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Serine protease inhibitors (SERPINS): Where mechanism meets medicine

Recent research expands our understanding of the biology of an important class of enzyme inhibitors.

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References

  1. Travis, J. & Salvesen, G.S. Human plasma proteinase inhibitors. Ann. Rev. Biochem. 52, 655–709 (1983).

    Article  CAS  Google Scholar 

  2. Eitzman, D.T. et al. Bleomycin-induced pulmonary fibrosis in transgenic mice that either lack or overexpress the murine plasminogen activator inhibitor-1 gene. J. Clin. Invest. 97, 232–237 (1996).

    Article  CAS  Google Scholar 

  3. Romer, J. et al. Impaired wound healing in mice with a disrupted plasminogen gene. Nature Med. 2, 287–292 (1996).

    Article  CAS  Google Scholar 

  4. Kopf, M. et al. Impaired immune and acute phase responses in interleukin-6-deficient mice. Nature 369, 339–342 (1994)

    Article  Google Scholar 

  5. Tanaka, M. et al. Fas ligand in human serum. Nature Med. 2, 317–322 (1996).

    Article  CAS  Google Scholar 

  6. 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).

    Article  CAS  Google Scholar 

  7. Kumar, S. & Harvey, N.L. Role of multiple cellular proteases in the execution of programmed cell death. FEBS Lett. 375, 169–173 (1995)

    Article  CAS  Google Scholar 

  8. Mignatti, P. & Rifkin, D.B. Biology and biochemistry of proteinases in tumor invasion. Physiol. Rev. 73, 161–195 (1993)

    Article  CAS  Google Scholar 

  9. 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).

    Article  CAS  Google Scholar 

  10. 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).

    Article  CAS  Google Scholar 

  11. 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).

    CAS  Google Scholar 

  12. Lawrence, D.A. et al. Serpin-protease complexes are trapped as stable acyl-enzyme intermediates. J. Biol. Chem. 270, 25309–25312 (1995).

    Article  CAS  Google Scholar 

  13. 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).

    Article  CAS  Google Scholar 

  14. 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).

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Rubin, H. Serine protease inhibitors (SERPINS): Where mechanism meets medicine. Nat Med 2, 632–633 (1996). https://doi.org/10.1038/nm0696-632

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