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Volumn 2, Issue 6, 1996, Pages 632-633

Serine protease inhibitors (serpins): Where mechanism meets medicine

Author keywords

[No Author keywords available]

Indexed keywords

SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR;

EID: 0029941477     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/nm0696-632     Document Type: Note
Times cited : (53)

References (14)
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  • 2
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    • Bleomycin-induced pulmonary fibrosis in transgenic mice that either lack or overexpress the murine plasminogen activator inhibitor-1 gene
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  • 3
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    • Impaired wound healing in mice with a disrupted plasminogen gene
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    • Romer, J.1
  • 4
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    • Impaired immune and acute phase responses in interleukin-6-deficient mice
    • Kopf, M. et al. Impaired immune and acute phase responses in interleukin-6-deficient mice. Nature 369, 339-342 (1994)
    • (1994) Nature , vol.369 , pp. 339-342
    • Kopf, M.1
  • 5
    • 13344268993 scopus 로고    scopus 로고
    • Fas ligand in human serum
    • Tanaka, M. et al. Fas ligand in human serum. Nature Med. 2, 317-322 (1996).
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    • Tanaka, M.1
  • 6
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    • Sequential activation of ICE-like and CPP32-like proteases during Fas-mediated apoptosis
    • Enari, M., Talanian, R.V., Wong, W.W. & Nagata, S. Sequential activation of ICE-like and CPP32-like proteases during Fas-mediated apoptosis. Nature 380, 723-726 (1996).
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    • Enari, M.1    Talanian, R.V.2    Wong, W.W.3    Nagata, S.4
  • 7
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    • Role of multiple cellular proteases in the execution of programmed cell death
    • Kumar, S. & Harvey, N.L. Role of multiple cellular proteases in the execution of programmed cell death. FEBS Lett. 375, 169-173 (1995)
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    • Kumar, S.1    Harvey, N.L.2
  • 8
    • 0027535914 scopus 로고
    • Biology and biochemistry of proteinases in tumor invasion
    • Mignatti, P. & Rifkin, D.B. Biology and biochemistry of proteinases in tumor invasion. Physiol. Rev. 73, 161-195 (1993)
    • (1993) Physiol. Rev. , vol.73 , pp. 161-195
    • Mignatti, P.1    Rifkin, D.B.2
  • 9
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    • Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop
    • Wei, A., Rubin, H., Cooperman, B.S. & Christianson, D.W. Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop. Nature Struct. Biol. 1, 251-258 (1994).
    • (1994) Nature Struct. Biol. , vol.1 , pp. 251-258
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  • 10
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    • The intact and cleaved human antithrombin III complex as a model for serpin-protease interactions
    • Schreuder, H.A. et al. The intact and cleaved human antithrombin III complex as a model for serpin-protease interactions. Nature Struct. Biol. 1, 48-54 (1994).
    • (1994) Nature Struct. Biol. , vol.1 , pp. 48-54
    • Schreuder, H.A.1
  • 11
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    • Biological implications of a 3A structure of dimeric antithrombin
    • Carrell, R.W., Stein, P.E., Fermi, G. & Wardell, M.R. Biological implications of a 3A structure of dimeric antithrombin. Nature Struct. Biol. 2, 257-270 (1994).
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    • Carrell, R.W.1    Stein, P.E.2    Fermi, G.3    Wardell, M.R.4
  • 12
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    • Serpin-protease complexes are trapped as stable acyl-enzyme intermediates
    • Lawrence, D.A. et al. Serpin-protease complexes are trapped as stable acyl-enzyme intermediates. J. Biol. Chem. 270, 25309-25312 (1995).
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  • 13
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    • The inhibition mechanism of serpins: Evidence that the mobile reactive center loop is cleaved in the native protease-inhibitor complex
    • Wilczynska, M., Fa, M., Ohlsson, P-I. & Ny, T. The inhibition mechanism of serpins: evidence that the mobile reactive center loop is cleaved in the native protease-inhibitor complex. J. Biol. Chem. 270, 29652-29655 (1995).
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    • Wilczynska, M.1    Fa, M.2    Ohlsson, P.-I.3    Ny, T.4
  • 14
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    • Distortion of the active site of chymotrypsin complexed with a serpin
    • in the press
    • Plotnick, M.I., Mayne, L., Schechter, N.M. & Rubin, H. Distortion of the active site of chymotrypsin complexed with a serpin. Biochemistry (in the press).
    • Biochemistry
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.