PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
20393016-3	2010	Recently, we reported that the pyruvate analog 3-bromopyruvate (3-BrPA) promoted tumor cell death by targeting GAPDH.	Pyruvic Acid	31-39	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	111-116	
4316548-1	1970	By competition with lactate dehydrogenase (LDH) for nicotinamide adenine dinucleotide (NAD), commonly occurring intracellular proteins, such as glyceraldehyde-3-phosphate dehydrogenase, malate dehydrogenase, and albumin, can protect LDH-1 and LDH-5 from inhibition and ternary complex formation with NAD and pyruvate.	Pyruvic Acid	308-316	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	144-184	
21895736-1	2012	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has long been recognized as an important enzyme for energy metabolism and the production of ATP and pyruvate through anaerobic glycolysis in the cytoplasm.	Pyruvic Acid	149-157	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	0-40	
21895736-1	2012	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has long been recognized as an important enzyme for energy metabolism and the production of ATP and pyruvate through anaerobic glycolysis in the cytoplasm.	Pyruvic Acid	149-157	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	42-47	
3392029-3	1988	Experiments performed on glucose- and pyruvate-perfused hearts demonstrated the presence of a large contribution to the unidirectional Pi----ATP rate catalyzed by glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate kinase.	Pyruvic Acid	38-46	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	163-203	
596059-1	1977	Pyruvate and K-ferricyanide stimulation of net ATP and 2,3-bisphosphoglycerate synthesis is very probably due to enhancement of glyceraldehyde 3-phosphate dehydrogenase activity.	Pyruvic Acid	0-8	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	128-168	
4341351-7	1972	Adding pyruvate with F increased NAD(+) production at the LDH step, thus reactivating GAPDH, PGK, and Na,K-ATPase and leading to the observed restoration of (22)Na release.	Pyruvic Acid	7-15	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	86-91	
15470234-11	2004	This suggests that the erythrocytic AsV reduction requires both NAD supply and operation of the lower part of the glycolytic pathway starting from glyceraldehyde-3-phosphate dehydrogenase (GAPDH) that, unlike the upper part, remains fed with substrates originating from the degradation of 2,3-bisphosphoglycerate in RBC depleted of glucose by pyruvate.	Pyruvic Acid	343-351	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	189-194