Results 191 to 200 of about 73,667 (245)
Some of the next articles are maybe not open access.
HIV nucleoside reverse transcriptase inhibitors
European Journal of Medicinal Chemistry, 2022More than 40 years into the pandemic, HIV remains a global burden and as of now, there is no cure in sight. Fortunately, highly active antiretroviral therapy (HAART) has been developed to manage and suppress HIV infection. Combinations of two to three drugs targeting key viral proteins, including compounds inhibiting HIV reverse transcriptase (RT ...
Raymond Schinazi +2 more
exaly +3 more sources
Fidelity of HIV-1 Reverse Transcriptase
Science, 1988The 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
openaire +2 more sources
HIV-1 reverse transcriptase inhibitors
Applied Microbiology and Biotechnology, 2007Reverse transcriptase (RT) is one of the three enzymes encoded by the human immunodeficiency virus type 1 (HIV-1), the etiological agent of AIDS. Together with protease inhibitors, drugs inhibiting the RNA- and DNA-dependant DNA polymerase activity of RT are the major components of highly active antiretroviral therapy (HAART), which has dramatically ...
El Safadi, Yazan +2 more
openaire +3 more sources
Inhibitors of HIV‐1 Reverse Transcriptase
2008Publisher 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
openaire +2 more sources
The Accuracy of Reverse Transcriptase from HIV-1
Science, 1988A 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
openaire +2 more sources
HIV Inhibitors Targeted at the Reverse Transcriptase
AIDS Research and Human Retroviruses, 1992HIV 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 ...
openaire +2 more sources
Targeting HIV reverse transcriptase in novel ways
Nature Medicine, 1995The 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
openaire +2 more sources
HIV reverse transcriptase structure-function relationships
Biochemistry, 1991HIV 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
openaire +2 more sources
Coumarins as Inhibitors of HIV Reverse Transcriptase
Current HIV Research, 2006Acquired 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).
openaire +2 more sources

