Results 141 to 150 of about 62,041 (172)

HIV reverse transcriptase structure-function relationships

Biochemistry, 1991
HIV reverse transcriptase (RT) is the target of the most widely used treatments for AIDS. Biochemical and mutagenesis studies performed on HIV-1 RT are reviewed in light of the enzyme's structure and functions. Features described include domain arrangement, dimerization, proteolytic processing, and specific recognition of the priming tRNA.
A, Jacobo-Molina, E, Arnold
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Fidelity of HIV-1 Reverse Transcriptase

Science, 1988
The human immunodeficiency virus type 1 (HIV-1) shows extensive genetic variation and undergoes rapid evolution. The fidelity of purified HIV-1 reverse transcriptase was measured during DNA polymerization in vitro by means of three different assays.
B D, Preston, B J, Poiesz, L A, Loeb
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Inhibitors of HIV‐1 Reverse Transcriptase

2008
Publisher Summary With the identification of human immunodeficiency virus (HIV)‐1 as the infectious agent leading to acquired immune deficiency syndrome (AIDS), the viral reverse transcriptase (RT) has been a primary focus for drug discovery and development. Currently, two classes of RT inhibitors are used clinically. Nucleoside reverse transcriptase
Tatiana, Ilina, Michael A, Parniak
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Colorimetric reverse transcriptase assay for HIV-1

Journal of Virological Methods, 1993
A colorimetric assay for reverse transcriptase (RT) of the human immunodeficiency virus type 1 (HIV-1) was developed using a double labelled (biotin and digoxigenin) deoxyuridine triphosphate mixture instead of tritiated thymidine triphosphate. After the RT reaction, the newly polymerized strand from oligodeoxythymidylic acid (oligo-dT) contained both ...
K, Suzuki, B P, Craddock, T, Kano, R T, Steigbigel   +3 more
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Targeting HIV reverse transcriptase in novel ways

Nature Medicine, 1995
The promising description of a potential basis for gene therapy in treating HIV infection does not mean that traditional approaches should be abandoned (pages 667–673).
M A, Wainberg, Z, Gu
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Novel HIV-1 reverse transcriptase inhibitors

Virus Research, 2008
HIV-1 reverse transcriptase (RT) was the first viral enzyme to be targeted by anti-HIV drugs. Despite 20 years of experience with RT inhibitors, new ways to inhibit this target and address viral resistance continue to emerge. In both licensed RT inhibitor classes, nucleosides (NRTIs) and non-nucleosides (NNRTIs), compounds with better resistance ...
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Chemiluminescent Enzyme-Linked Immunoassay for Reverse Transcriptase, Illustrated by Detection of HIV Reverse Transcriptase

Analytical Biochemistry, 1993
A chemiluminescent assay for reverse transcriptase (RT) of the human immunodeficiency virus 1 was developed using biotin-labeled oligodeoxythymidylic acid (biotin oligo-dT) and digoxigenin-deoxyuridine triphosphate instead of tritiated thymidine triphosphate. After the RT reaction, the newly polymerized strand from biotin oligo-dT contained digoxigenin
K, Suzuki, B P, Craddock, T, Kano, R T, Steigbigel   +3 more
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HIV-1 Reverse Transcriptase Resistance to Nonnucleoside Inhibitors

Biochemistry, 1996
The parameters governing the polymerization mechanism of reverse transcriptase containing the tyrosine to cysteine mutation at position 181 (Y181C) were determined using pre-steady-state techniques. The pathway for single nucleotide incorporation catalyzed by Y181C is similar to that determined for wild-type RT where a rate-limiting conformational ...
R A, Spence, K S, Anderson, K A, Johnson
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Coumarins as Inhibitors of HIV Reverse Transcriptase

Current HIV Research, 2006
Acquired immunodeficiency syndrome (AIDS), a degenerative disease of the immune and central nervous systems, is an enormous world-wide health threat. No cure has been found, and research is aimed at developing chemotherapy against the causative agent, human immunodeficiency virus (HIV).
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HIV Inhibitors Targeted at the Reverse Transcriptase

AIDS Research and Human Retroviruses, 1992
HIV inhibitors targeted at the virus-associated reverse transcriptase (RT) can be divided into two groups, depending on whether they are targeted at the substrate or nonsubstrate binding site. To the first group belong the 2',3'-dideoxynucleosides (i.e., DDC, DDI), 3'-azido-2',3'-dideoxynucleosides (i.e., AZT), 3'-fluoro-2',3'-dideoxynucleosides (i.e.,
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