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. 1994 Dec;94(6):2174–2175. doi: 10.1172/JCI117576

Studies of serpins unfold at a feverish pace.

E L Madison
PMCID: PMC330040  PMID: 7989570

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bone R., Silen J. L., Agard D. A. Structural plasticity broadens the specificity of an engineered protease. Nature. 1989 May 18;339(6221):191–195. doi: 10.1038/339191a0. [DOI] [PubMed] [Google Scholar]
  2. Bruce D., Perry D. J., Borg J. Y., Carrell R. W., Wardell M. R. Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen-VI (187 Asn-->Asp) J Clin Invest. 1994 Dec;94(6):2265–2274. doi: 10.1172/JCI117589. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Carrell R. W., Stein P. E., Fermi G., Wardell M. R. Biological implications of a 3 A structure of dimeric antithrombin. Structure. 1994 Apr 15;2(4):257–270. doi: 10.1016/s0969-2126(00)00028-9. [DOI] [PubMed] [Google Scholar]
  4. Hedstrom L., Perona J. J., Rutter W. J. Converting trypsin to chymotrypsin: residue 172 is a substrate specificity determinant. Biochemistry. 1994 Jul 26;33(29):8757–8763. doi: 10.1021/bi00195a017. [DOI] [PubMed] [Google Scholar]
  5. Keyt B. A., Paoni N. F., Refino C. J., Berleau L., Nguyen H., Chow A., Lai J., Peña L., Pater C., Ogez J. A faster-acting and more potent form of tissue plasminogen activator. Proc Natl Acad Sci U S A. 1994 Apr 26;91(9):3670–3674. doi: 10.1073/pnas.91.9.3670. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Loebermann H., Tokuoka R., Deisenhofer J., Huber R. Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. J Mol Biol. 1984 Aug 15;177(3):531–557. [PubMed] [Google Scholar]
  7. Madison E. L., Goldsmith E. J., Gerard R. D., Gething M. J., Sambrook J. F. Serpin-resistant mutants of human tissue-type plasminogen activator. Nature. 1989 Jun 29;339(6227):721–724. doi: 10.1038/339721a0. [DOI] [PubMed] [Google Scholar]
  8. Madison E. L., Kobe A., Gething M. J., Sambrook J. F., Goldsmith E. J. Converting tissue plasminogen activator to a zymogen: a regulatory triad of Asp-His-Ser. Science. 1993 Oct 15;262(5132):419–421. doi: 10.1126/science.8211162. [DOI] [PubMed] [Google Scholar]
  9. Matthews D. J., Wells J. A. Substrate phage: selection of protease substrates by monovalent phage display. Science. 1993 May 21;260(5111):1113–1117. doi: 10.1126/science.8493554. [DOI] [PubMed] [Google Scholar]
  10. Mottonen J., Strand A., Symersky J., Sweet R. M., Danley D. E., Geoghegan K. F., Gerard R. D., Goldsmith E. J. Structural basis of latency in plasminogen activator inhibitor-1. Nature. 1992 Jan 16;355(6357):270–273. doi: 10.1038/355270a0. [DOI] [PubMed] [Google Scholar]
  11. Schellenberger V., Turck C. W., Rutter W. J. Role of the S' subsites in serine protease catalysis. Active-site mapping of rat chymotrypsin, rat trypsin, alpha-lytic protease, and cercarial protease from Schistosoma mansoni. Biochemistry. 1994 Apr 12;33(14):4251–4257. doi: 10.1021/bi00180a020. [DOI] [PubMed] [Google Scholar]
  12. Schreuder H. A., de Boer B., Dijkema R., Mulders J., Theunissen H. J., Grootenhuis P. D., Hol W. G. The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions. Nat Struct Biol. 1994 Jan;1(1):48–54. doi: 10.1038/nsb0194-48. [DOI] [PubMed] [Google Scholar]
  13. Wei A., Rubin H., Cooperman B. S., Christianson D. W. Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop. Nat Struct Biol. 1994 Apr;1(4):251–258. doi: 10.1038/nsb0494-251. [DOI] [PubMed] [Google Scholar]

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