PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 29379364-3 2018 S-adenosyl-l-methionine (SAM) is an important intermediate of folic acid pathway and acts as methyl donor and substrate for DNA (cytosine-5)-methyltransferase 3B (DNMT3B - EC 2.1.1.37) de novo methylation processes during embryogenesis. S-Adenosylmethionine 0-23 DNA methyltransferase 3 beta Homo sapiens 124-161 30309036-2 2018 The methylation of DNA is regulated by DNA methyltransferases (DNMT1, DNMT3a, and DNMT3b) in the presence of S-adenosylmethionine (SAM), which serves as a methyl group donor. S-Adenosylmethionine 109-129 DNA methyltransferase 3 beta Homo sapiens 82-88 30309036-2 2018 The methylation of DNA is regulated by DNA methyltransferases (DNMT1, DNMT3a, and DNMT3b) in the presence of S-adenosylmethionine (SAM), which serves as a methyl group donor. S-Adenosylmethionine 131-134 DNA methyltransferase 3 beta Homo sapiens 82-88 29379364-3 2018 S-adenosyl-l-methionine (SAM) is an important intermediate of folic acid pathway and acts as methyl donor and substrate for DNA (cytosine-5)-methyltransferase 3B (DNMT3B - EC 2.1.1.37) de novo methylation processes during embryogenesis. S-Adenosylmethionine 0-23 DNA methyltransferase 3 beta Homo sapiens 163-169 29379364-3 2018 S-adenosyl-l-methionine (SAM) is an important intermediate of folic acid pathway and acts as methyl donor and substrate for DNA (cytosine-5)-methyltransferase 3B (DNMT3B - EC 2.1.1.37) de novo methylation processes during embryogenesis. S-Adenosylmethionine 25-28 DNA methyltransferase 3 beta Homo sapiens 124-161 29379364-3 2018 S-adenosyl-l-methionine (SAM) is an important intermediate of folic acid pathway and acts as methyl donor and substrate for DNA (cytosine-5)-methyltransferase 3B (DNMT3B - EC 2.1.1.37) de novo methylation processes during embryogenesis. S-Adenosylmethionine 25-28 DNA methyltransferase 3 beta Homo sapiens 163-169 23957506-3 2013 We tested the hypothesis that plasma S-adenosylmethionine (SAM) level alone or in combination with genetic variation in DNA methyltransferases (DNMT1, DNMT3A and DNMT3B) was associated with global DNA methylation extent at long interspersed nucleotide element-1 (LINE-1) sequences. S-Adenosylmethionine 37-57 DNA methyltransferase 3 beta Homo sapiens 162-168 25289094-1 2014 DNA methyltransferases (including DNMT1, DNMT3A and DNMT3B), catalyze the transfer of methyl groups from S-adenosyl-l-methionine to cytosine position 5; this methylation in promoter regions silences gene expression. S-Adenosylmethionine 105-128 DNA methyltransferase 3 beta Homo sapiens 52-58 23957506-3 2013 We tested the hypothesis that plasma S-adenosylmethionine (SAM) level alone or in combination with genetic variation in DNA methyltransferases (DNMT1, DNMT3A and DNMT3B) was associated with global DNA methylation extent at long interspersed nucleotide element-1 (LINE-1) sequences. S-Adenosylmethionine 59-62 DNA methyltransferase 3 beta Homo sapiens 162-168 21549127-4 2011 First, DNMT3B, unlike DNMT3A, requires a DNA cofactor in order to stably bind to S-adenosyl-l-methionine (SAM), suggesting that it proceeds according to an ordered catalytic scheme. S-Adenosylmethionine 81-104 DNA methyltransferase 3 beta Homo sapiens 7-13 21839172-4 2011 Herein we report long (>100ns) molecular dynamics simulations for human DNMT3B bound to nanaomycin A with and without the presence of the cofactor S-adenosyl-L-methionine (SAM). S-Adenosylmethionine 150-173 DNA methyltransferase 3 beta Homo sapiens 75-81 21839172-4 2011 Herein we report long (>100ns) molecular dynamics simulations for human DNMT3B bound to nanaomycin A with and without the presence of the cofactor S-adenosyl-L-methionine (SAM). S-Adenosylmethionine 175-178 DNA methyltransferase 3 beta Homo sapiens 75-81