PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16622717-3 2006 Recently, we demonstrated that CD26 binds caveolin-1 on antigen-presenting cell (APC), and that residues 201-211 of CD26 along with the serine catalytic site at residue 630, which constitute a pocket structure of CD26/DPPIV, contribute to binding to caveolin-1 scaffolding domain. Serine 136-142 dipeptidyl peptidase 4 Homo sapiens 218-223 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. Serine 51-54 dipeptidyl peptidase 4 Homo sapiens 0-6 19327104-5 2009 DPP IV removes the two amino terminal amino acids (Ser Pro) from BNP(1-32) to produce BNP(3-32), which has been detected in plasma of patients with congestive heart failure. Serine 51-54 dipeptidyl peptidase 4 Homo sapiens 0-6 18227430-4 2008 To investigate whether this serine addition is assisted by the catalytic His-Asp dyad, we generated two mutants of DPP-IV, S630A and H740Q, and assayed them for ability to bind inhibitor. Serine 28-34 dipeptidyl peptidase 4 Homo sapiens 115-121 17884461-5 2007 The drugs against these enzymes engage important enzyme functional groups, such as the active site serine in dipeptidyl peptidase IV. Serine 99-105 dipeptidyl peptidase 4 Homo sapiens 109-132 20942971-9 2010 As opposed to the expression of Tat alone, serine phosphorylation of the Tat protein was decreased when co-expressed with human-DPPIV protein. Serine 43-49 dipeptidyl peptidase 4 Homo sapiens 128-133 16364232-1 2006 Dipeptidyl peptidase-IV (DPP-IV) is a serine protease with a signature Asp-His-Ser motif at the active site. Serine 79-82 dipeptidyl peptidase 4 Homo sapiens 0-23 16364232-1 2006 Dipeptidyl peptidase-IV (DPP-IV) is a serine protease with a signature Asp-His-Ser motif at the active site. Serine 79-82 dipeptidyl peptidase 4 Homo sapiens 25-31 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. Serine 34-40 dipeptidyl peptidase 4 Homo sapiens 209-213 12525257-10 2003 These data indicate that substitution of the penultimate Ala2 in GIP by Gly or Ser confers resistance to plasma DPP IV degradation, resulting in enhanced biological activity, therefore raising the possibility of their use in the treatment of type 2 diabetes. Serine 79-82 dipeptidyl peptidase 4 Homo sapiens 112-118 12459266-5 2002 The presence of this motif, together with a conserved order and spacing of the Ser, Asp, and His residues that form the catalytic triad in DPP IV, places DPP9 in the "DPP IV gene family". Serine 79-82 dipeptidyl peptidase 4 Homo sapiens 167-173 15476821-7 2004 Comparison of the active sites of DPPX and DPP-IV reveals loss of the catalytic serine residue but the presence of an additional serine near the "active" site. Serine 80-86 dipeptidyl peptidase 4 Homo sapiens 43-49 15476821-7 2004 Comparison of the active sites of DPPX and DPP-IV reveals loss of the catalytic serine residue but the presence of an additional serine near the "active" site. Serine 129-135 dipeptidyl peptidase 4 Homo sapiens 43-49 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. Serine 34-40 dipeptidyl peptidase 4 Homo sapiens 214-237 9685737-4 1998 However, the N-terminal amino acid sequence of serum DPP IV lacked the transmembrane domain of the membrane-bound enzyme and started at the 39th position, serine, from the N-terminus predicted from the cDNA nucleotide sequence. Serine 155-161 dipeptidyl peptidase 4 Homo sapiens 53-59 10570924-4 1999 This observation suggests a novel role in proteolysis for residues of DPP IV distant from the Ser-Asp-His catalytic triad. Serine 94-97 dipeptidyl peptidase 4 Homo sapiens 70-76 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. Serine 47-50 dipeptidyl peptidase 4 Homo sapiens 96-119 8951616-3 1996 One of the remarkable properties of DPPIV is that its activity is greatly enhanced by Gly-X (X: especially, Gly, Gln, Glu and Ser) dipeptides. Serine 126-129 dipeptidyl peptidase 4 Homo sapiens 36-41 8951616-2 1996 Serum DPPIV, a serine enzyme with an apparent mass of 250 kDa, consists of two identical subunits with an apparent mass of 100 kDa and is inhibited by DPPIV-specific inhibitor Diprotin A and also by p-chloromercuribenzoate (p-CMB), 2-mercaptoethanol, HgCl2, CdCl2, SrCl2, and ZnCl2. Serine 15-21 dipeptidyl peptidase 4 Homo sapiens 6-11 8951616-2 1996 Serum DPPIV, a serine enzyme with an apparent mass of 250 kDa, consists of two identical subunits with an apparent mass of 100 kDa and is inhibited by DPPIV-specific inhibitor Diprotin A and also by p-chloromercuribenzoate (p-CMB), 2-mercaptoethanol, HgCl2, CdCl2, SrCl2, and ZnCl2. Serine 15-21 dipeptidyl peptidase 4 Homo sapiens 151-156 34920066-1 2022 Dipeptidyl peptidase IV (DPP-IV, EC 3.4.14.5) is an abundant serine aminopeptidase that preferentially cleaves N-terminal Xaa-Pro or Xaa-Ala dipeptides from oligopeptides. Serine 61-67 dipeptidyl peptidase 4 Homo sapiens 0-23 7509871-1 1993 Prolyl endopeptidase (PEP) and dipeptidyl peptidase IV (DP IV) are serine enzymes cleaving highly specific prolyl peptide bonds. Serine 67-73 dipeptidyl peptidase 4 Homo sapiens 31-54 7509871-1 1993 Prolyl endopeptidase (PEP) and dipeptidyl peptidase IV (DP IV) are serine enzymes cleaving highly specific prolyl peptide bonds. Serine 67-73 dipeptidyl peptidase 4 Homo sapiens 56-61 1459244-6 1992 The consensus sequence surrounding the active site serine in the three known X-prolyl dipeptidyl aminopeptidases (mammalian DPPIV, yeast DPAB and PepX) is G-X-S-Y-X-G, where X is a non-conserved amino acid. Serine 51-57 dipeptidyl peptidase 4 Homo sapiens 124-129 34920066-1 2022 Dipeptidyl peptidase IV (DPP-IV, EC 3.4.14.5) is an abundant serine aminopeptidase that preferentially cleaves N-terminal Xaa-Pro or Xaa-Ala dipeptides from oligopeptides. Serine 61-67 dipeptidyl peptidase 4 Homo sapiens 25-31 34716325-0 2021 The serine proteases dipeptidyl-peptidase 4 and urokinase are key molecules in human and mouse scar formation. Serine 4-10 dipeptidyl peptidase 4 Homo sapiens 21-43 34661092-2 2021 Dipeptidyl peptidase 4 (DPP4), also mentioned as a cluster of differentiation 26 (CD26) is a serine exopeptidase found in two arrangements: a soluble form (sDPP-4) and a plasma membrane-bound form. Serine 93-99 dipeptidyl peptidase 4 Homo sapiens 0-22 34661092-2 2021 Dipeptidyl peptidase 4 (DPP4), also mentioned as a cluster of differentiation 26 (CD26) is a serine exopeptidase found in two arrangements: a soluble form (sDPP-4) and a plasma membrane-bound form. Serine 93-99 dipeptidyl peptidase 4 Homo sapiens 24-28 2580948-8 1985 We conclude that the N-terminal region of substance P is not degraded by cholinesterase but by the contaminating dipeptidyl peptidase IV, a different serine enzyme. Serine 150-156 dipeptidyl peptidase 4 Homo sapiens 113-136 35371018-0 2022 Induction of IDO1 and Kynurenine by Serine Proteases Subtilisin, Prostate Specific Antigen, CD26 and HtrA: A New Form of Immunosuppression? Serine 36-42 dipeptidyl peptidase 4 Homo sapiens 92-96 35371018-3 2022 We now report that IDO1 mRNA and IDO1 protein expression (generating kynurenine) are induced in human monocyte-derived macrophages by several chymotryptic serine proteases with direct links to tumorigenesis, including Prostate Specific Antigen (PSA), CD26 (Dipeptidyl-peptidase-4, CD26/DPP-4), High Temperature Requirement protein-A (HtrA), and the bacterial virulence factor subtilisin. Serine 155-161 dipeptidyl peptidase 4 Homo sapiens 251-255 35371018-3 2022 We now report that IDO1 mRNA and IDO1 protein expression (generating kynurenine) are induced in human monocyte-derived macrophages by several chymotryptic serine proteases with direct links to tumorigenesis, including Prostate Specific Antigen (PSA), CD26 (Dipeptidyl-peptidase-4, CD26/DPP-4), High Temperature Requirement protein-A (HtrA), and the bacterial virulence factor subtilisin. Serine 155-161 dipeptidyl peptidase 4 Homo sapiens 257-279 35371018-3 2022 We now report that IDO1 mRNA and IDO1 protein expression (generating kynurenine) are induced in human monocyte-derived macrophages by several chymotryptic serine proteases with direct links to tumorigenesis, including Prostate Specific Antigen (PSA), CD26 (Dipeptidyl-peptidase-4, CD26/DPP-4), High Temperature Requirement protein-A (HtrA), and the bacterial virulence factor subtilisin. Serine 155-161 dipeptidyl peptidase 4 Homo sapiens 281-285 35371018-3 2022 We now report that IDO1 mRNA and IDO1 protein expression (generating kynurenine) are induced in human monocyte-derived macrophages by several chymotryptic serine proteases with direct links to tumorigenesis, including Prostate Specific Antigen (PSA), CD26 (Dipeptidyl-peptidase-4, CD26/DPP-4), High Temperature Requirement protein-A (HtrA), and the bacterial virulence factor subtilisin. Serine 155-161 dipeptidyl peptidase 4 Homo sapiens 286-291 35273901-1 2022 Proline specific serine protease enzyme, dipeptidyl peptidase IV (DPP-4) has become a promising target for diabetes, as it stops glucagon-like peptide 1 (GLP-1) from becoming inactive, resulting in higher levels of active GLP-1. Serine 17-23 dipeptidyl peptidase 4 Homo sapiens 41-64 35273901-1 2022 Proline specific serine protease enzyme, dipeptidyl peptidase IV (DPP-4) has become a promising target for diabetes, as it stops glucagon-like peptide 1 (GLP-1) from becoming inactive, resulting in higher levels of active GLP-1. Serine 17-23 dipeptidyl peptidase 4 Homo sapiens 66-71 33603422-4 2021 Dipeptidyl peptidase-4 (DPP-4) or CD26, a multifunctional serine protease with a dual function (regulatory protease and binding protein), can modulate inflammation and immune cell-mediated beta-cell destruction. Serine 58-64 dipeptidyl peptidase 4 Homo sapiens 0-22 32914379-5 2021 RESULTS: We reveal the consistent upregulation of serine protease DPP4 and structural protein SPP1 with the progression of PTC to metastatic disease, as well as with PDGFRA expression. Serine 50-56 dipeptidyl peptidase 4 Homo sapiens 66-70 33730493-6 2021 Both were selective for FAP over DPP-IV, a related serine protease. Serine 51-57 dipeptidyl peptidase 4 Homo sapiens 33-39 33691757-1 2021 BACKGROUND: Dipeptidyl peptidase 4 (DPP4) is a serine exopeptidase able to inactivate various oligopeptides, and also a hepatokine. Serine 47-53 dipeptidyl peptidase 4 Homo sapiens 12-34 33691757-1 2021 BACKGROUND: Dipeptidyl peptidase 4 (DPP4) is a serine exopeptidase able to inactivate various oligopeptides, and also a hepatokine. Serine 47-53 dipeptidyl peptidase 4 Homo sapiens 36-40 32662092-4 2021 We hypothesized that DPP-4 inhibitors block adverse complement activation by inhibiting complement-activating serine proteases. Serine 110-116 dipeptidyl peptidase 4 Homo sapiens 21-26 33603422-4 2021 Dipeptidyl peptidase-4 (DPP-4) or CD26, a multifunctional serine protease with a dual function (regulatory protease and binding protein), can modulate inflammation and immune cell-mediated beta-cell destruction. Serine 58-64 dipeptidyl peptidase 4 Homo sapiens 24-29 33603422-4 2021 Dipeptidyl peptidase-4 (DPP-4) or CD26, a multifunctional serine protease with a dual function (regulatory protease and binding protein), can modulate inflammation and immune cell-mediated beta-cell destruction. Serine 58-64 dipeptidyl peptidase 4 Homo sapiens 34-38 33139859-6 2021 Dipeptidylpeptidase4 (DPP4/CD26), a serine protease that cleaves select penultimate amino acids of various proteins, has been previously implicated in the regulation of hematopoiesis. Serine 36-42 dipeptidyl peptidase 4 Homo sapiens 0-20 33427376-1 2021 Acylpeptide hydrolase is a serine protease which, together with prolyl oligopeptidase, dipeptidyl peptidase IV and oligopeptidase B belongs to the prolyl oligopeptidase family. Serine 27-33 dipeptidyl peptidase 4 Homo sapiens 87-110 32998057-3 2020 Dipeptidyl peptidase-4 (DPP4), a serine peptidase, cleaves N-terminal dipeptides of GLP-1, rendering it inactive and responsible for its short half-life. Serine 33-39 dipeptidyl peptidase 4 Homo sapiens 24-28 33139859-6 2021 Dipeptidylpeptidase4 (DPP4/CD26), a serine protease that cleaves select penultimate amino acids of various proteins, has been previously implicated in the regulation of hematopoiesis. Serine 36-42 dipeptidyl peptidase 4 Homo sapiens 22-26 33139859-6 2021 Dipeptidylpeptidase4 (DPP4/CD26), a serine protease that cleaves select penultimate amino acids of various proteins, has been previously implicated in the regulation of hematopoiesis. Serine 36-42 dipeptidyl peptidase 4 Homo sapiens 27-31 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. Serine 36-42 dipeptidyl peptidase 4 Homo sapiens 0-22 32336007-1 2020 Dipeptidyl peptidase 4 (DPP4), also known as cluster of differentiation 26 (CD26), is a serine exopeptidase expressed ubiquitously in several tissues, including but not limited to lung, kidney, liver, gut, and immune cells. Serine 88-94 dipeptidyl peptidase 4 Homo sapiens 0-22 32336007-1 2020 Dipeptidyl peptidase 4 (DPP4), also known as cluster of differentiation 26 (CD26), is a serine exopeptidase expressed ubiquitously in several tissues, including but not limited to lung, kidney, liver, gut, and immune cells. Serine 88-94 dipeptidyl peptidase 4 Homo sapiens 24-28 32948146-1 2020 BACKGROUND: Dipeptidyl peptidase-4 (DPP-4) is a serine protease that inhibits the degradation of glucagon-like peptide 1. Serine 48-54 dipeptidyl peptidase 4 Homo sapiens 12-34 32948146-1 2020 BACKGROUND: Dipeptidyl peptidase-4 (DPP-4) is a serine protease that inhibits the degradation of glucagon-like peptide 1. Serine 48-54 dipeptidyl peptidase 4 Homo sapiens 36-41 32487805-1 2020 PURPOSE OF REVIEW: Dipeptidyl peptidase 4 (DPP4) is a serine protease with diverse regulatory functions in healthy and diseased cells. Serine 54-60 dipeptidyl peptidase 4 Homo sapiens 19-41 32487805-1 2020 PURPOSE OF REVIEW: Dipeptidyl peptidase 4 (DPP4) is a serine protease with diverse regulatory functions in healthy and diseased cells. Serine 54-60 dipeptidyl peptidase 4 Homo sapiens 43-47 32661206-3 2020 Cellular receptor ACE2, serine protease TMPRSS2 and exopeptidase CD26 (also known as DPP4) are the three membrane bound proteins potentially implicated in SARS-CoV-2 infection. Serine 24-30 dipeptidyl peptidase 4 Homo sapiens 85-89 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. Serine 36-42 dipeptidyl peptidase 4 Homo sapiens 24-29 30862104-4 2019 In this work, initially, molecular docking simulations revealed that a natural compound, Galangin, possess a binding energy of -24 KJ/mol and interaction residues SER 630 and TYR 547, that are responsible for potent DPP-4 inhibition. Serine 163-166 dipeptidyl peptidase 4 Homo sapiens 216-221 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. Serine 79-82 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. Serine 79-82 dipeptidyl peptidase 4 Homo sapiens 24-29