Journal of virological methods, 61(1-2), 113-125 (1996-09-01)
Many bacterial expression systems have been developed to study the reverse transcriptase (RT) of human immunodeficiency virus type 1 (HIV-1). This enzyme exists in the virions as a heterodimer of a 66 kDa (p66) subunit and a 51 kDa (p51)
The Journal of biological chemistry, 269(41), 25255-25258 (1994-10-14)
Determination of the three-dimensional structure of the human immunodeficiency virus type-1 (HIV-1) reverse transcriptase (RT) has indicated a totally different folding for the 51-kDa subunit (p51) than for the 66-kDa subunit (p66). The polymerase catalytic site is located on the
The Plant journal : for cell and molecular biology, 47(5), 802-810 (2006-07-22)
RNA editing is found in various transcripts from land plant chloroplasts. In tobacco chloroplasts, C-to-U conversion occurs at 36 specific sites including two sites identified in this work. Our RNA editing assay system using chloroplast extracts facilitated biochemical analyses of
Trp-229 is part of the non-nucleoside reverse transcriptase inhibitor (NNRTI)-binding pocket of HIV type 1 (HIV-1) reverse transcriptase (RT), and is also part of the "primer grip" of HIV-1 RT. Using site-directed mutagenesis, seven RT mutants were constructed bearing the
To map the determinants of the lack of susceptibility of feline immunodeficiency virus (FIV) reverse transcriptase (RT) to anti human immunodeficiency virus type 1 (HIV-1) non-nucleoside RT inhibitors (NNRTIs), a variety of chimeric HIV-1/FIV RTs were constructed. The majority of
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