PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3827929-0	1987	Characterization of the fusogenic properties of glyceraldehyde-3-phosphate dehydrogenase: fusion of phospholipid vesicles.	Phospholipids	100-112	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	48-88	
18793820-2	2008	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is considered a classical glycolytic protein that can promote the fusion of phospholipid vesicles and can also play a vital role on in vivo fusogenic events.	Phospholipids	125-137	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	0-40	
18793820-2	2008	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is considered a classical glycolytic protein that can promote the fusion of phospholipid vesicles and can also play a vital role on in vivo fusogenic events.	Phospholipids	125-137	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	42-47	
15301528-4	2004	In this study, we show that membranes containing phosphatidylserine (PS), a negatively charged phospholipid, induce a rapid formation of fibers by a variety of proteins, viz., lysozyme, insulin, glyceraldehyde-3-phosphate dehydrogenase, myoglobin, transthyretin, cytochrome c, histone H1, and alpha-lactalbumin.	Phospholipids	95-107	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	195-235	
10471367-1	1999	We have investigated the fusion of phospholipid vesicles induced by lysozyme and glyceraldehyde-3-phosphate dehydrogenase (GAPDH).	Phospholipids	35-47	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	81-121	
10471367-1	1999	We have investigated the fusion of phospholipid vesicles induced by lysozyme and glyceraldehyde-3-phosphate dehydrogenase (GAPDH).	Phospholipids	35-47	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	123-128	
9498570-3	1997	One polyclonal antibody, designated aPSD-2, crossreacted with GAPDH, and its binding to GAPDH was inhibited by PS but not by other phospholipids such as phosphatidylethanolamine and phosphatidylinositol.	Phospholipids	131-144	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	88-93	
9498570-4	1997	Kinetic analysis of GAPDH binding to phospholipid membranes by measuring surface plasmon resonance showed that GAPDH associated with the phospholipid membrane containing PS rapidly (k[on] =2.8 X 10(4) M(-1) X s[-1]) and dissociated extremely slowly (k[off]=5.9 X 10(-5) s[-1]), giving a low dissociation constant (KD=2.6nM).	Phospholipids	37-49	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	20-25	
9498570-4	1997	Kinetic analysis of GAPDH binding to phospholipid membranes by measuring surface plasmon resonance showed that GAPDH associated with the phospholipid membrane containing PS rapidly (k[on] =2.8 X 10(4) M(-1) X s[-1]) and dissociated extremely slowly (k[off]=5.9 X 10(-5) s[-1]), giving a low dissociation constant (KD=2.6nM).	Phospholipids	37-49	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	111-116	
9498570-4	1997	Kinetic analysis of GAPDH binding to phospholipid membranes by measuring surface plasmon resonance showed that GAPDH associated with the phospholipid membrane containing PS rapidly (k[on] =2.8 X 10(4) M(-1) X s[-1]) and dissociated extremely slowly (k[off]=5.9 X 10(-5) s[-1]), giving a low dissociation constant (KD=2.6nM).	Phospholipids	137-149	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	20-25	
9498570-4	1997	Kinetic analysis of GAPDH binding to phospholipid membranes by measuring surface plasmon resonance showed that GAPDH associated with the phospholipid membrane containing PS rapidly (k[on] =2.8 X 10(4) M(-1) X s[-1]) and dissociated extremely slowly (k[off]=5.9 X 10(-5) s[-1]), giving a low dissociation constant (KD=2.6nM).	Phospholipids	137-149	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	111-116	
12743-0	1976	Modification of glyceraldehyde 3-phosphate dehydrogenase activity by adsorption on phospholipid vesicles.	Phospholipids	83-95	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	16-56	
1001731-0	1976	Modification of glyceraldehyde 3-phosphate dehydrogenase activity by adsorption to erythrocyte membranes and phospholipid vesicles.	Phospholipids	109-121	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	16-56