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Volumn 13, Issue 4, 2003, Pages 499-510

Dipeptidyl peptidase IV inhibitors as new therapeutic agents for the treament of type 2 diabetes

Author keywords

Dipeptidyl peptidase (DPP) IV; DPP IV inhibitors; Glucagon like peptide 1 (GLP 1); Incretin hormones; Type 2 diabetes

Indexed keywords

2,4 THIAZOLIDINEDIONE DERIVATIVE; 6 [[2 [[2 (2 CYANO 1 PYRROLIDINYL) 2 OXOETHYL]AMINO]ETHYL]AMINO]NICOTINONITRILE; 7 BENZYL 1,3 BISMETHYL 8 (1 PIPERAZINYL)XANTHINE; ACARBOSE; ALKENE DERIVATIVE; ANTIDIABETIC AGENT; BIGUANIDE DERIVATIVE; CARBOXYLIC ACID DERIVATIVE; DIPEPTIDYL PEPTIDASE IV; DIPEPTIDYL PEPTIDASE IV INHIBITOR; FE 999011; GASTRIC INHIBITORY POLYPEPTIDE; GLUCAGON LIKE PEPTIDE 1; GLUCOSE; GLYCYLPROLYLISOLEUCYLTHIAZOLIDIDE; INSULIN; ISOLEUCINE THIAZOLIDIDE; ISOLEUCYLTHIAZOLIDIDE; METFORMIN; NITRILE; ORAL ANTIDIABETIC AGENT; PHOSPHONIC ACID DERIVATIVE; PYRROLIDINE DERIVATIVE; SULFONYLUREA DERIVATIVE; THIAZOLIDINE DERIVATIVE; THIOAMIDE; TSL 225; UNCLASSIFIED DRUG; UNINDEXED DRUG; VALYLPYRROLIDIDE; VILDAGLIPTIN; XANTHINE DERIVATIVE;

EID: 0037397603     PISSN: 13543776     EISSN: None     Source Type: Journal    
DOI: 10.1517/13543776.13.4.499     Document Type: Review
Times cited : (65)

References (62)
  • 1
    • 0034235964 scopus 로고    scopus 로고
    • Potential new treatments for Type 2 diabetes
    • BAILEY CJ: Potential new treatments for Type 2 diabetes. Trends In Pharmacol. Sci. (2000) 21:259-265.
    • (2000) Trends In Pharmacol. Sci. , vol.21 , pp. 259-265
    • Bailey, C.J.1
  • 2
    • 0033866831 scopus 로고    scopus 로고
    • New approaches in the treatment of Type 2 diabetes
    • ZHANG BB, MOLLER DE: New approaches in the treatment of Type 2 diabetes. Curr. Opin. Chem. Biol. (2000) 4:461-467.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 461-467
    • Zhang, B.B.1    Moller, D.E.2
  • 4
    • 0034967893 scopus 로고    scopus 로고
    • The entero-insular axis in Type 2 diabetes - Incretins as therapeutic agents
    • CREUTZFELDT W: The entero-insular axis in Type 2 diabetes - incretins as therapeutic agents. Exp. Clin. Endocrinol. Diabetes (2001) 109(Suppl.2):S288-S303.
    • (2001) Exp. Clin. Endocrinol. Diabetes , vol.109 , Issue.SUPPL. 2
    • Creutzfeldt, W.1
  • 5
    • 0022617246 scopus 로고
    • Reduced incretin effect in Type 2 (non-insulin-dependent) diabetes
    • NAUCK MA, STOCKMANN F, EBERT R, CREUTZFELDT W: Reduced incretin effect in Type 2 (non-insulin-dependent) diabetes. Diabetologia (1986) 29:46-52.
    • (1986) Diabetologia , vol.29 , pp. 46-52
    • Nauck, M.A.1    Stockmann, F.2    Ebert, R.3    Creutzfeldt, W.4
  • 6
    • 0027391607 scopus 로고
    • Preserved incretin activity of GLP-1 [7-36 amide] but not of synthetic human GIP in patients with Type-2-diabetes mellitus
    • NAUCK MA, HEIMESAAT MM, ÖRSKOV C, HOLST JJ, EBERT R, CREUTZFELDT W: Preserved incretin activity of GLP-1 [7-36 amide] but not of synthetic human GIP in patients with Type-2-diabetes mellitus. J. Clin. Invest. (1993) 91:301-307.
    • (1993) J. Clin. Invest. , vol.91 , pp. 301-307
    • Nauck, M.A.1    Heimesaat, M.M.2    örskov, C.3    Holst, J.J.4    Ebert, R.5    Creutzfeldt, W.6
  • 7
    • 0031033531 scopus 로고    scopus 로고
    • Near-normalisation of diurnal glucose concentrations by continuous administration of glucagon-like peptide 1 (GLP-1) in subjects with NIDDM
    • RACHMAN J, BARROW BA, LEVY JC, TURNER RC: Near-normalisation of diurnal glucose concentrations by continuous administration of glucagon-like peptide 1 (GLP-1) in subjects with NIDDM. Diabetologia (1997) 40:205-211.
    • (1997) Diabetologia , vol.40 , pp. 205-211
    • Rachman, J.1    Barrow, B.A.2    Levy, J.C.3    Turner, R.C.4
  • 8
  • 9
    • 0030607672 scopus 로고    scopus 로고
    • Glucagon-like peptide-1-[9-36] amide is a major metabolite of glucagon-like peptide-1-[7-36] amide after in vivo administration to dogs, and it acts as an antagonist on the pancreatic receptor
    • KNUDSEN LB, PRIDAL L: Glucagon-like peptide-1-[9-36] amide is a major metabolite of glucagon-like peptide-1-[7-36] amide after in vivo administration to dogs, and it acts as an antagonist on the pancreatic receptor. Eur. J. Pharmacol. (1996) 318:429-435.
    • (1996) Eur. J. Pharmacol. , vol.318 , pp. 429-435
    • Knudsen, L.B.1    Pridal, L.2
  • 11
    • 0034473089 scopus 로고    scopus 로고
    • Natural substrates of dipeptidyl peptidase IV
    • DE MEESTER I, DURINX C, BAL G et al.: Natural substrates of dipeptidyl peptidase IV. Adv. Exp. Med. Biol. (2000) 477:67-87.
    • (2000) Adv. Exp. Med. Biol. , vol.477 , pp. 67-87
    • De Meester, I.1    Durinx, C.2    Bal, G.3
  • 12
    • 0033619675 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides
    • MENTLEIN R: Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides. Regul. Pept. (1999) 85:9-24.
    • (1999) Regul. Pept. , vol.85 , pp. 9-24
    • Mentlein, R.1
  • 13
    • 0032961099 scopus 로고    scopus 로고
    • The unique properties of dipeptidyl-peptidase IV (DPP IV/CD26) and the therapeutic potential of DPP IV inhibitors
    • AUGUSTYNS K, BAL G, THONUS G et al.: The unique properties of dipeptidyl-peptidase IV (DPP IV/CD26) and the therapeutic potential of DPP IV inhibitors. Curr. Med. Chem. (1999) 6:311-327.
    • (1999) Curr. Med. Chem. , vol.6 , pp. 311-327
    • Augustyns, K.1    Bal, G.2    Thonus, G.3
  • 15
    • 0027215348 scopus 로고
    • Dipeptidyl-peptidase IV hydrolyses gastric inhihitory polypeptide, glucagon-like peptide-1[7-36]amide, peptide histidine methionine and is responsible for their degradation in human serum
    • MENTLEIN R, GALLWITZ B, SCHMIDT E: Dipeptidyl-peptidase IV hydrolyses gastric inhihitory polypeptide, glucagon-like peptide-1[7-36]amide, peptide histidine methionine and is responsible for their degradation in human serum. Eur. J. Biochem. (1993) 214:829-835.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 829-835
    • Mentlein, R.1    Gallwitz, B.2    Schmidt, E.3
  • 16
    • 0029118049 scopus 로고    scopus 로고
    • Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV
    • KIEFFER TJ, MCINTOSH CHS, PEDERSON RA. Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV. Endocrinology (1998) 136:3585-3596.
    • (1998) Endocrinology , vol.136 , pp. 3585-3596
    • Kieffer, T.J.1    Mcintosh, C.H.S.2    Pederson, R.A.3
  • 17
    • 0033303516 scopus 로고    scopus 로고
    • Glucagon-like peptide-1-[7-36] amide is transformed to glucagon-like peptide-1-[9-36]amide by dipeptidyl peptidase IV in the capillaries supplying the L cells of the porcine intestine
    • HANSEN L, DEACON CF, ORSKOV C, HOLST JJ: Glucagon-like peptide-1-[7-36] amide is transformed to glucagon-like peptide-1-[9-36]amide by dipeptidyl peptidase IV in the capillaries supplying the L cells of the porcine intestine. Endocrinology (1999) 140:5356-5363.
    • (1999) Endocrinology , vol.140 , pp. 5356-5363
    • Hansen, L.1    Deacon, C.F.2    Orskov, C.3    Holst, J.J.4
  • 19
    • 0032701468 scopus 로고    scopus 로고
    • Glucagon-like peptide-1, a gastrointestinal hormone with a pharmaceutical potential
    • HOLST JJ: Glucagon-like peptide-1, a gastrointestinal hormone with a pharmaceutical potential. Curr. Med. Chem. (1999) 6:1005-1017.
    • (1999) Curr. Med. Chem. , vol.6 , pp. 1005-1017
    • Holst, J.J.1
  • 20
    • 0034857141 scopus 로고    scopus 로고
    • Development of glucagon-like peptide-1-based pharmaceuticals as therapeutic agents for the treatment of diabetes
    • DRUCKER DJ: Development of glucagon-like peptide-1-based pharmaceuticals as therapeutic agents for the treatment of diabetes. Curr. Pharm. Des. (2001) 7:1399-1412.
    • (2001) Curr. Pharm. Des. , vol.7 , pp. 1399-1412
    • Drucker, D.J.1
  • 21
    • 0031916924 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibition potentiates the insulinotropic effect of glucagon-like peptide 1 in the anesthetized pig
    • DEACON CF, HUGHES TE, HOLST JJ: Dipeptidyl peptidase IV inhibition potentiates the insulinotropic effect of glucagon-like peptide 1 in the anesthetized pig. Diabetes (1998) 47:764-769.
    • (1998) Diabetes , vol.47 , pp. 764-769
    • Deacon, C.F.1    Hughes, T.E.2    Holst, J.J.3
  • 22
    • 0034612348 scopus 로고    scopus 로고
    • Enhanced insulin secretion and improved glucose tolerance in mice lacking CD26
    • MARGUET D, BAGGIO L, KOBAYASHI T et al.: Enhanced insulin secretion and improved glucose tolerance in mice lacking CD26. Proc. Nat. Acad. Sci. USA (2000) 97:6874-6879.
    • (2000) Proc. Nat. Acad. Sci. USA , vol.97 , pp. 6874-6879
    • Marguet, D.1    Baggio, L.2    Kobayashi, T.3
  • 23
    • 0034811909 scopus 로고    scopus 로고
    • Improved glucose tolerance via enhanced glucose-dependent insulin secretion in dipeptidyl peptidase IV-deficient fischer rats
    • NAGAKURA T, YASUDA N, YAMAZAKI K et al.: Improved glucose tolerance via enhanced glucose-dependent insulin secretion in dipeptidyl peptidase IV-deficient fischer rats. Biochem. Biophys. Res. Comm. (2001) 284:501-506.
    • (2001) Biochem. Biophys. Res. Comm. , vol.284 , pp. 501-506
    • Nagakura, T.1    Yasuda, N.2    Yamazaki, K.3
  • 24
    • 0037205175 scopus 로고    scopus 로고
    • Improvement of high fat-diet-induced insulin resistance in dipeptidyl peptidase IV-deficient Fischer rats
    • YASUDA N, NAGAKURA T, YAMAZAKI K, INOUE T, TANAKA I: Improvement of high fat-diet-induced insulin resistance in dipeptidyl peptidase IV-deficient Fischer rats. Life Sci (2002) 71:227-238.
    • (2002) Life Sci. , vol.71 , pp. 227-238
    • Yasuda, N.1    Nagakura, T.2    Yamazaki, K.3    Inoue, T.4    Tanaka, I.5
  • 25
    • 0035905372 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV-like molecules: Homologous proteins or homologous activities?
    • 1550
    • SEDO A, MALIK R: Dipeptidyl peptidase IV-like molecules: homologous proteins or homologous activities? Biochim. Biophys. Acta (2001) 1550:107-116.
    • (2001) Biochim. Biophys. Acta , pp. 107-116
    • Sedo, A.1    Malik, R.2
  • 26
    • 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
    • SCHÖN E, BORN I, DEMUTH HU 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 (1991) 372:305-311.
    • (1991) Biol. Chem. Hoppe Seyler , vol.372 , pp. 305-311
    • Schön, E.1    Born, I.2    Demuth, H.U.3
  • 27
    • 0030965178 scopus 로고    scopus 로고
    • Pyrrolidides: Synthesis and structure-activity relationship as inhibitors of dipeptidyl peptidase IV
    • AUGUSTYNS K, LAMBEIR AM, BORLOO M et al.: Pyrrolidides: synthesis and structure-activity relationship as inhibitors of dipeptidyl peptidase IV. Eur. J. Med. Chem. (1997) 32:301-309.
    • (1997) Eur. J. Med. Chem. , vol.32 , pp. 301-309
    • Augustyns, K.1    Lambeir, A.M.2    Borloo, M.3
  • 28
    • 0029992827 scopus 로고    scopus 로고
    • 2-cyanopyrrolidides as potent, stable inhibitors of dipeptidyl peptidase IV
    • ASHWORTH DM, ATRASH B, BAKER GR et al.: 2-cyanopyrrolidides as potent, stable inhibitors of dipeptidyl peptidase IV. Bioorg. Med. Chem. Lett. (1996) 6:1163-1166.
    • (1996) Bioorg. Med. Chem. Lett. , vol.6 , pp. 1163-1166
    • Ashworth, D.M.1    Atrash, B.2    Baker, G.R.3
  • 29
    • 0028803516 scopus 로고
    • Aminoacylpyrrolidine-2-nitriles: Potent and stable inhibitors of dipeptidyl-peptidase IV (CD 26)
    • LI J, WILK E, WILK S: Aminoacylpyrrolidine-2-nitriles: potent and stable inhibitors of dipeptidyl-peptidase IV (CD 26). Arch. Biochem. Biophys. (1995) 323:148-154.
    • (1995) Arch. Biochem. Biophys. , vol.323 , pp. 148-154
    • Li, J.1    Wilk, E.2    Wilk, S.3
  • 30
    • 0036312876 scopus 로고    scopus 로고
    • Chronic inhibition of circulating dipeptidyl peptidase IV by FE 999011 delays the occurrence of diabetes in male Zucker diabetic fatty rats
    • SUDRE B, BROQUA P, WHITE RB et al.: Chronic inhibition of circulating dipeptidyl peptidase IV by FE 999011 delays the occurrence of diabetes in male Zucker diabetic fatty rats. Diabetes (2002) 51:1461-1469.
    • (2002) Diabetes , vol.51 , pp. 1461-1469
    • Sudre, B.1    Broqua, P.2    White, R.B.3
  • 31
    • 0030593875 scopus 로고    scopus 로고
    • 4-cyanothiazolididies as very potent, stable inhibitors of dipeptidyl peptidase IV
    • ASHWORTH DM, ATRASH B, BAKER GR et al.: 4-cyanothiazolididies as very potent, stable inhibitors of dipeptidyl peptidase IV. Bioorg. Med. Chem. Lett. (1996) 6:2745-2748.
    • (1996) Bioorg. Med. Chem. Lett. , vol.6 , pp. 2745-2748
    • Ashworth, D.M.1    Atrash, B.2    Baker, G.R.3
  • 32
    • 0027305358 scopus 로고
    • Separation of L-Pro-DL-boroPro into its component diastereomers and kinetic analysis of their inhibition of dipeptidyl peptidase IV
    • GUTHEIL WG, BACHOVCHIN WW: Separation of L-Pro-DL-boroPro into its component diastereomers and kinetic analysis of their inhibition of dipeptidyl peptidase IV. Biochemistry (1993) 32:8723-8731.
    • (1993) Biochemistry , vol.32 , pp. 8723-8731
    • Gutheil, W.G.1    Bachovchin, W.W.2
  • 33
    • 0026100446 scopus 로고
    • Inhibition of dipeptidyl aminopeptidase IV (DP-IV) by Xaa-boroPro dipeptides and use of these inhibitors to examine the role of DP-IV in T cell function
    • FLENTKE GR, MUNOZ E, HUBER BT, PLAUT AG, KETTNER CA, BACHOVCHIN WW: Inhibition of dipeptidyl aminopeptidase IV (DP-IV) by Xaa-boroPro dipeptides and use of these inhibitors to examine the role of DP-IV in T cell function. Proc. Natl. Acad. Sci. USA (1991) 88:1556-1559.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1556-1559
    • Flentke, G.R.1    Munoz, E.2    Huber, B.T.3    Plaut, A.G.4    Kettner, C.A.5    Bachovchin, W.W.6
  • 34
    • 0024244544 scopus 로고
    • Reactions between dipeptidyl peptidase IV and diacyl hydroxylamines: Mechanistic investigations
    • DEMUTH HU, NEUMANN U, BARTH A: Reactions between dipeptidyl peptidase IV and diacyl hydroxylamines: mechanistic investigations. J. Enzym. Inhibit. (1989) 2:239-248.
    • (1989) J. Enzym. Inhibit. , vol.2 , pp. 239-248
    • Demuth, H.U.1    Neumann, U.2    Barth, A.3
  • 36
    • 0029953907 scopus 로고    scopus 로고
    • Dipeptide-derived diphenyl phosphonate esters: Mechanism-based inhibitors of dipeptidyl peptidase IV
    • 1290
    • LAMBEIR AM, BORLOO M, DE MEESTER I et al.: Dipeptide-derived diphenyl phosphonate esters: mechanism-based inhibitors of dipeptidyl peptidase IV. Biochim. Biophys. Acta (1996) 1290:76-82.
    • (1996) Biochim. Biophys. Acta , pp. 76-82
    • Lambeir, A.M.1    Borloo, M.2    De Meester, I.3
  • 37
    • 0030612395 scopus 로고    scopus 로고
    • In vivo inhibition of dipeptidyl peptidase IV activity by pro-pro-diphenyl-phosphonate (Prodipine)
    • DE MEESTER I, BELYAEV A, LAMBEIR AM et al.: In vivo inhibition of dipeptidyl peptidase IV activity by pro-pro-diphenyl-phosphonate (Prodipine). Biochem. Pharmacol. (1997) 54:173-179.
    • (1997) Biochem. Pharmacol. , vol.54 , pp. 173-179
    • De Meester, I.1    Belyaev, A.2    Lambeir, A.M.3
  • 39
    • 0037152421 scopus 로고    scopus 로고
    • Development of potent and selective dipeptidyl peptidase II inhibitors
    • SENTEN K, VAN DER VEKEN P, BAL G et al.: Development of potent and selective dipeptidyl peptidase II inhibitors. Bioorg. Med. Chem. Lett. (2002) 12:2825-2828.
    • (2002) Bioorg. Med. Chem. Lett. , vol.12 , pp. 2825-2828
    • Senten, K.1    Van Der Veken, P.2    Bal, G.3
  • 40
    • 0033533402 scopus 로고    scopus 로고
    • NVP-DPP728: (1-[[[2-[(5-cyanopyridin-2-yl) amino]ethyl]amino]acetyl]-2-cyano-(S)-ryrrolidine), a slow-binding inhibitor of dipeptidyl peptidase IV
    • HUGHES TE, MONE MD, RUSSELL ME, WELDON SC, VILLHAUER EB: NVP-DPP728: (1-[[[2-[(5-cyanopyridin-2-yl) amino]ethyl]amino]acetyl]-2-cyano-(S)-ryrrolidine), a slow-binding inhibitor of dipeptidyl peptidase IV. Biochemistry (1999) 38:11597-11603.
    • (1999) Biochemistry , vol.38 , pp. 11597-11603
    • Hughes, T.E.1    Mone, M.D.2    Russell, M.E.3    Weldon, S.C.4    Villhauer, E.B.5
  • 41
    • 0037030602 scopus 로고    scopus 로고
    • 1-[2-[(5-cyanopyridin-2-yl) amino]-ethylamino]acetyl-2-(S)-pyrrolidine-carbonitrile: A potent, selective, and orally bioavailable dipeptidyl peptidase IV inhibitor with antihyperglycemic properties
    • VILLHAUER EB, BRINKMAN JA, NADERI GB et al.: 1-[2-[(5-cyanopyridin-2-yl) amino]-ethylamino]acetyl-2-(S)-pyrrolidine-carbonitrile: a potent, selective, and orally bioavailable dipeptidyl peptidase IV inhibitor with antihyperglycemic properties. J. Med. Chem. (2002) 45:2362-2365.
    • (2002) J. Med. Chem. , vol.45 , pp. 2362-2365
    • Villhauer, E.B.1    Brinkman, J.A.2    Naderi, G.B.3
  • 42
    • 0013261969 scopus 로고    scopus 로고
    • NVP-LAF237, a highly selective and long-acting dipeptidyl peptidase IV inhibitor
    • HUGHES TE, RUSSELL ME, BOLOGNESE L: NVP-LAF237, a highly selective and long-acting dipeptidyl peptidase IV inhibitor. Diabetes (2002) 51(Suppl.2):A67.
    • (2002) Diabetes , vol.51 , Issue.SUPPL. 2
    • Hughes, T.E.1    Russell, M.E.2    Bolognese, L.3
  • 43
    • 0037449356 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl peptidase IV (DPP IV) by 2-(2-amino-1- fluoro-propylidene)-cyclopentanecarbonitrile, a fluoroolefin containing peptidomimetic
    • ZHAO K, LIM DS, FUNAKI T, WELCH JT. Inhibition of dipeptidyl peptidase IV (DPP IV) by 2-(2-amino-1- fluoro-propylidene)-cyclopentanecarbonitrile, a fluoroolefin containing peptidomimetic. Bioorg. Med. Chem. (2003) 11:207-215.
    • (2003) Bioorg. Med. Chem. , vol.11 , pp. 207-215
    • Zhao, K.1    Lim, D.S.2    Funaki, T.3    Welch, J.T.4
  • 44
    • 0032564474 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl peptidase IV by fluoroolefin-containing N-peptidyl-O-hydroxylamine peptidomimetics
    • LIN J, TOSCANO PJ, WELCH JT: Inhibition of dipeptidyl peptidase IV by fluoroolefin-containing N-peptidyl-O-hydroxylamine peptidomimetics. Proc. Natl. Acad. Sci. USA (1998) 95:14020-14024.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14020-14024
    • Lin, J.1    Toscano, P.J.2    Welch, J.T.3
  • 45
    • 0033602521 scopus 로고    scopus 로고
    • Structure-activity relationship of diaryl phosphonate esters as potent irreversible dipeptidyl peptidase IV inhibitors
    • BELYAEV A, ZHANG XM, AUGUSTYNS K et al.: Structure-activity relationship of diaryl phosphonate esters as potent irreversible dipeptidyl peptidase IV inhibitors. J. Med. Chem. (1999) 42:1041-1052.
    • (1999) J. Med. Chem. , vol.42 , pp. 1041-1052
    • Belyaev, A.1    Zhang, X.M.2    Augustyns, K.3
  • 46
    • 15944399603 scopus 로고    scopus 로고
    • BDPX
    • NO AUTHORS LISTED
    • NO AUTHORS LISTED: BDPX. Drug Data Report (2002) 24:620.
    • (2002) Drug Data Report , vol.24 , pp. 620
  • 48
    • 0032771262 scopus 로고    scopus 로고
    • Novel dipeptidyl peptidase IV inhibitors with antiarthritic effects
    • OHNUKI T, YAMADA M, SUGITA T: Novel dipeptidyl peptidase IV inhibitors with antiarthritic effects. Drugs of the Future (1999) 24:665-670.
    • (1999) Drugs of the Future , vol.24 , pp. 665-670
    • Ohnuki, T.1    Yamada, M.2    Sugita, T.3
  • 50
    • 0032969356 scopus 로고    scopus 로고
    • Improved glucose tolerance in rats treated with the dipeptidyl peptidase IV (CD26) inhibitor ile-thiazolidide
    • PAULY RP, DEMUTH HU, ROSCHE F et al.: Improved glucose tolerance in rats treated with the dipeptidyl peptidase IV (CD26) inhibitor ile-thiazolidide. Metabolism (1999) 48:385-389.
    • (1999) Metabolism , vol.48 , pp. 385-389
    • Pauly, R.P.1    Demuth, H.U.2    Rosche, F.3
  • 51
    • 0031870418 scopus 로고    scopus 로고
    • Improved glucose tolerance in Zucker fatty rats by oral administration of the dipeptidyl peptidase IV inhibitor isoleucine thiazolidide
    • PEDERSON RA, WHITE HA, SCHLENZIG D, PAULY RP, MCINTOSH CHS, DEMUTH HU: Improved glucose tolerance in Zucker fatty rats by oral administration of the dipeptidyl peptidase IV inhibitor isoleucine thiazolidide. Diabetes (1998) 47:1253-1258.
    • (1998) Diabetes , vol.47 , pp. 1253-1258
    • Pederson, R.A.1    White, H.A.2    Schlenzig, D.3    Pauly, R.P.4    Mcintosh, C.H.S.5    Demuth, H.U.6
  • 52
    • 0036228243 scopus 로고    scopus 로고
    • Long-term treatment with the dipeptidyl peptidase IV inhibitor P32/98 causes sustained improvements in glucose tolerance, insulin sensitivity, hyperinsulinemia, and β-cell glucose responsiveness in VDF (fa/fa) Zucker rats
    • POSPISILIK JA, STAFFORD SG, DEMUTH HU et al.: Long-term treatment with the dipeptidyl peptidase IV inhibitor P32/98 causes sustained improvements in glucose tolerance, insulin sensitivity, hyperinsulinemia, and β-cell glucose responsiveness in VDF (fa/fa) Zucker rats. Diabetes (2002) 51:943-950.
    • (2002) Diabetes , vol.51 , pp. 943-950
    • Pospisilik, J.A.1    Stafford, S.G.2    Demuth, H.U.3
  • 53
    • 0242432676 scopus 로고    scopus 로고
    • P32/98. Antidiabetic, dipeptidyl-peptidase IV inhibitor
    • SORBERA LA, REVEL L, CASTANER J: P32/98. Antidiabetic, dipeptidyl-peptidase IV inhibitor. Drugs of the Future (2001) 26:859-864.
    • (2001) Drugs of the Future , vol.26 , pp. 859-864
    • Sorbera, L.A.1    Revel, L.2    Castaner, J.3
  • 54
    • 0035403058 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibition reduces the degradation and clearance of GIP and potentiates its insulinotropic and antihyperglycemic effects in anesthetized pigs
    • DEACON CF, DANIELSEN P, KLARSKOV L, OLESEN M, HOLST JJ: Dipeptidyl peptidase IV inhibition reduces the degradation and clearance of GIP and potentiates its insulinotropic and antihyperglycemic effects in anesthetized pigs. Diabetes (2001) 50:1588-1597.
    • (2001) Diabetes , vol.50 , pp. 1588-1597
    • Deacon, C.F.1    Danielsen, P.2    Klarskov, L.3    Olesen, M.4    Holst, J.J.5
  • 55
    • 0034666562 scopus 로고    scopus 로고
    • Improved glucose tolerance and insulin secretion by inhibition of dipeptidyl peptidase IV in mice
    • AHREN B, HOLST JJ, MARTENSSON H, BALKAN B: Improved glucose tolerance and insulin secretion by inhibition of dipeptidyl peptidase IV in mice. Eur. J. Pharmacol. (2000) 404:239-245.
    • (2000) Eur. J. Pharmacol. , vol.404 , pp. 239-245
    • Ahren, B.1    Holst, J.J.2    Martensson, H.3    Balkan, B.4
  • 56
    • 0000135759 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl peptidase IV with NVP-DPP728 increases plasma GLP-1 [7-36 amide] concentrations and improves oral glucose tolerance in obese Zucker rats
    • BALKAN B, KWASNIK L, MISERENDINO R, HOLST JJ, LI X: Inhibition of dipeptidyl peptidase IV with NVP-DPP728 increases plasma GLP-1 [7-36 amide] concentrations and improves oral glucose tolerance in obese Zucker rats. Diabetologia (1999) 42:1324-1331.
    • (1999) Diabetologia , vol.42 , pp. 1324-1331
    • Balkan, B.1    Kwasnik, L.2    Miserendino, R.3    Holst, J.J.4    Li, X.5
  • 57
    • 0036583164 scopus 로고    scopus 로고
    • Inhibition of dipeptidyl peptidase IV improves metabolic control over a 4-week study period in Type 2 diabetes
    • AHREN B, SIMONSSON E, LARSSON H et al.: Inhibition of dipeptidyl peptidase IV improves metabolic control over a 4-week study period in Type 2 diabetes. Diabetes Care (2002) 25:869-875.
    • (2002) Diabetes Care , vol.25 , pp. 869-875
    • Ahren, B.1    Simonsson, E.2    Larsson, H.3
  • 58
    • 0036188070 scopus 로고    scopus 로고
    • Preservation of active incretin hormones by inhibition of dipeptidyl peptidase IV suppresses meal-induced incretin secretion in dogs
    • DEACON CF, WAMBERG S, BIE P, HUGHES TE, HOLST JJ: Preservation of active incretin hormones by inhibition of dipeptidyl peptidase IV suppresses meal-induced incretin secretion in dogs. J. Endocrinol. (2002) 172:355-362.
    • (2002) J. Endocrinol. , vol.172 , pp. 355-362
    • Deacon, C.F.1    Wamberg, S.2    Bie, P.3    Hughes, T.E.4    Holst, J.J.5
  • 59
    • 0036107064 scopus 로고    scopus 로고
    • Long-term inhibition of dipeptidyl peptidase IV improves glucose tolerance and preserves islet function in mice
    • REIMER MK, HOLST JJ, AHREN B: Long-term inhibition of dipeptidyl peptidase IV improves glucose tolerance and preserves islet function in mice. Eur. J. Endocrinol. (2002) 146:717-727.
    • (2002) Eur. J. Endocrinol. , vol.146 , pp. 717-727
    • Reimer, M.K.1    Holst, J.J.2    Ahren, B.3
  • 60
    • 0035985294 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibition improves impaired glucose tolerance in high-fat diet-fed rats: Study using a Fischer 344 rat substrain deficient in its enzyme activity
    • MITANI H, TAKIMOTO M, HUGHES TE, KIMURA M: Dipeptidyl peptidase IV inhibition improves impaired glucose tolerance in high-fat diet-fed rats: study using a Fischer 344 rat substrain deficient in its enzyme activity. Jpn. J. Pharmacol (2002) 88:442-450.
    • (2002) Jpn. J. Pharmacol. , vol.88 , pp. 442-450
    • Mitani, H.1    Takimoto, M.2    Hughes, T.E.3    Kimura, M.4
  • 61
    • 0035985285 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitor NVP-DPP728 ameliorates early insulin response and glucose tolerance in aged rats but not in aged Fischer 344 rats lacking its enzyme activity
    • MITANI H, TAKIMOTO M, KIMURA M: Dipeptidyl peptidase IV inhibitor NVP-DPP728 ameliorates early insulin response and glucose tolerance in aged rats but not in aged Fischer 344 rats lacking its enzyme activity. Jpn. J. Pharmacol. (2002) 88:451-458.
    • (2002) Jpn. J. Pharmacol. , vol.88 , pp. 451-458
    • Mitani, H.1    Takimoto, M.2    Kimura, M.3
  • 62
    • 0037219684 scopus 로고    scopus 로고
    • Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog
    • RASMUSSEN HB, BRANNER S, WIBERG FC, WAGTMANN N: Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog. Nat. Struct. Biol. (2003) 10:19-25.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 19-25
    • Rasmussen, H.B.1    Branner, S.2    Wiberg, F.C.3    Wagtmann, N.4


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