PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
9330697-2	1997	This protein, referred to as DPP IV-beta, shows a higher KM value for Gly-Pro-pNA than CD26 (0.31 mM compared to 0.11 mM, respectively).	Gly-Pro-pNA	70-81	dipeptidyl peptidase 4	Homo sapiens	29-35
1572909-2	1992	One activity removing dipeptides from the NH2-terminal end of Gly-Pro-pNA was specifically inhibited by di-isopropyl-fluorophosphate (DFP), phenylmethanesulphony fluoride (PMSF), and diprotin A, and thus was identified as dipeptidyl peptidase IV (DPP IV).	Gly-Pro-pNA	62-73	dipeptidyl peptidase 4	Homo sapiens	222-245
8574390-2	1995	In contrast to the conventional DP IV substrate glycyl-prolyl-p-nitroanilide (Gly-Pro-pNA), the hydrolysis of this peptide by DP IV was found to be significantly inhibited by anti-DP IV antibodies.	Gly-Pro-pNA	78-89	dipeptidyl peptidase 4	Homo sapiens	126-131
8574390-2	1995	In contrast to the conventional DP IV substrate glycyl-prolyl-p-nitroanilide (Gly-Pro-pNA), the hydrolysis of this peptide by DP IV was found to be significantly inhibited by anti-DP IV antibodies.	Gly-Pro-pNA	78-89	dipeptidyl peptidase 4	Homo sapiens	126-131
7714663-2	1995	Its hydrolysis by DPPIV resulted in the formation of a chromophore, 2,6-dibromophenol-indo-p-xylenol, and its maximal absorption wavelength (600 nm) was longer than that of p-nitroaniline (415 nm) released from conventional substrate, glycyl-L-proline p-nitroanilide (Gly-Pro-pNA).	Gly-Pro-pNA	268-279	dipeptidyl peptidase 4	Homo sapiens	18-23
1572909-2	1992	One activity removing dipeptides from the NH2-terminal end of Gly-Pro-pNA was specifically inhibited by di-isopropyl-fluorophosphate (DFP), phenylmethanesulphony fluoride (PMSF), and diprotin A, and thus was identified as dipeptidyl peptidase IV (DPP IV).	Gly-Pro-pNA	62-73	dipeptidyl peptidase 4	Homo sapiens	247-253
6151772-2	1984	The hydrolysis rate of Gly-Pro-pNA in suspensions of MNC correlates well with the number of DP IV reactive cells as determined by cytochemical staining.	Gly-Pro-pNA	23-34	dipeptidyl peptidase 4	Homo sapiens	92-97
2896517-5	1988	Derivatives of Gly-Pro-pNA where the N-terminal amino group is methylated are hydrolyzed by dipeptidyl peptidase IV.	Gly-Pro-pNA	15-26	dipeptidyl peptidase 4	Sus scrofa	92-115
16364232-0	2006	Mechanism of Gly-Pro-pNA cleavage catalyzed by dipeptidyl peptidase-IV and its inhibition by saxagliptin (BMS-477118).	Gly-Pro-pNA	13-24	dipeptidyl peptidase 4	Homo sapiens	47-70
16835316-7	2006	Attractin immunoprecipitates hydrolyzed Gly-Pro-pNA, indicating that monocyte-expressed attractin possesses DP IV-like activity.	Gly-Pro-pNA	40-51	attractin	Homo sapiens	0-9
16835316-7	2006	Attractin immunoprecipitates hydrolyzed Gly-Pro-pNA, indicating that monocyte-expressed attractin possesses DP IV-like activity.	Gly-Pro-pNA	40-51	attractin	Homo sapiens	88-97
16835316-7	2006	Attractin immunoprecipitates hydrolyzed Gly-Pro-pNA, indicating that monocyte-expressed attractin possesses DP IV-like activity.	Gly-Pro-pNA	40-51	dipeptidyl peptidase 4	Homo sapiens	108-113
16364232-2	2006	Our pH data suggest that Gly-Pro-pNA cleavage catalyzed by DPP-IV is facilitated by an ionization of a residue with a pK of 7.2 +/- 0.1.	Gly-Pro-pNA	25-36	dipeptidyl peptidase 4	Homo sapiens	59-65
15039077-5	2004	Using the chromogenic H-Gly-Pro-pNA as the substrate, a kinetic study shows that purified DPP8 is active and has a similar kcat value as that of DPP-IV, a prolyl dipeptidase that is a drug target for type II diabetes.	Gly-Pro-pNA	22-35	dipeptidyl peptidase 8	Homo sapiens	90-94
15039077-5	2004	Using the chromogenic H-Gly-Pro-pNA as the substrate, a kinetic study shows that purified DPP8 is active and has a similar kcat value as that of DPP-IV, a prolyl dipeptidase that is a drug target for type II diabetes.	Gly-Pro-pNA	22-35	dipeptidyl peptidase 4	Homo sapiens	145-151
11883961-5	2002	Inhibition of DP IV hydrolysis of the substrate Gly-Pro-pNA by metformin was examined spectrophotometrically.	Gly-Pro-pNA	48-59	dipeptidyl peptidase 4	Homo sapiens	14-19
14691230-7	2004	The kinetic parameters of dipeptidyl peptidase cleavage of wild-type DPPIV and the N-glycosylation site mutants were determined by using Ala-Pro-AFC and Gly-Pro-pNA as substrates and varied by <50%.	Gly-Pro-pNA	153-164	dipeptidyl peptidase 4	Homo sapiens	69-74