Article
Enzymatic properties of two mutants of reverse transcriptase of human immunodeficiency virus type 1 (tyrosine 181-->isoleucine and tyrosine 188-->leucine), resistant to nonnucleoside inhibitors.
AIDS research and human retroviruses - 1 Aug 1994
Loya S, Bakhanashvili M, Tal R, Hughes S H, Boyer P L, Hizi A
Abstract excerpt
A number of structurally diverse compounds have been shown to be potent inhibitors of the DNA polymerase activity of human immunodeficiency virus (HIV-1) reverse transcriptase (RT). The compounds can be grouped into two broad classes: nucleoside analogs and nonnucleoside inhibitors. The nonnucleoside inhibitors are quite specific for the polymerase activity of HIV-1 RT; they do not affect the polymerase activity...
Topics
- Amino Acid Sequence
- Base Sequence
- Binding Sites
- Catalysis
- DNA, Viral
- Deoxyguanine Nucleotides
- Dideoxynucleotides
- Drug Resistance, Microbial
- HIV Reverse Transcriptase
- HIV-1