PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
34682765-7	2021	The TGZ cytotoxicity was accompanied by increase in PRODH/POX expression, ROS production, expression of cleaved caspase-3, caspase-9 and PARP, inhibition of collagen biosynthesis, prolidase activity and decrease in intracellular proline concentration.	Troglitazone	4-7	peptidase D	Homo sapiens	180-189
35165443-5	2022	CQ31 inhibits the M24B aminopeptidases prolidase (PEPD) and Xaa-Pro aminopeptidase 1 (XPNPEP1), leading to the accumulation of proline-containing peptides that inhibit DPP8/9 and thereby activate CARD8.	Proline	127-134	peptidase D	Homo sapiens	39-48
34532344-1	2021	Prolidase (peptidase D), encoded by the PEPD gene, is a ubiquitously expressed cytosolic metalloproteinase, the only enzyme capable of cleaving imidodipeptides containing C-terminal proline or hydroxyproline.	imidodipeptides	144-159	peptidase D	Homo sapiens	0-9
34532344-1	2021	Prolidase (peptidase D), encoded by the PEPD gene, is a ubiquitously expressed cytosolic metalloproteinase, the only enzyme capable of cleaving imidodipeptides containing C-terminal proline or hydroxyproline.	imidodipeptides	144-159	peptidase D	Homo sapiens	40-44
34532344-1	2021	Prolidase (peptidase D), encoded by the PEPD gene, is a ubiquitously expressed cytosolic metalloproteinase, the only enzyme capable of cleaving imidodipeptides containing C-terminal proline or hydroxyproline.	Proline	182-189	peptidase D	Homo sapiens	0-9
34532344-1	2021	Prolidase (peptidase D), encoded by the PEPD gene, is a ubiquitously expressed cytosolic metalloproteinase, the only enzyme capable of cleaving imidodipeptides containing C-terminal proline or hydroxyproline.	Proline	182-189	peptidase D	Homo sapiens	40-44
34532344-1	2021	Prolidase (peptidase D), encoded by the PEPD gene, is a ubiquitously expressed cytosolic metalloproteinase, the only enzyme capable of cleaving imidodipeptides containing C-terminal proline or hydroxyproline.	Hydroxyproline	193-207	peptidase D	Homo sapiens	0-9
34532344-1	2021	Prolidase (peptidase D), encoded by the PEPD gene, is a ubiquitously expressed cytosolic metalloproteinase, the only enzyme capable of cleaving imidodipeptides containing C-terminal proline or hydroxyproline.	Hydroxyproline	193-207	peptidase D	Homo sapiens	40-44
34577574-11	2021	In MCF-7 breast cancer cells, Cx affected proline metabolism through upregulation of proline biosynthesis, PRODH/POX and PYCRs expressions, PEPD activity, and downregulation of collagen biosynthesis.	Proline	42-49	peptidase D	Homo sapiens	140-144
34449881-5	2022	A remarkable positive relationship of prolidase with vitamin E was observed in both patient and control group (r=0.892, p=0.001, r=0.659, p=0.001, respectively).	Vitamin E	53-62	peptidase D	Homo sapiens	38-47
34449881-6	2022	A positive weak relationship was identified between prolidase activity and TOS levels and also between vitamin E and TOS levels in UEI group (r=0.265, p=0.049, r=0.288, p=0.014, respectively).	tos	75-78	peptidase D	Homo sapiens	52-61
35165443-5	2022	CQ31 inhibits the M24B aminopeptidases prolidase (PEPD) and Xaa-Pro aminopeptidase 1 (XPNPEP1), leading to the accumulation of proline-containing peptides that inhibit DPP8/9 and thereby activate CARD8.	Proline	127-134	peptidase D	Homo sapiens	50-54
35165443-5	2022	CQ31 inhibits the M24B aminopeptidases prolidase (PEPD) and Xaa-Pro aminopeptidase 1 (XPNPEP1), leading to the accumulation of proline-containing peptides that inhibit DPP8/9 and thereby activate CARD8.	Peptides	146-154	peptidase D	Homo sapiens	39-48
35165443-5	2022	CQ31 inhibits the M24B aminopeptidases prolidase (PEPD) and Xaa-Pro aminopeptidase 1 (XPNPEP1), leading to the accumulation of proline-containing peptides that inhibit DPP8/9 and thereby activate CARD8.	Peptides	146-154	peptidase D	Homo sapiens	50-54
2924773-1	1989	Consideration of the active-site model of prolidase led us to examine azetidine, pyrrolidine and piperidine substrate analogs as potential in vivo inhibitors of the enzyme.	azetidine	70-79	peptidase D	Homo sapiens	42-51
35356903-6	2022	There was weak positive correlation between prolidase and FEV1 (r = 0.222, P = .033) and FEV1/forced vital capacity (r = 0.230, P = .027).Our study shows that systemic inflammation, prolidase activity, and SA levels in stable COPD patients are associated with airflow obstruction severity.	N-Acetylneuraminic Acid	206-208	peptidase D	Homo sapiens	44-53
35433830-4	2022	Inhibition of PEPD-dependent EGFR signaling by gefitinib supported the finding.	Gefitinib	47-56	peptidase D	Homo sapiens	14-18
35197125-1	2022	BACKGROUND: Prolidase deficiency (PD) is an autosomal recessive inborn multisystemic disease caused by mutations in the PEPD gene encoding the enzyme prolidase D, leading to defects in turnover of proline-containing proteins, such as collagen.	Proline	197-204	peptidase D	Homo sapiens	120-124
2673209-5	1989	Products of most loci have multiple, overlapping substrate affinities (except for the products of Pep-D, which react only with a peptide containing a carboxyterminal proline).	Proline	166-173	peptidase D	Homo sapiens	98-103
2924773-1	1989	Consideration of the active-site model of prolidase led us to examine azetidine, pyrrolidine and piperidine substrate analogs as potential in vivo inhibitors of the enzyme.	pyrrolidine	81-92	peptidase D	Homo sapiens	42-51
2924773-1	1989	Consideration of the active-site model of prolidase led us to examine azetidine, pyrrolidine and piperidine substrate analogs as potential in vivo inhibitors of the enzyme.	piperidine	97-107	peptidase D	Homo sapiens	42-51
2924773-2	1989	One of these, N-benzyloxycarbonyl-L-proline, was shown to be a potent competitive inhibitor of porcine kidney prolidase (Ki = 90 microM); its rapid protein-mediated permeation of human and sheep erythrocytes suggests that it may be effective in vivo.	carbobenzoxyproline	14-43	peptidase D	Homo sapiens	110-119
2924773-4	1989	Analysis of inhibitor action and consideration of X-ray crystallographic data of relevant Mn2+ complexes allowed the active-site model of prolidase to be further refined; a new model is presented in which the substrate acts as a bidentate ligand towards the active-site manganous ion.	Manganese(2+)	90-94	peptidase D	Homo sapiens	138-147
3139928-1	1988	A 17-year-old girl was shown to have prolidase deficiency on the basis of the presence of large amounts of proline-containing dipeptides in urine and an almost complete absence of prolidase in plasma and erythrocytes.	Proline	107-114	peptidase D	Homo sapiens	37-46
2713125-4	1989	Following this novel step, prolidase retains full activity, obviating the requirement for preincubation of each enzyme fraction with Mn2+ prior to assay.	Manganese(2+)	133-137	peptidase D	Homo sapiens	27-36
3139929-3	1988	Both normal and the patients" mother"s prolidase activity against gly-pro was reduced about 20% at 60 degrees C compared to the activity at 37 degrees C, but the addition of Mn2+ at 55 degrees C increased the activity about 1.8-fold, whereas prolidase activity of patients could not be increased by the addition of Mn2+.	Manganese(2+)	315-319	peptidase D	Homo sapiens	39-48
3205627-6	1988	As a consequence, the activity of prolidase in hemolysates increases to 159 mumol glycyl-L-proline hydrolyzed/h/ml compared to 5 mumol/h/ml for hemolysates of cells incubated in the absence of Mn++.	glycylproline	82-98	peptidase D	Homo sapiens	34-43
3205627-8	1988	After exogenous MnCl2 is removed from the storage buffer, high levels of erythrocyte prolidase activity persist for at least 13 days.	manganese chloride	16-21	peptidase D	Homo sapiens	85-94
3276413-0	1988	Effect of captopril and other inhibitors of angiotensin-converting enzyme on plasma prolidase activity.	Captopril	10-19	peptidase D	Homo sapiens	84-93
3148067-2	1988	With pro-val as substrate and manganese in the reaction buffer, prolinase activity was higher in prolidase-deficient cells than in control cells (mean (SEM) 917 (67) nmol min-1 mg-1, n = 3, control mean (SEM) 294, (50), n = 11).	prolylvaline	5-12	peptidase D	Homo sapiens	97-106
3148067-2	1988	With pro-val as substrate and manganese in the reaction buffer, prolinase activity was higher in prolidase-deficient cells than in control cells (mean (SEM) 917 (67) nmol min-1 mg-1, n = 3, control mean (SEM) 294, (50), n = 11).	Manganese	30-39	peptidase D	Homo sapiens	97-106
3148067-6	1988	We suggest that in prolidase-deficient fibroblasts, this rise in prolinase activity constitutes an attempt to compensate for the prolidase deficiency by increasing the greatly reduced intracellular proline pool.	Proline	198-205	peptidase D	Homo sapiens	19-28
3139928-1	1988	A 17-year-old girl was shown to have prolidase deficiency on the basis of the presence of large amounts of proline-containing dipeptides in urine and an almost complete absence of prolidase in plasma and erythrocytes.	Dipeptides	126-136	peptidase D	Homo sapiens	37-46
3139929-1	1988	Prolidase activity in serum from normal subjects and the mother of two patients was readily detected without adding Mn2+ to the assay, and the activity was increased by addition of Mn2+ to the assay or preincubation with Mn2+.	Manganese(2+)	116-120	peptidase D	Homo sapiens	0-9
3139929-1	1988	Prolidase activity in serum from normal subjects and the mother of two patients was readily detected without adding Mn2+ to the assay, and the activity was increased by addition of Mn2+ to the assay or preincubation with Mn2+.	Manganese(2+)	181-185	peptidase D	Homo sapiens	0-9
3139929-1	1988	Prolidase activity in serum from normal subjects and the mother of two patients was readily detected without adding Mn2+ to the assay, and the activity was increased by addition of Mn2+ to the assay or preincubation with Mn2+.	Manganese(2+)	181-185	peptidase D	Homo sapiens	0-9
3139929-3	1988	Both normal and the patients" mother"s prolidase activity against gly-pro was reduced about 20% at 60 degrees C compared to the activity at 37 degrees C, but the addition of Mn2+ at 55 degrees C increased the activity about 1.8-fold, whereas prolidase activity of patients could not be increased by the addition of Mn2+.	glycylproline	66-73	peptidase D	Homo sapiens	39-48
3139929-3	1988	Both normal and the patients" mother"s prolidase activity against gly-pro was reduced about 20% at 60 degrees C compared to the activity at 37 degrees C, but the addition of Mn2+ at 55 degrees C increased the activity about 1.8-fold, whereas prolidase activity of patients could not be increased by the addition of Mn2+.	glycylproline	66-73	peptidase D	Homo sapiens	242-251
3139929-3	1988	Both normal and the patients" mother"s prolidase activity against gly-pro was reduced about 20% at 60 degrees C compared to the activity at 37 degrees C, but the addition of Mn2+ at 55 degrees C increased the activity about 1.8-fold, whereas prolidase activity of patients could not be increased by the addition of Mn2+.	Manganese(2+)	174-178	peptidase D	Homo sapiens	242-251
3436060-1	1987	The effect of prolonged preincubation for 24 h at 37 degrees C in the presence of 1 mmol/l manganese at pH 7.8 was investigated on the two forms of human erythrocyte prolidase after their separation by DEAE-Sephadex chromatography.	Manganese	91-100	peptidase D	Homo sapiens	166-175
3436060-2	1987	Prolidase I activity, which was eluted in chromatographic fractions of low ionic strength of about 160 mmol/l NaCl, increased after preincubation and this activation was maintained throughout the subsequent steps of chromatofocusing, chromatography on Sephacryl S-200 in tandem with Blue-Sepharose, and Phenyl-Sepharose chromatography.	Sodium Chloride	110-114	peptidase D	Homo sapiens	0-9
3436060-2	1987	Prolidase I activity, which was eluted in chromatographic fractions of low ionic strength of about 160 mmol/l NaCl, increased after preincubation and this activation was maintained throughout the subsequent steps of chromatofocusing, chromatography on Sephacryl S-200 in tandem with Blue-Sepharose, and Phenyl-Sepharose chromatography.	sephacryl S 200	252-267	peptidase D	Homo sapiens	0-9
3436060-2	1987	Prolidase I activity, which was eluted in chromatographic fractions of low ionic strength of about 160 mmol/l NaCl, increased after preincubation and this activation was maintained throughout the subsequent steps of chromatofocusing, chromatography on Sephacryl S-200 in tandem with Blue-Sepharose, and Phenyl-Sepharose chromatography.	Sepharose	288-297	peptidase D	Homo sapiens	0-9
3436060-2	1987	Prolidase I activity, which was eluted in chromatographic fractions of low ionic strength of about 160 mmol/l NaCl, increased after preincubation and this activation was maintained throughout the subsequent steps of chromatofocusing, chromatography on Sephacryl S-200 in tandem with Blue-Sepharose, and Phenyl-Sepharose chromatography.	Sepharose	310-319	peptidase D	Homo sapiens	0-9
3436060-4	1987	When the protein environment was restored, isolated prolidase I was reactivated by preincubation, and as a result, gly-pro procollagen dipeptide became the best substrate.	Dipeptides	135-144	peptidase D	Homo sapiens	52-61
3436060-6	1987	The activity of prolidase II, which was eluted in high ionic strength fractions of about 260 mmol/l NaCl during DEAE-Sephadex chromatography, diminished markedly after preincubation and was very low against the gly-pro substrate.	Sodium Chloride	100-104	peptidase D	Homo sapiens	16-25
3436060-6	1987	The activity of prolidase II, which was eluted in high ionic strength fractions of about 260 mmol/l NaCl during DEAE-Sephadex chromatography, diminished markedly after preincubation and was very low against the gly-pro substrate.	2-diethylaminoethanol	112-116	peptidase D	Homo sapiens	16-25
3436060-6	1987	The activity of prolidase II, which was eluted in high ionic strength fractions of about 260 mmol/l NaCl during DEAE-Sephadex chromatography, diminished markedly after preincubation and was very low against the gly-pro substrate.	sephadex	117-125	peptidase D	Homo sapiens	16-25
3436060-6	1987	The activity of prolidase II, which was eluted in high ionic strength fractions of about 260 mmol/l NaCl during DEAE-Sephadex chromatography, diminished markedly after preincubation and was very low against the gly-pro substrate.	Glycine	211-214	peptidase D	Homo sapiens	16-25
3709569-5	1986	The reduced activities of two manganese-dependent enzymes, prolidase and arginase in erythrocytes in combination with an increased manganese content cannot be explained at the moment and leads to the speculation that manganese is inaccessible for enzyme activation.	Manganese	30-39	peptidase D	Homo sapiens	59-68
4042361-4	1985	Secondly, we studied the action of different cadmium and cobalt concentrations on prolidase activity.	Cadmium	45-52	peptidase D	Homo sapiens	82-91
3964660-1	1986	The in vitro hydrolysis by porcine kidney prolidase of the imidodipeptide L-alanyl-L-proline was monitored by using 1H high-resolution NMR spectroscopy.	alanylproline	74-92	peptidase D	Homo sapiens	42-51
3964660-1	1986	The in vitro hydrolysis by porcine kidney prolidase of the imidodipeptide L-alanyl-L-proline was monitored by using 1H high-resolution NMR spectroscopy.	Hydrogen	116-118	peptidase D	Homo sapiens	42-51
3964660-7	1986	1H NMR time courses of the prolidase-catalyzed hydrolysis of L-alanyl-L-proline showed a faster removal of the trans isomer as the [enzyme]/[substrate] ratio was increased.	Hydrogen	0-2	peptidase D	Homo sapiens	27-36
3964660-7	1986	1H NMR time courses of the prolidase-catalyzed hydrolysis of L-alanyl-L-proline showed a faster removal of the trans isomer as the [enzyme]/[substrate] ratio was increased.	alanylproline	61-79	peptidase D	Homo sapiens	27-36
3964660-9	1986	Numerical integration of the relevant differential equations using the experimentally determined rate constants gave simulated progress curves that enabled selection of one of the proposed schemes as being the most likely; this proposal entailed absolute specificity of prolidase for the trans isomer of L-alanyl-L-proline.	alanylproline	304-322	peptidase D	Homo sapiens	270-279
4084535-1	1985	In an effort to further develop the technique of isomer-specific proteolysis, a number of proline-containing substrates were subjected to hydrolysis in the presence of chymotrypsin, trypsin, or prolidase.	Proline	90-97	peptidase D	Homo sapiens	194-203
4084535-6	1985	There was also no indication that prolidase could cleave the dipeptide Phe-Pro when the active bond itself is in the cis form.	Phe-Pro	71-78	peptidase D	Homo sapiens	34-43
4042361-4	1985	Secondly, we studied the action of different cadmium and cobalt concentrations on prolidase activity.	Cobalt	57-63	peptidase D	Homo sapiens	82-91
6743286-10	1984	At concentrations of the dipeptide that saturated prolidase, hydrolysis of glycyl-L-proline by whole cells was approximately 130 times slower than by lysates.	Dipeptides	25-34	peptidase D	Homo sapiens	50-59
6498227-3	1984	For a fructose concentration of 25 mM, we observed that in the absence of glucose, intracellular total proteins increased 1.5-fold and prolidase specific activity, 1.8-fold.	Fructose	6-14	peptidase D	Homo sapiens	135-144
6498227-5	1984	Addition to cultures of 0.1 mM ascorbate increased total proteins 1.4-fold, and doubled prolidase activity.	Ascorbic Acid	31-40	peptidase D	Homo sapiens	88-97
3939542-1	1985	Two forms of prolidase can be separated for all the human cells and tissues examined by DEAE-cellulose column chromatography or batch methods.	DEAE-Cellulose	88-102	peptidase D	Homo sapiens	13-22
6743286-10	1984	At concentrations of the dipeptide that saturated prolidase, hydrolysis of glycyl-L-proline by whole cells was approximately 130 times slower than by lysates.	glycylproline	75-91	peptidase D	Homo sapiens	50-59
6429439-1	1984	Skin fibroblasts have a single enzyme, Mn2+-activated prolidase, that hydrolyses a range of amino acid-proline dipeptides.	amino acid-proline	92-110	peptidase D	Homo sapiens	54-63
6692525-1	1984	We describe here an easy method of determining prolidase (EC 3.4.13.9) in plasma after preincubation with Mn2+ for 24 h at 37 degrees C to maximize prolidase activity.	Manganese(2+)	106-110	peptidase D	Homo sapiens	47-56
6429439-1	1984	Skin fibroblasts have a single enzyme, Mn2+-activated prolidase, that hydrolyses a range of amino acid-proline dipeptides.	Dipeptides	111-121	peptidase D	Homo sapiens	54-63
6429439-4	1984	Control prolidase was stable to prolonged preincubation with Mn2+, whereas the abnormal prolidase was progressively inactivated.	Manganese(2+)	61-65	peptidase D	Homo sapiens	8-17
6888626-4	1983	It is suggested that decreased activities of prolidase and prolinase may contribute to the iminoacidopathy in uremia, including high contents of serum iminoacid containing peptides.	Imino Acids	91-100	peptidase D	Homo sapiens	45-54
6408304-0	1983	In-vitro responses to ascorbate and manganese in fibroblasts from a patient with prolidase deficiency and iminodipeptiduria: cell growth, prolidase activity and collagen metabolism.	Ascorbic Acid	22-31	peptidase D	Homo sapiens	81-90
6408304-0	1983	In-vitro responses to ascorbate and manganese in fibroblasts from a patient with prolidase deficiency and iminodipeptiduria: cell growth, prolidase activity and collagen metabolism.	Manganese	36-45	peptidase D	Homo sapiens	81-90
6408304-2	1983	Since in vivo, ascorbate and manganese seemed to be responsible for both biochemical and clinical improvement, they were also expected to activate prolidase activity in vitro.	Ascorbic Acid	15-24	peptidase D	Homo sapiens	147-156
6408304-2	1983	Since in vivo, ascorbate and manganese seemed to be responsible for both biochemical and clinical improvement, they were also expected to activate prolidase activity in vitro.	Manganese	29-38	peptidase D	Homo sapiens	147-156
6408304-6	1983	We believe that ascorbate allowed the prolidase-deficient cells to maintain a normal collagen pool by increasing collagen synthesis.	Ascorbic Acid	16-25	peptidase D	Homo sapiens	38-47
6888626-4	1983	It is suggested that decreased activities of prolidase and prolinase may contribute to the iminoacidopathy in uremia, including high contents of serum iminoacid containing peptides.	Peptides	172-180	peptidase D	Homo sapiens	45-54
7139961-0	1982	Optimal conditions for prolidase assay by proline colorimetric determination: application to iminodipeptiduria.	Proline	42-49	peptidase D	Homo sapiens	23-32
7139961-1	1982	Prolidase assay was reinvestigated by determining proline, using Chinard"s method.	Proline	50-57	peptidase D	Homo sapiens	0-9
7139961-4	1982	In addition, the reaction mixture was preincubated with Mn2+ for 24 h in order to triple prolidase activity.	Manganese(2+)	56-60	peptidase D	Homo sapiens	89-98
862347-11	1977	This correlation was not observed with unhydrolysed urine, and it appeared to reside in the diffusible fraction, part of whose proline could be liberated by prolidase digestion.	Proline	127-134	peptidase D	Homo sapiens	157-166
117843-1	1979	TRH and pseudo-hormone (pyro Glu-His-amphetamine) were submitted to the digestion of chymotrypsin and prolidase and independently to the digestion of enzymes of the digestive track: pepsin (stomach), pancreatins (pancreas) and enzymes extracted from the intestinal mucosa (small intestine).	pyro glu-his	24-36	peptidase D	Homo sapiens	102-111
117843-1	1979	TRH and pseudo-hormone (pyro Glu-His-amphetamine) were submitted to the digestion of chymotrypsin and prolidase and independently to the digestion of enzymes of the digestive track: pepsin (stomach), pancreatins (pancreas) and enzymes extracted from the intestinal mucosa (small intestine).	Amphetamine	37-48	peptidase D	Homo sapiens	102-111
44887-3	1979	The natriuretic substance in the 95% acetone-soluble F4 was totally destroyed by incubation with prolidase.	Acetone	37-44	peptidase D	Homo sapiens	97-106
570405-1	1979	The rates of hydrolysis of glycy-L-proline and L-phenylalanyl-L-proline, catalyzed by prolidase, have been measured at several temperatures under conditions where a high ratio of prolidase activity to substrate concentration existed.	glycy-l-proline	27-42	peptidase D	Homo sapiens	86-95
570405-1	1979	The rates of hydrolysis of glycy-L-proline and L-phenylalanyl-L-proline, catalyzed by prolidase, have been measured at several temperatures under conditions where a high ratio of prolidase activity to substrate concentration existed.	glycy-l-proline	27-42	peptidase D	Homo sapiens	179-188
570405-1	1979	The rates of hydrolysis of glycy-L-proline and L-phenylalanyl-L-proline, catalyzed by prolidase, have been measured at several temperatures under conditions where a high ratio of prolidase activity to substrate concentration existed.	Phe-Pro	47-71	peptidase D	Homo sapiens	86-95
570405-1	1979	The rates of hydrolysis of glycy-L-proline and L-phenylalanyl-L-proline, catalyzed by prolidase, have been measured at several temperatures under conditions where a high ratio of prolidase activity to substrate concentration existed.	Phe-Pro	47-71	peptidase D	Homo sapiens	179-188
772363-11	1976	Prolidase appears to have an important role in normal hydrolysis of peptide-bound hydroxyproline.	Hydroxyproline	82-96	peptidase D	Homo sapiens	0-9
244384-1	1977	Purification of the first dipeptidases, glycylleucine dipeptidase (EC 3.4.13.2) and proline dipeptidase (EC 3.4.13.9), from intestine, have shown them to be true dipeptidases, hydrolysing only dipeptides in their laevo form.	Dipeptides	193-203	peptidase D	Homo sapiens	84-103
32734598-11	2021	CONCLUSIONS: Three novel heterozygous missense mutations, including c.12614C>T (p.Pro4205Leu) in APOB, c.160G>C (p.Glu54Gln) in CILP2, and c.1199C>A (p.Ala400Glu) in PEPD were first identified in a patient with the triad of DKA, hypertriglyceridemia and AP.	pro4205leu	82-92	peptidase D	Homo sapiens	166-170
13174568-0	1954	Specificity of prolidase: effect of alterations in the pyrrolidine ring of glycyl-L-proline.	pyrrolidine	55-66	peptidase D	Homo sapiens	15-24
13174568-0	1954	Specificity of prolidase: effect of alterations in the pyrrolidine ring of glycyl-L-proline.	glycylproline	75-91	peptidase D	Homo sapiens	15-24
33045291-1	2021	Prolidase is a metal-dependent peptidase specialized in the cleavage of dipeptides containing proline or hydroxyproline on their C-termini.	Dipeptides	72-82	peptidase D	Homo sapiens	0-9
33045291-1	2021	Prolidase is a metal-dependent peptidase specialized in the cleavage of dipeptides containing proline or hydroxyproline on their C-termini.	Proline	94-101	peptidase D	Homo sapiens	0-9
33045291-1	2021	Prolidase is a metal-dependent peptidase specialized in the cleavage of dipeptides containing proline or hydroxyproline on their C-termini.	Hydroxyproline	105-119	peptidase D	Homo sapiens	0-9
33287453-9	2020	Proline concentration and collagen biosynthesis were increased in HaCaT cells under prolidase treatment.	Proline	0-7	peptidase D	Homo sapiens	84-93
32815823-2	2021	Prolidase is a metalloprotease found in various tissues, which has been associated with the concentrations of proline, a neurotransmitter, in the brain.	Proline	110-117	peptidase D	Homo sapiens	0-9
32515491-0	2020	Repurposing a bacterial prolidase for organophosphorus hydrolysis: reshaped catalytic cavity switches substrate selectivity.	organophosphorus	38-54	peptidase D	Homo sapiens	24-33
32918543-4	2020	In order to targeting proline for PRODH/POX-dependent pathways substrate for prolidase, glycyl-proline (GP) was provided and proline utilization for collagen biosynthesis was blocked using 2-methoxyestradiol (MOE).	Proline	22-29	peptidase D	Homo sapiens	77-86
32918543-4	2020	In order to targeting proline for PRODH/POX-dependent pathways substrate for prolidase, glycyl-proline (GP) was provided and proline utilization for collagen biosynthesis was blocked using 2-methoxyestradiol (MOE).	glycylproline	88-102	peptidase D	Homo sapiens	77-86
32918543-4	2020	In order to targeting proline for PRODH/POX-dependent pathways substrate for prolidase, glycyl-proline (GP) was provided and proline utilization for collagen biosynthesis was blocked using 2-methoxyestradiol (MOE).	glycylproline	104-106	peptidase D	Homo sapiens	77-86
32918543-4	2020	In order to targeting proline for PRODH/POX-dependent pathways substrate for prolidase, glycyl-proline (GP) was provided and proline utilization for collagen biosynthesis was blocked using 2-methoxyestradiol (MOE).	Proline	95-102	peptidase D	Homo sapiens	77-86
32918543-4	2020	In order to targeting proline for PRODH/POX-dependent pathways substrate for prolidase, glycyl-proline (GP) was provided and proline utilization for collagen biosynthesis was blocked using 2-methoxyestradiol (MOE).	2-Methoxyestradiol	189-207	peptidase D	Homo sapiens	77-86
32918543-10	2020	RESULTS: Prolidase overexpression in MCF-7PL cells contributed to 10-fold increase in the enzyme activity, 3-fold increase in cytoplasmic proline level and decrease in cell viability and DNA biosynthesis compared to wild type MCF-7 cells.	Proline	138-145	peptidase D	Homo sapiens	9-18
32918543-16	2020	CONCLUSION: The data suggest that overexpression of prolidase in MCF-7 cells contributes to increase in intracellular proline concentration and PRODH/POX-dependent autophagic cell death.	Proline	118-125	peptidase D	Homo sapiens	52-61
32598484-1	2020	Prolidase catalyzes the cleavage of dipeptides containing proline on their C-terminus.	Dipeptides	36-46	peptidase D	Homo sapiens	0-9
32598484-1	2020	Prolidase catalyzes the cleavage of dipeptides containing proline on their C-terminus.	Proline	58-65	peptidase D	Homo sapiens	0-9
32455636-1	2020	Prolidase is a ubiquitous enzyme that plays a major role in the metabolism of proline-rich proteins.	Proline	78-85	peptidase D	Homo sapiens	0-9
32824561-1	2020	Prolidase [EC 3.4.13.9], known as PEPD, cleaves di- and tripeptides containing carboxyl-terminal proline or hydroxyproline.	tripeptides	56-67	peptidase D	Homo sapiens	0-9
32824561-1	2020	Prolidase [EC 3.4.13.9], known as PEPD, cleaves di- and tripeptides containing carboxyl-terminal proline or hydroxyproline.	tripeptides	56-67	peptidase D	Homo sapiens	34-38
32824561-1	2020	Prolidase [EC 3.4.13.9], known as PEPD, cleaves di- and tripeptides containing carboxyl-terminal proline or hydroxyproline.	carboxyl-terminal	79-96	peptidase D	Homo sapiens	0-9
32824561-1	2020	Prolidase [EC 3.4.13.9], known as PEPD, cleaves di- and tripeptides containing carboxyl-terminal proline or hydroxyproline.	carboxyl-terminal	79-96	peptidase D	Homo sapiens	34-38
32824561-1	2020	Prolidase [EC 3.4.13.9], known as PEPD, cleaves di- and tripeptides containing carboxyl-terminal proline or hydroxyproline.	Proline	97-104	peptidase D	Homo sapiens	0-9
32824561-1	2020	Prolidase [EC 3.4.13.9], known as PEPD, cleaves di- and tripeptides containing carboxyl-terminal proline or hydroxyproline.	Proline	97-104	peptidase D	Homo sapiens	34-38
32824561-1	2020	Prolidase [EC 3.4.13.9], known as PEPD, cleaves di- and tripeptides containing carboxyl-terminal proline or hydroxyproline.	Hydroxyproline	108-122	peptidase D	Homo sapiens	0-9
32824561-1	2020	Prolidase [EC 3.4.13.9], known as PEPD, cleaves di- and tripeptides containing carboxyl-terminal proline or hydroxyproline.	Hydroxyproline	108-122	peptidase D	Homo sapiens	34-38
30796241-0	2019	A Novel Role of Prolidase in Cocaine-Mediated Breach in the Barrier of Brain Microvascular Endothelial Cells.	Cocaine	29-36	peptidase D	Homo sapiens	16-25
31933109-9	2020	Proline availability for PRODH/POX-dependent apoptosis/autophagy is regulated at the level of collagen biosynthesis (proline utilizing process) and prolidase activity (proline supporting process).	Proline	0-7	peptidase D	Homo sapiens	148-157
31733276-6	2020	RESULTS: VER decreased cell viability, DNA and collagen biosynthesis and increased prolidase activity in control fibroblast, while in "wounded" fibroblasts it significantly decreased all the processes.	Verapamil	9-12	peptidase D	Homo sapiens	83-92
31733276-11	2020	The VER-dependent inhibition of collagen biosynthesis was accompanied by inhibition of DNA biosynthesis at high prolidase activity, while COLL affected this process through inhibition of prolidase activity at high rate of DNA biosynthesis.	Verapamil	4-7	peptidase D	Homo sapiens	112-121
31733276-11	2020	The VER-dependent inhibition of collagen biosynthesis was accompanied by inhibition of DNA biosynthesis at high prolidase activity, while COLL affected this process through inhibition of prolidase activity at high rate of DNA biosynthesis.	Verapamil	4-7	peptidase D	Homo sapiens	187-196
30796241-2	2019	We show that the cellular enzyme "Prolidase" plays a key role in cocaine-induced disruption of the BBB.	Cocaine	65-72	peptidase D	Homo sapiens	34-43
30796241-13	2019	Knock-down of prolidase reduced cocaine-mediated monocyte transmigration, establishing a key role of prolidase in cocaine-induced breach in endothelial cell barrier.	Cocaine	32-39	peptidase D	Homo sapiens	14-23
30796241-13	2019	Knock-down of prolidase reduced cocaine-mediated monocyte transmigration, establishing a key role of prolidase in cocaine-induced breach in endothelial cell barrier.	Cocaine	114-121	peptidase D	Homo sapiens	14-23
30796241-6	2019	Cocaine exposure also induced prolidase expression and activity in HBMECs.	Cocaine	0-7	peptidase D	Homo sapiens	30-39
30796241-13	2019	Knock-down of prolidase reduced cocaine-mediated monocyte transmigration, establishing a key role of prolidase in cocaine-induced breach in endothelial cell barrier.	Cocaine	114-121	peptidase D	Homo sapiens	101-110
30796241-9	2019	To decipher the mechanism by which cocaine regulates prolidase, we probed the inducible nitric oxide synthase (iNOS) mediated phosphorylation of prolidase since mRNA levels of the protein were not altered upon cocaine treatment.	Cocaine	35-42	peptidase D	Homo sapiens	53-62
30796241-9	2019	To decipher the mechanism by which cocaine regulates prolidase, we probed the inducible nitric oxide synthase (iNOS) mediated phosphorylation of prolidase since mRNA levels of the protein were not altered upon cocaine treatment.	Cocaine	35-42	peptidase D	Homo sapiens	145-154
30066404-1	2018	Prolidase is a metallopeptidase that cleaves iminodipeptides containing a proline (Pro) or hydroxyproline (Hyp) residue at their C-terminal end.	Proline	74-81	peptidase D	Homo sapiens	0-9
30911252-2	2019	Prolidase has an extremely important role in proline recycling for collagen synthesis.	Proline	45-52	peptidase D	Homo sapiens	0-9
30066404-1	2018	Prolidase is a metallopeptidase that cleaves iminodipeptides containing a proline (Pro) or hydroxyproline (Hyp) residue at their C-terminal end.	Hydroxyproline	91-105	peptidase D	Homo sapiens	0-9
29930383-1	2018	Prolidase is cytosolic manganese dependent exopeptidase responsible for the catabolism of imido di and tripeptides.	imido di and tripeptides	90-114	peptidase D	Homo sapiens	0-9
28863383-2	2017	Previous studies suggested that this group of compounds affect prolidase activity (proline releasing enzyme from imidodipeptides) and collagen biosynthesis (proline utilizing process) providing substrate (proline) for proline oxidase (POX) dependent apoptosis.	Proline	83-90	peptidase D	Homo sapiens	63-72
29233996-4	2017	PEPD binds to the proline-rich domain in p53, which inhibits phosphorylation of nuclear p53 and MDM2-mediated mitochondrial translocation of nuclear and cytoplasmic p53.	Proline	18-25	peptidase D	Homo sapiens	0-4
29233996-5	2017	However, the PEPD-p53 complex is critical for p53 response to stress, as stress signals doxorubicin and H2O2 each must free p53 from PEPD in order to achieve robust p53 activation, which is mediated by reactive oxygen species.	Doxorubicin	88-99	peptidase D	Homo sapiens	13-17
29233996-5	2017	However, the PEPD-p53 complex is critical for p53 response to stress, as stress signals doxorubicin and H2O2 each must free p53 from PEPD in order to achieve robust p53 activation, which is mediated by reactive oxygen species.	Doxorubicin	88-99	peptidase D	Homo sapiens	133-137
29233996-5	2017	However, the PEPD-p53 complex is critical for p53 response to stress, as stress signals doxorubicin and H2O2 each must free p53 from PEPD in order to achieve robust p53 activation, which is mediated by reactive oxygen species.	Hydrogen Peroxide	104-108	peptidase D	Homo sapiens	13-17
29233996-5	2017	However, the PEPD-p53 complex is critical for p53 response to stress, as stress signals doxorubicin and H2O2 each must free p53 from PEPD in order to achieve robust p53 activation, which is mediated by reactive oxygen species.	Hydrogen Peroxide	104-108	peptidase D	Homo sapiens	133-137
29233996-5	2017	However, the PEPD-p53 complex is critical for p53 response to stress, as stress signals doxorubicin and H2O2 each must free p53 from PEPD in order to achieve robust p53 activation, which is mediated by reactive oxygen species.	Reactive Oxygen Species	202-225	peptidase D	Homo sapiens	13-17
29233996-5	2017	However, the PEPD-p53 complex is critical for p53 response to stress, as stress signals doxorubicin and H2O2 each must free p53 from PEPD in order to achieve robust p53 activation, which is mediated by reactive oxygen species.	Reactive Oxygen Species	202-225	peptidase D	Homo sapiens	133-137
29681859-6	2018	All studied polyphenols evoked anti-proliferative activity, accompanied by increased PRODH/POX, P53, active caspases-3 and -9 expressions and decreased collagen biosynthesis, prolidase activity and proline concentration in CAL-27 cells.	Polyphenols	12-23	peptidase D	Homo sapiens	175-184
29568391-6	2018	In these cells, glycyl-proline (GlyPro, substrate for prolidase) further inhibited DNA and collagen biosynthesis, maintained high prolidase activity, intracellular concentration of proline and up-regulated HIF-1alpha, AMPK, Atg7 and Beclin-1, compared to GlyPro-treated MCF-7 cells.	glycylproline	16-30	peptidase D	Homo sapiens	54-63
29568391-6	2018	In these cells, glycyl-proline (GlyPro, substrate for prolidase) further inhibited DNA and collagen biosynthesis, maintained high prolidase activity, intracellular concentration of proline and up-regulated HIF-1alpha, AMPK, Atg7 and Beclin-1, compared to GlyPro-treated MCF-7 cells.	glycylproline	16-30	peptidase D	Homo sapiens	130-139
29568391-6	2018	In these cells, glycyl-proline (GlyPro, substrate for prolidase) further inhibited DNA and collagen biosynthesis, maintained high prolidase activity, intracellular concentration of proline and up-regulated HIF-1alpha, AMPK, Atg7 and Beclin-1, compared to GlyPro-treated MCF-7 cells.	Proline	23-30	peptidase D	Homo sapiens	54-63
29568391-6	2018	In these cells, glycyl-proline (GlyPro, substrate for prolidase) further inhibited DNA and collagen biosynthesis, maintained high prolidase activity, intracellular concentration of proline and up-regulated HIF-1alpha, AMPK, Atg7 and Beclin-1, compared to GlyPro-treated MCF-7 cells.	Proline	23-30	peptidase D	Homo sapiens	130-139
29568391-6	2018	In these cells, glycyl-proline (GlyPro, substrate for prolidase) further inhibited DNA and collagen biosynthesis, maintained high prolidase activity, intracellular concentration of proline and up-regulated HIF-1alpha, AMPK, Atg7 and Beclin-1, compared to GlyPro-treated MCF-7 cells.	glycylproline	32-38	peptidase D	Homo sapiens	54-63
29568391-6	2018	In these cells, glycyl-proline (GlyPro, substrate for prolidase) further inhibited DNA and collagen biosynthesis, maintained high prolidase activity, intracellular concentration of proline and up-regulated HIF-1alpha, AMPK, Atg7 and Beclin-1, compared to GlyPro-treated MCF-7 cells.	glycylproline	32-38	peptidase D	Homo sapiens	130-139
28863383-10	2017	The data suggest that massive production of proline by proBet-dependent activation of prolidase and inhibition of proline utilization for collagen biosynthesis may represent mechanism for POX-dependent apoptosis in EA cells.	Proline	44-51	peptidase D	Homo sapiens	86-95
27320745-5	2017	Serum prolidase activity was positively correlated with the Tonnis grade of DDH and LOOH, TOS, and OSI levels (P < 0.001 for all), but inversely correlated with total -SH and TAC levels (P < 0.001 for all).	Lipid Peroxides	84-88	peptidase D	Homo sapiens	6-15
28867357-10	2017	In the Pearson"s correlation analysis, enzyme activity of prolidase was positively related with TOS (p<0.001, r=0.529) and OSI (p<0.001, r=0.519) as well as BMI (p<0.001, r=0.692) and inversely related with TAC (p<0.05, r=-0.405) in obese subjects.	tos	96-99	peptidase D	Homo sapiens	58-67
28677335-1	2017	Prolidase is a ubiquitously distributed dipeptidase and the only dipeptidase in humans capable of cleaving the peptide bond preceding the amino acids proline (Pro) or hydroxyproline (Hyp).	Proline	150-157	peptidase D	Homo sapiens	0-9
28677335-1	2017	Prolidase is a ubiquitously distributed dipeptidase and the only dipeptidase in humans capable of cleaving the peptide bond preceding the amino acids proline (Pro) or hydroxyproline (Hyp).	Hydroxyproline	167-181	peptidase D	Homo sapiens	0-9
28382686-4	2017	In cells treated with 0.01, 0.03 and 0.05% MP a dose-dependent decrease in collagen biosynthesis was revealed, which was positively correlated with the activity of prolidase responsible for the recovery of proline.	Proline	206-213	peptidase D	Homo sapiens	164-173
27320745-5	2017	Serum prolidase activity was positively correlated with the Tonnis grade of DDH and LOOH, TOS, and OSI levels (P < 0.001 for all), but inversely correlated with total -SH and TAC levels (P < 0.001 for all).	tos	90-93	peptidase D	Homo sapiens	6-15
27320745-5	2017	Serum prolidase activity was positively correlated with the Tonnis grade of DDH and LOOH, TOS, and OSI levels (P < 0.001 for all), but inversely correlated with total -SH and TAC levels (P < 0.001 for all).	silicon monoxide	99-102	peptidase D	Homo sapiens	6-15
27067078-1	2017	The enzyme prolidase cleaves dipeptides where the C-terminal amino acid corresponds to proline or hydroxyproline.	Dipeptides	29-39	peptidase D	Homo sapiens	11-20
28942439-3	2017	We have used inhibitor of proline utilization in collagen biosynthesis, 2-metoxyestradiol (MOE), inhibitor of prolidase that generate proline, rapamycin (Rap) and glycyl-proline (GlyPro), substrate for prolidase.	Proline	26-33	peptidase D	Homo sapiens	202-211
28942439-3	2017	We have used inhibitor of proline utilization in collagen biosynthesis, 2-metoxyestradiol (MOE), inhibitor of prolidase that generate proline, rapamycin (Rap) and glycyl-proline (GlyPro), substrate for prolidase.	2-metoxyestradiol	72-89	peptidase D	Homo sapiens	110-119
28942439-3	2017	We have used inhibitor of proline utilization in collagen biosynthesis, 2-metoxyestradiol (MOE), inhibitor of prolidase that generate proline, rapamycin (Rap) and glycyl-proline (GlyPro), substrate for prolidase.	2-metoxyestradiol	72-89	peptidase D	Homo sapiens	202-211
28942439-3	2017	We have used inhibitor of proline utilization in collagen biosynthesis, 2-metoxyestradiol (MOE), inhibitor of prolidase that generate proline, rapamycin (Rap) and glycyl-proline (GlyPro), substrate for prolidase.	Proline	134-141	peptidase D	Homo sapiens	110-119
28942439-3	2017	We have used inhibitor of proline utilization in collagen biosynthesis, 2-metoxyestradiol (MOE), inhibitor of prolidase that generate proline, rapamycin (Rap) and glycyl-proline (GlyPro), substrate for prolidase.	glycylproline	163-177	peptidase D	Homo sapiens	110-119
27067078-1	2017	The enzyme prolidase cleaves dipeptides where the C-terminal amino acid corresponds to proline or hydroxyproline.	Proline	87-94	peptidase D	Homo sapiens	11-20
27067078-1	2017	The enzyme prolidase cleaves dipeptides where the C-terminal amino acid corresponds to proline or hydroxyproline.	Hydroxyproline	98-112	peptidase D	Homo sapiens	11-20
28462712-1	2017	BACKGROUND: Human prolidase has weak hydrolytic activity for toxic organophosphorus compounds including diisopropyl fluorophosphates (DFP), chemical warfare nerve agents and pesticides.	organophosphorus	67-83	peptidase D	Homo sapiens	18-27
28462712-1	2017	BACKGROUND: Human prolidase has weak hydrolytic activity for toxic organophosphorus compounds including diisopropyl fluorophosphates (DFP), chemical warfare nerve agents and pesticides.	Isoflurophate	104-132	peptidase D	Homo sapiens	18-27
28462712-2	2017	OBJECTIVES: In order to use human prolidase as a catalytic bioscavenger against toxic organophosphorus compound exposure, protein engineering is an important issue to improve the catalytic activity of human prolidase towards the hydrolysis of toxic organophosphorus compounds.	organophosphorus	86-102	peptidase D	Homo sapiens	34-43
28462712-2	2017	OBJECTIVES: In order to use human prolidase as a catalytic bioscavenger against toxic organophosphorus compound exposure, protein engineering is an important issue to improve the catalytic activity of human prolidase towards the hydrolysis of toxic organophosphorus compounds.	organophosphorus	86-102	peptidase D	Homo sapiens	207-216
28462712-4	2017	RESULTS: Our results showed that the catalytic efficiencies of A252R and P365R towards DFP hydrolysis were 1.23- and 1.36-fold increases, respectively, than that of the wild type, while the prolidase activities of A252R and P365R towards Leu-Pro hydrolysis were 0.88- and 0.78-fold decreases that of the wild type, respectively, indicating that substitution mutations of A252R and P365R in human prolidase show improved hydrolytic activity for toxic organophosphorus compounds.	Leucine	238-241	peptidase D	Homo sapiens	190-199
28462712-4	2017	RESULTS: Our results showed that the catalytic efficiencies of A252R and P365R towards DFP hydrolysis were 1.23- and 1.36-fold increases, respectively, than that of the wild type, while the prolidase activities of A252R and P365R towards Leu-Pro hydrolysis were 0.88- and 0.78-fold decreases that of the wild type, respectively, indicating that substitution mutations of A252R and P365R in human prolidase show improved hydrolytic activity for toxic organophosphorus compounds.	organophosphorus	450-466	peptidase D	Homo sapiens	190-199
25943419-0	2016	High proline-related inhibition of serum prolidase enzyme activity in scleroderma.	Proline	5-12	peptidase D	Homo sapiens	41-50
27482243-2	2016	The prolidase enzyme is a cytosolic exopeptidase that detaches proline or hydroxyproline from the carboxyl terminal position of dipeptides.	Proline	63-70	peptidase D	Homo sapiens	4-13
27482243-2	2016	The prolidase enzyme is a cytosolic exopeptidase that detaches proline or hydroxyproline from the carboxyl terminal position of dipeptides.	Hydroxyproline	74-88	peptidase D	Homo sapiens	4-13
27482243-2	2016	The prolidase enzyme is a cytosolic exopeptidase that detaches proline or hydroxyproline from the carboxyl terminal position of dipeptides.	Dipeptides	128-138	peptidase D	Homo sapiens	4-13
27000973-3	2016	Prolidase plays an important role in collagen metabolism by degrading imidodipeptides, in which proline or hydroxyproline residue is located at the C-terminal end.	Proline	96-103	peptidase D	Homo sapiens	0-9
27000973-3	2016	Prolidase plays an important role in collagen metabolism by degrading imidodipeptides, in which proline or hydroxyproline residue is located at the C-terminal end.	Hydroxyproline	107-121	peptidase D	Homo sapiens	0-9
26575119-7	2016	Prolidase activity were positively correlated with TOS, OSI, LOOH and negatively correlated with -SH in patients with acromegaly (r=0.471, p<0.001; r=0.527, p<0.001; r=0.717, p<0.001; r=- 0.516, p<0.001, respectively).	tos	51-54	peptidase D	Homo sapiens	0-9
26575119-7	2016	Prolidase activity were positively correlated with TOS, OSI, LOOH and negatively correlated with -SH in patients with acromegaly (r=0.471, p<0.001; r=0.527, p<0.001; r=0.717, p<0.001; r=- 0.516, p<0.001, respectively).	silicon monoxide	56-59	peptidase D	Homo sapiens	0-9
26575119-7	2016	Prolidase activity were positively correlated with TOS, OSI, LOOH and negatively correlated with -SH in patients with acromegaly (r=0.471, p<0.001; r=0.527, p<0.001; r=0.717, p<0.001; r=- 0.516, p<0.001, respectively).	Lipid Peroxides	61-65	peptidase D	Homo sapiens	0-9
27040799-1	2016	Prolidase is a cytosolic imidodipeptidase that specifically splits imidodipeptides with C-terminal proline or hydroxyproline.	Proline	99-106	peptidase D	Homo sapiens	0-9
27040799-1	2016	Prolidase is a cytosolic imidodipeptidase that specifically splits imidodipeptides with C-terminal proline or hydroxyproline.	Proline	99-106	peptidase D	Homo sapiens	25-41
27040799-1	2016	Prolidase is a cytosolic imidodipeptidase that specifically splits imidodipeptides with C-terminal proline or hydroxyproline.	Hydroxyproline	110-124	peptidase D	Homo sapiens	0-9
27040799-1	2016	Prolidase is a cytosolic imidodipeptidase that specifically splits imidodipeptides with C-terminal proline or hydroxyproline.	Hydroxyproline	110-124	peptidase D	Homo sapiens	25-41
27040799-14	2016	Proline availability for PRODH/POX-dependent ATP or ROS generation depends on activity of prolidase and utilization of proline in process of collagen biosynthesis.	Proline	0-7	peptidase D	Homo sapiens	90-99
27040799-14	2016	Proline availability for PRODH/POX-dependent ATP or ROS generation depends on activity of prolidase and utilization of proline in process of collagen biosynthesis.	Adenosine Triphosphate	45-48	peptidase D	Homo sapiens	90-99
27040799-14	2016	Proline availability for PRODH/POX-dependent ATP or ROS generation depends on activity of prolidase and utilization of proline in process of collagen biosynthesis.	Reactive Oxygen Species	52-55	peptidase D	Homo sapiens	90-99
26364956-0	2016	Prolidase-Associated Trace Elements (Mn, Zn, Co, and Ni) in the Patients with Parkinson"s Disease.	Zinc	41-43	peptidase D	Homo sapiens	0-9
26364956-0	2016	Prolidase-Associated Trace Elements (Mn, Zn, Co, and Ni) in the Patients with Parkinson"s Disease.	Cobalt	45-47	peptidase D	Homo sapiens	0-9
26364956-3	2016	In present study, we aimed to study the association of prolidase-associated trace elements, such as Co, Mn, Ni, and Zn in the plasma of patients with PD by inductively coupled plasma spectrometry.	Cobalt	100-102	peptidase D	Homo sapiens	55-64
26364956-3	2016	In present study, we aimed to study the association of prolidase-associated trace elements, such as Co, Mn, Ni, and Zn in the plasma of patients with PD by inductively coupled plasma spectrometry.	Zinc	116-118	peptidase D	Homo sapiens	55-64
27546702-1	2016	Prolidase (EC.3.4.13.9) or proline dipeptidase, is one of the unique enzyme capable of degrading dipeptides, in which a proline or hydroxyproline residue is located at the C-terminal position.	Dipeptides	97-107	peptidase D	Homo sapiens	0-9
27546702-1	2016	Prolidase (EC.3.4.13.9) or proline dipeptidase, is one of the unique enzyme capable of degrading dipeptides, in which a proline or hydroxyproline residue is located at the C-terminal position.	Dipeptides	97-107	peptidase D	Homo sapiens	27-46
27546702-1	2016	Prolidase (EC.3.4.13.9) or proline dipeptidase, is one of the unique enzyme capable of degrading dipeptides, in which a proline or hydroxyproline residue is located at the C-terminal position.	Proline	27-34	peptidase D	Homo sapiens	0-9
27546702-1	2016	Prolidase (EC.3.4.13.9) or proline dipeptidase, is one of the unique enzyme capable of degrading dipeptides, in which a proline or hydroxyproline residue is located at the C-terminal position.	Hydroxyproline	131-145	peptidase D	Homo sapiens	0-9
27546702-1	2016	Prolidase (EC.3.4.13.9) or proline dipeptidase, is one of the unique enzyme capable of degrading dipeptides, in which a proline or hydroxyproline residue is located at the C-terminal position.	Hydroxyproline	131-145	peptidase D	Homo sapiens	27-46
26648698-5	2015	RESULTS: Ethanol in a dose-dependent manner lead to the impairment of collagen biosynthesis in fibroblast cultures through decreasing prolidase activity and expression of beta1 integrin and IGF-IR.	Ethanol	9-16	peptidase D	Homo sapiens	134-143
25982243-0	2016	Prolidase-dependent mechanism of (Z)-8,9-epoxyheptadeca-1,11,14-triene-induced inhibition of collagen biosynthesis in cultured human skin fibroblasts.	1,11,14-triene	56-70	peptidase D	Homo sapiens	0-9
25982243-5	2016	EHT-dependent inhibition of collagen biosynthesis results from inhibition of prolidase activity, the enzyme involved in collagen biosynthesis.	7-ethoxy-4-(3,4,5-trimethoxybenzyl)isoquinolin-8-amine	0-3	peptidase D	Homo sapiens	77-86
26198764-11	2015	Among the novel potential susceptibility genes is PEPD, a gene involved in proline metabolism, which is associated with a Mendelian disorder characterized by developmental delay and cognitive deficits.	Proline	75-82	peptidase D	Homo sapiens	50-54
25691319-2	2015	Deficiency of prolidase leads to the increased excretion of proline in urine, which causes impaired collagen synthesis and delay in wound healing.	Proline	60-67	peptidase D	Homo sapiens	14-23
25900177-9	2015	Prolidase levels were positively correlated with TOS and OSI and negatively correlated with -SH (r = 0.565, p = 0.003; r = 0.604, p = 0.001; r = -0.532, p = 0.006).	tos	49-52	peptidase D	Homo sapiens	0-9
25551736-9	2015	In BPH patients, the prolidase activity was significantly associated with TAC levels (r = -0.366, P < 0.05), TOS levels (r = 0.573, P < 0.001), and OSI (r = 0.618, P < 0.001) and peripheral mononuclear leukocyte DNA damage (r = 0.461, P < 0.001).	tos	112-115	peptidase D	Homo sapiens	21-30
25772062-0	2015	Enalapril stimulates collagen biosynthesis through prolidase-dependent mechanism in cultured fibroblasts.	Enalapril	0-9	peptidase D	Homo sapiens	51-60
25772062-3	2015	Since insulin-like growth factor (IGF-I) and transforming growth factor beta 1 (TGF-beta1) are the most potent stimulators of both collagen biosynthesis and prolidase activity, and prolidase is regulated by beta1 integrin signaling, the effect of enalapril and enalaprilat on IGF-IR, TGF-beta1, and beta1 integrin receptor expressions was evaluated.	Enalapril	247-256	peptidase D	Homo sapiens	181-190
25460580-3	2015	In humans, prolidase is the only enzyme able to hydrolyze dipeptides containing these amino acids at their C-terminal end, thus being a key player in collagen synthesis and turnover.	Dipeptides	58-68	peptidase D	Homo sapiens	11-20
25772062-4	2015	Cells were treated with milimolar concentrations (0.3 and 0.5 mM) of enalapril and enalaprilat for 24 h. The activity of prolidase was determined by colorimetic assay.	Enalapril	69-78	peptidase D	Homo sapiens	121-130
25772062-7	2015	It was found that enalapril- and enalaprilat-dependent increase in prolidase activity and expression was accompanied by parallel increase in collagen biosynthesis.	Enalapril	18-27	peptidase D	Homo sapiens	67-76
25772062-9	2015	Enalapril- and enalaprilat-dependent increase of collagen biosynthesis in fibroblasts results from increase of prolidase activity and expression, which may undergo through activation of alpha2beta1 integrin and IGF-IR signaling as well as upregulation of TGF-beta1 and NF-kappaB p65, the inhibitor of collagen gene expression.	Enalapril	0-9	peptidase D	Homo sapiens	111-120
25772062-9	2015	Enalapril- and enalaprilat-dependent increase of collagen biosynthesis in fibroblasts results from increase of prolidase activity and expression, which may undergo through activation of alpha2beta1 integrin and IGF-IR signaling as well as upregulation of TGF-beta1 and NF-kappaB p65, the inhibitor of collagen gene expression.	Enalaprilat	15-26	peptidase D	Homo sapiens	111-120
25626895-4	2015	Since phosphoenolpyruvate (PEP) is known as an inhibitor of prolidase-the enzyme that plays important role in collagen biosynthesis, the mechanism of pyruvate interconversion was considered as a regulatory switch in collagen biosynthesis.	Phosphoenolpyruvate	6-25	peptidase D	Homo sapiens	60-69
25626895-4	2015	Since phosphoenolpyruvate (PEP) is known as an inhibitor of prolidase-the enzyme that plays important role in collagen biosynthesis, the mechanism of pyruvate interconversion was considered as a regulatory switch in collagen biosynthesis.	Pyruvic Acid	17-25	peptidase D	Homo sapiens	60-69
25626895-5	2015	In fact, 3-MPA, specific inhibitor of phosphoenolpyruvate carboxykinase (PEPCK), contributed to up-regulation of prolidase activity, suggesting that down-regulation of PEP formation is an underlying mechanism.	3-Mercaptopropionic Acid	9-14	peptidase D	Homo sapiens	113-122
24412428-2	2014	Firstly, PAMAM combined with PtNPs was used as platform to assemble substantial Ru, prolidase (GPDA) and avidin labeled thrombin aptamer (avidin-TBA) to form PAMAM-PtNPs-Ru-GDPA-TBA bioconjugate.	Poly(amidoamine)	9-14	peptidase D	Homo sapiens	84-93
25540672-6	2014	Prolidase was negatively correlated with TAS and HDL-C (r = -0,362, p < 0.001; r = -0.320, p < 0.01, respectively) and positively correlated with BMI, weight, waist-c, SBP, DBP, TG, TC, LDL-C.	Triglycerides	184-186	peptidase D	Homo sapiens	0-9
25540672-6	2014	Prolidase was negatively correlated with TAS and HDL-C (r = -0,362, p < 0.001; r = -0.320, p < 0.01, respectively) and positively correlated with BMI, weight, waist-c, SBP, DBP, TG, TC, LDL-C.	Technetium	188-190	peptidase D	Homo sapiens	0-9
25540672-6	2014	Prolidase was negatively correlated with TAS and HDL-C (r = -0,362, p < 0.001; r = -0.320, p < 0.01, respectively) and positively correlated with BMI, weight, waist-c, SBP, DBP, TG, TC, LDL-C.	ldl-c	192-197	peptidase D	Homo sapiens	0-9
26087900-0	2015	Modulation of the Association between the PEPD Variant and the Risk of Type 2 Diabetes by n-3 Fatty Acids in Chinese Hans.	Fatty Acids, Omega-3	90-105	peptidase D	Homo sapiens	42-46
26087900-7	2015	RESULTS: Among the 9 SNPs, only rs3786897 at PEPD (peptidase D) showed a significant interaction with n-3 fatty acids (p(interaction) after Bonferroni correction = 0.027).	Fatty Acids, Omega-3	102-117	peptidase D	Homo sapiens	45-49
26087900-7	2015	RESULTS: Among the 9 SNPs, only rs3786897 at PEPD (peptidase D) showed a significant interaction with n-3 fatty acids (p(interaction) after Bonferroni correction = 0.027).	Fatty Acids, Omega-3	102-117	peptidase D	Homo sapiens	51-62
26087900-9	2015	CONCLUSIONS: The association between the PEPD genetic variant and the risk of T2D was modulated by n-3 fatty acids.	Fatty Acids, Omega-3	99-114	peptidase D	Homo sapiens	41-45
26087900-10	2015	Higher n-3 fatty acids may abolish the adverse effect of the risk allele at PEPD for T2D.	Fatty Acids, Omega-3	7-22	peptidase D	Homo sapiens	76-80
25377365-9	2014	CONCLUSION: Increased serum prolidase levels in patients with MDD may be interpreted as the interaction of prolidase activity, glutamate transmission and oxidative stress.	Glutamic Acid	127-136	peptidase D	Homo sapiens	28-37
24620938-7	2014	Serum prolidase activity was positively correlated with serum TOS, OSI, and visual analog scale pain and fatigue scores.	tos	62-65	peptidase D	Homo sapiens	6-15
24412428-2	2014	Firstly, PAMAM combined with PtNPs was used as platform to assemble substantial Ru, prolidase (GPDA) and avidin labeled thrombin aptamer (avidin-TBA) to form PAMAM-PtNPs-Ru-GDPA-TBA bioconjugate.	Poly(amidoamine)	158-163	peptidase D	Homo sapiens	84-93
24412428-4	2014	The proposed aptasensor possessed three attractive advantages: PAMAM, as a tertiary amine substance, not only served as a platform to immobilize the PtNPs for further assembling prolidase (GPDA) and avidin-TBA, but also used as a coreactant of Ru to amplify the ECL signal.	Poly(amidoamine)	63-68	peptidase D	Homo sapiens	178-187
24566305-5	2014	The hydrolysis of imidazole-related dipeptides in prokaryotes and eukaryotes is also catalyzed by aminoacyl-histidine dipeptidases like PepD (EC 3.4.13.3), PepV (EC 3.4.13.19) and anserinase (EC 3.4.13.5).	imidazole	18-27	peptidase D	Homo sapiens	136-140
24566305-5	2014	The hydrolysis of imidazole-related dipeptides in prokaryotes and eukaryotes is also catalyzed by aminoacyl-histidine dipeptidases like PepD (EC 3.4.13.3), PepV (EC 3.4.13.19) and anserinase (EC 3.4.13.5).	Dipeptides	36-46	peptidase D	Homo sapiens	136-140
24566305-5	2014	The hydrolysis of imidazole-related dipeptides in prokaryotes and eukaryotes is also catalyzed by aminoacyl-histidine dipeptidases like PepD (EC 3.4.13.3), PepV (EC 3.4.13.19) and anserinase (EC 3.4.13.5).	anserinase	180-190	peptidase D	Homo sapiens	136-140
23549681-4	2013	However, in MDA-MB-231 cells (expressing high prolidase activity) cultured in the presence of prolidase substrates, Gly-Pro or Gly-HyPro, HIF-1alpha expression was induced in a dose-dependent manner, independently of estrogen receptor activation.	glycylproline	116-123	peptidase D	Homo sapiens	46-55
25276429-0	2014	Serum prolidase activity and oxidative stress in diabetic nephropathy and end stage renal disease: a correlative study with glucose and creatinine.	Glucose	124-131	peptidase D	Homo sapiens	6-15
25276429-0	2014	Serum prolidase activity and oxidative stress in diabetic nephropathy and end stage renal disease: a correlative study with glucose and creatinine.	Creatinine	136-146	peptidase D	Homo sapiens	6-15
23479033-2	2013	Prolidase is known to have a crucial part in the recycling of proline for collagen synthesis.	Proline	62-69	peptidase D	Homo sapiens	0-9
23553128-5	2013	Serum prolidase assay is based on a colorimetric determination of proline by Chinard"s reagent.	Proline	66-73	peptidase D	Homo sapiens	6-15
23549681-4	2013	However, in MDA-MB-231 cells (expressing high prolidase activity) cultured in the presence of prolidase substrates, Gly-Pro or Gly-HyPro, HIF-1alpha expression was induced in a dose-dependent manner, independently of estrogen receptor activation.	Glycine	116-119	peptidase D	Homo sapiens	46-55
23549681-4	2013	However, in MDA-MB-231 cells (expressing high prolidase activity) cultured in the presence of prolidase substrates, Gly-Pro or Gly-HyPro, HIF-1alpha expression was induced in a dose-dependent manner, independently of estrogen receptor activation.	Glycine	116-119	peptidase D	Homo sapiens	94-103
23868621-10	2013	Prolidase activity was correlated with increased LOOH and decreased CAT levels (r = 0.507 p = 0.004; r = - 0.579, p = 0.001, respectively).	Lipid Peroxides	49-53	peptidase D	Homo sapiens	0-9
22677456-0	2013	In vitro characterization of organophosphorus compound hydrolysis by native and recombinant human prolidase.	organophosphorus	29-45	peptidase D	Homo sapiens	98-107
23287645-3	2013	This mutation results in addition of an extra alanine residue at the amino-acid position number 304 of prolidase peptide.	Alanine	46-53	peptidase D	Homo sapiens	103-112
22677456-1	2013	Human prolidase is a binuclear metalloenzyme, which can potentially function as a catalytic bioscavenger for organophosphorus (OP) nerve agents.	organophosphorus	109-125	peptidase D	Homo sapiens	6-15
22677456-5	2013	In this study, we established an Escherichia coli expression system, which produced a large amount of tagged human liver prolidase that was purified to over 95% purity from the soluble fraction of cell lysate by affinity chromatography on Streptavidin-agarose resin.	Sepharose	252-259	peptidase D	Homo sapiens	121-130
23212918-1	2013	Prolidase, also known as Xaa-Pro dipeptidase or peptidase D (PEPD), is a ubiquitously expressed cytosolic enzyme that hydrolyzes dipeptides with proline or hydroxyproline at the carboxyl terminus.	Dipeptides	129-139	peptidase D	Homo sapiens	0-9
23212918-1	2013	Prolidase, also known as Xaa-Pro dipeptidase or peptidase D (PEPD), is a ubiquitously expressed cytosolic enzyme that hydrolyzes dipeptides with proline or hydroxyproline at the carboxyl terminus.	Dipeptides	129-139	peptidase D	Homo sapiens	25-44
23212918-1	2013	Prolidase, also known as Xaa-Pro dipeptidase or peptidase D (PEPD), is a ubiquitously expressed cytosolic enzyme that hydrolyzes dipeptides with proline or hydroxyproline at the carboxyl terminus.	Dipeptides	129-139	peptidase D	Homo sapiens	48-59
23212918-1	2013	Prolidase, also known as Xaa-Pro dipeptidase or peptidase D (PEPD), is a ubiquitously expressed cytosolic enzyme that hydrolyzes dipeptides with proline or hydroxyproline at the carboxyl terminus.	Dipeptides	129-139	peptidase D	Homo sapiens	61-65
23212918-1	2013	Prolidase, also known as Xaa-Pro dipeptidase or peptidase D (PEPD), is a ubiquitously expressed cytosolic enzyme that hydrolyzes dipeptides with proline or hydroxyproline at the carboxyl terminus.	Proline	145-152	peptidase D	Homo sapiens	0-9
23212918-1	2013	Prolidase, also known as Xaa-Pro dipeptidase or peptidase D (PEPD), is a ubiquitously expressed cytosolic enzyme that hydrolyzes dipeptides with proline or hydroxyproline at the carboxyl terminus.	Proline	145-152	peptidase D	Homo sapiens	25-44
23212918-1	2013	Prolidase, also known as Xaa-Pro dipeptidase or peptidase D (PEPD), is a ubiquitously expressed cytosolic enzyme that hydrolyzes dipeptides with proline or hydroxyproline at the carboxyl terminus.	Proline	145-152	peptidase D	Homo sapiens	48-59
23212918-1	2013	Prolidase, also known as Xaa-Pro dipeptidase or peptidase D (PEPD), is a ubiquitously expressed cytosolic enzyme that hydrolyzes dipeptides with proline or hydroxyproline at the carboxyl terminus.	Proline	145-152	peptidase D	Homo sapiens	61-65
23212918-1	2013	Prolidase, also known as Xaa-Pro dipeptidase or peptidase D (PEPD), is a ubiquitously expressed cytosolic enzyme that hydrolyzes dipeptides with proline or hydroxyproline at the carboxyl terminus.	Hydroxyproline	156-170	peptidase D	Homo sapiens	0-9
23212918-1	2013	Prolidase, also known as Xaa-Pro dipeptidase or peptidase D (PEPD), is a ubiquitously expressed cytosolic enzyme that hydrolyzes dipeptides with proline or hydroxyproline at the carboxyl terminus.	Hydroxyproline	156-170	peptidase D	Homo sapiens	25-44
23212918-1	2013	Prolidase, also known as Xaa-Pro dipeptidase or peptidase D (PEPD), is a ubiquitously expressed cytosolic enzyme that hydrolyzes dipeptides with proline or hydroxyproline at the carboxyl terminus.	Hydroxyproline	156-170	peptidase D	Homo sapiens	48-59
23212918-1	2013	Prolidase, also known as Xaa-Pro dipeptidase or peptidase D (PEPD), is a ubiquitously expressed cytosolic enzyme that hydrolyzes dipeptides with proline or hydroxyproline at the carboxyl terminus.	Hydroxyproline	156-170	peptidase D	Homo sapiens	61-65
23516557-1	2013	Prolidase is the only human enzyme responsible for the digestion of iminodipeptides containing proline or hydroxyproline at their C-terminal end, being a key player in extracellular matrix remodeling.	Proline	95-102	peptidase D	Homo sapiens	0-9
22999980-0	2013	A Mn(II)-Mn(II) center in human prolidase.	Manganese(2+)	2-8	peptidase D	Homo sapiens	32-41
22999980-0	2013	A Mn(II)-Mn(II) center in human prolidase.	Manganese(2+)	9-15	peptidase D	Homo sapiens	32-41
22999980-1	2013	Human prolidase, the enzyme responsible for the hydrolysis of the Xaa-Pro/Hyp peptide bonds, is a key player in the recycling of imino acids during the final stage of protein catabolism and extracellular matrix remodeling.	Imino Acids	129-140	peptidase D	Homo sapiens	6-15
22999980-3	2013	Here, using EPR and ICP-MS on human recombinant prolidase produced in Escherichia coli (hRecProl), the Mn(II) ion organized in a dinuclear Mn(II)-Mn(II) center was identified as the protein cofactor.	Manganese(2+)	103-109	peptidase D	Homo sapiens	48-57
22999980-5	2013	The collected data provided a better knowledge of the human holo-prolidase and, although limited to the recombinant enzyme, the exact identity and organization of the metal cofactor as well as the conformational change required for activity were proven.	Metals	167-172	peptidase D	Homo sapiens	65-74
23581407-5	2013	It was found that in the presence of estradiol, prolactin inhibits prolidase activity and its down-stream signaling proteins: HIF-1alpha, mTOR, AKT and MAPK p-38, while in the absence of estradiol, an opposite effect was observed.	Estradiol	37-46	peptidase D	Homo sapiens	67-76
23516557-1	2013	Prolidase is the only human enzyme responsible for the digestion of iminodipeptides containing proline or hydroxyproline at their C-terminal end, being a key player in extracellular matrix remodeling.	Hydroxyproline	106-120	peptidase D	Homo sapiens	0-9
23457135-5	2012	RESULTS: It was found that the plasma activity of prolidase (Pro) was reduced to almost half together with the serum level of osteocalcin (BGL), and hydroxyproline (H-PRO) in the serum and urine of patients with MPN in comparison to the control group.	Hydroxyproline	149-163	peptidase D	Homo sapiens	50-59
23457135-5	2012	RESULTS: It was found that the plasma activity of prolidase (Pro) was reduced to almost half together with the serum level of osteocalcin (BGL), and hydroxyproline (H-PRO) in the serum and urine of patients with MPN in comparison to the control group.	Hydroxyproline	149-163	peptidase D	Homo sapiens	61-64
22512465-0	2012	Prolidase function in proline metabolism and its medical and biotechnological applications.	Proline	22-29	peptidase D	Homo sapiens	0-9
22512465-1	2012	Prolidase is a multifunctional enzyme that possesses the unique ability to degrade imidodipeptides in which a proline or hydroxyproline residue is located at the C-terminal end.	Proline	110-117	peptidase D	Homo sapiens	0-9
22512465-1	2012	Prolidase is a multifunctional enzyme that possesses the unique ability to degrade imidodipeptides in which a proline or hydroxyproline residue is located at the C-terminal end.	Hydroxyproline	121-135	peptidase D	Homo sapiens	0-9
22245250-0	2012	The retinoic acid-induced up-regulation of insulin-like growth factor 1 and 2 is associated with prolidase-dependent collagen synthesis in UVA-irradiated human dermal equivalents.	Tretinoin	4-17	peptidase D	Homo sapiens	97-106
22245250-6	2012	RESULTS: In addition to the expected changes in MMPs and collagen synthesis in HDEs in response to ATRA, prolidase, an important enzyme in the recycling of proline and hydroxyproline from degraded collagen molecules, was significantly decreased by UVA irradiation, and its down-regulation was antagonized by ATRA.	Proline	156-163	peptidase D	Homo sapiens	105-114
22245250-6	2012	RESULTS: In addition to the expected changes in MMPs and collagen synthesis in HDEs in response to ATRA, prolidase, an important enzyme in the recycling of proline and hydroxyproline from degraded collagen molecules, was significantly decreased by UVA irradiation, and its down-regulation was antagonized by ATRA.	Hydroxyproline	168-182	peptidase D	Homo sapiens	105-114
22245250-6	2012	RESULTS: In addition to the expected changes in MMPs and collagen synthesis in HDEs in response to ATRA, prolidase, an important enzyme in the recycling of proline and hydroxyproline from degraded collagen molecules, was significantly decreased by UVA irradiation, and its down-regulation was antagonized by ATRA.	Tretinoin	99-103	peptidase D	Homo sapiens	105-114
22245250-8	2012	ATRA inhibited the UVA irradiation-induced decrease in prolidase activity through an insulin-like growth factor (IGF) receptor signaling pathway in HDEs.	Tretinoin	0-4	peptidase D	Homo sapiens	55-64
22245250-10	2012	CONCLUSIONS: These data demonstrate that ATRA regulates prolidase activity in HDEs via IGF receptor signaling, suggesting one of the pharmacological mechanisms by which improves photo-aged human skin.	Tretinoin	41-45	peptidase D	Homo sapiens	56-65
23430876-2	2012	Prolidase is a ubiquitous enzyme that hydrolyses dipeptides with C-terminal proline or hydroxyproline residues and indeed, lack of this enzyme activity causes massive urine excretion of undigested iminodipeptides.	Dipeptides	49-59	peptidase D	Homo sapiens	0-9
21993963-4	2012	We studied the effects of echistatin (a well-known disintegrin) and thrombin (a serine protease capable of activation of integrin alpha(2)beta(1) receptor) on prolidase activity and expressions of prolidase, alpha(2)beta(1)-integrin receptor, focal adhesion kinase (FAK), MAP-kinases (ERK(1) and ERK(2)), and nuclear HIF-1alpha in human colon adenocarcinoma (DLD-1) cells.	echistatin	26-36	peptidase D	Homo sapiens	159-168
22120822-0	2012	Hydrolysis potential of recombinant human skin and kidney prolidase against diisopropylfluorophosphate and sarin by in vitro analysis.	Isoflurophate	76-102	peptidase D	Homo sapiens	58-67
22120822-1	2012	Human prolidase (PROL), which has structural homology to bacterial organophosphate acid anhydrolase that hydrolyze organophosphates and nerve agents has been proposed recently as a potential catalytic bioscavenger.	Organophosphates	115-131	peptidase D	Homo sapiens	6-15
22120822-1	2012	Human prolidase (PROL), which has structural homology to bacterial organophosphate acid anhydrolase that hydrolyze organophosphates and nerve agents has been proposed recently as a potential catalytic bioscavenger.	Organophosphates	115-131	peptidase D	Homo sapiens	17-21
22120822-2	2012	To develop PROL as a catalytic bioscavenger, we evaluated the in vitro hydrolysis efficiency of purified recombinant human PROL against organophosphates and nerve agents.	Organophosphates	136-152	peptidase D	Homo sapiens	123-127
22120822-4	2012	The catalytic efficiency of PROL against diisopropylfluorophosphate (DFP) and nerve agents was evaluated by acetylcholinesterase back-titration assay.	Isoflurophate	41-67	peptidase D	Homo sapiens	28-32
22120822-4	2012	The catalytic efficiency of PROL against diisopropylfluorophosphate (DFP) and nerve agents was evaluated by acetylcholinesterase back-titration assay.	Isoflurophate	69-72	peptidase D	Homo sapiens	28-32
23430876-2	2012	Prolidase is a ubiquitous enzyme that hydrolyses dipeptides with C-terminal proline or hydroxyproline residues and indeed, lack of this enzyme activity causes massive urine excretion of undigested iminodipeptides.	Proline	76-83	peptidase D	Homo sapiens	0-9
23430876-2	2012	Prolidase is a ubiquitous enzyme that hydrolyses dipeptides with C-terminal proline or hydroxyproline residues and indeed, lack of this enzyme activity causes massive urine excretion of undigested iminodipeptides.	Hydroxyproline	87-101	peptidase D	Homo sapiens	0-9
21425789-1	2011	The catalytic hydrolysis of the Gly-Pro substrate by the bimetallic prolidase active site model cluster has been investigated at the DF/B3LYP level of theory, in order to provide fundamental insights into the still poorly understood mechanism of prolidase catalysis.	glycylproline	32-39	peptidase D	Homo sapiens	68-77
21699887-1	2011	BACKGROUND: Prolidase is a metallo-exopeptidase hydrolyzing X-Pro and X-Hyp dipeptides.	Dipeptides	76-86	peptidase D	Homo sapiens	12-21
21699887-7	2011	RESULTS: An activation step consisting in prolidase incubation with 1 mmol/l MnCl(2) and 0.75 mmol/l reduced glutathione at 50 C for 20 min was necessary to obtain the maximum activity and to accurately determine, for the recombinant enzyme, V(max) (489 U/mg), K(m) (5.4 mM) and Mn(2+) affinity (54 mM(-1)).	mncl	77-81	peptidase D	Homo sapiens	42-51
21699887-7	2011	RESULTS: An activation step consisting in prolidase incubation with 1 mmol/l MnCl(2) and 0.75 mmol/l reduced glutathione at 50 C for 20 min was necessary to obtain the maximum activity and to accurately determine, for the recombinant enzyme, V(max) (489 U/mg), K(m) (5.4 mM) and Mn(2+) affinity (54 mM(-1)).	Glutathione	109-120	peptidase D	Homo sapiens	42-51
21699887-7	2011	RESULTS: An activation step consisting in prolidase incubation with 1 mmol/l MnCl(2) and 0.75 mmol/l reduced glutathione at 50 C for 20 min was necessary to obtain the maximum activity and to accurately determine, for the recombinant enzyme, V(max) (489 U/mg), K(m) (5.4 mM) and Mn(2+) affinity (54 mM(-1)).	Manganese(2+)	279-285	peptidase D	Homo sapiens	42-51
21304409-5	2011	Prolidase activity was positively correlated with TOS and OSI levels.	tos	50-53	peptidase D	Homo sapiens	0-9
21425789-1	2011	The catalytic hydrolysis of the Gly-Pro substrate by the bimetallic prolidase active site model cluster has been investigated at the DF/B3LYP level of theory, in order to provide fundamental insights into the still poorly understood mechanism of prolidase catalysis.	glycylproline	32-39	peptidase D	Homo sapiens	246-255
21425789-3	2011	In addition, it has been shown recently that two different metal ions in the active site of human prolidase (Zn and Mn) can coexist, with the protein remaining partially active.	Metals	59-64	peptidase D	Homo sapiens	98-107
21425789-4	2011	With the purpose of identifying which is the most efficient dimetallic center for the prolidase catalyzed reaction, Zn(II), Co(II), and Mn(II) have been examined as potential catalytic metals for this enzyme.	Zinc	116-122	peptidase D	Homo sapiens	86-95
21425789-4	2011	With the purpose of identifying which is the most efficient dimetallic center for the prolidase catalyzed reaction, Zn(II), Co(II), and Mn(II) have been examined as potential catalytic metals for this enzyme.	Manganese(2+)	136-142	peptidase D	Homo sapiens	86-95
20383038-2	2010	Prolidase is an enzyme that catalyzes the final step of collagen breakdown by liberating free proline for collagen recycling.	Proline	94-101	peptidase D	Homo sapiens	0-9
21254236-2	2011	Prolidase has an important role in the recycling of proline for collagen synthesis and cell growth.	Proline	52-59	peptidase D	Homo sapiens	0-9
20868675-4	2010	We found that inhibitors of prolidase activity (N-benzyloxycarbonyl-l-proline, Cbz-Pro and phosphoenolopyruvate, PEP) induced decrease in TGF beta1 and its receptor expressions.	carbobenzoxyproline	48-77	peptidase D	Homo sapiens	28-37
20868675-4	2010	We found that inhibitors of prolidase activity (N-benzyloxycarbonyl-l-proline, Cbz-Pro and phosphoenolopyruvate, PEP) induced decrease in TGF beta1 and its receptor expressions.	carbobenzoxyproline	79-86	peptidase D	Homo sapiens	28-37
20868675-4	2010	We found that inhibitors of prolidase activity (N-benzyloxycarbonyl-l-proline, Cbz-Pro and phosphoenolopyruvate, PEP) induced decrease in TGF beta1 and its receptor expressions.	phosphoenolopyruvate	91-111	peptidase D	Homo sapiens	28-37
20868675-5	2010	On the other hand, products of prolidase catalytic activity, proline (Pro) and hydroxyproline (HyPro) induced increase in the amount of TGF beta1 and TGF beta receptors.	Hydroxyproline	95-100	peptidase D	Homo sapiens	31-40
20868675-10	2010	Rapamycin (pharmacological inhibitor of mTOR) resulted in decrease in prolidase activity.	Sirolimus	0-9	peptidase D	Homo sapiens	70-79
20674353-2	2010	Proline prodrug of methotrexate (Pro-MTX) was designed as a substrate of prolidase which is specific for imido bond of dipeptide containing proline and expected to penetrate MDA-MB-231 cells more efficiently.	Proline	0-7	peptidase D	Homo sapiens	73-82
20674353-2	2010	Proline prodrug of methotrexate (Pro-MTX) was designed as a substrate of prolidase which is specific for imido bond of dipeptide containing proline and expected to penetrate MDA-MB-231 cells more efficiently.	Methotrexate	19-31	peptidase D	Homo sapiens	73-82
20674353-2	2010	Proline prodrug of methotrexate (Pro-MTX) was designed as a substrate of prolidase which is specific for imido bond of dipeptide containing proline and expected to penetrate MDA-MB-231 cells more efficiently.	pro-mtx	33-40	peptidase D	Homo sapiens	73-82
20674353-2	2010	Proline prodrug of methotrexate (Pro-MTX) was designed as a substrate of prolidase which is specific for imido bond of dipeptide containing proline and expected to penetrate MDA-MB-231 cells more efficiently.	Dipeptides	119-128	peptidase D	Homo sapiens	73-82
20674353-2	2010	Proline prodrug of methotrexate (Pro-MTX) was designed as a substrate of prolidase which is specific for imido bond of dipeptide containing proline and expected to penetrate MDA-MB-231 cells more efficiently.	Proline	140-147	peptidase D	Homo sapiens	73-82
20674353-5	2010	The results showed that Pro-MTX was a substrate of prolidase.	pro-mtx	24-31	peptidase D	Homo sapiens	51-60
20824963-2	2010	The facts that prolidase plays an important role in collagen biosynthesis and that captopril directly inhibits prolidase activity led us to evaluate its effect on collagen biosynthesis in cultured human skin fibroblasts.	Captopril	83-92	peptidase D	Homo sapiens	111-120
20824963-3	2010	Confluent fibroblasts were treated with milimolar concentrations (0.2-1 mM) of captopril (CAP) for 48 h. It was found that CAP-dependent decrease in prolidase activity was accompanied by parallel decrease in collagen biosynthesis.	milimolar	40-49	peptidase D	Homo sapiens	149-158
20824963-3	2010	Confluent fibroblasts were treated with milimolar concentrations (0.2-1 mM) of captopril (CAP) for 48 h. It was found that CAP-dependent decrease in prolidase activity was accompanied by parallel decrease in collagen biosynthesis.	Captopril	79-88	peptidase D	Homo sapiens	149-158
20824963-3	2010	Confluent fibroblasts were treated with milimolar concentrations (0.2-1 mM) of captopril (CAP) for 48 h. It was found that CAP-dependent decrease in prolidase activity was accompanied by parallel decrease in collagen biosynthesis.	Captopril	90-93	peptidase D	Homo sapiens	149-158
20824963-6	2010	The data suggest that CAP-dependent decrease of collagen biosynthesis in cultured human skin fibroblasts results from inhibition of prolidase activity that may occur through inhibition of alpha2beta1 integrin and IGF-IR signaling.	Captopril	22-25	peptidase D	Homo sapiens	132-141
19415262-5	2010	In particular, as for the metal ion occupation configuration of the recombinant human prolidase, we have found that one of the two active sites is occupied by two Zn ions and the second one by one Zn and one Mn ion.	Metals	26-31	peptidase D	Homo sapiens	86-95
19415262-5	2010	In particular, as for the metal ion occupation configuration of the recombinant human prolidase, we have found that one of the two active sites is occupied by two Zn ions and the second one by one Zn and one Mn ion.	Zinc	163-165	peptidase D	Homo sapiens	86-95
19415262-5	2010	In particular, as for the metal ion occupation configuration of the recombinant human prolidase, we have found that one of the two active sites is occupied by two Zn ions and the second one by one Zn and one Mn ion.	Zinc	197-199	peptidase D	Homo sapiens	86-95
19834130-1	2010	Prolidase is a cytosolic exopeptidase that cleaves iminodipeptides with carboxy-terminal proline or hydroxyproline and plays a major role in collagen turnover.	Proline	89-96	peptidase D	Homo sapiens	0-9
19834130-1	2010	Prolidase is a cytosolic exopeptidase that cleaves iminodipeptides with carboxy-terminal proline or hydroxyproline and plays a major role in collagen turnover.	Hydroxyproline	100-114	peptidase D	Homo sapiens	0-9
19263194-4	2009	D: -Ethionine, L: -ethionine, and D: ,L: -ethionine also enhanced the activity of prolidase I.	Deuterium	34-35	peptidase D	Homo sapiens	82-91
19695763-1	2009	OBJECTIVE: Prolidase is a cytosolic exopeptidase that cleaves iminodipeptides with C-terminal proline and hydroxyproline and plays a major role in collagen turnover.	Proline	94-101	peptidase D	Homo sapiens	11-20
19695763-1	2009	OBJECTIVE: Prolidase is a cytosolic exopeptidase that cleaves iminodipeptides with C-terminal proline and hydroxyproline and plays a major role in collagen turnover.	Hydroxyproline	106-120	peptidase D	Homo sapiens	11-20
19263194-1	2009	The effect of various sulfur-containing amino acids on the activities of prolidase isoenzymes I and II isolated from erythrocytes of healthy individuals, and erythrocyte lysates from a patient with prolidase deficiency was investigated.	Sulfur	22-28	peptidase D	Homo sapiens	73-82
20144170-7	2009	Prolidase activity was positively correlated with TOS and OSI values (rho = 0.552, P = 0.041 and rho = 0.635, P = 0.015, respectively) and negatively correlated with TAC and -SH levels (rho = -0.578, P = 0.030 and rho = -0.622, P = 0.018, respectively).	tos	50-53	peptidase D	Homo sapiens	0-9
20144170-7	2009	Prolidase activity was positively correlated with TOS and OSI values (rho = 0.552, P = 0.041 and rho = 0.635, P = 0.015, respectively) and negatively correlated with TAC and -SH levels (rho = -0.578, P = 0.030 and rho = -0.622, P = 0.018, respectively).	silicon monoxide	58-61	peptidase D	Homo sapiens	0-9
20144170-8	2009	CONCLUSION: The present study shows that serum prolidase activity and oxidative stress are significantly associated with the presence of FGR and that the correlation between serum prolidase activity and markers of oxidative stress are represented as increased serum TOS level and decreased serum TAC and -SH levels, suggesting an association of collagen turnover and oxidative stress in vascular dysfunction.	tos	266-269	peptidase D	Homo sapiens	180-189
19263194-4	2009	D: -Ethionine, L: -ethionine, and D: ,L: -ethionine also enhanced the activity of prolidase I.	Ethionine	18-28	peptidase D	Homo sapiens	82-91
19263194-6	2009	The activity of prolidase II against methionylproline was enhanced by D: -methionine, D: ,L: -methionine, and L: -methionine, but N-acetyl-L: -methionine had no effect.	H-Met-Pro-OH	37-53	peptidase D	Homo sapiens	16-25
19263194-2	2009	The activity of prolidase I against glycylproline was strongly enhanced by D: -methionine.	glycylproline	36-49	peptidase D	Homo sapiens	16-25
19263194-2	2009	The activity of prolidase I against glycylproline was strongly enhanced by D: -methionine.	d: -methionine	75-89	peptidase D	Homo sapiens	16-25
19263194-4	2009	D: -Ethionine, L: -ethionine, and D: ,L: -ethionine also enhanced the activity of prolidase I.	Deuterium	0-1	peptidase D	Homo sapiens	82-91
19263194-4	2009	D: -Ethionine, L: -ethionine, and D: ,L: -ethionine also enhanced the activity of prolidase I.	Ethionine	4-13	peptidase D	Homo sapiens	82-91
19263194-4	2009	D: -Ethionine, L: -ethionine, and D: ,L: -ethionine also enhanced the activity of prolidase I.	Ethionine	15-28	peptidase D	Homo sapiens	82-91
19426854-2	2009	Prolidase specifically hydrolyzes dipeptides with a prolyl residue in the carboxy terminus (NH(2)-X-/-Pro-COOH).	Dipeptides	34-44	peptidase D	Homo sapiens	0-9
19719045-4	2009	It was found that butyrate induced collagen biosynthesis and prolidase activity.	Butyrates	18-26	peptidase D	Homo sapiens	61-70
19263194-6	2009	The activity of prolidase II against methionylproline was enhanced by D: -methionine, D: ,L: -methionine, and L: -methionine, but N-acetyl-L: -methionine had no effect.	d: -methionine	70-84	peptidase D	Homo sapiens	16-25
19263194-6	2009	The activity of prolidase II against methionylproline was enhanced by D: -methionine, D: ,L: -methionine, and L: -methionine, but N-acetyl-L: -methionine had no effect.	Deuterium	70-71	peptidase D	Homo sapiens	16-25
19263194-6	2009	The activity of prolidase II against methionylproline was enhanced by D: -methionine, D: ,L: -methionine, and L: -methionine, but N-acetyl-L: -methionine had no effect.	Methionine	90-104	peptidase D	Homo sapiens	16-25
19263194-6	2009	The activity of prolidase II against methionylproline was enhanced by D: -methionine, D: ,L: -methionine, and L: -methionine, but N-acetyl-L: -methionine had no effect.	Methionine	110-124	peptidase D	Homo sapiens	16-25
19263194-6	2009	The activity of prolidase II against methionylproline was enhanced by D: -methionine, D: ,L: -methionine, and L: -methionine, but N-acetyl-L: -methionine had no effect.	N-acetylmethionine	130-153	peptidase D	Homo sapiens	16-25
19263194-7	2009	D: -Ethionine and D: ,L: -ethionine strongly enhanced the activity of prolidase II compared with L: -ethionine; D: ,L: -homocysteine weakly enhanced the activity.	Ethionine	4-13	peptidase D	Homo sapiens	70-79
19263194-7	2009	D: -Ethionine and D: ,L: -ethionine strongly enhanced the activity of prolidase II compared with L: -ethionine; D: ,L: -homocysteine weakly enhanced the activity.	Ethionine	23-35	peptidase D	Homo sapiens	70-79
19263194-7	2009	D: -Ethionine and D: ,L: -ethionine strongly enhanced the activity of prolidase II compared with L: -ethionine; D: ,L: -homocysteine weakly enhanced the activity.	Ethionine	22-35	peptidase D	Homo sapiens	70-79
19263194-7	2009	D: -Ethionine and D: ,L: -ethionine strongly enhanced the activity of prolidase II compared with L: -ethionine; D: ,L: -homocysteine weakly enhanced the activity.	Homocysteine	120-132	peptidase D	Homo sapiens	70-79
19263194-8	2009	D: ,L: -Homocysteine-thiolactone inhibited the activities of prolidase I and II in a concentration-dependent manner.	homocysteine thiolactone	8-32	peptidase D	Homo sapiens	61-70
19263194-9	2009	The effect of various sulfur-containing amino acids on prolidase activity against methionylproline in erythrocyte lysates from a patient with prolidase deficiency was almost the same as that on prolidase II.	Sulfur	22-28	peptidase D	Homo sapiens	55-64
19263194-9	2009	The effect of various sulfur-containing amino acids on prolidase activity against methionylproline in erythrocyte lysates from a patient with prolidase deficiency was almost the same as that on prolidase II.	Sulfur	22-28	peptidase D	Homo sapiens	142-151
19263194-9	2009	The effect of various sulfur-containing amino acids on prolidase activity against methionylproline in erythrocyte lysates from a patient with prolidase deficiency was almost the same as that on prolidase II.	H-Met-Pro-OH	82-98	peptidase D	Homo sapiens	55-64
19263194-9	2009	The effect of various sulfur-containing amino acids on prolidase activity against methionylproline in erythrocyte lysates from a patient with prolidase deficiency was almost the same as that on prolidase II.	H-Met-Pro-OH	82-98	peptidase D	Homo sapiens	142-151
19645322-4	2009	It was found that butyrate induced collagen biosynthesis and prolidase activity.	Butyrates	18-26	peptidase D	Homo sapiens	61-70
19426854-2	2009	Prolidase specifically hydrolyzes dipeptides with a prolyl residue in the carboxy terminus (NH(2)-X-/-Pro-COOH).	Carbonic Acid	106-110	peptidase D	Homo sapiens	0-9
19426854-5	2009	Prolidase is able to degrade toxic organophosphorus (OP) compounds, namely, by cleaving the P-F and P-O bonds in the nerve agents, sarin and soman.	organophosphorus	35-51	peptidase D	Homo sapiens	0-9
19426854-6	2009	Applications using prolidase to detoxify OP nerve agents include its incorporation into fire-fighting foams and as biosensors for OP compound detection.	Organophosphorus Compounds	130-141	peptidase D	Homo sapiens	19-28
19288447-2	2009	The enzyme prolidase plays an important role in the breakdown of collagen and the breakdown of intracellular protein especially in the final stage when peptides and dipeptides contain a high level of proline.	Dipeptides	165-175	peptidase D	Homo sapiens	11-20
19288447-2	2009	The enzyme prolidase plays an important role in the breakdown of collagen and the breakdown of intracellular protein especially in the final stage when peptides and dipeptides contain a high level of proline.	Proline	200-207	peptidase D	Homo sapiens	11-20
18491034-2	2008	The finding that prolidase plays an important role in collagen biosynthesis and phosphoenolpyruvate inhibits prolidase activity "in vitro" led to evaluate its effect on collagen biosynthesis in cultured human skin fibroblasts.	Phosphoenolpyruvate	80-99	peptidase D	Homo sapiens	109-118
18320291-1	2008	Prolidase [EC.3.4.13.9] is a cytosolic imidodipeptidase, which specifically splits imidodipeptides with C-terminal proline or hydroxyproline.	Proline	115-122	peptidase D	Homo sapiens	0-9
18320291-1	2008	Prolidase [EC.3.4.13.9] is a cytosolic imidodipeptidase, which specifically splits imidodipeptides with C-terminal proline or hydroxyproline.	Hydroxyproline	126-140	peptidase D	Homo sapiens	0-9
18340504-0	2008	Human prolidase and prolidase deficiency: an overview on the characterization of the enzyme involved in proline recycling and on the effects of its mutations.	Proline	104-111	peptidase D	Homo sapiens	6-15
18340504-2	2008	Among the peptidases, prolidase is the only metalloenzyme that cleaves the iminodipeptides containing a proline or hydroxyproline residue at the C-terminal end.	Proline	104-111	peptidase D	Homo sapiens	22-31
18340504-2	2008	Among the peptidases, prolidase is the only metalloenzyme that cleaves the iminodipeptides containing a proline or hydroxyproline residue at the C-terminal end.	Hydroxyproline	115-129	peptidase D	Homo sapiens	22-31
18340504-4	2008	Beside its intracellular functions, prolidase has an antitoxic effect against some organophosphorus molecules, can be used in dietary industry as bitterness reducing agent and recently has been used as target enzyme for specific melanoma prodrug activation.	organophosphorus	83-99	peptidase D	Homo sapiens	36-45
18806116-5	2008	Proline as substrate is stored as collagen in extracellular matrix, connective tissue, and bone and it is rapidly released from this reservoir by the sequential action of matrix metalloproteinases, peptidases, and prolidase.	Proline	0-7	peptidase D	Homo sapiens	214-223
18806117-16	2008	Prolidase catalyzes hydrolysis of dipeptide or oligopeptide with a C-terminal proline or hydroxyproline and its deficiency can cause mental retardation and severe skin ulcers.	Dipeptides	34-43	peptidase D	Homo sapiens	0-9
18806117-16	2008	Prolidase catalyzes hydrolysis of dipeptide or oligopeptide with a C-terminal proline or hydroxyproline and its deficiency can cause mental retardation and severe skin ulcers.	Proline	78-85	peptidase D	Homo sapiens	0-9
18806117-16	2008	Prolidase catalyzes hydrolysis of dipeptide or oligopeptide with a C-terminal proline or hydroxyproline and its deficiency can cause mental retardation and severe skin ulcers.	Hydroxyproline	89-103	peptidase D	Homo sapiens	0-9
18607169-10	2008	Independent predictors of serum prolidase activity were serum high-density lipoprotein cholesterol (beta=-0.138, P=0.023) and urea levels (beta=0.146, P=0.036), and Gensini score (beta=0.317, P<0.001).	Urea	126-130	peptidase D	Homo sapiens	32-41
18607169-1	2008	OBJECTIVES: Prolidase is a cytosolic exopeptidase that cleaves iminodipeptides with carboxy-terminal proline or hydroxyproline and plays major role in collagen turnover.	Proline	101-108	peptidase D	Homo sapiens	12-21
18607169-1	2008	OBJECTIVES: Prolidase is a cytosolic exopeptidase that cleaves iminodipeptides with carboxy-terminal proline or hydroxyproline and plays major role in collagen turnover.	Hydroxyproline	112-126	peptidase D	Homo sapiens	12-21
18491034-3	2008	Confluent fibroblasts were treated with millimolar concentrations (1-4 mM) of phosphoenolpyruvate monopotassium salt (PEP) for 24 h. It was found that PEP-dependent decrease in prolidase activity and expression was accompanied by parallel decrease in collagen biosynthesis.	Phosphoenolpyruvate	78-97	peptidase D	Homo sapiens	177-186
18491034-3	2008	Confluent fibroblasts were treated with millimolar concentrations (1-4 mM) of phosphoenolpyruvate monopotassium salt (PEP) for 24 h. It was found that PEP-dependent decrease in prolidase activity and expression was accompanied by parallel decrease in collagen biosynthesis.	monopotassium salt	98-116	peptidase D	Homo sapiens	177-186
18491034-3	2008	Confluent fibroblasts were treated with millimolar concentrations (1-4 mM) of phosphoenolpyruvate monopotassium salt (PEP) for 24 h. It was found that PEP-dependent decrease in prolidase activity and expression was accompanied by parallel decrease in collagen biosynthesis.	Phosphoenolpyruvate	118-121	peptidase D	Homo sapiens	177-186
18550075-2	2008	The different effects of reaction conditions including the concentration of Mn(2+), incubation temperature and pH on prolidase (PLD, EC 3.4.13.9) activity in erythrocyte lysates against three different substrates, Gly-Pro, Val-Pro and Leu-Pro were investigated.	glycylproline	214-221	peptidase D	Homo sapiens	117-126
18550075-2	2008	The different effects of reaction conditions including the concentration of Mn(2+), incubation temperature and pH on prolidase (PLD, EC 3.4.13.9) activity in erythrocyte lysates against three different substrates, Gly-Pro, Val-Pro and Leu-Pro were investigated.	glycylproline	214-221	peptidase D	Homo sapiens	128-131
18550075-2	2008	The different effects of reaction conditions including the concentration of Mn(2+), incubation temperature and pH on prolidase (PLD, EC 3.4.13.9) activity in erythrocyte lysates against three different substrates, Gly-Pro, Val-Pro and Leu-Pro were investigated.	L-valyl-L-proline	223-230	peptidase D	Homo sapiens	117-126
18550075-2	2008	The different effects of reaction conditions including the concentration of Mn(2+), incubation temperature and pH on prolidase (PLD, EC 3.4.13.9) activity in erythrocyte lysates against three different substrates, Gly-Pro, Val-Pro and Leu-Pro were investigated.	L-valyl-L-proline	223-230	peptidase D	Homo sapiens	128-131
18550075-2	2008	The different effects of reaction conditions including the concentration of Mn(2+), incubation temperature and pH on prolidase (PLD, EC 3.4.13.9) activity in erythrocyte lysates against three different substrates, Gly-Pro, Val-Pro and Leu-Pro were investigated.	leucylproline	235-242	peptidase D	Homo sapiens	117-126
18550075-2	2008	The different effects of reaction conditions including the concentration of Mn(2+), incubation temperature and pH on prolidase (PLD, EC 3.4.13.9) activity in erythrocyte lysates against three different substrates, Gly-Pro, Val-Pro and Leu-Pro were investigated.	leucylproline	235-242	peptidase D	Homo sapiens	128-131
18550075-3	2008	Also, the effects of colchicine which can prevent or delay cancer of liver on the PLD activity were studied.	Colchicine	21-31	peptidase D	Homo sapiens	82-85
18550075-4	2008	For Gly-Pro and Leu-Pro, colchicine enhanced PLD activity, while for the other substrate Val-Pro, it had a slight inhibiting effect on prolidase activity.	Colchicine	25-35	peptidase D	Homo sapiens	45-48
18550075-4	2008	For Gly-Pro and Leu-Pro, colchicine enhanced PLD activity, while for the other substrate Val-Pro, it had a slight inhibiting effect on prolidase activity.	Colchicine	25-35	peptidase D	Homo sapiens	135-144
18550075-5	2008	Kinetic study of colchicine on prolidase activity in erythrocytes indicated different effects for different substrates with the addition of colchicine.	Colchicine	17-27	peptidase D	Homo sapiens	31-40
18550075-5	2008	Kinetic study of colchicine on prolidase activity in erythrocytes indicated different effects for different substrates with the addition of colchicine.	Colchicine	140-150	peptidase D	Homo sapiens	31-40
17377743-0	2007	Proline prodrug of melphalan targeted to prolidase, a prodrug activating enzyme overexpressed in melanoma.	Proline	0-7	peptidase D	Homo sapiens	41-50
18455892-1	2008	The first aim of this work was to perform site-directed PEGylation of the enzyme prolidase at sulphydril groups by methoxy-polyethylene glycol-maleimide (Mal-PEG, Mw 5000 Da) in order to obtain a safe conjugation product more stable than the native enzyme.	sulphydril	94-104	peptidase D	Homo sapiens	81-90
18455892-1	2008	The first aim of this work was to perform site-directed PEGylation of the enzyme prolidase at sulphydril groups by methoxy-polyethylene glycol-maleimide (Mal-PEG, Mw 5000 Da) in order to obtain a safe conjugation product more stable than the native enzyme.	methoxy-polyethylene glycol-maleimide	115-152	peptidase D	Homo sapiens	81-90
18455892-1	2008	The first aim of this work was to perform site-directed PEGylation of the enzyme prolidase at sulphydril groups by methoxy-polyethylene glycol-maleimide (Mal-PEG, Mw 5000 Da) in order to obtain a safe conjugation product more stable than the native enzyme.	mal-peg	154-161	peptidase D	Homo sapiens	81-90
18455892-4	2008	The SDS-PAGE analysis and the ESI-MS spectra confirmed the presence of the PEGylated prolidase: in particular the main conjugation product (m/z=about 65,000 Da) corresponded to the enzyme with two residues of Mal-PEG.	Sodium Dodecyl Sulfate	4-7	peptidase D	Homo sapiens	85-94
18455892-4	2008	The SDS-PAGE analysis and the ESI-MS spectra confirmed the presence of the PEGylated prolidase: in particular the main conjugation product (m/z=about 65,000 Da) corresponded to the enzyme with two residues of Mal-PEG.	mal-peg	209-216	peptidase D	Homo sapiens	85-94
18157855-5	2008	Overexpression of prolidase in some neoplastic cells suggests that the proline analogue of alkylating agents may serve as a prolidase convertible prodrugs.	Proline	71-78	peptidase D	Homo sapiens	18-27
18157855-5	2008	Overexpression of prolidase in some neoplastic cells suggests that the proline analogue of alkylating agents may serve as a prolidase convertible prodrugs.	Proline	71-78	peptidase D	Homo sapiens	124-133
17982699-11	2007	Stimulation of collagen synthesis and prolidase activity by apigenin 7-O-glucuronide was accompanied by an increase in IGF-I receptor expression.	7-o-glucuronide	69-84	peptidase D	Homo sapiens	38-47
17654175-0	2007	Chitosan glutamate nanoparticles for protein delivery: development and effect on prolidase stability.	Glutamic Acid	9-18	peptidase D	Homo sapiens	81-90
17654175-1	2007	PURPOSE: To evaluate the feasibility of exploiting ultrasonication coupled with ionotropic gelation in order to prepare tripolyphosphate (TPP)-chitosan glutamate nanoparticles suitable for the delivery of the enzyme prolidase.	triphosphoric acid	120-136	peptidase D	Homo sapiens	216-225
17654175-1	2007	PURPOSE: To evaluate the feasibility of exploiting ultrasonication coupled with ionotropic gelation in order to prepare tripolyphosphate (TPP)-chitosan glutamate nanoparticles suitable for the delivery of the enzyme prolidase.	triphosphoric acid	138-141	peptidase D	Homo sapiens	216-225
17654175-1	2007	PURPOSE: To evaluate the feasibility of exploiting ultrasonication coupled with ionotropic gelation in order to prepare tripolyphosphate (TPP)-chitosan glutamate nanoparticles suitable for the delivery of the enzyme prolidase.	Glutamic Acid	152-161	peptidase D	Homo sapiens	216-225
17377743-1	2007	PURPOSE: To determine the bioactivation and uptake of prolidase-targeted proline prodrugs of melphalan in six cancer cell lines with variable prolidase expression and to evaluate prolidase-dependence of prodrug cytotoxicity in the cell lines compared to that of the parent drug, melphalan.	Proline	73-80	peptidase D	Homo sapiens	54-63
17377743-1	2007	PURPOSE: To determine the bioactivation and uptake of prolidase-targeted proline prodrugs of melphalan in six cancer cell lines with variable prolidase expression and to evaluate prolidase-dependence of prodrug cytotoxicity in the cell lines compared to that of the parent drug, melphalan.	Proline	73-80	peptidase D	Homo sapiens	142-151
17377743-1	2007	PURPOSE: To determine the bioactivation and uptake of prolidase-targeted proline prodrugs of melphalan in six cancer cell lines with variable prolidase expression and to evaluate prolidase-dependence of prodrug cytotoxicity in the cell lines compared to that of the parent drug, melphalan.	Proline	73-80	peptidase D	Homo sapiens	142-151
17377743-1	2007	PURPOSE: To determine the bioactivation and uptake of prolidase-targeted proline prodrugs of melphalan in six cancer cell lines with variable prolidase expression and to evaluate prolidase-dependence of prodrug cytotoxicity in the cell lines compared to that of the parent drug, melphalan.	Melphalan	93-102	peptidase D	Homo sapiens	54-63
17377743-1	2007	PURPOSE: To determine the bioactivation and uptake of prolidase-targeted proline prodrugs of melphalan in six cancer cell lines with variable prolidase expression and to evaluate prolidase-dependence of prodrug cytotoxicity in the cell lines compared to that of the parent drug, melphalan.	Melphalan	93-102	peptidase D	Homo sapiens	142-151
17377743-1	2007	PURPOSE: To determine the bioactivation and uptake of prolidase-targeted proline prodrugs of melphalan in six cancer cell lines with variable prolidase expression and to evaluate prolidase-dependence of prodrug cytotoxicity in the cell lines compared to that of the parent drug, melphalan.	Melphalan	93-102	peptidase D	Homo sapiens	142-151
17169973-0	2007	Prolidase-independent mechanism of camptothecin-induced inhibition of collagen biosynthesis in cultured human skin fibroblasts.	Camptothecin	35-47	peptidase D	Homo sapiens	0-9
16899234-8	2007	On the other hand, prolidase activity against glycylproline was enhanced by L-methionine, D-methionine, D,L-methionine, D,L-homocysteine thiolactone and D,L-ethionine.	Racemethionine	104-118	peptidase D	Homo sapiens	19-28
16899234-8	2007	On the other hand, prolidase activity against glycylproline was enhanced by L-methionine, D-methionine, D,L-methionine, D,L-homocysteine thiolactone and D,L-ethionine.	d,l-homocysteine thiolactone	120-148	peptidase D	Homo sapiens	19-28
16899234-6	2007	RESULTS: Prolinase activity against prolylglycine in normal and prolidase-deficient erythrocyte lysates was inhibited by L-methionine, NAc-L-methionine and D,L-methionine in a concentration-dependent manner, but D-methionine enhanced the activity in low concentrations (0-20 mmol/l).	prolylglycine	36-49	peptidase D	Homo sapiens	64-73
16899234-6	2007	RESULTS: Prolinase activity against prolylglycine in normal and prolidase-deficient erythrocyte lysates was inhibited by L-methionine, NAc-L-methionine and D,L-methionine in a concentration-dependent manner, but D-methionine enhanced the activity in low concentrations (0-20 mmol/l).	Methionine	121-133	peptidase D	Homo sapiens	64-73
16899234-6	2007	RESULTS: Prolinase activity against prolylglycine in normal and prolidase-deficient erythrocyte lysates was inhibited by L-methionine, NAc-L-methionine and D,L-methionine in a concentration-dependent manner, but D-methionine enhanced the activity in low concentrations (0-20 mmol/l).	Racemethionine	156-170	peptidase D	Homo sapiens	64-73
16899234-6	2007	RESULTS: Prolinase activity against prolylglycine in normal and prolidase-deficient erythrocyte lysates was inhibited by L-methionine, NAc-L-methionine and D,L-methionine in a concentration-dependent manner, but D-methionine enhanced the activity in low concentrations (0-20 mmol/l).	D-Methionine	212-224	peptidase D	Homo sapiens	64-73
16899234-8	2007	On the other hand, prolidase activity against glycylproline was enhanced by L-methionine, D-methionine, D,L-methionine, D,L-homocysteine thiolactone and D,L-ethionine.	glycylproline	46-59	peptidase D	Homo sapiens	19-28
16899234-8	2007	On the other hand, prolidase activity against glycylproline was enhanced by L-methionine, D-methionine, D,L-methionine, D,L-homocysteine thiolactone and D,L-ethionine.	Methionine	76-88	peptidase D	Homo sapiens	19-28
16899234-8	2007	On the other hand, prolidase activity against glycylproline was enhanced by L-methionine, D-methionine, D,L-methionine, D,L-homocysteine thiolactone and D,L-ethionine.	D-Methionine	90-102	peptidase D	Homo sapiens	19-28
16899234-8	2007	On the other hand, prolidase activity against glycylproline was enhanced by L-methionine, D-methionine, D,L-methionine, D,L-homocysteine thiolactone and D,L-ethionine.	DL-ETHIONINE	153-166	peptidase D	Homo sapiens	19-28
16899234-10	2007	CONCLUSION: The prolinase activity in normal and prolidase-deficient erythrocyte lysates was inhibited by L-methionine, D,L-ethionine and D,L-homocysteine.	Methionine	106-118	peptidase D	Homo sapiens	49-58
16899234-10	2007	CONCLUSION: The prolinase activity in normal and prolidase-deficient erythrocyte lysates was inhibited by L-methionine, D,L-ethionine and D,L-homocysteine.	DL-ETHIONINE	120-133	peptidase D	Homo sapiens	49-58
16899234-10	2007	CONCLUSION: The prolinase activity in normal and prolidase-deficient erythrocyte lysates was inhibited by L-methionine, D,L-ethionine and D,L-homocysteine.	DL-Homocysteine	138-154	peptidase D	Homo sapiens	49-58
16899234-11	2007	On the other hand, prolidase activity in their erythrocyte lysates was enhanced by D,L-ethionine, D-methionine and L-methionine.	DL-ETHIONINE	83-96	peptidase D	Homo sapiens	19-28
16899234-11	2007	On the other hand, prolidase activity in their erythrocyte lysates was enhanced by D,L-ethionine, D-methionine and L-methionine.	D-Methionine	98-110	peptidase D	Homo sapiens	19-28
16899234-11	2007	On the other hand, prolidase activity in their erythrocyte lysates was enhanced by D,L-ethionine, D-methionine and L-methionine.	Methionine	115-127	peptidase D	Homo sapiens	19-28
16899234-12	2007	These results indicate the effects of these sulfur amino acids on prolidase and prolinase activities were different.	Amino Acids, Sulfur	44-62	peptidase D	Homo sapiens	66-75
16991207-0	2006	Kinetic study of paracetamol on prolidase activity in erythrocytes by capillary electrophoresis with Ru(bpy)(3) (2+) electrochemiluminescence detection.	ru(bpy)(	101-109	peptidase D	Homo sapiens	32-41
17010622-4	2006	We have suggested that prolidase, an enzyme involved in collagen metabolism, may be one of the targets for aminoglycoside-induced inhibition of collagen biosynthesis.	Aminoglycosides	107-121	peptidase D	Homo sapiens	23-32
17010622-5	2006	We found that netilmicin strongly induced inhibition of prolidase activity (IC(50)<5microM) and collagen biosynthesis (IC(50) approximately 10microM).	Netilmicin	14-24	peptidase D	Homo sapiens	56-65
17010622-7	2006	Melanin at 100microg/mL produced about 30% inhibition of collagen biosynthesis and about 30% inhibition of prolidase activity in cultured fibroblasts.	Melanins	0-7	peptidase D	Homo sapiens	107-116
17010622-8	2006	However, the addition of melanin (100microg/mL) to netilmicin-treated cells (10microM) restored the prolidase activity in fibroblasts to almost 100% of control values and partially reversed the inhibitory action of the drug on collagen and DNA biosynthesis.	Melanins	25-32	peptidase D	Homo sapiens	100-109
17010622-8	2006	However, the addition of melanin (100microg/mL) to netilmicin-treated cells (10microM) restored the prolidase activity in fibroblasts to almost 100% of control values and partially reversed the inhibitory action of the drug on collagen and DNA biosynthesis.	Netilmicin	51-61	peptidase D	Homo sapiens	100-109
17010622-9	2006	The data suggest that the ability of netilmicin to form stable complexes with melanin may prevent its toxicity on prolidase activity and collagen biosynthesis.	Melanins	78-85	peptidase D	Homo sapiens	114-123
16991207-2	2006	Effects of four nonsteroidal anti-inflammatory drugs including aspirin, paracetamol, sodium salicylate and phenacetin on prolidase (PLD) activity in erythrocytes were investigated.	Sodium Salicylate	85-102	peptidase D	Homo sapiens	132-135
16991207-2	2006	Effects of four nonsteroidal anti-inflammatory drugs including aspirin, paracetamol, sodium salicylate and phenacetin on prolidase (PLD) activity in erythrocytes were investigated.	Phenacetin	107-117	peptidase D	Homo sapiens	121-130
16991207-2	2006	Effects of four nonsteroidal anti-inflammatory drugs including aspirin, paracetamol, sodium salicylate and phenacetin on prolidase (PLD) activity in erythrocytes were investigated.	Phenacetin	107-117	peptidase D	Homo sapiens	132-135
17081196-2	2006	Prolidase is a Mn(2+)-dependent dipeptidase that cleaves imidodipeptides containing C-terminal proline or hydroxyproline.	Proline	95-102	peptidase D	Homo sapiens	0-9
17081196-2	2006	Prolidase is a Mn(2+)-dependent dipeptidase that cleaves imidodipeptides containing C-terminal proline or hydroxyproline.	Hydroxyproline	106-120	peptidase D	Homo sapiens	0-9
17081196-4	2006	In this study, recombinant prolidase was produced as a fusion protein with an N-terminal histidine tag in eukaryotic and prokaryotic hosts and purified in a single step using immobilized metal affinity chromatography.	Histidine	89-98	peptidase D	Homo sapiens	27-36
17081196-4	2006	In this study, recombinant prolidase was produced as a fusion protein with an N-terminal histidine tag in eukaryotic and prokaryotic hosts and purified in a single step using immobilized metal affinity chromatography.	Metals	187-192	peptidase D	Homo sapiens	27-36
16991207-3	2006	Aspirin enhanced PLD activity whereas the other three had inhibiting effects.	Aspirin	0-7	peptidase D	Homo sapiens	17-20
16991207-2	2006	Effects of four nonsteroidal anti-inflammatory drugs including aspirin, paracetamol, sodium salicylate and phenacetin on prolidase (PLD) activity in erythrocytes were investigated.	Aspirin	63-70	peptidase D	Homo sapiens	132-135
16991207-5	2006	Kinetic study of paracetamol on PLD showed that the value of Michaelis constant K(m) for PLD was 1.23 mM.	Acetaminophen	17-28	peptidase D	Homo sapiens	32-35
16991207-2	2006	Effects of four nonsteroidal anti-inflammatory drugs including aspirin, paracetamol, sodium salicylate and phenacetin on prolidase (PLD) activity in erythrocytes were investigated.	Acetaminophen	72-83	peptidase D	Homo sapiens	132-135
16991207-5	2006	Kinetic study of paracetamol on PLD showed that the value of Michaelis constant K(m) for PLD was 1.23 mM.	Acetaminophen	17-28	peptidase D	Homo sapiens	89-92
16730667-5	2006	The greater potency of AB4 to suppress collagen synthesis was found to be accompanied by a stronger inhibition of prolidase activity and expression compared to melphalan.	CHEMBL371915	23-26	peptidase D	Homo sapiens	114-123
16991207-6	2006	The mechanism of PLD inhibition by paracetamol is noncompetitive inhibition, and the inhibitor constant K(i) value obtained in our research was 9.73 x 10(3) microg/L.	Acetaminophen	35-46	peptidase D	Homo sapiens	17-20
16541197-2	2006	Confluent human dermal fibroblasts were treated with 2 mM and 4 mM of sodium butyrate (NaB) for 48 h. It was found that butyrate induced collagen biosynthesis and prolidase activity independently of alpha2beta1 integrin signaling.	Butyric Acid	70-85	peptidase D	Homo sapiens	163-172
16541197-2	2006	Confluent human dermal fibroblasts were treated with 2 mM and 4 mM of sodium butyrate (NaB) for 48 h. It was found that butyrate induced collagen biosynthesis and prolidase activity independently of alpha2beta1 integrin signaling.	nab	87-90	peptidase D	Homo sapiens	163-172
16541197-2	2006	Confluent human dermal fibroblasts were treated with 2 mM and 4 mM of sodium butyrate (NaB) for 48 h. It was found that butyrate induced collagen biosynthesis and prolidase activity independently of alpha2beta1 integrin signaling.	Butyrates	77-85	peptidase D	Homo sapiens	163-172
16122899-5	2006	The SDS-PAGE of the recombinant human prolidase (rh-prolidase) in induction medium showed a molecular weight of 73 kDa.	Sodium Dodecyl Sulfate	4-7	peptidase D	Homo sapiens	38-47
16642978-0	2006	Characterization of prolidase activity using capillary electrophoresis with tris(2,2"-bipyridyl)ruthenium(II) electrochemiluminescence detection and application to evaluate collagen degradation in diabetes mellitus.	tris(2,2'-bipyridyl)ruthenium(II)	76-109	peptidase D	Homo sapiens	20-29
16642978-1	2006	A new method for prolidase (PLD, EC 3.4.13.9) activity assay was developed based on the determination of proline produced from enzymatic reaction through capillary electrophoresis (CE) with tris(2,2"-bipyridyl)ruthenium(II) [Ru(bpy)3(2+)] electrochemiluminescence detection (ECL).	Proline	105-112	peptidase D	Homo sapiens	17-26
16642978-1	2006	A new method for prolidase (PLD, EC 3.4.13.9) activity assay was developed based on the determination of proline produced from enzymatic reaction through capillary electrophoresis (CE) with tris(2,2"-bipyridyl)ruthenium(II) [Ru(bpy)3(2+)] electrochemiluminescence detection (ECL).	Proline	105-112	peptidase D	Homo sapiens	28-31
16642978-1	2006	A new method for prolidase (PLD, EC 3.4.13.9) activity assay was developed based on the determination of proline produced from enzymatic reaction through capillary electrophoresis (CE) with tris(2,2"-bipyridyl)ruthenium(II) [Ru(bpy)3(2+)] electrochemiluminescence detection (ECL).	tris(2,2"-bipyridyl)ruthenium	190-219	peptidase D	Homo sapiens	17-26
16642978-1	2006	A new method for prolidase (PLD, EC 3.4.13.9) activity assay was developed based on the determination of proline produced from enzymatic reaction through capillary electrophoresis (CE) with tris(2,2"-bipyridyl)ruthenium(II) [Ru(bpy)3(2+)] electrochemiluminescence detection (ECL).	tris(2,2"-bipyridyl)ruthenium	190-219	peptidase D	Homo sapiens	28-31
16642978-1	2006	A new method for prolidase (PLD, EC 3.4.13.9) activity assay was developed based on the determination of proline produced from enzymatic reaction through capillary electrophoresis (CE) with tris(2,2"-bipyridyl)ruthenium(II) [Ru(bpy)3(2+)] electrochemiluminescence detection (ECL).	(bpy)3	227-233	peptidase D	Homo sapiens	17-26
16642978-1	2006	A new method for prolidase (PLD, EC 3.4.13.9) activity assay was developed based on the determination of proline produced from enzymatic reaction through capillary electrophoresis (CE) with tris(2,2"-bipyridyl)ruthenium(II) [Ru(bpy)3(2+)] electrochemiluminescence detection (ECL).	(bpy)3	227-233	peptidase D	Homo sapiens	28-31
16642978-2	2006	A detection limit of 12.2 fmol (S/N = 3) for proline, corresponding to 1.22 x 10(-8) units of prolidase catalyzing for 1 min was achieved.	Proline	45-52	peptidase D	Homo sapiens	94-103
16634881-3	2006	Prolidase, an imidodipeptide-cleaving cytosolic enzyme, plays an important role in the collagen catabolic process by recycling proline for collagen synthesis.	Proline	127-134	peptidase D	Homo sapiens	0-9
16470701-1	2006	Encoded by the peptidase D (PEPD) gene located at 19q12-q13.11, prolidase is a ubiquitous cytosolic enzyme that catalyzes hydrolysis of oligopeptides with a C-terminal proline or hydroxyproline.	Proline	168-175	peptidase D	Homo sapiens	15-26
16470701-1	2006	Encoded by the peptidase D (PEPD) gene located at 19q12-q13.11, prolidase is a ubiquitous cytosolic enzyme that catalyzes hydrolysis of oligopeptides with a C-terminal proline or hydroxyproline.	Proline	168-175	peptidase D	Homo sapiens	28-32
16470701-1	2006	Encoded by the peptidase D (PEPD) gene located at 19q12-q13.11, prolidase is a ubiquitous cytosolic enzyme that catalyzes hydrolysis of oligopeptides with a C-terminal proline or hydroxyproline.	Proline	168-175	peptidase D	Homo sapiens	64-73
16470701-1	2006	Encoded by the peptidase D (PEPD) gene located at 19q12-q13.11, prolidase is a ubiquitous cytosolic enzyme that catalyzes hydrolysis of oligopeptides with a C-terminal proline or hydroxyproline.	Hydroxyproline	179-193	peptidase D	Homo sapiens	15-26
16470701-1	2006	Encoded by the peptidase D (PEPD) gene located at 19q12-q13.11, prolidase is a ubiquitous cytosolic enzyme that catalyzes hydrolysis of oligopeptides with a C-terminal proline or hydroxyproline.	Hydroxyproline	179-193	peptidase D	Homo sapiens	28-32
16470701-1	2006	Encoded by the peptidase D (PEPD) gene located at 19q12-q13.11, prolidase is a ubiquitous cytosolic enzyme that catalyzes hydrolysis of oligopeptides with a C-terminal proline or hydroxyproline.	Hydroxyproline	179-193	peptidase D	Homo sapiens	64-73
16122899-5	2006	The SDS-PAGE of the recombinant human prolidase (rh-prolidase) in induction medium showed a molecular weight of 73 kDa.	Sodium Dodecyl Sulfate	4-7	peptidase D	Homo sapiens	52-61
16122899-9	2006	The rh-prolidase purified from the supernatant by ion exchange gradient chromatography (DEAE-Sepharose Fast Flow) and gel filtration chromatography (Sephacryl S-200 High Resolution) showed a single band by SDS-PAGE analysis.	deae-sepharose	88-102	peptidase D	Homo sapiens	7-16
16122899-9	2006	The rh-prolidase purified from the supernatant by ion exchange gradient chromatography (DEAE-Sepharose Fast Flow) and gel filtration chromatography (Sephacryl S-200 High Resolution) showed a single band by SDS-PAGE analysis.	sephacryl s	149-160	peptidase D	Homo sapiens	7-16
16122899-9	2006	The rh-prolidase purified from the supernatant by ion exchange gradient chromatography (DEAE-Sepharose Fast Flow) and gel filtration chromatography (Sephacryl S-200 High Resolution) showed a single band by SDS-PAGE analysis.	Sodium Dodecyl Sulfate	206-209	peptidase D	Homo sapiens	7-16
15661571-6	2005	It has been found that treatment of the cells with 100nM echistatin contributes to inhibition of collagen production, as well as prolidase activity and expression compared to control cells.	echistatin	57-67	peptidase D	Homo sapiens	129-138
16167338-0	2005	Nitric oxide regulates prolidase activity by serine/threonine phosphorylation.	Nitric Oxide	0-12	peptidase D	Homo sapiens	23-32
16167338-0	2005	Nitric oxide regulates prolidase activity by serine/threonine phosphorylation.	Serine	45-51	peptidase D	Homo sapiens	23-32
16167338-0	2005	Nitric oxide regulates prolidase activity by serine/threonine phosphorylation.	Threonine	52-61	peptidase D	Homo sapiens	23-32
16167338-12	2005	We observed increased serine/threonine phosphorylation on prolidase protein in cells treated with NO donors and in cells transfected with iNOS.	Serine	22-28	peptidase D	Homo sapiens	58-67
16167338-12	2005	We observed increased serine/threonine phosphorylation on prolidase protein in cells treated with NO donors and in cells transfected with iNOS.	Threonine	29-38	peptidase D	Homo sapiens	58-67
16167338-13	2005	To determinate the pathways that may mediate prolidase induction by NO, we first used 8-Br-cGMP, a cGMP agonist, and found that 8-Br-cGMP strongly and rapidly stimulated prolidase activity accompanied by increased phosphorylation.	8-bromoguanosino-3',5'-cyclic monophosphorothioate	86-95	peptidase D	Homo sapiens	45-54
16167338-13	2005	To determinate the pathways that may mediate prolidase induction by NO, we first used 8-Br-cGMP, a cGMP agonist, and found that 8-Br-cGMP strongly and rapidly stimulated prolidase activity accompanied by increased phosphorylation.	8-bromoguanosino-3',5'-cyclic monophosphorothioate	86-95	peptidase D	Homo sapiens	170-179
16167338-13	2005	To determinate the pathways that may mediate prolidase induction by NO, we first used 8-Br-cGMP, a cGMP agonist, and found that 8-Br-cGMP strongly and rapidly stimulated prolidase activity accompanied by increased phosphorylation.	Cyclic GMP	91-95	peptidase D	Homo sapiens	45-54
16167338-13	2005	To determinate the pathways that may mediate prolidase induction by NO, we first used 8-Br-cGMP, a cGMP agonist, and found that 8-Br-cGMP strongly and rapidly stimulated prolidase activity accompanied by increased phosphorylation.	Cyclic GMP	91-95	peptidase D	Homo sapiens	170-179
16167338-13	2005	To determinate the pathways that may mediate prolidase induction by NO, we first used 8-Br-cGMP, a cGMP agonist, and found that 8-Br-cGMP strongly and rapidly stimulated prolidase activity accompanied by increased phosphorylation.	8-bromoguanosino-3',5'-cyclic monophosphorothioate	128-137	peptidase D	Homo sapiens	45-54
16167338-13	2005	To determinate the pathways that may mediate prolidase induction by NO, we first used 8-Br-cGMP, a cGMP agonist, and found that 8-Br-cGMP strongly and rapidly stimulated prolidase activity accompanied by increased phosphorylation.	8-bromoguanosino-3',5'-cyclic monophosphorothioate	128-137	peptidase D	Homo sapiens	170-179
16167338-14	2005	Rp-8-Br-pCPT-cGMP, an inhibitor of cGMP, reduced NO donor-stimulated prolidase activity to control levels.	rp-8-br-pcpt-cgmp	0-17	peptidase D	Homo sapiens	69-78
16167338-14	2005	Rp-8-Br-pCPT-cGMP, an inhibitor of cGMP, reduced NO donor-stimulated prolidase activity to control levels.	Cyclic GMP	13-17	peptidase D	Homo sapiens	69-78
16167338-16	2005	These results demonstrate that NO stimulates prolidase activity by increasing serine/threonine phosphorylation through PKG-cGMP pathway, but independent of MAPK and suggest an interaction between inflammatory signaling pathways and regulation of the terminal step of matrix degradation.	Serine	78-84	peptidase D	Homo sapiens	45-54
16167338-16	2005	These results demonstrate that NO stimulates prolidase activity by increasing serine/threonine phosphorylation through PKG-cGMP pathway, but independent of MAPK and suggest an interaction between inflammatory signaling pathways and regulation of the terminal step of matrix degradation.	Threonine	85-94	peptidase D	Homo sapiens	45-54
15878628-0	2005	N-benzyloxycarbonyl-L-proline: an in vitro and in vivo inhibitor of prolidase.	carbobenzoxyproline	0-29	peptidase D	Homo sapiens	68-77
15878628-1	2005	Prolidase deficiency (PD) is a recessive disorder of the connective tissue caused by mutations in the prolidase, a specific peptidase, cleaving the dipeptides with a C-terminal prolyl and hydroxyprolyl residue.	Dipeptides	148-158	peptidase D	Homo sapiens	102-111
15878628-4	2005	We studied the effect of a prolidase inhibitor, N-benzyloxycarbonyl-l-proline (Cbz-Pro), in vitro on prolidase from human fibroblasts and in vivo on murine erythrocytes prolidase.	carbobenzoxyproline	48-77	peptidase D	Homo sapiens	27-36
15878628-4	2005	We studied the effect of a prolidase inhibitor, N-benzyloxycarbonyl-l-proline (Cbz-Pro), in vitro on prolidase from human fibroblasts and in vivo on murine erythrocytes prolidase.	carbobenzoxyproline	48-77	peptidase D	Homo sapiens	101-110
15878628-4	2005	We studied the effect of a prolidase inhibitor, N-benzyloxycarbonyl-l-proline (Cbz-Pro), in vitro on prolidase from human fibroblasts and in vivo on murine erythrocytes prolidase.	carbobenzoxyproline	79-86	peptidase D	Homo sapiens	27-36
15878628-4	2005	We studied the effect of a prolidase inhibitor, N-benzyloxycarbonyl-l-proline (Cbz-Pro), in vitro on prolidase from human fibroblasts and in vivo on murine erythrocytes prolidase.	carbobenzoxyproline	79-86	peptidase D	Homo sapiens	101-110
15878628-10	2005	Our results demonstrated that Cbz-Pro is a potent inhibitor of prolidase in cultured fibroblasts and it can be used in vivo to better characterize the prolidase enzyme and further investigate PD physiopathology.	carbobenzoxyproline	30-37	peptidase D	Homo sapiens	63-72
15878628-10	2005	Our results demonstrated that Cbz-Pro is a potent inhibitor of prolidase in cultured fibroblasts and it can be used in vivo to better characterize the prolidase enzyme and further investigate PD physiopathology.	carbobenzoxyproline	30-37	peptidase D	Homo sapiens	151-160
16167338-16	2005	These results demonstrate that NO stimulates prolidase activity by increasing serine/threonine phosphorylation through PKG-cGMP pathway, but independent of MAPK and suggest an interaction between inflammatory signaling pathways and regulation of the terminal step of matrix degradation.	Cyclic GMP	123-127	peptidase D	Homo sapiens	45-54
21783632-6	2005	We considered prolidase as a potential target for nickel-dependent collagen biosynthesis regulation.	Nickel	50-56	peptidase D	Homo sapiens	14-23
21783632-7	2005	Prolidase [E.C.3.4.13.9] is a cytosolic metalloproteinase, which specifically splits imidodipeptides with C-terminal proline that is recycled for collagen biosynthesis.	Proline	117-124	peptidase D	Homo sapiens	0-9
21783632-9	2005	An addition of acetylsalicylic acid, known, non-specific inhibitor of prolidase to the cells treated with 100muM NiCl(II), significantly reduced both collagen biosynthesis and prolidase activity.	Aspirin	15-35	peptidase D	Homo sapiens	70-79
21783632-9	2005	An addition of acetylsalicylic acid, known, non-specific inhibitor of prolidase to the cells treated with 100muM NiCl(II), significantly reduced both collagen biosynthesis and prolidase activity.	Aspirin	15-35	peptidase D	Homo sapiens	176-185
21783632-10	2005	It suggests that acetylsalicylic acid prevents nickel-induced increase in collagen biosynthesis through inhibition of prolidase activity in human fibroblasts.	Aspirin	17-37	peptidase D	Homo sapiens	118-127
21783632-10	2005	It suggests that acetylsalicylic acid prevents nickel-induced increase in collagen biosynthesis through inhibition of prolidase activity in human fibroblasts.	Nickel	47-53	peptidase D	Homo sapiens	118-127
16009141-4	2005	RESULTS: The activities of prolidase I and II against glycylproline and methionylproline were enhanced by glycine, L- and D-isoforms of alanine and serine and D-isoforms of valine, leucine and isoleucine.	glycylproline	54-67	peptidase D	Homo sapiens	27-36
16009141-4	2005	RESULTS: The activities of prolidase I and II against glycylproline and methionylproline were enhanced by glycine, L- and D-isoforms of alanine and serine and D-isoforms of valine, leucine and isoleucine.	H-Met-Pro-OH	72-88	peptidase D	Homo sapiens	27-36
16009141-4	2005	RESULTS: The activities of prolidase I and II against glycylproline and methionylproline were enhanced by glycine, L- and D-isoforms of alanine and serine and D-isoforms of valine, leucine and isoleucine.	Glycine	106-113	peptidase D	Homo sapiens	27-36
16009141-4	2005	RESULTS: The activities of prolidase I and II against glycylproline and methionylproline were enhanced by glycine, L- and D-isoforms of alanine and serine and D-isoforms of valine, leucine and isoleucine.	Alanine	136-143	peptidase D	Homo sapiens	27-36
16009141-4	2005	RESULTS: The activities of prolidase I and II against glycylproline and methionylproline were enhanced by glycine, L- and D-isoforms of alanine and serine and D-isoforms of valine, leucine and isoleucine.	Serine	148-154	peptidase D	Homo sapiens	27-36
16009141-4	2005	RESULTS: The activities of prolidase I and II against glycylproline and methionylproline were enhanced by glycine, L- and D-isoforms of alanine and serine and D-isoforms of valine, leucine and isoleucine.	Valine	173-179	peptidase D	Homo sapiens	27-36
16009141-4	2005	RESULTS: The activities of prolidase I and II against glycylproline and methionylproline were enhanced by glycine, L- and D-isoforms of alanine and serine and D-isoforms of valine, leucine and isoleucine.	Leucine	181-188	peptidase D	Homo sapiens	27-36
16009141-4	2005	RESULTS: The activities of prolidase I and II against glycylproline and methionylproline were enhanced by glycine, L- and D-isoforms of alanine and serine and D-isoforms of valine, leucine and isoleucine.	Isoleucine	193-203	peptidase D	Homo sapiens	27-36
16009141-5	2005	L-isoforms of branched amino acids inhibited the activity of prolidase I.	branched amino acids	14-34	peptidase D	Homo sapiens	61-70
16009141-6	2005	On the other hand, the activity of prolidase II was enhanced by all of these L-branched amino acids.	l-branched amino acids	77-99	peptidase D	Homo sapiens	35-44
16009141-7	2005	The patient"s prolidase activity was also enhanced by all the L- and D-branched amino acids.	l- and d-branched amino acids	62-91	peptidase D	Homo sapiens	14-23
16009141-8	2005	CONCLUSION: The activities of prolidase I and II against various iminodipeptides were prominently enhanced by glycine, but the effect of L-valine differed between the two enzymes.	Glycine	110-117	peptidase D	Homo sapiens	30-39
16009141-8	2005	CONCLUSION: The activities of prolidase I and II against various iminodipeptides were prominently enhanced by glycine, but the effect of L-valine differed between the two enzymes.	Valine	137-145	peptidase D	Homo sapiens	30-39
21783578-3	2005	Increased ability of AB(1) to suppress the protein synthesis, compared to chlorambucil, was found to be related to an inhibition of prolidase activity and expression.	Chlorambucil	74-86	peptidase D	Homo sapiens	132-141
15902422-1	2005	The recombinant human liver prolidase (rh-prolidase, EC 3.4.13.9) from the lysate supernatant of engineering yeast Saccharomyces cerevisiae was purified in two steps employing anion-exchange gradient chromatography (DEAE-Sepharose fast flow) and gel filtration chromatography (Sephacryl S-200 high resolution).	deae-sepharose	216-230	peptidase D	Homo sapiens	28-37
15902422-1	2005	The recombinant human liver prolidase (rh-prolidase, EC 3.4.13.9) from the lysate supernatant of engineering yeast Saccharomyces cerevisiae was purified in two steps employing anion-exchange gradient chromatography (DEAE-Sepharose fast flow) and gel filtration chromatography (Sephacryl S-200 high resolution).	deae-sepharose	216-230	peptidase D	Homo sapiens	42-51
15902422-1	2005	The recombinant human liver prolidase (rh-prolidase, EC 3.4.13.9) from the lysate supernatant of engineering yeast Saccharomyces cerevisiae was purified in two steps employing anion-exchange gradient chromatography (DEAE-Sepharose fast flow) and gel filtration chromatography (Sephacryl S-200 high resolution).	sephacryl s	277-288	peptidase D	Homo sapiens	28-37
15902422-1	2005	The recombinant human liver prolidase (rh-prolidase, EC 3.4.13.9) from the lysate supernatant of engineering yeast Saccharomyces cerevisiae was purified in two steps employing anion-exchange gradient chromatography (DEAE-Sepharose fast flow) and gel filtration chromatography (Sephacryl S-200 high resolution).	sephacryl s	277-288	peptidase D	Homo sapiens	42-51
15902422-3	2005	Intensity scanning of the SDS-PAGE gel revealed that the prolidase accounted for more than 90% of total protein.	Sodium Dodecyl Sulfate	26-29	peptidase D	Homo sapiens	57-66
15530480-3	2004	Effects of various amino acids and their metabolites on prolidase activity against iminodipeptides in presence of 1 mmol/l MnCl(2) were investigated.	manganese chloride	123-130	peptidase D	Homo sapiens	56-65
15804176-0	2005	Prolidase, a potential enzyme target for melanoma: design of proline-containing dipeptide-like prodrugs.	Proline	61-68	peptidase D	Homo sapiens	0-9
15804176-0	2005	Prolidase, a potential enzyme target for melanoma: design of proline-containing dipeptide-like prodrugs.	Dipeptides	80-89	peptidase D	Homo sapiens	0-9
15804176-2	2005	The analyses indicated that prolidase might be a desirable enzyme target based on its differential expression in melanoma cancer cell lines and its high substrate specificity for dipeptides containing proline at the carboxy terminus.	Dipeptides	179-189	peptidase D	Homo sapiens	28-37
15804176-2	2005	The analyses indicated that prolidase might be a desirable enzyme target based on its differential expression in melanoma cancer cell lines and its high substrate specificity for dipeptides containing proline at the carboxy terminus.	Proline	201-208	peptidase D	Homo sapiens	28-37
15804176-3	2005	RT-PCR expression of prolidase and hydrolytic activity against N-glycyl-l-proline (GLY-PRO), a standard substrate of prolidase, determined in tumor cell lines, exhibited a high correlation (r(2) = 0.95).	glycylproline	63-81	peptidase D	Homo sapiens	21-30
15804176-3	2005	RT-PCR expression of prolidase and hydrolytic activity against N-glycyl-l-proline (GLY-PRO), a standard substrate of prolidase, determined in tumor cell lines, exhibited a high correlation (r(2) = 0.95).	glycylproline	63-81	peptidase D	Homo sapiens	117-126
15804176-3	2005	RT-PCR expression of prolidase and hydrolytic activity against N-glycyl-l-proline (GLY-PRO), a standard substrate of prolidase, determined in tumor cell lines, exhibited a high correlation (r(2) = 0.95).	glycylproline	83-90	peptidase D	Homo sapiens	21-30
15804176-3	2005	RT-PCR expression of prolidase and hydrolytic activity against N-glycyl-l-proline (GLY-PRO), a standard substrate of prolidase, determined in tumor cell lines, exhibited a high correlation (r(2) = 0.95).	glycylproline	83-90	peptidase D	Homo sapiens	117-126
15804176-5	2005	The feasibility of such a scenario was tested by (a) synthesizing prodrugs of melphalan that comprised linkage of the carboxy terminus of the l-phenylalanine moiety of melphalan to the N-terminus of l and d stereoisomers of proline and (b) determining their bioconversion and antiproliferative activities in SK-MEL-5 cells, a melanoma cancer cell line with high expression levels of prolidase.	Phenylalanine	142-157	peptidase D	Homo sapiens	383-392
15530480-8	2004	CONCLUSION: Prolidase activity against glycylproline in normal human erythrocytes and against methionylproline from the prolidase-deficient patient was enhanced strongly by glycine, alanine and serine with MnCl(2).	mncl	206-210	peptidase D	Homo sapiens	120-129
15530480-4	2004	RESULTS: Prolidase activity against glycylproline in erythrocytes from normal human was strongly enhanced by glycine, L-alanine, L-serine with MnCl(2), but the activity was strongly inhibited by L-valine, and L-leucine.	glycylproline	36-49	peptidase D	Homo sapiens	9-18
15530480-4	2004	RESULTS: Prolidase activity against glycylproline in erythrocytes from normal human was strongly enhanced by glycine, L-alanine, L-serine with MnCl(2), but the activity was strongly inhibited by L-valine, and L-leucine.	Glycine	109-116	peptidase D	Homo sapiens	9-18
15530480-4	2004	RESULTS: Prolidase activity against glycylproline in erythrocytes from normal human was strongly enhanced by glycine, L-alanine, L-serine with MnCl(2), but the activity was strongly inhibited by L-valine, and L-leucine.	Alanine	118-127	peptidase D	Homo sapiens	9-18
15530480-4	2004	RESULTS: Prolidase activity against glycylproline in erythrocytes from normal human was strongly enhanced by glycine, L-alanine, L-serine with MnCl(2), but the activity was strongly inhibited by L-valine, and L-leucine.	Serine	129-137	peptidase D	Homo sapiens	9-18
15530480-4	2004	RESULTS: Prolidase activity against glycylproline in erythrocytes from normal human was strongly enhanced by glycine, L-alanine, L-serine with MnCl(2), but the activity was strongly inhibited by L-valine, and L-leucine.	mncl	143-147	peptidase D	Homo sapiens	9-18
15530480-4	2004	RESULTS: Prolidase activity against glycylproline in erythrocytes from normal human was strongly enhanced by glycine, L-alanine, L-serine with MnCl(2), but the activity was strongly inhibited by L-valine, and L-leucine.	Valine	195-203	peptidase D	Homo sapiens	9-18
15530480-4	2004	RESULTS: Prolidase activity against glycylproline in erythrocytes from normal human was strongly enhanced by glycine, L-alanine, L-serine with MnCl(2), but the activity was strongly inhibited by L-valine, and L-leucine.	Leucine	209-218	peptidase D	Homo sapiens	9-18
15530480-6	2004	The prolidase activity against methionylproline in erythrocytes from the patient with prolidase deficiency was also enhanced by glycine, L-alanine and L-serine.	H-Met-Pro-OH	31-47	peptidase D	Homo sapiens	4-13
15530480-6	2004	The prolidase activity against methionylproline in erythrocytes from the patient with prolidase deficiency was also enhanced by glycine, L-alanine and L-serine.	Glycine	128-135	peptidase D	Homo sapiens	4-13
15530480-6	2004	The prolidase activity against methionylproline in erythrocytes from the patient with prolidase deficiency was also enhanced by glycine, L-alanine and L-serine.	Alanine	137-146	peptidase D	Homo sapiens	4-13
15530480-6	2004	The prolidase activity against methionylproline in erythrocytes from the patient with prolidase deficiency was also enhanced by glycine, L-alanine and L-serine.	Serine	151-159	peptidase D	Homo sapiens	4-13
15530480-8	2004	CONCLUSION: Prolidase activity against glycylproline in normal human erythrocytes and against methionylproline from the prolidase-deficient patient was enhanced strongly by glycine, alanine and serine with MnCl(2).	glycylproline	39-52	peptidase D	Homo sapiens	12-21
15530480-8	2004	CONCLUSION: Prolidase activity against glycylproline in normal human erythrocytes and against methionylproline from the prolidase-deficient patient was enhanced strongly by glycine, alanine and serine with MnCl(2).	glycylproline	39-52	peptidase D	Homo sapiens	120-129
15530480-8	2004	CONCLUSION: Prolidase activity against glycylproline in normal human erythrocytes and against methionylproline from the prolidase-deficient patient was enhanced strongly by glycine, alanine and serine with MnCl(2).	H-Met-Pro-OH	94-110	peptidase D	Homo sapiens	12-21
15530480-8	2004	CONCLUSION: Prolidase activity against glycylproline in normal human erythrocytes and against methionylproline from the prolidase-deficient patient was enhanced strongly by glycine, alanine and serine with MnCl(2).	H-Met-Pro-OH	94-110	peptidase D	Homo sapiens	120-129
15530480-8	2004	CONCLUSION: Prolidase activity against glycylproline in normal human erythrocytes and against methionylproline from the prolidase-deficient patient was enhanced strongly by glycine, alanine and serine with MnCl(2).	Glycine	173-180	peptidase D	Homo sapiens	12-21
15530480-8	2004	CONCLUSION: Prolidase activity against glycylproline in normal human erythrocytes and against methionylproline from the prolidase-deficient patient was enhanced strongly by glycine, alanine and serine with MnCl(2).	Glycine	173-180	peptidase D	Homo sapiens	120-129
15530480-8	2004	CONCLUSION: Prolidase activity against glycylproline in normal human erythrocytes and against methionylproline from the prolidase-deficient patient was enhanced strongly by glycine, alanine and serine with MnCl(2).	Alanine	182-189	peptidase D	Homo sapiens	12-21
15530480-8	2004	CONCLUSION: Prolidase activity against glycylproline in normal human erythrocytes and against methionylproline from the prolidase-deficient patient was enhanced strongly by glycine, alanine and serine with MnCl(2).	Alanine	182-189	peptidase D	Homo sapiens	120-129
15530480-8	2004	CONCLUSION: Prolidase activity against glycylproline in normal human erythrocytes and against methionylproline from the prolidase-deficient patient was enhanced strongly by glycine, alanine and serine with MnCl(2).	Serine	194-200	peptidase D	Homo sapiens	12-21
15530480-8	2004	CONCLUSION: Prolidase activity against glycylproline in normal human erythrocytes and against methionylproline from the prolidase-deficient patient was enhanced strongly by glycine, alanine and serine with MnCl(2).	Serine	194-200	peptidase D	Homo sapiens	120-129
15530480-8	2004	CONCLUSION: Prolidase activity against glycylproline in normal human erythrocytes and against methionylproline from the prolidase-deficient patient was enhanced strongly by glycine, alanine and serine with MnCl(2).	mncl	206-210	peptidase D	Homo sapiens	12-21
15337432-2	2004	In order to limit the action of prolidase on the pro-drug in normal cells, prolidase inhibitor, acetylsalicylic acid (ASA), was tested in fibroblasts (showing average prolidase activity for normal cells) and in MDA-MB 231 breast cancer cells (showing elevated activity of the enzyme).	Aspirin	118-121	peptidase D	Homo sapiens	75-84
15337432-0	2004	Acetylsalicylic acid as a potential regulator of prolidase-convertible pro-drugs in control and neoplastic cells.	Aspirin	0-20	peptidase D	Homo sapiens	49-58
15337432-2	2004	In order to limit the action of prolidase on the pro-drug in normal cells, prolidase inhibitor, acetylsalicylic acid (ASA), was tested in fibroblasts (showing average prolidase activity for normal cells) and in MDA-MB 231 breast cancer cells (showing elevated activity of the enzyme).	Aspirin	118-121	peptidase D	Homo sapiens	75-84
15337432-1	2004	Proline analogue of melphalan (Mel-pro) is one of the pro-drugs activated by prolidase, cytoplasmic imidodipeptidase highly expressed in some neoplastic tissues.	Proline	0-7	peptidase D	Homo sapiens	77-86
15337432-6	2004	It suggests that ASA may serve as an inhibitor of prolidase-convertible pro-drugs in normal cells.	Aspirin	17-20	peptidase D	Homo sapiens	50-59
15337432-2	2004	In order to limit the action of prolidase on the pro-drug in normal cells, prolidase inhibitor, acetylsalicylic acid (ASA), was tested in fibroblasts (showing average prolidase activity for normal cells) and in MDA-MB 231 breast cancer cells (showing elevated activity of the enzyme).	Aspirin	96-116	peptidase D	Homo sapiens	75-84
15337432-2	2004	In order to limit the action of prolidase on the pro-drug in normal cells, prolidase inhibitor, acetylsalicylic acid (ASA), was tested in fibroblasts (showing average prolidase activity for normal cells) and in MDA-MB 231 breast cancer cells (showing elevated activity of the enzyme).	Aspirin	96-116	peptidase D	Homo sapiens	75-84
15265726-1	2004	Proline-containing peptides of the X-proline type are cleaved by the dipeptidase prolidase.	Proline	0-7	peptidase D	Homo sapiens	81-90
15265726-1	2004	Proline-containing peptides of the X-proline type are cleaved by the dipeptidase prolidase.	x-proline	35-44	peptidase D	Homo sapiens	81-90
15265726-2	2004	The classical method of prolidase assay relied on the colorimetric estimation of the liberated proline with ninhydrin using acidic media and heat.	Ninhydrin	108-117	peptidase D	Homo sapiens	24-33
15265726-2	2004	The classical method of prolidase assay relied on the colorimetric estimation of the liberated proline with ninhydrin using acidic media and heat.	Proline	95-102	peptidase D	Homo sapiens	24-33
15173663-2	2004	The mechanism of their action on collagen biosynthesis involves inactivation of prolidase, the enzyme that recovers proline from collagen degradation products for collagen re-synthesis.	Proline	116-123	peptidase D	Homo sapiens	80-89
15173663-6	2004	RESULTS: In cells treated with acetylsalicylic acid, a concomitant decrease in prolidase activity, prolidase phosphorylation (at the threonine residue), and collagen biosynthesis were observed.	Aspirin	31-51	peptidase D	Homo sapiens	79-88
15552267-4	2004	The same studies on erythrocytes from a prolidase-deficient patient showed almost the same results as the normal control, except that prolinase activity against pro-gly and pro-ser was slightly inhibited by adding 0.1 mM MnCl2.	manganese chloride	221-226	peptidase D	Homo sapiens	40-49
15173663-6	2004	RESULTS: In cells treated with acetylsalicylic acid, a concomitant decrease in prolidase activity, prolidase phosphorylation (at the threonine residue), and collagen biosynthesis were observed.	Aspirin	31-51	peptidase D	Homo sapiens	99-108
15173663-6	2004	RESULTS: In cells treated with acetylsalicylic acid, a concomitant decrease in prolidase activity, prolidase phosphorylation (at the threonine residue), and collagen biosynthesis were observed.	Threonine	133-142	peptidase D	Homo sapiens	99-108
15173663-8	2004	This suggests that a decrease in prolidase activity may contribute to a decrease in the biosynthesis of proline-containing proteins, such as collagen and SOS.	Proline	104-111	peptidase D	Homo sapiens	33-42
15173663-10	2004	CONCLUSIONS: The inhibitory effect of acetylsalicylic acid on collagen biosynthesis in fibroblasts is coupled to the inhibition of prolidase phosphorylation (but not expression) and down-regulation of the intracellular signal transmitted by the b1-integrin receptor.	Aspirin	38-58	peptidase D	Homo sapiens	131-140
15178351-3	2004	The greater potency of AB(1) to suppress collagen synthesis was found to be accompanied by a stronger compared with chlorambucil inhibition of prolidase activity and expression.	Chlorambucil	116-128	peptidase D	Homo sapiens	143-152
15552267-5	2004	Some amino acids, glutamic acid and glutamine, slightly enhanced prolinase activity against pro-gly in erythrocytes from both the normal control and the prolidase-deficient patient, but N-acetyl-L-glutamic acid, gamma-aminobutyric acid (GABA) and beta-alanine showed no effect.	Glutamine	36-45	peptidase D	Homo sapiens	153-162
15142336-6	2004	The microparticulate drug delivery system described carried small amounts of active prolidase inside fibroblasts, ensuring a response to the intracellular accumulation of X-Pro dipeptides, the mechanism that is supposed to be responsible for the development of clinical manifestations of this disorder in man.	x-pro	171-176	peptidase D	Homo sapiens	84-93
15142336-6	2004	The microparticulate drug delivery system described carried small amounts of active prolidase inside fibroblasts, ensuring a response to the intracellular accumulation of X-Pro dipeptides, the mechanism that is supposed to be responsible for the development of clinical manifestations of this disorder in man.	Dipeptides	177-187	peptidase D	Homo sapiens	84-93
15552267-5	2004	Some amino acids, glutamic acid and glutamine, slightly enhanced prolinase activity against pro-gly in erythrocytes from both the normal control and the prolidase-deficient patient, but N-acetyl-L-glutamic acid, gamma-aminobutyric acid (GABA) and beta-alanine showed no effect.	Glutamic Acid	18-31	peptidase D	Homo sapiens	153-162
14572862-2	2003	Conjugation of melphalan (Mel) with proline (Pro) through imido-bond resulted in formation of a good substrate for prolidase.	Proline	36-43	peptidase D	Homo sapiens	115-124
14572862-2	2003	Conjugation of melphalan (Mel) with proline (Pro) through imido-bond resulted in formation of a good substrate for prolidase.	Proline	45-48	peptidase D	Homo sapiens	115-124
14572862-0	2003	Proline analogue of melphalan as a prodrug susceptible to the action of prolidase in breast cancer MDA-MB 231 cells.	Proline	0-7	peptidase D	Homo sapiens	72-81
14572862-3	2003	Cytosolic location of prolidase in neoplastic cell suggests that proline analogue of melphalan (Mel-pro) may serve as a prolidase convertible prodrug.	Proline	65-72	peptidase D	Homo sapiens	22-31
14572862-0	2003	Proline analogue of melphalan as a prodrug susceptible to the action of prolidase in breast cancer MDA-MB 231 cells.	Melphalan	20-29	peptidase D	Homo sapiens	72-81
14572862-3	2003	Cytosolic location of prolidase in neoplastic cell suggests that proline analogue of melphalan (Mel-pro) may serve as a prolidase convertible prodrug.	Proline	65-72	peptidase D	Homo sapiens	120-129
14572862-1	2003	Proline analogue of melphalan (Mel-pro) was synthesized as a prodrug susceptible to the action of ubiquitously distributed, cytosolic imidodipeptidase-prolidase [E.C.3.4.13.9].	Proline	0-7	peptidase D	Homo sapiens	151-160
14572862-1	2003	Proline analogue of melphalan (Mel-pro) was synthesized as a prodrug susceptible to the action of ubiquitously distributed, cytosolic imidodipeptidase-prolidase [E.C.3.4.13.9].	Melphalan	20-29	peptidase D	Homo sapiens	151-160
14572862-1	2003	Proline analogue of melphalan (Mel-pro) was synthesized as a prodrug susceptible to the action of ubiquitously distributed, cytosolic imidodipeptidase-prolidase [E.C.3.4.13.9].	mel-pro	31-38	peptidase D	Homo sapiens	151-160
14572862-2	2003	Conjugation of melphalan (Mel) with proline (Pro) through imido-bond resulted in formation of a good substrate for prolidase.	Melphalan	15-24	peptidase D	Homo sapiens	115-124
14580160-3	2003	Normal prolidase II was very labile in the absence of MnCl2 or mercaptoethanol.	manganese chloride	54-59	peptidase D	Homo sapiens	7-16
14533013-8	2003	Increase of collagen synthesis induced by raloxifene may be activated by both estrogen receptor dependent and independent pathways such as up-regulation of estrogen receptors, up-regulation of IGF receptor, transcriptional regulation of collagen genes by estrogen receptor-raloxifene complex, increasing of prolidase activity or finally by inhibition of MMP-9 expression.	Raloxifene Hydrochloride	42-52	peptidase D	Homo sapiens	307-316
14580160-4	2003	The activity of prolidase II was maintained at about 76% by pre-incubation with MnCl2; it was then activated up to 140% by treatment with mercaptoethanol for 60 minutes at 37 degrees C. Normal prolidases I and II showed the highest activity against glycylproline or methionylproline in the presence of MnCl2.	manganese chloride	80-85	peptidase D	Homo sapiens	16-25
14580160-4	2003	The activity of prolidase II was maintained at about 76% by pre-incubation with MnCl2; it was then activated up to 140% by treatment with mercaptoethanol for 60 minutes at 37 degrees C. Normal prolidases I and II showed the highest activity against glycylproline or methionylproline in the presence of MnCl2.	Mercaptoethanol	138-153	peptidase D	Homo sapiens	16-25
14580160-4	2003	The activity of prolidase II was maintained at about 76% by pre-incubation with MnCl2; it was then activated up to 140% by treatment with mercaptoethanol for 60 minutes at 37 degrees C. Normal prolidases I and II showed the highest activity against glycylproline or methionylproline in the presence of MnCl2.	glycylproline	249-262	peptidase D	Homo sapiens	16-25
14580160-4	2003	The activity of prolidase II was maintained at about 76% by pre-incubation with MnCl2; it was then activated up to 140% by treatment with mercaptoethanol for 60 minutes at 37 degrees C. Normal prolidases I and II showed the highest activity against glycylproline or methionylproline in the presence of MnCl2.	H-Met-Pro-OH	266-282	peptidase D	Homo sapiens	16-25
14580160-4	2003	The activity of prolidase II was maintained at about 76% by pre-incubation with MnCl2; it was then activated up to 140% by treatment with mercaptoethanol for 60 minutes at 37 degrees C. Normal prolidases I and II showed the highest activity against glycylproline or methionylproline in the presence of MnCl2.	manganese chloride	302-307	peptidase D	Homo sapiens	16-25
14580160-5	2003	The activity of prolidase I against glycylproline was enhanced strongly by glycine and MnCl2, but not activated in the absence of MnCl2.	glycylproline	36-49	peptidase D	Homo sapiens	16-25
14580160-5	2003	The activity of prolidase I against glycylproline was enhanced strongly by glycine and MnCl2, but not activated in the absence of MnCl2.	Glycine	75-82	peptidase D	Homo sapiens	16-25
14580160-5	2003	The activity of prolidase I against glycylproline was enhanced strongly by glycine and MnCl2, but not activated in the absence of MnCl2.	manganese chloride	87-92	peptidase D	Homo sapiens	16-25
14580160-6	2003	The activity of prolidase II against methionylproline was enhanced three-fold in the presence of glycine and MnCl2, but its activity against glycylproline was very low even in the presence of MnCl2.	H-Met-Pro-OH	37-53	peptidase D	Homo sapiens	16-25
14580160-6	2003	The activity of prolidase II against methionylproline was enhanced three-fold in the presence of glycine and MnCl2, but its activity against glycylproline was very low even in the presence of MnCl2.	Glycine	97-104	peptidase D	Homo sapiens	16-25
14580160-6	2003	The activity of prolidase II against methionylproline was enhanced three-fold in the presence of glycine and MnCl2, but its activity against glycylproline was very low even in the presence of MnCl2.	manganese chloride	109-114	peptidase D	Homo sapiens	16-25
14580160-6	2003	The activity of prolidase II against methionylproline was enhanced three-fold in the presence of glycine and MnCl2, but its activity against glycylproline was very low even in the presence of MnCl2.	glycylproline	141-154	peptidase D	Homo sapiens	16-25
14580160-6	2003	The activity of prolidase II against methionylproline was enhanced three-fold in the presence of glycine and MnCl2, but its activity against glycylproline was very low even in the presence of MnCl2.	manganese chloride	192-197	peptidase D	Homo sapiens	16-25
14580160-8	2003	The activity of prolidase II against methionylproline in all erythrocytes, of normal humans and of patients, was strongly activated by the addition of glycine with MnCl2 but suppressed by the addition of mercaptoethanol.	H-Met-Pro-OH	37-53	peptidase D	Homo sapiens	16-25
14580160-8	2003	The activity of prolidase II against methionylproline in all erythrocytes, of normal humans and of patients, was strongly activated by the addition of glycine with MnCl2 but suppressed by the addition of mercaptoethanol.	Glycine	151-158	peptidase D	Homo sapiens	16-25
14580160-8	2003	The activity of prolidase II against methionylproline in all erythrocytes, of normal humans and of patients, was strongly activated by the addition of glycine with MnCl2 but suppressed by the addition of mercaptoethanol.	manganese chloride	164-169	peptidase D	Homo sapiens	16-25
14580160-8	2003	The activity of prolidase II against methionylproline in all erythrocytes, of normal humans and of patients, was strongly activated by the addition of glycine with MnCl2 but suppressed by the addition of mercaptoethanol.	Mercaptoethanol	204-219	peptidase D	Homo sapiens	16-25
11698059-0	2001	Doxycycline-induced inhibition of prolidase activity in human skin fibroblasts and its involvement in impaired collagen biosynthesis.	Doxycycline	0-11	peptidase D	Homo sapiens	34-43
11733096-5	2001	The poly(D,L-lactide-co-glycolide) (PLGA) prolidase loaded microparticulate systems have been prepared utilizing the w-o-w double emulsion solvent evaporation method.	Polylactic Acid-Polyglycolic Acid Copolymer	4-34	peptidase D	Homo sapiens	42-51
11733096-5	2001	The poly(D,L-lactide-co-glycolide) (PLGA) prolidase loaded microparticulate systems have been prepared utilizing the w-o-w double emulsion solvent evaporation method.	w-o-w	117-122	peptidase D	Homo sapiens	42-51
12433302-1	2002	This work was aimed at studying enzyme prolidase stability and its interactions with the reagents and the process conditions involved in preparation, by an emulsification process, of prolidase loaded poly(lactide-co-glycolide) (PLGA) microparticulate systems.	Polyglactin 910	200-226	peptidase D	Homo sapiens	183-192
12433302-5	2002	The results obtained showed that the prolidase-loaded PLGA microspheres can be prepared only upon enzyme stabilization by addition of both BSA and MnCl(2) into its TRIS solution.	manganese chloride	147-154	peptidase D	Homo sapiens	37-46
12433302-5	2002	The results obtained showed that the prolidase-loaded PLGA microspheres can be prepared only upon enzyme stabilization by addition of both BSA and MnCl(2) into its TRIS solution.	Tromethamine	164-168	peptidase D	Homo sapiens	37-46
12098580-8	2002	We have suggested that prolidase, an enzyme involved in collagen metabolism, may be one of the targets for gentamicin-induced inhibition of collagen biosynthesis.	Gentamicins	107-117	peptidase D	Homo sapiens	23-32
12098580-9	2002	We found that gentamicin-induced inhibition of prolidase activity (IC(50) approximately 100 microM) and collagen biosynthesis (IC(50) approximately 100 microM).	Gentamicins	14-24	peptidase D	Homo sapiens	47-56
12098580-11	2002	Melanin at 100 microg/ml produced about 25% inhibition of DNA synthesis and about 30% inhibition of prolidase activity, but it had no effect on collagen biosynthesis in cultured fibroblasts.	Melanins	0-7	peptidase D	Homo sapiens	100-109
12098580-12	2002	However, the addition of melanin (100 microg/ml) to gentamicin-treated cells (100 microM) augmented the inhibitory action of gentamicin on collagen and DNA biosynthesis and partially reversed its inhibitory effect on prolidase activity.	Melanins	25-32	peptidase D	Homo sapiens	217-226
12098580-12	2002	However, the addition of melanin (100 microg/ml) to gentamicin-treated cells (100 microM) augmented the inhibitory action of gentamicin on collagen and DNA biosynthesis and partially reversed its inhibitory effect on prolidase activity.	Gentamicins	52-62	peptidase D	Homo sapiens	217-226
11733182-10	2002	Prolidase activity was almost 3-fold lower in the preeclamptic extract (240.6+/-29.3 nmol Pro x min(-1) x mg(-1) protein) in comparison to the control (608.2+/-63.7 nmol Pro x min(-1) x mg(-1)protein).	Proline	90-93	peptidase D	Homo sapiens	0-9
11916317-9	2001	The characteristic resonances in the urine from a prolidase-deficient patient, i.e. Ala-Pro, Val-Pro, Gly-Pro, and resonances of the (hydroxy)proline part of the imidodipeptides can be used to diagnose this disease.	alanylproline	84-91	peptidase D	Homo sapiens	50-59
11916317-9	2001	The characteristic resonances in the urine from a prolidase-deficient patient, i.e. Ala-Pro, Val-Pro, Gly-Pro, and resonances of the (hydroxy)proline part of the imidodipeptides can be used to diagnose this disease.	L-valyl-L-proline	93-100	peptidase D	Homo sapiens	50-59
11916317-9	2001	The characteristic resonances in the urine from a prolidase-deficient patient, i.e. Ala-Pro, Val-Pro, Gly-Pro, and resonances of the (hydroxy)proline part of the imidodipeptides can be used to diagnose this disease.	Hydroxyproline	133-149	peptidase D	Homo sapiens	50-59
11698059-4	2001	We considered prolidase, an enzyme involved in collagen metabolism, as a possible target for the doxycycline-induced inhibition of collagen synthesis.	Doxycycline	97-108	peptidase D	Homo sapiens	14-23
11698059-10	2001	We found that doxycycline induced coordinately inhibition of prolidase activity and collagen biosynthesis (IC50 at about 150 microg/ml) and gelatinolytic activity in cultured human skin fibroblasts.	Doxycycline	14-25	peptidase D	Homo sapiens	61-70
11698059-13	2001	The decrease in prolidase activity in fibroblasts treated with doxycycline was not accompanied by any differences in the amount of prolidase or beta1 integrin recovered from these cells, as shown by Western immunoblot analysis.	Doxycycline	63-74	peptidase D	Homo sapiens	16-25
11698059-14	2001	This suggests that the doxycycline-induced down-regulation of prolidase is a post-translational event.	Doxycycline	23-34	peptidase D	Homo sapiens	62-71
11698059-15	2001	The data presented here raise the possibility that the doxycycline-induced decrease in collagen biosynthesis is mostly due to the inhibition of prolidase activity.	Doxycycline	55-66	peptidase D	Homo sapiens	144-153
11470441-8	2001	Since prolidase is known to be involved in collagen metabolism, the enzyme activity assay was performed in fibroblasts cultured in the presence of Gln, Glu and P5C.	Glutamine	147-150	peptidase D	Homo sapiens	6-15
11680815-0	2001	Cytotoxicity and effect on collagen biosynthesis of proline analogue of melphalan as a prolidase-convertible prodrug in cultured human skin fibroblasts.	Proline	52-59	peptidase D	Homo sapiens	87-96
11680815-1	2001	Proline analogue of melphalan (MEL-PRO) was synthesised as a prodrug susceptible to the action of ubiquitously distributed, cytosolic imidodipeptidase--prolidase [E.C.3.4.13.9].	Proline	0-7	peptidase D	Homo sapiens	152-161
11680815-1	2001	Proline analogue of melphalan (MEL-PRO) was synthesised as a prodrug susceptible to the action of ubiquitously distributed, cytosolic imidodipeptidase--prolidase [E.C.3.4.13.9].	Melphalan	20-29	peptidase D	Homo sapiens	152-161
11680815-1	2001	Proline analogue of melphalan (MEL-PRO) was synthesised as a prodrug susceptible to the action of ubiquitously distributed, cytosolic imidodipeptidase--prolidase [E.C.3.4.13.9].	mel-pro	31-38	peptidase D	Homo sapiens	152-161
11680815-2	2001	Conjugation of melphalan (MEL) with proline (PRO) through an imido-bond resulted in formation of a good substrate for prolidase.	Melphalan	15-24	peptidase D	Homo sapiens	118-127
11680815-2	2001	Conjugation of melphalan (MEL) with proline (PRO) through an imido-bond resulted in formation of a good substrate for prolidase.	Proline	36-43	peptidase D	Homo sapiens	118-127
11680815-2	2001	Conjugation of melphalan (MEL) with proline (PRO) through an imido-bond resulted in formation of a good substrate for prolidase.	Proline	45-48	peptidase D	Homo sapiens	118-127
11680815-3	2001	The susceptibility of MEL-PRO to the action of prolidase was found to be similar, compared to glycyl-proline--the most abundant, endogenous substrate for prolidase and about 6-fold higher compared to its substrate--glycyl-hydroxyproline.	mel-pro	22-29	peptidase D	Homo sapiens	47-56
11680815-3	2001	The susceptibility of MEL-PRO to the action of prolidase was found to be similar, compared to glycyl-proline--the most abundant, endogenous substrate for prolidase and about 6-fold higher compared to its substrate--glycyl-hydroxyproline.	glycylproline	94-108	peptidase D	Homo sapiens	154-163
11680815-3	2001	The susceptibility of MEL-PRO to the action of prolidase was found to be similar, compared to glycyl-proline--the most abundant, endogenous substrate for prolidase and about 6-fold higher compared to its substrate--glycyl-hydroxyproline.	glycyl-hydroxyproline	215-236	peptidase D	Homo sapiens	47-56
11680815-11	2001	The data suggest that MEL-PRO may serve as a prolidase-convertible prodrug that evokes lower cytotoxicity, antimitotic activity, and lower inhibitory effect on collagen biosynthesis in fibroblast cultures, compared to the free drug.	mel-pro	22-29	peptidase D	Homo sapiens	45-54
11470441-8	2001	Since prolidase is known to be involved in collagen metabolism, the enzyme activity assay was performed in fibroblasts cultured in the presence of Gln, Glu and P5C.	Glutamic Acid	152-155	peptidase D	Homo sapiens	6-15
11470441-8	2001	Since prolidase is known to be involved in collagen metabolism, the enzyme activity assay was performed in fibroblasts cultured in the presence of Gln, Glu and P5C.	delta-1-pyrroline-5-carboxylate	160-163	peptidase D	Homo sapiens	6-15
11470441-9	2001	While Gln and Glu required 24 h for maximal stimulation of prolidase activity, P5C induced it after 6-12 h. The data suggest that P5C induced collagen biosynthesis and prolidase activity in a shorter time than Gln and Glu.	delta-1-pyrroline-5-carboxylate	79-82	peptidase D	Homo sapiens	168-177
11470441-9	2001	While Gln and Glu required 24 h for maximal stimulation of prolidase activity, P5C induced it after 6-12 h. The data suggest that P5C induced collagen biosynthesis and prolidase activity in a shorter time than Gln and Glu.	delta-1-pyrroline-5-carboxylate	130-133	peptidase D	Homo sapiens	59-68
11470441-9	2001	While Gln and Glu required 24 h for maximal stimulation of prolidase activity, P5C induced it after 6-12 h. The data suggest that P5C induced collagen biosynthesis and prolidase activity in a shorter time than Gln and Glu.	delta-1-pyrroline-5-carboxylate	130-133	peptidase D	Homo sapiens	168-177
11470441-12	2001	We have found that dehydroepiandrosterone (DHEA), a potent inhibitor of G6P dehydrogenase, inhibited a stimulatory effect of P5C on collagen synthesis, expression of type I collagen and prolidase activity.	Dehydroepiandrosterone	19-41	peptidase D	Homo sapiens	186-195
11470441-12	2001	We have found that dehydroepiandrosterone (DHEA), a potent inhibitor of G6P dehydrogenase, inhibited a stimulatory effect of P5C on collagen synthesis, expression of type I collagen and prolidase activity.	Dehydroepiandrosterone	43-47	peptidase D	Homo sapiens	186-195
11470441-12	2001	We have found that dehydroepiandrosterone (DHEA), a potent inhibitor of G6P dehydrogenase, inhibited a stimulatory effect of P5C on collagen synthesis, expression of type I collagen and prolidase activity.	delta-1-pyrroline-5-carboxylate	125-128	peptidase D	Homo sapiens	186-195
11451388-1	2001	Prolidase [EC 3.4.13.9] is a ubiquitously distributed imidodipeptidase that catalyzes the hydrolysis of C-terminal proline-containing dipeptides.	Proline	115-122	peptidase D	Homo sapiens	0-9
11447735-3	2001	Raloxifene at concentrations of 1 microM and 4 microM inhibited collagen biosynthesis by about 10-fold and prolidase activity by about 50%, while at a concentration of 10 microM it inhibited these processes by only about 25%.	Raloxifene Hydrochloride	0-10	peptidase D	Homo sapiens	107-116
11447735-10	2001	The data raise the possibility that in estrogen-stimulated MCF-7 cells, raloxifene at low concentrations (1 and 4 microM) evokes antiestrogenic effect on collagen biosynthesis and prolidase activity on the one hand, and an estrogenic effect on gelatinolytic activity on the other, while at higher concentrations (about 10 microM) it evokes an estrogenic effect on collagen biosynthesis and prolidase activity, and an antiestrogenic effect on gelatinolytic activity.	Raloxifene Hydrochloride	72-82	peptidase D	Homo sapiens	180-189
11447735-10	2001	The data raise the possibility that in estrogen-stimulated MCF-7 cells, raloxifene at low concentrations (1 and 4 microM) evokes antiestrogenic effect on collagen biosynthesis and prolidase activity on the one hand, and an estrogenic effect on gelatinolytic activity on the other, while at higher concentrations (about 10 microM) it evokes an estrogenic effect on collagen biosynthesis and prolidase activity, and an antiestrogenic effect on gelatinolytic activity.	Raloxifene Hydrochloride	72-82	peptidase D	Homo sapiens	390-399
11447735-11	2001	Our data suggest that the effects of raloxifene on collagen synthesis, prolidase and metalloproteinase activities in breast cancer may explain its role in the prevention of breast cancer development.	Raloxifene Hydrochloride	37-47	peptidase D	Homo sapiens	71-80
11426835-8	2001	We have suggested that prolidase, an enzyme involved in collagen metabolism, may be one of the targets for anthracycline-induced inhibition of collagen synthesis.	Anthracyclines	107-120	peptidase D	Homo sapiens	23-32
11426835-9	2001	We found that daunorubicin induced inhibition of prolidase activity (IC50 = 10 microM), collagen biosynthesis (IC50 = 70 microM) and DNA biosynthesis (IC50= 10 microM) in human skin fibroblasts.	Daunorubicin	14-26	peptidase D	Homo sapiens	49-58
11426835-10	2001	Melanin (100 microg/ml) by itself produced about 25% inhibition of DNA synthesis and prolidase activity but it had no effect on collagen biosynthesis in cultured fibroblasts.	Melanins	0-7	peptidase D	Homo sapiens	85-94
11426835-11	2001	However, the addition of melanin (100 microg/ml) to daunorubicin-treated cells (at IC50 concentration) augmented the inhibitory action of daunorubicin on collagen and DNA biosynthesis without having any effect on prolidase activity.	Melanins	25-32	peptidase D	Homo sapiens	213-222
11451388-1	2001	Prolidase [EC 3.4.13.9] is a ubiquitously distributed imidodipeptidase that catalyzes the hydrolysis of C-terminal proline-containing dipeptides.	Proline	115-122	peptidase D	Homo sapiens	54-70
11451388-1	2001	Prolidase [EC 3.4.13.9] is a ubiquitously distributed imidodipeptidase that catalyzes the hydrolysis of C-terminal proline-containing dipeptides.	Dipeptides	134-144	peptidase D	Homo sapiens	0-9
11451388-1	2001	Prolidase [EC 3.4.13.9] is a ubiquitously distributed imidodipeptidase that catalyzes the hydrolysis of C-terminal proline-containing dipeptides.	Dipeptides	134-144	peptidase D	Homo sapiens	54-70
10965990-3	2000	We have suggested that prolidase, an enzyme involved in collagen metabolism may be one of the targets for anthracyclines-induced inhibition of synthesis of this protein.	Anthracyclines	106-120	peptidase D	Homo sapiens	23-32
11820612-3	2001	Cytosolic location of prolidase in neoplastic cells suggests that proline analogue of melphalan (Mel-pro) may serve as a prolidase convertable pro-drug.	Proline	66-73	peptidase D	Homo sapiens	121-130
11338665-0	2001	Decreased cytotoxicity and increased antimitotic activity of a proline analogue of chlorambucil as a prodrug susceptible to the action of fibroblast"s prolidase.	Proline	63-70	peptidase D	Homo sapiens	151-160
11338665-0	2001	Decreased cytotoxicity and increased antimitotic activity of a proline analogue of chlorambucil as a prodrug susceptible to the action of fibroblast"s prolidase.	Chlorambucil	83-95	peptidase D	Homo sapiens	151-160
11338665-1	2001	We synthesized an proline analogue of chlorambucil (CH-pro) as a prodrug susceptible to the action of ubiquitously distributed, cytosolic imidopeptidase--prolidase [E.C.3.4.13.9].	Proline	18-25	peptidase D	Homo sapiens	154-163
11338665-1	2001	We synthesized an proline analogue of chlorambucil (CH-pro) as a prodrug susceptible to the action of ubiquitously distributed, cytosolic imidopeptidase--prolidase [E.C.3.4.13.9].	Chlorambucil	38-50	peptidase D	Homo sapiens	154-163
11338665-1	2001	We synthesized an proline analogue of chlorambucil (CH-pro) as a prodrug susceptible to the action of ubiquitously distributed, cytosolic imidopeptidase--prolidase [E.C.3.4.13.9].	ch-pro	52-58	peptidase D	Homo sapiens	154-163
11338665-2	2001	A conjugation of chlorambucil (CH) with proline through an imido-bond resulted in the formation of a good substrate for prolidase.	Chlorambucil	17-29	peptidase D	Homo sapiens	120-129
11338665-2	2001	A conjugation of chlorambucil (CH) with proline through an imido-bond resulted in the formation of a good substrate for prolidase.	Chlorambucil	31-33	peptidase D	Homo sapiens	120-129
11338665-2	2001	A conjugation of chlorambucil (CH) with proline through an imido-bond resulted in the formation of a good substrate for prolidase.	Proline	40-47	peptidase D	Homo sapiens	120-129
11137854-3	2001	We have suggested that prolidase, an enzyme involved in collagen metabolism, may be one of the targets for anthracyclines-induced inhibition of synthesis of this protein.	Anthracyclines	107-121	peptidase D	Homo sapiens	23-32
11137854-4	2001	Prolidase [EC 3.4.13.9] cleaves imidodipeptides containing C-terminal proline, providing large amount of proline for collagen synthesis.	Proline	70-77	peptidase D	Homo sapiens	0-9
11137854-4	2001	Prolidase [EC 3.4.13.9] cleaves imidodipeptides containing C-terminal proline, providing large amount of proline for collagen synthesis.	Proline	105-112	peptidase D	Homo sapiens	0-9
11137854-5	2001	Therefore, we compared the effect of daunorubicin and doxorubicin on prolidase activity and collagen biosynthesis in confluent cultured human skin fibroblasts.	Daunorubicin	37-49	peptidase D	Homo sapiens	69-78
11137854-5	2001	Therefore, we compared the effect of daunorubicin and doxorubicin on prolidase activity and collagen biosynthesis in confluent cultured human skin fibroblasts.	Doxorubicin	54-65	peptidase D	Homo sapiens	69-78
11137854-6	2001	We have found that daunorubicin and doxorubicin coordinately induced the inhibition of prolidase activity (IC(50)=0.3 and 10 microM, respectively) and collagen biosynthesis (IC(50)=1 and 15 microM, respectively) in cultured human skin fibroblasts.	Daunorubicin	19-31	peptidase D	Homo sapiens	87-96
11137854-6	2001	We have found that daunorubicin and doxorubicin coordinately induced the inhibition of prolidase activity (IC(50)=0.3 and 10 microM, respectively) and collagen biosynthesis (IC(50)=1 and 15 microM, respectively) in cultured human skin fibroblasts.	Doxorubicin	36-47	peptidase D	Homo sapiens	87-96
11137854-7	2001	The inhibitory effect of daunorubicin or doxorubicin on prolidase activity and collagen biosynthesis was not due to anti-proliferative activity of these drugs as shown by cell viability tetrazoline test.	Daunorubicin	25-37	peptidase D	Homo sapiens	56-65
11137854-7	2001	The inhibitory effect of daunorubicin or doxorubicin on prolidase activity and collagen biosynthesis was not due to anti-proliferative activity of these drugs as shown by cell viability tetrazoline test.	Doxorubicin	41-52	peptidase D	Homo sapiens	56-65
11137854-8	2001	The decrease in prolidase activity due to the treatment of confluent cells with the anthracyclines was not accompanied by any difference in the amount of enzyme protein recovered from these cells as shown by Western immunoblot analysis.	Anthracyclines	84-98	peptidase D	Homo sapiens	16-25
11137854-10	2001	Since prolidase is metalloprotease, requiring manganese for catalytic activity, and anthracyclines are known as chelators of divalent cations, we considered that the chelating ability of anthracyclines might be an underlying mechanism for the anthracyclines-induced inhibition of prolidase activity.	Manganese	46-55	peptidase D	Homo sapiens	6-15
11137854-10	2001	Since prolidase is metalloprotease, requiring manganese for catalytic activity, and anthracyclines are known as chelators of divalent cations, we considered that the chelating ability of anthracyclines might be an underlying mechanism for the anthracyclines-induced inhibition of prolidase activity.	Anthracyclines	84-98	peptidase D	Homo sapiens	280-289
11137854-10	2001	Since prolidase is metalloprotease, requiring manganese for catalytic activity, and anthracyclines are known as chelators of divalent cations, we considered that the chelating ability of anthracyclines might be an underlying mechanism for the anthracyclines-induced inhibition of prolidase activity.	Anthracyclines	187-201	peptidase D	Homo sapiens	6-15
11137854-10	2001	Since prolidase is metalloprotease, requiring manganese for catalytic activity, and anthracyclines are known as chelators of divalent cations, we considered that the chelating ability of anthracyclines might be an underlying mechanism for the anthracyclines-induced inhibition of prolidase activity.	Anthracyclines	187-201	peptidase D	Homo sapiens	280-289
11137854-10	2001	Since prolidase is metalloprotease, requiring manganese for catalytic activity, and anthracyclines are known as chelators of divalent cations, we considered that the chelating ability of anthracyclines might be an underlying mechanism for the anthracyclines-induced inhibition of prolidase activity.	Anthracyclines	187-201	peptidase D	Homo sapiens	6-15
11137854-10	2001	Since prolidase is metalloprotease, requiring manganese for catalytic activity, and anthracyclines are known as chelators of divalent cations, we considered that the chelating ability of anthracyclines might be an underlying mechanism for the anthracyclines-induced inhibition of prolidase activity.	Anthracyclines	187-201	peptidase D	Homo sapiens	280-289
11137854-15	2001	The higher ability of daunorubicin vs. doxorubicin to chelate manganese and inhibit prolidase activity may explain the potential mechanism for its greater potency to inhibit collagen biosynthesis.	Daunorubicin	22-34	peptidase D	Homo sapiens	84-93
11137854-15	2001	The higher ability of daunorubicin vs. doxorubicin to chelate manganese and inhibit prolidase activity may explain the potential mechanism for its greater potency to inhibit collagen biosynthesis.	Doxorubicin	39-50	peptidase D	Homo sapiens	84-93
11820611-2	2001	Prolidase evokes the ability to hydrolyse the imido-bond of various low molecular weight compounds coupled to L-proline.	Proline	110-119	peptidase D	Homo sapiens	0-9
11820611-4	2001	Treatment of these prodrugs with prolidase generated L-proline and the free drug, demonstrating their substrate susceptibility prolidase.	Proline	53-62	peptidase D	Homo sapiens	33-42
11820611-4	2001	Treatment of these prodrugs with prolidase generated L-proline and the free drug, demonstrating their substrate susceptibility prolidase.	Proline	53-62	peptidase D	Homo sapiens	127-136
11820612-0	2001	Proline analogue of melphalan as a prolidase-convertible pro-drug in breast cancer MCF-7 cells.	Proline	0-7	peptidase D	Homo sapiens	35-44
11820612-0	2001	Proline analogue of melphalan as a prolidase-convertible pro-drug in breast cancer MCF-7 cells.	Melphalan	20-29	peptidase D	Homo sapiens	35-44
11820612-1	2001	Prolidase [E.C.3.4.13.9] is ubiquitously distributed cytosolic egzopeptidase that is known to cleave imido-bond of some low molecular weight compounds coupled to L-proline.	Proline	162-171	peptidase D	Homo sapiens	0-9
11820612-2	2001	Previously we have found that conjugation of antineoplastic drug--melphalan (Mel) with proline (pro) through imido-bond resulted in formation of a good substrate for purified prolidase.	Proline	87-94	peptidase D	Homo sapiens	175-184
11820612-2	2001	Previously we have found that conjugation of antineoplastic drug--melphalan (Mel) with proline (pro) through imido-bond resulted in formation of a good substrate for purified prolidase.	Proline	87-90	peptidase D	Homo sapiens	175-184
11820612-3	2001	Cytosolic location of prolidase in neoplastic cells suggests that proline analogue of melphalan (Mel-pro) may serve as a prolidase convertable pro-drug.	Proline	66-73	peptidase D	Homo sapiens	22-31
11204951-0	2000	Prolidase-activated prodrug for cancer chemotherapy cytotoxic activity of proline analogue of chlorambucil in breast cancer MCF-7 cells.	Proline	74-81	peptidase D	Homo sapiens	0-9
11204951-0	2000	Prolidase-activated prodrug for cancer chemotherapy cytotoxic activity of proline analogue of chlorambucil in breast cancer MCF-7 cells.	Chlorambucil	94-106	peptidase D	Homo sapiens	0-9
11204951-2	2000	Because prolidase possesses the ability to hydrolyse imido bonds of various low molecular weight compounds coupled to L-proline, we hypothesized that coupling of L-proline through an imido bond to anticancer drugs might create prodrugs which would be locally activated by tumour-associated prolidase and consequently would be less toxic to normal cells that evoke lower prolidase activity.	Proline	118-127	peptidase D	Homo sapiens	8-17
11204951-2	2000	Because prolidase possesses the ability to hydrolyse imido bonds of various low molecular weight compounds coupled to L-proline, we hypothesized that coupling of L-proline through an imido bond to anticancer drugs might create prodrugs which would be locally activated by tumour-associated prolidase and consequently would be less toxic to normal cells that evoke lower prolidase activity.	Proline	118-127	peptidase D	Homo sapiens	290-299
11204951-2	2000	Because prolidase possesses the ability to hydrolyse imido bonds of various low molecular weight compounds coupled to L-proline, we hypothesized that coupling of L-proline through an imido bond to anticancer drugs might create prodrugs which would be locally activated by tumour-associated prolidase and consequently would be less toxic to normal cells that evoke lower prolidase activity.	Proline	118-127	peptidase D	Homo sapiens	290-299
11204951-2	2000	Because prolidase possesses the ability to hydrolyse imido bonds of various low molecular weight compounds coupled to L-proline, we hypothesized that coupling of L-proline through an imido bond to anticancer drugs might create prodrugs which would be locally activated by tumour-associated prolidase and consequently would be less toxic to normal cells that evoke lower prolidase activity.	Proline	162-171	peptidase D	Homo sapiens	8-17
11204951-2	2000	Because prolidase possesses the ability to hydrolyse imido bonds of various low molecular weight compounds coupled to L-proline, we hypothesized that coupling of L-proline through an imido bond to anticancer drugs might create prodrugs which would be locally activated by tumour-associated prolidase and consequently would be less toxic to normal cells that evoke lower prolidase activity.	Proline	162-171	peptidase D	Homo sapiens	290-299
11204951-2	2000	Because prolidase possesses the ability to hydrolyse imido bonds of various low molecular weight compounds coupled to L-proline, we hypothesized that coupling of L-proline through an imido bond to anticancer drugs might create prodrugs which would be locally activated by tumour-associated prolidase and consequently would be less toxic to normal cells that evoke lower prolidase activity.	Proline	162-171	peptidase D	Homo sapiens	290-299
11204951-4	2000	Treatment of this prodrug with prolidase generated the L-proline and the free drug, demonstrating its substrate susceptibility to prolidase.	Proline	55-64	peptidase D	Homo sapiens	31-40
11204951-4	2000	Treatment of this prodrug with prolidase generated the L-proline and the free drug, demonstrating its substrate susceptibility to prolidase.	Proline	55-64	peptidase D	Homo sapiens	130-139
10965990-0	2000	The mechanism of daunorubicin-induced inhibition of prolidase activity in human skin fibroblasts and its implication to impaired collagen biosynthesis.	Daunorubicin	17-29	peptidase D	Homo sapiens	52-61
10965990-6	2000	We have found that daunorubicin (DNR) induced coordinately inhibition of prolidase activity (IC50 = 0.3 microM) and collagen biosynthesis (IC50 = 1 microM) in cultured human skin fibroblasts.	Daunorubicin	19-31	peptidase D	Homo sapiens	73-82
10965990-8	2000	Since prolidase is metaloprotease, requiring manganese for catalytic activity and anthracyclines are known as a chelators of divalent cations we considered that the chelating ability of anthracyclines may be an underlying mechanism for daunorubicin-induced inhibition of prolidase activity.	Manganese	45-54	peptidase D	Homo sapiens	6-15
10965990-8	2000	Since prolidase is metaloprotease, requiring manganese for catalytic activity and anthracyclines are known as a chelators of divalent cations we considered that the chelating ability of anthracyclines may be an underlying mechanism for daunorubicin-induced inhibition of prolidase activity.	Anthracyclines	82-96	peptidase D	Homo sapiens	6-15
10965990-8	2000	Since prolidase is metaloprotease, requiring manganese for catalytic activity and anthracyclines are known as a chelators of divalent cations we considered that the chelating ability of anthracyclines may be an underlying mechanism for daunorubicin-induced inhibition of prolidase activity.	Anthracyclines	82-96	peptidase D	Homo sapiens	271-280
10965990-8	2000	Since prolidase is metaloprotease, requiring manganese for catalytic activity and anthracyclines are known as a chelators of divalent cations we considered that the chelating ability of anthracyclines may be an underlying mechanism for daunorubicin-induced inhibition of prolidase activity.	Anthracyclines	186-200	peptidase D	Homo sapiens	6-15
10965990-8	2000	Since prolidase is metaloprotease, requiring manganese for catalytic activity and anthracyclines are known as a chelators of divalent cations we considered that the chelating ability of anthracyclines may be an underlying mechanism for daunorubicin-induced inhibition of prolidase activity.	Anthracyclines	186-200	peptidase D	Homo sapiens	271-280
10965990-8	2000	Since prolidase is metaloprotease, requiring manganese for catalytic activity and anthracyclines are known as a chelators of divalent cations we considered that the chelating ability of anthracyclines may be an underlying mechanism for daunorubicin-induced inhibition of prolidase activity.	Daunorubicin	236-248	peptidase D	Homo sapiens	6-15
10965990-8	2000	Since prolidase is metaloprotease, requiring manganese for catalytic activity and anthracyclines are known as a chelators of divalent cations we considered that the chelating ability of anthracyclines may be an underlying mechanism for daunorubicin-induced inhibition of prolidase activity.	Daunorubicin	236-248	peptidase D	Homo sapiens	271-280
10965990-12	2000	The strong ability of DNR to chelate manganese may explain the potential mechanism for inhibition of prolidase activity, subsequently collagen biosynthesis and poor wound healing in patients administered DNR.	Manganese	37-46	peptidase D	Homo sapiens	101-110
9879669-1	1998	Prolidase [E.C.3.4.13.9] is a cytosolic exopeptidase that catalyses the hydrolysis of C-terminal proline containing dipeptides or tripeptides.	Proline	97-104	peptidase D	Homo sapiens	0-9
10697434-2	1999	Synthesis of proline analogues of melphalan and theirs susceptibility to the action of prolidase.	Proline	13-20	peptidase D	Homo sapiens	87-96
10697434-4	1999	The synthesis of proline analogues of melphalan (well known antineoplastic agent) conjugated through imido-bond (potential target for prolidase action) has been performed.	Proline	17-24	peptidase D	Homo sapiens	134-143
10697434-5	1999	One of the compounds, N-[[[[(S)-carboxy]pyrrolidin-1-yl]carbonyl]methyl]-4-[bis(2-chloro ethyl) amino]-2-phenylalanine, was found as very good prolidase substrate with susceptibility over 2 fold higher compared to standard, endogenous its substrate--Gly-L-Pro.	n-[[[[(s)-carboxy]pyrrolidin-1-yl]carbonyl]methyl]-4-[bis(2-chloro ethyl) amino]-2-phenylalanine	22-118	peptidase D	Homo sapiens	143-152
10697434-6	1999	It suggests that targeting of prolidase as a proline analogue of melphalan-converting enzyme may serve as a novel strategy in therapy of neoplastic diseases.	Proline	45-52	peptidase D	Homo sapiens	30-39
10451808-1	1999	Prolidase [EC 3.4.13.9] plays an important role in the recycling of proline for collagen synthesis and cell growth.	Proline	68-75	peptidase D	Homo sapiens	0-9
10451808-4	1999	The effects of estrogen and antiestrogen (tamoxifen on the prolidase and collagenase activities and collagen biosynthesis) were measured in the estrogen-receptor (ER)-positive breast cancer cell line.	Tamoxifen	42-51	peptidase D	Homo sapiens	59-68
10451808-5	1999	Estradiol stimulated collagen biosynthesis and extracellular prolidase and collagenase activities in cultured MCF-7 cells without an effect on collagen accumulation in the extracellular matrix produced by these cells.	Estradiol	0-9	peptidase D	Homo sapiens	61-70
10582130-1	1999	Glycyl-L-proline (gly-pro) is an end product of collagen metabolism that is further cleaved by prolidase (EC 3.4.13.9); the resulting proline molecules are recycled into collagen or other proteins.	glycylproline	0-16	peptidase D	Homo sapiens	95-104
10582130-1	1999	Glycyl-L-proline (gly-pro) is an end product of collagen metabolism that is further cleaved by prolidase (EC 3.4.13.9); the resulting proline molecules are recycled into collagen or other proteins.	glycylproline	18-25	peptidase D	Homo sapiens	95-104
10582130-1	1999	Glycyl-L-proline (gly-pro) is an end product of collagen metabolism that is further cleaved by prolidase (EC 3.4.13.9); the resulting proline molecules are recycled into collagen or other proteins.	Proline	9-16	peptidase D	Homo sapiens	95-104
9879669-1	1998	Prolidase [E.C.3.4.13.9] is a cytosolic exopeptidase that catalyses the hydrolysis of C-terminal proline containing dipeptides or tripeptides.	Dipeptides	116-126	peptidase D	Homo sapiens	0-9
9879669-1	1998	Prolidase [E.C.3.4.13.9] is a cytosolic exopeptidase that catalyses the hydrolysis of C-terminal proline containing dipeptides or tripeptides.	tripeptides	130-141	peptidase D	Homo sapiens	0-9
9798267-0	1998	Doxorubicin-induced inhibition of prolidase activity in human skin fibroblasts and its implication to impaired collagen biosynthesis.	Doxorubicin	0-11	peptidase D	Homo sapiens	34-43
9619859-1	1998	Prolidase (EC 3.4.13.9) is an ubiquitously distributed imidodipeptidase that catalyzes the hydrolysis of dipeptides containing C-terminal proline or hydroxyproline.	Dipeptides	105-115	peptidase D	Homo sapiens	0-9
9619859-1	1998	Prolidase (EC 3.4.13.9) is an ubiquitously distributed imidodipeptidase that catalyzes the hydrolysis of dipeptides containing C-terminal proline or hydroxyproline.	Proline	138-145	peptidase D	Homo sapiens	0-9
9619859-1	1998	Prolidase (EC 3.4.13.9) is an ubiquitously distributed imidodipeptidase that catalyzes the hydrolysis of dipeptides containing C-terminal proline or hydroxyproline.	Hydroxyproline	149-163	peptidase D	Homo sapiens	0-9
9798267-3	1998	We considered prolidase, an enzyme involved in collagen metabolism as a possible target for doxorubicin-induced inhibition of synthesis of this protein.	Doxorubicin	92-103	peptidase D	Homo sapiens	14-23
9798267-4	1998	Prolidase [E.C.3.4.13.9] cleaves imidodipeptides containing C-terminal proline, providing large amount of proline for collagen resynthesis.	Proline	71-78	peptidase D	Homo sapiens	0-9
9798267-4	1998	Prolidase [E.C.3.4.13.9] cleaves imidodipeptides containing C-terminal proline, providing large amount of proline for collagen resynthesis.	Proline	106-113	peptidase D	Homo sapiens	0-9
9798267-5	1998	Therefore, we compared the effect of doxorubicin on prolidase activity and collagen biosynthesis in cultured human skin fibroblasts.	Doxorubicin	37-48	peptidase D	Homo sapiens	52-61
9798267-6	1998	We have found that doxorubicin induces coordinately inhibition of prolidase activity (IC50 approximately 10 +/- 3 microM) and collagen biosynthesis (IC50 approximately 15 +/- 3 microM) in cultured human skin fibroblasts.	Doxorubicin	19-30	peptidase D	Homo sapiens	66-75
9798267-7	1998	The inhibitory effect of doxorubicin on prolidase activity and collagen biosynthesis was not due to cytotoxicity of this drug as shown by cell viability tetrazoline test.	Doxorubicin	25-36	peptidase D	Homo sapiens	40-49
9798267-8	1998	The decrease in prolidase activity in fibroblasts treated with doxorubicin was not accompanied by differences in the amount of the enzyme protein recovered from these cells as shown by western immunoblot analysis.	Doxorubicin	63-74	peptidase D	Homo sapiens	16-25
9798267-10	1998	The data presented here rise possibility that doxorubicin-induced decrease in collagen biosynthesis is mostly due to the inhibition of prolidase activity.	Doxorubicin	46-57	peptidase D	Homo sapiens	135-144
9972056-2	1998	Synthesis of proline analogue of anthraquinone-2-carboxylic acid and its susceptibility to the action of prolidase.	Proline	13-20	peptidase D	Homo sapiens	105-114
9972056-2	1998	Synthesis of proline analogue of anthraquinone-2-carboxylic acid and its susceptibility to the action of prolidase.	anthraquinone-2-carboxylic acid	33-64	peptidase D	Homo sapiens	105-114
9972056-4	1998	The synthesis of proline analogue of anthraquinone-2-carboxylic acid (potential antineoplastic agent) conjugated through imido-bond (potential target for prolidase action) has been performed.	Proline	17-24	peptidase D	Homo sapiens	154-163
9972056-4	1998	The synthesis of proline analogue of anthraquinone-2-carboxylic acid (potential antineoplastic agent) conjugated through imido-bond (potential target for prolidase action) has been performed.	anthraquinone-2-carboxylic acid	37-68	peptidase D	Homo sapiens	154-163
9972056-7	1998	It has been presented that product of synthesis, N-(anthraquinone-2-carbonyl)-L-proline evokes susceptibility to the action of purified prolidase, comparable to the susceptibility of glycyl-L-proline (standard substrate for prolidase).	n-(anthraquinone-2-carbonyl)-l-proline	49-87	peptidase D	Homo sapiens	136-145
9972056-7	1998	It has been presented that product of synthesis, N-(anthraquinone-2-carbonyl)-L-proline evokes susceptibility to the action of purified prolidase, comparable to the susceptibility of glycyl-L-proline (standard substrate for prolidase).	n-(anthraquinone-2-carbonyl)-l-proline	49-87	peptidase D	Homo sapiens	224-233
9972056-7	1998	It has been presented that product of synthesis, N-(anthraquinone-2-carbonyl)-L-proline evokes susceptibility to the action of purified prolidase, comparable to the susceptibility of glycyl-L-proline (standard substrate for prolidase).	glycylproline	183-199	peptidase D	Homo sapiens	136-145
9972056-8	1998	Although insolubility of the proline analogue of anthraquinone-2-carboxylic acid in aqueous solutions limit its potential therapeutic value, the presented data suggest that prolidase may have a broader substrate specificity than thought previously.	Proline	29-36	peptidase D	Homo sapiens	173-182
9972056-8	1998	Although insolubility of the proline analogue of anthraquinone-2-carboxylic acid in aqueous solutions limit its potential therapeutic value, the presented data suggest that prolidase may have a broader substrate specificity than thought previously.	anthraquinone-2-carboxylic acid	49-80	peptidase D	Homo sapiens	173-182
9328822-1	1997	Prolidase (EC 3.4.13.9) is a ubiquitously distributed imidodipeptidase that catalyzes the hydrolysis of C-terminal proline or hydroxyproline containing dipeptides.	Proline	115-122	peptidase D	Homo sapiens	0-9
9328822-1	1997	Prolidase (EC 3.4.13.9) is a ubiquitously distributed imidodipeptidase that catalyzes the hydrolysis of C-terminal proline or hydroxyproline containing dipeptides.	Hydroxyproline	126-140	peptidase D	Homo sapiens	0-9
9328822-1	1997	Prolidase (EC 3.4.13.9) is a ubiquitously distributed imidodipeptidase that catalyzes the hydrolysis of C-terminal proline or hydroxyproline containing dipeptides.	Dipeptides	152-162	peptidase D	Homo sapiens	0-9
9581474-4	1997	The methanol in 30% concentration reduces catalytic activity of prolidase to 40% of values found in aqueous solution, although it allows in such conditions the measurement of substrate susceptibility to the action of this enzyme.	Methanol	4-12	peptidase D	Homo sapiens	64-73
9062907-0	1997	Fibroblast chemotaxis and prolidase activity modulation by insulin-like growth factor II and mannose 6-phosphate.	mannose-6-phosphate	93-112	peptidase D	Homo sapiens	26-35
9062907-9	1997	It has been found that mannose 6-phosphate stimulates also fibroblast prolidase activity with concomitant increase in lysosomal enzymes activity.	mannose-6-phosphate	23-42	peptidase D	Homo sapiens	70-79
8814549-3	1996	In situ hybridization using non-isotopic riboprobes labeled with digoxigenin and an isotopic riboprobe labeled with [35S]UTP localized prolidase gene expression to fibroblasts and endothelial cells of small vessels in scar tissue.	Sulfur-35	117-120	peptidase D	Homo sapiens	135-144
9581474-0	1997	Prolidase as a prodrug converting enzyme I. Synthesis of proline analogue of chlorambucil and its susceptibility to the action of prolidase.	Proline	57-64	peptidase D	Homo sapiens	0-9
9581474-0	1997	Prolidase as a prodrug converting enzyme I. Synthesis of proline analogue of chlorambucil and its susceptibility to the action of prolidase.	Proline	57-64	peptidase D	Homo sapiens	130-139
9581474-0	1997	Prolidase as a prodrug converting enzyme I. Synthesis of proline analogue of chlorambucil and its susceptibility to the action of prolidase.	Chlorambucil	77-89	peptidase D	Homo sapiens	0-9
9581474-0	1997	Prolidase as a prodrug converting enzyme I. Synthesis of proline analogue of chlorambucil and its susceptibility to the action of prolidase.	Chlorambucil	77-89	peptidase D	Homo sapiens	130-139
9581474-2	1997	The synthesis of proline analogue of chlorambucil (well known antineoplastic agent) conjugated through imido-bond (potential target for prolidase action) has been performed.	Proline	17-24	peptidase D	Homo sapiens	136-145
9581474-2	1997	The synthesis of proline analogue of chlorambucil (well known antineoplastic agent) conjugated through imido-bond (potential target for prolidase action) has been performed.	Chlorambucil	37-49	peptidase D	Homo sapiens	136-145
9112701-0	1996	Inhibition of prolidase activity by non-steroid antiinflammatory drugs in cultured human skin fibroblasts.	Steroids	40-47	peptidase D	Homo sapiens	14-23
9112701-4	1996	Prolidase activity was measured in cultured human skin fibroblasts, treated with some non-steroid antiinflammatory drugs (acetyl-salicylic acid, sodium salicylate, phenylbutazone, indometacin).	Steroids	90-97	peptidase D	Homo sapiens	0-9
9112701-4	1996	Prolidase activity was measured in cultured human skin fibroblasts, treated with some non-steroid antiinflammatory drugs (acetyl-salicylic acid, sodium salicylate, phenylbutazone, indometacin).	Aspirin	122-143	peptidase D	Homo sapiens	0-9
9112701-4	1996	Prolidase activity was measured in cultured human skin fibroblasts, treated with some non-steroid antiinflammatory drugs (acetyl-salicylic acid, sodium salicylate, phenylbutazone, indometacin).	Sodium Salicylate	145-162	peptidase D	Homo sapiens	0-9
9112701-4	1996	Prolidase activity was measured in cultured human skin fibroblasts, treated with some non-steroid antiinflammatory drugs (acetyl-salicylic acid, sodium salicylate, phenylbutazone, indometacin).	Phenylbutazone	164-178	peptidase D	Homo sapiens	0-9
9112701-4	1996	Prolidase activity was measured in cultured human skin fibroblasts, treated with some non-steroid antiinflammatory drugs (acetyl-salicylic acid, sodium salicylate, phenylbutazone, indometacin).	Indomethacin	180-191	peptidase D	Homo sapiens	0-9
9112701-7	1996	These observations suggest that non-steroid antiinflammatory drugs affect the metabolism of collagen through inhibition of prolidase activity in the collagen synthesizing cells.	Steroids	36-43	peptidase D	Homo sapiens	123-132
8782407-1	1996	An EDTA-insensitive prolidase (proline dipeptidase, EC 3.4.13.9) was isolated from a cell-free extract of Aureobacterium esteraromaticum IFO 3752.	Edetic Acid	3-7	peptidase D	Homo sapiens	31-50
15378943-2	1994	The enzyme prolidase cleaves iminodipeptides containing C-terminal prolyl or hydroxyprolyl residues and is important in the final stages of protein catabolism.	Peptide oostatic hormone	67-73	peptidase D	Homo sapiens	11-20
7748973-1	1995	Prolidase (EC: 3.4.13.9) catalyses the hydrolysis of the peptide bond involving the imino nitrogen of proline or hydroxyproline.	Nitrogen	90-98	peptidase D	Homo sapiens	0-9
7748973-1	1995	Prolidase (EC: 3.4.13.9) catalyses the hydrolysis of the peptide bond involving the imino nitrogen of proline or hydroxyproline.	Proline	102-109	peptidase D	Homo sapiens	0-9
7748973-1	1995	Prolidase (EC: 3.4.13.9) catalyses the hydrolysis of the peptide bond involving the imino nitrogen of proline or hydroxyproline.	Hydroxyproline	113-127	peptidase D	Homo sapiens	0-9
7748973-6	1995	Prolidase I activity was positively correlated with lecithin levels (n = 30; r = 0.42; p < 0.02), and also with birth weight of the babies (n = 30; r = 0.52; p < 0.01) in the term-mature group.	Lecithins	52-60	peptidase D	Homo sapiens	0-9
9020526-4	1996	Prolidase plays an important role in the recycling of proline for collagen synthesis and cell growth and probably serves as an interface between protein nutrition and matrix breakdown.	Proline	54-61	peptidase D	Homo sapiens	0-9
8821003-5	1995	In addition, both the transporter and the prolidase activities affected the overall transport of Phe when given as the dipeptide Phe-Pro, supporting the notion that intestinal absorption of peptides is an essential component of amino acid absorption.	Phenylalanine	97-100	peptidase D	Homo sapiens	42-51
8821003-5	1995	In addition, both the transporter and the prolidase activities affected the overall transport of Phe when given as the dipeptide Phe-Pro, supporting the notion that intestinal absorption of peptides is an essential component of amino acid absorption.	Dipeptides	119-128	peptidase D	Homo sapiens	42-51
8821003-5	1995	In addition, both the transporter and the prolidase activities affected the overall transport of Phe when given as the dipeptide Phe-Pro, supporting the notion that intestinal absorption of peptides is an essential component of amino acid absorption.	Phe-Pro	129-136	peptidase D	Homo sapiens	42-51
7817771-2	1994	These peaks of prolidase isozymes I and II differed from each other in their responses to preincubation with Mn2+, their substrate specificity, optimal pH, and heat stability.	Manganese(2+)	109-113	peptidase D	Homo sapiens	15-24
8174756-2	1994	Prolidase I (EC 3.4.13.9) was purified from human kidney to SDS-PAGE homogeneity.	Sodium Dodecyl Sulfate	60-63	peptidase D	Homo sapiens	0-9
15378943-6	1994	RESULTS: Prolidase activity was found to be deficient, especially against gly-pro.	glycylproline	74-81	peptidase D	Homo sapiens	9-18
8357941-8	1993	In patients, the excretion of large quantities of X-Pro is due to their very low prolidase activity towards this type of substrate.	x-pro	50-55	peptidase D	Homo sapiens	81-90
8069586-10	1994	In conclusion, the transmembrane uptake of Phe-Pro is dependent on a proton gradient, and the intracellular metabolism of Phe-Pro is complete via hydrolysis by prolidase.	Phe-Pro	43-50	peptidase D	Homo sapiens	160-169
8069586-10	1994	In conclusion, the transmembrane uptake of Phe-Pro is dependent on a proton gradient, and the intracellular metabolism of Phe-Pro is complete via hydrolysis by prolidase.	Phe-Pro	122-129	peptidase D	Homo sapiens	160-169
1536787-2	1992	Prolidase activity of erythrocytes against substrate glycyl-proline was deficient, but after blood transfusions this was increased to 15.7% of donor activity and declined to 12% and 3.4% of normal activity after 8 and 45 days, respectively.	glycylproline	53-67	peptidase D	Homo sapiens	0-9
8339543-3	1993	Although most of the hydroxy-[14]proline derived from the intracellular degradation of newly synthesized collagen in prolidase-deficient fibroblasts occurred in imidodipeptides, with a similar chromatographic profile to those occurring in the patient"s urine, the proportion of collagen undergoing such degradation was as in control cells.	hydroxy-[14]proline	21-40	peptidase D	Homo sapiens	117-126
1437403-2	1992	The enzyme prolidase hydrolyzes dipeptides containing C-terminal proline or hydroxyproline.	Dipeptides	32-42	peptidase D	Homo sapiens	11-20
1437403-2	1992	The enzyme prolidase hydrolyzes dipeptides containing C-terminal proline or hydroxyproline.	Proline	65-72	peptidase D	Homo sapiens	11-20
1437403-2	1992	The enzyme prolidase hydrolyzes dipeptides containing C-terminal proline or hydroxyproline.	Hydroxyproline	76-90	peptidase D	Homo sapiens	11-20
1437403-5	1992	Our results indicate that prolidase plays a major role in the recycling of dipeptide-bound proline.	Dipeptides	75-84	peptidase D	Homo sapiens	26-35
1437403-5	1992	Our results indicate that prolidase plays a major role in the recycling of dipeptide-bound proline.	Proline	91-98	peptidase D	Homo sapiens	26-35
1551457-6	1992	The activity of prolidase I, eluted at the lowest ionic strength, was stimulated by 24 hr of preincubation with 1 mM MnCl2, but prolidase II activity was strongly inhibited by this long preincubation.	manganese chloride	117-122	peptidase D	Homo sapiens	16-25
1545347-2	1992	The enzymatic hydrolysis by prolidase of substrates for the peptide transporter L-alpha-methyldopa-pro and several dipeptide analogues without an N-terminal alpha-amino group (phenylpropionylproline, phenylacetylproline, N-benzoylproline, and N-acetylproline) was investigated.	l-alpha-methyldopa-pro	80-102	peptidase D	Homo sapiens	28-37
1545347-2	1992	The enzymatic hydrolysis by prolidase of substrates for the peptide transporter L-alpha-methyldopa-pro and several dipeptide analogues without an N-terminal alpha-amino group (phenylpropionylproline, phenylacetylproline, N-benzoylproline, and N-acetylproline) was investigated.	Dipeptides	115-124	peptidase D	Homo sapiens	28-37
1545347-2	1992	The enzymatic hydrolysis by prolidase of substrates for the peptide transporter L-alpha-methyldopa-pro and several dipeptide analogues without an N-terminal alpha-amino group (phenylpropionylproline, phenylacetylproline, N-benzoylproline, and N-acetylproline) was investigated.	L-Proline, 1-(1-oxo-3-phenylpropyl)-	176-198	peptidase D	Homo sapiens	28-37
1545347-2	1992	The enzymatic hydrolysis by prolidase of substrates for the peptide transporter L-alpha-methyldopa-pro and several dipeptide analogues without an N-terminal alpha-amino group (phenylpropionylproline, phenylacetylproline, N-benzoylproline, and N-acetylproline) was investigated.	phenylacetylproline	200-219	peptidase D	Homo sapiens	28-37
1545347-2	1992	The enzymatic hydrolysis by prolidase of substrates for the peptide transporter L-alpha-methyldopa-pro and several dipeptide analogues without an N-terminal alpha-amino group (phenylpropionylproline, phenylacetylproline, N-benzoylproline, and N-acetylproline) was investigated.	1-benzoylpyrrolidine-2-carboxylic acid	221-237	peptidase D	Homo sapiens	28-37
1545347-2	1992	The enzymatic hydrolysis by prolidase of substrates for the peptide transporter L-alpha-methyldopa-pro and several dipeptide analogues without an N-terminal alpha-amino group (phenylpropionylproline, phenylacetylproline, N-benzoylproline, and N-acetylproline) was investigated.	N-acetylproline	243-258	peptidase D	Homo sapiens	28-37
1545347-5	1992	These results demonstrate that prolidase may serve as a prodrug-converting enzyme for the dipeptide-type prodrugs, utilizing the peptide carrier for transport of prodrugs into the mucosal cells and prolidase, a cytosolic enzyme, to release the drug.	Dipeptides	90-99	peptidase D	Homo sapiens	31-40
1545347-5	1992	These results demonstrate that prolidase may serve as a prodrug-converting enzyme for the dipeptide-type prodrugs, utilizing the peptide carrier for transport of prodrugs into the mucosal cells and prolidase, a cytosolic enzyme, to release the drug.	Dipeptides	90-99	peptidase D	Homo sapiens	198-207
1681807-1	1991	Reagents phenylglyoxal or 1-cyclohexyl-3-(2-morpholinoethyl)carbodiimide metho-p-toluenesulfonate inactivate the enzyme prolidase, with protection conferred by the competitive inhibitor N-acetylproline.	Phenylglyoxal	9-22	peptidase D	Homo sapiens	120-129
1681807-1	1991	Reagents phenylglyoxal or 1-cyclohexyl-3-(2-morpholinoethyl)carbodiimide metho-p-toluenesulfonate inactivate the enzyme prolidase, with protection conferred by the competitive inhibitor N-acetylproline.	1-Cyclohexyl-3-(2-(4-morpholinyl)ethyl)carbodiimide	26-72	peptidase D	Homo sapiens	120-129
1681807-1	1991	Reagents phenylglyoxal or 1-cyclohexyl-3-(2-morpholinoethyl)carbodiimide metho-p-toluenesulfonate inactivate the enzyme prolidase, with protection conferred by the competitive inhibitor N-acetylproline.	metho-p-toluenesulfonate	73-97	peptidase D	Homo sapiens	120-129
1681807-1	1991	Reagents phenylglyoxal or 1-cyclohexyl-3-(2-morpholinoethyl)carbodiimide metho-p-toluenesulfonate inactivate the enzyme prolidase, with protection conferred by the competitive inhibitor N-acetylproline.	N-acetylproline	186-201	peptidase D	Homo sapiens	120-129
2246245-1	1990	Catalytic pH dependence for the hydrolytic activity of the enzyme prolidase with a series of dipeptide substrates is found to be generally bell-shaped (kcat/Km) or simple sigmoidal (kcat).	Dipeptides	93-102	peptidase D	Homo sapiens	66-75
2246245-3	1990	Significant catalysis at a pH of 6.6 is also observed for prolidase with (alkylthio)acetylprolines and with haloacetylprolines.	(alkylthio)acetylprolines	73-98	peptidase D	Homo sapiens	58-67
2246245-3	1990	Significant catalysis at a pH of 6.6 is also observed for prolidase with (alkylthio)acetylprolines and with haloacetylprolines.	haloacetylprolines	108-126	peptidase D	Homo sapiens	58-67
2246246-1	1990	The pH dependence of Ki for inhibition of prolidase by acetylproline, proline, and trans-1,2-cyclopentanedicarboxylate follows a different pattern in each case, although deprotonation of an enzymic functional group with a pKa value of 6.6 perturbs ligand binding in every instance.	N-acetylproline	55-68	peptidase D	Homo sapiens	42-51
2246246-1	1990	The pH dependence of Ki for inhibition of prolidase by acetylproline, proline, and trans-1,2-cyclopentanedicarboxylate follows a different pattern in each case, although deprotonation of an enzymic functional group with a pKa value of 6.6 perturbs ligand binding in every instance.	Proline	61-68	peptidase D	Homo sapiens	42-51
2246246-1	1990	The pH dependence of Ki for inhibition of prolidase by acetylproline, proline, and trans-1,2-cyclopentanedicarboxylate follows a different pattern in each case, although deprotonation of an enzymic functional group with a pKa value of 6.6 perturbs ligand binding in every instance.	1,2-cyclopentanedicarboxylate	83-118	peptidase D	Homo sapiens	42-51
2246246-1	1990	The pH dependence of Ki for inhibition of prolidase by acetylproline, proline, and trans-1,2-cyclopentanedicarboxylate follows a different pattern in each case, although deprotonation of an enzymic functional group with a pKa value of 6.6 perturbs ligand binding in every instance.	perturbs	239-247	peptidase D	Homo sapiens	42-51
1972707-1	1990	Prolidase (peptidase D) catalyzes hydrolysis of the di- and tripeptide with carboxyl-terminal proline and plays an important role in recycling proline in various cells and tissues.	Proline	94-101	peptidase D	Homo sapiens	11-22
2073490-5	1990	The substrate specificity of partially purified prolidase-I and II in control fibroblasts was estimated against Gly-Pro, Ala-Pro, Met-Pro.	glycylproline	112-119	peptidase D	Homo sapiens	48-57
2073490-5	1990	The substrate specificity of partially purified prolidase-I and II in control fibroblasts was estimated against Gly-Pro, Ala-Pro, Met-Pro.	alanylproline	121-128	peptidase D	Homo sapiens	48-57
2073490-5	1990	The substrate specificity of partially purified prolidase-I and II in control fibroblasts was estimated against Gly-Pro, Ala-Pro, Met-Pro.	met-pro	130-137	peptidase D	Homo sapiens	48-57
1972707-1	1990	Prolidase (peptidase D) catalyzes hydrolysis of the di- and tripeptide with carboxyl-terminal proline and plays an important role in recycling proline in various cells and tissues.	Proline	143-150	peptidase D	Homo sapiens	0-9
1972707-1	1990	Prolidase (peptidase D) catalyzes hydrolysis of the di- and tripeptide with carboxyl-terminal proline and plays an important role in recycling proline in various cells and tissues.	Proline	143-150	peptidase D	Homo sapiens	11-22
34085157-9	2021	The mechanism for down-regulation of p53 expression in MCF-7iPOX cells was found at the level of p53-PEPD complex formation that was counteracted by hydrogen peroxide treatment.	Hydrogen Peroxide	149-166	peptidase D	Homo sapiens	101-105
1972707-1	1990	Prolidase (peptidase D) catalyzes hydrolysis of the di- and tripeptide with carboxyl-terminal proline and plays an important role in recycling proline in various cells and tissues.	di- and tripeptide	52-70	peptidase D	Homo sapiens	0-9
1972707-1	1990	Prolidase (peptidase D) catalyzes hydrolysis of the di- and tripeptide with carboxyl-terminal proline and plays an important role in recycling proline in various cells and tissues.	di- and tripeptide	52-70	peptidase D	Homo sapiens	11-22
1972707-1	1990	Prolidase (peptidase D) catalyzes hydrolysis of the di- and tripeptide with carboxyl-terminal proline and plays an important role in recycling proline in various cells and tissues.	Proline	94-101	peptidase D	Homo sapiens	0-9
2317925-4	1990	The Km values for Gly-Pro of the control"s and the patient"s mother"s prolidase I were 2.90 +/- 0.22 and 2.88 +/- 0.27 mM, but the Vmax values for Gly-Pro of the mother"s enzyme was reduced about 30% compared to that of control enzymes (mother: 6.02 units/mg protein, control: 22.21 units/mg protein).	glycylproline	18-25	peptidase D	Homo sapiens	70-79
33818628-6	2021	Proline availability is regulated by prolidase (proline supporting enzyme), collagen biosynthesis (proline utilizing process) and proline synthesis from glutamine, glutamate, alpha-ketoglutarate (alpha-KG) and ornithine.	Proline	0-7	peptidase D	Homo sapiens	37-46
34943229-8	2021	The amount of this amino acid is regulated at the level of prolidase (proline releasing enzyme), collagen biosynthesis (proline utilizing process), and glutamine, glutamate, alpha-ketoglutarate, and ornithine metabolism.	Proline	70-77	peptidase D	Homo sapiens	59-68
34943229-10	2021	It seems that in estrogen receptor-positive breast cancer cells, prolidase supports proline for collagen biosynthesis, limiting its availability for PRODH/POX-dependent apoptosis.	Proline	84-91	peptidase D	Homo sapiens	65-74
34880421-3	2021	We recently found that p53 binds via its proline-rich domain to peptidase D (PEPD) and is activated when the binding is disrupted.	Proline	41-48	peptidase D	Homo sapiens	64-75
34880421-3	2021	We recently found that p53 binds via its proline-rich domain to peptidase D (PEPD) and is activated when the binding is disrupted.	Proline	41-48	peptidase D	Homo sapiens	77-81
34880421-6	2021	Once freed from PEPD, p53 mutants undergo multiple posttranslational modifications, especially lysine 373 acetylation, which cause them to refold and regain tumor suppressor activities that are typically displayed by p53.	Lysine	95-101	peptidase D	Homo sapiens	16-20