PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29913347-6	2018	RNA methyltransferases, including METTL3/METTL14 responsible for N6-methyladensosine (m6A) formation, share a common structural core and utilize S-adenosyl methionine as a methyl donor.	S-Adenosylmethionine	145-166	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	34-40	
32159918-1	2020	The RNA methylase METTL3 catalyzes the transfer of a methyl group from the cofactor S-adenosyl-L-methionine (SAM) to the N6 atom of adenine.	S-Adenosylmethionine	84-107	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	18-24	
32159918-1	2020	The RNA methylase METTL3 catalyzes the transfer of a methyl group from the cofactor S-adenosyl-L-methionine (SAM) to the N6 atom of adenine.	S-Adenosylmethionine	109-112	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	18-24	
32195181-2	2020	ATTM is also an identified H2S donor and endogenous H2S facilitates VitB12-induced S-adenosylmethionine (SAM) generation, which have been confirmed in m6A methylation and lung cancer development.	S-Adenosylmethionine	83-103	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	151-154	
32195181-2	2020	ATTM is also an identified H2S donor and endogenous H2S facilitates VitB12-induced S-adenosylmethionine (SAM) generation, which have been confirmed in m6A methylation and lung cancer development.	S-Adenosylmethionine	105-108	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	151-154	
34517946-1	2021	The RNA methyltransferase (MTase) complex METTL3-METTL14 transfers methyl groups from S-adenosyl-l-methionine (AdoMet) to the N6-position of adenosines within its consensus sequence, the DRACH motif (D=A, G, U; R=A, G; H=A, C, U).	S-Adenosylmethionine	86-109	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	42-48	
34517946-1	2021	The RNA methyltransferase (MTase) complex METTL3-METTL14 transfers methyl groups from S-adenosyl-l-methionine (AdoMet) to the N6-position of adenosines within its consensus sequence, the DRACH motif (D=A, G, U; R=A, G; H=A, C, U).	S-Adenosylmethionine	111-117	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	42-48	
35143475-7	2022	Finally, control over METTL3/METTL14 condensation is determined by its small molecule cofactor, S-adenosylmethionine (SAM), which regulates conformations of 2 gate loops, and some cancer-associated mutations near gate loops can impair METTL3 condensation.	S-Adenosylmethionine	96-116	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	22-28	
35143475-7	2022	Finally, control over METTL3/METTL14 condensation is determined by its small molecule cofactor, S-adenosylmethionine (SAM), which regulates conformations of 2 gate loops, and some cancer-associated mutations near gate loops can impair METTL3 condensation.	S-Adenosylmethionine	96-116	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	235-241	
35143475-7	2022	Finally, control over METTL3/METTL14 condensation is determined by its small molecule cofactor, S-adenosylmethionine (SAM), which regulates conformations of 2 gate loops, and some cancer-associated mutations near gate loops can impair METTL3 condensation.	S-Adenosylmethionine	118-121	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	22-28	
35143475-7	2022	Finally, control over METTL3/METTL14 condensation is determined by its small molecule cofactor, S-adenosylmethionine (SAM), which regulates conformations of 2 gate loops, and some cancer-associated mutations near gate loops can impair METTL3 condensation.	S-Adenosylmethionine	118-121	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	235-241	
35060905-1	2022	Methyltransferase like-3 (METTL3) and METTL14 complex transfers a methyl group from S-adenosyl-L-methionine to N6 amino group of adenosine bases in RNA (m6A) and DNA (m6dA).	S-Adenosylmethionine	84-107	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	0-24	
35060905-1	2022	Methyltransferase like-3 (METTL3) and METTL14 complex transfers a methyl group from S-adenosyl-L-methionine to N6 amino group of adenosine bases in RNA (m6A) and DNA (m6dA).	S-Adenosylmethionine	84-107	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	26-32	
29913347-6	2018	RNA methyltransferases, including METTL3/METTL14 responsible for N6-methyladensosine (m6A) formation, share a common structural core and utilize S-adenosyl methionine as a methyl donor.	S-Adenosylmethionine	145-166	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	65-89	
27373337-4	2016	We present crystal structures of the complex of Mettl3/Mettl14 methyltransferase domains in apo form as well as with bound S-adenosylmethionine (SAM) or S-adenosylhomocysteine (SAH) in the catalytic site.	S-Adenosylmethionine	123-143	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	48-54	
12355263-1	2002	MT-A70 is the S-adenosylmethionine-binding subunit of human mRNA:m(6)A methyl-transferase (MTase), an enzyme that sequence-specifically methylates adenines in pre-mRNAs.	S-Adenosylmethionine	16-34	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	0-6	
11551827-4	2001	The two splice-variant mRNAs produced from the MT-A70 gene are transcribed at different rates depending on the level of S-adenosyl-L-methionine inhibition.	S-Adenosylmethionine	122-143	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	47-53	
11551827-7	2001	This result indicates that the control of MT-A70 gene expression is directly related to methionine availability and the subsequent synthesis of S-adenosyl-L-methionine.	S-Adenosylmethionine	144-167	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	42-48	
27281194-5	2016	Here we report the crystal structures of the METTL3-METTL14 heterodimer with MTase domains in the ligand-free, S-adenosyl methionine (AdoMet)-bound and S-adenosyl homocysteine (AdoHcy)-bound states, with resolutions of 1.9, 1.71 and 1.61 A, respectively.	S-Adenosylmethionine	111-132	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	45-51	
27281194-5	2016	Here we report the crystal structures of the METTL3-METTL14 heterodimer with MTase domains in the ligand-free, S-adenosyl methionine (AdoMet)-bound and S-adenosyl homocysteine (AdoHcy)-bound states, with resolutions of 1.9, 1.71 and 1.61 A, respectively.	S-Adenosylmethionine	134-140	methyltransferase 3, N6-adenosine-methyltransferase complex catalytic subunit	Homo sapiens	45-51