Results 151 to 160 of about 62,041 (172)
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Nontemplated Nucleotide Addition by HIV-1 Reverse Transcriptase

Biochemistry, 2002
We studied the kinetics of nontemplated nucleotide addition by the reverse transcriptase (RT) of human immunodeficiency virus type 1 (HIV-1) using model substrates derived from the 3' end of HIV-1 minus-strand strong-stop DNA. The addition of a nontemplated nucleotide was highly dependent on the nature of the base (fastest addition with dATP), type of ...
Marie-Pierre, Golinelli   +1 more
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The Accuracy of Reverse Transcriptase from HIV-1

Science, 1988
A study was conducted to determine the fidelity of DNA synthesis catalyzed in vitro by the reverse transcriptase from a human immunodeficiency virus type 1 (HIV-1). Like other retroviral reverse transcriptases, the HIV-1 enzyme does not correct errors by exonucleolytic proofreading.
J D, Roberts, K, Bebenek, T A, Kunkel
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An HIV Reverse Transcriptase-Selective Nucleoside Chain Terminator

Journal of the American Chemical Society, 2002
The synthesis of a 2',3'-dideoxynucleoside cytidine analogue, but one that lacks the O2-carbonyl, is described from 2-aminopyridine in an overall yield of 60%. The synthesis of the 2-pyridone C-nucleoside relies upon the use of a Heck-type coupling between an appropriately protected sugar glycal and the 5-iodo derivative of 2-aminopyridone.
Andrew W, Fraley   +3 more
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Active site labeling of HIV-1 reverse transcriptase

Biochemistry, 1993
The human immunodeficiency virus-1 reverse transcriptase (HIV-1 RT) heterodimer (M(r) = 66,000 and M(r) = 51,000) has been photoaffinity labeled using 4-thiodeoxyuridine triphosphate (S4-dUTP) as a probe. A nascent polymerization complex was assembled from a single-stranded DNA template, a 12-mer DNA primer, and the necessary dNTPs (one of which was ...
N, Sheng, D, Dennis
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Inhibitors of HIV- I reverse transcriptase

2000
Publisher Summary This chapter discusses the current clinically used reverse transcriptase (RT) inhibitors and some promising new inhibitors still in preclinical development, emphasizing the mechanisms of action of RT inhibitors and the mechanisms of viral resistance that develop upon continued exposure of the virus to these compounds.
Michael A. Parniak, Nicolas Sluis-Cremer
openaire   +1 more source

Structure-activity analyses of HIV-1 reverse transcriptase

Biochemical and Biophysical Research Communications, 1992
HIV-1 reverse transcriptase is a dimeric enzyme which can exist in both homodimeric (p66/p66) and heterodimeric (p66/p51) forms. The monomeric subunits are catalytically inert. However, during DNA synthesis by the dimeric enzyme, only one subunit (p66) appears to carry out the catalysis, while the second subunit serves only a supportive role.
A, Basu, S, Basu, M J, Modak
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Theoretical studies of HIV-1 reverse transcriptase inhibition

Physical Chemistry Chemical Physics, 2012
Computational methods for accurately calculating the binding affinity of a ligand for a protein play a pivotal role in rational drug design. We herein present a theoretical study of the binding of five different ligands to one of the proteins responsible for the human immunodeficiency virus type 1 (HIV-1) cycle replication; the HIV-1 reverse ...
Katarzyna, Świderek   +2 more
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Specific HIV-1 Reverse Transcriptase Inhibitors

Journal of Enzyme Inhibition, 1992
Z, Debyser   +3 more
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Nucleotide HIV reverse transcriptase inhibitors: tenofovir and beyond

Current Opinion in HIV and AIDS, 2006
This review describes the class of nucleotide HIV reverse transcriptase inhibitors and summarises recent findings related to tenofovir and its oral prodrug tenofovir disoproxil fumarate, currently the only nucleotide approved for the treatment of HIV infection.
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Evaluation of Compounds Against Recombinant HIV Reverse Transcriptase

2003
Reverse transcriptase (RT) has attracted particular attention as a target enzyme for AIDS chemotherapy, because the enzyme catalyzes a crucial step in the HIV replicative cycle. Effective inhibition of this enzyme prevents the formation of proviral DNA. RT is endowed with three independent enzymatic activities (1,2).
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