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Interaction of Mutant Forms of the HIV-1 Protease with Substrate and Inhibitors

  • Paul L. Darke
  • Nancy E. Kohl
  • Michelle G. Hanobik
  • Chih-Tai Leu
  • Joseph P. Vacca
  • James P. Guare
  • Jill C. Heimbach
  • Richard A. F. Dixon
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 306)

Abstract

The protease of HIV-1 is considered to be a prime target for the treatment of AIDS with small molecular weight inhibitors. 1,2,3 Many groups have now demonstrated that compounds designed as potent inhibitors of the enzyme in vitro are effective inhibitors of viral polyprotein processing and viral spread in cultured cells.4–7 Continued effort to discover new potent inhibitors with suitable properties for use in humans is thus justified.

Keywords

Simian Immunodeficiency Virus Native Enzyme Inhibitor Binding Hydrophobic Interaction Chromatography Aspartyl Protease 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1991

Authors and Affiliations

  • Paul L. Darke
    • 1
  • Nancy E. Kohl
    • 1
  • Michelle G. Hanobik
    • 1
  • Chih-Tai Leu
    • 1
  • Joseph P. Vacca
    • 1
  • James P. Guare
    • 1
  • Jill C. Heimbach
    • 1
  • Richard A. F. Dixon
    • 1
  1. 1.Merck Sharp and Dohme Research LaboratoriesWest PointUSA

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