ArticleJournal of virology2018
Developing and Evaluating Inhibitors against the RNase H Active Site of HIV-1 Reverse Transcriptase.
Article in Journal of virology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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The trial behind it
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Who cites it
20 citing papers in PubMed, 39 citations in OpenAlex.
- Potential Benefits of In Silico Methods: A Promising Alternative in Natural Compound's Drug Discovery and Repurposing for HBV Therapy.Pharmaceuticals (Basel, Switzerland) · 2025Review
- An ultrasensitive label-free RNase H assay based onNanoscale advances · 2024Article
- Targeting the Structural Maturation Pathway of HIV-1 Reverse Transcriptase.Biomolecules · 2023Article
- 5-Nitro-3-(2-(4-phenylthiazol-2-yl)hydrazineylidene)indolin-2-one derivatives inhibit HIV-1 replication by a multitarget mechanism of action.Frontiers in cellular and infection microbiology · 2023Article
- RNase HI Depletion Strongly Potentiates Cell Killing by Rifampicin in Mycobacteria.Antimicrobial agents and chemotherapy · 2022Article
- Contribution of the HIV-1 Envelope Glycoprotein to AIDS Pathogenesis and Clinical Progression.Biomedicines · 2022Review
- A Combination of Amino Acid Mutations Leads to Resistance to Multiple Nucleoside Analogs in Reverse Transcriptases from HIV-1 Subtypes B and C.Antimicrobial agents and chemotherapy · 2022Article
- Quinolinonyl Non-Diketo Acid Derivatives as Inhibitors of HIV-1 Ribonuclease H and Polymerase Functions of Reverse Transcriptase.Journal of medicinal chemistry · 2021Article
- Exploring New Scaffolds for the Dual Inhibition of HIV-1 RT Polymerase and Ribonuclease Associated Functions.Molecules (Basel, Switzerland) · 2021Article
- Structural Insights to Human Immunodeficiency Virus (HIV-1) Targets and Their Inhibition.Advances in experimental medicine and biology · 2021Article
- Retroviral RNase H: Structure, mechanism, and inhibition.The Enzymes · 2021Review
- Scaffold hopping and optimisation of 3',4'-dihydroxyphenyl- containing thienopyrimidinones: synthesis of quinazolinone derivatives as novel allosteric inhibitors of HIV-1 reverse transcriptase-associated ribonuclease H.Journal of enzyme inhibition and medicinal chemistry · 2020Article
- Ribonuclease-Responsive DNA Nanoswitches.Cell reports. Physical science · 2020Article
- Targeting HIV-1 RNase H:Viruses · 2020Article
- Pyrrolyl Pyrazoles as Non-Diketo Acid Inhibitors of the HIV-1 Ribonuclease H Function of Reverse Transcriptase.ACS medicinal chemistry letters · 2020Article
- Evolving understanding of HIV-1 reverse transcriptase structure, function, inhibition, and resistance.Current opinion in structural biology · 2020Review
- 2-(Arylamino)-6-(trifluoromethyl)nicotinic Acid Derivatives: New HIV-1 RT Dual Inhibitors Active on Viral Replication.Molecules (Basel, Switzerland) · 2020Article
- Cutting into the Substrate Dominance: Pharmacophore and Structure-Based Approaches toward Inhibiting Human Immunodeficiency Virus Reverse Transcriptase-Associated Ribonuclease H.Accounts of chemical research · 2020Review
- New targets for HIV drug discovery.Drug discovery today · 2019Review
- Current and Future Therapeutic Strategies for Lentiviral Eradication from Macrophage Reservoirs.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2019Review
Corrections and comments
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Authors and funding
8 authors at 5 institutions in 2 countries.
Funding
Abstract
We tested three compounds for their ability to inhibit the RNase H (RH) and polymerase activities of HIV-1 reverse transcriptase (RT). A high-resolution crystal structure (2.2 Å) of one of the compounds showed that it chelates the two magnesium ions at the RH active site; this prevents the RH active site from interacting with, and cleaving, the RNA strand of an RNA-DNA heteroduplex. The compounds were tested using a variety of substrates: all three compounds inhibited the polymerase-independent RH activity of HIV-1 RT. Time-of-addition experiments showed that the compounds were more potent if they were bound to RT before the nucleic acid substrate was added. The compounds significantly inhibited the site-specific cleavage required to generate the polypurine tract (PPT) RNA primer that initiates the second strand of viral DNA synthesis. The compounds also reduced the polymerase activity of RT; this ability was a result of the compounds binding to the RH active site. These compounds appear to be relatively specific; they do not inhibit either
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Registered trials
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