PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24126418-7 2014 Down-regulation of MAT1A could lead to decreases in S-adenosylmethionine (SAMe), which is known to protect against APAP toxicity. S-Adenosylmethionine 52-72 methionine adenosyltransferase I, alpha Mus musculus 19-24 23221482-1 2013 DNA methylation is linked to homocysteine metabolism through the generation of S-adenosylmethionine (AdoMet) and S-Adenosylhomocysteine (AdoHcy). S-Adenosylmethionine 79-99 methionine adenosyltransferase I, alpha Mus musculus 101-107 23505042-1 2013 UNLABELLED: Methionine adenosyltransferase 1A (MAT1A) and glycine N-methyltransferase (GNMT) are the primary genes involved in hepatic S-adenosylmethionine (SAMe) synthesis and degradation, respectively. S-Adenosylmethionine 135-155 methionine adenosyltransferase I, alpha Mus musculus 12-45 23505042-1 2013 UNLABELLED: Methionine adenosyltransferase 1A (MAT1A) and glycine N-methyltransferase (GNMT) are the primary genes involved in hepatic S-adenosylmethionine (SAMe) synthesis and degradation, respectively. S-Adenosylmethionine 135-155 methionine adenosyltransferase I, alpha Mus musculus 47-52 21481189-2 2011 We show here that the mouse Dnmt3a DNA methyltransferase is able to transfer the methyl group from S-adenosyl-l-methionine (AdoMet) to a cysteine residue in its catalytic center. S-Adenosylmethionine 124-130 methionine adenosyltransferase I, alpha Mus musculus 99-122 23073625-1 2012 S-adenosylmethionine (AdoMet, also known as SAM and SAMe) is the principal biological methyl donor synthesized in all mammalian cells but most abundantly in the liver. S-Adenosylmethionine 0-20 methionine adenosyltransferase I, alpha Mus musculus 22-28 20815019-2 2010 Mice lacking the methionine adenosyltransferase (MAT) gene MAT1A exhibit a chronic reduction in hepatic S-adenosylmethionine (SAMe) levels, basal activation of LKB1, and spontaneous development of nonalcoholic steatohepatitis (NASH) and hepatocellular carcinoma (HCC). S-Adenosylmethionine 104-124 methionine adenosyltransferase I, alpha Mus musculus 17-47 21362551-1 2011 Protein methylation pathways comprise methionine adenosyltransferase (MAT), which produces S-adenosylmethionine (SAM) and SAM-dependent substrate-specific methyltransferases. S-Adenosylmethionine 91-111 methionine adenosyltransferase I, alpha Mus musculus 38-68 21362551-1 2011 Protein methylation pathways comprise methionine adenosyltransferase (MAT), which produces S-adenosylmethionine (SAM) and SAM-dependent substrate-specific methyltransferases. S-Adenosylmethionine 91-111 methionine adenosyltransferase I, alpha Mus musculus 70-73 21362551-1 2011 Protein methylation pathways comprise methionine adenosyltransferase (MAT), which produces S-adenosylmethionine (SAM) and SAM-dependent substrate-specific methyltransferases. S-Adenosylmethionine 113-116 methionine adenosyltransferase I, alpha Mus musculus 38-68 21362551-1 2011 Protein methylation pathways comprise methionine adenosyltransferase (MAT), which produces S-adenosylmethionine (SAM) and SAM-dependent substrate-specific methyltransferases. S-Adenosylmethionine 113-116 methionine adenosyltransferase I, alpha Mus musculus 70-73 20815019-2 2010 Mice lacking the methionine adenosyltransferase (MAT) gene MAT1A exhibit a chronic reduction in hepatic S-adenosylmethionine (SAMe) levels, basal activation of LKB1, and spontaneous development of nonalcoholic steatohepatitis (NASH) and hepatocellular carcinoma (HCC). S-Adenosylmethionine 104-124 methionine adenosyltransferase I, alpha Mus musculus 59-64 18695670-2 2008 Lipopolysaccharide (LPS) was shown to inactivate hepatic methionine adenosyltransferase (MAT), the enzyme responsible for S-adenosylmethionine (SAMe) biosynthesis. S-Adenosylmethionine 122-142 methionine adenosyltransferase I, alpha Mus musculus 57-87 19565184-1 2009 Hyperhomocysteinemia and factors of homocysteine metabolism, S-adenosylhomocysteine (AdoHcy) and S-adenosylmethionine (AdoMet), may play a role in Alzheimer"s disease (AD). S-Adenosylmethionine 97-117 methionine adenosyltransferase I, alpha Mus musculus 119-125 18983843-3 2009 Mice deficient in methionine adenosyltransferase 1a (Mat1a KO) have chronic hepatic deficiency of S-adenosylmethionine (SAMe) and increased oxidative stress, and develop HCC. S-Adenosylmethionine 98-118 methionine adenosyltransferase I, alpha Mus musculus 53-58 18695670-2 2008 Lipopolysaccharide (LPS) was shown to inactivate hepatic methionine adenosyltransferase (MAT), the enzyme responsible for S-adenosylmethionine (SAMe) biosynthesis. S-Adenosylmethionine 122-142 methionine adenosyltransferase I, alpha Mus musculus 89-92 11320206-1 2001 Liver-specific and nonliver-specific methionine adenosyltransferases (MATs) are products of two genes, MAT1A and MAT2A, respectively, that catalyze the formation of S-adenosylmethionine (AdoMet), the principal biological methyl donor. S-Adenosylmethionine 165-185 methionine adenosyltransferase I, alpha Mus musculus 187-193 16472822-6 2006 D96A (motif III) showed reduced AdoMet binding but increased activity under conditions of saturation with S-adenosyl-L-methionine (AdoMet), indicating that the contact of Asp96 to AdoMet is not required for catalysis. S-Adenosylmethionine 106-129 methionine adenosyltransferase I, alpha Mus musculus 131-137 16472822-6 2006 D96A (motif III) showed reduced AdoMet binding but increased activity under conditions of saturation with S-adenosyl-L-methionine (AdoMet), indicating that the contact of Asp96 to AdoMet is not required for catalysis. S-Adenosylmethionine 106-129 methionine adenosyltransferase I, alpha Mus musculus 131-137 12736147-0 2003 S-adenosylmethionine (AdoMet) modulates endotoxin stimulated interleukin-10 production in monocytes. S-Adenosylmethionine 0-20 methionine adenosyltransferase I, alpha Mus musculus 22-28 12736147-3 2003 Intracellular deficiency of S-adenosylmethionine (AdoMet) is a hallmark of toxin-induced liver injury. S-Adenosylmethionine 28-48 methionine adenosyltransferase I, alpha Mus musculus 50-56 12060674-3 2002 Mice lacking MAT1A have reduced hepatic S-adenosylmethionine content and hyperplasia and spontaneously develop nonalcoholic steatohepatitis. S-Adenosylmethionine 42-60 methionine adenosyltransferase I, alpha Mus musculus 13-18 34449924-1 2022 BACKGROUND & AIMS: Methionine adenosyltransferase 1A (MAT1A) is responsible for S-adenosylmethionine (SAMe) biosynthesis in the liver. S-Adenosylmethionine 80-100 methionine adenosyltransferase I, alpha Mus musculus 19-52 8468468-1 1993 Defects in the enzymes involved in the pathway of S-adenosylmethionine (AdoMet) metabolism, or inhibition of those enzymes, results in profound immunodeficiency. S-Adenosylmethionine 50-70 methionine adenosyltransferase I, alpha Mus musculus 72-78 2013278-2 1991 A potent irreversible inhibitor of S-adenosylmethionine (AdoMet) decarboxylase, S-(5"-adenosyl)-methylthio-2-aminooxyethane (AdoMeSaoe), was used to study the regulatory control of this key enzyme in the polyamine biosynthetic pathway. S-Adenosylmethionine 35-55 methionine adenosyltransferase I, alpha Mus musculus 57-63 34449924-1 2022 BACKGROUND & AIMS: Methionine adenosyltransferase 1A (MAT1A) is responsible for S-adenosylmethionine (SAMe) biosynthesis in the liver. S-Adenosylmethionine 80-100 methionine adenosyltransferase I, alpha Mus musculus 54-59 34505434-20 2021 MAT1A encodes methionine adenosyltransferase 1A, an essential enzyme that catalyzes the formation of S-adenosylmethionine. S-Adenosylmethionine 101-121 methionine adenosyltransferase I, alpha Mus musculus 0-5 3530324-1 1986 The chirality of biologically active S-adenosyl-L-methionine (AdoMet) is S,S, where the designations refer to the sulfur and the alpha-carbon, respectively. S-Adenosylmethionine 62-68 methionine adenosyltransferase I, alpha Mus musculus 37-60 3426538-1 1987 Treatment of cultured L1210 cells with 1 mM-L-2-amino-4-methoxy-cis-but-3-enoic acid (L-cisAMB), a methionine-analogue inhibitor of S-adenosylmethionine (AdoMet) synthetase (EC 2.5.1.6), produced a rapid and near-total depletion of AdoMet by 4 h. After this, the pools recovered to 60% of control by 48 h, apparently because of an increase in AdoMet synthetase activity. S-Adenosylmethionine 154-160 methionine adenosyltransferase I, alpha Mus musculus 132-152 6330482-4 1984 The concentration of S-adenosylmethionine (AdoMet) and S-adenosylhomocysteine (AdoHcy), the substrate and physiological inhibitor of transmethylation reactions, respectively, were measured in the spleens of control and viral infected mice. S-Adenosylmethionine 21-41 methionine adenosyltransferase I, alpha Mus musculus 43-49