ArticleNucleic acids research2008
Aptamers that recognize drug-resistant HIV-1 reverse transcriptase.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 47 citations in OpenAlex.
- Selection and identification of an RNA aptamer that specifically binds the HIV-1 capsid lattice and inhibits viral replication.Nucleic acids research · 2022Article
- Review
- Functionalized gold nanoparticles: promising and efficient diagnostic and therapeutic tools for HIV/AIDS.RSC medicinal chemistry · 2020Review
- Predicting Future Prospects of Aptamers in Field-Effect Transistor Biosensors.Molecules (Basel, Switzerland) · 2020Article
- Aptamers against pathogenic microorganisms.Critical reviews in microbiology · 2016Review
- Application of aptamers in diagnostics, drug-delivery and imaging.Journal of biosciences · 2016Article
- High-affinity RNA Aptamers Against the HIV-1 Protease Inhibit Both In Vitro Protease Activity and Late Events of Viral Replication.Molecular therapy. Nucleic acids · 2015Article
- New Technologies Provide Quantum Changes in the Scale, Speed, and Success of SELEX Methods and Aptamer Characterization.Molecular therapy. Nucleic acids · 2014Article
- Aptamers: multifunctional molecules for biomedical research.Journal of molecular medicine (Berlin, Germany) · 2013Review
- Aptamer-based therapeutics: new approaches to combat human viral diseases.Pharmaceuticals (Basel, Switzerland) · 2013Article
- Potent Inhibition of HIV-1 Reverse Transcriptase and Replication by Nonpseudoknot, "UCAA-motif" RNA Aptamers.Molecular therapy. Nucleic acids · 2013Article
- High-throughput sequence analysis reveals structural diversity and improved potency among RNA inhibitors of HIV reverse transcriptase.Nucleic acids research · 2013Article
- Robust suppression of HIV replication by intracellularly expressed reverse transcriptase aptamers is independent of ribozyme processing.Molecular therapy : the journal of the American Society of Gene Therapy · 2012Article
- Selection strategy to generate aptamer pairs that bind to distinct sites on protein targets.Analytical chemistry · 2012Article
- Selection and analytical applications of aptamers binding microbial pathogens.Trends in analytical chemistry : TRAC · 2011Review
- Broad-spectrum aptamer inhibitors of HIV reverse transcriptase closely mimic natural substrates.Nucleic acids research · 2011Article
- Inhibition of cell proliferation by an anti-EGFR aptamer.PloS one · 2011Article
- Therapeutic applications of DNA and RNA aptamers.Oligonucleotides · 2009Review
- Aptamers and aptamer targeted delivery.RNA biologyReview
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Drug-resistant variants of HIV-1 reverse transcriptase (RT) are also known to be resistant to anti-RT RNA aptamers. In order to be able to develop diagnostics and therapies that can focus on otherwise drug-resistant viruses, we have isolated two aptamers against a well-known, drug-resistant HIV-1 RT, Mutant 3 (M3) from the multidrug-resistant HIV-1 RT panel. One aptamer, M302, bound M3 but showed no significant affinity for wild-type (WT) HIV-1 RT, while another aptamer, 12.01, bound to both M3 and WT HIV-1 RTs. In contrast to all previously selected anti-RT aptamers, neither of these aptamers showed observable inhibition of either polymerase or RNase H activities. Aptamers M302 and 12.01 competed with one another for binding to M3, but they did not compete with a pseudoknot aptamer for binding to the template/primer cleft of WT HIV-1 RT. These results represent the surprising identification of an additional RNA-binding epitope on the surface of HIV-1 RT. M3 and WT HIV-1 RTs could be distinguished using an aptamer-based microarray. By probing protein conformation as a correlate to drug resistance we introduce an additional and useful measure for determining HIV-1 drug resistance.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.