Interface Peptides as Structure-based Human Immunodeficiency Virus Reverse Transcriptase Inhibitors

This publication has 29 references indexed in Scilit:

• Dimerization Kinetics of HIV-1 and HIV-2 Reverse Transcriptase: A Two Step Process
  Journal of Molecular Biology, 1995
• Crystal structure of human immunodeficiency virus type 1 reverse transcriptase complexed with double-stranded DNA at 3.0 A resolution shows bent DNA.
  Proceedings of the National Academy of Sciences, 1993
• Characterization of the dimerization process of HIV‐1 reverse transcriptase heterodimer using intrinsic protein fluorescence
  FEBS Letters, 1993
• Crystal Structure at 3.5 Å Resolution of HIV-1 Reverse Transcriptase Complexed with an Inhibitor
  Science, 1992
• Purification and Partial Characterization of Human Immunodeficiency Virus Type 2 Reverse Transcriptase
  AIDS Research and Human Retroviruses, 1989
• Serological relationship between reverse transcriptases from human T‐cell lymphotropic viruses denned by monoclonal antibodies
  FEBS Letters, 1986
• Specific inhibition of herpesvirus ribonucleotide reductase by a nonapeptide derived from the carboxy terminus of subunit 2
  Nature, 1986
• Specific inhibition of herpesvirus ribonucleotide reductase by synthetic peptides
  Nature, 1986
• Characterization of Highly Immunogenic p66/p51 as the Reverse Transcriptase of HTLV-III/LAV
  Science, 1986
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976