PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 3544718-2 1986 However, post proline cleaving enzyme (PPCE; EC 3.4.21.26), a proline specific endopeptidase which specifically hydrolyzes internal peptide bonds on the carboxyl side of proline residues, has been shown to inactivate numerous vasoactive peptides including angiotensins, kinins, substance P, vasopressin and oxytocin. Proline 14-21 prolyl endopeptidase Homo sapiens 39-43 3544718-2 1986 However, post proline cleaving enzyme (PPCE; EC 3.4.21.26), a proline specific endopeptidase which specifically hydrolyzes internal peptide bonds on the carboxyl side of proline residues, has been shown to inactivate numerous vasoactive peptides including angiotensins, kinins, substance P, vasopressin and oxytocin. Proline 62-69 prolyl endopeptidase Homo sapiens 9-37 3544718-2 1986 However, post proline cleaving enzyme (PPCE; EC 3.4.21.26), a proline specific endopeptidase which specifically hydrolyzes internal peptide bonds on the carboxyl side of proline residues, has been shown to inactivate numerous vasoactive peptides including angiotensins, kinins, substance P, vasopressin and oxytocin. Proline 62-69 prolyl endopeptidase Homo sapiens 39-43 33878557-4 2021 Characterisation of the peptides in treated beer showed that prolyl-endopeptidase activity was not complete with many peptides containing (multiple) internal proline-residues. Proline 158-165 prolyl endopeptidase Homo sapiens 61-81 476124-4 1979 This substrate showed a higher affinity (Km = 0.02 mM) for the enzyme than the proline containing substrates studied previously and allowed the detection of 10-50 ng post-proline cleaving enzyme activity per ml sample after a 1 min incubation period. Proline 79-86 prolyl endopeptidase Homo sapiens 166-194 32315321-1 2020 The proline-specific enzymes dipeptidyl peptidase 4 (DPP4), prolylcarboxypeptidase (PRCP), fibroblast activation protein alpha (FAP) and prolyl oligopeptidase (PREP) are known for their involvement in the immune system and blood pressure regulation. Proline 4-11 prolyl endopeptidase Homo sapiens 137-158 32297517-5 2020 We redesigned Sphaerobacter thermophiles PEP with high-temperature activity/stability, a wide range of pH stabilities, and high proline specificity. Proline 128-135 prolyl endopeptidase Homo sapiens 41-44 32315321-1 2020 The proline-specific enzymes dipeptidyl peptidase 4 (DPP4), prolylcarboxypeptidase (PRCP), fibroblast activation protein alpha (FAP) and prolyl oligopeptidase (PREP) are known for their involvement in the immune system and blood pressure regulation. Proline 4-11 prolyl endopeptidase Homo sapiens 160-164 25564858-1 2015 Prolyl oligopeptidase (POP) is a large 80 kDa protease, which cleaves oligopeptides at the C-terminal side of proline residues and constitutes an important pharmaceutical target. Proline 110-117 prolyl endopeptidase Homo sapiens 0-21 28070831-1 2017 BACKGROUND: Prolyl oligopeptidase (POP, EC 3.4.1.26) is a serine peptidase that hydrolyzes post-proline peptide bonds in peptides that are <30 amino acids in length. Proline 96-103 prolyl endopeptidase Homo sapiens 12-33 28070831-1 2017 BACKGROUND: Prolyl oligopeptidase (POP, EC 3.4.1.26) is a serine peptidase that hydrolyzes post-proline peptide bonds in peptides that are <30 amino acids in length. Proline 96-103 prolyl endopeptidase Homo sapiens 35-38 27503084-1 2017 Prolyl oligopeptidase (also named prolyl endopeptidase; PREP) hydrolyzes the Pro-Xaa bonds of biologically active oligopeptides on their carboxyl side. Proline 0-3 prolyl endopeptidase Homo sapiens 56-60 29047268-3 2017 Barley-based beers crafted to remove gluten using proprietary precipitation and/or application of enzymes, e.g. prolyl endopeptidases (PEP) that degrade the proline-rich gluten molecules, are available commercially. Proline 157-164 prolyl endopeptidase Homo sapiens 135-138 25863351-1 2015 Prolyl oligopeptidase is a cytosolic serine peptidase that hydrolyses proline-containing peptides at the carboxy terminus of proline residues. Proline 70-77 prolyl endopeptidase Homo sapiens 0-21 25863351-1 2015 Prolyl oligopeptidase is a cytosolic serine peptidase that hydrolyses proline-containing peptides at the carboxy terminus of proline residues. Proline 125-132 prolyl endopeptidase Homo sapiens 0-21 25564858-1 2015 Prolyl oligopeptidase (POP) is a large 80 kDa protease, which cleaves oligopeptides at the C-terminal side of proline residues and constitutes an important pharmaceutical target. Proline 110-117 prolyl endopeptidase Homo sapiens 23-26 21539473-1 2011 INTRODUCTION: Prolyl Oligopeptidase (POP) is a serine peptidase that cleaves post-proline bonds in short peptides. Proline 82-89 prolyl endopeptidase Homo sapiens 14-35 24016298-2 2014 We tested the hypothesis that this T cell reactivity could be abolished by using prolyl-endopeptidase (PEP), an enzyme that cleaves peptide bonds after proline. Proline 152-159 prolyl endopeptidase Homo sapiens 103-106 22750443-0 2012 Comparative analysis of the substrate preferences of two post-proline cleaving endopeptidases, prolyl oligopeptidase and fibroblast activation protein alpha. Proline 62-69 prolyl endopeptidase Homo sapiens 95-116 21620802-1 2011 Prolyl oligopeptidase (POP) is a post-proline cleaving enzyme, which is widely distributed in various organs, with high levels in the brain. Proline 38-45 prolyl endopeptidase Homo sapiens 0-21 21620802-1 2011 Prolyl oligopeptidase (POP) is a post-proline cleaving enzyme, which is widely distributed in various organs, with high levels in the brain. Proline 38-45 prolyl endopeptidase Homo sapiens 23-26 21222622-1 2011 Prolyl oligopeptidase (POP) is a serine protease that cleaves peptides shorter than 30-mer at the carboxyl side of an internal proline. Proline 127-134 prolyl endopeptidase Homo sapiens 0-21 21222622-1 2011 Prolyl oligopeptidase (POP) is a serine protease that cleaves peptides shorter than 30-mer at the carboxyl side of an internal proline. Proline 127-134 prolyl endopeptidase Homo sapiens 23-26 21222626-1 2011 Prolyl oligopeptidase or prolyl endopeptidase (PREP; EC 3.4.21.26) is an atypical serine protease that hydrolyses peptides and peptide hormones after proline in peptides up to around 30 residues long. Proline 150-157 prolyl endopeptidase Homo sapiens 0-21 21222626-1 2011 Prolyl oligopeptidase or prolyl endopeptidase (PREP; EC 3.4.21.26) is an atypical serine protease that hydrolyses peptides and peptide hormones after proline in peptides up to around 30 residues long. Proline 150-157 prolyl endopeptidase Homo sapiens 25-45 21222626-1 2011 Prolyl oligopeptidase or prolyl endopeptidase (PREP; EC 3.4.21.26) is an atypical serine protease that hydrolyses peptides and peptide hormones after proline in peptides up to around 30 residues long. Proline 150-157 prolyl endopeptidase Homo sapiens 47-51 21222628-2 2011 3.4.21.26, PREP) also known as prolyl oligopeptidase is an enzyme which cleaves several peptides at the carboxyl side of proline residues. Proline 121-128 prolyl endopeptidase Homo sapiens 11-15 21222628-2 2011 3.4.21.26, PREP) also known as prolyl oligopeptidase is an enzyme which cleaves several peptides at the carboxyl side of proline residues. Proline 121-128 prolyl endopeptidase Homo sapiens 31-52 21222629-1 2011 Prolyl oligopeptidase (POP), is an 80-kDa serine protease that hydrolyzes peptides smaller than 30-mer at the carboxyl side of an internal proline-residue. Proline 139-146 prolyl endopeptidase Homo sapiens 0-21 21222629-1 2011 Prolyl oligopeptidase (POP), is an 80-kDa serine protease that hydrolyzes peptides smaller than 30-mer at the carboxyl side of an internal proline-residue. Proline 139-146 prolyl endopeptidase Homo sapiens 23-26 24269815-1 2014 Prolyl oligopeptidase (POP) is a serine endopeptidase that hydrolyzes post-proline peptide bonds in peptides that are <30 amino acids in length. Proline 75-82 prolyl endopeptidase Homo sapiens 0-21 24269815-1 2014 Prolyl oligopeptidase (POP) is a serine endopeptidase that hydrolyzes post-proline peptide bonds in peptides that are <30 amino acids in length. Proline 75-82 prolyl endopeptidase Homo sapiens 23-26 23348613-1 2013 Prolyl oligopeptidase is a serine protease that cleaves peptides shorter 30-mer at carboxyl side of an internal proline. Proline 112-119 prolyl endopeptidase Homo sapiens 0-21 21539473-1 2011 INTRODUCTION: Prolyl Oligopeptidase (POP) is a serine peptidase that cleaves post-proline bonds in short peptides. Proline 82-89 prolyl endopeptidase Homo sapiens 37-40 20978968-7 2011 POP is a ubiquitous post-proline cleaving enzyme with particularly high expression levels in the mammalian brain, where it participates in the metabolism of neuroactive peptides and peptide-like hormones (e.g. thyroliberin, gonadotropin-releasing hormone). Proline 25-32 prolyl endopeptidase Homo sapiens 0-3 19687473-1 2009 Prolyl oligopeptidase (POP) is a serine endopeptidase that hydrolyses proline-containing peptides shorter than 30 amino acids. Proline 70-77 prolyl endopeptidase Homo sapiens 0-21 19875179-1 2009 Prolyl endopeptidase (PE), a protease that cleaves after proline residues in oligopeptides, is highly active in brain and degrades neuropeptides in vitro. Proline 57-64 prolyl endopeptidase Homo sapiens 0-20 19875179-1 2009 Prolyl endopeptidase (PE), a protease that cleaves after proline residues in oligopeptides, is highly active in brain and degrades neuropeptides in vitro. Proline 57-64 prolyl endopeptidase Homo sapiens 22-24 19687473-1 2009 Prolyl oligopeptidase (POP) is a serine endopeptidase that hydrolyses proline-containing peptides shorter than 30 amino acids. Proline 70-77 prolyl endopeptidase Homo sapiens 23-26 18792035-1 2008 Prolyl oligopeptidase (POP) is a cytosolic serine peptidase that hydrolyzes proline-containing peptides at the carboxy terminus of proline residues. Proline 76-83 prolyl endopeptidase Homo sapiens 0-21 19290936-1 2009 The proline-, glutamic acid-, serine- and threonine-rich (PEST) family of protein tyrosine phosphatases (PTPs) includes proline-enriched phosphatase (PEP)/lymphoid tyrosine phosphatase (LYP), PTP-PEST, and PTP-hematopoietic stem cell fraction (HSCF). Proline 4-11 prolyl endopeptidase Homo sapiens 120-148 19290936-1 2009 The proline-, glutamic acid-, serine- and threonine-rich (PEST) family of protein tyrosine phosphatases (PTPs) includes proline-enriched phosphatase (PEP)/lymphoid tyrosine phosphatase (LYP), PTP-PEST, and PTP-hematopoietic stem cell fraction (HSCF). Proline 4-11 prolyl endopeptidase Homo sapiens 150-153 18718510-1 2008 Prolyl oligopeptidase (POP) is an endopeptidase which cleaves short proline-containing neuropeptides, and it is involved in memory and learning. Proline 68-75 prolyl endopeptidase Homo sapiens 0-21 18718510-1 2008 Prolyl oligopeptidase (POP) is an endopeptidase which cleaves short proline-containing neuropeptides, and it is involved in memory and learning. Proline 68-75 prolyl endopeptidase Homo sapiens 23-26 18792035-1 2008 Prolyl oligopeptidase (POP) is a cytosolic serine peptidase that hydrolyzes proline-containing peptides at the carboxy terminus of proline residues. Proline 76-83 prolyl endopeptidase Homo sapiens 23-26 18792035-1 2008 Prolyl oligopeptidase (POP) is a cytosolic serine peptidase that hydrolyzes proline-containing peptides at the carboxy terminus of proline residues. Proline 131-138 prolyl endopeptidase Homo sapiens 0-21 18792035-1 2008 Prolyl oligopeptidase (POP) is a cytosolic serine peptidase that hydrolyzes proline-containing peptides at the carboxy terminus of proline residues. Proline 131-138 prolyl endopeptidase Homo sapiens 23-26 16919454-2 2006 The study was performed on previously developed prolyl oligopeptidase inhibitors with proline mimetics at the P2 position. Proline 86-93 prolyl endopeptidase Homo sapiens 48-69 18657187-1 2008 Prolyl oligopeptidase (POP) is a serine protease that cleaves small peptides at the carboxyl side of an internal proline residue. Proline 113-120 prolyl endopeptidase Homo sapiens 0-21 18657187-1 2008 Prolyl oligopeptidase (POP) is a serine protease that cleaves small peptides at the carboxyl side of an internal proline residue. Proline 113-120 prolyl endopeptidase Homo sapiens 23-26 17714777-1 2007 Prolyl endopeptidase (PEP, EC 3.4.21.26) is a proline-specific endopeptidase with a serine-type mechanism, which digests small peptide-like hormones, neuroactive peptides, and various cellular factors. Proline 46-53 prolyl endopeptidase Homo sapiens 0-20 17714777-1 2007 Prolyl endopeptidase (PEP, EC 3.4.21.26) is a proline-specific endopeptidase with a serine-type mechanism, which digests small peptide-like hormones, neuroactive peptides, and various cellular factors. Proline 46-53 prolyl endopeptidase Homo sapiens 22-25 17904692-1 2007 Prolyl oligopeptidase (POP, EC 3.4.21.26) is a member of a family of serine peptidases with post-proline cleaving activity towards peptides. Proline 97-104 prolyl endopeptidase Homo sapiens 0-21 17878957-1 2007 Prolyl oligopeptidase (POP) is a ubiquitous post-proline cleaving enzyme that is highly expressed in brain. Proline 49-56 prolyl endopeptidase Homo sapiens 0-21 17878957-1 2007 Prolyl oligopeptidase (POP) is a ubiquitous post-proline cleaving enzyme that is highly expressed in brain. Proline 49-56 prolyl endopeptidase Homo sapiens 23-26 17295371-1 2007 Prolyl oligopeptidase is a cytosolic serine peptidase that hydrolyzes proline-containing peptides at the carboxy terminus. Proline 70-77 prolyl endopeptidase Homo sapiens 0-21 17160352-2 2007 The most well studied PEP family has a two-domain structure whose unique seven-blade beta-propeller domain works with the catalytic domain to hydrolyze the peptide bond on the carboxyl side of internal proline residues of an oligopeptide substrate. Proline 202-209 prolyl endopeptidase Homo sapiens 22-25 18650094-1 2008 Prolyl oligopeptidase is a cytosolic serine peptidase that hydrolyzes proline-containing peptides at the carboxy terminus of proline residues. Proline 70-77 prolyl endopeptidase Homo sapiens 0-21 18650094-1 2008 Prolyl oligopeptidase is a cytosolic serine peptidase that hydrolyzes proline-containing peptides at the carboxy terminus of proline residues. Proline 125-132 prolyl endopeptidase Homo sapiens 0-21 16406204-8 2006 In contrast, PEP hydrolyzed human urotensin II at the canonical post-proline site. Proline 69-76 prolyl endopeptidase Homo sapiens 13-16 15932649-1 2005 BACKGROUND: Prolyl Endopeptidase (PEP, EC 3.4.21.26), a cytosolic endopeptidase, hydrolyses peptide bonds on the carboxyl side of proline residue in proteins with a relatively small molecular weight. Proline 130-137 prolyl endopeptidase Homo sapiens 12-32 16628753-1 2006 Prolyl oligopeptidase is a cytosolic serine peptidase that hydrolyzes proline-containing peptides at the carboxy termini of the proline residues. Proline 70-77 prolyl endopeptidase Homo sapiens 0-21 16628753-1 2006 Prolyl oligopeptidase is a cytosolic serine peptidase that hydrolyzes proline-containing peptides at the carboxy termini of the proline residues. Proline 128-135 prolyl endopeptidase Homo sapiens 0-21 16212427-10 2005 Prolyl endopeptidase treatment was shown to abolish the antigenicity of both the 33-mer and the 26-mer peptides, and was also predicted to have comparable effects on other proline-rich putatively immunotoxic peptides identified from other polypeptides within the gluten proteome. Proline 172-179 prolyl endopeptidase Homo sapiens 0-20 15932649-1 2005 BACKGROUND: Prolyl Endopeptidase (PEP, EC 3.4.21.26), a cytosolic endopeptidase, hydrolyses peptide bonds on the carboxyl side of proline residue in proteins with a relatively small molecular weight. Proline 130-137 prolyl endopeptidase Homo sapiens 34-37 15217351-1 2004 POP (prolyl oligopeptidase) specifically hydrolyses a number of small proline-containing peptides at the carboxy end of the proline residue and POP inhibitors have been shown to have cognition-enhancing properties. Proline 70-77 prolyl endopeptidase Homo sapiens 0-3 15509157-0 2004 A cyclopent-2-enecarbonyl group mimics proline at the P2 position of prolyl oligopeptidase inhibitors. Proline 39-46 prolyl endopeptidase Homo sapiens 69-90 15509157-1 2004 With the aim to replace the natural amino acid proline by a proline mimetic structure, a cyclopent-2-enecarbonyl moiety was studied at the P2 position of prolyl oligopeptidase (POP) inhibitors. Proline 60-67 prolyl endopeptidase Homo sapiens 154-175 15509157-2 2004 The cyclopent-2-enecarbonyl moiety proved to be an excellent proline mimetic at the P2 position of POP inhibitors. Proline 61-68 prolyl endopeptidase Homo sapiens 99-102 15217351-1 2004 POP (prolyl oligopeptidase) specifically hydrolyses a number of small proline-containing peptides at the carboxy end of the proline residue and POP inhibitors have been shown to have cognition-enhancing properties. Proline 70-77 prolyl endopeptidase Homo sapiens 5-26 15217351-1 2004 POP (prolyl oligopeptidase) specifically hydrolyses a number of small proline-containing peptides at the carboxy end of the proline residue and POP inhibitors have been shown to have cognition-enhancing properties. Proline 70-77 prolyl endopeptidase Homo sapiens 144-147 15217351-1 2004 POP (prolyl oligopeptidase) specifically hydrolyses a number of small proline-containing peptides at the carboxy end of the proline residue and POP inhibitors have been shown to have cognition-enhancing properties. Proline 124-131 prolyl endopeptidase Homo sapiens 0-3 15217351-1 2004 POP (prolyl oligopeptidase) specifically hydrolyses a number of small proline-containing peptides at the carboxy end of the proline residue and POP inhibitors have been shown to have cognition-enhancing properties. Proline 124-131 prolyl endopeptidase Homo sapiens 5-26 11404383-6 2001 Degradation was completely inhibited by proline-specific serine protease (prolyl endopeptidase) inhibitors but not by proteasome, calpain, and metalloprotease inhibitors. Proline 40-47 prolyl endopeptidase Homo sapiens 74-94 12941425-3 2003 More distant members include prolyl oligopeptidase (POP; post proline cleaving enzyme) and acylaminoacylpeptidase (AAP; acylpeptide hydrolase). Proline 62-69 prolyl endopeptidase Homo sapiens 29-50 12941425-3 2003 More distant members include prolyl oligopeptidase (POP; post proline cleaving enzyme) and acylaminoacylpeptidase (AAP; acylpeptide hydrolase). Proline 62-69 prolyl endopeptidase Homo sapiens 52-55 11685249-1 2001 C-terminal Src kinase (Csk) takes part in a highly specific, high affinity interaction via its Src homology 3 (SH3) domain with the proline-enriched tyrosine phosphatase PEP in hematopoietic cells. Proline 132-139 prolyl endopeptidase Homo sapiens 170-173 11685249-2 2001 The solution structure of the Csk-SH3 domain in complex with a 25-residue peptide from the Pro/Glu/Ser/Thr-rich (PEST) domain of PEP reveals the basis for this specific peptide recognition motif involving an SH3 domain. Proline 91-94 prolyl endopeptidase Homo sapiens 129-132 11685249-3 2001 Three residues, Ala 40, Thr 42 and Lys 43, in the SH3 domain of Csk specifically recognize two hydrophobic residues, Ile 625 and Val 626, in the proline-rich sequence of the PEST domain of PEP. Proline 145-152 prolyl endopeptidase Homo sapiens 189-192 11685249-4 2001 These two residues are C-terminal to the conventional proline-rich SH3 domain recognition sequence of PEP. Proline 54-61 prolyl endopeptidase Homo sapiens 102-105 11004527-1 2000 Aminopeptidase P (APP), dipeptidyl peptidase II (DP II), dipeptidyl peptidase IV (DP IV) and prolyl oligopeptidase (POP) are proline specific peptidases. Proline 125-132 prolyl endopeptidase Homo sapiens 93-114 11543693-8 2001 Lowered serum activity of prolyl endopeptidase (PEP), a cytosolic endopeptidase that cleaves peptide bonds on the carboxyl side of proline in proteins of relatively small molecular mass, may play a role in the biophysiology of fibromyalgia through diminished inactivation of algesic and depression-related peptides, e.g. substance P. Proline 131-138 prolyl endopeptidase Homo sapiens 26-46 11543693-8 2001 Lowered serum activity of prolyl endopeptidase (PEP), a cytosolic endopeptidase that cleaves peptide bonds on the carboxyl side of proline in proteins of relatively small molecular mass, may play a role in the biophysiology of fibromyalgia through diminished inactivation of algesic and depression-related peptides, e.g. substance P. Proline 131-138 prolyl endopeptidase Homo sapiens 48-51 11070331-1 2001 The aim of this study was to examine whether anorexia and bulimia nervosa are accompanied by lower serum activity of prolyl endopeptidase (PEP;EC 3.4.21.26; post-proline cleaving enzyme), a cytosolic endopeptidase which cleaves peptide bonds on the carboxyl side of proline in proteins of relatively small molecular mass. Proline 162-169 prolyl endopeptidase Homo sapiens 117-137 11070331-1 2001 The aim of this study was to examine whether anorexia and bulimia nervosa are accompanied by lower serum activity of prolyl endopeptidase (PEP;EC 3.4.21.26; post-proline cleaving enzyme), a cytosolic endopeptidase which cleaves peptide bonds on the carboxyl side of proline in proteins of relatively small molecular mass. Proline 266-273 prolyl endopeptidase Homo sapiens 117-137 11004527-1 2000 Aminopeptidase P (APP), dipeptidyl peptidase II (DP II), dipeptidyl peptidase IV (DP IV) and prolyl oligopeptidase (POP) are proline specific peptidases. Proline 125-132 prolyl endopeptidase Homo sapiens 116-119 7959018-1 1994 The human cDNA encoding prolyl endopeptidase, a cytoplasmic endoprotease which hydrolyses the peptide bond at the C-terminal side of proline, was sequenced. Proline 133-140 prolyl endopeptidase Homo sapiens 24-44 10363664-1 1999 BACKGROUND: It is reported that psychiatric disorders, such as depression and schizophrenia, are associated with changes in serum activity of prolyl endopeptidase (EC 3.4.21.26), a cytosolic endopeptidase, which cleaves peptide bonds on the carboxylside of proline in proteins of relatively small molecular mass. Proline 257-264 prolyl endopeptidase Homo sapiens 142-162 8318538-1 1993 Prolylendopeptidase is a cytoplasmic serine proteinase which hydrolyses peptide bonds at the C-terminal side of prolines. Proline 112-120 prolyl endopeptidase Homo sapiens 0-19 1355343-1 1992 Prolyl endopeptidase and dipeptidyl peptidase IV are serine proteases which cleave the peptide bonds at the carboxy group of proline residues. Proline 125-132 prolyl endopeptidase Homo sapiens 0-20 1590775-2 1992 Peptidyldiazomethanes with proline in the P1 position were found to be competitive slow-binding inhibitors of prolyl endopeptidase. Proline 27-34 prolyl endopeptidase Homo sapiens 110-130 23562579-1 2013 Prolyl oligopeptidase (EC 3.4.21.26, PREP) is a serine protease that hydrolyzes proline-containing peptides shorter than 30-mer but it has also nonhydrolytic functions. Proline 80-87 prolyl endopeptidase Homo sapiens 0-21 23562579-1 2013 Prolyl oligopeptidase (EC 3.4.21.26, PREP) is a serine protease that hydrolyzes proline-containing peptides shorter than 30-mer but it has also nonhydrolytic functions. Proline 80-87 prolyl endopeptidase Homo sapiens 37-41