PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11988094-2	2002	In this study the role of NO in the shedding of the glycosylphosphatidylinositol (GPI)-anchored form of renal dipeptidase (RDPase) was examined.	Glycosylphosphatidylinositols	52-80	dipeptidase 1	Homo sapiens	104-121	
17615681-0	2007	Release of renal dipeptidase from glycosylphosphatidylinositol anchor by insulin-triggered phospholipase C/intracellular Ca2+.	Glycosylphosphatidylinositols	34-62	dipeptidase 1	Homo sapiens	11-28	
11988094-2	2002	In this study the role of NO in the shedding of the glycosylphosphatidylinositol (GPI)-anchored form of renal dipeptidase (RDPase) was examined.	Glycosylphosphatidylinositols	52-80	dipeptidase 1	Homo sapiens	123-129	
11988094-2	2002	In this study the role of NO in the shedding of the glycosylphosphatidylinositol (GPI)-anchored form of renal dipeptidase (RDPase) was examined.	Glycosylphosphatidylinositols	82-85	dipeptidase 1	Homo sapiens	104-121	
11988094-2	2002	In this study the role of NO in the shedding of the glycosylphosphatidylinositol (GPI)-anchored form of renal dipeptidase (RDPase) was examined.	Glycosylphosphatidylinositols	82-85	dipeptidase 1	Homo sapiens	123-129	
2168407-8	1990	These results suggest that the mature hrDP molecule lacks the carboxyl-terminal hydrophobic peptide extension predicted from the cDNA sequence and is anchored at Ser369 via glycosylphosphatidylinositol to the membrane.	Glycosylphosphatidylinositols	173-201	dipeptidase 1	Homo sapiens	38-42	
11834871-0	2002	Glycosyl-phosphatidylinositol (GPI)-anchored renal dipeptidase is released by a phospholipase C in vivo.	Glycosylphosphatidylinositols	0-29	dipeptidase 1	Homo sapiens	45-62	
11834871-0	2002	Glycosyl-phosphatidylinositol (GPI)-anchored renal dipeptidase is released by a phospholipase C in vivo.	Glycosylphosphatidylinositols	31-34	dipeptidase 1	Homo sapiens	45-62	
2137335-0	1990	Characterization of the glycosyl-phosphatidylinositol-anchored human renal dipeptidase reveals that it is more extensively glycosylated than the pig enzyme.	Glycosylphosphatidylinositols	24-53	dipeptidase 1	Homo sapiens	69-86	
2137335-4	1990	The glycosyl-phosphatidylinositol anchor of purified human renal dipeptidase was hydrolysed by a range of bacterial PI-PLCs and by a plasma phospholipase D. Mild acid treatment and nitrous acid deamination of the hydrophilic form revealed that the cross-reacting determinant, characteristic of the glycosyl-phosphatidylinositol anchor, was due exclusively to the inositol 1,2-cyclic phosphate ring epitope.	Glycosylphosphatidylinositols	4-33	dipeptidase 1	Homo sapiens	59-76	
2137335-4	1990	The glycosyl-phosphatidylinositol anchor of purified human renal dipeptidase was hydrolysed by a range of bacterial PI-PLCs and by a plasma phospholipase D. Mild acid treatment and nitrous acid deamination of the hydrophilic form revealed that the cross-reacting determinant, characteristic of the glycosyl-phosphatidylinositol anchor, was due exclusively to the inositol 1,2-cyclic phosphate ring epitope.	Glycosylphosphatidylinositols	298-327	dipeptidase 1	Homo sapiens	59-76