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Volumn 31, Issue SUPPL. 1, 1998, Pages

Characterization of CGS 31447, a potent and nonpeptidic endothelin-converting enzyme inhibitor

Author keywords

Big endothelin 1; CGS 31447; Endothelin 1; Endothelin converting enzyme; Perfused kidney

Indexed keywords

ASPARTIC PROTEINASE; CGS 31447; ENDOTHELIN; ENDOTHELIN 1; ENDOTHELIN CONVERTING ENZYME; ENDOTHELIN-CONVERTING ENZYME 1; METALLOPROTEINASE; PHOSPHONIC ACID DERIVATIVE; PROTEIN PRECURSOR; PROTEINASE INHIBITOR; RECOMBINANT PROTEIN; TETRAZOLE DERIVATIVE;

EID: 0031639677     PISSN: 01602446     EISSN: None     Source Type: Journal    
DOI: 10.1097/00005344-199800001-00022     Document Type: Article
Times cited : (10)

References (10)
  • 1
    • 0030454012 scopus 로고    scopus 로고
    • Molecular pharmacology and pathophysiological significance of endothelin
    • Goto K, Hama H, Kasuya Y. Molecular pharmacology and pathophysiological significance of endothelin. Jpn J Pharmacol 1996; 72:261-90.
    • (1996) Jpn J Pharmacol , vol.72 , pp. 261-290
    • Goto, K.1    Hama, H.2    Kasuya, Y.3
  • 2
    • 0027992642 scopus 로고
    • ECE-1: A membrane-bound metalloprotease that catalyzes the proteolytic activation of big endothelin-1
    • Xu D, Emoto N, Giaid A, et al. ECE-1: a membrane-bound metalloprotease that catalyzes the proteolytic activation of big endothelin-1. Cell 1994;78:473-85.
    • (1994) Cell , vol.78 , pp. 473-485
    • Xu, D.1    Emoto, N.2    Giaid, A.3
  • 3
    • 0029017876 scopus 로고
    • Endothelin-converting enzyme is a membrane-bound, phosphoramidon sensitive metalloprotease with acidic pH optimum
    • Emoto N, Yanagisawa M. Endothelin-converting enzyme is a membrane-bound, phosphoramidon sensitive metalloprotease with acidic pH optimum. J Biol Chem 1995;270:15262-8.
    • (1995) J Biol Chem , vol.270 , pp. 15262-15268
    • Emoto, N.1    Yanagisawa, M.2
  • 4
    • 0030934793 scopus 로고    scopus 로고
    • Potent non-peptidic dual inhibitors of endothelin-converting enzyme and neutral endopeptidase 24.11
    • De Lombaert S, Stamford LB, Blanchard L, et al. Potent non-peptidic dual inhibitors of endothelin-converting enzyme and neutral endopeptidase 24.11. Bioorg Med Chem Lett 1997;7:1059-64.
    • (1997) Bioorg Med Chem Lett , vol.7 , pp. 1059-1064
    • De Lombaert, S.1    Stamford, L.B.2    Blanchard, L.3
  • 5
    • 0027787555 scopus 로고
    • Effects of metalloprotease inhibitors on the conversion of proendothelin-1 to endothelm-1
    • Trapani AJ, Balwierczak JL, Lappe RW, et al. Effects of metalloprotease inhibitors on the conversion of proendothelin-1 to endothelm-1. Biochem Mol Biol Int 1993;31:861-7.
    • (1993) Biochem Mol Biol Int , vol.31 , pp. 861-867
    • Trapani, A.J.1    Balwierczak, J.L.2    Lappe, R.W.3
  • 7
    • 0025011716 scopus 로고
    • Characterization of three inhibitors of endothelial nitric oxide synthase in vitro and in vivo
    • Rees DD, Palmer RMJ, Schulz R, Hodson HF, Moncada S. Characterization of three inhibitors of endothelial nitric oxide synthase in vitro and in vivo. Br J Pharmacol 1990;101:746-52.
    • (1990) Br J Pharmacol , vol.101 , pp. 746-752
    • Rees, D.D.1    Palmer, R.M.J.2    Schulz, R.3    Hodson, H.F.4    Moncada, S.5
  • 8
    • 0024581086 scopus 로고
    • Endothelin-1 and endothelin-3 release EDRF from isolated perfused arterial vessels of rat and rabbit
    • Warner TD, Mitchell JA, DeNucci G, Vane JR. Endothelin-1 and endothelin-3 release EDRF from isolated perfused arterial vessels of rat and rabbit. J Cardiovasc Pharmacol 1989;13(suppl 5):S85-8.
    • (1989) J Cardiovasc Pharmacol , vol.13 , Issue.5 SUPPL.
    • Warner, T.D.1    Mitchell, J.A.2    DeNucci, G.3    Vane, J.R.4
  • 9
    • 0027771483 scopus 로고
    • Phosphoramidon inhibits the conversion of big ET-1 into ET-1 in the pithed rat and in isolated perfused rat kidneys
    • Verbeuren TJ, Mennecier P, Merceron D, et al. Phosphoramidon inhibits the conversion of big ET-1 into ET-1 in the pithed rat and in isolated perfused rat kidneys. J Cardiovasc Pharmacol 1993;22 (suppl 8):S81-4.
    • (1993) J Cardiovasc Pharmacol , vol.22 , Issue.8 SUPPL.
    • Verbeuren, T.J.1    Mennecier, P.2    Merceron, D.3
  • 10
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter I, Berger A. On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun 1967;27:157-62.
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.