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Volumn 36, Issue 5, 1998, Pages 719-728

Enkephalin-processing oligopeptidases in cobra venom: Inhibition by thiorphan and bestatin reveals co-operative actions

Author keywords

[No Author keywords available]

Indexed keywords

BESTATIN; PEPTIDASE; SNAKE VENOM; THIORPHAN;

EID: 0031813780     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0041-0101(97)00134-7     Document Type: Article
Times cited : (8)

References (11)
  • 1
    • 0030844625 scopus 로고    scopus 로고
    • The action of Taiwan cobra venom on enkephalin: A useful assay for oligopeptidase content
    • Anderson, L. and Dufton, M. J. (1997) The action of Taiwan cobra venom on enkephalin: A useful assay for oligopeptidase content. Toxicon 35, 1113-1123.
    • (1997) Toxicon , vol.35 , pp. 1113-1123
    • Anderson, L.1    Dufton, M.J.2
  • 2
    • 0344345946 scopus 로고    scopus 로고
    • Oligopeptidases
    • ed. G. S. Bailey. Alaken Inc., in press
    • Anderson, L. and Dufton, M. J. (1998) Oligopeptidases. In Snake Venom Enzymes, ed. G. S. Bailey. Alaken Inc., in press.
    • (1998) Snake Venom Enzymes
    • Anderson, L.1    Dufton, M.J.2
  • 4
    • 0027517889 scopus 로고
    • Characteristics of the peptidase activity contained in Taiwan cobra (Naja naja atra) venom
    • Boumrah, D., Suckling, C. J. and Dufton, M. J. (1993) Characteristics of the peptidase activity contained in Taiwan cobra (Naja naja atra) venom. Toxicon 31, 1293-1303.
    • (1993) Toxicon , vol.31 , pp. 1293-1303
    • Boumrah, D.1    Suckling, C.J.2    Dufton, M.J.3
  • 6
    • 0027199490 scopus 로고
    • Endopeptidase 24.11: Putative substrates and possible roles
    • Kenny, J. (1993) Endopeptidase 24.11: Putative substrates and possible roles. Biochemical Society Transactions 21, 663-668.
    • (1993) Biochemical Society Transactions , vol.21 , pp. 663-668
    • Kenny, J.1
  • 7
    • 0022631293 scopus 로고
    • Cell surface peptidases are neither peptide- Nor organ-specific
    • Kenny, J. (1986) Cell surface peptidases are neither peptide- nor organ-specific. Trends in Biochemical Science 11, 40-42.
    • (1986) Trends in Biochemical Science , vol.11 , pp. 40-42
    • Kenny, J.1
  • 8
    • 0021277915 scopus 로고
    • Inhibition of aminopeptidases by amastatin and bestatin derivatives. Effect of inhibitor structure on slow-binding processes
    • Rich, D. H., Monn, B. J. and Harbeson, S. (1984) Inhibition of aminopeptidases by amastatin and bestatin derivatives. Effect of inhibitor structure on slow-binding processes. Journal of Medicinal Chemistry 27, 417-422.
    • (1984) Journal of Medicinal Chemistry , vol.27 , pp. 417-422
    • Rich, D.H.1    Monn, B.J.2    Harbeson, S.3
  • 10
    • 0013473918 scopus 로고
    • Peptidase inactivation of enkephalins; Design of inhibitors and biochemical, pharmacological and clinical applications
    • ed. A. Herz, Springer-Verlag, Berlin
    • Roques, B. P., Beaumont, A., Dauge, V. and Fournie'-Zaluski, M. C. (1993) Peptidase inactivation of enkephalins; Design of inhibitors and biochemical, pharmacological and clinical applications. In Opioids I, Handbook of Experimental Pharmacology, Vol 104/I, ed. A. Herz, pp. 547-584. Springer-Verlag, Berlin.
    • (1993) Opioids I, Handbook of Experimental Pharmacology , vol.104 , Issue.1 , pp. 547-584
    • Roques, B.P.1    Beaumont, A.2    Dauge, V.3    Fournie'-Zaluski, M.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.