PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23579020-3 2013 Dipeptidyl peptidases II and IV (DPPII and DPPIV) are serine proteases removing N-terminal dipeptides from polypeptides and proteins with proline or alanine on the penultimate position. Proline 138-145 dipeptidyl peptidase 4 Homo sapiens 43-48 25140306-1 2014 A cell surface serine protease, dipeptidyl peptidase 4 (DPP-4), cleaves dipeptide from peptides containing proline or alanine in the N-terminal penultimate position. Proline 107-114 dipeptidyl peptidase 4 Homo sapiens 32-54 25140306-1 2014 A cell surface serine protease, dipeptidyl peptidase 4 (DPP-4), cleaves dipeptide from peptides containing proline or alanine in the N-terminal penultimate position. Proline 107-114 dipeptidyl peptidase 4 Homo sapiens 56-61 24038034-1 2013 DPP8 and DPP9 are recently identified members of the dipeptidyl peptidase IV (DPPIV) enzyme family, which is characterized by the rare ability to cleave a post-proline bond two residues from the N-terminus of a substrate. Proline 160-167 dipeptidyl peptidase 4 Homo sapiens 53-76 24038034-1 2013 DPP8 and DPP9 are recently identified members of the dipeptidyl peptidase IV (DPPIV) enzyme family, which is characterized by the rare ability to cleave a post-proline bond two residues from the N-terminus of a substrate. Proline 160-167 dipeptidyl peptidase 4 Homo sapiens 78-83 23637126-1 2013 Dipeptidylpeptidase (DPP) 4 has the potential to truncate proteins with a penultimate alanine, proline, or other selective amino acids at the N-terminus. Proline 95-102 dipeptidyl peptidase 4 Homo sapiens 0-27 23677473-3 2013 DPPIV is a serine protease present in extracellular fluids that cleaves peptides with a proline or alanine in the second position. Proline 88-95 dipeptidyl peptidase 4 Homo sapiens 0-5 23519473-1 2013 Dipeptidyl peptidases (DP) 8 and 9 are homologous, cytoplasmic N-terminal post-proline-cleaving enzymes that are anti-targets for the development of DP4 (DPPIV/CD26) inhibitors for treating type II diabetes. Proline 79-86 dipeptidyl peptidase 4 Homo sapiens 154-159 22525314-3 2012 The inhibitors displayed inhibitory potency in the micromolar to nanomolar range and showed good to excellent selectivity with respect to the proline selective dipeptidyl peptidases (DPPs) DPP IV, DPP9 and DPP II. Proline 142-149 dipeptidyl peptidase 4 Homo sapiens 189-195 22726613-0 2012 Discovering novel alpha-aminoacyl-containing proline derivatives with potent and selective inhibitory activity against dipeptidyl peptidase IV: design, synthesis, biological evaluation, and molecular modeling. Proline 45-52 dipeptidyl peptidase 4 Homo sapiens 119-142 22561447-1 2012 BACKGROUND: Dipeptidyl peptidase 4 (DP4) is a serine protease that preferentially cleaves N-terminal dipeptides from polypeptides containing proline or alanine as the penultimate amino acid. Proline 141-148 dipeptidyl peptidase 4 Homo sapiens 12-34 22561447-1 2012 BACKGROUND: Dipeptidyl peptidase 4 (DP4) is a serine protease that preferentially cleaves N-terminal dipeptides from polypeptides containing proline or alanine as the penultimate amino acid. Proline 141-148 dipeptidyl peptidase 4 Homo sapiens 36-39 21834515-0 2011 Proline in transmembrane domain of type II protein DPP-IV governs its translocation behavior through endoplasmic reticulum. Proline 0-7 dipeptidyl peptidase 4 Homo sapiens 51-57 22001206-1 2011 The dipeptidyl peptidase (DPP) family members, including DPP-IV, DPP8, DPP9 and others, cleave the peptide bond after the penultimate proline residue and are drug target rich. Proline 134-141 dipeptidyl peptidase 4 Homo sapiens 57-63 23675206-1 2010 Functioning as an extracellular protease, dipeptidyl peptidase IV (DPP-IV) preferentially cleaves the peptide bond after the penultimate proline residue. Proline 137-144 dipeptidyl peptidase 4 Homo sapiens 42-65 21510839-1 2011 Dipeptidyl peptidase-IV (DPP-IV), a serine protease that specifically cleaves the N-terminal dipeptide with a preference for L-proline or L-alanine at the penultimate position, is involved in the degradation of incretin hormones, including glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP). Proline 125-134 dipeptidyl peptidase 4 Homo sapiens 0-23 21510839-1 2011 Dipeptidyl peptidase-IV (DPP-IV), a serine protease that specifically cleaves the N-terminal dipeptide with a preference for L-proline or L-alanine at the penultimate position, is involved in the degradation of incretin hormones, including glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP). Proline 125-134 dipeptidyl peptidase 4 Homo sapiens 25-31 23675206-1 2010 Functioning as an extracellular protease, dipeptidyl peptidase IV (DPP-IV) preferentially cleaves the peptide bond after the penultimate proline residue. Proline 137-144 dipeptidyl peptidase 4 Homo sapiens 67-73 20540760-5 2010 Structural comparisons with prolylendopeptidase and DPP4 identify the S1 proline binding site of PRCP. Proline 73-80 dipeptidyl peptidase 4 Homo sapiens 52-56 20572019-8 2010 However, these TM proline mutations result in a significant reduction of DPP-IV enzymatic activity, comparable to what is found with mutations near the active site. Proline 18-25 dipeptidyl peptidase 4 Homo sapiens 73-79 20406072-3 2010 DPP IV removes the two amino-terminal amino acids (Ser and Pro) from BNP(1-32) to produce BNP(3-32), which has been detected in plasma of patients with heart failure. Proline 59-62 dipeptidyl peptidase 4 Homo sapiens 0-6 19545486-2 2009 Just a small number of proline-specific hydrolases including dipeptidyl peptidase IV (DPP-IV) and related molecules is capable of cleaving such post-prolyl bond. Proline 23-30 dipeptidyl peptidase 4 Homo sapiens 61-84 19217790-4 2009 DPP-4, a protease that specifically cleaves dipeptides from proteins and oligopeptides after a penultimate N-terminal proline or alanine, is involved in the degradation of a number of neuropeptides, peptide hormones and cytokines, including the incretins GLP-1 and GIP. Proline 118-125 dipeptidyl peptidase 4 Homo sapiens 0-5 19545486-2 2009 Just a small number of proline-specific hydrolases including dipeptidyl peptidase IV (DPP-IV) and related molecules is capable of cleaving such post-prolyl bond. Proline 23-30 dipeptidyl peptidase 4 Homo sapiens 86-92 17676345-1 2007 Dipeptidyl peptidase IV (DPP-IV) deactivates the incretin hormones GLP-1 and GIP by cleaving the penultimate proline or alanine from the N-terminal (P1-position) of the peptide. Proline 109-116 dipeptidyl peptidase 4 Homo sapiens 0-23 23495778-1 2008 BACKGROUND: The dipeptidyl peptidase-IV (DPP-IV) family has outgrown its humble origins as a simple enzymatic activity cleaving dipeptides from peptides with an accessible N-terminal penultimate proline with no clear role in metabolism. Proline 195-202 dipeptidyl peptidase 4 Homo sapiens 16-39 23495778-1 2008 BACKGROUND: The dipeptidyl peptidase-IV (DPP-IV) family has outgrown its humble origins as a simple enzymatic activity cleaving dipeptides from peptides with an accessible N-terminal penultimate proline with no clear role in metabolism. Proline 195-202 dipeptidyl peptidase 4 Homo sapiens 41-47 17676345-1 2007 Dipeptidyl peptidase IV (DPP-IV) deactivates the incretin hormones GLP-1 and GIP by cleaving the penultimate proline or alanine from the N-terminal (P1-position) of the peptide. Proline 109-116 dipeptidyl peptidase 4 Homo sapiens 25-31 17113301-3 2007 To discover a structure for the gamma-substituent of the proline moiety more suitable for interacting with the S(2) pocket of DPP-IV, optimization focused on the gamma-substituent was carried out. Proline 57-64 dipeptidyl peptidase 4 Homo sapiens 126-132 17317162-1 2007 In the search for an inhibitor of dipeptidyl peptidase IV (DPP-IV) highly potent both in vitro and in vivo, we synthesized a series of L-prolylthiazolidine-based DPP-IV inhibitors having 4-arylpiperazine or 4-arylpiperidine at the gamma-position of the proline structure. Proline 253-260 dipeptidyl peptidase 4 Homo sapiens 34-57 17317162-1 2007 In the search for an inhibitor of dipeptidyl peptidase IV (DPP-IV) highly potent both in vitro and in vivo, we synthesized a series of L-prolylthiazolidine-based DPP-IV inhibitors having 4-arylpiperazine or 4-arylpiperidine at the gamma-position of the proline structure. Proline 253-260 dipeptidyl peptidase 4 Homo sapiens 59-65 17300591-3 2007 These drugs reversibly block DPP-IV-mediated inactivation of incretin hormones, for example, glucagon-like peptide 1 (GLP-1) and also other peptides that have alanine or proline as the penultimate N-terminal amino acid. Proline 170-177 dipeptidyl peptidase 4 Homo sapiens 29-35 17113301-6 2007 Indoline compounds such as 22e have a rigid conformation with double restriction of the aromatic moiety by proline and indoline structures to promote interaction with the binding site in the S(2) pocket of DPP-IV. Proline 107-114 dipeptidyl peptidase 4 Homo sapiens 206-212 17352682-2 2007 This review will mainly focus on proline-specific dipeptidyl peptidases related to DPP IV: fibroblast activation protein (FAP), dipeptidyl peptidase 8 (DPP8), dipeptidyl peptidase 9 (DPP9) and dipeptidyl peptidase II (DPP II). Proline 33-40 dipeptidyl peptidase 4 Homo sapiens 83-89 16913724-2 2006 DPP IV has high substrate selectivity for peptides with a proline (or an alanine) at the penultimate amino acid position at the N-terminus but tolerates a wide range of natural amino acids at the amino terminal end. Proline 58-65 dipeptidyl peptidase 4 Homo sapiens 0-6 16376544-1 2006 The co-crystal structure of beta-phenethylamine fragment inhibitor 5 bound to DPP-IV revealed that the phenyl ring occupied the proline pocket of the enzyme. Proline 128-135 dipeptidyl peptidase 4 Homo sapiens 78-84 16756746-3 2006 After secretion, dipeptidyl peptidase IV (DPP-IV) cleaves the N-terminal Tyrosine-Proline residues from PYY(1-36), producing PYY(3-36). Proline 82-89 dipeptidyl peptidase 4 Homo sapiens 17-40 16756746-3 2006 After secretion, dipeptidyl peptidase IV (DPP-IV) cleaves the N-terminal Tyrosine-Proline residues from PYY(1-36), producing PYY(3-36). Proline 82-89 dipeptidyl peptidase 4 Homo sapiens 42-48 16687037-7 2006 After release, dipeptidyl peptidase IV (DPP-IV; CD 26) cleaves the N-terminal tyrosine-proline residues forming PYY(3-36). Proline 87-94 dipeptidyl peptidase 4 Homo sapiens 15-38 16687037-7 2006 After release, dipeptidyl peptidase IV (DPP-IV; CD 26) cleaves the N-terminal tyrosine-proline residues forming PYY(3-36). Proline 87-94 dipeptidyl peptidase 4 Homo sapiens 40-46 16769036-1 2006 Dipeptidyl peptidase IV (DPP-IV) and seprase belong to a small group of membrane-bound, proline-specific serine proteases, the serine integral membrane proteases (SIMPs). Proline 88-95 dipeptidyl peptidase 4 Homo sapiens 0-23 16769036-1 2006 Dipeptidyl peptidase IV (DPP-IV) and seprase belong to a small group of membrane-bound, proline-specific serine proteases, the serine integral membrane proteases (SIMPs). Proline 88-95 dipeptidyl peptidase 4 Homo sapiens 25-31 16321524-1 2006 Dipeptidyl peptidase IV is a clinically validated target for type-2 diabetes and belongs to a family of peptidases with a quite unique post-proline cleavage specificity. Proline 140-147 dipeptidyl peptidase 4 Homo sapiens 0-23 16388667-0 2006 Proline-catalyzed, asymmetric mannich reactions in the synthesis of a DPP-IV inhibitor. Proline 0-7 dipeptidyl peptidase 4 Homo sapiens 70-76 15380217-1 2004 In-house screening of the Merck sample collection identified proline derived homophenylalanine 3 as a DPP-IV inhibitor with modest potency (DPP-IV IC50=1.9 microM). Proline 61-68 dipeptidyl peptidase 4 Homo sapiens 102-108 15448155-1 2004 DPP-IV is a prolyl dipeptidase, cleaving the peptide bond after the penultimate proline residue. Proline 80-87 dipeptidyl peptidase 4 Homo sapiens 0-6 15380217-1 2004 In-house screening of the Merck sample collection identified proline derived homophenylalanine 3 as a DPP-IV inhibitor with modest potency (DPP-IV IC50=1.9 microM). Proline 61-68 dipeptidyl peptidase 4 Homo sapiens 140-146 15375776-3 2004 The substrates of CD26/DPPIV are proline-containing peptides and include growth factors, chemokines, neuropeptides, and vasoactive peptides. Proline 33-40 dipeptidyl peptidase 4 Homo sapiens 18-22 15375776-3 2004 The substrates of CD26/DPPIV are proline-containing peptides and include growth factors, chemokines, neuropeptides, and vasoactive peptides. Proline 33-40 dipeptidyl peptidase 4 Homo sapiens 23-28 15245913-1 2004 Dipeptidyl peptidase (DP) IV has a distinct substrate specificity in hydrolyzing a post-proline bond. Proline 88-95 dipeptidyl peptidase 4 Homo sapiens 0-28 14579742-3 2003 CD26/DPPIV catalyzes cleavage of peptides from the amino terminus of peptides with proline at the penultimate position. Proline 83-90 dipeptidyl peptidase 4 Homo sapiens 0-4 14579742-3 2003 CD26/DPPIV catalyzes cleavage of peptides from the amino terminus of peptides with proline at the penultimate position. Proline 83-90 dipeptidyl peptidase 4 Homo sapiens 5-10 12471135-3 2002 CD26/DPPIV has the ability to cleave the chemokine CXCL12/stromal cell-derived factor 1alpha (SDF-1alpha) at its position two proline. Proline 126-133 dipeptidyl peptidase 4 Homo sapiens 0-4 12471135-3 2002 CD26/DPPIV has the ability to cleave the chemokine CXCL12/stromal cell-derived factor 1alpha (SDF-1alpha) at its position two proline. Proline 126-133 dipeptidyl peptidase 4 Homo sapiens 5-10 12101279-2 2002 Purified DPP IV has been recognized to inactivate peptide hormones, neuropeptides, and some chemokines by cleavage behind a proline residue at the penultimate N-terminal amino acid position. Proline 124-131 dipeptidyl peptidase 4 Homo sapiens 9-15 11755200-5 2001 Among the rare group of proline-specific proteases, dipeptidyl peptidase IV (DPP-IV, EC 3.4.14.5) was originally believed to be the only membrane-bound enzyme specific for proline as the penultimate residue at the amino-terminus of the polypeptide chain. Proline 24-31 dipeptidyl peptidase 4 Homo sapiens 52-75 11755200-5 2001 Among the rare group of proline-specific proteases, dipeptidyl peptidase IV (DPP-IV, EC 3.4.14.5) was originally believed to be the only membrane-bound enzyme specific for proline as the penultimate residue at the amino-terminus of the polypeptide chain. Proline 24-31 dipeptidyl peptidase 4 Homo sapiens 77-83 11755200-5 2001 Among the rare group of proline-specific proteases, dipeptidyl peptidase IV (DPP-IV, EC 3.4.14.5) was originally believed to be the only membrane-bound enzyme specific for proline as the penultimate residue at the amino-terminus of the polypeptide chain. Proline 172-179 dipeptidyl peptidase 4 Homo sapiens 52-75 11755200-5 2001 Among the rare group of proline-specific proteases, dipeptidyl peptidase IV (DPP-IV, EC 3.4.14.5) was originally believed to be the only membrane-bound enzyme specific for proline as the penultimate residue at the amino-terminus of the polypeptide chain. Proline 172-179 dipeptidyl peptidase 4 Homo sapiens 77-83 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 dipeptidyl peptidase 4 Homo sapiens 57-80 11389867-1 2001 A proline-specific dipeptidyl aminopeptidase, dipeptidyl peptidase IV (EC 3.4.14.5), was purified from a cell sonicate soluble fraction of Prevotella loescheii ATCC 15930 by sequential column chromatography. Proline 2-9 dipeptidyl peptidase 4 Homo sapiens 46-69 11227212-1 2000 We recently isolated and cloned an intracellular post-proline cleaving aminodipeptidase, quiescent cell proline dipeptidase (QPP), which has a substrate specificity very similar to that of dipeptidyl peptidase IV (CD26/DPPIV). Proline 54-61 dipeptidyl peptidase 4 Homo sapiens 189-212 11227212-1 2000 We recently isolated and cloned an intracellular post-proline cleaving aminodipeptidase, quiescent cell proline dipeptidase (QPP), which has a substrate specificity very similar to that of dipeptidyl peptidase IV (CD26/DPPIV). Proline 54-61 dipeptidyl peptidase 4 Homo sapiens 214-218 11227212-1 2000 We recently isolated and cloned an intracellular post-proline cleaving aminodipeptidase, quiescent cell proline dipeptidase (QPP), which has a substrate specificity very similar to that of dipeptidyl peptidase IV (CD26/DPPIV). Proline 54-61 dipeptidyl peptidase 4 Homo sapiens 219-224 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 dipeptidyl peptidase 4 Homo sapiens 82-87 10678923-0 2000 Emerging family of proline-specific peptidases of Porphyromonas gingivalis: purification and characterization of serine dipeptidyl peptidase, a structural and functional homologue of mammalian prolyl dipeptidyl peptidase IV. Proline 19-26 dipeptidyl peptidase 4 Homo sapiens 200-223 10701757-1 2000 Proline-specific dipeptidyl peptidase (DPP IV) is an established enzyme known to degrade neuropeptides and peptide hormones in vertebrate tissues. Proline 0-7 dipeptidyl peptidase 4 Homo sapiens 39-45 11467771-2 2000 DPPIV has numerous functions including involvement in T-cell activation, cell adhesion, digestion of proline containing peptides in the kidney and intestines, HIV infection and apoptosis, and regulation of tumorigenicity in certain melanoma cells. Proline 101-108 dipeptidyl peptidase 4 Homo sapiens 0-5 10373631-2 1999 The post proline cleaving substrate specificity makes DP IV relatively unique among other proteases. Proline 9-16 dipeptidyl peptidase 4 Homo sapiens 54-59 10567372-8 1999 The putative active site residues serine, aspartic acid, and histidine of QPP show an ordering of the catalytic triad similar to that seen in the post-proline cleaving exopeptidases prolylcarboxypeptidase and CD26/dipeptidyl peptidase IV. Proline 151-158 dipeptidyl peptidase 4 Homo sapiens 209-213 10567372-8 1999 The putative active site residues serine, aspartic acid, and histidine of QPP show an ordering of the catalytic triad similar to that seen in the post-proline cleaving exopeptidases prolylcarboxypeptidase and CD26/dipeptidyl peptidase IV. Proline 151-158 dipeptidyl peptidase 4 Homo sapiens 214-237 9826645-1 1998 Dipeptidyl peptidase IV (EC 3.4.14.5; DPP IV), also known as the leukocyte differentiation antigen CD26 when found as an extracellular membrane-bound proline specific serine protease, cleaves a dipeptide from the N terminus of a polypeptide chain containing a proline residue in the penultimate position. Proline 150-157 dipeptidyl peptidase 4 Homo sapiens 0-23 10202035-3 1999 Human eotaxin has a penultimate proline, indicating that it might be a substrate for dipeptidyl-peptidase IV (CD26/DPP IV). Proline 32-39 dipeptidyl peptidase 4 Homo sapiens 85-108 10101215-3 1999 The following aspects of DPP IV/CD26 will be discussed : the structure of DPP IV and the new family of serine proteases to which it belongs, the substrate specificity, the distribution in the human body, specific DPP IV inhibitors and the role of CD26 in the intestinal and renal handling of proline containing peptides, in cell adhesion, in peptide metabolism, in the immune system and in HIV infection. Proline 292-299 dipeptidyl peptidase 4 Homo sapiens 25-31 10101215-3 1999 The following aspects of DPP IV/CD26 will be discussed : the structure of DPP IV and the new family of serine proteases to which it belongs, the substrate specificity, the distribution in the human body, specific DPP IV inhibitors and the role of CD26 in the intestinal and renal handling of proline containing peptides, in cell adhesion, in peptide metabolism, in the immune system and in HIV infection. Proline 292-299 dipeptidyl peptidase 4 Homo sapiens 32-36 9826645-1 1998 Dipeptidyl peptidase IV (EC 3.4.14.5; DPP IV), also known as the leukocyte differentiation antigen CD26 when found as an extracellular membrane-bound proline specific serine protease, cleaves a dipeptide from the N terminus of a polypeptide chain containing a proline residue in the penultimate position. Proline 150-157 dipeptidyl peptidase 4 Homo sapiens 38-44 9826645-1 1998 Dipeptidyl peptidase IV (EC 3.4.14.5; DPP IV), also known as the leukocyte differentiation antigen CD26 when found as an extracellular membrane-bound proline specific serine protease, cleaves a dipeptide from the N terminus of a polypeptide chain containing a proline residue in the penultimate position. Proline 150-157 dipeptidyl peptidase 4 Homo sapiens 99-103 9826645-1 1998 Dipeptidyl peptidase IV (EC 3.4.14.5; DPP IV), also known as the leukocyte differentiation antigen CD26 when found as an extracellular membrane-bound proline specific serine protease, cleaves a dipeptide from the N terminus of a polypeptide chain containing a proline residue in the penultimate position. Proline 260-267 dipeptidyl peptidase 4 Homo sapiens 0-23 9826645-1 1998 Dipeptidyl peptidase IV (EC 3.4.14.5; DPP IV), also known as the leukocyte differentiation antigen CD26 when found as an extracellular membrane-bound proline specific serine protease, cleaves a dipeptide from the N terminus of a polypeptide chain containing a proline residue in the penultimate position. Proline 260-267 dipeptidyl peptidase 4 Homo sapiens 38-44 9826645-1 1998 Dipeptidyl peptidase IV (EC 3.4.14.5; DPP IV), also known as the leukocyte differentiation antigen CD26 when found as an extracellular membrane-bound proline specific serine protease, cleaves a dipeptide from the N terminus of a polypeptide chain containing a proline residue in the penultimate position. Proline 260-267 dipeptidyl peptidase 4 Homo sapiens 99-103 35053615-7 2022 CD26/dipeptidyl peptidase 4 (DPP4) functions as a serine protease, selectively cleaving polypeptides with a proline or alanine at the penultimate N-terminal position, such as chemokines. Proline 108-115 dipeptidyl peptidase 4 Homo sapiens 0-27 9622551-1 1998 The dipeptidyl peptidase IV (DPP IV) activity of CD26 is characterized by its post-proline-cleaving capacity that plays an important but not yet understood role in biological processes. Proline 83-90 dipeptidyl peptidase 4 Homo sapiens 4-27 9622551-1 1998 The dipeptidyl peptidase IV (DPP IV) activity of CD26 is characterized by its post-proline-cleaving capacity that plays an important but not yet understood role in biological processes. Proline 83-90 dipeptidyl peptidase 4 Homo sapiens 29-35 9622551-1 1998 The dipeptidyl peptidase IV (DPP IV) activity of CD26 is characterized by its post-proline-cleaving capacity that plays an important but not yet understood role in biological processes. Proline 83-90 dipeptidyl peptidase 4 Homo sapiens 49-53 9622551-3 1998 Taking into account the substrate specificity of DPP IV for P2-P1><-P1" cleavage, we have designed and synthesized cyclopeptides c[(alphaH2N+)-Lys-Pro-Aba-(6-CH2-S+R2)-Glyn] 2TFA- (Aba = 3-aminobenzoic acid, R = alkyl) possessing a proline at the P1 position and a lysine in the P2 position, which allows the closing of the cycle on its side chain. Proline 238-245 dipeptidyl peptidase 4 Homo sapiens 49-55 9149329-1 1997 Previous research in this laboratory has shown that major depression is accompanied by decreased serum activity of dipeptidyl peptidase IV (DPP IV), a serine protease that cleaves N terminal dipeptides from peptides with penultimate proline or alanine. Proline 233-240 dipeptidyl peptidase 4 Homo sapiens 115-138 9149329-1 1997 Previous research in this laboratory has shown that major depression is accompanied by decreased serum activity of dipeptidyl peptidase IV (DPP IV), a serine protease that cleaves N terminal dipeptides from peptides with penultimate proline or alanine. Proline 233-240 dipeptidyl peptidase 4 Homo sapiens 140-146 8706727-1 1996 The T-cell activation antigen CD26, is a type II membrane glycoprotein with intrinsic dipeptidyl-peptidase IV (DPP IV) activity, characterized by its capacity to cleave off N-terminal dipeptides containing proline as the penultimate residue. Proline 206-213 dipeptidyl peptidase 4 Homo sapiens 30-34 8706727-1 1996 The T-cell activation antigen CD26, is a type II membrane glycoprotein with intrinsic dipeptidyl-peptidase IV (DPP IV) activity, characterized by its capacity to cleave off N-terminal dipeptides containing proline as the penultimate residue. Proline 206-213 dipeptidyl peptidase 4 Homo sapiens 86-109 8706727-1 1996 The T-cell activation antigen CD26, is a type II membrane glycoprotein with intrinsic dipeptidyl-peptidase IV (DPP IV) activity, characterized by its capacity to cleave off N-terminal dipeptides containing proline as the penultimate residue. Proline 206-213 dipeptidyl peptidase 4 Homo sapiens 111-117 7911611-1 1994 Dipeptidyl peptidase IV (DPP IV, EC 3.4.14.5) is a highly specific serine protease which cleaves off N-terminal dipeptides from peptides with a penultimate proline or alanine. Proline 156-163 dipeptidyl peptidase 4 Homo sapiens 0-23 7911611-1 1994 Dipeptidyl peptidase IV (DPP IV, EC 3.4.14.5) is a highly specific serine protease which cleaves off N-terminal dipeptides from peptides with a penultimate proline or alanine. Proline 156-163 dipeptidyl peptidase 4 Homo sapiens 25-31 7911611-7 1994 N-Peptidyl-O-acylhydroxylamines and boronic acid analogues of proline and alanine are two known DPP IV inhibitors. Proline 62-69 dipeptidyl peptidase 4 Homo sapiens 96-102 8100523-2 1993 They either start with Tyr-Ala, His-Ala or His-Ser which might be in part potential targets for dipeptidyl-peptidase IV, a highly specialized aminopeptidase removing dipeptides only from peptides with N-terminal penultimate proline or alanine. Proline 224-231 dipeptidyl peptidase 4 Homo sapiens 96-119 1361094-1 1992 The N-terminus of bradykinin is shown to be sequentially degraded by the human proline-specific aminopeptidases aminopeptidase P (EC 3.4.11.9) and dipeptidyl peptidase IV (EC 3.4.14.5). Proline 79-86 dipeptidyl peptidase 4 Homo sapiens 147-170 34783283-4 2021 Angiotensin-converting enzyme (ACE) (hypertension-responsible glycoprotein) and dipeptidyl peptidase IV (DPP-IV) (proline-specific dimeric aminopeptidase) have been widely used as molecular target sites of action of bioactive compounds possessing antihypertensive and antidiabetic effects. Proline 114-121 dipeptidyl peptidase 4 Homo sapiens 80-103 34783283-4 2021 Angiotensin-converting enzyme (ACE) (hypertension-responsible glycoprotein) and dipeptidyl peptidase IV (DPP-IV) (proline-specific dimeric aminopeptidase) have been widely used as molecular target sites of action of bioactive compounds possessing antihypertensive and antidiabetic effects. Proline 114-121 dipeptidyl peptidase 4 Homo sapiens 105-111 34575782-0 2021 Proline-Specific Fungal Peptidases: Genomic Analysis and Identification of Secreted DPP4 in Alkaliphilic and Alkalitolerant Fungi. Proline 0-7 dipeptidyl peptidase 4 Homo sapiens 84-88 9183643-1 1996 CD26 is a 110 kDa T cell activation antigen and has been shown to have DPPIV enzyme activity which cleaves amino-terminal dipeptides with either L-proline or L-alanine at the penultimate position. Proline 145-154 dipeptidyl peptidase 4 Homo sapiens 0-4 8897476-5 1996 These approaches reveal that NPY is processed at its N-terminus by two proline-preferring aminopeptidases: aminopeptidase P and dipeptidyl peptidase IV. Proline 71-78 dipeptidyl peptidase 4 Homo sapiens 128-151 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 dipeptidyl peptidase 4 Homo sapiens 25-48 1671716-4 1991 Here we report that Ala-boroPro and Pro-boroPro, where boroPro is the alpha-amino boronic acid analog of proline, are potent and specific inhibitors of DP-IV, having Ki values in the nanomolar range. Proline 105-112 dipeptidyl peptidase 4 Homo sapiens 152-157 1671823-1 1991 Dipeptidyl peptidase IV preferably hydrolyzes peptides and proteins with a penultimate proline residue. Proline 87-94 dipeptidyl peptidase 4 Homo sapiens 0-23 1671823-5 1991 We could show that both compounds as well as other tripeptides with a penultimate proline residue are substrates for dipeptidyl peptidase IV. Proline 82-89 dipeptidyl peptidase 4 Homo sapiens 117-140 35053615-7 2022 CD26/dipeptidyl peptidase 4 (DPP4) functions as a serine protease, selectively cleaving polypeptides with a proline or alanine at the penultimate N-terminal position, such as chemokines. Proline 108-115 dipeptidyl peptidase 4 Homo sapiens 29-33 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 dipeptidyl peptidase 4 Homo sapiens 29-51 6152335-0 1984 Similarities of the substrate cleavage catalyzed by proline specific endopeptidase and dipeptidyl peptidase IV. Proline 52-59 dipeptidyl peptidase 4 Homo sapiens 87-110 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 dipeptidyl peptidase 4 Homo sapiens 53-57 30255759-1 2019 BACKGROUND: Dipeptidyl Peptidase 4 (DPP 4) enzyme cleaves an incretin-based glucoregulatory hormone Glucagon Like Peptide -1 from N-terminal where penultimate amino acid is either alanine or proline. Proline 191-198 dipeptidyl peptidase 4 Homo sapiens 12-34 31357088-1 2019 Dipeptidyl peptidase 4 (DPP-4) is a serine protease, which has enzymatic activity to selectively clean the N-terminal dipeptide of peptides and proteins with proline or alanine in the second position. Proline 158-165 dipeptidyl peptidase 4 Homo sapiens 0-22 31357088-1 2019 Dipeptidyl peptidase 4 (DPP-4) is a serine protease, which has enzymatic activity to selectively clean the N-terminal dipeptide of peptides and proteins with proline or alanine in the second position. Proline 158-165 dipeptidyl peptidase 4 Homo sapiens 24-29 30255759-1 2019 BACKGROUND: Dipeptidyl Peptidase 4 (DPP 4) enzyme cleaves an incretin-based glucoregulatory hormone Glucagon Like Peptide -1 from N-terminal where penultimate amino acid is either alanine or proline. Proline 191-198 dipeptidyl peptidase 4 Homo sapiens 36-41 27395781-1 2016 Dipeptidyl peptidase 4 (DPP 4) is a proline specific serine peptidase that plays an important role in different regulatory processes in mammals. Proline 36-43 dipeptidyl peptidase 4 Homo sapiens 24-29 29963014-6 2018 The DPP-IV half maximal inhibitory concentration (IC50) values of the 25 peptides evaluated ranged from 3.9 +- 1.0 microM (Ile-Pro-Ile) to 247.0 +- 32.7 microM (Phe-Pro-Phe). Proline 127-130 dipeptidyl peptidase 4 Homo sapiens 4-10 29963014-6 2018 The DPP-IV half maximal inhibitory concentration (IC50) values of the 25 peptides evaluated ranged from 3.9 +- 1.0 microM (Ile-Pro-Ile) to 247.0 +- 32.7 microM (Phe-Pro-Phe). Proline 165-168 dipeptidyl peptidase 4 Homo sapiens 4-10 27484974-1 2016 Dipeptidyl peptidase-4 (DPP-4), glycyl-prolyl-naphthylamidase, is a serine protease that catalyzes the hydrolysis of various proline-containing polypeptides. Proline 125-132 dipeptidyl peptidase 4 Homo sapiens 0-22 27484974-1 2016 Dipeptidyl peptidase-4 (DPP-4), glycyl-prolyl-naphthylamidase, is a serine protease that catalyzes the hydrolysis of various proline-containing polypeptides. Proline 125-132 dipeptidyl peptidase 4 Homo sapiens 24-29 29806214-1 2019 Dipeptidyl peptidase-4 (DPP-4) cleaves N-terminal dipeptides, with Pro, Ala or Ser at the penultimate position, and, in that way, modulates biological activity of certain polypeptides. Proline 67-70 dipeptidyl peptidase 4 Homo sapiens 0-22 29806214-1 2019 Dipeptidyl peptidase-4 (DPP-4) cleaves N-terminal dipeptides, with Pro, Ala or Ser at the penultimate position, and, in that way, modulates biological activity of certain polypeptides. Proline 67-70 dipeptidyl peptidase 4 Homo sapiens 24-29 30007720-4 2018 beta-casomorphin (BCM) from milk casein, gluteomorphin (GM) from wheat gluten, and soymorphin (SM) from the soybean beta-conglycinin beta-subunit are natural substrates of DPPIV because of their amino acid sequences and proline location. Proline 220-227 dipeptidyl peptidase 4 Homo sapiens 172-177 29426867-1 2018 Dipeptidyl peptidase IV (DPP IV, DPP4, or DAP IV) preferentially cleaves substrate peptides with Pro or Ala at the P1 position. Proline 97-100 dipeptidyl peptidase 4 Homo sapiens 0-23 29426867-1 2018 Dipeptidyl peptidase IV (DPP IV, DPP4, or DAP IV) preferentially cleaves substrate peptides with Pro or Ala at the P1 position. Proline 97-100 dipeptidyl peptidase 4 Homo sapiens 25-31 29426867-1 2018 Dipeptidyl peptidase IV (DPP IV, DPP4, or DAP IV) preferentially cleaves substrate peptides with Pro or Ala at the P1 position. Proline 97-100 dipeptidyl peptidase 4 Homo sapiens 33-37 27410463-1 2016 The enzyme members of the dipeptidyl peptidase 4 (DPP4) gene family have the very unusual capacity to cleave the post-proline bond to release dipeptides from the N-terminus of peptide/protein substrates. Proline 118-125 dipeptidyl peptidase 4 Homo sapiens 26-48 27410463-1 2016 The enzyme members of the dipeptidyl peptidase 4 (DPP4) gene family have the very unusual capacity to cleave the post-proline bond to release dipeptides from the N-terminus of peptide/protein substrates. Proline 118-125 dipeptidyl peptidase 4 Homo sapiens 50-54 25723507-3 2015 Dipeptidyl peptidase 4 (DPP4) cleaves N-terminal dipeptides from polypeptides when the second residue is proline, hydroxyproline, dehydroproline or alanine. Proline 105-112 dipeptidyl peptidase 4 Homo sapiens 0-22 25723507-3 2015 Dipeptidyl peptidase 4 (DPP4) cleaves N-terminal dipeptides from polypeptides when the second residue is proline, hydroxyproline, dehydroproline or alanine. Proline 105-112 dipeptidyl peptidase 4 Homo sapiens 24-28 24099035-1 2014 The proline-specific dipeptidyl aminopeptidase IV (DPP IV, DPP-4, CD26), widely expressed in mammalians, releases X-Pro/Ala dipeptides from the N-terminus of peptides. Proline 4-11 dipeptidyl peptidase 4 Homo sapiens 51-57 24099035-1 2014 The proline-specific dipeptidyl aminopeptidase IV (DPP IV, DPP-4, CD26), widely expressed in mammalians, releases X-Pro/Ala dipeptides from the N-terminus of peptides. Proline 4-11 dipeptidyl peptidase 4 Homo sapiens 59-64 24099035-1 2014 The proline-specific dipeptidyl aminopeptidase IV (DPP IV, DPP-4, CD26), widely expressed in mammalians, releases X-Pro/Ala dipeptides from the N-terminus of peptides. Proline 4-11 dipeptidyl peptidase 4 Homo sapiens 66-70 26919392-1 2016 CD26/DPP4 (dipeptidyl peptidase 4/DP4/DPPIV) is a surface T cell activation antigen and has been shown to have DPP4 enzymatic activity, cleaving-off amino-terminal dipeptides with either L-proline or L-alanine at the penultimate position. Proline 187-196 dipeptidyl peptidase 4 Homo sapiens 0-4 26919392-1 2016 CD26/DPP4 (dipeptidyl peptidase 4/DP4/DPPIV) is a surface T cell activation antigen and has been shown to have DPP4 enzymatic activity, cleaving-off amino-terminal dipeptides with either L-proline or L-alanine at the penultimate position. Proline 187-196 dipeptidyl peptidase 4 Homo sapiens 5-9 26919392-1 2016 CD26/DPP4 (dipeptidyl peptidase 4/DP4/DPPIV) is a surface T cell activation antigen and has been shown to have DPP4 enzymatic activity, cleaving-off amino-terminal dipeptides with either L-proline or L-alanine at the penultimate position. Proline 187-196 dipeptidyl peptidase 4 Homo sapiens 11-33 26919392-1 2016 CD26/DPP4 (dipeptidyl peptidase 4/DP4/DPPIV) is a surface T cell activation antigen and has been shown to have DPP4 enzymatic activity, cleaving-off amino-terminal dipeptides with either L-proline or L-alanine at the penultimate position. Proline 187-196 dipeptidyl peptidase 4 Homo sapiens 38-43 26919392-1 2016 CD26/DPP4 (dipeptidyl peptidase 4/DP4/DPPIV) is a surface T cell activation antigen and has been shown to have DPP4 enzymatic activity, cleaving-off amino-terminal dipeptides with either L-proline or L-alanine at the penultimate position. Proline 187-196 dipeptidyl peptidase 4 Homo sapiens 111-115 27431629-1 2016 CD26 is a 110 kDa, type II transmembrane glycoprotein with dipeptidyl peptidase IV activity and is capable of cleaving Nterminal dipeptides with either L-proline or L-alanine at the penultimate position. Proline 152-161 dipeptidyl peptidase 4 Homo sapiens 0-4 26988064-1 2016 BACKGROUND: Dipeptidyl peptidase 4 (DPP4; EC 3.4.14.5; CD26) is a membrane-bound or shedded serine protease that hydrolyzes dipeptides from the N-terminus of peptides with either proline or alanine at the penultimate position. Proline 179-186 dipeptidyl peptidase 4 Homo sapiens 12-34 26988064-1 2016 BACKGROUND: Dipeptidyl peptidase 4 (DPP4; EC 3.4.14.5; CD26) is a membrane-bound or shedded serine protease that hydrolyzes dipeptides from the N-terminus of peptides with either proline or alanine at the penultimate position. Proline 179-186 dipeptidyl peptidase 4 Homo sapiens 36-40 26988064-1 2016 BACKGROUND: Dipeptidyl peptidase 4 (DPP4; EC 3.4.14.5; CD26) is a membrane-bound or shedded serine protease that hydrolyzes dipeptides from the N-terminus of peptides with either proline or alanine at the penultimate position. Proline 179-186 dipeptidyl peptidase 4 Homo sapiens 55-59 25216328-2 2014 Both membrane-associated and soluble DPP4 exert catalytic activity, cleaving proteins containing a position 2 alanine or proline. Proline 121-128 dipeptidyl peptidase 4 Homo sapiens 37-41 24516103-2 2014 Dipeptidyl peptidase-4 degrades other peptides with a penultimate proline or alanine, including bradykinin and substance P, which are also substrates of angiotensin-converting enzyme (ACE). Proline 66-73 dipeptidyl peptidase 4 Homo sapiens 0-22