PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 18340504-2 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 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 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 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 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 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 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 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 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 1437403-2 1992 The enzyme prolidase hydrolyzes dipeptides containing C-terminal proline or hydroxyproline. Hydroxyproline 76-90 peptidase D Homo sapiens 11-20 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 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 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