PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
9108263-7	1997	In the presence of 350 nM Z-Pro-prolinal, a specific inhibitor of prolyl endopeptidase, residual Z-Gly-Pro-NH-Mec hydrolysis of 2.6 U/mg protein was observed.	N-benzyloxycarbonylprolylprolinal	26-40	prolyl endopeptidase	Bos taurus	66-86
11437605-3	2001	Unlike PO, however, this peptidase is completely insensitive to the PO-specific inhibitor Z-Pro-prolinal and has been designated Z-Pro-prolinal-insensitive Z-Gly-Pro-MCA-hydrolyzing peptidase (ZIP).	N-benzyloxycarbonylprolylprolinal	90-104	prolyl endopeptidase	Homo sapiens	7-9
11437605-3	2001	Unlike PO, however, this peptidase is completely insensitive to the PO-specific inhibitor Z-Pro-prolinal and has been designated Z-Pro-prolinal-insensitive Z-Gly-Pro-MCA-hydrolyzing peptidase (ZIP).	N-benzyloxycarbonylprolylprolinal	129-143	prolyl endopeptidase	Homo sapiens	7-9
9108263-8	1997	This residual activity was resistant to inhibition by Z-Pro-prolinal at concentrations in excess of 200 times its reported Ki value for prolyl endopeptidase and could not be inhibited under conditions of prolonged incubation with the inhibitor.	N-benzyloxycarbonylprolylprolinal	54-68	prolyl endopeptidase	Bos taurus	136-156
9108263-13	1997	It was subsequently designated Z-Pro-prolinal-insensitive Z-Gly-Pro-NH-Mec-hydrolysing peptidase (ZIP).	N-benzyloxycarbonylprolylprolinal	31-45	fibroblast activation protein alpha	Bos taurus	98-101
9148758-7	1997	It is concluded that Z-Pro-prolinal, a putative transition-state analogue for prolyl oligopeptidase, forms a tetrahedral complex with the enzyme at its catalytic serine, rather than at a neighbouring cysteine that was found to be highly reactive according to chemical modification studies.	N-benzyloxycarbonylprolylprolinal	21-35	prolyl endopeptidase	Homo sapiens	78-99
8089089-5	1994	This fused protein exhibited PEP activity, which was inhibited by Z-Pro-prolinal, a specific inhibitor of PEP.	N-benzyloxycarbonylprolylprolinal	66-80	prolyl endopeptidase	Homo sapiens	29-32
8175672-5	1994	Indeed, both bacitracin and Z-Pro-prolinal, inhibitors of this enzyme, markedly reduced GnRH degradation to any product.	N-benzyloxycarbonylprolylprolinal	28-42	gonadotropin releasing hormone 1	Rattus norvegicus	88-92
8089089-5	1994	This fused protein exhibited PEP activity, which was inhibited by Z-Pro-prolinal, a specific inhibitor of PEP.	N-benzyloxycarbonylprolylprolinal	66-80	prolyl endopeptidase	Homo sapiens	106-109
3330562-2	1987	Among the compounds tested, Z-Gly-Pro-CH2Cl, Z-Val-prolinal, Boc-Pro-prolinal, Z-Pro-prolinal, aniracetam and pramiracetam inhibited the enzyme activities at Ki values in the order of nM to microM, and the effect of the prolinal-containing peptide derivatives was specific for prolyl endopeptidase.	N-benzyloxycarbonylprolylprolinal	79-93	prolyl endopeptidase	Rattus norvegicus	277-297
8392718-2	1993	Bestatin and puromycin were used to inhibit aminopeptidase activity, lisinopril for angiotensin-converting enzyme, phosphoramidon for neutral endopeptidase 24.11, and Z-Pro-prolinal for prolyl endopeptidase.	N-benzyloxycarbonylprolylprolinal	167-181	prolyl endopeptidase	Homo sapiens	186-206
2241932-3	1990	41, 69-75] have shown that benzyloxycarbonyl-prolyl-prolinal (Z-prolyl-prolinal) is a potent inhibitor of prolyl endopeptidase.	N-benzyloxycarbonylprolylprolinal	62-79	prolyl endopeptidase	Mus musculus	106-126
2241932-4	1990	We show that Z-prolyl-prolinal is a slow-binding inhibitor of mouse brain prolyl endopeptidase with Ki 0.35 +/- 0.05 nM.	N-benzyloxycarbonylprolylprolinal	13-30	prolyl endopeptidase	Homo sapiens	74-94
2241932-8	1990	Prolyl endopeptidase from human brain is also inhibited by Z-prolyl-prolinal with kinetics similar to those of the mouse brain enzyme.	N-benzyloxycarbonylprolylprolinal	59-76	prolyl endopeptidase	Homo sapiens	0-20
3071531-4	1988	Thus, N-benzyloxycarbonyl-L-thioprolyl-thiazolidine (Z-Thiopro-thiazolidine) and Z-L-Thiopro-L-thioprolinal showed Ki values of 0.36 and 0.01 nM, respectively, for prolyl endopeptidase from bovine brain; both values were significantly lower than that of Z-Pro-prolinal (Ki, 3.7 nM).	N-benzyloxycarbonylprolylprolinal	254-268	prolyl endopeptidase	Bos taurus	164-184
1653799-8	1991	In contrast, addition of Z-Pro-Prolinal (1 mumol/l), a specific inhibitor of prolyl endopeptidase, prevented the generation of 125I-angiotensin-(1-7) from 125I-angiotensin I by 47.0 +/- 8.0% (n = 6).	N-benzyloxycarbonylprolylprolinal	25-39	prolyl endopeptidase	Canis lupus familiaris	77-97
2162536-4	1990	N-benzyloxycarbonyl-prolyl-prolinal (ZPP), a specific inhibitor of prolyl endopeptidase, inhibited the formation of Ang-(1-7) from Ang I by 35%.	N-benzyloxycarbonylprolylprolinal	0-35	angiotensinogen (serpin peptidase inhibitor, clade A, member 8)	Mus musculus	131-136
6358414-0	1984	Prolyl endopeptidase: inhibition in vivo by N-benzyloxycarbonyl-prolyl-prolinal.	N-benzyloxycarbonylprolylprolinal	44-79	prolyl endopeptidase	Mus musculus	0-20
3681301-8	1987	A combination of the protease inhibitors 1,10-phenanthroline and Z-Pro-Prolinal was able to inhibit almost completely the degradation of neurotensin by clone N1E-115.	N-benzyloxycarbonylprolylprolinal	65-79	neurotensin	Mus musculus	137-148
6358414-1	1984	The activity of prolyl endopeptidase in homogenates of mouse tissues was determined 30 min after intraperitoneal injection of N-benzyloxycarbonyl-prolyl-prolinal (1.25 mg/kg), a potent transition state analog inhibitor (K1 = 14 nM) of prolyl endopeptidase (EC 3.4.21.26).	N-benzyloxycarbonylprolylprolinal	126-161	prolyl endopeptidase	Mus musculus	16-36
25564858-6	2015	Here, we present an exhaustive sampling of POP with a known inhibitor, Z-pro-prolinal.	N-benzyloxycarbonylprolylprolinal	71-85	prolyl endopeptidase	Homo sapiens	43-46
6345724-0	1983	Inhibition of rabbit brain prolyl endopeptidase by n-benzyloxycarbonyl-prolyl-prolinal, a transition state aldehyde inhibitor.	N-benzyloxycarbonylprolylprolinal	51-86	prolyl endopeptidase	Oryctolagus cuniculus	27-47
31786979-5	2020	By contrast, a POP inhibitor, Z-Pro-Prolinal reduced the rise in plasma Ang-(1-7) after infusing Ang II to control WT mice.	N-benzyloxycarbonylprolylprolinal	30-44	angiogenin, ribonuclease, RNase A family, 5	Mus musculus	72-80
31786979-5	2020	By contrast, a POP inhibitor, Z-Pro-Prolinal reduced the rise in plasma Ang-(1-7) after infusing Ang II to control WT mice.	N-benzyloxycarbonylprolylprolinal	30-44	angiotensinogen (serpin peptidase inhibitor, clade A, member 8)	Mus musculus	97-103
23392115-6	2013	Furthermore, the dual prolyl carboxypeptidase (PCP)-prolyl endopeptidase (PEP) inhibitor Z-prolyl-prolinal reduced ANG-(1-7) formation in ACE2 KO mice, while the ACE2 inhibitor MLN-4760 had no effect.	N-benzyloxycarbonylprolylprolinal	89-106	prolyl endopeptidase	Mus musculus	74-77
23392115-6	2013	Furthermore, the dual prolyl carboxypeptidase (PCP)-prolyl endopeptidase (PEP) inhibitor Z-prolyl-prolinal reduced ANG-(1-7) formation in ACE2 KO mice, while the ACE2 inhibitor MLN-4760 had no effect.	N-benzyloxycarbonylprolylprolinal	89-106	angiotensin I converting enzyme (peptidyl-dipeptidase A) 2	Mus musculus	138-142
23392115-6	2013	Furthermore, the dual prolyl carboxypeptidase (PCP)-prolyl endopeptidase (PEP) inhibitor Z-prolyl-prolinal reduced ANG-(1-7) formation in ACE2 KO mice, while the ACE2 inhibitor MLN-4760 had no effect.	N-benzyloxycarbonylprolylprolinal	89-106	angiotensin I converting enzyme (peptidyl-dipeptidase A) 2	Mus musculus	162-166
22318946-10	2012	The ACE2 inhibitor MLN-4760 and PCP/PEP inhibitor Z-pro-prolinal reduced cortical Ang-(1-7) formation.	N-benzyloxycarbonylprolylprolinal	50-64	prolyl endopeptidase	Mus musculus	36-39
22318946-10	2012	The ACE2 inhibitor MLN-4760 and PCP/PEP inhibitor Z-pro-prolinal reduced cortical Ang-(1-7) formation.	N-benzyloxycarbonylprolylprolinal	50-64	angiogenin, ribonuclease, RNase A family, 5	Mus musculus	82-90
20024801-1	2009	We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex.	N-benzyloxycarbonylprolylprolinal	72-86	prolyl endopeptidase	Homo sapiens	33-54
26596426-0	2011	Use of Umbrella Sampling to Calculate the Entrance/Exit Pathway for Z-Pro-Prolinal Inhibitor in Prolyl Oligopeptidase.	N-benzyloxycarbonylprolylprolinal	68-82	prolyl endopeptidase	Homo sapiens	96-117
26596426-4	2011	We examined three possible binding pathways using Steered Molecular Dynamics (SMD) and Umbrella Sampling (US) on a crystal structure of porcine POP with bound Z-pro-prolinal (ZPP).	N-benzyloxycarbonylprolylprolinal	159-173	prolyl endopeptidase	Homo sapiens	144-147
26596426-4	2011	We examined three possible binding pathways using Steered Molecular Dynamics (SMD) and Umbrella Sampling (US) on a crystal structure of porcine POP with bound Z-pro-prolinal (ZPP).	N-benzyloxycarbonylprolylprolinal	175-178	prolyl endopeptidase	Homo sapiens	144-147
21297000-6	2011	Pharmacologic inhibition of PRCP with Z-Pro-Prolinal or plasma kallikrein with soybean trypsin inhibitor, Pro-Phe-Arg-chloromethylketone or PKSI 527 also shortens carotid artery occlusion times.	N-benzyloxycarbonylprolylprolinal	38-52	prolylcarboxypeptidase (angiotensinase C)	Mus musculus	28-32
20371359-7	2010	Activated KLK3 was reversibly inhibited by Z-Pro-Prolinal and competitively inhibited by ortho-phenantroline.	N-benzyloxycarbonylprolylprolinal	43-57	kallikrein related peptidase 3	Homo sapiens	10-14
20024801-1	2009	We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex.	N-benzyloxycarbonylprolylprolinal	72-86	prolyl endopeptidase	Homo sapiens	56-59
20024801-1	2009	We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex.	N-benzyloxycarbonylprolylprolinal	72-86	prolyl endopeptidase	Homo sapiens	200-203
20024801-1	2009	We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex.	N-benzyloxycarbonylprolylprolinal	88-91	prolyl endopeptidase	Homo sapiens	33-54
20024801-1	2009	We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex.	N-benzyloxycarbonylprolylprolinal	88-91	prolyl endopeptidase	Homo sapiens	56-59
20024801-1	2009	We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex.	N-benzyloxycarbonylprolylprolinal	204-207	prolyl endopeptidase	Homo sapiens	33-54
20024801-1	2009	We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex.	N-benzyloxycarbonylprolylprolinal	204-207	prolyl endopeptidase	Homo sapiens	56-59
20024801-1	2009	We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex.	N-benzyloxycarbonylprolylprolinal	204-207	prolyl endopeptidase	Homo sapiens	200-203
20024801-2	2009	We performed 100 ns of simulation with the hemiacetal bond, through which the ZPP is bound to the POP, removed in order to better investigate the binding cavity environment.	N-benzyloxycarbonylprolylprolinal	78-81	prolyl endopeptidase	Homo sapiens	98-101
18927208-10	2009	When CCRF-CEM human leukemia cells were treated with N-benzyloxycarbonylprolylprolinal (BCPP), an inhibitor of prolyl oligopeptidase, there was a 30-fold increase in the IC(50) of tasidotin and a marked increase in intracellular [(3)H]tasidotin.	N-benzyloxycarbonylprolylprolinal	53-86	prolyl endopeptidase	Homo sapiens	111-132
18927208-10	2009	When CCRF-CEM human leukemia cells were treated with N-benzyloxycarbonylprolylprolinal (BCPP), an inhibitor of prolyl oligopeptidase, there was a 30-fold increase in the IC(50) of tasidotin and a marked increase in intracellular [(3)H]tasidotin.	N-benzyloxycarbonylprolylprolinal	88-92	prolyl endopeptidase	Homo sapiens	111-132
16942854-0	2006	A prolyl oligopeptidase inhibitor, Z-Pro-Prolinal, inhibits glyceraldehyde-3-phosphate dehydrogenase translocation and production of reactive oxygen species in CV1-P cells exposed to 6-hydroxydopamine.	N-benzyloxycarbonylprolylprolinal	35-49	prolyl endopeptidase	Homo sapiens	2-23
16942854-0	2006	A prolyl oligopeptidase inhibitor, Z-Pro-Prolinal, inhibits glyceraldehyde-3-phosphate dehydrogenase translocation and production of reactive oxygen species in CV1-P cells exposed to 6-hydroxydopamine.	N-benzyloxycarbonylprolylprolinal	35-49	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	60-100