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Volumn 74, Issue , 2014, Pages 574-605

Recent approaches to medicinal chemistry and therapeutic potential of dipeptidyl peptidase-4 (DPP-4) inhibitors

Author keywords

Diabetes; Dipeptidyl peptidase 4; Glucagon like peptide (GLP) 1; Non peptidomimetics; Peptidomimetics

Indexed keywords

2 CYANO PYRROLIDINE DERIVATIVE; ALKENE DERIVATIVE; BETA PHENETHYLAMINE INHIBITOR; BORONIC ACID DERIVATIVE; DIPEPTIDYL PEPTIDASE IV; DIPEPTIDYL PEPTIDASE IV INHIBITOR; FLUORINATED PYRROLIDINE AMIDE; FLUORO OLEFIN DERIVATIVE; GLUCAGON LIKE PEPTIDE 1; IMIDAZOLE DERIVATIVE; IMIDAZOPYRAZINONE DERIVATIVE; INCRETIN; OXADIAZOLE DERIVATIVE; OXAZOLOPYRAZINONE DERIVATIVE; PEPTIDOMIMETIC AGENT; PEPTIDOMIMETIC INHIBITOR; PHOSPHONIC ACID DERIVATIVE; PIPERAZINE DERIVATIVE; PIPERIDINE DERIVATIVE; PROTEIN INHIBITOR; PYRAZOLINE DERIVATIVE; PYRIDINE DERIVATIVE; PYRROLIDINE BASED INHIBITOR; PYRROLIDINE DERIVATIVE; SULFONAMIDE; THIAZOLE DERIVATIVE; THIAZOLIDINE DERIVATIVE; TRIAZOLOPIPERAZINE DERIVATIVE; UNCLASSIFIED DRUG; UNINDEXED DRUG; XANTHINE DERIVATIVE;

EID: 84894175214     PISSN: 02235234     EISSN: 17683254     Source Type: Journal    
DOI: 10.1016/j.ejmech.2013.12.038     Document Type: Short Survey
Times cited : (87)

References (312)
  • 1
    • 84881044531 scopus 로고    scopus 로고
    • sixth ed. The Global Burden (accessed 26.12.13)
    • International Diabetes Federation - Diabetes Atlas sixth ed. 2013 The Global Burden 29 50 http://www.idf.org/diabetesatlas/download-book (accessed 26.12.13)
    • (2013) International Diabetes Federation - Diabetes Atlas , pp. 29-50
  • 2
    • 75149130955 scopus 로고    scopus 로고
    • Diagnosis and classification of diabetes mellitus
    • American Diabetes Association
    • American Diabetes Association Diagnosis and classification of diabetes mellitus Diabetes Care 33 2010 S62 S69
    • (2010) Diabetes Care , vol.33
  • 4
    • 84861389721 scopus 로고    scopus 로고
    • India's diabetes time bomb
    • P. Shetty India's diabetes time bomb Nat. Outlook: Diabetes 485 2012 S14 S16
    • (2012) Nat. Outlook: Diabetes , vol.485
    • Shetty, P.1
  • 6
    • 79960262492 scopus 로고    scopus 로고
    • Management of type 2 diabetes: New and future developments in treatment
    • A.A. Tahrani, C.J. Bailey, S.D. Prato, and A.H. Barnett Management of type 2 diabetes: new and future developments in treatment Lancet 378 2011 182 197
    • (2011) Lancet , vol.378 , pp. 182-197
    • Tahrani, A.A.1    Bailey, C.J.2    Prato, S.D.3    Barnett, A.H.4
  • 7
    • 33645071360 scopus 로고    scopus 로고
    • Human duodenal enteroendocrine cells: Source of both incretin peptides, GLP-1 and GIP
    • M.J. Theodorakis, O. Carlson, and S. Michopoulo et al. Human duodenal enteroendocrine cells: source of both incretin peptides, GLP-1 and GIP Am. J. Physiol. Endocrinol. Metab. 290 2006 E550 E559
    • (2006) Am. J. Physiol. Endocrinol. Metab. , vol.290
    • Theodorakis, M.J.1    Carlson, O.2    Michopoulo, S.3
  • 8
    • 0141785429 scopus 로고    scopus 로고
    • Glucose-dependent insulinotropic polypeptide promotes β-(INS-1) cell survival via cyclic adenosine monophosphate-mediated caspase-3 inhibition and regulation of p38 mitogen-activated protein kinase
    • DOI 10.1210/en.2002-0068
    • J.A. Ehses, V.R. Casilla, and T. Doty et al. Glucose-dependent insulinotropic polypeptide promotes beta-(INS-1) cell survival via cyclic adenosine monophosphate-mediated caspase-3 inhibition and regulation of p38 mitogen-activated protein kinase Endocrinology 144 2003 4433 4445 (Pubitemid 37204843)
    • (2003) Endocrinology , vol.144 , Issue.10 , pp. 4433-4445
    • Ehses, J.A.1    Casilla, V.R.2    Doty, T.3    Pospisilik, J.A.4    Winter, K.D.5    Demuth, H.-U.6    Pederson, R.A.7    McIntosh, C.H.S.8
  • 10
    • 0034522773 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 induces cell proliferation and pancreatic-duodenum homeobox-1 expression and increases endocrine cell mass in the pancreas of old, glucose-intolerant rats
    • DOI 10.1210/en.141.12.4600
    • R. Perfetti, J. Zhou, M.E. Doyle, and J.M. Egan Glucagon-like peptide-1 induces cell proliferation and pancreatic- duodenum homeobox-1 expression and increases endocrine cell mass in the pancreas of old, glucose-intolerant rats Endocrinology 141 2000 4600 4605 (Pubitemid 32055138)
    • (2000) Endocrinology , vol.141 , Issue.12 , pp. 4600-4605
    • Perfetti, R.1    Zhou, J.I.E.2    Doyle, M.E.3    Egan, J.M.4
  • 11
    • 0037312821 scopus 로고    scopus 로고
    • The influence of GLP-1 on glucose-stimulated insulin secretion: Effects on β-cell sensitivity in type 2 and nondiabetic subjects
    • DOI 10.2337/diabetes.52.2.380
    • L.L. Kjems, J.J. Holst, A. Volund, and S. Madsbad The influence of GLP-1 on glucose-stimulated insulin secretion: effects on beta-cell sensitivity in type 2 and nondiabetic subjects Diabetes 52 2003 380 386 (Pubitemid 36173193)
    • (2003) Diabetes , vol.52 , Issue.2 , pp. 380-386
    • Kjems, L.L.1    Holst, J.J.2    Volund, A.3    Madsbad, S.4
  • 12
    • 0033766716 scopus 로고    scopus 로고
    • Degradation of endogenous and exogenous gastric inhibitory polypeptide in healthy and in type 2 diabetic subjects as revealed using a new assay for the intact peptide
    • C.F. Deacon, M.A. Nauck, and J. Meier et al. Degradation of endogenous and exogenous gastric inhibitory polypeptide in healthy and in type 2 diabetic subjects as revealed using a new assay for the intact peptide J. Clin. Endocrinol. Metab. 85 2000 3575 3581
    • (2000) J. Clin. Endocrinol. Metab. , vol.85 , pp. 3575-3581
    • Deacon, C.F.1    Nauck, M.A.2    Meier, J.3
  • 13
    • 0037241085 scopus 로고    scopus 로고
    • Similar elimination rates of glucagon-like peptide-1 in obese type 2 diabetic patients and healthy subjects
    • DOI 10.1210/jc.2002-021053
    • T. Vilsboll, H. Agerso, T. Krarup, and J.J. Holst Similar elimination rates of glucagon-like peptide-1 in obese type 2 diabetic patients and healthy subjects J. Clin. Endocrinol. Metab. 88 2003 220 224 (Pubitemid 36115169)
    • (2003) Journal of Clinical Endocrinology and Metabolism , vol.88 , Issue.1 , pp. 220-224
    • Vilsboll, T.1    Agerso, H.2    Krarup, T.3    Holst, J.J.4
  • 14
    • 1442350411 scopus 로고    scopus 로고
    • Secretion, Degradation, and Elimination of Glucagon-Like Peptide 1 and Gastric Inhibitory Polypeptide in Patients with Chronic Renal Insufficiency and Healthy Control Subjects
    • DOI 10.2337/diabetes.53.3.654
    • J.J. Meier, M.A. Nauck, and D. Kranz et al. Secretion, degradation, and elimination of glucagon-like peptide 1 and gastric inhibitory polypeptide in patients with chronic renal insufficiency and healthy control subjects Diabetes 53 2004 654 662 (Pubitemid 38270634)
    • (2004) Diabetes , vol.53 , Issue.3 , pp. 654-662
    • Meier, J.J.1    Nauck, M.A.2    Kranz, D.3    Holst, J.J.4    Deacon, C.F.5    Gaeckler, D.6    Schmidt, W.E.7    Gallwitz, B.8
  • 15
    • 0014155217 scopus 로고
    • Purification and characterization of an aminopeptidase hydrolysing glycyl-proline-naphthylamide
    • V.K. Hopsu-Havu, and S.S. Sarimo Purification and characterization of an aminopeptidase hydrolysing glycyl-proline-naphthylamide Hoppe Seylers Z. Physiol. Chem. 384 1967 1540 1550
    • (1967) Hoppe Seylers Z. Physiol. Chem. , vol.384 , pp. 1540-1550
    • Hopsu-Havu, V.K.1    Sarimo, S.S.2
  • 17
    • 84861095436 scopus 로고    scopus 로고
    • DPP IV inhibitors: Successes, failures and future prospects
    • A.D. Kshirsagar, and A.S. Aggarwal et al. DPP IV inhibitors: successes, failures and future prospects Diabetes Metab. Syndr. 5 2011 105 112
    • (2011) Diabetes Metab. Syndr. , vol.5 , pp. 105-112
    • Kshirsagar, A.D.1    Aggarwal, A.S.2
  • 18
    • 0027982677 scopus 로고
    • Genomic organization, exact localization, and tissue expression of the human CD26 (dipeptidyl peptidase IV) gene
    • C.A. Abbott, E. Baker, and G.R. Sutherland et al. Genomic organization, exact localization, and tissue expression of the human CD26 (dipeptidyl peptidase IV) gene Immunogenetics 40 1994 31 38
    • (1994) Immunogenetics , vol.40 , pp. 31-38
    • Abbott, C.A.1    Baker, E.2    Sutherland, G.R.3
  • 19
    • 33947705084 scopus 로고    scopus 로고
    • Molecular recognition of ligands in dipeptidyl peptidase IV
    • DOI 10.2174/156802607780091064
    • B. Kuhn, M. Hennig, and P. Mattei Molecular recognition of ligands in dipeptidyl peptidase IV Curr. Top. Med. Chem. 7 2007 609 619 (Pubitemid 46488283)
    • (2007) Current Topics in Medicinal Chemistry , vol.7 , Issue.6 , pp. 609-619
    • Kuhn, B.1    Hennig, M.2    Mattei, P.3
  • 20
    • 0033619675 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides
    • DOI 10.1016/S0167-0115(99)00089-0, PII S0167011599000890
    • R. Mentlein Dipeptidyl-peptidase IV (CD26) - role in the inactivation of regulatory peptides Regul. Pept. 85 1999 9 24 (Pubitemid 29505281)
    • (1999) Regulatory Peptides , vol.85 , Issue.1 , pp. 9-24
    • Mentlein, R.1
  • 22
    • 0037219684 scopus 로고    scopus 로고
    • Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog
    • DOI 10.1038/nsb882
    • H.B. Rasmussen, S. Branner, F.C. Wiberg, and N. Wagtmann Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog Nat. Struct. Biol. 10 2003 19 25 (Pubitemid 36034172)
    • (2003) Nature Structural Biology , vol.10 , Issue.1 , pp. 19-25
    • Rasmussen, H.B.1    Branner, S.2    Wiberg, F.C.3    Wagtmann, N.4
  • 23
    • 0042131827 scopus 로고    scopus 로고
    • Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV
    • DOI 10.1016/S0969-2126(03)00160-6
    • R. Thoma, B. Loeffler, M. Stihle, W. Huber, A. Ruf, and M. Hennig Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV Structure 11 2003 947 959 (Pubitemid 36966784)
    • (2003) Structure , vol.11 , Issue.8 , pp. 947-959
    • Thoma, R.1    Loffler, B.2    Stihle, M.3    Huber, W.4    Ruf, A.5    Hennig, M.6
  • 24
    • 10644296948 scopus 로고    scopus 로고
    • One site mutation disrupts dimer formation in human DPP-IV proteins
    • C.H. Chien, L.H. Huang, C.Y. Chou, and Y.S. Chen et al. One site mutation disrupts dimer formation in human DPP-IV proteins J. Biol. Chem. 279 2004 52338 52345
    • (2004) J. Biol. Chem. , vol.279 , pp. 52338-52345
    • Chien, C.H.1    Huang, L.H.2    Chou, C.Y.3    Chen, Y.S.4
  • 26
    • 84877061867 scopus 로고    scopus 로고
    • A comparative study of the binding modes of recently launched dipeptidyl peptidase IV inhibitors in the active site, Biochem
    • M. Nabeno, F. Akahoshi, and H. Kishida et al. A comparative study of the binding modes of recently launched dipeptidyl peptidase IV inhibitors in the active site, Biochem Biophys. Res. Commun. 434 2013 191 196
    • (2013) Biophys. Res. Commun. , vol.434 , pp. 191-196
    • Nabeno, M.1    Akahoshi, F.2    Kishida, H.3
  • 27
    • 0038793576 scopus 로고    scopus 로고
    • High-resolution structure of human apo dipeptidyl peptidase IV/CD26 and its complex with 1-[({2-[(5-iodopyridin-2-yl)amino]-ethyl}amino)- acetyl]-2-cyano-(S)-pyrrolidine
    • DOI 10.1107/S0907444903010059
    • Oefner, A. D'Arcy, and A.M. Sweeney et al. High resolution structure of human apo dipeptidyl peptidase IV/CD26 and its complex with 1-[({2-[(5- iodopyridin-2-yl)amino]-ethyl}-amino)-acetyl]-2-cyano-(S)-pyrrolidine Acta Crystallogr. Sect. D. 59 2003 1206 1212 (Pubitemid 36872357)
    • (2003) Acta Crystallographica Section D: Biological Crystallography , vol.59 , Issue.7 , pp. 1206-1212
    • Oefner, C.1    D'Arcy, A.2    Mac Sweeney, A.3    Pierau, S.4    Gardiner, R.5    Dale, G.E.6
  • 29
    • 33845339435 scopus 로고    scopus 로고
    • Protease inhibitors in the clinic
    • G. Abbenante, and D.P. Fairlie Protease inhibitors in the clinic Med. Chem. 1 2005 71 104
    • (2005) Med. Chem. , vol.1 , pp. 71-104
    • Abbenante, G.1    Fairlie, D.P.2
  • 30
    • 34250206962 scopus 로고    scopus 로고
    • Docking-based 3D-QSAR study for selectivity of DPP4, DPP8, and DPP9 inhibitors
    • DOI 10.1016/j.bmcl.2007.04.031, PII S0960894X07004519
    • N.S. Kang, J.H. Ahn, S.S. Kim, C.H. Chae, and S. Yoo Docking-based 3D-QSAR study for selectivity of DPP4, DPP8, and DPP9 inhibitors Bioorg. Med. Chem. Lett. 17 2007 3716 3721 (Pubitemid 46901103)
    • (2007) Bioorganic and Medicinal Chemistry Letters , vol.17 , Issue.13 , pp. 3716-3721
    • Kang, N.S.1    Ahn, J.H.2    Kim, S.S.3    Chae, C.H.4    Yoo, S.-E.5
  • 32
    • 33845648469 scopus 로고    scopus 로고
    • Homology models of dipeptidyl peptidases 8 and 9 with a focus on loop predictions near the active site
    • DOI 10.1002/prot.21138
    • C. Rummey, and G. Metz Homology models of dipeptidyl peptidases 8 and 9 with a focus on loop predictions near the active site Proteins: Struct. Funct. Bioinform. 66 2007 160 171 (Pubitemid 44955988)
    • (2007) Proteins: Structure, Function and Genetics , vol.66 , Issue.1 , pp. 160-171
    • Rummey, C.1    Metz, G.2
  • 33
    • 3843072211 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitors for the treatment of diabetes
    • DOI 10.1021/jm030628v
    • A.E. Weber Dipeptidyl peptidase IV inhibitors for the treatment of diabetes J. Med. Chem. 47 2004 4135 4141 (Pubitemid 39045417)
    • (2004) Journal of Medicinal Chemistry , vol.47 , Issue.17 , pp. 4135-4141
    • Weber, A.E.1
  • 34
    • 70350513013 scopus 로고    scopus 로고
    • Efficacy and safety of incretin based therapies: Clinical trial data
    • J. White Efficacy and safety of incretin based therapies: clinical trial data J. Am. Pharm. Assoc. 49 2009 S30 S40
    • (2009) J. Am. Pharm. Assoc. , vol.49
    • White, J.1
  • 35
    • 84873852937 scopus 로고    scopus 로고
    • Choosing between GLP-1 receptor agonists & DPP-4 inhibitors: A pharmacological perspective
    • 10.1155/2012/381713
    • D.X. Brown, and M. Evans Choosing between GLP-1 receptor agonists & DPP-4 inhibitors: a pharmacological perspective J. Nutr. Metab. 2012 10.1155/2012/381713
    • (2012) J. Nutr. Metab.
    • Brown, D.X.1    Evans, M.2
  • 36
    • 41149118550 scopus 로고    scopus 로고
    • (R)-8-(3-amino-piperidin-1-yl)-7-but-2-ynyl-3-methyl-1-(4-methyl- quinazolin-2-ylmethyl)-3,7-dihydro-purine-2,6-dione (BI 1356), a novel xanthine-based dipeptidyl peptidase 4 inhibitor, has a superior potency and longer duration of action compared with other dipeptidyl peptidase-4 inhibitors
    • DOI 10.1124/jpet.107.135723
    • L. Thomas, M. Eckhardt, E. Langkopf, M. Tadayyon, F. Himmelsbach, and M. Mark (R)-8-(3-amino-piperidin-1-yl)-7-but-2-ynyl-3-methyl-1-(4-methylquinazolin- 2-ylmethyl)-3,7-dihydro-purine-2,6-dione (BI 1356), a novel xanthine-based dipeptidyl peptidase 4 inhibitor, has a superior potency and longer duration of action compared with other dipeptidyl peptidase-4 inhibitors J. Pharmacol. Exp. Ther. 325 2008 175 182 (Pubitemid 351439162)
    • (2008) Journal of Pharmacology and Experimental Therapeutics , vol.325 , Issue.1 , pp. 175-182
    • Thomas, L.1    Eckhardt, M.2    Langkopf, E.3    Tadayyon, M.4    Himmelsbach, F.5    Mark, M.6
  • 37
    • 78649686908 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 inhibitors in the treatment of type 2 diabetes: A comparative review
    • C.F. Deacon Dipeptidyl peptidase-4 inhibitors in the treatment of type 2 diabetes: a comparative review Diabetes Obes. Metab. 13 2011 7 18
    • (2011) Diabetes Obes. Metab. , vol.13 , pp. 7-18
    • Deacon, C.F.1
  • 43
    • 77951702763 scopus 로고    scopus 로고
    • Safety, tolerability, pharmacokinetics and pharmacodynamics of once daily oral doses of saxagliptin for 2 weeks in type 2 diabetic and healthy subjects (poster 0606-P)
    • D.W. Boulton, and M. Geraldes Safety, tolerability, pharmacokinetics and pharmacodynamics of once daily oral doses of saxagliptin for 2 weeks in type 2 diabetic and healthy subjects (poster 0606-P) Diabetes 56 2007 A161
    • (2007) Diabetes , vol.56 , pp. 161
    • Boulton, D.W.1    Geraldes, M.2
  • 44
    • 41649083174 scopus 로고    scopus 로고
    • Pharmacokinetic, pharmacodynamic, and tolerability profiles of the dipeptidyl peptidase-4 inhibitor alogliptin: A randomized, double-blind, placebo-controlled, multiple-dose study in adult patients with type 2 diabetes
    • DOI 10.1016/j.clinthera.2008.03.004, PII S0149291808001173
    • P. Covington, R. Christopher, and M. Davenport et al. Pharmacokinetic, pharmacodynamic, and tolerability profiles of the dipeptidyl peptidase-4 inhibitor alogliptin: a randomized, double-blind, placebo-controlled, multiple-dose study in adult patients with type 2 diabetes Clin. Ther. 30 2008 499 512 (Pubitemid 351483925)
    • (2008) Clinical Therapeutics , vol.30 , Issue.3 , pp. 499-512
    • Covington, P.1    Christopher, R.2    Davenport, M.3    Fleck, P.4    Mekki, Q.A.5    Wann, E.R.6    Karim, A.7
  • 45
    • 67649998759 scopus 로고    scopus 로고
    • Pharmacokinetics, pharmacodynamics and tolerability of multiple oral doses of linagliptin, a dipeptidyl peptidase-4 inhibitor in male type 2 diabetes patients
    • T. Heise, E.U. Graefe-Mody, S. Huttner, and A. Ring et al. Pharmacokinetics, pharmacodynamics and tolerability of multiple oral doses of linagliptin, a dipeptidyl peptidase-4 inhibitor in male type 2 diabetes patients Diabetes Obes. Metab. 11 2009 786 794
    • (2009) Diabetes Obes. Metab. , vol.11 , pp. 786-794
    • Heise, T.1    Graefe-Mody, E.U.2    Huttner, S.3    Ring, A.4
  • 47
    • 63849095884 scopus 로고    scopus 로고
    • Role of dipeptidyl peptidase IV (DP IV)-like enzymes in T lymphocyte activation: Investigations in DP IV/CD26-knockout mice
    • D. Reinhold, A. Goihl, and S. Wrenger et al. Role of dipeptidyl peptidase IV (DP IV)-like enzymes in T lymphocyte activation: investigations in DP IV/CD26-knockout mice Clin. Chem. Lab. Med. 47 2009 268 274
    • (2009) Clin. Chem. Lab. Med. , vol.47 , pp. 268-274
    • Reinhold, D.1    Goihl, A.2    Wrenger, S.3
  • 49
    • 65649147246 scopus 로고    scopus 로고
    • Biochemistry, pharmacokinetics, and toxicology of a potent and selective DPP8/9 inhibitor
    • J. Wu, H. Tang, T. Yeh, and C. Chen et al. Biochemistry, pharmacokinetics, and toxicology of a potent and selective DPP8/9 inhibitor Biochem. Pharmacol. 78 2009 203 210
    • (2009) Biochem. Pharmacol. , vol.78 , pp. 203-210
    • Wu, J.1    Tang, H.2    Yeh, T.3    Chen, C.4
  • 50
    • 84859172957 scopus 로고    scopus 로고
    • Potency, selectivity and prolonged binding of saxagliptin to DPP4: Maintenance of DPP4 inhibition by saxagliptin in vitro and ex vivo when compared to a rapidly-dissociating DPP4 inhibitor
    • M.S. Kirby, A. Wang, and C. Dorso et al. Potency, selectivity and prolonged binding of saxagliptin to DPP4: maintenance of DPP4 inhibition by saxagliptin in vitro and ex vivo when compared to a rapidly-dissociating DPP4 inhibitor BMC Pharmacol. 12 2012 2 12
    • (2012) BMC Pharmacol. , vol.12 , pp. 2-12
    • Kirby, M.S.1    Wang, A.2    Dorso, C.3
  • 52
    • 66649134595 scopus 로고    scopus 로고
    • In vitro enzymologic characteristics of saxagliptin, a highly potent and selective DPP4 inhibitor with ''slow binding'' characteristic (Abstract)
    • M.S. Kirby, C. Dorso, and A. Wang et al. In vitro enzymologic characteristics of saxagliptin, a highly potent and selective DPP4 inhibitor with ''slow binding'' characteristic (Abstract) Clin. Chem. Lab. Med. 46 2008 A79
    • (2008) Clin. Chem. Lab. Med. , vol.46 , pp. 79
    • Kirby, M.S.1    Dorso, C.2    Wang, A.3
  • 53
    • 53149100519 scopus 로고    scopus 로고
    • Seprase: An overview of an important matrix serine protease
    • P. O'Brien, and B.F. O'Connor Seprase: an overview of an important matrix serine protease Biochim. Biophys. Acta 1784 2008 1130 1145
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1130-1145
    • O'Brien, P.1    O'Connor, B.F.2
  • 54
    • 0035432607 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 infusion must be maintained for 24 h/day to obtain acceptable glycemia in type 2 diabetic patients who are poorly controlled on sulphonylurea treatment
    • J. Larsen, B. Hylleberg, K. Ng, and P. Damsbo Glucagon-like peptide-1 infusion must be maintained for 24 h/day to obtain acceptable glycemia in type 2 diabetic patients who are poorly controlled on sulphonylurea treatment Diabetes Care 24 2001 1416 1421 (Pubitemid 33716430)
    • (2001) Diabetes Care , vol.24 , Issue.8 , pp. 1416-1421
    • Larsen, J.1    Hylleberg, B.2    Ng, K.3    Damsbo, P.4
  • 55
    • 61349143225 scopus 로고    scopus 로고
    • Medicinal chemistry approaches to the inhibition of dipeptidyl peptidase-4 for the treatment of type 2 diabetes
    • M. Pal, and S.H. Havale Medicinal chemistry approaches to the inhibition of dipeptidyl peptidase-4 for the treatment of type 2 diabetes Bioorg. Med. Chem. 17 2009 1783 1802
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 1783-1802
    • Pal, M.1    Havale, S.H.2
  • 56
    • 59149106467 scopus 로고    scopus 로고
    • Medicinal chemistry approaches to the inhibition of dipeptidyl peptidase IV
    • S.L. Gwaltney II Medicinal chemistry approaches to the inhibition of dipeptidyl peptidase IV Curr. Top. Med. Chem. 8 2008 1545 1552
    • (2008) Curr. Top. Med. Chem. , vol.8 , pp. 1545-1552
    • Gwaltney, I.I.S.L.1
  • 57
    • 84865785890 scopus 로고    scopus 로고
    • Recent advances in non-peptidomimetic dipeptidyl peptidase 4 inhibitors: Medicinal chemistry and preclinical aspects
    • Y. Liu, Y. Hu, and T. Liu Recent advances in non-peptidomimetic dipeptidyl peptidase 4 inhibitors: medicinal chemistry and preclinical aspects Curr. Med. Chem. 19 2012 3982 3999
    • (2012) Curr. Med. Chem. , vol.19 , pp. 3982-3999
    • Liu, Y.1    Hu, Y.2    Liu, T.3
  • 58
    • 20444406121 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl-peptidase IV catalyzed peptide truncation by Vildagliptin ((2S)-{[(3-hydroxyadamantan-1-yl)amino]acetyl}-pyrrolidine-2- carbonitrile)
    • DOI 10.1016/j.bcp.2005.04.009, PII S0006295205002376
    • I. Brandt, J. Joossens, and X. Chen et al. Inhibition of dipeptidyl-peptidase IV catalyzed peptide truncation by vildagliptin ((2S)-{[(3-hydroxyadamantan-1-yl)amino]acetyl}-pyrrolidine-2-carbonitrile) Biochem Pharmacol. 70 2005 134 143 (Pubitemid 40797877)
    • (2005) Biochemical Pharmacology , vol.70 , Issue.1 , pp. 134-143
    • Brandt, I.1    Joossens, J.2    Chen, X.3    Maes, M.-B.4    Scharpe, S.5    De Meester, I.6    Lambeir, A.-M.7
  • 59
    • 33847613829 scopus 로고    scopus 로고
    • Vildagliptin displays slow tight-binding to dipeptidyl peptidase (DPP)-4, but not DPP-8 or DPP-9 (Abstract 0788)
    • B.F. Burkey, M. Russell, K. Wang, J. Trappe, and T.E. Hughes Vildagliptin displays slow tight-binding to dipeptidyl peptidase (DPP)-4, but not DPP-8 or DPP-9 (Abstract 0788) Diabetologia 49 2006 477
    • (2006) Diabetologia , vol.49 , pp. 477
    • Burkey, B.F.1    Russell, M.2    Wang, K.3    Trappe, J.4    Hughes, T.E.5
  • 61
    • 84894182216 scopus 로고    scopus 로고
    • DPP-IV Inhibition: Promising therapy for the treatment of type 2 diabetes
    • W. Paul DPP-IV Inhibition: promising therapy for the treatment of type 2 diabetes Prog. Med. Chem. 45 2007 71 73
    • (2007) Prog. Med. Chem. , vol.45 , pp. 71-73
    • Paul, W.1
  • 62
    • 67349123804 scopus 로고    scopus 로고
    • Synthesis and evaluation of structurally constrained imidazolidin derivatives as potent dipeptidyl peptidase IV inhibitors
    • X. Wang, Y. Wu, L. Wang, and B. Zhang et al. Synthesis and evaluation of structurally constrained imidazolidin derivatives as potent dipeptidyl peptidase IV inhibitors Eur. J. Med. Chem. 44 2009 3318 3322
    • (2009) Eur. J. Med. Chem. , vol.44 , pp. 3318-3322
    • Wang, X.1    Wu, Y.2    Wang, L.3    Zhang, B.4
  • 64
    • 62149152364 scopus 로고    scopus 로고
    • Rational design and synthesis of potent and long-lasting glutamic acid-based dipeptidyl peptidase IV inhibitors
    • W.-T. Jiaang, T.-Y. Tsai, T. Hsu, and C.-T. Chen et al. Rational design and synthesis of potent and long-lasting glutamic acid-based dipeptidyl peptidase IV inhibitors Bioorg. Med. Chem. Lett. 19 2009 1908 1912
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 1908-1912
    • Jiaang, W.-T.1    Tsai, T.-Y.2    Hsu, T.3    Chen, C.-T.4
  • 67
    • 77954218296 scopus 로고    scopus 로고
    • (2S,4S)-1-[2-(1,1-Dimethyl-3-oxo-3-pyrrolidin-1-yl-propylamino)acetyl] -4-fluoro-pyrrolidine-2-carbonitrile: A potent, selective, and orally bioavailable dipeptide-derived inhibitor of dipeptidyl peptidase IV
    • C.-T. Chen, W.-T. Jiaang, T.-K. Yeh, and T.-Y. Tsai et al. (2S,4S)-1-[2-(1,1-Dimethyl-3-oxo-3-pyrrolidin-1-yl-propylamino)acetyl] -4-fluoro-pyrrolidine-2-carbonitrile: a potent, selective, and orally bioavailable dipeptide-derived inhibitor of dipeptidyl peptidase IV Bioorg. Med. Chem. Lett. 20 2010 3596 3600
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 3596-3600
    • Chen, C.-T.1    Jiaang, W.-T.2    Yeh, T.-K.3    Tsai, T.-Y.4
  • 68
    • 62549138270 scopus 로고    scopus 로고
    • Novel trans-2-aryl-cyclopropylamine analogues as potent and selective dipeptidyl peptidase IV inhibitors
    • T.-Y. Tsai, T. Hsu, C.-T. Chen, J.-H. Cheng, and T.-K. Yeh et al. Novel trans-2-aryl-cyclopropylamine analogues as potent and selective dipeptidyl peptidase IV inhibitors Bioorg. Med. Chem. 17 2009 2388 2399
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 2388-2399
    • Tsai, T.-Y.1    Hsu, T.2    Chen, C.-T.3    Cheng, J.-H.4    Yeh, T.-K.5
  • 70
    • 47149101243 scopus 로고    scopus 로고
    • Discovery of conformationally rigid 3-azabicyclo[3.1.0]hexane-derived dipeptidyl peptidase-IV inhibitors
    • J.A. Sattigeri, M.M.S. Andappan, K. Kishore, and S. Thangathirupathy et al. Discovery of conformationally rigid 3-azabicyclo[3.1.0]hexane-derived dipeptidyl peptidase-IV inhibitors Bioorg. Med. Chem. Lett. 18 2008 4087 4091
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 4087-4091
    • Sattigeri, J.A.1    Andappan, M.M.S.2    Kishore, K.3    Thangathirupathy, S.4
  • 71
    • 74649085040 scopus 로고    scopus 로고
    • Design and synthesis of DPP-4 inhibitor for the treatment of type 2 diabetes
    • P.C. Tang, Z.G. Lin, Y. Wang, F.L. Yang, and Q. Wang Design and synthesis of DPP-4 inhibitor for the treatment of type 2 diabetes Chin. Chem. Lett. 21 2010 253 256
    • (2010) Chin. Chem. Lett. , vol.21 , pp. 253-256
    • Tang, P.C.1    Lin, Z.G.2    Wang, Y.3    Yang, F.L.4    Wang, Q.5
  • 75
    • 80655131901 scopus 로고    scopus 로고
    • Synthesis and pharmacological characterization of potent, selective, and orally bioavailable isoindoline class dipeptidyl peptidase IV inhibitors
    • N. Kato, M. Oka, T. Murase, M. Yoshida, and M. Sakairi et al. Synthesis and pharmacological characterization of potent, selective, and orally bioavailable isoindoline class dipeptidyl peptidase IV inhibitors Org. Med. Chem. Lett. 1 2011 1 7
    • (2011) Org. Med. Chem. Lett. , vol.1 , pp. 1-7
    • Kato, N.1    Oka, M.2    Murase, T.3    Yoshida, M.4    Sakairi, M.5
  • 76
    • 80655146931 scopus 로고    scopus 로고
    • Discovery and pharmacological characterization of N-[2-({2-[(2S)-2- cyanopyrrolidin-1-yl]-2-oxoethyl}amino)-2-methylpropyl]-2- methylpyrazolo[1,5-a] pyrimidine-6-carboxamide hydrochloride (anagliptin hydrochloride salt) as a potent and selective DPP-IV inhibitor
    • N. Kato, M. Oka, T. Murase, M. Yoshida, M. Sakairi, and S. Yamashita Discovery and pharmacological characterization of N-[2-({2-[(2S)-2- cyanopyrrolidin-1-yl]-2-oxoethyl}amino)-2-methylpropyl]-2- methylpyrazolo[1,5-a] pyrimidine-6-carboxamide hydrochloride (anagliptin hydrochloride salt) as a potent and selective DPP-IV inhibitor Bioorg. Med. Chem. 19 2011 7221 7227
    • (2011) Bioorg. Med. Chem. , vol.19 , pp. 7221-7227
    • Kato, N.1    Oka, M.2    Murase, T.3    Yoshida, M.4    Sakairi, M.5    Yamashita, S.6
  • 78
    • 0032564474 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl peptidase IV by fluoroolefin-containing N-peptidyl-O-hydroxylamine peptidomimetics
    • J. Lin, P.J. Toscano, and J.T. Welch Inhibition of dipeptidyl peptidase IV by fluoroolefin-containing N-peptidyl-O-hydroxylamine peptidomimetics Proc. Natl. Acad. Sci. U.S.A. 95 1998 14020 14024
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 14020-14024
    • Lin, J.1    Toscano, P.J.2    Welch, J.T.3
  • 79
    • 0037449356 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl peptidase IV (DPP IV) by 2-(2-amino-1-fluoro- propylidene)-cyclopentanecarbonitrile, a fluoroolefin containing peptidomimetic
    • DOI 10.1016/S0968-0896(02)00384-X, PII S096808960200384X
    • K. Zhao, D.S. Lim, T. Funaki, and J.T. Welch Inhibition of dipeptidyl peptidase IV (DPP IV) by 2-(2-amino-1-fluoro-propylidene)- cyclopentanecarbonitrile, a fluoroolefin containing peptidomimetic Bioorg. Med. Chem. 11 2003 207 215 (Pubitemid 35418263)
    • (2003) Bioorganic and Medicinal Chemistry , vol.11 , Issue.2 , pp. 207-215
    • Zhao, K.1    Lim, D.S.2    Funaki, T.3    Welch, J.T.4
  • 80
    • 0029946714 scopus 로고    scopus 로고
    • Structure-activity relationships of boronic acid inhibitors of dipeptidyl peptidase IV. 1. Variation of the P2 position of Xaa-boroPro dipeptides
    • J. Coutts, T.A. Kelly, R.J. Snow, and C.A. Kennedy et al. Structure-activity relationships of boronic acid inhibitors of dipeptidyl peptidase IV. 1. Variation of the P2 position of Xaa-boroPro dipeptides J. Med. Chem. 39 1996 2087 2094
    • (1996) J. Med. Chem. , vol.39 , pp. 2087-2094
    • Coutts, J.1    Kelly, T.A.2    Snow, R.J.3    Kennedy, C.A.4
  • 83
    • 79953792552 scopus 로고    scopus 로고
    • Pro-Soft Val-boroPro: A strategy for enhancing in vivo performance of boronic acid inhibitors of serine proteases
    • W. William, S.E. Bachovchin, J.H. Poplawski, and D.G. Lai et al. Pro-Soft Val-boroPro: a strategy for enhancing in vivo performance of boronic acid inhibitors of serine proteases J. Med. Chem. 54 2011 2022 2028
    • (2011) J. Med. Chem. , vol.54 , pp. 2022-2028
    • William, W.1    Bachovchin, S.E.2    Poplawski, J.H.3    Lai, D.G.4
  • 84
    • 0001387705 scopus 로고
    • Boronic acid inhibitors of dipeptidyl peptidase IV: A new class of immunosuppressive
    • R.J. Snow, and W.W. Bachovchin Boronic acid inhibitors of dipeptidyl peptidase IV: a new class of immunosuppressive Adv. Med. Chem. 3 1995 149 177
    • (1995) Adv. Med. Chem. , vol.3 , pp. 149-177
    • Snow, R.J.1    Bachovchin, W.W.2
  • 86
    • 0028566173 scopus 로고
    • Studies on proline boronic acid dipeptide inhibitors of dipeptidyl peptidase IV: Identification of a cyclic species containing a B-N bond
    • R.J. Snow, W.W. Bachovchin, R.W. Barton, and S.J. Campbell et al. Studies on proline boronic acid dipeptide inhibitors of dipeptidyl peptidase IV: identification of a cyclic species containing a B-N bond J. Am. Chem. Soc. 116 1994 10860 10869
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 10860-10869
    • Snow, R.J.1    Bachovchin, W.W.2    Barton, R.W.3    Campbell, S.J.4
  • 89
    • 0038791462 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitors
    • D.M. Evans Dipeptidyl peptidase IV inhibitors Idrugs 5 2002 577 585 (Pubitemid 37214117)
    • (2002) IDrugs , vol.5 , Issue.6 , pp. 577-585
    • Evans, D.M.1
  • 90
    • 0026166647 scopus 로고
    • Dipeptidyl peptidase IV in the immune system. Effects of specific enzyme inhibitors on activity of dipeptidyl peptidase IV and proliferation of human lymphocytes
    • E. Schoen, I. Norn, and H.U. Demuth et al. Dipeptidyl peptidase IV in the immune system. Effects of specific enzyme inhibitors on activity of dipeptidyl peptidase IV and proliferation of human lymphocytes Biol. Chem. Hoppe-Seyler 372 1991 305 311
    • (1991) Biol. Chem. Hoppe-Seyler , vol.372 , pp. 305-311
    • Schoen, E.1    Norn, I.2    Demuth, H.U.3
  • 93
    • 33646033123 scopus 로고    scopus 로고
    • [(S)-γ-(Arylamino)prolyl]thiazolidine compounds as a novel series of potent and stable DPP-IV inhibitors
    • H. Sakashita, F. Akahoshi, H. Kitajima, R. Tsutsumiuchi, and Y. Hayashi [(S)-γ-(Arylamino)prolyl]thiazolidine compounds as a novel series of potent and stable DPP-IV inhibitors Bioorg. Med. Chem. 14 2006 3662 3671
    • (2006) Bioorg. Med. Chem. , vol.14 , pp. 3662-3671
    • Sakashita, H.1    Akahoshi, F.2    Kitajima, H.3    Tsutsumiuchi, R.4    Hayashi, Y.5
  • 94
    • 84864436192 scopus 로고    scopus 로고
    • Fused bicyclic heteroarylpiperazine-substituted L-prolylthiazolidines as highly potent DPP-4 inhibitors lacking the electrophilic nitrile group
    • T. Yoshida, F. Akahoshi, H. Sakashita, and S. Sonda et al. Fused bicyclic heteroarylpiperazine-substituted L-prolylthiazolidines as highly potent DPP-4 inhibitors lacking the electrophilic nitrile group Bioorg. Med. Chem. 20 2012 5033 5041
    • (2012) Bioorg. Med. Chem. , vol.20 , pp. 5033-5041
    • Yoshida, T.1    Akahoshi, F.2    Sakashita, H.3    Sonda, S.4
  • 95
    • 84866353450 scopus 로고    scopus 로고
    • Discovery and preclinical profile of teneligliptin (3-[(2S,4S)-4-[4-(3- methyl-1-phenyl-1H-pyrazol-5-yl)piperazin-1-yl]pyrrolidin-2-ylcarbonyl] thiazolidine): A highly potent, selective, long-lasting and orally active dipeptidyl peptidase IV inhibitor for the treatment of type 2 diabetes
    • T. Yoshida, F. Akahoshi, and H. Sakashita et al. Discovery and preclinical profile of teneligliptin (3-[(2S,4S)-4-[4-(3-methyl-1-phenyl-1H- pyrazol-5-yl)piperazin-1-yl]pyrrolidin-2-ylcarbonyl]thiazolidine): a highly potent, selective, long-lasting and orally active dipeptidyl peptidase IV inhibitor for the treatment of type 2 diabetes Bioorganic Med. Chem. 20 2012 5705 5719
    • (2012) Bioorganic Med. Chem. , vol.20 , pp. 5705-5719
    • Yoshida, T.1    Akahoshi, F.2    Sakashita, H.3
  • 96
    • 84877594042 scopus 로고    scopus 로고
    • Teneligliptin: A DPP-4 inhibitor for the treatment of type 2 diabetes
    • Miyako Kishimoto Teneligliptin: a DPP-4 inhibitor for the treatment of type 2 diabetes Diab. Metab. Synd. Obes. Target. Ther. 6 2013 187 195
    • (2013) Diab. Metab. Synd. Obes. Target. Ther. , vol.6 , pp. 187-195
    • Kishimoto, M.1
  • 97
    • 84862829036 scopus 로고    scopus 로고
    • Design, synthesis and primary activity of thiomorpholine derivatives as DPP-IV inhibitors
    • H.H. Huang, B. Han, J.L. Liu, and Y. Huan et al. Design, synthesis and primary activity of thiomorpholine derivatives as DPP-IV inhibitors Chin. Chem. Lett. 23 2012 297 300
    • (2012) Chin. Chem. Lett. , vol.23 , pp. 297-300
    • Huang, H.H.1    Han, B.2    Liu, J.L.3    Huan, Y.4
  • 102
    • 61849146383 scopus 로고    scopus 로고
    • (3,3-Difluoro-pyrrolidin-1-yl)-[(2S,4S)-(4-(4-pyrimidin-2-yl-piperazin-1- yl)-pyrrolidin-2-yl] methanone: A potent, selective, orally active dipeptidyl peptidase IV inhibitor
    • M.J. Ammirati, K.M. Andrews, D.D. Boyer, and A.M. Brodeur et al. (3,3-Difluoro-pyrrolidin-1-yl)-[(2S,4S)-(4-(4-pyrimidin-2-yl-piperazin-1-yl) -pyrrolidin-2-yl] methanone: a potent, selective, orally active dipeptidyl peptidase IV inhibitor Bioorg. Med. Chem. Lett. 19 2009 1991 1995
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 1991-1995
    • Ammirati, M.J.1    Andrews, K.M.2    Boyer, D.D.3    Brodeur, A.M.4
  • 103
    • 84872336284 scopus 로고    scopus 로고
    • Design, synthesis, structure-activity relationships, and docking studies of 1-(γ-1,2,3-triazol substituted prolyl)-(S)-3,3-difluoropyrrolidines as a novel series of potent and selective dipeptidyl peptidase-4 inhibitors
    • L. Zhang, M. Su, J. Li, and X. Ji et al. Design, synthesis, structure-activity relationships, and docking studies of 1-(γ-1,2,3- triazol substituted prolyl)-(S)-3,3-difluoropyrrolidines as a novel series of potent and selective dipeptidyl peptidase-4 inhibitors Chem. Biol. Drug. Des. 81 2013 198 207
    • (2013) Chem. Biol. Drug. Des. , vol.81 , pp. 198-207
    • Zhang, L.1    Su, M.2    Li, J.3    Ji, X.4
  • 111
    • 79952364204 scopus 로고    scopus 로고
    • Discovery of potent dipeptidyl peptidase IV inhibitors derived from β-aminoamides bearing substituted [1,2,3]-triazolopiperidines for the treatment of type 2 diabetes
    • Y. Chen, Z. Shan, M. Peng, and H. Fan et al. Discovery of potent dipeptidyl peptidase IV inhibitors derived from β-aminoamides bearing substituted [1,2,3]-triazolopiperidines for the treatment of type 2 diabetes Bioorg. Med. Chem. Lett. 21 2011 1731 1735
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 1731-1735
    • Chen, Y.1    Shan, Z.2    Peng, M.3    Fan, H.4
  • 112
    • 77957837734 scopus 로고    scopus 로고
    • Synthesis, biological assay in vitro and molecular docking studies of new imidazopyrazinone derivatives as potential dipeptidyl peptidase IV inhibitors
    • P. Lu, G. Song, Y. Zhu, and S. Xia et al. Synthesis, biological assay in vitro and molecular docking studies of new imidazopyrazinone derivatives as potential dipeptidyl peptidase IV inhibitors Eur. J. Med. Chem. 45 2010 4953 4962
    • (2010) Eur. J. Med. Chem. , vol.45 , pp. 4953-4962
    • Lu, P.1    Song, G.2    Zhu, Y.3    Xia, S.4
  • 113
    • 79957865337 scopus 로고    scopus 로고
    • Discovery of DA-1229: A potent, long acting dipeptidyl peptidase-4 inhibitor for the treatment of type 2 diabetes
    • B.J. Lee, H.J. Kim, W.Y. Kwak, and J.P. Min et al. Discovery of DA-1229: a potent, long acting dipeptidyl peptidase-4 inhibitor for the treatment of type 2 diabetes Bioorg. Med. Chem. Lett. 21 2011 3809 3812
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 3809-3812
    • Lee, B.J.1    Kim, H.J.2    Kwak, W.Y.3    Min, J.P.4
  • 114
    • 79951722945 scopus 로고    scopus 로고
    • Discovery of β-aminoacyl containing thiazolidine derivatives as potent and selective dipeptidyl peptidase IV inhibitors
    • J.H. Ahn, S.S. Kim, W.S. Park, and S.K. Kang et al. Discovery of β-aminoacyl containing thiazolidine derivatives as potent and selective dipeptidyl peptidase IV inhibitors Bioorg. Med. Chem. Lett. 21 2011 1366 1370
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 1366-1370
    • Ahn, J.H.1    Kim, S.S.2    Park, W.S.3    Kang, S.K.4
  • 117
    • 67649922154 scopus 로고    scopus 로고
    • Discovery of β-homophenylalanine based pyrrolidin-2-ylmethyl amides and sulfonamides as highly potent and selective inhibitors of dipeptidyl peptidase IV
    • S. Nordhoff, S. Cerezo-Galvez, H. Deppe, and O. Hill et al. Discovery of β-homophenylalanine based pyrrolidin-2-ylmethyl amides and sulfonamides as highly potent and selective inhibitors of dipeptidyl peptidase IV Bioorg. Med. Chem. Lett. 19 2009 4201 4203
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 4201-4203
    • Nordhoff, S.1    Cerezo-Galvez, S.2    Deppe, H.3    Hill, O.4
  • 118
    • 67651087356 scopus 로고    scopus 로고
    • From lead to preclinical candidate: Optimization of β- homophenylalanine based inhibitors of dipeptidyl peptidase IV
    • S. Nordhoff, M. Lopez-Canet, B. Hoffmann-Enger, and S. Bulat et al. From lead to preclinical candidate: optimization of β-homophenylalanine based inhibitors of dipeptidyl peptidase IV Bioorg. Med. Chem. Lett. 19 2009 4818 4823
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 4818-4823
    • Nordhoff, S.1    Lopez-Canet, M.2    Hoffmann-Enger, B.3    Bulat, S.4
  • 119
    • 71049150927 scopus 로고    scopus 로고
    • The design of potent and selective inhibitors of DPP-4: Optimization of ADME properties by amide replacements
    • S. Nordhoff, S. Bulat, S. Cerezo-Galvez, and O. Hill et al. The design of potent and selective inhibitors of DPP-4: optimization of ADME properties by amide replacements Bioorg. Med. Chem. Lett. 19 2009 6340 6345
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 6340-6345
    • Nordhoff, S.1    Bulat, S.2    Cerezo-Galvez, S.3    Hill, O.4
  • 123
    • 50949120037 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of pyrazoline analogues with β-amino acyl group as dipeptidyl peptidase IV inhibitors
    • M.A. Jun, W.S. Park, S.K. Kang, and K.Y. Kim et al. Synthesis and biological evaluation of pyrazoline analogues with β-amino acyl group as dipeptidyl peptidase IV inhibitors Eur. J. Med. Chem. 43 2008 1889 1902
    • (2008) Eur. J. Med. Chem. , vol.43 , pp. 1889-1902
    • Jun, M.A.1    Park, W.S.2    Kang, S.K.3    Kim, K.Y.4
  • 125
    • 70350072361 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of triazepane derivatives as DPP-IV inhibitors
    • J.H. Ahn, W.S. Park, M.A. Jun, M.S. Shin, and S.S. Kim et al. Synthesis and biological evaluation of triazepane derivatives as DPP-IV inhibitors J. Fluor. Chem. 130 2009 1001 1010
    • (2009) J. Fluor. Chem. , vol.130 , pp. 1001-1010
    • Ahn, J.H.1    Park, W.S.2    Jun, M.A.3    Shin, M.S.4    Kim, S.S.5
  • 126
    • 79952363348 scopus 로고    scopus 로고
    • Synthesis and evaluation of [(1R)-1-amino-2-(2,5-difluorophenyl)ethyl] cyclohexanes and 4-[(1R)-1-amino-2-(2,5-difluorophenyl)ethyl]piperidines as DPP-4 inhibitors
    • P. Chen, C.G. Caldwell, W. Ashton, and J.K. Wub et al. Synthesis and evaluation of [(1R)-1-amino-2-(2,5-difluorophenyl)ethyl]cyclohexanes and 4-[(1R)-1-amino-2-(2,5-difluorophenyl)ethyl]piperidines as DPP-4 inhibitors Bioorg. Med. Chem. Lett. 21 2011 1880 1886
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 1880-1886
    • Chen, P.1    Caldwell, C.G.2    Ashton, W.3    Wub, J.K.4
  • 129
    • 37349073397 scopus 로고    scopus 로고
    • 8-(3-(R)-aminopiperidin-1-yl)-7-but-2-ynyl-3-methyl-1-(4-methyl- quinazolin- 2-ylmethyl)-3,7-dihydropurine-2,6-dione (BI 1356), a highly potent, selective, long-acting, and orally bioavailable DPP-4 inhibitor for the treatment of type 2 diabetes
    • DOI 10.1021/jm701280z
    • M. Eckhardt, E. Langkopf, M. Mark, and M. Tadayyon et al. 8-(3-(R)-Aminopiperidin-1-yl)-7-but-2-ynyl-3- methyl-1-(4-methyl-quinazolin-2- ylmethyl)-3,7-dihydropurine-2,6-dione (BI 1356), a highly potent, selective, long-acting, and orally bioavailable DPP-4 inhibitor for the treatment of type 2 diabetes J. Med. Chem. 50 2007 6450 6453 (Pubitemid 350309082)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.26 , pp. 6450-6453
    • Eckhardt, M.1    Langkopf, E.2    Mark, M.3    Tadayyon, M.4    Thomas, L.5    Nar, H.6    Pfrengle, W.7    Guth, B.8    Lotz, R.9    Sieger, P.10    Fuchs, H.11    Himmelsbach, F.12
  • 131
    • 84856210285 scopus 로고    scopus 로고
    • Novel heterocyclic DPP-4 inhibitors for the treatment of type 2 diabetes
    • J.M. Sutton, D.E. Clark, S.J. Dunsdon, and G. Fenton et al. Novel heterocyclic DPP-4 inhibitors for the treatment of type 2 diabetes Bioorg. Med. Chem. Lett. 22 2012 1464 1468
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , pp. 1464-1468
    • Sutton, J.M.1    Clark, D.E.2    Dunsdon, S.J.3    Fenton, G.4
  • 135
    • 78650192270 scopus 로고    scopus 로고
    • Design, synthesis, and in vitro evaluation of novel aminomethyl-pyridines as DPP-4 inhibitors
    • K. Kaczanowska, K.-H. Wiesmuller, and A.-P. Schaffner Design, synthesis, and in vitro evaluation of novel aminomethyl-pyridines as DPP-4 inhibitors ACS Med. Chem. Lett. 1 2010 530 535
    • (2010) ACS Med. Chem. Lett. , vol.1 , pp. 530-535
    • Kaczanowska, K.1    Wiesmuller, K.-H.2    Schaffner, A.-P.3
  • 137
    • 77955367308 scopus 로고    scopus 로고
    • Synthesis and SAR of azolopyrimidines as potent and selective dipeptidyl peptidase-4 (DPP4) inhibitors for type 2 diabetes
    • R.P. Brigance, W. Meng, A. Fura, and T. Harrity et al. Synthesis and SAR of azolopyrimidines as potent and selective dipeptidyl peptidase-4 (DPP4) inhibitors for type 2 diabetes Bioorg Med. Chem. Lett. 20 2010 4395 4398
    • (2010) Bioorg Med. Chem. Lett. , vol.20 , pp. 4395-4398
    • Brigance, R.P.1    Meng, W.2    Fura, A.3    Harrity, T.4
  • 138
    • 77955387970 scopus 로고    scopus 로고
    • Discovery of 6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2- a]pyrimidine-2-carboxamides as potent, selective dipeptidyl peptidase-4 (DPP4) inhibitors
    • W. Meng, R.P. Brigance, H.J. Chao, and A. Fura et al. Discovery of 6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-a] pyrimidine-2-carboxamides as potent, selective dipeptidyl peptidase-4 (DPP4) inhibitors J. Med. Chem. 53 2010 5620 5628
    • (2010) J. Med. Chem. , vol.53 , pp. 5620-5628
    • Meng, W.1    Brigance, R.P.2    Chao, H.J.3    Fura, A.4
  • 139
    • 78449276647 scopus 로고    scopus 로고
    • Discovery of new chemotype dipeptidyl peptidase IV inhibitors having (R)-3-amino-3-methyl piperidine as a pharmacophore
    • Y. Nishio, H. Kimura, S. Tosaki, and E. Sugaru et al. Discovery of new chemotype dipeptidyl peptidase IV inhibitors having (R)-3-amino-3-methyl piperidine as a pharmacophore Bioorg Med. Chem. Lett. 20 2010 7246 7249
    • (2010) Bioorg Med. Chem. Lett. , vol.20 , pp. 7246-7249
    • Nishio, Y.1    Kimura, H.2    Tosaki, S.3    Sugaru, E.4
  • 140
    • 80052571269 scopus 로고    scopus 로고
    • 2-({6-[(3R)-3-amino-3-methylpiperidine-1-yl]-1,3-dimethyl-2,4-dioxo-1,2, 3,4-tetrahydro-5H-pyrrolo[3,2-d]pyrimidine-5 yl}methyl)-4- fluorobenzonitrile(DSR-12727): A potent, orally active dipeptidyl peptidase IV inhibitor without mechanism-based inactivation of CYP3A
    • Y. Nishio, H. Kimura, N. Sawada, E. Sugaru, and M. Horiguchi et al. 2-({6-[(3R)-3-amino-3-methylpiperidine-1-yl]-1,3-dimethyl-2,4-dioxo-1,2,3, 4-tetrahydro-5H-pyrrolo[3,2-d]pyrimidine-5 yl}methyl)-4-fluorobenzonitrile(DSR- 12727): a potent, orally active dipeptidyl peptidase IV inhibitor without mechanism-based inactivation of CYP3A Bioorg Med. Chem. Lett. 19 2011 5490 5499
    • (2011) Bioorg Med. Chem. Lett. , vol.19 , pp. 5490-5499
    • Nishio, Y.1    Kimura, H.2    Sawada, N.3    Sugaru, E.4    Horiguchi, M.5
  • 141
    • 80054734762 scopus 로고    scopus 로고
    • 7-Oxopyrrolopyridine-derived DPP4 inhibitors - Mitigation of CYP and hERG liabilities via introduction of polar functionalities in the active site
    • W. Wang, P. Devasthale, A. Wang, and T. Harrity et al. 7-Oxopyrrolopyridine-derived DPP4 inhibitors - mitigation of CYP and hERG liabilities via introduction of polar functionalities in the active site Bioorg Med. Chem. Lett. 21 2011 6646 6651
    • (2011) Bioorg Med. Chem. Lett. , vol.21 , pp. 6646-6651
    • Wang, W.1    Devasthale, P.2    Wang, A.3    Harrity, T.4
  • 146
    • 33750456573 scopus 로고    scopus 로고
    • Discovery of ((4R,5S)-5-amino-4-(2,4,5- trifluorophenyl)cyclohex-1-enyl)- (3- (trifluoromethyl)-5,6-dihydro- [1,2,4]triazolo[4,3-a]pyrazin-7(8H)-yl) methanone (ABT-341), a highly potent, selective, orally efficacious, and safe dipeptidyl peptidase IV inhibitor for the treatment of type 2 Diabetes
    • Z. Pei, X. Li, T.W. von Geldern, D.J. Madar, and K. Longenecker et al. Discovery of ((4R,5S)-5-amino-4-(2,4,5- trifluorophenyl)cyclohex-1-enyl)-(3- (trifluoromethyl)-5,6-dihydro- [1,2,4]triazolo[4,3-a]pyrazin-7(8H)-yl)methanone (ABT-341), a highly potent, selective, orally efficacious, and safe dipeptidyl peptidase IV inhibitor for the treatment of type 2 Diabetes J. Med. Chem. 49 2006 6439
    • (2006) J. Med. Chem. , vol.49 , pp. 6439
    • Pei, Z.1    Li, X.2    Von Geldern, T.W.3    Madar, D.J.4    Longenecker, K.5
  • 150
    • 79952363044 scopus 로고    scopus 로고
    • 1-((3S,4S)-4-Amino-1-(4-substituted-1,3,5-triazin-2-yl) pyrrolidin-3-yl)-5,5-difluoropiperidin-2-one inhibitors of DPP-4 for the treatment of type 2 diabetes
    • K.M. Andrews, D.A. Beebe, J.W. Benbow, and D.A. Boyer et al. 1-((3S,4S)-4-Amino-1-(4-substituted-1,3,5-triazin-2-yl) pyrrolidin-3-yl)-5,5- difluoropiperidin-2-one inhibitors of DPP-4 for the treatment of type 2 diabetes Bioorg. Med. Chem. Lett. 21 2011 1810 1814
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 1810-1814
    • Andrews, K.M.1    Beebe, D.A.2    Benbow, J.W.3    Boyer, D.A.4
  • 154
    • 74049162952 scopus 로고    scopus 로고
    • Discovery of carmegliptin: A potent and long-acting dipeptidyl peptidase IV inhibitor for the treatment of type 2 diabetes
    • P. Mattei, M. Boehringer, P. Di Giorgio, and H. Fischer et al. Discovery of carmegliptin: a potent and long-acting dipeptidyl peptidase IV inhibitor for the treatment of type 2 diabetes Bioorg. Med. Chem. Lett. 20 2010 1109 1113
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 1109-1113
    • Mattei, P.1    Boehringer, M.2    Di Giorgio, P.3    Fischer, H.4
  • 155
    • 74049094489 scopus 로고    scopus 로고
    • Aryl- and heteroaryl-substituted aminobenzo[a]quinolizines as dipeptidyl peptidase IV inhibitors
    • M. Boehringer, H. Fischer, M. Hennig, and D. Hunziker et al. Aryl- and heteroaryl-substituted aminobenzo[a]quinolizines as dipeptidyl peptidase IV inhibitors Bioorg. Med. Chem. Lett. 20 2010 1106 1108
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 1106-1108
    • Boehringer, M.1    Fischer, H.2    Hennig, M.3    Hunziker, D.4
  • 159
    • 84894148484 scopus 로고    scopus 로고
    • World patent (2002)2002068420
    • F. Himmelsbach,; M.Mark; M.Eckhardt; E.Langkopf; R.Maier; R.Lotz, World patent (2002)2002068420.
    • Himmelsbach, F.1
  • 160
    • 78751651182 scopus 로고    scopus 로고
    • Design and synthesis of pyrimidinone and pyrimidinedione inhibitors of dipeptidyl peptidase IV
    • Z. Zhang, M.B. Wallace, J. Feng, and J.A. Stafford et al. Design and synthesis of pyrimidinone and pyrimidinedione inhibitors of dipeptidyl peptidase IV J. Med. Chem. 54 2011 510 524
    • (2011) J. Med. Chem. , vol.54 , pp. 510-524
    • Zhang, Z.1    Wallace, M.B.2    Feng, J.3    Stafford, J.A.4
  • 161
    • 78650513267 scopus 로고    scopus 로고
    • The highly potent and selective dipeptidyl peptidase IV inhibitors bearing a thienopyrimidine scaffold effectively treat type 2 diabetes
    • J. Deng, L. Peng, G. Zhang, and X. Lan et al. The highly potent and selective dipeptidyl peptidase IV inhibitors bearing a thienopyrimidine scaffold effectively treat type 2 diabetes Eur. J. Med. Chem. 46 2011 71 76
    • (2011) Eur. J. Med. Chem. , vol.46 , pp. 71-76
    • Deng, J.1    Peng, L.2    Zhang, G.3    Lan, X.4
  • 162
    • 84860342035 scopus 로고    scopus 로고
    • Novel pyrrolopyrimidine analogues as potent dipeptidyl peptidase IV inhibitors based on pharmacokinetic property-driven optimization
    • H. Xie, L. Zeng, S. Zeng, and X. Lu et al. Novel pyrrolopyrimidine analogues as potent dipeptidyl peptidase IV inhibitors based on pharmacokinetic property-driven optimization Eur. J. Med. Chem. 52 2012 205 212
    • (2012) Eur. J. Med. Chem. , vol.52 , pp. 205-212
    • Xie, H.1    Zeng, L.2    Zeng, S.3    Lu, X.4
  • 163
    • 79961165720 scopus 로고    scopus 로고
    • Identification of 3-Aminomethyl-1,2-dihydro-4-phenyl-1-isoquinolones: A new class of potent, selective, and orally active non-peptide dipeptidyl peptidase iv inhibitors that form a unique interaction with Lys554
    • Y. Banno, Y. Miyamoto, M. Sasaki, S. Oi, and T. Asakawa et al. Identification of 3-Aminomethyl-1,2-dihydro-4-phenyl-1-isoquinolones: a new class of potent, selective, and orally active non-peptide dipeptidyl peptidase iv inhibitors that form a unique interaction with Lys554 Bioorg. Med. Chem. 19 2011 4953 4970
    • (2011) Bioorg. Med. Chem. , vol.19 , pp. 4953-4970
    • Banno, Y.1    Miyamoto, Y.2    Sasaki, M.3    Oi, S.4    Asakawa, T.5
  • 164
    • 79960553998 scopus 로고    scopus 로고
    • Discovery of potent, selective, and orally bioavailable quinoline-based dipeptidyl peptidase IV inhibitors targeting Lys554
    • H. Maezaki, Y. Banno, Y. Miyamoto, and Y. Moritou et al. Discovery of potent, selective, and orally bioavailable quinoline-based dipeptidyl peptidase IV inhibitors targeting Lys554 Bioorg. Med. Chem. 19 2011 4482 4498
    • (2011) Bioorg. Med. Chem. , vol.19 , pp. 4482-4498
    • Maezaki, H.1    Banno, Y.2    Miyamoto, Y.3    Moritou, Y.4
  • 165
    • 79851501708 scopus 로고    scopus 로고
    • Discovery of a 3-pyridylacetic acid derivative (TAK-100) as a potent, selective and orally active dipeptidyl peptidase IV (DPP-4) inhibitor
    • Y. Miyamoto, Y. Banno, T. Yamashita, and T. Fujimoto et al. Discovery of a 3-pyridylacetic acid derivative (TAK-100) as a potent, selective and orally active dipeptidyl peptidase IV (DPP-4) inhibitor J. Med. Chem. 54 2011 831 850
    • (2011) J. Med. Chem. , vol.54 , pp. 831-850
    • Miyamoto, Y.1    Banno, Y.2    Yamashita, T.3    Fujimoto, T.4
  • 166
    • 78650744466 scopus 로고    scopus 로고
    • Design and synthesis of 3-pyridylacetamide derivatives as dipeptidyl peptidase IV (DPP-4) inhibitors targeting a bidentate interaction with Arg125
    • Y. Miyamoto, Y. Banno, T. Yamashita, and T. Fujimoto et al. Design and synthesis of 3-pyridylacetamide derivatives as dipeptidyl peptidase IV (DPP-4) inhibitors targeting a bidentate interaction with Arg125 Bioorg. Med. Chem. 19 2011 172 185
    • (2011) Bioorg. Med. Chem. , vol.19 , pp. 172-185
    • Miyamoto, Y.1    Banno, Y.2    Yamashita, T.3    Fujimoto, T.4
  • 167
    • 84866424769 scopus 로고    scopus 로고
    • Discovery of 3H-imidazo[4,5-c]quinolin-4(5H)-ones as potent and selective dipeptidyl peptidase IV (DPP-4) inhibitors
    • Y. Ikuma, H. Hochigai, H. Kimura, and N. Nunami et al. Discovery of 3H-imidazo[4,5-c]quinolin-4(5H)-ones as potent and selective dipeptidyl peptidase IV (DPP-4) inhibitors Bioorg. Med. Chem. 20 2012 5864 5883
    • (2012) Bioorg. Med. Chem. , vol.20 , pp. 5864-5883
    • Ikuma, Y.1    Hochigai, H.2    Kimura, H.3    Nunami, N.4
  • 168
    • 53549098210 scopus 로고    scopus 로고
    • Thalidomide as a multi-template for development of biologically active compounds
    • Y. Hashimoto Thalidomide as a multi-template for development of biologically active compounds Arch. Pharm. Chem. Life. Sci. 341 2008 536 547
    • (2008) Arch. Pharm. Chem. Life. Sci. , vol.341 , pp. 536-547
    • Hashimoto, Y.1
  • 169
    • 0036158279 scopus 로고    scopus 로고
    • Structural development of biological response modifiers based on thalidomide
    • DOI 10.1016/S0968-0896(01)00308-X, PII S096808960100308X
    • Y. Hashimoto Structural development of biological response modifiers based on thalidomide Bioorg. Med. Chem. 10 2002 461 479 (Pubitemid 34112438)
    • (2002) Bioorganic and Medicinal Chemistry , vol.10 , Issue.3 , pp. 461-479
    • Hashimoto, Y.1
  • 170
    • 0041324659 scopus 로고    scopus 로고
    • Structural development of synthetic retinoids and thalidomide-related molecules
    • Y. Hashimoto Structural development of synthetic retinoids and thalidomide-related molecules Cancer Chemother. Pharmacol. 52 2003 S16 S23
    • (2003) Cancer Chemother. Pharmacol. , vol.52
    • Hashimoto, Y.1
  • 171
    • 2642512949 scopus 로고    scopus 로고
    • Thalidomide as a multitarget drug and its application as a template for drug design
    • DOI 10.1358/dof.2004.029.04.792298
    • Y. Hashimoto, A. Tanatani, K. Nagasawa, and H. Miyachi Thalidomide as a target drug and its application as a template for drug design Drugs Future 29 2004 383 391 (Pubitemid 38724680)
    • (2004) Drugs of the Future , vol.29 , Issue.4 , pp. 383-391
    • Hashimoto, Y.1    Tanatani, A.2    Nagasawa, K.3    Miyachi, H.4
  • 172
    • 0031837706 scopus 로고    scopus 로고
    • Novel biological response modifiers derived from thalidomide
    • Y. Hashimoto Novel biological response modifiers derived from thalidomide Curr. Med. Chem. 5 1998 163 178 (Pubitemid 28238487)
    • (1998) Current Medicinal Chemistry , vol.5 , Issue.3 , pp. 163-178
    • Hashimoto, Y.1
  • 173
    • 0013212945 scopus 로고    scopus 로고
    • Structural development of biological response modifiers based on retinoids and thalidomide
    • Y. Hashimoto Structural development of biological response modifiers based on retinoids and thalidomide Mini-Rev. Med. Chem. 2 2002 543 551
    • (2002) Mini-Rev. Med. Chem. , vol.2 , pp. 543-551
    • Hashimoto, Y.1
  • 174
    • 79955551684 scopus 로고    scopus 로고
    • Non-competitive and selective dipeptidyl peptidase IV inhibitors with phenethylphenylphthalimide skeleton derived from thalidomide-related α-glucosidase inhibitors and liver X receptor antagonists
    • K. Motoshima, K. Sugita, Y. Hashimoto, and M. Ishikawa Non-competitive and selective dipeptidyl peptidase IV inhibitors with phenethylphenylphthalimide skeleton derived from thalidomide-related α-glucosidase inhibitors and liver X receptor antagonists Bioorg. Med. Chem. Lett. 21 2011 3041 3045
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 3041-3045
    • Motoshima, K.1    Sugita, K.2    Hashimoto, Y.3    Ishikawa, M.4
  • 175
    • 80054933500 scopus 로고    scopus 로고
    • Recent patents of dipeptidyl peptidase IV inhibitors
    • E. Giralt, L. Mendieta, and T. Tarrago et al. Recent patents of dipeptidyl peptidase IV inhibitors Expert Opin. Ther. Pat. 21 2011 1693 1741
    • (2011) Expert Opin. Ther. Pat. , vol.21 , pp. 1693-1741
    • Giralt, E.1    Mendieta, L.2    Tarrago, T.3
  • 178
    • 84894162720 scopus 로고    scopus 로고
    • Nippi, DPP-4 inhibitor, May 10 (2013)WO 2013/65832 A1
    • Nippi, DPP-4 inhibitor, May 10 (2013)WO 2013/65832 A1.
  • 270
    • 0037787851 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV from bench to bedside: An update on structural properties, functions, and clinical aspects of the enzyme DPP IV
    • A.M. Lambeir, C. Durinx, and S. Scharpe et al. Dipeptidylpeptidase IV from bench to bedside: an update on structural properties, functions, and clinical aspects of the enzyme DPP IV Crit. Rev. Clin. Lab. Sci. 40 2003 209 294 (Pubitemid 36775376)
    • (2003) Critical Reviews in Clinical Laboratory Sciences , vol.40 , Issue.3 , pp. 209-294
    • Lambeir, A.-M.1    Durinx, C.2    Scharpe, S.3    De Meester, I.4
  • 271
    • 34248223285 scopus 로고    scopus 로고
    • Biology of Incretins: GLP-1 and GIP
    • DOI 10.1053/j.gastro.2007.03.054, PII S001650850700580X
    • L.L. Baggio, and D.J. Drucker Biology of incretins: GLP-1 and GIP Gastroenterology 132 2007 2131 2157 (Pubitemid 46711096)
    • (2007) Gastroenterology , vol.132 , Issue.6 , pp. 2131-2157
    • Baggio, L.L.1    Drucker, D.J.2
  • 273
    • 27844453866 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV activity and/or structure homologs: Contributing factors in the pathogenesis of rheumatoid arthritis?
    • DOI 10.1186/ar1852
    • Sedo, J.S. Duke-Cohan, and E. Balaziova et al. Dipeptidyl peptidase IV activity and/or structure homologs: contributing factors in the pathogenesis of rheumatoid arthritis? Arthritis Res. Ther. 7 2005 253 269 (Pubitemid 41646256)
    • (2005) Arthritis Research and Therapy , vol.7 , Issue.6 , pp. 253-269
    • Sedo, A.1    Duke-Cohan, J.S.2    Balaziova, E.3    Sedova, L.R.4
  • 274
    • 84866988553 scopus 로고    scopus 로고
    • Is dipeptidyl peptidase IV (DPP IV) associated with inflammation present in human spondyloarthritides and rheumatoid arthritis
    • D. Detel, T. Kehler, and S. Buljevic et al. Is dipeptidyl peptidase IV (DPP IV) associated with inflammation present in human spondyloarthritides and rheumatoid arthritis Croat. Chem. Acta 85 2012 231 238
    • (2012) Croat. Chem. Acta , vol.85 , pp. 231-238
    • Detel, D.1    Kehler, T.2    Buljevic, S.3
  • 275
    • 0024346019 scopus 로고
    • Activities of dipeptidyl peptidase II and dipeptidyl peptidase IV in synovial fluid from patients with rheumatoid arthritis and osteoarthritis
    • H. Gotoh et al. Activities of dipeptidyl peptidase II and dipeptidyl peptidase IV in synovial fluid from patients with rheumatoid arthritis and osteoarthritis Clin. Chem. 35 1989 1016 1018 (Pubitemid 19161276)
    • (1989) Clinical Chemistry , vol.35 , Issue.6 , pp. 1016-1018
    • Gotoh, H.1    Hagihara, M.2    Nagatsu, T.3    Iwata, H.4    Miura, T.5
  • 276
    • 77951725805 scopus 로고    scopus 로고
    • Inhibition of fibroblast activation protein and dipeptidylpeptidase 4 increases cartilage invasion by rheumatoid arthritissynovial fibroblasts
    • C. Ospelt, J.C. Mertens, and A. Jungel et al. Inhibition of fibroblast activation protein and dipeptidylpeptidase 4 increases cartilage invasion by rheumatoid arthritissynovial fibroblasts Arthritis Rheum. 62 2010 1224 1235
    • (2010) Arthritis Rheum. , vol.62 , pp. 1224-1235
    • Ospelt, C.1    Mertens, J.C.2    Jungel, A.3
  • 278
    • 69049119483 scopus 로고    scopus 로고
    • Duke-Cohan. Dipeptidyl peptidase-IV and related molecules: Markers of malignancy?
    • J. Sedo, P. Stremenova, and J. Busek Duke-Cohan. Dipeptidyl peptidase-IV and related molecules: markers of malignancy? Expert Opin. Med. Diag. 2 2008 677 689
    • (2008) Expert Opin. Med. Diag. , vol.2 , pp. 677-689
    • Sedo, J.1    Stremenova, P.2    Busek, J.3
  • 280
    • 33646416468 scopus 로고    scopus 로고
    • The protease complex consisting of dipeptidyl peptidase IV and seprase plays a role in the migration and invasion of human endothelial cells in collagenous matrices
    • G. Ghersi, Q. Zhao, M. Salamone, and Y. Yeh et al. The protease complex consisting of dipeptidyl peptidase IV and seprase plays a role in the migration and invasion of human endothelial cells in collagenous matrices Cancer Res. 66 2006 4652 4661
    • (2006) Cancer Res. , vol.66 , pp. 4652-4661
    • Ghersi, G.1    Zhao, Q.2    Salamone, M.3    Yeh, Y.4
  • 281
    • 59149096596 scopus 로고    scopus 로고
    • Suppression of neuroblastoma growth by dipeptidyl peptidase IV: Relevance of chemokine regulation and caspase activation
    • W.T. Arscott, A.E. LaBauve, V. May, and U.V. Wesley Suppression of neuroblastoma growth by dipeptidyl peptidase IV: relevance of chemokine regulation and caspase activation Oncogene 28 2009 479 491
    • (2009) Oncogene , vol.28 , pp. 479-491
    • Arscott, W.T.1    Labauve, A.E.2    May, V.3    Wesley, U.V.4
  • 282
    • 6344253102 scopus 로고    scopus 로고
    • CD26/dipeptidyl peptidase IV and its role in cancer
    • B. Pro, and N.H. Dang CD26/dipeptidyl peptidase IV and its role in cancer Histol. Histopathol. 19 2004 1345 1351 (Pubitemid 39386791)
    • (2004) Histology and Histopathology , vol.19 , Issue.4 , pp. 1345-1351
    • Pro, B.1    Dang, N.H.2
  • 283
    • 77952814507 scopus 로고    scopus 로고
    • Inhibition of multifunctional dipeptidyl peptidase-IV: Is there a risk of oncological and immunological adverse effects?
    • T. Stulc, and A. Sedo Inhibition of multifunctional dipeptidyl peptidase-IV: is there a risk of oncological and immunological adverse effects? Diabetes Res. Clin. Pr. 88 2010 125 131
    • (2010) Diabetes Res. Clin. Pr. , vol.88 , pp. 125-131
    • Stulc, T.1    Sedo, A.2
  • 284
    • 84886587432 scopus 로고    scopus 로고
    • Prescribing gliptins: Enthusiasm should be coupled with caution
    • M.K. Garg, S. Kharb, and A. Pandit Prescribing gliptins: enthusiasm should be coupled with caution Ind. J. Endocrinol. Metab. 16 2012 324 325
    • (2012) Ind. J. Endocrinol. Metab. , vol.16 , pp. 324-325
    • Garg, M.K.1    Kharb, S.2    Pandit, A.3
  • 285
    • 84860638209 scopus 로고    scopus 로고
    • The cardiovascular effects of GLP-1 receptor agonists
    • T. Okerson, and R.J. Chilton The cardiovascular effects of GLP-1 receptor agonists Cardiovasc. Ther. 30 2012 e146 e155
    • (2012) Cardiovasc. Ther. , vol.30
    • Okerson, T.1    Chilton, R.J.2
  • 286
    • 79951884751 scopus 로고    scopus 로고
    • Glucagon-like peptide-1-based therapies and cardiovascular disease: Looking beyond glycaemic control
    • P. Anagnostis, V.G. Athyros, F. Adamidou, and A. Panagiotou et al. Glucagon-like peptide-1-based therapies and cardiovascular disease: looking beyond glycaemic control Diabetes Obes. Metab. 13 2011 302 312
    • (2011) Diabetes Obes. Metab. , vol.13 , pp. 302-312
    • Anagnostis, P.1    Athyros, V.G.2    Adamidou, F.3    Panagiotou, A.4
  • 287
    • 80051795160 scopus 로고    scopus 로고
    • Cardiovascular effects of DPP-4 inhibition: Beyond GLP-1
    • G.P. Fadini, and A. Avogaro Cardiovascular effects of DPP-4 inhibition: beyond GLP-1 Vasc. Pharmacol. 55 2011 10 16
    • (2011) Vasc. Pharmacol. , vol.55 , pp. 10-16
    • Fadini, G.P.1    Avogaro, A.2
  • 288
    • 62949195390 scopus 로고    scopus 로고
    • Synergy between CD26/DPP IV inhibition and G-CSF improves cardiac function after acute myocardial infarction
    • M.M. Zaruba, H.D. Theiss, M. Vallaster, and U. Mehl et al. Synergy between CD26/DPP IV inhibition and G-CSF improves cardiac function after acute myocardial infarction Cell. Stem Cell. 4 2009 313 323
    • (2009) Cell. Stem Cell. , vol.4 , pp. 313-323
    • Zaruba, M.M.1    Theiss, H.D.2    Vallaster, M.3    Mehl, U.4
  • 289
    • 36448936053 scopus 로고    scopus 로고
    • Common pathological processes in Alzheimer disease and type 2 diabetes: A review
    • DOI 10.1016/j.brainresrev.2007.09.001, PII S0165017307001907
    • L. Li, and C. Holscher Common pathological processes in Alzheimer disease and type 2 diabetes: a review Brain Res. Rev. 56 2007 384 402 (Pubitemid 350166529)
    • (2007) Brain Research Reviews , vol.56 , Issue.2 , pp. 384-402
    • Li, L.1    Holscher, C.2
  • 290
    • 76749116176 scopus 로고    scopus 로고
    • Long-term inhibition of dipeptidyl peptidase-4 in Alzheimer's prone mice
    • M.D. Amico, C.D. Filippo, and R. Marfella et al. Long-term inhibition of dipeptidyl peptidase-4 in Alzheimer's prone mice Exp. Gerontol. 45 2010 202 207
    • (2010) Exp. Gerontol. , vol.45 , pp. 202-207
    • Amico, M.D.1    Filippo, C.D.2    Marfella, R.3
  • 293
    • 49849094738 scopus 로고    scopus 로고
    • Physiochemical drug properties associated with in vivo toxicological outcomes
    • J.D. Hughes, J. Blagg, D.A. Price, and S. Bailey et al. Physiochemical drug properties associated with in vivo toxicological outcomes Bioorg. Med. Chem. Lett. 18 2008 4872 4875
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 4872-4875
    • Hughes, J.D.1    Blagg, J.2    Price, D.A.3    Bailey, S.4
  • 294
    • 78650915884 scopus 로고    scopus 로고
    • RBx-0597, a potent, selective and slow-binding inhibitor of dipeptidyl peptidase-IV for the treatment of type 2 diabetes
    • S. Singh, S. Sethi, V. Khanna, and B. Benjamin et al. RBx-0597, a potent, selective and slow-binding inhibitor of dipeptidyl peptidase-IV for the treatment of type 2 diabetes Eur. J. Pharmacol. 652 2011 157 163
    • (2011) Eur. J. Pharmacol. , vol.652 , pp. 157-163
    • Singh, S.1    Sethi, S.2    Khanna, V.3    Benjamin, B.4
  • 295
    • 77955456705 scopus 로고    scopus 로고
    • Pharmacokinetics of dipeptidylpeptidase-4 inhibitors
    • A.J. Scheen Pharmacokinetics of dipeptidylpeptidase-4 inhibitors Diabetes Obes. Metab. 12 2010 648 658
    • (2010) Diabetes Obes. Metab. , vol.12 , pp. 648-658
    • Scheen, A.J.1
  • 296
    • 84861683713 scopus 로고    scopus 로고
    • Clinical pharmacokinetics and pharmacodynamics of linalglitin
    • U. Graefe-Mody, S. Retlich, and C. Friedrich Clinical pharmacokinetics and pharmacodynamics of linalglitin Clin. Pharmacokinet. 51 2012 411 427
    • (2012) Clin. Pharmacokinet. , vol.51 , pp. 411-427
    • Graefe-Mody, U.1    Retlich, S.2    Friedrich, C.3
  • 297
    • 84863735141 scopus 로고    scopus 로고
    • Modulation of cytochrome-P450 inhibition (CYP) in drug discovery: A medicinal chemistry perspective
    • S. Kumar, R. Sharma, and A. Roychowdhury modulation of cytochrome-P450 inhibition (CYP) in drug discovery: a medicinal chemistry perspective Curr. Med. Chem. 19 2012 3605 3621
    • (2012) Curr. Med. Chem. , vol.19 , pp. 3605-3621
    • Kumar, S.1    Sharma, R.2    Roychowdhury, A.3
  • 298
    • 33745413284 scopus 로고    scopus 로고
    • Quantitative structure - Activity relationship studies on inhibition of HERG potassium channels
    • DOI 10.1021/ci050450g
    • K. Yoshida, and T. Niwa Quantitative structure-activity relationship studies on inhibition of hERG potassium channels J. Chem. Inf. Model 46 2006 1371 1378 (Pubitemid 43999180)
    • (2006) Journal of Chemical Information and Modeling , vol.46 , Issue.3 , pp. 1371-1378
    • Yoshida, K.1    Niwa, T.2
  • 299
    • 78049442434 scopus 로고    scopus 로고
    • In silico binary classification QSAR models based on 4D-fingerprints and MOE descriptors for prediction of hERG blockage
    • B.-H. Su, M.-Y. Shen, E.X. Esposito, and A.J. Hopfinger et al. In silico binary classification QSAR models based on 4D-fingerprints and MOE descriptors for prediction of hERG blockage J. Chem. Inf. Model 50 2010 1304 1318
    • (2010) J. Chem. Inf. Model , vol.50 , pp. 1304-1318
    • Su, B.-H.1    Shen, M.-Y.2    Esposito, E.X.3    Hopfinger, A.J.4
  • 300
    • 0038487659 scopus 로고    scopus 로고
    • Prediction of hERG potassium channel affinity by traditional and hologram QSAR methods
    • DOI 10.1016/S0960-894X(03)00492-X
    • G. Keseru Prediction of hERG potassium channel affinity by traditional and hologram qSAR methods Bioorg. Chem. Med. Lett. 13 2003 2773 2775 (Pubitemid 36851568)
    • (2003) Bioorganic and Medicinal Chemistry Letters , vol.13 , Issue.16 , pp. 2773-2775
    • Keseru, G.M.1
  • 301
    • 33244474244 scopus 로고    scopus 로고
    • Development and evaluation of an in silico model for hERG binding
    • M. Song, and M. Clark Development and evaluation of an in silico model for hERG binding J. Chem. Inf. Model 46 2005 392 400
    • (2005) J. Chem. Inf. Model , vol.46 , pp. 392-400
    • Song, M.1    Clark, M.2
  • 302
    • 33644971220 scopus 로고    scopus 로고
    • Prediction of hERG potassium channel affinity by the CODESSA approach
    • Coi, I. Massarelli, L. Murgia, and M. Saraceno et al. Prediction of hERG potassium channel affinity by the CODESSA approach Bioorg. Med. Chem. 14 2006 3153 3159
    • (2006) Bioorg. Med. Chem. , vol.14 , pp. 3153-3159
    • Coi1    Massarelli, I.2    Murgia, L.3    Saraceno, M.4
  • 303
    • 82355160734 scopus 로고    scopus 로고
    • A critical assessment of combined ligand- and structure-based approaches to hERG channel blocker modeling
    • L. Du-Cuny, L. Chen, and S. Zhang A critical assessment of combined ligand- and structure-based approaches to hERG channel blocker modeling J. Chem. Inf. Model 51 2011 2948 2960
    • (2011) J. Chem. Inf. Model , vol.51 , pp. 2948-2960
    • Du-Cuny, L.1    Chen, L.2    Zhang, S.3
  • 304
    • 0037194634 scopus 로고    scopus 로고
    • + channel blockers
    • DOI 10.1021/jm0208875
    • Cavalli, E. Poluzzi, F. De Ponti, and M. Recanatini Toward a pharmacophore for drugs inducing the long QT syndrome: insights from a CoMFA study of hERG K+ channel blockers J. Med. Chem. 45 2002 3844 3853 (Pubitemid 35024289)
    • (2002) Journal of Medicinal Chemistry , vol.45 , Issue.18 , pp. 3844-3853
    • Cavalli, A.1    Poluzzi, E.2    De Ponti, F.3    Recanatini, M.4
  • 305
    • 0036229805 scopus 로고    scopus 로고
    • Three-dimensional quantitative structure-activity relationship for inhibition of human ether-a-go-go-related gene potassium channel
    • DOI 10.1124/jpet.301.2.427
    • S. Ekins, W.J. Crumb, R.D. Sarazan, and J.H. Wikel et al. A three-dimensional quantitative stucture-activity relationship for inhibition of human ether-a-go-go-related gene potassium channel J. Pharmacol. Exp. Ther. 301 2002 427 434 (Pubitemid 34429951)
    • (2002) Journal of Pharmacology and Experimental Therapeutics , vol.301 , Issue.2 , pp. 427-434
    • Ekins, S.1    Crumb, W.J.2    Dustan Sarazan, R.3    Wikel, J.H.4    Wrighton, S.A.5
  • 307
    • 33750998518 scopus 로고    scopus 로고
    • Common pharmacophores for uncharged human ether-a-go-go-related gene (hERG) blockers
    • DOI 10.1021/jm060500o
    • A.M. Aronov Common pharmacophores for uncharged human ether-a-go-go-related gene (hERG) blockers J. Med. Chem. 49 2006 6917 6921 (Pubitemid 44749757)
    • (2006) Journal of Medicinal Chemistry , vol.49 , Issue.23 , pp. 6917-6921
    • Aronov, A.M.1
  • 309
    • 79952124934 scopus 로고    scopus 로고
    • Combined receptor and ligand-based approach to the universal pharmacophore model development for studies of drug blockade to the hERG pore domain
    • S. Durdagi, H.J. Duff, and S.Y. Noskov Combined receptor and ligand-based approach to the universal pharmacophore model development for studies of drug blockade to the hERG pore domain J. Chem. Inf. Model. 51 2011 463 474
    • (2011) J. Chem. Inf. Model. , vol.51 , pp. 463-474
    • Durdagi, S.1    Duff, H.J.2    Noskov, S.Y.3
  • 311
    • 84860310064 scopus 로고    scopus 로고
    • Computational design and discovery of "minimally structured" hERG blockers
    • A. Cavalli, R. Buonfiglio, and C. Ianni et al. Computational design and discovery of "minimally structured" hERG blockers J. Med. Chem. 55 2012 4010 4014
    • (2012) J. Med. Chem. , vol.55 , pp. 4010-4014
    • Cavalli, A.1    Buonfiglio, R.2    Ianni, C.3
  • 312
    • 13844254976 scopus 로고    scopus 로고
    • Predictive in silico modeling for hERG channel blockers
    • DOI 10.1016/S1359-6446(04)03278-7, PII S1359644604032787
    • A.M. Aronov Predictive in-silico modelling for hERG channel blockers Drug. Discov. Today 10 2005 149 155 (Pubitemid 40247813)
    • (2005) Drug Discovery Today , vol.10 , Issue.2 , pp. 149-155
    • Aronov, A.M.1


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