HIV Reverse Transcriptase
"HIV Reverse Transcriptase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A reverse transcriptase encoded by the POL GENE of HIV. It is a heterodimer of 66 kDa and 51 kDa subunits that are derived from a common precursor protein. The heterodimer also includes an RNAse H activity (RIBONUCLEASE H, HUMAN IMMUNODEFICIENCY VIRUS) that plays an essential role the viral replication process.
| Descriptor ID |
D054303
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| MeSH Number(s) |
D08.811.913.696.445.308.300.750.187 D12.776.964.775.375.545.875 D12.776.964.775.375.750.187 D12.776.964.775.562.764.875 D12.776.964.970.600.850.375.545.875 D12.776.964.970.600.850.375.750.187
|
| Concept/Terms |
HIV Reverse Transcriptase- HIV Reverse Transcriptase
- Transcriptase, HIV Reverse
- Reverse Transcriptase, Human Immunodeficiency Virus
- Reverse Transcriptase, HIV
|
Below are MeSH descriptors whose meaning is more general than "HIV Reverse Transcriptase".
Below are MeSH descriptors whose meaning is more specific than "HIV Reverse Transcriptase".
This graph shows the total number of publications written about "HIV Reverse Transcriptase" by people in this website by year, and whether "HIV Reverse Transcriptase" was a major or minor topic of these publications.
To see the data from this visualization as text,
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1996 | 0 | 1 | 1 |
| 2000 | 1 | 0 | 1 |
| 2002 | 0 | 1 | 1 |
| 2007 | 1 | 0 | 1 |
| 2009 | 0 | 1 | 1 |
| 2013 | 1 | 1 | 2 |
| 2015 | 1 | 0 | 1 |
| 2017 | 3 | 0 | 3 |
| 2018 | 1 | 0 | 1 |
| 2024 | 0 | 1 | 1 |
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Below are the most recent publications written about "HIV Reverse Transcriptase" by people in Profiles.
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Variable antiviral activity of islatravir against M184I/V mutant HIV-1 selected during antiretroviral therapy. J Antimicrob Chemother. 2024 02 01; 79(2):370-374.
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Diaryl ethers with carboxymethoxyphenacyl motif as potent HIV-1 reverse transcriptase inhibitors with improved solubility. J Enzyme Inhib Med Chem. 2018 Dec; 33(1):9-16.
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Oxygen binding isotope effects of triazole-based HIV-1 reverse transcriptase inhibitors indicate the actual binding site. Arch Biochem Biophys. 2017 12 01; 635:87-95.
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A Search for Dual Action HIV-1 Reverse Transcriptase, Bacterial RNA Polymerase Inhibitors. Molecules. 2017 Oct 25; 22(11).
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The ?1'-?2' Motif of the RNase H Domain of Human Immunodeficiency Virus Type 1 Reverse Transcriptase Is Responsible for Conferring Open Conformation to the p66 Subunit by Displacing the Connection Domain from the Polymerase Cleft. Biochemistry. 2017 07 11; 56(27):3434-3442.
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Searching for novel scaffold of triazole non-nucleoside inhibitors of HIV-1 reverse transcriptase. J Enzyme Inhib Med Chem. 2016; 31(3):481-9.
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Assessing molecular docking tools for relative biological activity prediction: a case study of triazole HIV-1 NNRTIs. J Chem Inf Model. 2013 Dec 23; 53(12):3326-42.
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Complete and repeatable inactivation of HIV-1 viral particles in suspension using a photo-labeled non-nucleoside reverse transcriptase inhibitor. J Virol Methods. 2013 Apr; 189(1):125-8.
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Clinical evidence of interaction between itraconazole and nonnucleoside reverse transcriptase inhibitors in HIV-infected patients with disseminated histoplasmosis. Ann Pharmacother. 2009 May; 43(5):908-13.
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Suppression of viremia and evolution of human immunodeficiency virus type 1 drug resistance in a macaque model for antiretroviral therapy. J Virol. 2007 Nov; 81(22):12145-55.