PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6289905-1	1982	Two derivatives of NAD+ spin-labeled at N6 or C-8 of the adenine ring have been shown previously to be active coenzymes of glyceraldehyde-3-phosphate dehydrogenase (D-glyceraldehyde-3-phosphate: NAD+ oxidoreductase (phosphorylating), EC 1.2.1.12).	Adenine	57-64	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	123-163	
8912669-13	1996	Studies with the NAD+ molecule radio-labelled in the nicotinamide or adenine portion revealed that both portions of the NAD+ molecule are linked to GAPDH.	Adenine	69-76	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	148-153	
8327504-2	1993	Incubations of GAPDH with the NO-releasing agent sodium nitroprusside (SNP) and NAD resulted, however, in essentially equal incorporation of radiolabel from the adenine, phosphate, and nicotinamide moieties to the extent of approximately 0.02 mol of NAD.mol of GAPDH-1.	Adenine	161-168	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	15-20	
18467771-4	2007	Comparison of the NAD;{+} binding pocket of the modeled TvGAPDH with human GAPDH (hGAPDH) reveals the presence of a hydrophobic pocket near the N-6 position of adenine ring as well as a hydrophobic cleft near O-2" of the adenosine ribose that are absent in the human enzyme.	Adenine	160-167	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	58-63	
27135296-8	2017	In all five cases, a replacement of guanine by adenine was revealed in the intron region between the sixth and the seventh exons of GAPDS.	Adenine	47-54	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	132-137	
204787-0	1977	The role of the nicotinamide and adenine subsites in the negative co-operativity of coenzyme binding to glyceraldehyde-3-phosphate dehydrogenase.	Adenine	33-40	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	104-144	
18467771-4	2007	Comparison of the NAD;{+} binding pocket of the modeled TvGAPDH with human GAPDH (hGAPDH) reveals the presence of a hydrophobic pocket near the N-6 position of adenine ring as well as a hydrophobic cleft near O-2" of the adenosine ribose that are absent in the human enzyme.	Adenine	160-167	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	82-88	
18467771-6	2007	Our docking result suggests that bulkier hydrophobic substitution at the N-6 position of the adenine ring could form more stable complexes with TvGAPDH than with hGAPDH.	Adenine	93-100	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	162-168	
10964654-3	2000	Previously, we have characterized the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as an RNA-binding protein with preference to adenine-uracil-rich sequences.	Adenine	150-157	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	56-96	
10964654-3	2000	Previously, we have characterized the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as an RNA-binding protein with preference to adenine-uracil-rich sequences.	Adenine	150-157	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	98-103