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Volumn 53, Issue 18, 2010, Pages 6572-6583

Substituted 4-carboxymethylpyroglutamic acid diamides as potent and selective inhibitors of fibroblast activation protein

Author keywords

[No Author keywords available]

Indexed keywords

1 [4 [2 (5 CHLORO 1,3 DIHYDROISOINDOL 2 YL) 2 OXOETHYL] 5 OXOPYRROLIDINE 2 CARBONYL] 4 FLUOROPYRROLIDINE 2 CARBONITRILE; 1 [[4 [2 (1,3 DIHYDRO 2H ISOINDOL 2 YL) 2 OXOETHYL] 5 OXOPYRROLIDIN 2 YL]CARBONYL] 4 FLUOROPYRROLIDINE 2 CARBONITRILE; 1 [[4 [2 (1,3 DIHYDRO 2H ISOINDOL 2 YL) 2 OXOETHYL] 5 OXOPYRROLIDIN 2 YL]CARBONYL] 4,4 DIFLUOROPYRROLIDINE 2 CARBONITRILE; 4 CARBOXYMETHYLPYROGLUTAMIC ACID DIAMIDE DERIVATIVE; CYSTEINE PROTEINASE; DIPEPTIDYL PEPTIDASE; DIPEPTIDYL PEPTIDASE II; DIPEPTIDYL PEPTIDASE IV; DIPEPTIDYL PEPTIDASE IX; DIPEPTIDYL PEPTIDASE VIII; FIBROBLAST ACTIVATION PROTEIN INHIBITOR; PEPTIDE HYDROLASE INHIBITOR; PROLINE IMINOPEPTIDASE; UNCLASSIFIED DRUG; AMIDE; DIPEPTIDASE; DIPEPTIDYL PEPTIDASE IV INHIBITOR; DPP8 PROTEIN, HUMAN; DPP9 PROTEIN, HUMAN; GELATINASE; MEMBRANE PROTEIN; PYROGLUTAMIC ACID; SEPRASE; SERINE PROTEINASE;

EID: 77956717491     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm1002556     Document Type: Article
Times cited : (62)

References (43)
  • 1
    • 0036178438 scopus 로고    scopus 로고
    • The prolyl oligopeptidase family
    • Polgar, L. The prolyl oligopeptidase family Cell. Mol. Life Sci. 2002, 59, 349-362
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 349-362
    • Polgar, L.1
  • 2
    • 0043073112 scopus 로고    scopus 로고
    • Prolyl peptidases: A serine protease subfamily with high potential for drug discovery
    • Rosenblum, J. S.; Kozarich, J. W. Prolyl peptidases: a serine protease subfamily with high potential for drug discovery Curr. Opin. Chem. Biol. 2003, 7, 496-504
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 496-504
    • Rosenblum, J.S.1    Kozarich, J.W.2
  • 3
    • 0025083528 scopus 로고
    • Cell surface glycoprotein of reactive stromal fibroblasts as a potential antibody target in human epithelial cancers
    • Garin-Chesa, P.; Old, L. J.; Rettig, W. J. Cell surface glycoprotein of reactive stromal fibroblasts as a potential antibody target in human epithelial cancers Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 7235-7239
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 7235-7239
    • Garin-Chesa, P.1    Old, L.J.2    Rettig, W.J.3
  • 4
    • 0005429990 scopus 로고
    • Cell-surface glycoproteins of human sarcomas: Differential expression in normal and malignant tissues and cultured cells
    • Rettig, W. J.; Garin-Chesa, P.; Beresford, H. R.; Oettgen, H. F.; Melamed, M. R.; Old, L. J. Cell-surface glycoproteins of human sarcomas: differential expression in normal and malignant tissues and cultured cells Proc. Natl. Acad. Sci. U.S.A. 1988, 85, 3110-3114
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 3110-3114
    • Rettig, W.J.1    Garin-Chesa, P.2    Beresford, H.R.3    Oettgen, H.F.4    Melamed, M.R.5    Old, L.J.6
  • 6
    • 0037102412 scopus 로고    scopus 로고
    • Promotion of tumor growth by murine fibroblast activation protein, a serine protease, in an animal model
    • Cheng, J. D.; Dunbrack, R. L.; Valianou, M.; Rogarto, A.; Aplaugh, R. K.; Weiner, L. M. Promotion of tumor growth by murine fibroblast activation protein, a serine protease, in an animal model Cancer Res. 2002, 62, 4767-4772
    • (2002) Cancer Res. , vol.62 , pp. 4767-4772
    • Cheng, J.D.1    Dunbrack, R.L.2    Valianou, M.3    Rogarto, A.4    Aplaugh, R.K.5    Weiner, L.M.6
  • 8
    • 33344475312 scopus 로고    scopus 로고
    • Peptide substrate profiling defines fibroblast activation protein as an endopeptidase of strict Gly(2)-Pro(1)-cleaving specificity
    • Edosada, C. Y.; Quan, C.; Tran, T.; Pham, V.; Wiesmann, C.; Fairbrother, W.; Wolf, B. B. Peptide substrate profiling defines fibroblast activation protein as an endopeptidase of strict Gly(2)-Pro(1)-cleaving specificity FEBS Lett. 2006, 580, 1581-1586
    • (2006) FEBS Lett. , vol.580 , pp. 1581-1586
    • Edosada, C.Y.1    Quan, C.2    Tran, T.3    Pham, V.4    Wiesmann, C.5    Fairbrother, W.6    Wolf, B.B.7
  • 9
    • 0037777695 scopus 로고    scopus 로고
    • 1-[[(3-Hydroxy-1-adamantyl)amino]acetyl]-2-cyano-(S)-pyrrolidine: A potent, selective, and orally bioavailable dipeptidyl peptidase IV inhibitor with antihyperglycemic properties
    • Villhauer, E. B.; Brinkman, J. A.; Naderi, G. B.; Burkey, B. F.; Dunning, B. E.; Prasad, K.; Mangold, B. L.; Russell., M. E.; Hughes, T. E. 1-[[(3-Hydroxy-1-adamantyl)amino]acetyl]-2-cyano-(S)-pyrrolidine: a potent, selective, and orally bioavailable dipeptidyl peptidase IV inhibitor with antihyperglycemic properties J. Med. Chem. 2003, 46, 2774-2789
    • (2003) J. Med. Chem. , vol.46 , pp. 2774-2789
    • Villhauer, E.B.1    Brinkman, J.A.2    Naderi, G.B.3    Burkey, B.F.4    Dunning, B.E.5    Prasad, K.6    Mangold, B.L.7    Russell, M.E.8    Hughes, T.E.9
  • 11
    • 61349143225 scopus 로고    scopus 로고
    • Medicinal chemistry approaches to the inhibition of dipeptidyl peptidase-4 for the treatment of type 2 diabetes
    • Shrikanth, H. H.; Manojit, P. Medicinal chemistry approaches to the inhibition of dipeptidyl peptidase-4 for the treatment of type 2 diabetes Bioorg. Med. Chem. 2009, 17, 1783-1802
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 1783-1802
    • Shrikanth, H.H.1    Manojit, P.2
  • 13
    • 2442719012 scopus 로고    scopus 로고
    • Gamma-amino-substituted analogues of 1-[(S)-2,4-diaminobutanoyl] piperidine as highly potent and selective dipeptidyl peptidase II inhibitors
    • Senten, K.; Van der Veken, P.; De Meester, I.; Lambeir, A. M.; Scharpé, S.; Haemers, A.; Augustyns, K. Gamma-amino-substituted analogues of 1-[(S)-2,4-diaminobutanoyl]piperidine as highly potent and selective dipeptidyl peptidase II inhibitors J. Med. Chem. 2004, 47, 2906-2916
    • (2004) J. Med. Chem. , vol.47 , pp. 2906-2916
    • Senten, K.1    Van Der Veken, P.2    De Meester, I.3    Lambeir, A.M.4    Scharpé, S.5    Haemers, A.6    Augustyns, K.7
  • 16
    • 33846904812 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationship of N-acyl-Gly-, N-acyl-Sar-and N-blocked-boroPro inhibitors of FAP, DPP4, and POP
    • Tran, T.; Quan, C.; Edosada, C. Y.; Mayeda, M.; Wiesmann, C.; Sutherlin, D.; Wolf, B. B. Synthesis and structure-activity relationship of N-acyl-Gly-, N-acyl-Sar-and N-blocked-boroPro inhibitors of FAP, DPP4, and POP Bioorg. Med. Chem. Lett. 2007, 17, 1438-1442
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , pp. 1438-1442
    • Tran, T.1    Quan, C.2    Edosada, C.Y.3    Mayeda, M.4    Wiesmann, C.5    Sutherlin, D.6    Wolf, B.B.7
  • 17
    • 0029991059 scopus 로고    scopus 로고
    • Probing the specificity of the serine proteases subtilisin Carlsberg and α-chymotrypsin with enantiomeric 1-acetamido boronic acids. An unexpected reversal of the normal "l"-stereoselectivity preference
    • Martichonok, V.; Jones, J. B. Probing the specificity of the serine proteases subtilisin Carlsberg and α-chymotrypsin with enantiomeric 1-acetamido boronic acids. An unexpected reversal of the normal "L"-stereoselectivity preference J. Am. Chem. Soc. 1996, 118, 950-958
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 950-958
    • Martichonok, V.1    Jones, J.B.2
  • 19
    • 0036158954 scopus 로고    scopus 로고
    • Biological actions and therapeutic potential of the glucagon-like peptides
    • Drucker, D. J. Biological actions and therapeutic potential of the glucagon-like peptides Gastroenterology 2002, 122, 531-544
    • (2002) Gastroenterology , vol.122 , pp. 531-544
    • Drucker, D.J.1
  • 21
    • 0033028297 scopus 로고    scopus 로고
    • Is GLP-1 an incretin hormone?
    • Nauck, M. A. Is GLP-1 an incretin hormone? Diabetologia 1999, 42, 373-379
    • (1999) Diabetologia , vol.42 , pp. 373-379
    • Nauck, M.A.1
  • 22
    • 0036965113 scopus 로고    scopus 로고
    • The insulinotropic effect of acute exendin-4-administered to humans: Comparison of nondiabetic state to type 2 diabetes
    • Egan, J.; Clocquet, A. R.; Elahi, D. The insulinotropic effect of acute exendin-4-administered to humans: comparison of nondiabetic state to type 2 diabetes J. Clin. Endocrinol. Metab. 2002, 87, 1282-1290
    • (2002) J. Clin. Endocrinol. Metab. , vol.87 , pp. 1282-1290
    • Egan, J.1    Clocquet, A.R.2    Elahi, D.3
  • 23
    • 0026596851 scopus 로고
    • Antidiabetogenic effect of glucagon-like peptide-1 (7-36) amide in normal subjects and patients with diabetes mellitus
    • Gutniak, M.; Orskov, C.; Holst, J. J.; Ahren, B.; Efendic, S. Antidiabetogenic effect of glucagon-like peptide-1 (7-36) amide in normal subjects and patients with diabetes mellitus N. Engl. J. Med. 1992, 326, 1316-1322
    • (1992) N. Engl. J. Med. , vol.326 , pp. 1316-1322
    • Gutniak, M.1    Orskov, C.2    Holst, J.J.3    Ahren, B.4    Efendic, S.5
  • 24
    • 0028071448 scopus 로고
    • Subcutaneous injection of the incretin hormone glucagons-like peptide 1 abolishes postprandial glycemia in NIDDM
    • Gutniak, M. K.; Linde, B.; Holst, J. J.; Efendic, S. Subcutaneous injection of the incretin hormone glucagons-like peptide 1 abolishes postprandial glycemia in NIDDM Diabetes Care 1994, 17, 1039-1044
    • (1994) Diabetes Care , vol.17 , pp. 1039-1044
    • Gutniak, M.K.1    Linde, B.2    Holst, J.J.3    Efendic, S.4
  • 25
    • 0024604473 scopus 로고
    • Lysosomal heterogenity of dipeptidyl peptidase II active on collagen-related peptides
    • Andersen, K. J.; McDonald, J. K. Lysosomal heterogenity of dipeptidyl peptidase II active on collagen-related peptides Renal Physiol. Biochem. 1989, 12, 32-40
    • (1989) Renal Physiol. Biochem. , vol.12 , pp. 32-40
    • Andersen, K.J.1    McDonald, J.K.2
  • 26
    • 0024592793 scopus 로고
    • Purification of two dipeptidyl peptidases II from rat brain and their action on proline-containing neuropeptides
    • Mentlein, R.; Struckhoff, G. Purification of two dipeptidyl peptidases II from rat brain and their action on proline-containing neuropeptides J. Neurochem. 1989, 52, 1284-1293
    • (1989) J. Neurochem. , vol.52 , pp. 1284-1293
    • Mentlein, R.1    Struckhoff, G.2
  • 27
    • 0033780088 scopus 로고    scopus 로고
    • Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8
    • Abbott, C. A.; Yu, D. M.; Woollatt, E.; Sutherland, G. R.; McCaughan, G. W.; Gorrell, M. D. Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8 Eur. J. Biochem. 2000, 267, 6140-6150
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6140-6150
    • Abbott, C.A.1    Yu, D.M.2    Woollatt, E.3    Sutherland, G.R.4    McCaughan, G.W.5    Gorrell, M.D.6
  • 34
    • 4744338689 scopus 로고    scopus 로고
    • Hetero-Diels-Alder and pyroglutamate approaches to (2 S,4 R)-2-methylamino-5-hydroxy-4-methylpentanoic acid
    • Tarver, J. E., Jr.; Terranova, K. M.; Joullie, M. M. Hetero-Diels-Alder and pyroglutamate approaches to (2 S,4 R)-2-methylamino-5-hydroxy-4- methylpentanoic acid Tetrahedron 2004, 60, 10277-10284
    • (2004) Tetrahedron , vol.60 , pp. 10277-10284
    • Tarver Jr., J.E.1    Terranova, K.M.2    Joullie, M.M.3
  • 40
    • 33745045683 scopus 로고    scopus 로고
    • Identification of hydrophobic residues critical for DPP-IV dimerization
    • Chien, C. H.; Tsai, C. H.; Lin, C. H.; Chou, C. Y.; Chen, X. Identification of hydrophobic residues critical for DPP-IV dimerization Biochemistry 2006, 45, 7006-7012
    • (2006) Biochemistry , vol.45 , pp. 7006-7012
    • Chien, C.H.1    Tsai, C.H.2    Lin, C.H.3    Chou, C.Y.4    Chen, X.5
  • 41
    • 33845984033 scopus 로고    scopus 로고
    • Investigation of the dimer interface and substrate specificity of prolyl dipeptidase DPP8
    • Lee, H. J.; Chen, Y. S.; Chou, C. Y.; Chien, C. H.; Lin, C. H.; Chang, G. G.; Chen, X. Investigation of the dimer interface and substrate specificity of prolyl dipeptidase DPP8 J. Biol. Chem. 2006, 281, 38653-38662
    • (2006) J. Biol. Chem. , vol.281 , pp. 38653-38662
    • Lee, H.J.1    Chen, Y.S.2    Chou, C.Y.3    Chien, C.H.4    Lin, C.H.5    Chang, G.G.6    Chen, X.7


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