Three-dimensional solution structure of the HIV-1 protease complexed with DMP323, a novel cyclic urea-type inhibitor, determined by nuclear magnetic resonance spectroscopy.

Ítems similars

• Potency and selectivity of inhibition of human immunodeficiency virus protease by a small nonpeptide cyclic urea, DMP 323.
  per: Erickson-Viitanen, S, et al.
  Publicat: (1994)
• DMP 323, a nonpeptide cyclic urea inhibitor of human immunodeficiency virus (HIV) protease, specifically and persistently blocks intracellular processing of HIV gag polyprotein.
  per: Rayner, M M, et al.
  Publicat: (1994)
• Solvation studies of DMP323 and A76928 bound to HIV protease: analysis of water sites using grand canonical Monte Carlo simulations.
  per: Marrone, T. J., et al.
  Publicat: (1998)
• In vitro anti-human immunodeficiency virus (HIV) activity of XM323, a novel HIV protease inhibitor.
  per: Otto, M J, et al.
  Publicat: (1993)
• Evolution of cyclic peptide protease inhibitors
  per: Young, Travis S., et al.
  Publicat: (2011)