled wood lignins to furnish the functional SAMs anchoring lignins covalently.	Lignin	4-10	methionine adenosyltransferase 1A	Homo sapiens	131-135
31458905-3	2018	The lignin-anchored SAMs were prepared for the first time by click chemistry based on an azide-alkyne Huisgen cycloaddition: mixed SAMs are fabricated on gold thin film using a mixture of alkynyl and methyl thioalkyloligo(ethylene oxide) disulfides and then reacted with azidated milled wood lignins to furnish the functional SAMs anchoring lignins covalently.	Lignin	4-10	methionine adenosyltransferase 1A	Homo sapiens	131-135
31458905-3	2018	The lignin-anchored SAMs were prepared for the first time by click chemistry based on an azide-alkyne Huisgen cycloaddition: mixed SAMs are fabricated on gold thin film using a mixture of alkynyl and methyl thioalkyloligo(ethylene oxide) disulfides and then reacted with azidated milled wood lignins to furnish the functional SAMs anchoring lignins covalently.	azide-alkyne huisgen	89-109	methionine adenosyltransferase 1A	Homo sapiens	20-24
31458905-3	2018	The lignin-anchored SAMs were prepared for the first time by click chemistry based on an azide-alkyne Huisgen cycloaddition: mixed SAMs are fabricated on gold thin film using a mixture of alkynyl and methyl thioalkyloligo(ethylene oxide) disulfides and then reacted with azidated milled wood lignins to furnish the functional SAMs anchoring lignins covalently.	azide-alkyne huisgen	89-109	methionine adenosyltransferase 1A	Homo sapiens	131-135
31458905-3	2018	The lignin-anchored SAMs were prepared for the first time by click chemistry based on an azide-alkyne Huisgen cycloaddition: mixed SAMs are fabricated on gold thin film using a mixture of alkynyl and methyl thioalkyloligo(ethylene oxide) disulfides and then reacted with azidated milled wood lignins to furnish the functional SAMs anchoring lignins covalently.	azide-alkyne huisgen	89-109	methionine adenosyltransferase 1A	Homo sapiens	131-135
31458905-3	2018	The lignin-anchored SAMs were prepared for the first time by click chemistry based on an azide-alkyne Huisgen cycloaddition: mixed SAMs are fabricated on gold thin film using a mixture of alkynyl and methyl thioalkyloligo(ethylene oxide) disulfides and then reacted with azidated milled wood lignins to furnish the functional SAMs anchoring lignins covalently.	and methyl thioalkyloligo(ethylene oxide) disulfides	196-248	methionine adenosyltransferase 1A	Homo sapiens	20-24
31458905-3	2018	The lignin-anchored SAMs were prepared for the first time by click chemistry based on an azide-alkyne Huisgen cycloaddition: mixed SAMs are fabricated on gold thin film using a mixture of alkynyl and methyl thioalkyloligo(ethylene oxide) disulfides and then reacted with azidated milled wood lignins to furnish the functional SAMs anchoring lignins covalently.	and methyl thioalkyloligo(ethylene oxide) disulfides	196-248	methionine adenosyltransferase 1A	Homo sapiens	131-135
31458905-3	2018	The lignin-anchored SAMs were prepared for the first time by click chemistry based on an azide-alkyne Huisgen cycloaddition: mixed SAMs are fabricated on gold thin film using a mixture of alkynyl and methyl thioalkyloligo(ethylene oxide) disulfides and then reacted with azidated milled wood lignins to furnish the functional SAMs anchoring lignins covalently.	and methyl thioalkyloligo(ethylene oxide) disulfides	196-248	methionine adenosyltransferase 1A	Homo sapiens	131-135
31458905-3	2018	The lignin-anchored SAMs were prepared for the first time by click chemistry based on an azide-alkyne Huisgen cycloaddition: mixed SAMs are fabricated on gold thin film using a mixture of alkynyl and methyl thioalkyloligo(ethylene oxide) disulfides and then reacted with azidated milled wood lignins to furnish the functional SAMs anchoring lignins covalently.	Lignin	292-299	methionine adenosyltransferase 1A	Homo sapiens	20-24
31458905-3	2018	The lignin-anchored SAMs were prepared for the first time by click chemistry based on an azide-alkyne Huisgen cycloaddition: mixed SAMs are fabricated on gold thin film using a mixture of alkynyl and methyl thioalkyloligo(ethylene oxide) disulfides and then reacted with azidated milled wood lignins to furnish the functional SAMs anchoring lignins covalently.	Lignin	341-348	methionine adenosyltransferase 1A	Homo sapiens	20-24
31458905-4	2018	The resulting SAMs were characterized using infrared reflection-absorption, Raman, and X-ray photoelectron spectroscopies to confirm covalent immobilization of the lignins to the SAMs via triazole linkages and also to reveal that the SAM formation induces a helical conformation of the ethylene oxide chains.	Lignin	164-171	methionine adenosyltransferase 1A	Homo sapiens	14-18
31458905-4	2018	The resulting SAMs were characterized using infrared reflection-absorption, Raman, and X-ray photoelectron spectroscopies to confirm covalent immobilization of the lignins to the SAMs via triazole linkages and also to reveal that the SAM formation induces a helical conformation of the ethylene oxide chains.	Lignin	164-171	methionine adenosyltransferase 1A	Homo sapiens	179-183
31458905-4	2018	The resulting SAMs were characterized using infrared reflection-absorption, Raman, and X-ray photoelectron spectroscopies to confirm covalent immobilization of the lignins to the SAMs via triazole linkages and also to reveal that the SAM formation induces a helical conformation of the ethylene oxide chains.	Triazoles	188-196	methionine adenosyltransferase 1A	Homo sapiens	179-183
29542320-6	2018	Using VAC for the MOF film growth on gold surfaces modified with thiol SAMs and on a bare silicon surface yielded oriented MOF films, rendering the VAC process robust toward chemical surface variations.	Sulfhydryl Compounds	65-70	methionine adenosyltransferase 1A	Homo sapiens	71-75
30044095-2	2018	Patterned SAMs are formed by delivering gas-phase organotrichlorosilane precursors to a reactive silica surface using a heated glass capillary.	organotrichlorosilane	50-71	methionine adenosyltransferase 1A	Homo sapiens	10-14
30044095-2	2018	Patterned SAMs are formed by delivering gas-phase organotrichlorosilane precursors to a reactive silica surface using a heated glass capillary.	Silicon Dioxide	97-103	methionine adenosyltransferase 1A	Homo sapiens	10-14
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
30146992-3	2018	Medication-assisted treatment or MAT (i.e. methadone, buprenorphine) is the gold standard for treatment of opioid use disorder.	Methadone	43-52	methionine adenosyltransferase 1A	Homo sapiens	33-36
30146992-3	2018	Medication-assisted treatment or MAT (i.e. methadone, buprenorphine) is the gold standard for treatment of opioid use disorder.	Buprenorphine	54-67	methionine adenosyltransferase 1A	Homo sapiens	33-36
28917731-3	2018	Herein, we studied the influence of chain length of n-alkanethiols SAMs on the immunoreaction kinetics employing attenuated total reflection surface-enhanced infrared absorption spectroscopy (ATR-SEIRAS).	n-alkanethiols	52-66	methionine adenosyltransferase 1A	Homo sapiens	67-71
29191423-6	2018	The anodic and cathodic peak potentials of Cyt c/CS-MPA-AuNPs/SAMs-Au electrode were at 0.006V and -0.043V (vs. Ag/AgCl), respectively.	Chitosan	49-51	methionine adenosyltransferase 1A	Homo sapiens	62-66
29191423-6	2018	The anodic and cathodic peak potentials of Cyt c/CS-MPA-AuNPs/SAMs-Au electrode were at 0.006V and -0.043V (vs. Ag/AgCl), respectively.	aunps	56-61	methionine adenosyltransferase 1A	Homo sapiens	62-66
28574708-1	2018	Self-assembled monolayers of n-octadecylamine (ODA-SAMs) on mica have been prepared and studied by contact and jumping mode atomic force microscopy (AFM).	stearylamine	29-45	methionine adenosyltransferase 1A	Homo sapiens	51-55
28917731-4	2018	Antibody (rabbit immunoglobulin) is assembled on carboxyl terminated SAMs of n-alkanethiols with different chain lengths (n = 3, 6, 11, 16).	n-alkanethiols	77-91	methionine adenosyltransferase 1A	Homo sapiens	69-73
28813143-5	2017	For this purpose, we have constructed transistors based on SAMs of two molecules that consist of the organic p-type semiconductor benzothieno[3,2-b][1]benzothiophene (BTBT), linked to a C11 or C12 alkylphosphonic acid.	benzothieno[3,2-b][1]benzothiophene	130-165	methionine adenosyltransferase 1A	Homo sapiens	59-63
29022887-0	2017	Delocalized versus localized excitations in the photoisomerization of azobenzene-functionalized alkanethiolate SAMs.	azobenzene	70-80	methionine adenosyltransferase 1A	Homo sapiens	111-115
28441494-0	2017	Role of the Reducing Agent in the Electroless Deposition of Copper on Functionalized SAMs.	Copper	60-66	methionine adenosyltransferase 1A	Homo sapiens	85-89
28441494-4	2017	We have investigated the role of amine borane reducing agents in the electroless deposition of copper on -CH3-, -OH-, and -COOH-terminated SAMs adsorbed on gold using time-of-flight secondary ion mass spectrometry, optical microscopy, and complementary MP2 calculations.	amine borane	33-45	methionine adenosyltransferase 1A	Homo sapiens	139-143
28441494-4	2017	We have investigated the role of amine borane reducing agents in the electroless deposition of copper on -CH3-, -OH-, and -COOH-terminated SAMs adsorbed on gold using time-of-flight secondary ion mass spectrometry, optical microscopy, and complementary MP2 calculations.	Copper	95-101	methionine adenosyltransferase 1A	Homo sapiens	139-143
28441494-4	2017	We have investigated the role of amine borane reducing agents in the electroless deposition of copper on -CH3-, -OH-, and -COOH-terminated SAMs adsorbed on gold using time-of-flight secondary ion mass spectrometry, optical microscopy, and complementary MP2 calculations.	Carbonic Acid	123-127	methionine adenosyltransferase 1A	Homo sapiens	139-143
28441494-6	2017	At pH &gt;9, -COOH-terminated SAMs form copper-carboxylate complexes, which serve as nucleation sites for subsequent copper deposition.	Carbonic Acid	14-18	methionine adenosyltransferase 1A	Homo sapiens	30-34
28441494-6	2017	At pH &gt;9, -COOH-terminated SAMs form copper-carboxylate complexes, which serve as nucleation sites for subsequent copper deposition.	copper-carboxylate	40-58	methionine adenosyltransferase 1A	Homo sapiens	30-34
28441494-6	2017	At pH &gt;9, -COOH-terminated SAMs form copper-carboxylate complexes, which serve as nucleation sites for subsequent copper deposition.	Copper	40-46	methionine adenosyltransferase 1A	Homo sapiens	30-34
28441494-9	2017	However, in contrast to -COOH-terminated SAMs, copper deposition does not begin immediately.	Carbonic Acid	25-29	methionine adenosyltransferase 1A	Homo sapiens	41-45
28441494-10	2017	If the terminal group contains polar bonds, such as the C-OH bond of -OH-terminated SAMs, deposition is dominated by the interaction of the reducing agent with the terminal group rather than the relative bond strengths of the amine borane reducing agents.	amine borane	226-238	methionine adenosyltransferase 1A	Homo sapiens	84-88
28531650-4	2017	Orientation of the molecular perylene cores primarily governs the molecular orientation in the SAMs by pi-pi interaction of the molecule-substrate through uttermost matching the graphite surface lattice.	Perylene	29-37	methionine adenosyltransferase 1A	Homo sapiens	95-99
28531650-4	2017	Orientation of the molecular perylene cores primarily governs the molecular orientation in the SAMs by pi-pi interaction of the molecule-substrate through uttermost matching the graphite surface lattice.	Graphite	178-186	methionine adenosyltransferase 1A	Homo sapiens	95-99
28813143-5	2017	For this purpose, we have constructed transistors based on SAMs of two molecules that consist of the organic p-type semiconductor benzothieno[3,2-b][1]benzothiophene (BTBT), linked to a C11 or C12 alkylphosphonic acid.	btbt	167-171	methionine adenosyltransferase 1A	Homo sapiens	59-63
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
27523488-2	2016	But the nanoscale aspects of the rich microscopic kinetics of this reaction may remain hidden due to ensemble-averaging in colloidal samples, which is why we investigated in real-time how alkanethiol SAMs form on a single Ag nanoparticle.	alkanethiol	188-199	methionine adenosyltransferase 1A	Homo sapiens	200-204
28530270-1	2017	In this study, we have employed dual-color photoelectron emission microscopy (2P-PEEM) to visualize surface plasmon polaritons (SPPs) propagating along a chemically modified organic/metal interface of alkanethiolate self-assembled monolayers (Cn-SAMs; n is the number of alkyl carbon atoms) formed on Au(111).	alkanethiolate	201-215	methionine adenosyltransferase 1A	Homo sapiens	246-250
28530270-2	2017	In dual-color 2P-PEEM, near-infrared photons around 900 nm generate SPPs at the Cn-SAMs/Au(111) interface, which interfere with the remaining light field.	Gold	88-90	methionine adenosyltransferase 1A	Homo sapiens	83-87
28530270-4	2017	Through dual-color 2P-PEEM for various alkyl chain lengths of Cn-SAMs, it is revealed that SPP properties are largely modified by an interfacial electronic state, particularly formed by the chemical interaction between surface Au atoms and adsorbate thiol molecules, thereby allowing the quantification of their group velocity at ~0.86 times the speed of light.	N-succinimidyl 4-(2-pyridyldithio)pentanoate	91-94	methionine adenosyltransferase 1A	Homo sapiens	65-69
28530270-4	2017	Through dual-color 2P-PEEM for various alkyl chain lengths of Cn-SAMs, it is revealed that SPP properties are largely modified by an interfacial electronic state, particularly formed by the chemical interaction between surface Au atoms and adsorbate thiol molecules, thereby allowing the quantification of their group velocity at ~0.86 times the speed of light.	Sulfhydryl Compounds	250-255	methionine adenosyltransferase 1A	Homo sapiens	65-69
29387085-0	2017	Preparation and Anticorrosion of Octadecyl Trichlorosilane SAMs for Copper Surface.	Copper	68-74	methionine adenosyltransferase 1A	Homo sapiens	59-63
29387085-3	2017	The results showed that OTS SAMs exhibit the better corrosion resistance; the corrosion potential of copper OTS SAMs protection increased by about 1.02 V, while the corrosion current density decreased to 0.59 muA/cm2.	Copper	101-107	methionine adenosyltransferase 1A	Homo sapiens	28-32
29387085-3	2017	The results showed that OTS SAMs exhibit the better corrosion resistance; the corrosion potential of copper OTS SAMs protection increased by about 1.02 V, while the corrosion current density decreased to 0.59 muA/cm2.	Copper	101-107	methionine adenosyltransferase 1A	Homo sapiens	112-116
27539781-3	2016	Glass surfaces have been functionalized with pyridine-terminated SAMs and subsequently with multilayers of macrocycles through layer-by-layer self assembly.	pyridine	45-53	methionine adenosyltransferase 1A	Homo sapiens	65-69
28340533-1	2017	We show that 4"-nitro-1,1"-biphenyl-4-thiol self-assembled monolayers (NBPT SAMs) on gold can be exchanged with 11-(mercaptoundecyl)triethylene glycol (C11EG3OH) SAMs via vapor deposition (VD).	SCHEMBL1847802	13-43	methionine adenosyltransferase 1A	Homo sapiens	76-80
28340533-1	2017	We show that 4"-nitro-1,1"-biphenyl-4-thiol self-assembled monolayers (NBPT SAMs) on gold can be exchanged with 11-(mercaptoundecyl)triethylene glycol (C11EG3OH) SAMs via vapor deposition (VD).	SCHEMBL1847802	13-43	methionine adenosyltransferase 1A	Homo sapiens	162-166
28340533-1	2017	We show that 4"-nitro-1,1"-biphenyl-4-thiol self-assembled monolayers (NBPT SAMs) on gold can be exchanged with 11-(mercaptoundecyl)triethylene glycol (C11EG3OH) SAMs via vapor deposition (VD).	11-(mercaptoundecyl)triethylene glycol	112-150	methionine adenosyltransferase 1A	Homo sapiens	76-80
28340533-1	2017	We show that 4"-nitro-1,1"-biphenyl-4-thiol self-assembled monolayers (NBPT SAMs) on gold can be exchanged with 11-(mercaptoundecyl)triethylene glycol (C11EG3OH) SAMs via vapor deposition (VD).	11-(mercaptoundecyl)triethylene glycol	112-150	methionine adenosyltransferase 1A	Homo sapiens	162-166
28340533-1	2017	We show that 4"-nitro-1,1"-biphenyl-4-thiol self-assembled monolayers (NBPT SAMs) on gold can be exchanged with 11-(mercaptoundecyl)triethylene glycol (C11EG3OH) SAMs via vapor deposition (VD).	c11eg3oh	152-160	methionine adenosyltransferase 1A	Homo sapiens	76-80
28337758-3	2017	MAT-I/III activity is stimulated by Met, but inhibited by S-nitrosoglutathione, and the methylation index (MI) increases after Met stimulation of L02 cells.	S-Nitrosoglutathione	58-78	methionine adenosyltransferase 1A	Homo sapiens	0-9
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
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
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.	Racemethionine	193-199	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.	Racemethionine	193-199	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.	alpha-hydroxy-gamma-methylmercaptobutyric acid	203-206	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.	alpha-hydroxy-gamma-methylmercaptobutyric acid	203-206	methionine adenosyltransferase 1A	Homo sapiens	42-47
26992370-2	2016	Poly[2-methacryloyloxyethyl phosphorylcholine (MPC)-ran-N-methacryloyl-(l)-tyrosinemethylester (MAT)] (P(MPC/MAT)) was synthesized by conventional radical polymerization, with the MAT units capable of being oxidized by 254nm UV irradiation.	2-methacryloyloxyethyl phosphorylcholine	47-50	methionine adenosyltransferase 1A	Homo sapiens	109-112
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
26992370-2	2016	Poly[2-methacryloyloxyethyl phosphorylcholine (MPC)-ran-N-methacryloyl-(l)-tyrosinemethylester (MAT)] (P(MPC/MAT)) was synthesized by conventional radical polymerization, with the MAT units capable of being oxidized by 254nm UV irradiation.	poly(2-methacryloyloxyethyl-phosphorylcholine)	0-45	methionine adenosyltransferase 1A	Homo sapiens	96-99
26992370-2	2016	Poly[2-methacryloyloxyethyl phosphorylcholine (MPC)-ran-N-methacryloyl-(l)-tyrosinemethylester (MAT)] (P(MPC/MAT)) was synthesized by conventional radical polymerization, with the MAT units capable of being oxidized by 254nm UV irradiation.	poly(2-methacryloyloxyethyl-phosphorylcholine)	0-45	methionine adenosyltransferase 1A	Homo sapiens	103-112
26992370-2	2016	Poly[2-methacryloyloxyethyl phosphorylcholine (MPC)-ran-N-methacryloyl-(l)-tyrosinemethylester (MAT)] (P(MPC/MAT)) was synthesized by conventional radical polymerization, with the MAT units capable of being oxidized by 254nm UV irradiation.	poly(2-methacryloyloxyethyl-phosphorylcholine)	0-45	methionine adenosyltransferase 1A	Homo sapiens	109-112
26992370-2	2016	Poly[2-methacryloyloxyethyl phosphorylcholine (MPC)-ran-N-methacryloyl-(l)-tyrosinemethylester (MAT)] (P(MPC/MAT)) was synthesized by conventional radical polymerization, with the MAT units capable of being oxidized by 254nm UV irradiation.	2-methacryloyloxyethyl phosphorylcholine	47-50	methionine adenosyltransferase 1A	Homo sapiens	96-99
26992370-2	2016	Poly[2-methacryloyloxyethyl phosphorylcholine (MPC)-ran-N-methacryloyl-(l)-tyrosinemethylester (MAT)] (P(MPC/MAT)) was synthesized by conventional radical polymerization, with the MAT units capable of being oxidized by 254nm UV irradiation.	2-methacryloyloxyethyl phosphorylcholine	47-50	methionine adenosyltransferase 1A	Homo sapiens	103-112
26992370-2	2016	Poly[2-methacryloyloxyethyl phosphorylcholine (MPC)-ran-N-methacryloyl-(l)-tyrosinemethylester (MAT)] (P(MPC/MAT)) was synthesized by conventional radical polymerization, with the MAT units capable of being oxidized by 254nm UV irradiation.	-n-methacryloyl-(l)-tyrosinemethylester	55-94	methionine adenosyltransferase 1A	Homo sapiens	96-99
26992370-2	2016	Poly[2-methacryloyloxyethyl phosphorylcholine (MPC)-ran-N-methacryloyl-(l)-tyrosinemethylester (MAT)] (P(MPC/MAT)) was synthesized by conventional radical polymerization, with the MAT units capable of being oxidized by 254nm UV irradiation.	-n-methacryloyl-(l)-tyrosinemethylester	55-94	methionine adenosyltransferase 1A	Homo sapiens	103-112
26992370-4	2016	A silicon wafer was subjected to surface modification through spin coating of P(MPC/MAT) from an aqueous solution for use as a model substrate.	Silicon	2-9	methionine adenosyltransferase 1A	Homo sapiens	78-87
26992370-6	2016	The thickness of the polymer layers formed on the Si wafers was influenced by various parameters such as polymer concentration, UV irradiation time, and composition of the MAT units in P(MPC/MAT).	Polymers	21-28	methionine adenosyltransferase 1A	Homo sapiens	172-175
26992370-6	2016	The thickness of the polymer layers formed on the Si wafers was influenced by various parameters such as polymer concentration, UV irradiation time, and composition of the MAT units in P(MPC/MAT).	Polymers	21-28	methionine adenosyltransferase 1A	Homo sapiens	185-194
26992370-6	2016	The thickness of the polymer layers formed on the Si wafers was influenced by various parameters such as polymer concentration, UV irradiation time, and composition of the MAT units in P(MPC/MAT).	Silicon	50-52	methionine adenosyltransferase 1A	Homo sapiens	172-175
26992370-6	2016	The thickness of the polymer layers formed on the Si wafers was influenced by various parameters such as polymer concentration, UV irradiation time, and composition of the MAT units in P(MPC/MAT).	Silicon	50-52	methionine adenosyltransferase 1A	Homo sapiens	185-194
26992370-7	2016	Oxidized MAT units were advantageous not only for polymer adhesion to a solid surface but also for protein conjugation with the adhered polymers.	Polymers	50-57	methionine adenosyltransferase 1A	Homo sapiens	9-12
26992370-7	2016	Oxidized MAT units were advantageous not only for polymer adhesion to a solid surface but also for protein conjugation with the adhered polymers.	Polymers	136-144	methionine adenosyltransferase 1A	Homo sapiens	9-12
26992370-9	2016	Furthermore, it was confirmed that protein immobilization on the polymer occurred through the oxidized MAT units because the protein adsorption was significantly reduced upon blocking these units through pretreatment with glycine.	Glycine	222-229	methionine adenosyltransferase 1A	Homo sapiens	103-106
27134014-3	2016	After hydrolysis, the mixed SAMs exhibit behaviors from antimicrobial to antifouling, since the COOCH3-thiols were translated into carboxylic acid (COO(-)-) terminated thiols, which carried a net charge of -1 e. Simulation results showed that the main differences between COOCH3-/N(CH3)3(+)-SAM and COO(-)-/N(CH3)3(+)-SAM are the charged property and the hydration layer above the surface.	cooch3-thiols	96-109	methionine adenosyltransferase 1A	Homo sapiens	28-32
27134014-3	2016	After hydrolysis, the mixed SAMs exhibit behaviors from antimicrobial to antifouling, since the COOCH3-thiols were translated into carboxylic acid (COO(-)-) terminated thiols, which carried a net charge of -1 e. Simulation results showed that the main differences between COOCH3-/N(CH3)3(+)-SAM and COO(-)-/N(CH3)3(+)-SAM are the charged property and the hydration layer above the surface.	Carboxylic Acids	131-146	methionine adenosyltransferase 1A	Homo sapiens	28-32
27134014-3	2016	After hydrolysis, the mixed SAMs exhibit behaviors from antimicrobial to antifouling, since the COOCH3-thiols were translated into carboxylic acid (COO(-)-) terminated thiols, which carried a net charge of -1 e. Simulation results showed that the main differences between COOCH3-/N(CH3)3(+)-SAM and COO(-)-/N(CH3)3(+)-SAM are the charged property and the hydration layer above the surface.	carboxyl radical	148-156	methionine adenosyltransferase 1A	Homo sapiens	28-32
27134014-3	2016	After hydrolysis, the mixed SAMs exhibit behaviors from antimicrobial to antifouling, since the COOCH3-thiols were translated into carboxylic acid (COO(-)-) terminated thiols, which carried a net charge of -1 e. Simulation results showed that the main differences between COOCH3-/N(CH3)3(+)-SAM and COO(-)-/N(CH3)3(+)-SAM are the charged property and the hydration layer above the surface.	Sulfhydryl Compounds	103-109	methionine adenosyltransferase 1A	Homo sapiens	28-32
27134014-3	2016	After hydrolysis, the mixed SAMs exhibit behaviors from antimicrobial to antifouling, since the COOCH3-thiols were translated into carboxylic acid (COO(-)-) terminated thiols, which carried a net charge of -1 e. Simulation results showed that the main differences between COOCH3-/N(CH3)3(+)-SAM and COO(-)-/N(CH3)3(+)-SAM are the charged property and the hydration layer above the surface.	cooch3-	96-103	methionine adenosyltransferase 1A	Homo sapiens	28-32
27134014-3	2016	After hydrolysis, the mixed SAMs exhibit behaviors from antimicrobial to antifouling, since the COOCH3-thiols were translated into carboxylic acid (COO(-)-) terminated thiols, which carried a net charge of -1 e. Simulation results showed that the main differences between COOCH3-/N(CH3)3(+)-SAM and COO(-)-/N(CH3)3(+)-SAM are the charged property and the hydration layer above the surface.	n(ch3)3(+)-sam	280-294	methionine adenosyltransferase 1A	Homo sapiens	28-32
27134014-3	2016	After hydrolysis, the mixed SAMs exhibit behaviors from antimicrobial to antifouling, since the COOCH3-thiols were translated into carboxylic acid (COO(-)-) terminated thiols, which carried a net charge of -1 e. Simulation results showed that the main differences between COOCH3-/N(CH3)3(+)-SAM and COO(-)-/N(CH3)3(+)-SAM are the charged property and the hydration layer above the surface.	carboxyl radical	148-155	methionine adenosyltransferase 1A	Homo sapiens	28-32
27134014-3	2016	After hydrolysis, the mixed SAMs exhibit behaviors from antimicrobial to antifouling, since the COOCH3-thiols were translated into carboxylic acid (COO(-)-) terminated thiols, which carried a net charge of -1 e. Simulation results showed that the main differences between COOCH3-/N(CH3)3(+)-SAM and COO(-)-/N(CH3)3(+)-SAM are the charged property and the hydration layer above the surface.	n(ch3)3(+)-sam	307-321	methionine adenosyltransferase 1A	Homo sapiens	28-32
27134014-14	2016	The mixed SAMs, constructed from a 1:1 combination of COOCH3- and N(CH3)3(+)-terminated thiols, can induce protein adsorption mainly through the electrostatic interaction.	Nitrogen	66-67	methionine adenosyltransferase 1A	Homo sapiens	10-14
27134014-14	2016	The mixed SAMs, constructed from a 1:1 combination of COOCH3- and N(CH3)3(+)-terminated thiols, can induce protein adsorption mainly through the electrostatic interaction.	Sulfhydryl Compounds	88-94	methionine adenosyltransferase 1A	Homo sapiens	10-14
27134014-15	2016	When the COOCH3-terminated thiols were hydrolyzed to negatively charged COO(-)-terminated thiols, the mixed-charged SAMs switched from antimicrobial to antifouling.	cooch3	9-15	methionine adenosyltransferase 1A	Homo sapiens	116-120
27134014-15	2016	When the COOCH3-terminated thiols were hydrolyzed to negatively charged COO(-)-terminated thiols, the mixed-charged SAMs switched from antimicrobial to antifouling.	Sulfhydryl Compounds	27-33	methionine adenosyltransferase 1A	Homo sapiens	116-120
27134014-15	2016	When the COOCH3-terminated thiols were hydrolyzed to negatively charged COO(-)-terminated thiols, the mixed-charged SAMs switched from antimicrobial to antifouling.	carboxyl radical	72-78	methionine adenosyltransferase 1A	Homo sapiens	116-120
27134014-15	2016	When the COOCH3-terminated thiols were hydrolyzed to negatively charged COO(-)-terminated thiols, the mixed-charged SAMs switched from antimicrobial to antifouling.	Sulfhydryl Compounds	90-96	methionine adenosyltransferase 1A	Homo sapiens	116-120
30226952-2	2016	In this study, through detailed investigations and analyses, it was confirmed that the introduction of technology and knowledge on streptomycin was strongly supported by Brigadier General CRAWFORD SAms, the chief of the Public Health and Welfare Section (PHW) of the Supreme Commander for Allied Powers/General Headquarters, via the Ministry of Welfare in Japan.	Streptomycin	131-143	methionine adenosyltransferase 1A	Homo sapiens	197-201
28660047-4	2016	We also found that the DNA-SAMs on gold substrates could be used as a potentially universal cell culture substrate, which showed properties similar to cationic polymers (e.g. poly-l lysine, PLL) substrates.	Polymers	160-168	methionine adenosyltransferase 1A	Homo sapiens	27-31
27268402-6	2016	By combining this method with an ex situ determination of the effective thickness of the resulting layers via ellipsometry, we observe a large difference of the permittivity (1 kHz) of the examined aminosilanes in the liquid state (epsilonliquid = 5.5-8.8) and in SAMs (epsilonSAM = 22-52, electric field in the plane of the layer).	aminosilanes	198-210	methionine adenosyltransferase 1A	Homo sapiens	264-268
27109872-6	2016	Our results show that it is possible to improve stability and optimum coverage of alkyl functionalized SAMs linked through a direct Si-C bond by incorporating alkyl chains linked to Si through a different linker group, while preserving the interface electronic structure that determines key electronic properties.	Silicon	132-134	methionine adenosyltransferase 1A	Homo sapiens	103-107
27109872-6	2016	Our results show that it is possible to improve stability and optimum coverage of alkyl functionalized SAMs linked through a direct Si-C bond by incorporating alkyl chains linked to Si through a different linker group, while preserving the interface electronic structure that determines key electronic properties.	Carbon	135-136	methionine adenosyltransferase 1A	Homo sapiens	103-107
27109872-6	2016	Our results show that it is possible to improve stability and optimum coverage of alkyl functionalized SAMs linked through a direct Si-C bond by incorporating alkyl chains linked to Si through a different linker group, while preserving the interface electronic structure that determines key electronic properties.	Silicon	182-184	methionine adenosyltransferase 1A	Homo sapiens	103-107
28660047-4	2016	We also found that the DNA-SAMs on gold substrates could be used as a potentially universal cell culture substrate, which showed properties similar to cationic polymers (e.g. poly-l lysine, PLL) substrates.	poly-l lysine	175-188	methionine adenosyltransferase 1A	Homo sapiens	27-31
26980271-5	2016	One is similar to that characterized in the experiments for Cyt-c adsorbed on the NH2-SAMs, in which the heme group points far away from the surface.	Heme	105-109	methionine adenosyltransferase 1A	Homo sapiens	86-90
26618274-2	2016	The SAMs are formed on graphene via noncovalent bonds without altering the structure of the graphene.	Graphite	23-31	methionine adenosyltransferase 1A	Homo sapiens	4-8
27109872-3	2016	In this paper we study the H:Si(111) surface functionalized with binary SAMs: these are composed of alkyl chains that are linked to the surface by two different linker groups.	Silicon	29-31	methionine adenosyltransferase 1A	Homo sapiens	72-76
26870989-0	2016	Orbital dependent ultrafast charge transfer dynamics of ferrocenyl-functionalized SAMs on gold studied by core-hole clock spectroscopy.	ferrocenyl	56-66	methionine adenosyltransferase 1A	Homo sapiens	82-86
26583377-2	2016	Ile-Gly-Asp-Gln-(IGDQ)-exposing SAMs sustain the adhesion of MDA-MB-231 cells by triggering focal adhesion kinase phosphorylation, similarly to the analogous Gly-Arg-Gly-Asp-(GRGD)-terminating surfaces.	ile-gly-asp-gln	0-15	methionine adenosyltransferase 1A	Homo sapiens	32-36
26583377-2	2016	Ile-Gly-Asp-Gln-(IGDQ)-exposing SAMs sustain the adhesion of MDA-MB-231 cells by triggering focal adhesion kinase phosphorylation, similarly to the analogous Gly-Arg-Gly-Asp-(GRGD)-terminating surfaces.	glycyl-arginyl-glycyl-aspartic acid	158-173	methionine adenosyltransferase 1A	Homo sapiens	32-36
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).	Methionine	41-51	methionine adenosyltransferase 1A	Homo sapiens	0-5
26579883-5	2015	The interfacial properties of SAMs can be menu-selected by choice of adsorbate structure using omega-terminated thiols on gold surfaces as a convenient system for studying and utilizing these properties.	Sulfhydryl Compounds	112-118	methionine adenosyltransferase 1A	Homo sapiens	30-34
26579883-8	2015	With regard to the first category, we analyze the impact of permanent dipoles on the wettability of alkanethiolate SAMs generated from adsorbates possessing well-defined transitions between terminal fluorocarbon and underlying hydrocarbon chain segments.	Fluorocarbons	199-211	methionine adenosyltransferase 1A	Homo sapiens	115-119
26579883-9	2015	The second category covers recent reports of light-responsive SAMs formed from azobenzene-based adsorbates.	azobenzene	79-89	methionine adenosyltransferase 1A	Homo sapiens	62-66
26579883-11	2015	Our analysis of the SAMs formed from these carefully crafted adsorbates encompassing several series of fluorocarbon-containing thiols provides support for a conclusion that oriented surface dipoles exert a significant influence on interfacial energetics and wettability.	Fluorocarbons	103-115	methionine adenosyltransferase 1A	Homo sapiens	20-24
26579883-11	2015	Our analysis of the SAMs formed from these carefully crafted adsorbates encompassing several series of fluorocarbon-containing thiols provides support for a conclusion that oriented surface dipoles exert a significant influence on interfacial energetics and wettability.	Sulfhydryl Compounds	127-133	methionine adenosyltransferase 1A	Homo sapiens	20-24
26565476-1	2015	By combining molecular dynamics simulations and quantum mechanics calculations, we show the formation of a composite structure composed of embedded water molecules and the COOH matrix on carboxyl-terminated self-assembled monolayers (COOH SAMs) with appropriate packing densities.	Water	148-153	methionine adenosyltransferase 1A	Homo sapiens	239-243
26565476-1	2015	By combining molecular dynamics simulations and quantum mechanics calculations, we show the formation of a composite structure composed of embedded water molecules and the COOH matrix on carboxyl-terminated self-assembled monolayers (COOH SAMs) with appropriate packing densities.	Carbonic Acid	172-176	methionine adenosyltransferase 1A	Homo sapiens	239-243
26565476-1	2015	By combining molecular dynamics simulations and quantum mechanics calculations, we show the formation of a composite structure composed of embedded water molecules and the COOH matrix on carboxyl-terminated self-assembled monolayers (COOH SAMs) with appropriate packing densities.	Carbonic Acid	234-238	methionine adenosyltransferase 1A	Homo sapiens	239-243
26565476-3	2015	This explains the seeming contradiction on the stability of the surface water on COOH SAMs observed in experiments.	Water	72-77	methionine adenosyltransferase 1A	Homo sapiens	86-90
26565476-3	2015	This explains the seeming contradiction on the stability of the surface water on COOH SAMs observed in experiments.	Carbonic Acid	81-85	methionine adenosyltransferase 1A	Homo sapiens	86-90
26565476-4	2015	The existence of the composite structure at appropriate packing densities results in the two-step distribution of contact angles of water droplets on COOH SAMs, around 0  and 35 , which compares favorably to the experimental measurements of contact angles collected from forty research articles over the past 25 years.	Water	132-137	methionine adenosyltransferase 1A	Homo sapiens	155-159
26565476-4	2015	The existence of the composite structure at appropriate packing densities results in the two-step distribution of contact angles of water droplets on COOH SAMs, around 0  and 35 , which compares favorably to the experimental measurements of contact angles collected from forty research articles over the past 25 years.	Carbonic Acid	150-154	methionine adenosyltransferase 1A	Homo sapiens	155-159
26592257-3	2015	The mixed SAMs were formed by immersing AuNPs in a mixed alkanethiol solution at different molar ratios.	alkanethiol	57-68	methionine adenosyltransferase 1A	Homo sapiens	10-14
26592257-6	2015	The surface coverage of the colloidal films increased by forming equimolar or dodecanethiolate-dominant mixed SAMs on AuNPs instead of a pure dodecanethiolate or octadecanethiolate SAM.	dodecanethiolate	78-94	methionine adenosyltransferase 1A	Homo sapiens	110-114
26592257-8	2015	This improvement is attributed to the high dispersion stability of AuNPs covered with equimolar or dodecanethiolate-dominant mixed SAMs.	dodecanethiolate	99-115	methionine adenosyltransferase 1A	Homo sapiens	131-135
26597057-2	2015	In this study, we performed an atomistic molecular dynamics (MD) simulation in combination with free-energy calculations to study the morphology of azobenzene-terminated SAMs (Azo-SAMs) grafted on a silica substrate and their interactions with lysozyme.	azobenzene	148-158	methionine adenosyltransferase 1A	Homo sapiens	170-174
26597057-2	2015	In this study, we performed an atomistic molecular dynamics (MD) simulation in combination with free-energy calculations to study the morphology of azobenzene-terminated SAMs (Azo-SAMs) grafted on a silica substrate and their interactions with lysozyme.	azobenzene	148-158	methionine adenosyltransferase 1A	Homo sapiens	180-184
26597057-2	2015	In this study, we performed an atomistic molecular dynamics (MD) simulation in combination with free-energy calculations to study the morphology of azobenzene-terminated SAMs (Azo-SAMs) grafted on a silica substrate and their interactions with lysozyme.	Silicon Dioxide	199-205	methionine adenosyltransferase 1A	Homo sapiens	170-174
26597057-2	2015	In this study, we performed an atomistic molecular dynamics (MD) simulation in combination with free-energy calculations to study the morphology of azobenzene-terminated SAMs (Azo-SAMs) grafted on a silica substrate and their interactions with lysozyme.	Silicon Dioxide	199-205	methionine adenosyltransferase 1A	Homo sapiens	180-184
26367250-7	2015	On the contrary, SAMs with a small terminal group generate smooth surfaces with uninterrupted periodicity, thus favoring the formation of an ordered pentacene monolayer that increases the mobility of charge carriers and improves the overall performances of the OTFT devices.	pentacene	149-158	methionine adenosyltransferase 1A	Homo sapiens	17-21
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).	Methionine	41-51	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).	Methionine	41-51	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).	Adenosine Triphosphate	169-172	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).	Adenosine Triphosphate	169-172	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).	Adenosine Triphosphate	169-172	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	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
26289392-4	2015	Individuals, with hypermethioninemia due to one of the MAT1A mutations that in heterozygotes cause relatively mild and clinically benign hypermethioninemia are currently often being flagged in screening programs measuring methionine elevation to identify newborns with defective cystathionine beta-synthase activity.	Methionine	23-33	methionine adenosyltransferase 1A	Homo sapiens	55-60
25648513-4	2015	Such unusual packing is favored as it facilitates SAMs with anomalously high coverage (30%), much larger than that for enantiomerically resolved 2-butanethiol or secondary-branched butanethiol (25%) and near that for linear-chain 1-butanethiol (33%).	n-butyl mercaptan	230-243	methionine adenosyltransferase 1A	Homo sapiens	50-54
25996449-3	2015	The nanoshells having surface environment modified by hexanethiol SAMs provided high capacity both for hydrophilic DNAzyme (Dz) to induce gene silencing and for hydrophobic SN38 (7-ethyl-10-hydroxycamptothecin), anticancer drug.	1-HEXANETHIOL	54-65	methionine adenosyltransferase 1A	Homo sapiens	66-70
25996449-3	2015	The nanoshells having surface environment modified by hexanethiol SAMs provided high capacity both for hydrophilic DNAzyme (Dz) to induce gene silencing and for hydrophobic SN38 (7-ethyl-10-hydroxycamptothecin), anticancer drug.	Irinotecan	179-209	methionine adenosyltransferase 1A	Homo sapiens	66-70
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
25736428-1	2015	A new vinyl sulfone (VS) disulfide, 1,2-bis(11-(vinyl sulfonyl)undecyl)disulfane, was synthesized to enable the preparation of VS-presenting self-assembled monolayers (VS SAMs) on Au substrates.	vinyl sulfone (vs) disulfide	6-34	methionine adenosyltransferase 1A	Homo sapiens	171-175
25736428-1	2015	A new vinyl sulfone (VS) disulfide, 1,2-bis(11-(vinyl sulfonyl)undecyl)disulfane, was synthesized to enable the preparation of VS-presenting self-assembled monolayers (VS SAMs) on Au substrates.	1,2-bis(11-(vinyl sulfonyl)undecyl)disulfane	36-80	methionine adenosyltransferase 1A	Homo sapiens	171-175
25736428-2	2015	The VS SAMs were used as a model system to assess the reaction kinetics of bioactive ligands, i.e., glutathione (GSH), N-(5-amino-1-carboxypentyl)iminodiacetic acid (ab-NTA), and mannose, toward the VS groups on the SAM surface.	Glutathione	100-111	methionine adenosyltransferase 1A	Homo sapiens	7-11
25736428-2	2015	The VS SAMs were used as a model system to assess the reaction kinetics of bioactive ligands, i.e., glutathione (GSH), N-(5-amino-1-carboxypentyl)iminodiacetic acid (ab-NTA), and mannose, toward the VS groups on the SAM surface.	Glutathione	113-116	methionine adenosyltransferase 1A	Homo sapiens	7-11
25736428-2	2015	The VS SAMs were used as a model system to assess the reaction kinetics of bioactive ligands, i.e., glutathione (GSH), N-(5-amino-1-carboxypentyl)iminodiacetic acid (ab-NTA), and mannose, toward the VS groups on the SAM surface.	(S)-2,2'-((5-Amino-1-carboxypentyl)azanediyl)diacetic acid	166-172	methionine adenosyltransferase 1A	Homo sapiens	7-11
25736428-2	2015	The VS SAMs were used as a model system to assess the reaction kinetics of bioactive ligands, i.e., glutathione (GSH), N-(5-amino-1-carboxypentyl)iminodiacetic acid (ab-NTA), and mannose, toward the VS groups on the SAM surface.	Mannose	179-186	methionine adenosyltransferase 1A	Homo sapiens	7-11
25668124-3	2015	The results yield insight into the properties of the alkylsilane SAMs, which complement experimental studies from the literature.	alkylsilane	53-64	methionine adenosyltransferase 1A	Homo sapiens	65-69
25668124-4	2015	Relationships are reported between thickness, tilt angle, and coverage of alkylsilane SAMs, which also hold for alkylsilanes other than DTS and OTS.	alkylsilanes	112-124	methionine adenosyltransferase 1A	Homo sapiens	86-90
25668124-4	2015	Relationships are reported between thickness, tilt angle, and coverage of alkylsilane SAMs, which also hold for alkylsilanes other than DTS and OTS.	dibenzyl trisulfide	136-139	methionine adenosyltransferase 1A	Homo sapiens	86-90
25668124-4	2015	Relationships are reported between thickness, tilt angle, and coverage of alkylsilane SAMs, which also hold for alkylsilanes other than DTS and OTS.	octadecyltrichlorosilane	144-147	methionine adenosyltransferase 1A	Homo sapiens	86-90
25665649-5	2015	The graphene and phenyl group in the SAMs induced pi-pi interactions with C60, which facilitated the formation of a C60 coating.	Graphite	4-12	methionine adenosyltransferase 1A	Homo sapiens	37-41
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.	ethylene	105-113	methionine adenosyltransferase 1A	Homo sapiens	40-44
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.	Polyamines	118-128	methionine adenosyltransferase 1A	Homo sapiens	40-44
25271158-6	2014	We found that AdoMet homeostasis was disrupted by Dex and that Dex directly regulated MAT1A expression by enhancing the binding of the glucocorticoid receptor (GR) to the glucocorticoid-response element (GRE) of the MAT1A promoter.	Dexamethasone	63-66	methionine adenosyltransferase 1A	Homo sapiens	86-91
25437300-0	2014	Effect of leaving group on the structures of alkylsilane SAMs.	alkylsilane	45-56	methionine adenosyltransferase 1A	Homo sapiens	57-61
25437300-3	2014	It was observed that the chlorosilanes form much denser and crystalline-like SAMs and ethoxysilanes form thin SAMs, while methoxysilanes form extremely thin SAMs.	dichlorosilane	25-38	methionine adenosyltransferase 1A	Homo sapiens	77-81
25437300-3	2014	It was observed that the chlorosilanes form much denser and crystalline-like SAMs and ethoxysilanes form thin SAMs, while methoxysilanes form extremely thin SAMs.	ethoxysilanes	86-99	methionine adenosyltransferase 1A	Homo sapiens	110-114
25437300-3	2014	It was observed that the chlorosilanes form much denser and crystalline-like SAMs and ethoxysilanes form thin SAMs, while methoxysilanes form extremely thin SAMs.	ethoxysilanes	86-99	methionine adenosyltransferase 1A	Homo sapiens	110-114
25437300-7	2014	SAMs of chlorosilanes resemble a structure of snow moguls or densely packed umbrellas.	dichlorosilane	8-21	methionine adenosyltransferase 1A	Homo sapiens	0-4
25437300-8	2014	SAMs of ethoxysilanes, on the other hand, look like stacks of fallen trees, while the molecules of the ultrathin methoxysilane SAMs are lying nearly parallel to the surface, resembling creepers.	ethoxysilanes	8-21	methionine adenosyltransferase 1A	Homo sapiens	0-4
25437300-8	2014	SAMs of ethoxysilanes, on the other hand, look like stacks of fallen trees, while the molecules of the ultrathin methoxysilane SAMs are lying nearly parallel to the surface, resembling creepers.	ultrathin methoxysilane	103-126	methionine adenosyltransferase 1A	Homo sapiens	127-131
25495479-6	2015	Moreover, this method enables study of the influence of the Au surface atom arrangement on SAMs that were created and analyzed, both under identical conditions, something that can be challenging for the typical studies of this kind using individual gold single crystal electrodes.	Gold	60-62	methionine adenosyltransferase 1A	Homo sapiens	91-95
25271158-6	2014	We found that AdoMet homeostasis was disrupted by Dex and that Dex directly regulated MAT1A expression by enhancing the binding of the glucocorticoid receptor (GR) to the glucocorticoid-response element (GRE) of the MAT1A promoter.	Dexamethasone	63-66	methionine adenosyltransferase 1A	Homo sapiens	216-221
24491327-2	2014	We observed that the work functions of the Au metal surfaces modified with SAMs changed differently under elevated-temperature conditions based on the type of SAMs categorized by three different features based on chemical anchoring group, molecular backbone structure, and the direction of the dipole moment.	Metals	46-51	methionine adenosyltransferase 1A	Homo sapiens	159-163
25290370-6	2014	A negative potential bias was subsequently applied to the pattern to selectively desorb the layer of SAMs electrochemically from the Cu surface while preserving the MLD films on Si.	Copper	133-135	methionine adenosyltransferase 1A	Homo sapiens	101-105
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).	Glutathione	34-37	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	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
24954531-0	2014	Synthesis and surface-spectroscopic characterization of photoisomerizable glyco-SAMs on Au(111).	Gold	88-90	methionine adenosyltransferase 1A	Homo sapiens	80-84
24954531-1	2014	Photoisomerizable glyco-SAMs (self-assembled monolayers), utilizing synthetic azobenzene glycoside derivatives were fabricated.	azobenzene glycoside	78-98	methionine adenosyltransferase 1A	Homo sapiens	24-28
24954531-5	2014	In particular and unprecedented to date, we prove reversible E Z E isomerization of azobenzene glycoside-terminated SAMs.	azobenzene glycoside	84-104	methionine adenosyltransferase 1A	Homo sapiens	116-120
24452131-1	2014	Binding behaviors of streptavidin were investigated with different lateral packing densities of biotin-functionalized, non-biofouling pOEGMA brushes, synthesized by surface-initiated polymerization from mixed SAMs with different mole fractions of the polymerization initiator on gold surfaces.	Biotin	96-102	methionine adenosyltransferase 1A	Homo sapiens	209-213
24851249-6	2014	Catechol-terminated SAMs are also obtained on high-roughness gold substrates that show the ability to assemble magnetic nanoparticles, despite their lack of enhanced adhesion at the molecular level.	catechol	0-8	methionine adenosyltransferase 1A	Homo sapiens	20-24
24491327-2	2014	We observed that the work functions of the Au metal surfaces modified with SAMs changed differently under elevated-temperature conditions based on the type of SAMs categorized by three different features based on chemical anchoring group, molecular backbone structure, and the direction of the dipole moment.	Gold	43-45	methionine adenosyltransferase 1A	Homo sapiens	75-79
24491327-2	2014	We observed that the work functions of the Au metal surfaces modified with SAMs changed differently under elevated-temperature conditions based on the type of SAMs categorized by three different features based on chemical anchoring group, molecular backbone structure, and the direction of the dipole moment.	Gold	43-45	methionine adenosyltransferase 1A	Homo sapiens	159-163
24491327-2	2014	We observed that the work functions of the Au metal surfaces modified with SAMs changed differently under elevated-temperature conditions based on the type of SAMs categorized by three different features based on chemical anchoring group, molecular backbone structure, and the direction of the dipole moment.	Metals	46-51	methionine adenosyltransferase 1A	Homo sapiens	75-79
25233063-3	2014	We measured static contact angles (thetas) made by water droplets on n-alkanethiolate SAMs with an odd (SAM(O)) or even (SAM(E)) number of carbons (average thetas range of 105.8-112.1 ).	Water	51-56	methionine adenosyltransferase 1A	Homo sapiens	86-90
25233063-8	2014	From these results, we deduce that the roughness of the metal substrate (from comparison of M(AD) versus M(TS)) and orientation of the terminal -CH2CH3 (by comparing SAM(E) and SAM(O) on Au(TS) versus Ag(TS)) play major roles in the hydrophobicity and, by extension, general wetting properties of n-alkanethiolate SAMs.	Metals	56-61	methionine adenosyltransferase 1A	Homo sapiens	314-318
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.	Adenosine Triphosphate	86-89	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.	Adenosine Triphosphate	86-89	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.	Methionine	94-104	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.	Methionine	94-104	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	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
24649856-2	2014	Here, we report that the MAT from Sulfolobus solfataricus (sMAT), an enzyme from a poorly explored class of the MAT family, has the ability to produce a range of differentially alkylated AdoMet analogs in the presence of non-native methionine analogs and ATP.	Methionine	232-242	methionine adenosyltransferase 1A	Homo sapiens	25-28
24649856-2	2014	Here, we report that the MAT from Sulfolobus solfataricus (sMAT), an enzyme from a poorly explored class of the MAT family, has the ability to produce a range of differentially alkylated AdoMet analogs in the presence of non-native methionine analogs and ATP.	Methionine	232-242	methionine adenosyltransferase 1A	Homo sapiens	60-63
24649856-2	2014	Here, we report that the MAT from Sulfolobus solfataricus (sMAT), an enzyme from a poorly explored class of the MAT family, has the ability to produce a range of differentially alkylated AdoMet analogs in the presence of non-native methionine analogs and ATP.	Adenosine Triphosphate	255-258	methionine adenosyltransferase 1A	Homo sapiens	25-28
24649856-2	2014	Here, we report that the MAT from Sulfolobus solfataricus (sMAT), an enzyme from a poorly explored class of the MAT family, has the ability to produce a range of differentially alkylated AdoMet analogs in the presence of non-native methionine analogs and ATP.	Adenosine Triphosphate	255-258	methionine adenosyltransferase 1A	Homo sapiens	60-63
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
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.	Methionine	136-146	methionine adenosyltransferase 1A	Homo sapiens	77-82
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
24807699-0	2014	Adjusting the surface areal density of click-reactive azide groups by kinetic control of the azide substitution reaction on bromine-functional SAMs.	Azides	54-59	methionine adenosyltransferase 1A	Homo sapiens	143-147
24807699-0	2014	Adjusting the surface areal density of click-reactive azide groups by kinetic control of the azide substitution reaction on bromine-functional SAMs.	Azides	93-98	methionine adenosyltransferase 1A	Homo sapiens	143-147
24807699-0	2014	Adjusting the surface areal density of click-reactive azide groups by kinetic control of the azide substitution reaction on bromine-functional SAMs.	Bromine	124-131	methionine adenosyltransferase 1A	Homo sapiens	143-147
24128087-4	2014	SAM is generated from adenosine triphosphate (ATP) and methionine by methionine adenosyltransferase (MAT), a redox-sensitive enzyme in the SAM cycle.	Adenosine Triphosphate	22-44	methionine adenosyltransferase 1A	Homo sapiens	69-99
24128087-4	2014	SAM is generated from adenosine triphosphate (ATP) and methionine by methionine adenosyltransferase (MAT), a redox-sensitive enzyme in the SAM cycle.	Adenosine Triphosphate	22-44	methionine adenosyltransferase 1A	Homo sapiens	101-104
24128087-4	2014	SAM is generated from adenosine triphosphate (ATP) and methionine by methionine adenosyltransferase (MAT), a redox-sensitive enzyme in the SAM cycle.	Adenosine Triphosphate	46-49	methionine adenosyltransferase 1A	Homo sapiens	69-99
24128087-4	2014	SAM is generated from adenosine triphosphate (ATP) and methionine by methionine adenosyltransferase (MAT), a redox-sensitive enzyme in the SAM cycle.	Adenosine Triphosphate	46-49	methionine adenosyltransferase 1A	Homo sapiens	101-104
24128087-4	2014	SAM is generated from adenosine triphosphate (ATP) and methionine by methionine adenosyltransferase (MAT), a redox-sensitive enzyme in the SAM cycle.	Methionine	55-65	methionine adenosyltransferase 1A	Homo sapiens	69-99
24128087-4	2014	SAM is generated from adenosine triphosphate (ATP) and methionine by methionine adenosyltransferase (MAT), a redox-sensitive enzyme in the SAM cycle.	Methionine	55-65	methionine adenosyltransferase 1A	Homo sapiens	101-104
24128087-10	2014	The depletion of ATP in lupus T cells may affect MAT activity as well as adenosine monophosphate (AMP) activated protein kinase (AMPK), which phosphorylates histones and inhibits mechanistic target of rapamycin (mTOR).	Adenosine Triphosphate	17-20	methionine adenosyltransferase 1A	Homo sapiens	49-52
24491327-2	2014	We observed that the work functions of the Au metal surfaces modified with SAMs changed differently under elevated-temperature conditions based on the type of SAMs categorized by three different features based on chemical anchoring group, molecular backbone structure, and the direction of the dipole moment.	dipole	294-300	methionine adenosyltransferase 1A	Homo sapiens	75-79
24491327-3	2014	The temperature-dependent work function of the SAM-modified Au metal could be explained in terms of the molecular binding energy and the thermal stability of the SAMs, which were investigated with thermal desorption spectroscopic measurements and were explained with molecular modeling.	Gold	60-62	methionine adenosyltransferase 1A	Homo sapiens	162-166
24491327-3	2014	The temperature-dependent work function of the SAM-modified Au metal could be explained in terms of the molecular binding energy and the thermal stability of the SAMs, which were investigated with thermal desorption spectroscopic measurements and were explained with molecular modeling.	Metals	63-68	methionine adenosyltransferase 1A	Homo sapiens	162-166
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
24445979-10	2014	CONCLUSION: These cases show that individuals with even single changes in the MAT1A gene may have elevations in methionine identified by newborn screening, which may persist for months after birth without any clinical consequences.	Methionine	112-122	methionine adenosyltransferase 1A	Homo sapiens	78-83
24099574-2	2013	Characterization of the SAMs by X-ray photoelectron spectroscopy (XPS) revealed that all sulfur atoms of the tridentate adsorbates were bound to the surface of gold, and that the tailgroups were in general less densely packed than the SAM derived from octadecanethiol (C18SH).	Sulfur	89-95	methionine adenosyltransferase 1A	Homo sapiens	24-28
24099574-2	2013	Characterization of the SAMs by X-ray photoelectron spectroscopy (XPS) revealed that all sulfur atoms of the tridentate adsorbates were bound to the surface of gold, and that the tailgroups were in general less densely packed than the SAM derived from octadecanethiol (C18SH).	n-octadecyl mercaptan	252-267	methionine adenosyltransferase 1A	Homo sapiens	24-28
24156365-1	2013	The use of self-assembled monolayers (SAMs) as a polymer-free platform to deliver an antiproliferative drug, paclitaxel (PAT), from a stent material cobalt-chromium (CoCr) alloy has been previously demonstrated.	Polymers	49-56	methionine adenosyltransferase 1A	Homo sapiens	38-42
24156365-1	2013	The use of self-assembled monolayers (SAMs) as a polymer-free platform to deliver an antiproliferative drug, paclitaxel (PAT), from a stent material cobalt-chromium (CoCr) alloy has been previously demonstrated.	Paclitaxel	109-119	methionine adenosyltransferase 1A	Homo sapiens	38-42
24041237-8	2013	In addition, the relative energies of Au40(SCH3)24 nanoparticles and Au-thiolate SAMs are calculated using the updated parameters.	au-thiolate	69-80	methionine adenosyltransferase 1A	Homo sapiens	81-85
24156365-1	2013	The use of self-assembled monolayers (SAMs) as a polymer-free platform to deliver an antiproliferative drug, paclitaxel (PAT), from a stent material cobalt-chromium (CoCr) alloy has been previously demonstrated.	Paclitaxel	121-124	methionine adenosyltransferase 1A	Homo sapiens	38-42
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
23665184-7	2013	In HCC cells, MAT1A/MAT2A switch is associated with global DNA hypomethylation, decrease in DNA repair, genomic instability, and signaling deregulation including c-MYC overexpression, rise in polyamine synthesis, upregulation of RAS/ERK, IKK/NF-kB, PI3K/AKT, and LKB1/AMPK axis.	Polyamines	192-201	methionine adenosyltransferase 1A	Homo sapiens	14-19
23985021-1	2013	SAMs formed from mixtures of alkyne-silanes and alkane-silanes are used to control the areal density of click-reactive alkyne groups on the surface of flat germanium substrates, silicon wafers, and silica nanoparticles.	Alkynes	29-35	methionine adenosyltransferase 1A	Homo sapiens	0-4
23985021-1	2013	SAMs formed from mixtures of alkyne-silanes and alkane-silanes are used to control the areal density of click-reactive alkyne groups on the surface of flat germanium substrates, silicon wafers, and silica nanoparticles.	Silanes	36-43	methionine adenosyltransferase 1A	Homo sapiens	0-4
23985021-1	2013	SAMs formed from mixtures of alkyne-silanes and alkane-silanes are used to control the areal density of click-reactive alkyne groups on the surface of flat germanium substrates, silicon wafers, and silica nanoparticles.	Alkanes	48-54	methionine adenosyltransferase 1A	Homo sapiens	0-4
23985021-1	2013	SAMs formed from mixtures of alkyne-silanes and alkane-silanes are used to control the areal density of click-reactive alkyne groups on the surface of flat germanium substrates, silicon wafers, and silica nanoparticles.	Silanes	55-62	methionine adenosyltransferase 1A	Homo sapiens	0-4
23985021-1	2013	SAMs formed from mixtures of alkyne-silanes and alkane-silanes are used to control the areal density of click-reactive alkyne groups on the surface of flat germanium substrates, silicon wafers, and silica nanoparticles.	Alkynes	119-125	methionine adenosyltransferase 1A	Homo sapiens	0-4
23985021-1	2013	SAMs formed from mixtures of alkyne-silanes and alkane-silanes are used to control the areal density of click-reactive alkyne groups on the surface of flat germanium substrates, silicon wafers, and silica nanoparticles.	Germanium	156-165	methionine adenosyltransferase 1A	Homo sapiens	0-4
23985021-1	2013	SAMs formed from mixtures of alkyne-silanes and alkane-silanes are used to control the areal density of click-reactive alkyne groups on the surface of flat germanium substrates, silicon wafers, and silica nanoparticles.	Silicon Dioxide	198-204	methionine adenosyltransferase 1A	Homo sapiens	0-4
23829546-3	2013	The SAMs exhibited proton-coupled electron transfer (PCET) reactions when the electrochemistry was studied in aqueous electrolyte solution (0.1 M NaClO4 with Britton-Robinson buffer to adjust the solution pH).	sodium perchlorate	146-152	methionine adenosyltransferase 1A	Homo sapiens	4-8
23349144-6	2013	These analyses revealed that the formation of PA SAMs accelerate the deposition of poorly crystallized HA, in an alkyl chain length-dependent manner.	Protactinium	46-48	methionine adenosyltransferase 1A	Homo sapiens	49-53
23819458-3	2013	The correlation between the electrochemical results and those acquired by SPR and QCM indicated the presence of an adlayer of Cyt c adsorbed on the thiolate SAMs.	thiolate	148-156	methionine adenosyltransferase 1A	Homo sapiens	157-161
23901478-3	2013	Then, Nc were immobilized onto oxidized SAM silicon substrate (SAMs/Si) through electrostatic interaction between cationic Nc and anionic SAMs/Si.	Silicon	44-51	methionine adenosyltransferase 1A	Homo sapiens	63-67
23901478-3	2013	Then, Nc were immobilized onto oxidized SAM silicon substrate (SAMs/Si) through electrostatic interaction between cationic Nc and anionic SAMs/Si.	Silicon	44-51	methionine adenosyltransferase 1A	Homo sapiens	138-142
23901478-3	2013	Then, Nc were immobilized onto oxidized SAM silicon substrate (SAMs/Si) through electrostatic interaction between cationic Nc and anionic SAMs/Si.	Silicon	68-70	methionine adenosyltransferase 1A	Homo sapiens	138-142
23901478-3	2013	Then, Nc were immobilized onto oxidized SAM silicon substrate (SAMs/Si) through electrostatic interaction between cationic Nc and anionic SAMs/Si.	12-nitrocamptothecin	6-8	methionine adenosyltransferase 1A	Homo sapiens	63-67
23901478-3	2013	Then, Nc were immobilized onto oxidized SAM silicon substrate (SAMs/Si) through electrostatic interaction between cationic Nc and anionic SAMs/Si.	12-nitrocamptothecin	6-8	methionine adenosyltransferase 1A	Homo sapiens	138-142
23901478-3	2013	Then, Nc were immobilized onto oxidized SAM silicon substrate (SAMs/Si) through electrostatic interaction between cationic Nc and anionic SAMs/Si.	Silicon	143-145	methionine adenosyltransferase 1A	Homo sapiens	63-67
23901478-4	2013	The characterization results clearly show that the well-graphitized MWCNTs were synthesized by using functionalized silicon substrate (Nc/SAMs/Si) as a template having appropriate density of catalyst.	Silicon	116-123	methionine adenosyltransferase 1A	Homo sapiens	138-142
23657719-5	2013	Here the biorepulsivity of the middle part of the SAMs as well as specific binding to the carbohydrate termini could be clearly demonstrated.	Carbohydrates	90-102	methionine adenosyltransferase 1A	Homo sapiens	50-54
23829546-5	2013	We also demonstrated that the interfacial redox processes were modulated by the addition of Lewis acids such as BF3 or Al(3+) to the electrolyte media, in which the externally added Lewis acids interacted with mu-O of the dinuclear moiety within the SAMs.	Lewis Acids	92-103	methionine adenosyltransferase 1A	Homo sapiens	250-254
23829546-5	2013	We also demonstrated that the interfacial redox processes were modulated by the addition of Lewis acids such as BF3 or Al(3+) to the electrolyte media, in which the externally added Lewis acids interacted with mu-O of the dinuclear moiety within the SAMs.	boron trifluoride	112-115	methionine adenosyltransferase 1A	Homo sapiens	250-254
23829546-5	2013	We also demonstrated that the interfacial redox processes were modulated by the addition of Lewis acids such as BF3 or Al(3+) to the electrolyte media, in which the externally added Lewis acids interacted with mu-O of the dinuclear moiety within the SAMs.	ALUMINUM ION	119-125	methionine adenosyltransferase 1A	Homo sapiens	250-254
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
23558312-2	2013	Low-energy electron induced chemical modifications of 11-mercaptoundecanoic acid (MUA, HS-(CH2)10-COOH) SAMs deposited on gold were probed in situ as a function of the irradiation energy (&lt;11 eV) by combining two complementary techniques: High Resolution Electron Energy Loss Spectroscopy (HREELS), a surface sensitive vibrational spectroscopy technique, and Electron Stimulated Desorption (ESD) analysis of neutral fragments.	11-mercaptoundecanoic acid	54-80	methionine adenosyltransferase 1A	Homo sapiens	104-108
23558312-2	2013	Low-energy electron induced chemical modifications of 11-mercaptoundecanoic acid (MUA, HS-(CH2)10-COOH) SAMs deposited on gold were probed in situ as a function of the irradiation energy (&lt;11 eV) by combining two complementary techniques: High Resolution Electron Energy Loss Spectroscopy (HREELS), a surface sensitive vibrational spectroscopy technique, and Electron Stimulated Desorption (ESD) analysis of neutral fragments.	Hydrogen	87-89	methionine adenosyltransferase 1A	Homo sapiens	104-108
23558312-2	2013	Low-energy electron induced chemical modifications of 11-mercaptoundecanoic acid (MUA, HS-(CH2)10-COOH) SAMs deposited on gold were probed in situ as a function of the irradiation energy (&lt;11 eV) by combining two complementary techniques: High Resolution Electron Energy Loss Spectroscopy (HREELS), a surface sensitive vibrational spectroscopy technique, and Electron Stimulated Desorption (ESD) analysis of neutral fragments.	Carbonic Acid	98-102	methionine adenosyltransferase 1A	Homo sapiens	104-108
23558312-4	2013	CO2 and H2O were also directly identified at low temperature by vibrational analysis of the irradiated SAMs.	Water	8-11	methionine adenosyltransferase 1A	Homo sapiens	103-107
23425511-1	2013	MAT (methionine adenosyltransferase) utilizes L-methionine and ATP to form SAM (S-adenosylmethionine), the principal methyl donor in biological methylation.	Methionine	46-58	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.	Adenosine Triphosphate	63-66	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	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
23737726-6	2013	By imaging under water, the capillary force is eliminated on ODT SAMs, which leads to a lower lateral force.	Water	17-22	methionine adenosyltransferase 1A	Homo sapiens	65-69
23737726-7	2013	However, the lateral force image was reversed on MHA SAMs, which suggested that hydrophobic forces dominated in water.	Water	112-117	methionine adenosyltransferase 1A	Homo sapiens	53-57
23527630-1	2013	Nanoparticles functionalized with mixed self-assembled monolayers (m-SAMs) comprising positively and negatively charged thiols are stable at both low and high pH but precipitate sharply at the pH where the charges on the particle are balanced (pH(prec)).	Sulfhydryl Compounds	120-126	methionine adenosyltransferase 1A	Homo sapiens	69-73
23537075-0	2013	Oxygen attachment on alkanethiolate SAMs induced by low-energy electron irradiation.	Oxygen	0-6	methionine adenosyltransferase 1A	Homo sapiens	36-40
23537075-0	2013	Oxygen attachment on alkanethiolate SAMs induced by low-energy electron irradiation.	alkanethiolate	21-35	methionine adenosyltransferase 1A	Homo sapiens	36-40
23537075-2	2013	Dosing the SAMs with (18)O2 at 50 K results in the ESD of (18)O(-) and (18)OH(-).	Oxygen	25-27	methionine adenosyltransferase 1A	Homo sapiens	11-15
23537075-4	2013	A minimum incident electron energy of 6-7 eV is required to initiate the binding of (18)O2 to the SAMs.	Oxygen	88-90	methionine adenosyltransferase 1A	Homo sapiens	98-102
23540684-7	2013	These results provide new insights into the formation of disulfide-based SAMs on gold but also raise some fundamental questions about the intimate mechanism involved in the facilitated adsorption/desorption of SAMs under electrode polarization.	Disulfides	57-66	methionine adenosyltransferase 1A	Homo sapiens	73-77
23540684-7	2013	These results provide new insights into the formation of disulfide-based SAMs on gold but also raise some fundamental questions about the intimate mechanism involved in the facilitated adsorption/desorption of SAMs under electrode polarization.	Disulfides	57-66	methionine adenosyltransferase 1A	Homo sapiens	210-214
23540684-8	2013	Finally, the possibility to easily and selectively address the formation/removal of thioctic-based SAMs on gold by applying a moderate cathodic/anodic potential offers another degree of freedom in tailoring their properties and in controlling their self-assembly, nanostructuration, and/or release.	thioctic	84-92	methionine adenosyltransferase 1A	Homo sapiens	99-103
23462864-0	2013	Reversible binding and quantification of heparin and chondroitin sulfate in water using redox-stable biferrocenylene SAMs.	Heparin	41-48	methionine adenosyltransferase 1A	Homo sapiens	117-121
23462864-0	2013	Reversible binding and quantification of heparin and chondroitin sulfate in water using redox-stable biferrocenylene SAMs.	Chondroitin Sulfates	53-72	methionine adenosyltransferase 1A	Homo sapiens	117-121
23462864-0	2013	Reversible binding and quantification of heparin and chondroitin sulfate in water using redox-stable biferrocenylene SAMs.	Water	76-81	methionine adenosyltransferase 1A	Homo sapiens	117-121
23462864-2	2013	The resulting SAMs with their extraordinary stability in the monocationic state were used to detect and quantify heparin (3-300 x 10(-5) g L(-1) = 0.003-0.3 U mL(-1)) and chondroitin sulfate (3-250 x 10(-5) g L(-1)) in aqueous buffer by cyclic voltammetry, square wave voltammetry and surface plasmon resonance.	Heparin	113-120	methionine adenosyltransferase 1A	Homo sapiens	14-18
23462864-2	2013	The resulting SAMs with their extraordinary stability in the monocationic state were used to detect and quantify heparin (3-300 x 10(-5) g L(-1) = 0.003-0.3 U mL(-1)) and chondroitin sulfate (3-250 x 10(-5) g L(-1)) in aqueous buffer by cyclic voltammetry, square wave voltammetry and surface plasmon resonance.	Chondroitin Sulfates	171-190	methionine adenosyltransferase 1A	Homo sapiens	14-18
23234602-3	2012	The SAMs exhibit excellent hydrophobicity, with static water contact angles of up to 119  and low critical surface tensions of 5-20 mN/m depending on the number of F atoms per molecule.	Water	55-60	methionine adenosyltransferase 1A	Homo sapiens	4-8
23244178-8	2013	Micrometer-scale patterns were fabricated by carrying out exposures of the aryl azide terminated SAMs through a mask submerged under a film of primary amine.	aryl azide	75-85	methionine adenosyltransferase 1A	Homo sapiens	97-101
23189954-6	2012	We have demonstrated the successful reactions of the conversion of the vinyl-terminated SAMs successively into SAM-COOH and SAM-NHS without any degradation of the monolayer.	Carbonic Acid	115-119	methionine adenosyltransferase 1A	Homo sapiens	88-92
23189954-6	2012	We have demonstrated the successful reactions of the conversion of the vinyl-terminated SAMs successively into SAM-COOH and SAM-NHS without any degradation of the monolayer.	sam-nhs	124-131	methionine adenosyltransferase 1A	Homo sapiens	88-92
23083520-1	2012	Selective generation of an amine-terminated self-assembled monolayer bound to silicon wafers via a silicon-carbon linkage was realized by photocatalytically reducing the corresponding azide-terminated, self-assembled monolayers (Az-SAMs).	Amines	27-32	methionine adenosyltransferase 1A	Homo sapiens	232-236
23083520-1	2012	Selective generation of an amine-terminated self-assembled monolayer bound to silicon wafers via a silicon-carbon linkage was realized by photocatalytically reducing the corresponding azide-terminated, self-assembled monolayers (Az-SAMs).	Silicon	78-85	methionine adenosyltransferase 1A	Homo sapiens	232-236
23083520-1	2012	Selective generation of an amine-terminated self-assembled monolayer bound to silicon wafers via a silicon-carbon linkage was realized by photocatalytically reducing the corresponding azide-terminated, self-assembled monolayers (Az-SAMs).	Carbon	107-113	methionine adenosyltransferase 1A	Homo sapiens	232-236
23083520-1	2012	Selective generation of an amine-terminated self-assembled monolayer bound to silicon wafers via a silicon-carbon linkage was realized by photocatalytically reducing the corresponding azide-terminated, self-assembled monolayers (Az-SAMs).	Azides	184-189	methionine adenosyltransferase 1A	Homo sapiens	232-236
23317370-0	2013	What happens to the thiolates created by reductively desorbing SAMs?	thiolates	20-29	methionine adenosyltransferase 1A	Homo sapiens	63-67
23286894-0	2013	Mono-fluorinated alkyne-derived SAMs on oxide-free Si(111) surfaces: preparation, characterization and tuning of the Si workfunction.	Oxides	40-45	methionine adenosyltransferase 1A	Homo sapiens	32-36
23286894-0	2013	Mono-fluorinated alkyne-derived SAMs on oxide-free Si(111) surfaces: preparation, characterization and tuning of the Si workfunction.	Silicon	51-53	methionine adenosyltransferase 1A	Homo sapiens	32-36
23286894-0	2013	Mono-fluorinated alkyne-derived SAMs on oxide-free Si(111) surfaces: preparation, characterization and tuning of the Si workfunction.	Silicon	117-119	methionine adenosyltransferase 1A	Homo sapiens	32-36
24377546-0	2013	5-Aza-2&lt;-deoxycytidine induces hepatoma cell apoptosis via enhancing methionine adenosyltransferase 1A expression and inducing S-adenosylmethionine production.	5-aza-2&lt;-deoxycytidine	0-25	methionine adenosyltransferase 1A	Homo sapiens	72-104
24377546-4	2013	We studied the effect of the demethylating reagent 5-aza-2&lt;-deoxycitidine (5-Aza-CdR) on MAT1A gene expression, DNA methylation and S-adenosylmethionine (SAMe) production in the HCC cell line Huh7.	5-aza-2&lt	51-61	methionine adenosyltransferase 1A	Homo sapiens	92-97
24377546-4	2013	We studied the effect of the demethylating reagent 5-aza-2&lt;-deoxycitidine (5-Aza-CdR) on MAT1A gene expression, DNA methylation and S-adenosylmethionine (SAMe) production in the HCC cell line Huh7.	deoxycitidine	63-76	methionine adenosyltransferase 1A	Homo sapiens	92-97
23010044-9	2013	Moreover, all of these sulfobetaine-terminated SAMs showed a fairly negative zeta potential in PBS at pH 7.4.	sulfobetaine	23-35	methionine adenosyltransferase 1A	Homo sapiens	47-51
23010044-9	2013	Moreover, all of these sulfobetaine-terminated SAMs showed a fairly negative zeta potential in PBS at pH 7.4.	Lead	95-98	methionine adenosyltransferase 1A	Homo sapiens	47-51
23010044-10	2013	After contact with blood, these sulfobetaine-terminated SAMs demonstrated distinct platelet reactivity among each other.	sulfobetaine	32-44	methionine adenosyltransferase 1A	Homo sapiens	56-60
23010044-13	2013	This study demonstrated that optimizing solvent and concentration conditions could control the structural organization of zwitterionic sulfobetaine-terminated SAMs and, consequently, modify biomedical properties.	sulfobetaine	135-147	methionine adenosyltransferase 1A	Homo sapiens	159-163
23023396-0	2012	Heme plane orientation dependent direct electron transfer of cytochrome c at SAMs/Au electrodes with different wettability.	Heme	0-4	methionine adenosyltransferase 1A	Homo sapiens	77-81
23078107-1	2012	The formation of aromatic SAMs on Au(111) using three nitro-substituted arene sulfenyl chlorides (4-nitrophenyl sulfenyl chloride (1), 2-nitrophenyl sulfenyl chloride (2), and 2,4-dinitrophenyl sulfenyl chloride (3)) is studied.	2-nitrobenzenesulfenyl chloride	135-166	methionine adenosyltransferase 1A	Homo sapiens	26-30
23078107-1	2012	The formation of aromatic SAMs on Au(111) using three nitro-substituted arene sulfenyl chlorides (4-nitrophenyl sulfenyl chloride (1), 2-nitrophenyl sulfenyl chloride (2), and 2,4-dinitrophenyl sulfenyl chloride (3)) is studied.	2,4-dinitrobenzenesulfenyl chloride	176-211	methionine adenosyltransferase 1A	Homo sapiens	26-30
23234602-5	2012	Upon increasing the number of fluorine atoms in the alkyne chains from 0 to 17, the adhesion of bare silica probes to the SAMs in air decreases from 11.6 +- 0.20 mJ/m(2) for fluorine-free (F0) alkyne monolayers to as low as 3.2 +- 0.03 mJ/m(2) for a heptadecafluoro-hexadecyne (F17)-based monolayer.	Fluorine	30-38	methionine adenosyltransferase 1A	Homo sapiens	122-126
23078107-2	2012	The formation of SAMs and their quality are investigated as a function of the position of the nitro substituent(s) on the aromatic ring.	nitro	94-99	methionine adenosyltransferase 1A	Homo sapiens	17-21
23078107-8	2012	Compounds 2 and 3 both form lower-quality SAMs where the adsorbed nitro-phenyl thiolates are more tilted.	nitro-phenyl thiolates	66-88	methionine adenosyltransferase 1A	Homo sapiens	42-46
23078107-9	2012	These SAMs are less stable than the ones obtained with the 4-nitrosubsituted precursor and decompose with time, leaving only sulfur on the gold surface.	Sulfur	125-131	methionine adenosyltransferase 1A	Homo sapiens	6-10
23234602-5	2012	Upon increasing the number of fluorine atoms in the alkyne chains from 0 to 17, the adhesion of bare silica probes to the SAMs in air decreases from 11.6 +- 0.20 mJ/m(2) for fluorine-free (F0) alkyne monolayers to as low as 3.2 +- 0.03 mJ/m(2) for a heptadecafluoro-hexadecyne (F17)-based monolayer.	Alkynes	52-58	methionine adenosyltransferase 1A	Homo sapiens	122-126
23234602-5	2012	Upon increasing the number of fluorine atoms in the alkyne chains from 0 to 17, the adhesion of bare silica probes to the SAMs in air decreases from 11.6 +- 0.20 mJ/m(2) for fluorine-free (F0) alkyne monolayers to as low as 3.2 +- 0.03 mJ/m(2) for a heptadecafluoro-hexadecyne (F17)-based monolayer.	Silicon Dioxide	101-107	methionine adenosyltransferase 1A	Homo sapiens	122-126
23234602-5	2012	Upon increasing the number of fluorine atoms in the alkyne chains from 0 to 17, the adhesion of bare silica probes to the SAMs in air decreases from 11.6 +- 0.20 mJ/m(2) for fluorine-free (F0) alkyne monolayers to as low as 3.2 +- 0.03 mJ/m(2) for a heptadecafluoro-hexadecyne (F17)-based monolayer.	Fluorine	174-182	methionine adenosyltransferase 1A	Homo sapiens	122-126
23234602-5	2012	Upon increasing the number of fluorine atoms in the alkyne chains from 0 to 17, the adhesion of bare silica probes to the SAMs in air decreases from 11.6 +- 0.20 mJ/m(2) for fluorine-free (F0) alkyne monolayers to as low as 3.2 +- 0.03 mJ/m(2) for a heptadecafluoro-hexadecyne (F17)-based monolayer.	Alkynes	193-199	methionine adenosyltransferase 1A	Homo sapiens	122-126
23234602-5	2012	Upon increasing the number of fluorine atoms in the alkyne chains from 0 to 17, the adhesion of bare silica probes to the SAMs in air decreases from 11.6 +- 0.20 mJ/m(2) for fluorine-free (F0) alkyne monolayers to as low as 3.2 +- 0.03 mJ/m(2) for a heptadecafluoro-hexadecyne (F17)-based monolayer.	heptadecafluoro-hexadecyne	250-276	methionine adenosyltransferase 1A	Homo sapiens	122-126
22941120-6	2012	We then describe the anchoring process of carboxylic molecules on amine based SAMs we have recently reported on.	Amines	66-71	methionine adenosyltransferase 1A	Homo sapiens	78-82
22807109-0	2012	Human liver methionine cycle: MAT1A and GNMT gene resequencing, functional genomics, and hepatic genotype-phenotype correlation.	Methionine	12-22	methionine adenosyltransferase 1A	Homo sapiens	30-35
22807109-8	2012	Correlation analyses among hepatic protein levels for methionine cycle enzymes showed significant correlations between GNMT and MAT1A (p = 1.5 x 10(-3)) and between GNMT and betaine homocysteine methyltransferase (p = 1.6 x 10(-7)).	Methionine	54-64	methionine adenosyltransferase 1A	Homo sapiens	128-133
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
22958159-1	2012	The electronic properties of alkanethiol self-assembled monolayers (alkanethiolate SAMs) associated with their molecular-scale geometry are investigated using scanning tunneling microscopy and spectroscopy (STM/STS).	alkanethiol	29-40	methionine adenosyltransferase 1A	Homo sapiens	83-87
22958159-1	2012	The electronic properties of alkanethiol self-assembled monolayers (alkanethiolate SAMs) associated with their molecular-scale geometry are investigated using scanning tunneling microscopy and spectroscopy (STM/STS).	alkanethiolate	68-82	methionine adenosyltransferase 1A	Homo sapiens	83-87
22958159-2	2012	We have selectively formed the three types of alkanethiolate SAMs with standing-up, lying-down, and lattice-gas phases by precise thermal annealing of the SAMs which are conventionally prepared by depositing alkanethiol molecules onto Au(111) surface in solution.	alkanethiolate	46-60	methionine adenosyltransferase 1A	Homo sapiens	61-65
22958159-2	2012	We have selectively formed the three types of alkanethiolate SAMs with standing-up, lying-down, and lattice-gas phases by precise thermal annealing of the SAMs which are conventionally prepared by depositing alkanethiol molecules onto Au(111) surface in solution.	alkanethiolate	46-60	methionine adenosyltransferase 1A	Homo sapiens	155-159
22958159-2	2012	We have selectively formed the three types of alkanethiolate SAMs with standing-up, lying-down, and lattice-gas phases by precise thermal annealing of the SAMs which are conventionally prepared by depositing alkanethiol molecules onto Au(111) surface in solution.	alkanethiol	46-57	methionine adenosyltransferase 1A	Homo sapiens	61-65
22958159-2	2012	We have selectively formed the three types of alkanethiolate SAMs with standing-up, lying-down, and lattice-gas phases by precise thermal annealing of the SAMs which are conventionally prepared by depositing alkanethiol molecules onto Au(111) surface in solution.	alkanethiol	46-57	methionine adenosyltransferase 1A	Homo sapiens	155-159
22958159-2	2012	We have selectively formed the three types of alkanethiolate SAMs with standing-up, lying-down, and lattice-gas phases by precise thermal annealing of the SAMs which are conventionally prepared by depositing alkanethiol molecules onto Au(111) surface in solution.	Gold	235-237	methionine adenosyltransferase 1A	Homo sapiens	61-65
22784021-2	2012	Surface-sensitive spectroscopic techniques are used to provide feedback on the processing conditions in which solution temperature, silane concentration, and reaction time are optimized to improve the quality of these SAMs.	Silanes	132-138	methionine adenosyltransferase 1A	Homo sapiens	218-222
22784021-5	2012	A comparison is also presented for two approaches to fill defects within these solvent extracted monolayers with more perfluoroalkylsilane molecules, aiming to improve the quality of these SAMs.	perfluoroalkylsilane	118-138	methionine adenosyltransferase 1A	Homo sapiens	189-193
22784021-6	2012	A detailed XPS analysis is used to assess both the relative changes in density and average tilt of molecules within the monolayers as the process temperature is increased in increments from 20 to 80  C. The observed differences in quality of the SAMs are attributed to temperature- and time-dependent organization and reactivity of the silane molecules.	Silanes	336-342	methionine adenosyltransferase 1A	Homo sapiens	246-250
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
23078107-0	2012	Nitro-substituted arene sulfenyl chlorides as precursors to the formation of aromatic SAMs.	nitro-substituted arene sulfenyl chlorides	0-42	methionine adenosyltransferase 1A	Homo sapiens	86-90
23078107-1	2012	The formation of aromatic SAMs on Au(111) using three nitro-substituted arene sulfenyl chlorides (4-nitrophenyl sulfenyl chloride (1), 2-nitrophenyl sulfenyl chloride (2), and 2,4-dinitrophenyl sulfenyl chloride (3)) is studied.	Gold	34-36	methionine adenosyltransferase 1A	Homo sapiens	26-30
23078107-1	2012	The formation of aromatic SAMs on Au(111) using three nitro-substituted arene sulfenyl chlorides (4-nitrophenyl sulfenyl chloride (1), 2-nitrophenyl sulfenyl chloride (2), and 2,4-dinitrophenyl sulfenyl chloride (3)) is studied.	nitro-substituted arene sulfenyl chlorides	54-96	methionine adenosyltransferase 1A	Homo sapiens	26-30
23078107-1	2012	The formation of aromatic SAMs on Au(111) using three nitro-substituted arene sulfenyl chlorides (4-nitrophenyl sulfenyl chloride (1), 2-nitrophenyl sulfenyl chloride (2), and 2,4-dinitrophenyl sulfenyl chloride (3)) is studied.	4-nitrophenyl sulfenyl chloride	98-129	methionine adenosyltransferase 1A	Homo sapiens	26-30
22894534-7	2012	The results indicated that cobaltferritin was selectively immobilised onto succinimidyl alkanedisulfide-modified Au electrode by the covalent interaction between cobaltferritin and the terminal functional groups of the SAMs.	cobaltferritin	27-41	methionine adenosyltransferase 1A	Homo sapiens	219-223
22894534-7	2012	The results indicated that cobaltferritin was selectively immobilised onto succinimidyl alkanedisulfide-modified Au electrode by the covalent interaction between cobaltferritin and the terminal functional groups of the SAMs.	succinimidyl alkanedisulfide	75-103	methionine adenosyltransferase 1A	Homo sapiens	219-223
22894534-7	2012	The results indicated that cobaltferritin was selectively immobilised onto succinimidyl alkanedisulfide-modified Au electrode by the covalent interaction between cobaltferritin and the terminal functional groups of the SAMs.	Gold	113-115	methionine adenosyltransferase 1A	Homo sapiens	219-223
22894534-9	2012	The electrochemically regulated uptake and release of cobalts for cobaltferritin immobilised on the SAMs were demonstrated.	Cobalt	54-61	methionine adenosyltransferase 1A	Homo sapiens	100-104
22717889-2	2012	In this work, we performed systematic analysis with SAMs having various terminal groups (-OEG, -OH, -COOH, -NH(2), and -CH(3)).	Diglycolic acid	90-93	methionine adenosyltransferase 1A	Homo sapiens	52-56
22717889-2	2012	In this work, we performed systematic analysis with SAMs having various terminal groups (-OEG, -OH, -COOH, -NH(2), and -CH(3)).	Carbonic Acid	101-105	methionine adenosyltransferase 1A	Homo sapiens	52-56
22717889-8	2012	The repulsion between OEG-SAMs was always observed independent of solution conditions [NaCl concentration (between 0 and 1 M) and pH (between 3 and 11)] and was not observed in solution mixed with ethanol, which disrupts the three-dimensional network of the water molecules.	Sodium Chloride	87-91	methionine adenosyltransferase 1A	Homo sapiens	26-30
22717889-8	2012	The repulsion between OEG-SAMs was always observed independent of solution conditions [NaCl concentration (between 0 and 1 M) and pH (between 3 and 11)] and was not observed in solution mixed with ethanol, which disrupts the three-dimensional network of the water molecules.	Water	258-263	methionine adenosyltransferase 1A	Homo sapiens	26-30
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
22193356-0	2012	Low-dose methotrexate inhibits methionine S-adenosyltransferase in vitro and in vivo.	Methotrexate	9-21	methionine adenosyltransferase 1A	Homo sapiens	31-63
22499176-3	2012	NO signals have been shown to transcriptionally repress the expression of genes involved in ethylene biosynthesis enzymes and post-translationally modify methionine adenosyl transferase (MAT) activity through S-nitrosylation to reduce the availably of methyl groups required to produce ethylene.	ethylene	286-294	methionine adenosyltransferase 1A	Homo sapiens	154-185
22097883-0	2012	Radical-mediated enzymatic methylation: a tale of two SAMS.	radical	0-7	methionine adenosyltransferase 1A	Homo sapiens	54-58
22499176-3	2012	NO signals have been shown to transcriptionally repress the expression of genes involved in ethylene biosynthesis enzymes and post-translationally modify methionine adenosyl transferase (MAT) activity through S-nitrosylation to reduce the availably of methyl groups required to produce ethylene.	ethylene	286-294	methionine adenosyltransferase 1A	Homo sapiens	187-190
22044068-8	2011	Furthermore, a pronounced maximum in SFG intensity of the C(60) band is observed for SAMs, which are deposited from solutions with ~75% C(60)C(18)-PA and ~25% FC(12)-PA.	Protactinium	145-149	methionine adenosyltransferase 1A	Homo sapiens	85-89
21185701-0	2012	MAT1A variants modulate the effect of dietary fatty acids on plasma homocysteine concentrations.	dietary fatty acids	38-57	methionine adenosyltransferase 1A	Homo sapiens	0-5
21185701-0	2012	MAT1A variants modulate the effect of dietary fatty acids on plasma homocysteine concentrations.	Homocysteine	68-80	methionine adenosyltransferase 1A	Homo sapiens	0-5
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.	Methionine	14-24	methionine adenosyltransferase 1A	Homo sapiens	44-49
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
22260268-7	2012	CONCLUSIONS: Our results suggest that DHA up-regulates CSE and MTHFR mRNA expression and down-regulates MAT mRNA expression involved in Hcy metabolism.	Docosahexaenoic Acids	38-41	methionine adenosyltransferase 1A	Homo sapiens	104-107
21999956-4	2012	Our results show that the surface free energy is higher for PAMAM coatings than for analogously terminated SAMs and also higher for carboxyl than amine functionalized coatings.	Poly(amidoamine)	60-65	methionine adenosyltransferase 1A	Homo sapiens	107-111
22724053-14	2012	The MAT1A genetic polymorphism may impact plasma SAM concentrations in men with low plasma methionine concentrations.	Methionine	91-101	methionine adenosyltransferase 1A	Homo sapiens	4-9
23430947-2	2012	One case was confirmed to be a deficiency of cystathionine beta-synthase and 20 cases were confirmed by MAT1A gene analysis to have an elevation of methionine due to MAT I/III deficiency, which indicates an incidence for this condition of 1/26,000.	Methionine	148-158	methionine adenosyltransferase 1A	Homo sapiens	104-109
22353776-0	2012	Pravastatin inhibits cell proliferation and increased MAT1A expression in hepatocarcinoma cells and in vivo models.	Pravastatin	0-11	methionine adenosyltransferase 1A	Homo sapiens	54-59
22353776-8	2012	The MAT1A levels, was significantly higher in Pravastatin group (D 62%, P 94%, S 71%, P + S 91%).	Pravastatin	46-57	methionine adenosyltransferase 1A	Homo sapiens	4-9
22229807-10	2012	The use of reactive boron hydride SAMs as templates on which further chemistry may be carried out is unprecedented, and the principle may be extended to other binary boron hydride clusters.	Boranes	20-33	methionine adenosyltransferase 1A	Homo sapiens	34-38
22229807-10	2012	The use of reactive boron hydride SAMs as templates on which further chemistry may be carried out is unprecedented, and the principle may be extended to other binary boron hydride clusters.	Boranes	166-179	methionine adenosyltransferase 1A	Homo sapiens	34-38
22044068-8	2011	Furthermore, a pronounced maximum in SFG intensity of the C(60) band is observed for SAMs, which are deposited from solutions with ~75% C(60)C(18)-PA and ~25% FC(12)-PA.	Protactinium	164-168	methionine adenosyltransferase 1A	Homo sapiens	85-89
21986883-2	2011	We studied the crystallization of DL-glutamic acid on chiral self-assembled monolayers and showed that crystallization of DL-glutamic acid on the chiral SAMs resulted in stabilization of the metastable conglomerate form.	Glutamic Acid	34-50	methionine adenosyltransferase 1A	Homo sapiens	153-157
21994917-0	2011	An electrochemical platform for acetylcholinesterase activity assay and inhibitors screening based on Michael addition reaction between thiocholine and catechol-terminated SAMs.	Thiocholine	136-147	methionine adenosyltransferase 1A	Homo sapiens	172-176
21994917-0	2011	An electrochemical platform for acetylcholinesterase activity assay and inhibitors screening based on Michael addition reaction between thiocholine and catechol-terminated SAMs.	catechol	152-160	methionine adenosyltransferase 1A	Homo sapiens	172-176
21994917-1	2011	An electrochemical platform for acetylcholinesterase (AChE) activity assay and its inhibitors screening is developed based on the Michael addition reaction of thiocholine, the hydrolysis product of acetylthiocholine (AsCh) in the presence of AChE, with the electrogenerated o-quinone of catechol-terminated SAMs on a gold electrode.	Thiocholine	159-170	methionine adenosyltransferase 1A	Homo sapiens	307-311
21994917-1	2011	An electrochemical platform for acetylcholinesterase (AChE) activity assay and its inhibitors screening is developed based on the Michael addition reaction of thiocholine, the hydrolysis product of acetylthiocholine (AsCh) in the presence of AChE, with the electrogenerated o-quinone of catechol-terminated SAMs on a gold electrode.	asch	217-221	methionine adenosyltransferase 1A	Homo sapiens	307-311
21994917-2	2011	For understanding and confirming the mechanism of the reaction, the electrochemical behaviors of Michael addition reaction of two model compounds, cysteine (CYS) and glutathione (GSH), towards the catechol-terminated SAMs have been studied.	Cysteine	147-155	methionine adenosyltransferase 1A	Homo sapiens	217-221
21994917-2	2011	For understanding and confirming the mechanism of the reaction, the electrochemical behaviors of Michael addition reaction of two model compounds, cysteine (CYS) and glutathione (GSH), towards the catechol-terminated SAMs have been studied.	Cysteine	157-160	methionine adenosyltransferase 1A	Homo sapiens	217-221
21994917-2	2011	For understanding and confirming the mechanism of the reaction, the electrochemical behaviors of Michael addition reaction of two model compounds, cysteine (CYS) and glutathione (GSH), towards the catechol-terminated SAMs have been studied.	Glutathione	166-177	methionine adenosyltransferase 1A	Homo sapiens	217-221
21994917-2	2011	For understanding and confirming the mechanism of the reaction, the electrochemical behaviors of Michael addition reaction of two model compounds, cysteine (CYS) and glutathione (GSH), towards the catechol-terminated SAMs have been studied.	Glutathione	179-182	methionine adenosyltransferase 1A	Homo sapiens	217-221
21994917-2	2011	For understanding and confirming the mechanism of the reaction, the electrochemical behaviors of Michael addition reaction of two model compounds, cysteine (CYS) and glutathione (GSH), towards the catechol-terminated SAMs have been studied.	catechol	197-205	methionine adenosyltransferase 1A	Homo sapiens	217-221
21986883-2	2011	We studied the crystallization of DL-glutamic acid on chiral self-assembled monolayers and showed that crystallization of DL-glutamic acid on the chiral SAMs resulted in stabilization of the metastable conglomerate form.	Glutamic Acid	122-138	methionine adenosyltransferase 1A	Homo sapiens	153-157
21970561-1	2011	Long-range-ordered aromatic SAMs are formed on Au(111) using 4-nitrophenyl sulfenyl chloride as a precursor.	Gold	47-49	methionine adenosyltransferase 1A	Homo sapiens	28-32
21955058-5	2011	Without any external perturbation, in oligopyrimidine SAMs one encounters an energy gradient that is generated by the dipole moments of the pyrimidine repeat units.	oligopyrimidine	38-53	methionine adenosyltransferase 1A	Homo sapiens	54-58
21955058-5	2011	Without any external perturbation, in oligopyrimidine SAMs one encounters an energy gradient that is generated by the dipole moments of the pyrimidine repeat units.	pyrimidine	43-53	methionine adenosyltransferase 1A	Homo sapiens	54-58
21970561-1	2011	Long-range-ordered aromatic SAMs are formed on Au(111) using 4-nitrophenyl sulfenyl chloride as a precursor.	4-nitrophenyl sulfenyl chloride	61-92	methionine adenosyltransferase 1A	Homo sapiens	28-32
21757254-1	2011	S-Adenosyl-l-methionine synthetase (SAMS) [EC 2.5.1.6] catalyzes to produce SAM (S-adenosyl-l-methionine), a universal methyl group donor in biochemical reactions in cells.	sam (s-adenosyl-l-methionine	76-104	methionine adenosyltransferase 1A	Homo sapiens	0-34
21757254-1	2011	S-Adenosyl-l-methionine synthetase (SAMS) [EC 2.5.1.6] catalyzes to produce SAM (S-adenosyl-l-methionine), a universal methyl group donor in biochemical reactions in cells.	sam (s-adenosyl-l-methionine	76-104	methionine adenosyltransferase 1A	Homo sapiens	36-40
22400342-2	2011	The possibility of using as-obtained APTMS SAMs for anchoring functional molecular moieties is then studied with fullerene C60.	Fullerenes	113-122	methionine adenosyltransferase 1A	Homo sapiens	43-47
21703681-6	2011	The quantification of unspecific and specific protein binding to mixed SAMs showed increased adsorption of albumin with increasing benzylguanine/(ethylene glycol) ratios.	2-(benzylamino)-9H-purin-6-ol	131-144	methionine adenosyltransferase 1A	Homo sapiens	71-75
21703681-6	2011	The quantification of unspecific and specific protein binding to mixed SAMs showed increased adsorption of albumin with increasing benzylguanine/(ethylene glycol) ratios.	Ethylene Glycol	146-161	methionine adenosyltransferase 1A	Homo sapiens	71-75
22400342-6	2011	We show that those APTMS SAMs can be used to graft C60 molecules deposited from a solution and forming about one monolayer anchored on amine terminal moieties.	Amines	135-140	methionine adenosyltransferase 1A	Homo sapiens	25-29
21946612-7	2011	Our results illustrate the importance of crystal edges and grain boundaries in interface chemistry and have broad implications for the application of thiol-based SAMs, ranging from nanomechanical sensors to coating technologies.	Sulfhydryl Compounds	150-155	methionine adenosyltransferase 1A	Homo sapiens	162-166
21812419-1	2011	Azobenzene-based self-assembled monolayers (azo-SAMs) are photoactive and become orientationally ordered when illuminated with linearly polarized light (LPL), making them attractive as dynamic alignment layers in liquid crystal cells.	azobenzene	0-10	methionine adenosyltransferase 1A	Homo sapiens	48-52
21812419-5	2011	Azo-SAMs in an argon atmosphere, in contrast, are chemically stable and remain photoactive even after exposure to CPL.	Argon	15-20	methionine adenosyltransferase 1A	Homo sapiens	4-8
21711048-2	2011	The degree of adhesion resistance is comparable to that achieved with the self-assembled monolayers, SAMs, of oligo(ethylene glycol) alkanethiolates.	oligo(ethylene glycol) alkanethiolates	110-148	methionine adenosyltransferase 1A	Homo sapiens	101-105
21812419-5	2011	Azo-SAMs in an argon atmosphere, in contrast, are chemically stable and remain photoactive even after exposure to CPL.	cpl	114-117	methionine adenosyltransferase 1A	Homo sapiens	4-8
21601214-1	2011	We have developed a novel strategy to generate self-assembled monolayer microarray (SAMs-Array) of alkanethiolates on gold surfaces for the study of human mesenchymal stem cells (hMSCs) differentiation.	alkanethiolates	99-114	methionine adenosyltransferase 1A	Homo sapiens	84-88
21663587-7	2011	The addition of DHA and VP16, in comparison to VP16 added alone, resulted in marked suppression in the expression of several genes involved in DNA damage repair, cell proliferation, survival, invasion, and angiogenesis, including PRKDC, Survivin, PIK3R1, MAPK14, NFkappaB1, NFkappaBIA, BCL2, CD44, and MAT1.	Docosahexaenoic Acids	16-19	methionine adenosyltransferase 1A	Homo sapiens	302-306
21108044-6	2011	Real-time PCR indicated that gene expression of MAT1A, MAT2A and DNMT1 were lower in IUGR piglets but could be elevated by maternal folic acid supplementation.	Folic Acid	132-142	methionine adenosyltransferase 1A	Homo sapiens	48-53
21321707-1	2011	Soft attachment of streptavidin to beta-cyclodextrin-modified pegylated SAMs was efficiently performed in a reversible and repetitive way via orthogonal bifunctional linkers involving streptavidin-biotin recognition and redox-driven multivalent host-guest (beta-cyclodextrin-ferrocene) interactions.	betadex	35-52	methionine adenosyltransferase 1A	Homo sapiens	72-76
21682261-2	2011	The method is based on exchange reactions between Fe(II)bis-terpyridine complexed SAMs and ssDNA-ttpy, and allows efficient hybrydization of the cDNA strands.	fe(ii)bis-terpyridine complexed	50-81	methionine adenosyltransferase 1A	Homo sapiens	82-86
21534549-0	2011	Detection of 2,4-dinitrotoluene (DNT) as a model system for nitroaromatic compounds via molecularly imprinted short-alkyl-chain SAMs.	2,4-dinitrotoluene	13-31	methionine adenosyltransferase 1A	Homo sapiens	128-132
21534549-0	2011	Detection of 2,4-dinitrotoluene (DNT) as a model system for nitroaromatic compounds via molecularly imprinted short-alkyl-chain SAMs.	2,4-dinitrotoluene	33-36	methionine adenosyltransferase 1A	Homo sapiens	128-132
21534549-0	2011	Detection of 2,4-dinitrotoluene (DNT) as a model system for nitroaromatic compounds via molecularly imprinted short-alkyl-chain SAMs.	nitroaromatic	60-73	methionine adenosyltransferase 1A	Homo sapiens	128-132
21534549-5	2011	A switching mechanism was invoked on the basis of the ability of the template analyte to alter the packing arrangement of the alkylthiol SAMs near defect sites as influenced by the DNT-ethanol solvent complex.	alkylthiol	126-136	methionine adenosyltransferase 1A	Homo sapiens	137-141
21534549-5	2011	A switching mechanism was invoked on the basis of the ability of the template analyte to alter the packing arrangement of the alkylthiol SAMs near defect sites as influenced by the DNT-ethanol solvent complex.	2,4-dinitrotoluene	181-184	methionine adenosyltransferase 1A	Homo sapiens	137-141
21534549-5	2011	A switching mechanism was invoked on the basis of the ability of the template analyte to alter the packing arrangement of the alkylthiol SAMs near defect sites as influenced by the DNT-ethanol solvent complex.	Ethanol	185-192	methionine adenosyltransferase 1A	Homo sapiens	137-141
21504221-3	2011	The catalytic polyurethane-acrylate stamp was used to form micrometer-scale features of chemically distinct SAMs on germanium.	Polyurethanes	14-26	methionine adenosyltransferase 1A	Homo sapiens	108-112
21504221-3	2011	The catalytic polyurethane-acrylate stamp was used to form micrometer-scale features of chemically distinct SAMs on germanium.	acrylic acid	27-35	methionine adenosyltransferase 1A	Homo sapiens	108-112
21603069-5	2011	For the C16 COOH-SAMs, as the size of AuNPs decreased the XPS C/Au atomic ratio and the apparent SAM thickness increased due to the increased curvature of the smaller AuNPs.	Carbonic Acid	12-16	methionine adenosyltransferase 1A	Homo sapiens	17-21
21603069-6	2011	The C16 COOH-SAMs on the flat Au had the lowest XPS C/Au atomic ratio and apparent SAM thickness of any C16 COOH-SAM covered Au surface.	Carbonic Acid	8-12	methionine adenosyltransferase 1A	Homo sapiens	13-17
21603069-6	2011	The C16 COOH-SAMs on the flat Au had the lowest XPS C/Au atomic ratio and apparent SAM thickness of any C16 COOH-SAM covered Au surface.	Carbonic Acid	108-112	methionine adenosyltransferase 1A	Homo sapiens	13-17
21603069-12	2011	Fourier transform IR spectroscopy in the attenuated total reflectance mode (FTIR-ATR) was used to characterize the crystallinity of the COOH-SAMs.	Carbonic Acid	136-140	methionine adenosyltransferase 1A	Homo sapiens	141-145
21321707-1	2011	Soft attachment of streptavidin to beta-cyclodextrin-modified pegylated SAMs was efficiently performed in a reversible and repetitive way via orthogonal bifunctional linkers involving streptavidin-biotin recognition and redox-driven multivalent host-guest (beta-cyclodextrin-ferrocene) interactions.	Biotin	197-203	methionine adenosyltransferase 1A	Homo sapiens	72-76
21321707-1	2011	Soft attachment of streptavidin to beta-cyclodextrin-modified pegylated SAMs was efficiently performed in a reversible and repetitive way via orthogonal bifunctional linkers involving streptavidin-biotin recognition and redox-driven multivalent host-guest (beta-cyclodextrin-ferrocene) interactions.	betadex	257-274	methionine adenosyltransferase 1A	Homo sapiens	72-76
21321707-1	2011	Soft attachment of streptavidin to beta-cyclodextrin-modified pegylated SAMs was efficiently performed in a reversible and repetitive way via orthogonal bifunctional linkers involving streptavidin-biotin recognition and redox-driven multivalent host-guest (beta-cyclodextrin-ferrocene) interactions.	ferrocene	275-284	methionine adenosyltransferase 1A	Homo sapiens	72-76
21041070-4	2011	Exposure to bovine serum albumin (BSA) shows the self-limiting (d=1.2nm) [S(EO)(6)](2) SAMs to be the most highly protein resistant surfaces relative to bare Au and completely-formed SAMs of the two analogous thiols and octadecanethiol (ODT).	Sulfhydryl Compounds	209-215	methionine adenosyltransferase 1A	Homo sapiens	87-91
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
21041070-4	2011	Exposure to bovine serum albumin (BSA) shows the self-limiting (d=1.2nm) [S(EO)(6)](2) SAMs to be the most highly protein resistant surfaces relative to bare Au and completely-formed SAMs of the two analogous thiols and octadecanethiol (ODT).	n-octadecyl mercaptan	220-235	methionine adenosyltransferase 1A	Homo sapiens	87-91
21041070-4	2011	Exposure to bovine serum albumin (BSA) shows the self-limiting (d=1.2nm) [S(EO)(6)](2) SAMs to be the most highly protein resistant surfaces relative to bare Au and completely-formed SAMs of the two analogous thiols and octadecanethiol (ODT).	n-octadecyl mercaptan	237-240	methionine adenosyltransferase 1A	Homo sapiens	87-91
21214203-6	2011	For multilayer SAMs assembled from short alkane chains with six methylene groups, we find that molecules in the incomplete adlayer organize themselves randomly over the underlying monolayer.	Alkanes	41-47	methionine adenosyltransferase 1A	Homo sapiens	15-19
21166385-0	2011	Orthogonally reactive SAMs as a general platform for bifunctional silica surfaces.	Silicon Dioxide	66-72	methionine adenosyltransferase 1A	Homo sapiens	22-26
20949962-4	2010	From DFT data, the positive charge on the Au topmost surface atoms is markedly smaller than that found for Au atoms in alkanethiolate SAMs.	Gold	42-44	methionine adenosyltransferase 1A	Homo sapiens	134-138
20949962-4	2010	From DFT data, the positive charge on the Au topmost surface atoms is markedly smaller than that found for Au atoms in alkanethiolate SAMs.	alkanethiolate	119-133	methionine adenosyltransferase 1A	Homo sapiens	134-138
20890492-6	2010	From a theoretical perspective, molecular dynamics (MD) simulations of CO(2) + fluorinated self-assembled monolayer surface (F-SAMs) yield translational probability distributions that are also compared with experimental results.	co(2) +	71-78	methionine adenosyltransferase 1A	Homo sapiens	127-131
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
21461313-0	2010	Reduction of 3T3 Fibroblast Adhesion on SS316L by Methyl-Terminated SAMs.	ss316l	40-46	methionine adenosyltransferase 1A	Homo sapiens	68-72
20830428-0	2010	Generation of surface-confined catechol terminated SAMs via electrochemically triggered Michael addition: characterization, electrochemistry and complex with Ni(II) and Cu(II) cations.	catechol	31-39	methionine adenosyltransferase 1A	Homo sapiens	51-55
20830428-0	2010	Generation of surface-confined catechol terminated SAMs via electrochemically triggered Michael addition: characterization, electrochemistry and complex with Ni(II) and Cu(II) cations.	Nickel(2+)	158-164	methionine adenosyltransferase 1A	Homo sapiens	51-55
20830428-0	2010	Generation of surface-confined catechol terminated SAMs via electrochemically triggered Michael addition: characterization, electrochemistry and complex with Ni(II) and Cu(II) cations.	cu(ii)	169-175	methionine adenosyltransferase 1A	Homo sapiens	51-55
20830428-3	2010	The catechol-terminated SAMs, via electrochemically triggered Michael addition reaction, exhibit reversible redox response.	catechol	4-12	methionine adenosyltransferase 1A	Homo sapiens	24-28
20830428-4	2010	In addition, we find that catechol-terminated SAMs can complex with Ni(2+) and Cu(2+) with different electrochemical behaviors.	catechol	26-34	methionine adenosyltransferase 1A	Homo sapiens	46-50
20830428-4	2010	In addition, we find that catechol-terminated SAMs can complex with Ni(2+) and Cu(2+) with different electrochemical behaviors.	Nickel(2+)	68-74	methionine adenosyltransferase 1A	Homo sapiens	46-50
20830428-4	2010	In addition, we find that catechol-terminated SAMs can complex with Ni(2+) and Cu(2+) with different electrochemical behaviors.	cupric ion	79-85	methionine adenosyltransferase 1A	Homo sapiens	46-50
20830428-5	2010	Moreover, the mechanism of complexation of Ni(2+)and Cu(2+) with catechol-terminated SAMs is also demonstrated with electrochemical and spectrometric methods.	Nickel(2+)	43-49	methionine adenosyltransferase 1A	Homo sapiens	85-89
20830428-5	2010	Moreover, the mechanism of complexation of Ni(2+)and Cu(2+) with catechol-terminated SAMs is also demonstrated with electrochemical and spectrometric methods.	cupric ion	53-59	methionine adenosyltransferase 1A	Homo sapiens	85-89
20830428-5	2010	Moreover, the mechanism of complexation of Ni(2+)and Cu(2+) with catechol-terminated SAMs is also demonstrated with electrochemical and spectrometric methods.	catechol	65-73	methionine adenosyltransferase 1A	Homo sapiens	85-89
20830428-6	2010	Based on the different electrochemical behaviors of Cu(2+) and Ni(2+) complex, the catechol-terminated SAMs provide a potential platform for metal ions recognition.	cupric ion	52-58	methionine adenosyltransferase 1A	Homo sapiens	103-107
20830428-6	2010	Based on the different electrochemical behaviors of Cu(2+) and Ni(2+) complex, the catechol-terminated SAMs provide a potential platform for metal ions recognition.	Nickel(2+)	63-69	methionine adenosyltransferase 1A	Homo sapiens	103-107
20830428-6	2010	Based on the different electrochemical behaviors of Cu(2+) and Ni(2+) complex, the catechol-terminated SAMs provide a potential platform for metal ions recognition.	catechol	83-91	methionine adenosyltransferase 1A	Homo sapiens	103-107
20830428-6	2010	Based on the different electrochemical behaviors of Cu(2+) and Ni(2+) complex, the catechol-terminated SAMs provide a potential platform for metal ions recognition.	Metals	141-146	methionine adenosyltransferase 1A	Homo sapiens	103-107
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
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.	Sulfonium	221-234	methionine adenosyltransferase 1A	Homo sapiens	111-116
20675163-3	2010	During the past 15years 28 MAT1A mutations have been described in patients with elevated plasma methionines, total homocysteines at most only moderately elevated, and normal levels of tyrosine and other aminoacids.	Methionine	96-107	methionine adenosyltransferase 1A	Homo sapiens	27-32
20675163-3	2010	During the past 15years 28 MAT1A mutations have been described in patients with elevated plasma methionines, total homocysteines at most only moderately elevated, and normal levels of tyrosine and other aminoacids.	Tyrosine	184-192	methionine adenosyltransferase 1A	Homo sapiens	27-32
20718464-2	2010	It was found that hemicyanine thiolate SAMs mainly form in the upper hemisphere region of the gold nanospheres in the early stage, followed by the additional SAM formation in the lower region of gold nanospheres.	hemicyanine thiolate	18-38	methionine adenosyltransferase 1A	Homo sapiens	39-43
20586451-7	2010	The immobilization of a cell adhesive Arg-Gly-Asp (RGD)-ketone peptide to the SPREAD stamped oxyamine-alkanethiol SAMs provides a stable interfacial oxime linkage for biospecific studies of cell adhesion, polarity, and migration.	arg-gly-asp (rgd)	38-55	methionine adenosyltransferase 1A	Homo sapiens	114-118
20715271-0	2010	Metallization of ultra-thin, non-thiol SAMs with flat-lying molecular units: Pd on 1, 4-dicyanobenzene.	Sulfhydryl Compounds	33-38	methionine adenosyltransferase 1A	Homo sapiens	39-43
20715271-0	2010	Metallization of ultra-thin, non-thiol SAMs with flat-lying molecular units: Pd on 1, 4-dicyanobenzene.	1,4-dicyanobenzene	83-102	methionine adenosyltransferase 1A	Homo sapiens	39-43
20532327-8	2010	However, SAMs which are still crystalline in air, but less perfect, show rather amorphous spectral features under aqueous conditions indicating a strong interaction with water.	Water	170-175	methionine adenosyltransferase 1A	Homo sapiens	9-13
20701392-1	2010	Ferrocene-terminated self-assembled monolayers (Fc-SAMs) are one of the most studied molecular aggregates on metal electrodes.	ferrocene	0-9	methionine adenosyltransferase 1A	Homo sapiens	51-55
20701392-4	2010	Mixed SAMs were fabricated by coimmobilization on Au electrodes of thiolated alkane chains with three different head groups: hydroxy terminating head group, ferrocene head group, and a functional head group such as biotin.	Gold	50-52	methionine adenosyltransferase 1A	Homo sapiens	6-10
20701392-4	2010	Mixed SAMs were fabricated by coimmobilization on Au electrodes of thiolated alkane chains with three different head groups: hydroxy terminating head group, ferrocene head group, and a functional head group such as biotin.	Alkanes	77-83	methionine adenosyltransferase 1A	Homo sapiens	6-10
20586451-7	2010	The immobilization of a cell adhesive Arg-Gly-Asp (RGD)-ketone peptide to the SPREAD stamped oxyamine-alkanethiol SAMs provides a stable interfacial oxime linkage for biospecific studies of cell adhesion, polarity, and migration.	Ketones	56-62	methionine adenosyltransferase 1A	Homo sapiens	114-118
20586451-7	2010	The immobilization of a cell adhesive Arg-Gly-Asp (RGD)-ketone peptide to the SPREAD stamped oxyamine-alkanethiol SAMs provides a stable interfacial oxime linkage for biospecific studies of cell adhesion, polarity, and migration.	Mechlorethamine	93-101	methionine adenosyltransferase 1A	Homo sapiens	114-118
20586451-7	2010	The immobilization of a cell adhesive Arg-Gly-Asp (RGD)-ketone peptide to the SPREAD stamped oxyamine-alkanethiol SAMs provides a stable interfacial oxime linkage for biospecific studies of cell adhesion, polarity, and migration.	alkanethiol	102-113	methionine adenosyltransferase 1A	Homo sapiens	114-118
20552121-4	2010	SAMs of 17 were demonstrated to sense the perrhenate anion in aqueous solutions.	perrhenate anion	42-58	methionine adenosyltransferase 1A	Homo sapiens	0-4
20417075-3	2010	In this study, two different series of mixed SAMs prepared by lab-synthesized sulfonic acid terminated alkanethiol with hydrophobic -CH(3) or hydrophilic -OH terminated one were characterized.	Sulfonic Acids	78-91	methionine adenosyltransferase 1A	Homo sapiens	45-49
20417075-3	2010	In this study, two different series of mixed SAMs prepared by lab-synthesized sulfonic acid terminated alkanethiol with hydrophobic -CH(3) or hydrophilic -OH terminated one were characterized.	alkanethiol	103-114	methionine adenosyltransferase 1A	Homo sapiens	45-49
20417075-4	2010	It was noted that the surface hydrophilicity of -SO(3)H/-CH(3) mixed SAMs was increased with the solution mole fraction of -SO(3)H terminated thiol.	Sulfhydryl Compounds	142-147	methionine adenosyltransferase 1A	Homo sapiens	69-73
20703376-2	2010	SAMs can be readily formed from thiols prepared by in situ deprotection of the thioacetates in the presence of a gold-coated silicon wafer.	Sulfhydryl Compounds	32-38	methionine adenosyltransferase 1A	Homo sapiens	0-4
20703376-2	2010	SAMs can be readily formed from thiols prepared by in situ deprotection of the thioacetates in the presence of a gold-coated silicon wafer.	thioacetates	79-91	methionine adenosyltransferase 1A	Homo sapiens	0-4
20703376-2	2010	SAMs can be readily formed from thiols prepared by in situ deprotection of the thioacetates in the presence of a gold-coated silicon wafer.	Silicon	125-132	methionine adenosyltransferase 1A	Homo sapiens	0-4
20432412-0	2010	Synthesis of benzaldehyde-functionalized glycans: a novel approach towards glyco-SAMs as a tool for surface plasmon resonance studies.	benzaldehyde	13-25	methionine adenosyltransferase 1A	Homo sapiens	81-85
20586413-6	2010	Formation of enediyne SAMs on a template followed by the processing sequence developed in this work is promising to construct carbon materials with various nanoscopic morphology, such as carbon nanotube, graphene, and giant fullerene.	Carbon	126-132	methionine adenosyltransferase 1A	Homo sapiens	22-26
20586413-6	2010	Formation of enediyne SAMs on a template followed by the processing sequence developed in this work is promising to construct carbon materials with various nanoscopic morphology, such as carbon nanotube, graphene, and giant fullerene.	Carbon	187-193	methionine adenosyltransferase 1A	Homo sapiens	22-26
20586413-6	2010	Formation of enediyne SAMs on a template followed by the processing sequence developed in this work is promising to construct carbon materials with various nanoscopic morphology, such as carbon nanotube, graphene, and giant fullerene.	Graphite	204-212	methionine adenosyltransferase 1A	Homo sapiens	22-26
20586413-6	2010	Formation of enediyne SAMs on a template followed by the processing sequence developed in this work is promising to construct carbon materials with various nanoscopic morphology, such as carbon nanotube, graphene, and giant fullerene.	Fullerenes	224-233	methionine adenosyltransferase 1A	Homo sapiens	22-26
20432412-0	2010	Synthesis of benzaldehyde-functionalized glycans: a novel approach towards glyco-SAMs as a tool for surface plasmon resonance studies.	Polysaccharides	41-48	methionine adenosyltransferase 1A	Homo sapiens	81-85
20450146-3	2010	The driving force to form highly ordered SAMs is packing of the liquid crystalline molecules caused by the interactions between the linear alkane moieties and the pi-pi stacking of the conjugated thiophene units.	Alkanes	139-145	methionine adenosyltransferase 1A	Homo sapiens	41-45
20450146-3	2010	The driving force to form highly ordered SAMs is packing of the liquid crystalline molecules caused by the interactions between the linear alkane moieties and the pi-pi stacking of the conjugated thiophene units.	Thiophenes	196-205	methionine adenosyltransferase 1A	Homo sapiens	41-45
20402532-2	2010	Reported here is a method by which to construct multifunctional, multilayer, patterned structures, using alkanethiolate SAMs adsorbed on Au, UV photopatterning, and chemoselective covalent bond formation.	alkanethiolate	105-119	methionine adenosyltransferase 1A	Homo sapiens	120-124
20146079-8	2010	Together, these findings suggest that the expression of the MAT1A gene is mediated by C/EBP and is indirectly upregulated by T(3).	Triiodothyronine	125-129	methionine adenosyltransferase 1A	Homo sapiens	60-65
20402532-3	2010	We demonstrate that amide coupling is efficient for producing multilayer structures on -COOH-terminated SAMs, while oxime coupling is efficient for producing multilayer structures on -CHO-terminated SAMs.	Amides	20-25	methionine adenosyltransferase 1A	Homo sapiens	104-108
20402532-3	2010	We demonstrate that amide coupling is efficient for producing multilayer structures on -COOH-terminated SAMs, while oxime coupling is efficient for producing multilayer structures on -CHO-terminated SAMs.	Oximes	116-121	methionine adenosyltransferase 1A	Homo sapiens	199-203
20402532-3	2010	We demonstrate that amide coupling is efficient for producing multilayer structures on -COOH-terminated SAMs, while oxime coupling is efficient for producing multilayer structures on -CHO-terminated SAMs.	CAV protocol	184-187	methionine adenosyltransferase 1A	Homo sapiens	199-203
20407712-0	2010	Relative stability of thiol and selenol based SAMs on Au(111) - exchange experiments.	selenol	32-39	methionine adenosyltransferase 1A	Homo sapiens	46-50
20407712-3	2010	Two main results obtained by these study are: (1) the selenium-based BPnSe/Au(111) series is significantly more stable than their sulfur analogues; (2) a clear odd-even effect exists for the stability of both BPnS/Au(111) and BPnSe/Au(111) SAMs towards exchange processes with the even-numbered systems being less stable.	Selenium	54-62	methionine adenosyltransferase 1A	Homo sapiens	240-244
20407712-3	2010	Two main results obtained by these study are: (1) the selenium-based BPnSe/Au(111) series is significantly more stable than their sulfur analogues; (2) a clear odd-even effect exists for the stability of both BPnS/Au(111) and BPnSe/Au(111) SAMs towards exchange processes with the even-numbered systems being less stable.	bpnse	69-74	methionine adenosyltransferase 1A	Homo sapiens	240-244
20225883-5	2010	The study of thiols with functionalized end groups (-CF(3), -OH, -SH, -COOH, and -NH(2)) gave specific insights in orientation, packing, and structure of the molecules in the SAMs.	Sulfhydryl Compounds	13-19	methionine adenosyltransferase 1A	Homo sapiens	175-179
20407712-3	2010	Two main results obtained by these study are: (1) the selenium-based BPnSe/Au(111) series is significantly more stable than their sulfur analogues; (2) a clear odd-even effect exists for the stability of both BPnS/Au(111) and BPnSe/Au(111) SAMs towards exchange processes with the even-numbered systems being less stable.	Brompheniramine	69-73	methionine adenosyltransferase 1A	Homo sapiens	240-244
20407712-4	2010	The results obtained are discussed in view of previously reported microscopic and spectroscopic data of the same SAMs addressing the issue of the relative stability of S-Au(111) and Se-Au(111) bonding, which is an important factor for the rational design of SAMs.	Gold	168-172	methionine adenosyltransferase 1A	Homo sapiens	113-117
20407712-4	2010	The results obtained are discussed in view of previously reported microscopic and spectroscopic data of the same SAMs addressing the issue of the relative stability of S-Au(111) and Se-Au(111) bonding, which is an important factor for the rational design of SAMs.	se-au	182-187	methionine adenosyltransferase 1A	Homo sapiens	113-117
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
20363925-7	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
20363925-7	2010	Huh7 cells overexpressing MAT1A had higher S-adenosylmethionine levels but lower bromodeoxyuridine incorporation than control cells.	Bromodeoxyuridine	81-98	methionine adenosyltransferase 1A	Homo sapiens	26-31
19839568-2	2010	We demonstrate that PCC, a mild oxidant, can be used to convert hydroxyl-terminated SAMs to aldehydes and decorated with a variety of oxyamine-containing molecules.	Hydroxyl Radical	64-72	methionine adenosyltransferase 1A	Homo sapiens	84-88
20102719-1	2010	BACKGROUND &amp; 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).	Adenosine Monophosphate	12-15	methionine adenosyltransferase 1A	Homo sapiens	199-232
20102719-1	2010	BACKGROUND &amp; 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 &amp; 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
20358901-1	2010	Cu pattern on 3-mercaptopropyltrimethoxysilane self-assembled monolayers (MPTS-SAMs) modified glass substrate was achieved by a combination of hydrophobic treatment through microcontact printing, activation and electroless plating.	Copper	0-2	methionine adenosyltransferase 1A	Homo sapiens	79-83
20358901-1	2010	Cu pattern on 3-mercaptopropyltrimethoxysilane self-assembled monolayers (MPTS-SAMs) modified glass substrate was achieved by a combination of hydrophobic treatment through microcontact printing, activation and electroless plating.	(3-mercaptopropyl)trimethoxysilane	14-46	methionine adenosyltransferase 1A	Homo sapiens	79-83
20358901-2	2010	The MPTS-SAMs modified glass substrate was selectively deactivated by microcontact printing 1-hexadecanethiol ethanol solution.	1-maleimidopyrene-3,6,8-trisulfonate	4-8	methionine adenosyltransferase 1A	Homo sapiens	9-13
20358901-2	2010	The MPTS-SAMs modified glass substrate was selectively deactivated by microcontact printing 1-hexadecanethiol ethanol solution.	1-hexadecanethiol ethanol	92-117	methionine adenosyltransferase 1A	Homo sapiens	9-13
20358901-6	2010	SEM showed that the microstructure of Cu pattern on MPTS-SAMs was in good agreement with the corresponding silicon master with a resolution of 10 microm.	Copper	38-40	methionine adenosyltransferase 1A	Homo sapiens	57-61
20358901-6	2010	SEM showed that the microstructure of Cu pattern on MPTS-SAMs was in good agreement with the corresponding silicon master with a resolution of 10 microm.	Silicon	107-114	methionine adenosyltransferase 1A	Homo sapiens	57-61
20358901-8	2010	The results suggested that microcontact printing deactivating reagents on SAMs is a potential technique for Cu patterns preparation.	Copper	108-110	methionine adenosyltransferase 1A	Homo sapiens	74-78
20379501-2	2010	Silicon substrates are coated with CH(3)-terminated silane SAMs as resists.	Silicon	0-7	methionine adenosyltransferase 1A	Homo sapiens	59-63
20379501-3	2010	A fine beam of Ga(+) ions, applying different doses, damages/removes these SAMs to correspondingly form a pattern containing sets of lines.	Gallium	15-17	methionine adenosyltransferase 1A	Homo sapiens	75-79
20379501-5	2010	The FIB nano-lithographically patterned SAMs are re-filled with an SH-terminated silane SAM.	Silanes	81-87	methionine adenosyltransferase 1A	Homo sapiens	40-44
20020762-0	2010	Fabrication of hierarchical CaCO3 mesoporous spheres: particle-mediated self-organization induced by biphase interfaces and SAMs.	Calcium Carbonate	28-33	methionine adenosyltransferase 1A	Homo sapiens	124-128
19839568-2	2010	We demonstrate that PCC, a mild oxidant, can be used to convert hydroxyl-terminated SAMs to aldehydes and decorated with a variety of oxyamine-containing molecules.	Aldehydes	92-101	methionine adenosyltransferase 1A	Homo sapiens	84-88
19839568-2	2010	We demonstrate that PCC, a mild oxidant, can be used to convert hydroxyl-terminated SAMs to aldehydes and decorated with a variety of oxyamine-containing molecules.	Mechlorethamine	134-142	methionine adenosyltransferase 1A	Homo sapiens	84-88
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
20041682-3	2010	Moreover, the addressability of amino groups within the films was investigated by chemical derivatization of ATPn SAMs with 3,5-bis(trifluoromethyl)phenyl isothiocyanate (ITC) forming fluorinated thiourea ATPn-F films.	3,5-Bis(trifluoromethyl)phenyl isothiocyanate	124-169	methionine adenosyltransferase 1A	Homo sapiens	114-118
20041682-3	2010	Moreover, the addressability of amino groups within the films was investigated by chemical derivatization of ATPn SAMs with 3,5-bis(trifluoromethyl)phenyl isothiocyanate (ITC) forming fluorinated thiourea ATPn-F films.	isothiocyanic acid	171-174	methionine adenosyltransferase 1A	Homo sapiens	114-118
20041682-3	2010	Moreover, the addressability of amino groups within the films was investigated by chemical derivatization of ATPn SAMs with 3,5-bis(trifluoromethyl)phenyl isothiocyanate (ITC) forming fluorinated thiourea ATPn-F films.	Thiourea	196-204	methionine adenosyltransferase 1A	Homo sapiens	114-118
19891457-4	2010	The excess oxygen detected by XPS and the H(3)O(+) signal detected by ToF-SIMS for the SAMs with adsorbed peptides indicated that water molecules are associated with the adsorbed peptides, even under ultrahigh-vacuum conditions.	Water	130-135	methionine adenosyltransferase 1A	Homo sapiens	87-91
20335551-0	2010	MAT1A variants are associated with hypertension, stroke, and markers of DNA damage and are modulated by plasma vitamin B-6 and folate.	Vitamin B 6	111-122	methionine adenosyltransferase 1A	Homo sapiens	0-5
20335551-0	2010	MAT1A variants are associated with hypertension, stroke, and markers of DNA damage and are modulated by plasma vitamin B-6 and folate.	Folic Acid	127-133	methionine adenosyltransferase 1A	Homo sapiens	0-5
20335551-1	2010	BACKGROUND: The S-adenosylmethionine synthetase type 1 (MAT1A) gene encodes a key enzyme in one-carbon nutrient metabolism.	Carbon	96-102	methionine adenosyltransferase 1A	Homo sapiens	16-61
20335551-2	2010	OBJECTIVE: This study aimed to determine the association of MAT1A variants with homocysteine, DNA damage, and cardiovascular disease (CVD).	Homocysteine	80-92	methionine adenosyltransferase 1A	Homo sapiens	60-65
20335551-3	2010	DESIGN: Eight variants of MAT1A were examined for associations with hypertension, stroke, CVD, homocysteine, and DNA damage in 1006 participants of the Boston Puerto Rican Health Study.	Homocysteine	95-107	methionine adenosyltransferase 1A	Homo sapiens	26-31
20335551-8	2010	Furthermore, strong interactions between MAT1A genotypes and vitamin B-6 status were found.	Vitamin B 6	61-72	methionine adenosyltransferase 1A	Homo sapiens	41-46
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).	n-alkyl phosphonic acid	28-51	methionine adenosyltransferase 1A	Homo sapiens	158-162
20126759-0	2010	Pore size and surface charge control in mesoporous TiO(2) using post-grafted SAMs.	mesoporous tio(2)	40-57	methionine adenosyltransferase 1A	Homo sapiens	77-81
20126772-7	2010	We propose that these nanographenes provide plausible building-blocks for the structure of the carbon layers formed by electron irradiation of BPT-SAMs.	Carbon	95-101	methionine adenosyltransferase 1A	Homo sapiens	147-151
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
19950970-3	2010	The approach represents the first example of a soft lithographic printing technique that creates patterns of chemically distinctive SAMs on oxide-free silicon substrates.	Oxides	140-145	methionine adenosyltransferase 1A	Homo sapiens	132-136
19950970-3	2010	The approach represents the first example of a soft lithographic printing technique that creates patterns of chemically distinctive SAMs on oxide-free silicon substrates.	Silicon	151-158	methionine adenosyltransferase 1A	Homo sapiens	132-136
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).	phosphonic acid	53-55	methionine adenosyltransferase 1A	Homo sapiens	158-162
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).	hafnium oxide	88-101	methionine adenosyltransferase 1A	Homo sapiens	158-162
19678633-5	2010	We observed rate constants (k degrees (ET)) of 12-20 s(-1) for the protein at SAMs of shorter alkanethiolates that decays exponentially (beta = 0.9/CH(2) or 0.8/A) at SAMs of longer alkanethiolates (9-11 methylene units) or an estimated distance of 1.23 nm and is representative of classical electronic tunneling behavior over increasing distance.	alkanethiolates	94-109	methionine adenosyltransferase 1A	Homo sapiens	78-82
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).	1,3,3,3-tetrafluoropropene	103-106	methionine adenosyltransferase 1A	Homo sapiens	158-162
19772330-3	2010	It was revealed that the IR dipoles of the band at around 1630 cm(-1), which were almost parallel to the long molecular axis of the adenine ring, were less tilted with respect to the substrate surface in the SAMs with longer chains (n = 9 and 10) in comparison to those with shorter chains (n = 2, 4, and 5).	Adenine	132-139	methionine adenosyltransferase 1A	Homo sapiens	208-212
19678633-5	2010	We observed rate constants (k degrees (ET)) of 12-20 s(-1) for the protein at SAMs of shorter alkanethiolates that decays exponentially (beta = 0.9/CH(2) or 0.8/A) at SAMs of longer alkanethiolates (9-11 methylene units) or an estimated distance of 1.23 nm and is representative of classical electronic tunneling behavior over increasing distance.	alkanethiolates	94-109	methionine adenosyltransferase 1A	Homo sapiens	167-171
19678633-5	2010	We observed rate constants (k degrees (ET)) of 12-20 s(-1) for the protein at SAMs of shorter alkanethiolates that decays exponentially (beta = 0.9/CH(2) or 0.8/A) at SAMs of longer alkanethiolates (9-11 methylene units) or an estimated distance of 1.23 nm and is representative of classical electronic tunneling behavior over increasing distance.	alkanethiolates	182-197	methionine adenosyltransferase 1A	Homo sapiens	78-82
19678633-5	2010	We observed rate constants (k degrees (ET)) of 12-20 s(-1) for the protein at SAMs of shorter alkanethiolates that decays exponentially (beta = 0.9/CH(2) or 0.8/A) at SAMs of longer alkanethiolates (9-11 methylene units) or an estimated distance of 1.23 nm and is representative of classical electronic tunneling behavior over increasing distance.	alkanethiolates	182-197	methionine adenosyltransferase 1A	Homo sapiens	167-171
19791779-1	2010	The thermal stability of SAMs generated from the adsorption of n-octadecanethiol (n-C18), 2-hexadecylpropane-1,3-dithiol (C18C2), 2-hexadecyl-2-methylpropane-1,3-dithiol (C18C3), and 1,1,1-tris(mercaptomethyl)heptadecane (t-C18) on colloidal gold and evaporated "flat" gold was investigated.	n-octadecyl mercaptan	63-80	methionine adenosyltransferase 1A	Homo sapiens	25-29
19950928-0	2010	Inkless microcontact printing on SAMs of Boc- and TBS-protected thiols.	Sulfhydryl Compounds	64-70	methionine adenosyltransferase 1A	Homo sapiens	33-37
19791779-1	2010	The thermal stability of SAMs generated from the adsorption of n-octadecanethiol (n-C18), 2-hexadecylpropane-1,3-dithiol (C18C2), 2-hexadecyl-2-methylpropane-1,3-dithiol (C18C3), and 1,1,1-tris(mercaptomethyl)heptadecane (t-C18) on colloidal gold and evaporated "flat" gold was investigated.	n-c18	82-87	methionine adenosyltransferase 1A	Homo sapiens	25-29
19791779-1	2010	The thermal stability of SAMs generated from the adsorption of n-octadecanethiol (n-C18), 2-hexadecylpropane-1,3-dithiol (C18C2), 2-hexadecyl-2-methylpropane-1,3-dithiol (C18C3), and 1,1,1-tris(mercaptomethyl)heptadecane (t-C18) on colloidal gold and evaporated "flat" gold was investigated.	2-hexadecylpropane-1,3-dithiol	90-120	methionine adenosyltransferase 1A	Homo sapiens	25-29
19791779-1	2010	The thermal stability of SAMs generated from the adsorption of n-octadecanethiol (n-C18), 2-hexadecylpropane-1,3-dithiol (C18C2), 2-hexadecyl-2-methylpropane-1,3-dithiol (C18C3), and 1,1,1-tris(mercaptomethyl)heptadecane (t-C18) on colloidal gold and evaporated "flat" gold was investigated.	c18c2	122-127	methionine adenosyltransferase 1A	Homo sapiens	25-29
19791779-1	2010	The thermal stability of SAMs generated from the adsorption of n-octadecanethiol (n-C18), 2-hexadecylpropane-1,3-dithiol (C18C2), 2-hexadecyl-2-methylpropane-1,3-dithiol (C18C3), and 1,1,1-tris(mercaptomethyl)heptadecane (t-C18) on colloidal gold and evaporated "flat" gold was investigated.	2-hexadecyl-2-methylpropane-1,3-dithiol	130-169	methionine adenosyltransferase 1A	Homo sapiens	25-29
19791779-1	2010	The thermal stability of SAMs generated from the adsorption of n-octadecanethiol (n-C18), 2-hexadecylpropane-1,3-dithiol (C18C2), 2-hexadecyl-2-methylpropane-1,3-dithiol (C18C3), and 1,1,1-tris(mercaptomethyl)heptadecane (t-C18) on colloidal gold and evaporated "flat" gold was investigated.	c18c3	171-176	methionine adenosyltransferase 1A	Homo sapiens	25-29
19791779-1	2010	The thermal stability of SAMs generated from the adsorption of n-octadecanethiol (n-C18), 2-hexadecylpropane-1,3-dithiol (C18C2), 2-hexadecyl-2-methylpropane-1,3-dithiol (C18C3), and 1,1,1-tris(mercaptomethyl)heptadecane (t-C18) on colloidal gold and evaporated "flat" gold was investigated.	1,1,1-tris(mercaptomethyl)heptadecane	183-220	methionine adenosyltransferase 1A	Homo sapiens	25-29
19791779-1	2010	The thermal stability of SAMs generated from the adsorption of n-octadecanethiol (n-C18), 2-hexadecylpropane-1,3-dithiol (C18C2), 2-hexadecyl-2-methylpropane-1,3-dithiol (C18C3), and 1,1,1-tris(mercaptomethyl)heptadecane (t-C18) on colloidal gold and evaporated "flat" gold was investigated.	t-c18	222-227	methionine adenosyltransferase 1A	Homo sapiens	25-29
19791779-5	2010	In these studies, SAMs generated from monodentate n-C18 showed the fastest desorption while SAMs generated from tridentate t-C18 showed the slowest desorption, with those derived from the bidentates C18C2 and C18C3 falling in between, again suggesting a correlation between film stability and the degree of chelation.	1-octadecene	51-55	methionine adenosyltransferase 1A	Homo sapiens	18-22
20042251-8	2010	Benzaldehyde-functionalized glycosides of mono and disaccharides were synthesized by metathesis and could be used for the formation of novel glyco-self assembled monolayers (glyco-SAMs) employing various tether structures and attached to gold surfaces.	benzaldehyde	0-12	methionine adenosyltransferase 1A	Homo sapiens	180-184
20042251-8	2010	Benzaldehyde-functionalized glycosides of mono and disaccharides were synthesized by metathesis and could be used for the formation of novel glyco-self assembled monolayers (glyco-SAMs) employing various tether structures and attached to gold surfaces.	Glycosides	28-38	methionine adenosyltransferase 1A	Homo sapiens	180-184
20042251-8	2010	Benzaldehyde-functionalized glycosides of mono and disaccharides were synthesized by metathesis and could be used for the formation of novel glyco-self assembled monolayers (glyco-SAMs) employing various tether structures and attached to gold surfaces.	mono and disaccharides	42-64	methionine adenosyltransferase 1A	Homo sapiens	180-184
19950928-1	2010	We report a new inkless catalytic muCP technique that achieves accurate, fast, and complete pattern reproduction on SAMs of Boc- and TBS-protected thiols immobilized on gold using a polyurethane-acrylate stamp functionalized with covalently bound sulfonic acids.	Sulfhydryl Compounds	147-153	methionine adenosyltransferase 1A	Homo sapiens	116-120
19950928-1	2010	We report a new inkless catalytic muCP technique that achieves accurate, fast, and complete pattern reproduction on SAMs of Boc- and TBS-protected thiols immobilized on gold using a polyurethane-acrylate stamp functionalized with covalently bound sulfonic acids.	polyurethane-acrylate	182-203	methionine adenosyltransferase 1A	Homo sapiens	116-120
19950928-1	2010	We report a new inkless catalytic muCP technique that achieves accurate, fast, and complete pattern reproduction on SAMs of Boc- and TBS-protected thiols immobilized on gold using a polyurethane-acrylate stamp functionalized with covalently bound sulfonic acids.	Sulfonic Acids	247-261	methionine adenosyltransferase 1A	Homo sapiens	116-120
20024435-0	2009	A multi-technique approach to the analysis of SAMs of aromatic thiols on copper.	aromatic thiols	54-69	methionine adenosyltransferase 1A	Homo sapiens	46-50
20024435-0	2009	A multi-technique approach to the analysis of SAMs of aromatic thiols on copper.	Copper	73-79	methionine adenosyltransferase 1A	Homo sapiens	46-50
19831352-7	2009	Our results demonstrate the key role of the chain length and the procedure (solvent nature and oxygen presence) in controlling the surface structure and chemistry of SAMs dithiols on Au(111).	Oxygen	95-101	methionine adenosyltransferase 1A	Homo sapiens	166-170
19831352-7	2009	Our results demonstrate the key role of the chain length and the procedure (solvent nature and oxygen presence) in controlling the surface structure and chemistry of SAMs dithiols on Au(111).	Gold	183-185	methionine adenosyltransferase 1A	Homo sapiens	166-170
19655797-3	2009	High-performance field-effect transistors based on the Au-NPs-embedded pentacene films can be prepared if the nanoparticles are made "hydrophobic" as well as "oleophobic" by appropriate SAMs.	pentacene	71-80	methionine adenosyltransferase 1A	Homo sapiens	186-190
19762918-7	2009	Depleting SAM in HepG2 cells using MAT1alpha siRNA or cycloleucine resulted in enhanced activation of the UPR upon exposure to thapsigargin.	Thapsigargin	127-139	methionine adenosyltransferase 1A	Homo sapiens	35-44
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
19711923-6	2010	Both, the d-alkane chain and long axis of the OEG part make an angle of 26.0 degrees +/- 1.5 degrees with respect to the surface normal, a value characteristic for the tilt of solid n-alkane thiols in the SAMs on Au.	d-alkane	10-18	methionine adenosyltransferase 1A	Homo sapiens	205-209
19711923-6	2010	Both, the d-alkane chain and long axis of the OEG part make an angle of 26.0 degrees +/- 1.5 degrees with respect to the surface normal, a value characteristic for the tilt of solid n-alkane thiols in the SAMs on Au.	Diglycolic acid	46-49	methionine adenosyltransferase 1A	Homo sapiens	205-209
19711923-6	2010	Both, the d-alkane chain and long axis of the OEG part make an angle of 26.0 degrees +/- 1.5 degrees with respect to the surface normal, a value characteristic for the tilt of solid n-alkane thiols in the SAMs on Au.	n-alkane thiols	182-197	methionine adenosyltransferase 1A	Homo sapiens	205-209
19711923-8	2010	The D-OEG SAMs were exposed to 25 muM Br(2) in two ways: (i) by immersion into the Br(2) solution and (ii) in the galvanic cell Au D-OEG SAM 25 muM Br(2) + 0.1 M Na(2)SO(4)   50 muM KBr + 0.1 M Na(2)SO(4) Au.	Bromine	38-43	methionine adenosyltransferase 1A	Homo sapiens	10-14
19572504-4	2009	Upon the attachment of gold nanoparticles, distinct Faradaic electrochemistry of the ruthenium hexamine was observed for all four length SAMs with the electrochemistry being similar to that observed on a bare electrode.	ruthenium hexamine	85-103	methionine adenosyltransferase 1A	Homo sapiens	137-141
19408903-5	2009	A rather high plasma deposition on SAMs was decreased by grafting PEG chains.	Polyethylene Glycols	66-69	methionine adenosyltransferase 1A	Homo sapiens	35-39
21828453-0	2009	Growth dynamics of L-cysteine SAMs on single-crystal gold surfaces: a metastable deexcitation spectroscopy study.	Cysteine	19-29	methionine adenosyltransferase 1A	Homo sapiens	30-34
19449821-0	2009	Description of ferrocenylalkylthiol SAMs on gold by molecular dynamics simulations.	ferrocenylalkylthiol	15-35	methionine adenosyltransferase 1A	Homo sapiens	36-40
19449821-4	2009	The angular distributions are described in terms of the relative contributions from isolated and clustered ferrocene moieties in the binary SAMs.	ferrocene	107-116	methionine adenosyltransferase 1A	Homo sapiens	140-144
19361929-4	2009	The PFDP/Cu and ODP/Cu SAMs were found to be very hydrophobic having water sessile drop static contact angles of more than 140 degrees , while DP/Cu and OP/Cu have contact angles of 119 degrees and 76 degrees , respectively.	pfdp	4-8	methionine adenosyltransferase 1A	Homo sapiens	23-27
19361929-4	2009	The PFDP/Cu and ODP/Cu SAMs were found to be very hydrophobic having water sessile drop static contact angles of more than 140 degrees , while DP/Cu and OP/Cu have contact angles of 119 degrees and 76 degrees , respectively.	ISODECYL OCTYL PHTHALATE	16-19	methionine adenosyltransferase 1A	Homo sapiens	23-27
19361929-4	2009	The PFDP/Cu and ODP/Cu SAMs were found to be very hydrophobic having water sessile drop static contact angles of more than 140 degrees , while DP/Cu and OP/Cu have contact angles of 119 degrees and 76 degrees , respectively.	Copper	20-22	methionine adenosyltransferase 1A	Homo sapiens	23-27
19361929-4	2009	The PFDP/Cu and ODP/Cu SAMs were found to be very hydrophobic having water sessile drop static contact angles of more than 140 degrees , while DP/Cu and OP/Cu have contact angles of 119 degrees and 76 degrees , respectively.	Water	69-74	methionine adenosyltransferase 1A	Homo sapiens	23-27
19361929-4	2009	The PFDP/Cu and ODP/Cu SAMs were found to be very hydrophobic having water sessile drop static contact angles of more than 140 degrees , while DP/Cu and OP/Cu have contact angles of 119 degrees and 76 degrees , respectively.	Copper	20-22	methionine adenosyltransferase 1A	Homo sapiens	23-27
19361929-4	2009	The PFDP/Cu and ODP/Cu SAMs were found to be very hydrophobic having water sessile drop static contact angles of more than 140 degrees , while DP/Cu and OP/Cu have contact angles of 119 degrees and 76 degrees , respectively.	Copper	20-22	methionine adenosyltransferase 1A	Homo sapiens	23-27
19361929-9	2009	Hydrophobic phosphonate SAMs could be useful as corrosion inhibitors in micro/nanoelectronic devices and/or as promoters for anti-wetting, low adhesion surfaces.	Organophosphonates	12-23	methionine adenosyltransferase 1A	Homo sapiens	24-28
19053491-4	2009	SAMs with different end-groups (-CH(3) and -COOH) were also considered to contrast with the adsorption behavior on the amine-terminated SAM substrates.	Carbonic Acid	44-48	methionine adenosyltransferase 1A	Homo sapiens	0-4
19240929-4	2009	By comparing with the formation of SAMs on a nanostructured gold surface, we demonstrate that cluster deposition through the organic monolayer can be used to control the patterning of a gold surface covered with alkanethiol SAM.	alkanethiol sam	212-227	methionine adenosyltransferase 1A	Homo sapiens	35-39
19199724-3	2009	The resulting ion-pair SAMs exhibit a 1:1 molar ratio of MHA:TAA+ on the surface and are covalently bound to the gold surface through the thiol headgroup of MHA.	Sulfhydryl Compounds	138-143	methionine adenosyltransferase 1A	Homo sapiens	23-27
19138073-2	2009	Studies of the interactions between the designed SAMs and human fibroblast (hTERT-BJ1) cells have been reported, and it was observed that cells attach and spread efficiently for monolayer presenting a terminal aromatic pyrene platform with a polyoxometalate Mn-Anderson cluster as linker, demonstrating the crucial role played by the polyoxometalate metal oxide cluster as an intermediary in cell adhesion to the surface.	aromatic pyrene	210-225	methionine adenosyltransferase 1A	Homo sapiens	49-53
19138073-2	2009	Studies of the interactions between the designed SAMs and human fibroblast (hTERT-BJ1) cells have been reported, and it was observed that cells attach and spread efficiently for monolayer presenting a terminal aromatic pyrene platform with a polyoxometalate Mn-Anderson cluster as linker, demonstrating the crucial role played by the polyoxometalate metal oxide cluster as an intermediary in cell adhesion to the surface.	polyoxometalate metal oxide	334-361	methionine adenosyltransferase 1A	Homo sapiens	49-53
19053491-4	2009	SAMs with different end-groups (-CH(3) and -COOH) were also considered to contrast with the adsorption behavior on the amine-terminated SAM substrates.	Amines	119-124	methionine adenosyltransferase 1A	Homo sapiens	0-4
19117446-3	2009	The specific interaction between thrombin and aptamer could weaken the electrostatic barrier effect from the negative charged aptamer SAMs to the diffusion process of the positively charged CV from the bulk solution to the Au nanoparticle surface.	Gold	223-225	methionine adenosyltransferase 1A	Homo sapiens	134-138
19180612-0	2009	Formation of patches on 3D SAMs driven by thiols with immiscible chains observed by ESR spectroscopy.	Sulfhydryl Compounds	42-48	methionine adenosyltransferase 1A	Homo sapiens	27-31
18849157-2	2009	The channel with an appropriate diameter of about 3A ( approximately 3A) existing in SAMs on Au is deduced, which is found large enough for ions and water molecules to permeate; (2) through summarizing the literature reports for various experiments (e.g. scan microscopy techniques and electrochemical methods, etc.	Water	149-154	methionine adenosyltransferase 1A	Homo sapiens	85-89
18849157-3	2009	), the existence of the ion and water channels ( approximately 3A) in close-packed C(n)SH-SAMs is verified; (3) furthermore, the effect of the ions and water molecules permeation on the studies of the SAMs" electron tunneling process is discussed.	Water	32-37	methionine adenosyltransferase 1A	Homo sapiens	90-94
18849157-3	2009	), the existence of the ion and water channels ( approximately 3A) in close-packed C(n)SH-SAMs is verified; (3) furthermore, the effect of the ions and water molecules permeation on the studies of the SAMs" electron tunneling process is discussed.	Water	152-157	methionine adenosyltransferase 1A	Homo sapiens	90-94
18849157-3	2009	), the existence of the ion and water channels ( approximately 3A) in close-packed C(n)SH-SAMs is verified; (3) furthermore, the effect of the ions and water molecules permeation on the studies of the SAMs" electron tunneling process is discussed.	Water	152-157	methionine adenosyltransferase 1A	Homo sapiens	201-206
18849157-4	2009	This simple ideal model of the close-packed C(n)SH-SAMs established by us may clarify the controversies about the permeation mechanism of ions and water molecules in C(n)SH-SAMs.	Water	147-152	methionine adenosyltransferase 1A	Homo sapiens	51-55
18849157-4	2009	This simple ideal model of the close-packed C(n)SH-SAMs established by us may clarify the controversies about the permeation mechanism of ions and water molecules in C(n)SH-SAMs.	Water	147-152	methionine adenosyltransferase 1A	Homo sapiens	173-177
22573954-2	2009	First, the formation of these SAMs on the nanopillar modified electrodes was characterized by the cyclic voltammetry and electrochemical impedance spectroscopy techniques, and then the detection sensitivity of these functionalized electrodes to glucose was evaluated by the amperometry technique.	Glucose	245-252	methionine adenosyltransferase 1A	Homo sapiens	30-34
18597470-6	2008	The results show that high surface coverage SAMs with low surface-oxide content can be achieved for thin, evaporated Ni and Co films using our electroreduction process with thiols.	Oxides	66-71	methionine adenosyltransferase 1A	Homo sapiens	44-48
18823135-0	2008	Toposelective electrochemical desorption of thiol SAMs from neighboring polycrystalline gold surfaces.	Sulfhydryl Compounds	44-49	methionine adenosyltransferase 1A	Homo sapiens	50-54
18823135-5	2008	In this study operating windows were established for 1-dodecanethiol-based SAMs in phosphate buffer, phosphate-buffered saline, and sodium hydroxide solution, and selective SAM removal was successfully performed in a four-electrode configuration.	dodecylmercaptan	53-68	methionine adenosyltransferase 1A	Homo sapiens	75-79
18823135-5	2008	In this study operating windows were established for 1-dodecanethiol-based SAMs in phosphate buffer, phosphate-buffered saline, and sodium hydroxide solution, and selective SAM removal was successfully performed in a four-electrode configuration.	Phosphates	83-92	methionine adenosyltransferase 1A	Homo sapiens	75-79
18823135-5	2008	In this study operating windows were established for 1-dodecanethiol-based SAMs in phosphate buffer, phosphate-buffered saline, and sodium hydroxide solution, and selective SAM removal was successfully performed in a four-electrode configuration.	Phosphate-Buffered Saline	101-126	methionine adenosyltransferase 1A	Homo sapiens	75-79
18755471-0	2008	Preparation and characterization of asymmetric planar supported bilayers composed of poly(bis-sorbylphosphatidylcholine) on n-octadecyltrichlorosilane SAMs.	poly(bis-sorbyl phosphatidylcholine)	85-120	methionine adenosyltransferase 1A	Homo sapiens	151-155
18690727-7	2008	Finally, we find that E-AB signal gain is sensitive to the nature of the alkanethiol SAM employed to passivate the interrogating electrode; while thinner SAMs lead to higher absolute sensor currents, reducing the length of the SAM from 6-carbons to 2-carbons reduces the observed signal gain of our cocaine sensor 10-fold.	alkanethiol	73-84	methionine adenosyltransferase 1A	Homo sapiens	154-158
18690727-7	2008	Finally, we find that E-AB signal gain is sensitive to the nature of the alkanethiol SAM employed to passivate the interrogating electrode; while thinner SAMs lead to higher absolute sensor currents, reducing the length of the SAM from 6-carbons to 2-carbons reduces the observed signal gain of our cocaine sensor 10-fold.	Carbon	251-258	methionine adenosyltransferase 1A	Homo sapiens	154-158
18690727-7	2008	Finally, we find that E-AB signal gain is sensitive to the nature of the alkanethiol SAM employed to passivate the interrogating electrode; while thinner SAMs lead to higher absolute sensor currents, reducing the length of the SAM from 6-carbons to 2-carbons reduces the observed signal gain of our cocaine sensor 10-fold.	Cocaine	299-306	methionine adenosyltransferase 1A	Homo sapiens	154-158
20408690-6	2008	In this article, the authors review simulations of water at the interface with hydrophilic SAMs.	Water	51-56	methionine adenosyltransferase 1A	Homo sapiens	91-95
20408690-9	2008	SAMs terminated with ethylene glycol monomers have proven to be excellent at resisting protein adsorption.	Ethylene Glycol	21-36	methionine adenosyltransferase 1A	Homo sapiens	0-4
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
18597470-6	2008	The results show that high surface coverage SAMs with low surface-oxide content can be achieved for thin, evaporated Ni and Co films using our electroreduction process with thiols.	Sulfhydryl Compounds	173-179	methionine adenosyltransferase 1A	Homo sapiens	44-48
18471004-3	2008	Octanethiol SAMs vapor deposited in situ onto UHV TS Au show a c(4 x 2) superlattice with (square root 3 x square root 3) R30 degrees basic molecular structure having an ordered domain size up to 100 nm wide.	n-octanethiol	0-11	methionine adenosyltransferase 1A	Homo sapiens	12-16
18211108-2	2008	Through a comparison with standard alkylthiol SAMs deposited on Au(111) flat surfaces, we show that on the vicinal surface the octanethiol monolayer (OT SAM) reproduces the nanopatterned staircase structure, giving rise to a new kind of molecular layer self-ordered on the nanometer scale.	n-octanethiol	127-138	methionine adenosyltransferase 1A	Homo sapiens	46-50
17706871-0	2008	Effect of lateral morphology formation of polymer blend towards patterning silane-based SAMs using selective dissolution method.	Polymers	42-49	methionine adenosyltransferase 1A	Homo sapiens	88-92
17706871-2	2008	Here we have discussed a customized strategy for surface patterning of nanosized, silane-based SAMs and monolayer thickness measurement investigated using atomic force microscope (AFM).	Silanes	82-88	methionine adenosyltransferase 1A	Homo sapiens	95-99
17706871-3	2008	We have utilized the versatile morphology of a binary polymer blend to generate patterned SAMs over silicon substrate by employing a selective dissolution procedure.	Polymers	54-61	methionine adenosyltransferase 1A	Homo sapiens	90-94
17706871-3	2008	We have utilized the versatile morphology of a binary polymer blend to generate patterned SAMs over silicon substrate by employing a selective dissolution procedure.	Silicon	100-107	methionine adenosyltransferase 1A	Homo sapiens	90-94
18452318-1	2008	In this paper we report the use of the optical properties of porous silicon photonic crystals, combined with the chemical versatility of acetylene-terminated SAMs, to demonstrate the applicability of "click" chemistry to mesoporous materials.	Acetylene	137-146	methionine adenosyltransferase 1A	Homo sapiens	158-162
18163611-1	2008	1-methyl-5-aminotetrazole (4, MAT) can easily be protonated by strong acids, yielding known but largely uninvestigated 1-methyl-5-aminotetrazolium nitrate (4a) and perchlorate (4b).	1-methyl-1H-tetrazol-5-amine	0-25	methionine adenosyltransferase 1A	Homo sapiens	30-33
18163611-1	2008	1-methyl-5-aminotetrazole (4, MAT) can easily be protonated by strong acids, yielding known but largely uninvestigated 1-methyl-5-aminotetrazolium nitrate (4a) and perchlorate (4b).	1-methyl-5-aminotetrazolium nitrate	119-154	methionine adenosyltransferase 1A	Homo sapiens	30-33
18163611-1	2008	1-methyl-5-aminotetrazole (4, MAT) can easily be protonated by strong acids, yielding known but largely uninvestigated 1-methyl-5-aminotetrazolium nitrate (4a) and perchlorate (4b).	perchlorate	164-175	methionine adenosyltransferase 1A	Homo sapiens	30-33
18179184-0	2008	Ab initio modeling of defect signatures in infrared reflection-absorption spectra of SAMs exposing methyl- and hydrogen-terminated oligo(ethylene glycols).	Hydrogen	111-119	methionine adenosyltransferase 1A	Homo sapiens	85-89
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
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.	Polyamines	165-175	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.	Polyamines	165-175	methionine adenosyltransferase 1A	Homo sapiens	32-35
18041713-10	2008	Treatment with SAMe or its metabolite methylthioadenosine (MTA) lowered expression of MAT2A and MAT2beta and blocked leptin-induced signaling, including an increase in MAT gene expression and growth.	5'-methylthioadenosine	38-57	methionine adenosyltransferase 1A	Homo sapiens	86-89
18179184-0	2008	Ab initio modeling of defect signatures in infrared reflection-absorption spectra of SAMs exposing methyl- and hydrogen-terminated oligo(ethylene glycols).	Ethylene Glycols	137-153	methionine adenosyltransferase 1A	Homo sapiens	85-89
18179184-1	2008	Extensive ab initio modeling has been performed to explain quantitatively the apparent shapes of characteristic bands, which are systematically observed in the fingerprint region of infrared (IR) reflection-absorption (RA) spectra of oligo(ethylene glycol) (OEG)-terminated SAMs.	Ethylene Glycol	240-256	methionine adenosyltransferase 1A	Homo sapiens	274-278
18179184-1	2008	Extensive ab initio modeling has been performed to explain quantitatively the apparent shapes of characteristic bands, which are systematically observed in the fingerprint region of infrared (IR) reflection-absorption (RA) spectra of oligo(ethylene glycol) (OEG)-terminated SAMs.	Diglycolic acid	258-261	methionine adenosyltransferase 1A	Homo sapiens	274-278
18179184-3	2008	These data were then used to simulate RA spectra of SAMs with different content of defects and to compare them with experiments.	Radium	38-40	methionine adenosyltransferase 1A	Homo sapiens	52-56
18179184-8	2008	For this family of SAMs, the presence of about 10% of all-trans conformers gives a satisfactory quantitative agreement between the calculated RA spectra and experimental observations.	Radium	142-144	methionine adenosyltransferase 1A	Homo sapiens	19-23
18167590-4	2007	The data show the organization of alkanethiol SAMs occurs at approximately the same rate for aliphatic chain lengths in the range of C(9)-C(16), as long as the thiol is readily soluble in the solvent system used.	alkanethiol	34-45	methionine adenosyltransferase 1A	Homo sapiens	46-50
18167590-4	2007	The data show the organization of alkanethiol SAMs occurs at approximately the same rate for aliphatic chain lengths in the range of C(9)-C(16), as long as the thiol is readily soluble in the solvent system used.	Sulfhydryl Compounds	40-45	methionine adenosyltransferase 1A	Homo sapiens	46-50
17326142-4	2007	The contact angle values of NH(2) + COOH mixed SAMs were between those of the pure SAMs, except that it was prepared with solution mole fraction of amine-terminated alkanethiol at 0.2.	alkanethiol	165-176	methionine adenosyltransferase 1A	Homo sapiens	47-51
17912419-1	2007	The influence of conformational and electrical properties of azobenzene molecules on the electron transfer barrier properties of their SAMs was studied by SECM and ellipsometry.	azobenzene	61-71	methionine adenosyltransferase 1A	Homo sapiens	135-139
21817632-10	2008	Then the SiO(2) background was backfilled using poly(L-lysine)-graft-poly(ethylene glycol) and finally streptavidin was adsorbed to the hydrophobic alkane phosphate SAMs, allowing subsequent binding and hybridization of biotinylated DNA.	Silicon Dioxide	9-15	methionine adenosyltransferase 1A	Homo sapiens	165-169
21817632-10	2008	Then the SiO(2) background was backfilled using poly(L-lysine)-graft-poly(ethylene glycol) and finally streptavidin was adsorbed to the hydrophobic alkane phosphate SAMs, allowing subsequent binding and hybridization of biotinylated DNA.	alkane phosphate	148-164	methionine adenosyltransferase 1A	Homo sapiens	165-169
17326142-7	2007	XPS analysis has also revealed that the surface of NH(2) + COOH mixed SAMs was "amine-rich".	Amines	51-56	methionine adenosyltransferase 1A	Homo sapiens	70-74
17326142-7	2007	XPS analysis has also revealed that the surface of NH(2) + COOH mixed SAMs was "amine-rich".	Carbonic Acid	59-63	methionine adenosyltransferase 1A	Homo sapiens	70-74
17326142-7	2007	XPS analysis has also revealed that the surface of NH(2) + COOH mixed SAMs was "amine-rich".	Amines	80-85	methionine adenosyltransferase 1A	Homo sapiens	70-74
17696377-6	2007	This protection allows metal surfaces intended to support SAMs to be prepared in large batch lots, stored, and then used as needed.	Metals	23-28	methionine adenosyltransferase 1A	Homo sapiens	58-62
17665935-0	2007	One-dimensional SAMs of (12-pyrrol-1-yl-dodecyl)-phosphonic acid templated by polyelectrolyte molecules.	(12-pyrrol-1-yl-dodecyl)-phosphonic acid	24-64	methionine adenosyltransferase 1A	Homo sapiens	16-20
17665935-1	2007	We present a novel method for the fabrication of one-dimensional (1-D) self-assembled monolayers and multilayers (SAMs) of (12-pyrrol-1-yl-dodecyl)-phosphonic acid (Py-DPA) on various polar surfaces using polyelectrolyte nanostructures as positive templates.	(12-pyrrol-1-yl-dodecyl)-phosphonic acid	123-163	methionine adenosyltransferase 1A	Homo sapiens	114-118
17665935-1	2007	We present a novel method for the fabrication of one-dimensional (1-D) self-assembled monolayers and multilayers (SAMs) of (12-pyrrol-1-yl-dodecyl)-phosphonic acid (Py-DPA) on various polar surfaces using polyelectrolyte nanostructures as positive templates.	py-dpa	165-171	methionine adenosyltransferase 1A	Homo sapiens	114-118
17665935-2	2007	Particularly, we demonstrate that (i) patterns of aligned 1-D polycation structures on a poly(dimethylsiloxane) stamp can be prepared by moving a droplet of polycation solution along the surface; (ii) these patterns can be used as templates for the ordered assembly of Py-DPA in water where Py-DPA carries a charge opposite to the charge of the template; and (iii) Py-DPA SAMs can then be transferred onto mica or silicon wafers by a printing process.	baysilon	89-111	methionine adenosyltransferase 1A	Homo sapiens	372-376
17631143-1	2007	BACKGROUND &amp; AIMS: Two genes (MAT1A and MAT2A) encode for methionine adenosyltransferase, an essential enzyme responsible for S-adenosylmethionine (SAMe) biosynthesis.	Adenosine Monophosphate	12-15	methionine adenosyltransferase 1A	Homo sapiens	34-39
17603555-5	2007	AMPK activity was measured as the amount of radiolabelled phosphate transferred to the SAMS peptide.	Phosphates	58-67	methionine adenosyltransferase 1A	Homo sapiens	87-91
17631143-1	2007	BACKGROUND &amp; 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
17397195-9	2007	Finally, molecular dynamics studies were used to understand the packing structures of stable polymorphs of thiophene SAMs.	Thiophenes	107-116	methionine adenosyltransferase 1A	Homo sapiens	117-121
17222902-2	2007	N-Methacryloyl-(L)-tyrosinemethylester (MAT) was chosen as the complexing monomer.	n-methacryloyl-(l)-tyrosinemethylester	0-38	methionine adenosyltransferase 1A	Homo sapiens	40-43
17222902-3	2007	In the first step, functional monomer MAT was synthesized by the reaction of L-tyrosine methylester and methacryloyl chloride and characterized by FTIR and NMR.	Tyrosine	77-87	methionine adenosyltransferase 1A	Homo sapiens	38-41
17222902-3	2007	In the first step, functional monomer MAT was synthesized by the reaction of L-tyrosine methylester and methacryloyl chloride and characterized by FTIR and NMR.	methacryloyl chloride	104-125	methionine adenosyltransferase 1A	Homo sapiens	38-41
17222902-4	2007	Then, cholesterol was complexed with MAT in different mol ratios and the cholesterol-imprinted poly(2-hydroxyethyl methacrylate-N-methacryloyl-(L)-tyrosine methylester) [MIP] particles were synthesized by bulk polymerization.	Cholesterol	6-17	methionine adenosyltransferase 1A	Homo sapiens	37-40
17540142-4	2007	RESULTS: Of 213 episodes of SAB, 131 (61.5%) were due to SAMS and 82 (38.5%) to SAMR.	sab	28-31	methionine adenosyltransferase 1A	Homo sapiens	57-61
17425347-1	2007	In this paper we present a study of using oxygen plasma for chemically modifying inert hydrocarbon self-assembled monolayers of octadecyltrichlorosilane (OTS-SAMs) and rendering active surfaces for protein immobilization.	Oxygen	42-48	methionine adenosyltransferase 1A	Homo sapiens	158-162
17425347-1	2007	In this paper we present a study of using oxygen plasma for chemically modifying inert hydrocarbon self-assembled monolayers of octadecyltrichlorosilane (OTS-SAMs) and rendering active surfaces for protein immobilization.	Hydrocarbons	87-98	methionine adenosyltransferase 1A	Homo sapiens	158-162
17425347-1	2007	In this paper we present a study of using oxygen plasma for chemically modifying inert hydrocarbon self-assembled monolayers of octadecyltrichlorosilane (OTS-SAMs) and rendering active surfaces for protein immobilization.	octadecyltrichlorosilane	128-152	methionine adenosyltransferase 1A	Homo sapiens	158-162
17425347-3	2007	Our XPS results showed that the surface reaction between OTS-SAMs and oxygen plasma can generate new surface functional groups such as alcohol (C-O), aldehyde (C=O), and carboxylic acid (O-C=O), and their compositions can be controlled by using different treatment times and powers.	Oxygen	70-76	methionine adenosyltransferase 1A	Homo sapiens	61-65
17425347-3	2007	Our XPS results showed that the surface reaction between OTS-SAMs and oxygen plasma can generate new surface functional groups such as alcohol (C-O), aldehyde (C=O), and carboxylic acid (O-C=O), and their compositions can be controlled by using different treatment times and powers.	Alcohols	135-142	methionine adenosyltransferase 1A	Homo sapiens	61-65
17425347-3	2007	Our XPS results showed that the surface reaction between OTS-SAMs and oxygen plasma can generate new surface functional groups such as alcohol (C-O), aldehyde (C=O), and carboxylic acid (O-C=O), and their compositions can be controlled by using different treatment times and powers.	Carbon	144-145	methionine adenosyltransferase 1A	Homo sapiens	61-65
17425347-3	2007	Our XPS results showed that the surface reaction between OTS-SAMs and oxygen plasma can generate new surface functional groups such as alcohol (C-O), aldehyde (C=O), and carboxylic acid (O-C=O), and their compositions can be controlled by using different treatment times and powers.	Aldehydes	150-158	methionine adenosyltransferase 1A	Homo sapiens	61-65
17425347-3	2007	Our XPS results showed that the surface reaction between OTS-SAMs and oxygen plasma can generate new surface functional groups such as alcohol (C-O), aldehyde (C=O), and carboxylic acid (O-C=O), and their compositions can be controlled by using different treatment times and powers.	Carboxylic Acids	170-185	methionine adenosyltransferase 1A	Homo sapiens	61-65
17425347-3	2007	Our XPS results showed that the surface reaction between OTS-SAMs and oxygen plasma can generate new surface functional groups such as alcohol (C-O), aldehyde (C=O), and carboxylic acid (O-C=O), and their compositions can be controlled by using different treatment times and powers.	Carbon	160-161	methionine adenosyltransferase 1A	Homo sapiens	61-65
17432882-2	2007	After self-assembled monolayer (SAM) formation on gold, the vicinal diols were converted into aldehyde functions by exposure to aqueous NaIO4, as previously used for SAMs with OEG chains buried in the center of the SAM [Jang et al.	vicinal diols	60-73	methionine adenosyltransferase 1A	Homo sapiens	166-170
17432882-2	2007	After self-assembled monolayer (SAM) formation on gold, the vicinal diols were converted into aldehyde functions by exposure to aqueous NaIO4, as previously used for SAMs with OEG chains buried in the center of the SAM [Jang et al.	Aldehydes	94-102	methionine adenosyltransferase 1A	Homo sapiens	166-170
17432882-2	2007	After self-assembled monolayer (SAM) formation on gold, the vicinal diols were converted into aldehyde functions by exposure to aqueous NaIO4, as previously used for SAMs with OEG chains buried in the center of the SAM [Jang et al.	metaperiodate	136-141	methionine adenosyltransferase 1A	Homo sapiens	166-170
17432882-2	2007	After self-assembled monolayer (SAM) formation on gold, the vicinal diols were converted into aldehyde functions by exposure to aqueous NaIO4, as previously used for SAMs with OEG chains buried in the center of the SAM [Jang et al.	Diglycolic acid	176-179	methionine adenosyltransferase 1A	Homo sapiens	166-170
17432882-5	2007	Mixed SAMs with latent aldehydes on 5% of the OEG termini showed high protein resistance, which greatly slowed the kinetics of protein coupling on the time scale of minutes.	Aldehydes	23-32	methionine adenosyltransferase 1A	Homo sapiens	6-10
17432882-5	2007	Mixed SAMs with latent aldehydes on 5% of the OEG termini showed high protein resistance, which greatly slowed the kinetics of protein coupling on the time scale of minutes.	Diglycolic acid	46-49	methionine adenosyltransferase 1A	Homo sapiens	6-10
17432882-7	2007	In conclusion, OEG-terminated SAMs with latent aldehydes serve as protein-resistant sensor surfaces which are easily functionalized with small ligands or with heterobifunctional crosslinkers to which the bait molecule is attached in a subsequent step.	Diglycolic acid	15-18	methionine adenosyltransferase 1A	Homo sapiens	30-34
17432882-7	2007	In conclusion, OEG-terminated SAMs with latent aldehydes serve as protein-resistant sensor surfaces which are easily functionalized with small ligands or with heterobifunctional crosslinkers to which the bait molecule is attached in a subsequent step.	Aldehydes	47-56	methionine adenosyltransferase 1A	Homo sapiens	30-34
17441811-6	2007	In addition, silencing MAT2A gene resulted in the stimulation of MAT1A mRNA production, which was blocked by 3-deazaadenosine and l-ethionine, but not d-ethionine, suggesting that such effect was specific and mediated by upregulation of SAM level and SAM : S-adenosylethionine (SAH) ratio.	3-deazaadenosine	109-125	methionine adenosyltransferase 1A	Homo sapiens	65-70
17441811-6	2007	In addition, silencing MAT2A gene resulted in the stimulation of MAT1A mRNA production, which was blocked by 3-deazaadenosine and l-ethionine, but not d-ethionine, suggesting that such effect was specific and mediated by upregulation of SAM level and SAM : S-adenosylethionine (SAH) ratio.	Ethionine	130-141	methionine adenosyltransferase 1A	Homo sapiens	65-70
17441811-6	2007	In addition, silencing MAT2A gene resulted in the stimulation of MAT1A mRNA production, which was blocked by 3-deazaadenosine and l-ethionine, but not d-ethionine, suggesting that such effect was specific and mediated by upregulation of SAM level and SAM : S-adenosylethionine (SAH) ratio.	S-adenosylethionine	257-276	methionine adenosyltransferase 1A	Homo sapiens	65-70
17341099-3	2007	Cyt c on a PySH-SAM shows a quasi-reversible, monoelectronic, adsorption-controlled CV response with a formal reduction potential of -0.061 V (vs SCE), which is comparable to the values found for native cyt c adsorbed on different SAMs.	pysh-sam	11-19	methionine adenosyltransferase 1A	Homo sapiens	231-235
20408633-5	2007	In tBLMs based on SAMs of pure WC14, the hexa(ethylene oxide) tether region had low hydration even though FT-IRRAS showed that this region is structurally disordered.	tblms	3-8	methionine adenosyltransferase 1A	Homo sapiens	18-22
17318518-2	2007	The functional sensing surface was fabricated by the immobilization of a benzaldehyde-ovalbumin conjugate (BZ-OVA) on Au-thiolate SAMs containing carboxyl end groups.	benzaldehyde	73-85	methionine adenosyltransferase 1A	Homo sapiens	130-134
17318518-2	2007	The functional sensing surface was fabricated by the immobilization of a benzaldehyde-ovalbumin conjugate (BZ-OVA) on Au-thiolate SAMs containing carboxyl end groups.	bz-ova	107-113	methionine adenosyltransferase 1A	Homo sapiens	130-134
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
17326604-1	2007	We have utilized protective oligonucleotides to modify DNA fragments with osmium tetroxide complexes without compromising their ability to hybridize with immobilized thiol-linked probe-SAMs on gold electrodes.	Sulfhydryl Compounds	166-171	methionine adenosyltransferase 1A	Homo sapiens	185-189
17192974-2	2006	The transfer of high-molar-mass polyamidoamine (PAMAM) dendrimers (generation 5) and the rapid in situ covalent attachment of the deposited adsorbates onto reactive N-hydroxysuccinimide (NHS) terminated SAMs on gold and NHS-activated polystyrene-block-poly(tert-butyl acrylate) (PS(690)-b-PtBA(1210)) block copolymer thin films were investigated as strategies to suppress line broadening by surface diffusion in DPN.	N-hydroxysuccinimide	165-185	methionine adenosyltransferase 1A	Homo sapiens	203-207
17154616-0	2006	Deposition of DNA rafts on cationic SAMs on silicon [100].	Silicon	44-51	methionine adenosyltransferase 1A	Homo sapiens	36-40
17154616-3	2006	The rafts bind to cationic SAMs on silicon wafers.	Silicon	35-42	methionine adenosyltransferase 1A	Homo sapiens	27-31
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
16518866-1	2006	Herein, the scanning electrochemical microscopy (SECM) approach is applied to study the formation of thiol-porphyrin self-assembled monolayer (SAMs).	thiol-porphyrin	101-116	methionine adenosyltransferase 1A	Homo sapiens	143-147
16863372-1	2006	The reaction of a transition metal coordination complex, Ti[N(CH(3))(2)](4), with self-assembled monolayers (SAMs) possessing-OH, -NH(2), and -CH(3) terminations has been examined using supersonic molecular beam techniques.	Metals	29-34	methionine adenosyltransferase 1A	Homo sapiens	109-113
16649770-5	2006	Unlike SAMs of some benzenoid aryl isocyanides, the nonbenzenoid isocyanoazule-based SAMs proved resistant to oxidation, oligomerization, and isomerization into the corresponding nitriles under ambient conditions, which is an important prerequisite to their future applications.	benzenoid	20-29	methionine adenosyltransferase 1A	Homo sapiens	85-89
16649770-5	2006	Unlike SAMs of some benzenoid aryl isocyanides, the nonbenzenoid isocyanoazule-based SAMs proved resistant to oxidation, oligomerization, and isomerization into the corresponding nitriles under ambient conditions, which is an important prerequisite to their future applications.	aryl isocyanides	30-46	methionine adenosyltransferase 1A	Homo sapiens	85-89
16649770-5	2006	Unlike SAMs of some benzenoid aryl isocyanides, the nonbenzenoid isocyanoazule-based SAMs proved resistant to oxidation, oligomerization, and isomerization into the corresponding nitriles under ambient conditions, which is an important prerequisite to their future applications.	isocyanoazule	65-78	methionine adenosyltransferase 1A	Homo sapiens	7-11
16649770-5	2006	Unlike SAMs of some benzenoid aryl isocyanides, the nonbenzenoid isocyanoazule-based SAMs proved resistant to oxidation, oligomerization, and isomerization into the corresponding nitriles under ambient conditions, which is an important prerequisite to their future applications.	isocyanoazule	65-78	methionine adenosyltransferase 1A	Homo sapiens	85-89
16518866-4	2006	In K(3)Fe(CN)(6) , the SAMs show a strong electron-transfer (ET) blocking effect on a pure porphyrin-modified electrode.	KS 3	3-7	methionine adenosyltransferase 1A	Homo sapiens	23-27
16518866-4	2006	In K(3)Fe(CN)(6) , the SAMs show a strong electron-transfer (ET) blocking effect on a pure porphyrin-modified electrode.	Iron	7-9	methionine adenosyltransferase 1A	Homo sapiens	23-27
16518866-4	2006	In K(3)Fe(CN)(6) , the SAMs show a strong electron-transfer (ET) blocking effect on a pure porphyrin-modified electrode.	Porphyrins	91-100	methionine adenosyltransferase 1A	Homo sapiens	23-27
16450040-4	2006	The techniques for the formation and dissociation of biotinylated SAMs from aqueous solvents reported here may be applied towards the development of Au-based sensor devices and microfluidics chips in the future.	Gold	149-151	methionine adenosyltransferase 1A	Homo sapiens	66-70
16548554-3	2006	The results suggested that SH-TPP and SH-MTPP could form high-quality SAMs on gold surfaces.	sh-tpp	27-33	methionine adenosyltransferase 1A	Homo sapiens	70-74
16548554-3	2006	The results suggested that SH-TPP and SH-MTPP could form high-quality SAMs on gold surfaces.	sh-mtpp	38-45	methionine adenosyltransferase 1A	Homo sapiens	70-74
16461892-3	2006	Our method is based on the observation that SWNTs are strongly attracted to COOH-terminated self-assembled monolayers (COOH-SAMs) and that SWNTs with lengths greater than the dimensions of a COOH-SAM feature will align along the boundary between the COOH-SAM feature and a passivating CH3-terminated SAM.	Carbonic Acid	119-123	methionine adenosyltransferase 1A	Homo sapiens	124-128
16461892-3	2006	Our method is based on the observation that SWNTs are strongly attracted to COOH-terminated self-assembled monolayers (COOH-SAMs) and that SWNTs with lengths greater than the dimensions of a COOH-SAM feature will align along the boundary between the COOH-SAM feature and a passivating CH3-terminated SAM.	Carbonic Acid	119-123	methionine adenosyltransferase 1A	Homo sapiens	124-128
16461892-3	2006	Our method is based on the observation that SWNTs are strongly attracted to COOH-terminated self-assembled monolayers (COOH-SAMs) and that SWNTs with lengths greater than the dimensions of a COOH-SAM feature will align along the boundary between the COOH-SAM feature and a passivating CH3-terminated SAM.	Carbonic Acid	119-123	methionine adenosyltransferase 1A	Homo sapiens	124-128
16461892-5	2006	Experiment and theory (Monte Carlo simulations) suggest that the COOH-SAMs localize the solvent carrying the nanotubes on the SAM features, and that van der Waals interactions between the tubes and the COOH-rich feature drive the assembly process.	Carbonic Acid	65-69	methionine adenosyltransferase 1A	Homo sapiens	70-74
16519441-4	2006	Acetylenes possessing redox-active ferrocene substituents react with the azide-terminated mixed SAMs and electrochemical measurements of the ferrocene-modified SAM electrodes have been used to quantify the redox centers attached to these platforms.	Alkynes	0-10	methionine adenosyltransferase 1A	Homo sapiens	96-100
16519441-4	2006	Acetylenes possessing redox-active ferrocene substituents react with the azide-terminated mixed SAMs and electrochemical measurements of the ferrocene-modified SAM electrodes have been used to quantify the redox centers attached to these platforms.	ferrocene	35-44	methionine adenosyltransferase 1A	Homo sapiens	96-100
16519441-4	2006	Acetylenes possessing redox-active ferrocene substituents react with the azide-terminated mixed SAMs and electrochemical measurements of the ferrocene-modified SAM electrodes have been used to quantify the redox centers attached to these platforms.	Azides	73-78	methionine adenosyltransferase 1A	Homo sapiens	96-100
16174526-9	2006	Silicone shunts coated with SAMs may be suitable for future clinical applications to improve the treatment of hydrocephalus.	Silicones	0-8	methionine adenosyltransferase 1A	Homo sapiens	28-32
16471747-2	2006	The SAMs were prepared by immersing Au(111) into an ethanol solution containing 1 microM decanethiol with different immersion times.	Gold	36-38	methionine adenosyltransferase 1A	Homo sapiens	4-8
16471747-2	2006	The SAMs were prepared by immersing Au(111) into an ethanol solution containing 1 microM decanethiol with different immersion times.	Ethanol	52-59	methionine adenosyltransferase 1A	Homo sapiens	4-8
16471747-2	2006	The SAMs were prepared by immersing Au(111) into an ethanol solution containing 1 microM decanethiol with different immersion times.	1-DECANETHIOL	89-100	methionine adenosyltransferase 1A	Homo sapiens	4-8
16471747-11	2006	The formation process and structure of decanethiol SAMs are well related to sample preparation conditions.	1-DECANETHIOL	39-50	methionine adenosyltransferase 1A	Homo sapiens	51-55
16413417-11	2006	Increased flux of (13)C-labeled methionine to S-adenosylhomocysteine (SAH) in A549 demonstrated that SAM"s methyl group was utilized, and increased formation of cystathionine indicated that at least part of SAM generated was directed toward cysteine/GSH in the transsulfuration pathway.	Carbon-13	18-23	methionine adenosyltransferase 1A	Homo sapiens	101-106
16413417-11	2006	Increased flux of (13)C-labeled methionine to S-adenosylhomocysteine (SAH) in A549 demonstrated that SAM"s methyl group was utilized, and increased formation of cystathionine indicated that at least part of SAM generated was directed toward cysteine/GSH in the transsulfuration pathway.	Methionine	32-42	methionine adenosyltransferase 1A	Homo sapiens	101-106
16413417-11	2006	Increased flux of (13)C-labeled methionine to S-adenosylhomocysteine (SAH) in A549 demonstrated that SAM"s methyl group was utilized, and increased formation of cystathionine indicated that at least part of SAM generated was directed toward cysteine/GSH in the transsulfuration pathway.	Cysteine	60-68	methionine adenosyltransferase 1A	Homo sapiens	101-106
16853372-5	2005	EIS measurements also showed that the covalently bonded spirobifluorene SAMs act as an effective barrier to both ion penetration and heterogeneous electron transfer.	spirobifluorene	56-71	methionine adenosyltransferase 1A	Homo sapiens	72-76
16471542-6	2006	Our results are consistent with a small population of electrochemically active MB species very close to the Au surface that reach this position driven by their lipophilic (hydrophobic) character through defects at SAMs.	Gold	108-110	methionine adenosyltransferase 1A	Homo sapiens	214-218
16482256-2	2006	A mathematical treatment, based on calculating the electrochemical potential difference at the monolayer-electrolyte interface, has followed our recent work which dealt with the acid-base equilibrium at the interface as a means of calculating the pK of ionizable SAMs and their binding with Cd(2+).	base	26-30	methionine adenosyltransferase 1A	Homo sapiens	263-267
16382178-4	2006	Radioactivity incorporated into GST-SAMS can be recovered easily by precipitation with glutathione-agarose.	Glutathione	87-98	methionine adenosyltransferase 1A	Homo sapiens	36-40
16382178-4	2006	Radioactivity incorporated into GST-SAMS can be recovered easily by precipitation with glutathione-agarose.	Sepharose	99-106	methionine adenosyltransferase 1A	Homo sapiens	36-40
16116661-3	2005	This method involves electrodeposition onto a conducting master covered by a self-assembled alkanethiolate monolayer (SAMs).	alkanethiolate	92-106	methionine adenosyltransferase 1A	Homo sapiens	118-122
16340382-4	2005	SAM levels were significantly reduced in levodopa-treated PD patients, but they showed increased enzyme methionine adenosyl transferase (MAT) activity, which induces SAM synthesis from methionine (MET).	Levodopa	41-49	methionine adenosyltransferase 1A	Homo sapiens	104-135
16340382-4	2005	SAM levels were significantly reduced in levodopa-treated PD patients, but they showed increased enzyme methionine adenosyl transferase (MAT) activity, which induces SAM synthesis from methionine (MET).	Levodopa	41-49	methionine adenosyltransferase 1A	Homo sapiens	137-140
16340382-4	2005	SAM levels were significantly reduced in levodopa-treated PD patients, but they showed increased enzyme methionine adenosyl transferase (MAT) activity, which induces SAM synthesis from methionine (MET).	Methionine	104-114	methionine adenosyltransferase 1A	Homo sapiens	137-140
16342971-3	2005	These results suggest that SAMs of densely packed or polypodal thiols may be substantially less stable under tensile stress than previously recognized and that the additional thiolate linkages may not only fail to increase the overall strength of attachment but could actually reduce it.	Sulfhydryl Compounds	63-69	methionine adenosyltransferase 1A	Homo sapiens	27-31
16292818-2	2005	SAMs of calix[n]arene (n = 4, 6, 8) derivatives 1-5 were formed on gold bead electrodes.	arene	16-21	methionine adenosyltransferase 1A	Homo sapiens	0-4
16292818-3	2005	Cyclic voltammetry with Ru(NH3)6(3+/2+) as a redox probe, together with impedance spectroscopy and reductive desorption, indicates that SAMs of 5 have a higher coverage than those of 3 and 4 due to the presence of hydrogen bonding and possibly its conformation.	ru(nh3)6	24-32	methionine adenosyltransferase 1A	Homo sapiens	136-140
16292818-3	2005	Cyclic voltammetry with Ru(NH3)6(3+/2+) as a redox probe, together with impedance spectroscopy and reductive desorption, indicates that SAMs of 5 have a higher coverage than those of 3 and 4 due to the presence of hydrogen bonding and possibly its conformation.	Hydrogen	214-222	methionine adenosyltransferase 1A	Homo sapiens	136-140
16292818-4	2005	Noncovalent immobilization of C60 on gold surfaces was achieved with SAMs of calix[8]arene derivative 5 but not with those of 1-4.	Calix[8]arene	77-90	methionine adenosyltransferase 1A	Homo sapiens	69-73
15963701-2	2005	In this study, the metabolic consequences of the pathological changes associated with the key pathway enzymes, methionine adenosyl transferase (MAT), glycine N-methyl transferase (GNMT) and cystathionine beta-synthase (CBS) as well as an activation of polyamine metabolism, were analyzed using a simple mathematical model describing methionine metabolism in liver.	Methionine	111-121	methionine adenosyltransferase 1A	Homo sapiens	144-147
16171358-2	2005	The fullerene-containing SAMs were investigated by cyclic voltammetry and water contact angle measurements.	Fullerenes	4-13	methionine adenosyltransferase 1A	Homo sapiens	25-29
16171358-2	2005	The fullerene-containing SAMs were investigated by cyclic voltammetry and water contact angle measurements.	Water	74-79	methionine adenosyltransferase 1A	Homo sapiens	25-29
16171358-3	2005	Two reversible, surface-confined redox couples were obtained for the fullerene-containing SAMs on TMF/GCE in CH(2)Cl(2) solution.	Fullerenes	69-78	methionine adenosyltransferase 1A	Homo sapiens	90-94
16171358-3	2005	Two reversible, surface-confined redox couples were obtained for the fullerene-containing SAMs on TMF/GCE in CH(2)Cl(2) solution.	triflumuron	98-101	methionine adenosyltransferase 1A	Homo sapiens	90-94
16171358-3	2005	Two reversible, surface-confined redox couples were obtained for the fullerene-containing SAMs on TMF/GCE in CH(2)Cl(2) solution.	GCE	102-105	methionine adenosyltransferase 1A	Homo sapiens	90-94
16171358-3	2005	Two reversible, surface-confined redox couples were obtained for the fullerene-containing SAMs on TMF/GCE in CH(2)Cl(2) solution.	Methylene Chloride	109-119	methionine adenosyltransferase 1A	Homo sapiens	90-94
15963701-5	2005	Application of the characteristics of transformed hepatocytes to our model, i.e., substitution of the MAT I/III isozyme by MAT II, loss of GNMT activity and activation of polyamine biosynthesis, leads to the prediction of a significantly different dependence of methionine metabolism on methionine concentrations.	Methionine	262-272	methionine adenosyltransferase 1A	Homo sapiens	102-111
15963701-5	2005	Application of the characteristics of transformed hepatocytes to our model, i.e., substitution of the MAT I/III isozyme by MAT II, loss of GNMT activity and activation of polyamine biosynthesis, leads to the prediction of a significantly different dependence of methionine metabolism on methionine concentrations.	Methionine	287-297	methionine adenosyltransferase 1A	Homo sapiens	102-111
16011359-2	2005	Scanning tunneling microscopy (STM) measurements of compound 2 inserted into a SAM of C11 thiol reveal that molecule 2 exhibits (i) the stochastic switching characteristic of wire molecules embedded in insulating SAMs and (ii) higher conductivity than the C11 thiol SAM.	Sulfhydryl Compounds	90-95	methionine adenosyltransferase 1A	Homo sapiens	213-217
16011359-2	2005	Scanning tunneling microscopy (STM) measurements of compound 2 inserted into a SAM of C11 thiol reveal that molecule 2 exhibits (i) the stochastic switching characteristic of wire molecules embedded in insulating SAMs and (ii) higher conductivity than the C11 thiol SAM.	Sulfhydryl Compounds	260-265	methionine adenosyltransferase 1A	Homo sapiens	213-217
15982011-2	2005	SAMs presenting the disaccharide maltose as a neoglycoconjugate were produced, and the structure was studied by high resolution atomic force microscopy.	Disaccharides	20-32	methionine adenosyltransferase 1A	Homo sapiens	0-4
15982011-2	2005	SAMs presenting the disaccharide maltose as a neoglycoconjugate were produced, and the structure was studied by high resolution atomic force microscopy.	Maltose	33-40	methionine adenosyltransferase 1A	Homo sapiens	0-4
15853337-2	2005	For comparison, a chemically oxidized Si surface, which serves as the starting point for formation of the SAMs, has also been investigated.	Silicon	38-40	methionine adenosyltransferase 1A	Homo sapiens	106-110
16852424-5	2005	Amino-terminated SAMs were prepared from p-aminophenyl-trimethoxysilane through chemical vapor deposition.	p-aminophenyl-trimethoxysilane	41-71	methionine adenosyltransferase 1A	Homo sapiens	17-21
15835965-6	2005	Our studies showed that hyperbranched polyglycerol is adsorbed to polar as well as to nonpolar SAMs.	polyglycerol	38-50	methionine adenosyltransferase 1A	Homo sapiens	95-99
15835965-8	2005	The adsorption of hyperbranched polyglycerol to the SAMs with different surface polarities resulted in the formation of aragonite for alkyl-terminated SAMs and no phase selection for carboxylate-terminated SAMs.	polyglycerol	32-44	methionine adenosyltransferase 1A	Homo sapiens	52-56
15835965-8	2005	The adsorption of hyperbranched polyglycerol to the SAMs with different surface polarities resulted in the formation of aragonite for alkyl-terminated SAMs and no phase selection for carboxylate-terminated SAMs.	polyglycerol	32-44	methionine adenosyltransferase 1A	Homo sapiens	151-155
15835965-8	2005	The adsorption of hyperbranched polyglycerol to the SAMs with different surface polarities resulted in the formation of aragonite for alkyl-terminated SAMs and no phase selection for carboxylate-terminated SAMs.	polyglycerol	32-44	methionine adenosyltransferase 1A	Homo sapiens	151-155
15835965-8	2005	The adsorption of hyperbranched polyglycerol to the SAMs with different surface polarities resulted in the formation of aragonite for alkyl-terminated SAMs and no phase selection for carboxylate-terminated SAMs.	Calcium Carbonate	120-129	methionine adenosyltransferase 1A	Homo sapiens	52-56
16851923-3	2005	Surprisingly, localized lattice packing of crystalline dithiolated furan oligoaryls on Au(111) can be assembled by immersing preadsorbed n-dodecanethiol SAMs in the corresponding deposition solutions.	furan	67-72	methionine adenosyltransferase 1A	Homo sapiens	153-157
16851923-3	2005	Surprisingly, localized lattice packing of crystalline dithiolated furan oligoaryls on Au(111) can be assembled by immersing preadsorbed n-dodecanethiol SAMs in the corresponding deposition solutions.	dodecylmercaptan	137-152	methionine adenosyltransferase 1A	Homo sapiens	153-157
16851923-6	2005	The absence of crystalline packing is mainly attributed to the difficulty for the dithiols to simultaneously break two S-Au bonds, to desorb, and then to readsorb, the key step to improve the intermolecular attractions for crystalline SAMs.	dithiol	82-90	methionine adenosyltransferase 1A	Homo sapiens	235-239
16851923-6	2005	The absence of crystalline packing is mainly attributed to the difficulty for the dithiols to simultaneously break two S-Au bonds, to desorb, and then to readsorb, the key step to improve the intermolecular attractions for crystalline SAMs.	Gold	121-123	methionine adenosyltransferase 1A	Homo sapiens	235-239
15796562-2	2005	We find that the orientation of the cyclobis(paraquat-p-phenylene) (CBPQT) ring depends dramatically on the coverage, changing in order to obtain highly packed SAMs.	paraquat-p-phenylene	45-65	methionine adenosyltransferase 1A	Homo sapiens	160-164
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.	Glutathione	224-235	methionine adenosyltransferase 1A	Homo sapiens	11-16
15589539-4	2005	The zwitterionic telomer SAM in general did not adsorb proteins significantly, suggesting the usability of zwitterionic polymer SAMs and brushes to coat various materials used in biomedical fields.	Polymers	120-127	methionine adenosyltransferase 1A	Homo sapiens	128-132
15835737-5	2005	However, sulphonic acid terminated SAMs showed almost exclusively electrostatic interactions with human serum albumin.	sulphonic acid	9-23	methionine adenosyltransferase 1A	Homo sapiens	35-39
15835965-8	2005	The adsorption of hyperbranched polyglycerol to the SAMs with different surface polarities resulted in the formation of aragonite for alkyl-terminated SAMs and no phase selection for carboxylate-terminated SAMs.	Calcium Carbonate	120-129	methionine adenosyltransferase 1A	Homo sapiens	151-155
15835965-8	2005	The adsorption of hyperbranched polyglycerol to the SAMs with different surface polarities resulted in the formation of aragonite for alkyl-terminated SAMs and no phase selection for carboxylate-terminated SAMs.	Calcium Carbonate	120-129	methionine adenosyltransferase 1A	Homo sapiens	151-155
15835965-8	2005	The adsorption of hyperbranched polyglycerol to the SAMs with different surface polarities resulted in the formation of aragonite for alkyl-terminated SAMs and no phase selection for carboxylate-terminated SAMs.	carboxylate	183-194	methionine adenosyltransferase 1A	Homo sapiens	52-56
15835737-4	2005	The adsorption of human serum albumin to carboxylic and amine terminated SAMs was shown to be predominantly via non-electrostatic interactions (hydrophobic or hydrogen bonding).	Amines	56-61	methionine adenosyltransferase 1A	Homo sapiens	73-77
15835737-4	2005	The adsorption of human serum albumin to carboxylic and amine terminated SAMs was shown to be predominantly via non-electrostatic interactions (hydrophobic or hydrogen bonding).	Hydrogen	159-167	methionine adenosyltransferase 1A	Homo sapiens	73-77
15589539-5	2005	The correlation between the structure of water in the vicinity of zwitterionic telomers and the resistance of the zwitterionic telomer SAMs against the nonspecific adsorption of proteins was discussed.	Water	41-46	methionine adenosyltransferase 1A	Homo sapiens	135-139
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
15697276-5	2005	The K(assoc) values for all the BPs except for bisphenol B with the SAM of LP-beta-CD were always larger than those with the SAM of DTUA-beta-CD, due to a difference in the orientation of the beta-CD moiety in the SAMs.	bis(4-hydroxyphenyl)sulfone	32-35	methionine adenosyltransferase 1A	Homo sapiens	214-218
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
15670956-4	2005	As an anti-TB drug target, Mtb-MAT has been well validated.	Terbium	11-13	methionine adenosyltransferase 1A	Homo sapiens	31-34
15339153-3	2004	The thiols further spread on the metal surface, forming highly ordered SAMs in the form of a ring pattern.	Sulfhydryl Compounds	4-10	methionine adenosyltransferase 1A	Homo sapiens	71-75
15506746-5	2004	TFTs, where these polymers were laminated onto gate dielectrics coated with SAMs from octyltrichlorosilane, had effective field-effect mobilities of 0.03 and 0.005 cm2/(V s), respectively.	Polymers	18-26	methionine adenosyltransferase 1A	Homo sapiens	76-80
15506746-5	2004	TFTs, where these polymers were laminated onto gate dielectrics coated with SAMs from octyltrichlorosilane, had effective field-effect mobilities of 0.03 and 0.005 cm2/(V s), respectively.	octyltrichlorosilane	86-106	methionine adenosyltransferase 1A	Homo sapiens	76-80
15522691-1	2004	4-Amino-2-mercaptopyrimidine self-assembled monolayer (AMP SAMs/Au) was prepared on a gold electrode.	4-amino-2-mercaptopyrimidine	0-28	methionine adenosyltransferase 1A	Homo sapiens	59-63
15522691-2	2004	The AMP SAMs/Au was characterized by using attenuated total reflection-fourier transform infrared (ATR-FTIR) and A.C. Impedance.	Adenosine Monophosphate	4-7	methionine adenosyltransferase 1A	Homo sapiens	8-12
15522691-3	2004	The electrochemical behavior of brucine on AMP SAMs/Au was studied by cyclic voltammetry (CV) and square wave adsorptive stripping voltammetry (SWASV).	brucine	32-39	methionine adenosyltransferase 1A	Homo sapiens	47-51
15522691-3	2004	The electrochemical behavior of brucine on AMP SAMs/Au was studied by cyclic voltammetry (CV) and square wave adsorptive stripping voltammetry (SWASV).	Adenosine Monophosphate	43-46	methionine adenosyltransferase 1A	Homo sapiens	47-51
15339153-3	2004	The thiols further spread on the metal surface, forming highly ordered SAMs in the form of a ring pattern.	Metals	33-38	methionine adenosyltransferase 1A	Homo sapiens	71-75
15323531-6	2004	The adhesion of proteins with uncharged SAMs showed a general "step" dependence on the wettability of the surface as determined by the water contact angle under cyclooctane (thetaco).	Water	135-140	methionine adenosyltransferase 1A	Homo sapiens	40-44
15323531-6	2004	The adhesion of proteins with uncharged SAMs showed a general "step" dependence on the wettability of the surface as determined by the water contact angle under cyclooctane (thetaco).	cyclooctane	161-172	methionine adenosyltransferase 1A	Homo sapiens	40-44
15274566-3	2004	The sequence corresponds to the direction of increasing hydration energy of the corresponding anion, suggesting that highly hydrated ions promote electrocatalytic electron transfer to the ferrocene-terminated SAMs, while poorly hydrated ions inhibit it.	ferrocene	188-197	methionine adenosyltransferase 1A	Homo sapiens	209-213
16459600-5	2004	This has been illustrated by immersing both the as-deposited (trans form) SAMs and the photoswitched (predominantly cis form) SAMs into solutions of cobalt and zinc tetraphenylporphyrin (CoTPP and ZnTPP, respectively) and an octaoctyl-substituted cobalt phthalocyanine.	Cobalt	149-155	methionine adenosyltransferase 1A	Homo sapiens	126-130
16459600-5	2004	This has been illustrated by immersing both the as-deposited (trans form) SAMs and the photoswitched (predominantly cis form) SAMs into solutions of cobalt and zinc tetraphenylporphyrin (CoTPP and ZnTPP, respectively) and an octaoctyl-substituted cobalt phthalocyanine.	zinc tetraphenylporphyrin	160-185	methionine adenosyltransferase 1A	Homo sapiens	126-130
16459600-5	2004	This has been illustrated by immersing both the as-deposited (trans form) SAMs and the photoswitched (predominantly cis form) SAMs into solutions of cobalt and zinc tetraphenylporphyrin (CoTPP and ZnTPP, respectively) and an octaoctyl-substituted cobalt phthalocyanine.	cobalt(III)-tetrakis(4-sulfonatophenyl)porphyrin	187-192	methionine adenosyltransferase 1A	Homo sapiens	126-130
16459600-5	2004	This has been illustrated by immersing both the as-deposited (trans form) SAMs and the photoswitched (predominantly cis form) SAMs into solutions of cobalt and zinc tetraphenylporphyrin (CoTPP and ZnTPP, respectively) and an octaoctyl-substituted cobalt phthalocyanine.	zinc tetraphenylporphine	197-202	methionine adenosyltransferase 1A	Homo sapiens	126-130
16459600-5	2004	This has been illustrated by immersing both the as-deposited (trans form) SAMs and the photoswitched (predominantly cis form) SAMs into solutions of cobalt and zinc tetraphenylporphyrin (CoTPP and ZnTPP, respectively) and an octaoctyl-substituted cobalt phthalocyanine.	octaoctyl-substituted cobalt phthalocyanine	225-268	methionine adenosyltransferase 1A	Homo sapiens	126-130
15144810-1	2004	We studied the direct micropatterning of a lanthanum-based thin film on a template of self-assembled monolayers in an aqueous solution at 80 degrees C. The template composed of silanol and octadecyl areas was prepared by UV-modified octadecyltrichlorosilane SAMs through a photomask.	Lanthanum	43-52	methionine adenosyltransferase 1A	Homo sapiens	258-262
15198607-3	2004	According to the FTIR and (29)Si NMR spectra, molecules in the SAMs demonstrated "horizontal" cross-linking (Si-O-Si and Si-OH.HO-Si bonds) and little or no "vertical" bonds with the metal oxide forming an amorphous, yet ordered film.	Silicon	30-32	methionine adenosyltransferase 1A	Homo sapiens	63-67
15198607-3	2004	According to the FTIR and (29)Si NMR spectra, molecules in the SAMs demonstrated "horizontal" cross-linking (Si-O-Si and Si-OH.HO-Si bonds) and little or no "vertical" bonds with the metal oxide forming an amorphous, yet ordered film.	Silicon	109-111	methionine adenosyltransferase 1A	Homo sapiens	63-67
15198607-3	2004	According to the FTIR and (29)Si NMR spectra, molecules in the SAMs demonstrated "horizontal" cross-linking (Si-O-Si and Si-OH.HO-Si bonds) and little or no "vertical" bonds with the metal oxide forming an amorphous, yet ordered film.	Silicon	109-111	methionine adenosyltransferase 1A	Homo sapiens	63-67
15198607-3	2004	According to the FTIR and (29)Si NMR spectra, molecules in the SAMs demonstrated "horizontal" cross-linking (Si-O-Si and Si-OH.HO-Si bonds) and little or no "vertical" bonds with the metal oxide forming an amorphous, yet ordered film.	Silicon	109-111	methionine adenosyltransferase 1A	Homo sapiens	63-67
15198607-3	2004	According to the FTIR and (29)Si NMR spectra, molecules in the SAMs demonstrated "horizontal" cross-linking (Si-O-Si and Si-OH.HO-Si bonds) and little or no "vertical" bonds with the metal oxide forming an amorphous, yet ordered film.	Silicon	109-111	methionine adenosyltransferase 1A	Homo sapiens	63-67
15198607-3	2004	According to the FTIR and (29)Si NMR spectra, molecules in the SAMs demonstrated "horizontal" cross-linking (Si-O-Si and Si-OH.HO-Si bonds) and little or no "vertical" bonds with the metal oxide forming an amorphous, yet ordered film.	metal oxide	183-194	methionine adenosyltransferase 1A	Homo sapiens	63-67
15984265-3	2004	The degree of surface heterogeneity at the SAMs increases as the number of C units (n) in the hydrocarbon chain decreases from n = 6.	Hydrocarbons	94-105	methionine adenosyltransferase 1A	Homo sapiens	43-47
15984265-4	2004	Defective regions act as preferred paths for MB incorporation into the methyl-terminated SAMs, driven by hydrophobic forces.	Methylene Blue	45-47	methionine adenosyltransferase 1A	Homo sapiens	89-93
15984265-6	2004	Only MB molecules incorporated into the SAMs close to the Au(111) surface (at a distance &lt; 0.5 nm) are electrochemically active.	Methylene Blue	5-7	methionine adenosyltransferase 1A	Homo sapiens	40-44
15984265-6	2004	Only MB molecules incorporated into the SAMs close to the Au(111) surface (at a distance &lt; 0.5 nm) are electrochemically active.	Gold	58-60	methionine adenosyltransferase 1A	Homo sapiens	40-44
15984265-8	2004	The heterogeneous charge-transfer rate constants for MB immobilized into methyl-terminated thiolate SAMs are higher than those estimated for carboxylate- terminated SAMs, suggesting a different orientation of the immobilized molecule in the thiolate environment.	thiolate	91-99	methionine adenosyltransferase 1A	Homo sapiens	100-104
15984265-8	2004	The heterogeneous charge-transfer rate constants for MB immobilized into methyl-terminated thiolate SAMs are higher than those estimated for carboxylate- terminated SAMs, suggesting a different orientation of the immobilized molecule in the thiolate environment.	carboxylate	141-152	methionine adenosyltransferase 1A	Homo sapiens	100-104
15984265-8	2004	The heterogeneous charge-transfer rate constants for MB immobilized into methyl-terminated thiolate SAMs are higher than those estimated for carboxylate- terminated SAMs, suggesting a different orientation of the immobilized molecule in the thiolate environment.	carboxylate	141-152	methionine adenosyltransferase 1A	Homo sapiens	165-169
15984265-8	2004	The heterogeneous charge-transfer rate constants for MB immobilized into methyl-terminated thiolate SAMs are higher than those estimated for carboxylate- terminated SAMs, suggesting a different orientation of the immobilized molecule in the thiolate environment.	thiolate	241-249	methionine adenosyltransferase 1A	Homo sapiens	100-104
15984265-8	2004	The heterogeneous charge-transfer rate constants for MB immobilized into methyl-terminated thiolate SAMs are higher than those estimated for carboxylate- terminated SAMs, suggesting a different orientation of the immobilized molecule in the thiolate environment.	thiolate	241-249	methionine adenosyltransferase 1A	Homo sapiens	165-169
15137749-4	2004	The results suggest an additional dimension in the control of structure and properties of thiol monolayers if different factors contributing to the energetics of SAMs enter in a competing rather than a cooperative way.	Sulfhydryl Compounds	90-95	methionine adenosyltransferase 1A	Homo sapiens	162-166
14962551-3	2004	We first characterised the SAMs on glass or silicon wafers by measuring wettability, layer thickness and roughness.	Silicon	44-51	methionine adenosyltransferase 1A	Homo sapiens	27-31
14962551-6	2004	The SDS-PAGE analysis of proteins adsorbed from bovine serum to the SAMs showed less protein adsorption to PEG and OH than to CH(3), NH(2) and COOH.	Sodium Dodecyl Sulfate	4-7	methionine adenosyltransferase 1A	Homo sapiens	68-72
14962551-6	2004	The SDS-PAGE analysis of proteins adsorbed from bovine serum to the SAMs showed less protein adsorption to PEG and OH than to CH(3), NH(2) and COOH.	Polyethylene Glycols	107-110	methionine adenosyltransferase 1A	Homo sapiens	68-72
14962551-6	2004	The SDS-PAGE analysis of proteins adsorbed from bovine serum to the SAMs showed less protein adsorption to PEG and OH than to CH(3), NH(2) and COOH.	Carbonic Acid	143-147	methionine adenosyltransferase 1A	Homo sapiens	68-72
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
15268544-2	2004	For short atomic oxygen exposures, CF-SAMs remain intact, an effect ascribed to the inertness of C-F and C-C bonds toward atomic oxygen and the well-ordered structure of the CF-SAMs.	Oxygen	17-23	methionine adenosyltransferase 1A	Homo sapiens	177-181
15122759-4	2004	Ethanol feeding or folate deficiency, separately or in combination, decreased transcript levels of methylenetetrahydrofolate reductase (MTHFR), methionine adenosyltransferase (MAT1A), glycine-N-methyltransferase (GNMT) and S-adenosylhomocysteine hydrolase (SAHH).	Ethanol	0-7	methionine adenosyltransferase 1A	Homo sapiens	176-181
15122759-4	2004	Ethanol feeding or folate deficiency, separately or in combination, decreased transcript levels of methylenetetrahydrofolate reductase (MTHFR), methionine adenosyltransferase (MAT1A), glycine-N-methyltransferase (GNMT) and S-adenosylhomocysteine hydrolase (SAHH).	Folic Acid	19-25	methionine adenosyltransferase 1A	Homo sapiens	176-181
15268544-5	2004	In contrast, the reactivity of atomic oxygen with alkanethiolate SAMs is initiated at the vacuum/film interface, producing oxygen-containing carbon functional groups.	Oxygen	38-44	methionine adenosyltransferase 1A	Homo sapiens	65-69
15268544-5	2004	In contrast, the reactivity of atomic oxygen with alkanethiolate SAMs is initiated at the vacuum/film interface, producing oxygen-containing carbon functional groups.	Oxygen	123-129	methionine adenosyltransferase 1A	Homo sapiens	65-69
15268544-5	2004	In contrast, the reactivity of atomic oxygen with alkanethiolate SAMs is initiated at the vacuum/film interface, producing oxygen-containing carbon functional groups.	Carbon	141-147	methionine adenosyltransferase 1A	Homo sapiens	65-69
14552630-0	2003	Synthesis of a copper [3]rotaxane able to function as an electrochemically driven oscillatory machine in solution, and to form SAMs on a metal surface.	Copper	15-21	methionine adenosyltransferase 1A	Homo sapiens	127-131
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
14670055-3	2003	The formations of SAMs of 3-mercaptopropanoic acid and thioctic acid were monitored by magnetoelastic transduction.	3-Mercaptopropionic Acid	26-50	methionine adenosyltransferase 1A	Homo sapiens	18-22
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
14719942-0	2004	In situ FTIR-ATR analysis and titration of carboxylic acid-terminated SAMs.	Carboxylic Acids	43-58	methionine adenosyltransferase 1A	Homo sapiens	70-74
14552630-0	2003	Synthesis of a copper [3]rotaxane able to function as an electrochemically driven oscillatory machine in solution, and to form SAMs on a metal surface.	3]rotaxane	23-33	methionine adenosyltransferase 1A	Homo sapiens	127-131
14552630-0	2003	Synthesis of a copper [3]rotaxane able to function as an electrochemically driven oscillatory machine in solution, and to form SAMs on a metal surface.	Metals	137-142	methionine adenosyltransferase 1A	Homo sapiens	127-131
14587735-0	2003	Model systems for flavoenzyme activity: flavin-functionalised SAMs as models for probing redox modulation through hydrogen bonding.	4,6-dinitro-o-cresol	40-46	methionine adenosyltransferase 1A	Homo sapiens	62-66
14587735-0	2003	Model systems for flavoenzyme activity: flavin-functionalised SAMs as models for probing redox modulation through hydrogen bonding.	Hydrogen	114-122	methionine adenosyltransferase 1A	Homo sapiens	62-66
12818541-4	2003	Both techniques have demonstrated that HSA adsorption to the different SAM-modified electrodes increases in the following order: OH&lt;COOH&lt;CH(3)-terminated SAMs.	Carbonic Acid	135-139	methionine adenosyltransferase 1A	Homo sapiens	160-164
12818541-4	2003	Both techniques have demonstrated that HSA adsorption to the different SAM-modified electrodes increases in the following order: OH&lt;COOH&lt;CH(3)-terminated SAMs.	methyl radical	143-148	methionine adenosyltransferase 1A	Homo sapiens	160-164