High resolution structures of HIV-1 RT from four RT-inhibitor complexes.

Eitemau Tebyg

• A proline-to-histidine substitution at position 225 of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) sensitizes HIV-1 RT to BHAP U-90152.
  gan: Pelemans, H, et al.
  Cyhoeddwyd: (1998)
• Crystals of HIV-1 reverse transcriptase diffracting to 2.2 A resolution.
  gan: Stammers, D, et al.
  Cyhoeddwyd: (1994)
• Mutational analysis of trp-229 of human immunodeficiency virus type 1 reverse transcriptase (RT) identifies this amino acid residue as a prime target for the rational design of new non-nucleoside RT inhibitors.
  gan: Pelemans, H, et al.
  Cyhoeddwyd: (2000)
• The phenylmethylthiazolylthiourea nonnucleoside reverse transcriptase (RT) inhibitor MSK-076 selects for a resistance mutation in the active site of human immunodeficiency virus type 2 RT.
  gan: Auwerx, J, et al.
  Cyhoeddwyd: (2004)
• Structural studies of benzophenone/HIV-1 RT complexes: insights into the potency of the next generation NNRTls against WT and mutant HIV-1
  gan: Stammers, D, et al.
  Cyhoeddwyd: (2004)