ArticleRNA (New York, N.Y.)2004
Isolation of specific and high-affinity RNA aptamers against NS3 helicase domain of hepatitis C virus.
Article in RNA (New York, N.Y.), 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 51 citations in OpenAlex.
- Generation of hepatitis C virus-resistant liver cells by genome editing-mediated stable expression of RNA aptamer.Molecular therapy. Methods & clinical development · 2023Article
- Designing of peptide aptamer targeting the receptor-binding domain of spike protein of SARS-CoV-2: an in silico study.Molecular diversity · 2022Article
- Aptamers for Anti-Viral Therapeutics and Diagnostics.International journal of molecular sciences · 2021Review
- Aptamers: Uptake mechanisms and intracellular applications.Advanced drug delivery reviews · 2018Review
- Targeting the ATP-dependent formation of herpesvirus ribonucleoprotein particle assembly as an antiviral approach.Nature microbiology · 2016Article
- Pharmacokinetics of a Cholesterol-conjugated Aptamer Against the Hepatitis C Virus (HCV) NS5B Protein.Molecular therapy. Nucleic acids · 2015Article
- Facilitated Tau Degradation by USP14 Aptamers via Enhanced Proteasome Activity.Scientific reports · 2015Article
- Aptamers as a novel tool for diagnostics and therapy.Investigational new drugs · 2015Review
- Prospects for nucleic acid-based therapeutics against hepatitis C virus.World journal of gastroenterology · 2013Review
- Discovering new medicines targeting helicases: challenges and recent progress.Journal of biomolecular screening · 2013Review
- Inhibition of hepatitis C virus (HCV) replication by specific RNA aptamers against HCV NS5B RNA replicase.Journal of virology · 2013Article
- Selection and analytical applications of aptamers binding microbial pathogens.Trends in analytical chemistry : TRAC · 2011Review
- CS-SELEX generates high-affinity ssDNA aptamers as molecular probes for hepatitis C virus envelope glycoprotein E2.PloS one · 2009Article
- Aptasensors for detection of microbial and viral pathogens.Biosensors & bioelectronics · 2009Review
- Helicase inhibitors as specifically targeted antiviral therapy for hepatitis C.Future virology · 2009Article
- Isolation of inhibitory RNA aptamers against severe acute respiratory syndrome (SARS) coronavirus NTPase/Helicase.Biochemical and biophysical research communications · 2008Article
- The hepatitis C virus NS3 protein: a model RNA helicase and potential drug target.Current issues in molecular biology · 2007Review
- Selection and characterization of RNA aptamers to the RNA-dependent RNA polymerase from foot-and-mouth disease virus.RNA (New York, N.Y.) · 2006Article
- Understanding helicases as a means of virus control.Current pharmaceutical design · 2006Review
- Bis-aptazyme sensors for hepatitis C virus replicase and helicase without blank signal.Nucleic acids research · 2005Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hepatitis C virus (HCV)-encoded nonstructural protein 3 (NS3) possesses protease, NTPase, and helicase activities, which are considered essential for viral proliferation. Thus, HCV NS3 is a good putative therapeutic target protein for the development of anti-HCV agents. In this study, we isolated specific RNA aptamers to the helicase domain of HCV NS3 from a combinatorial RNA library with 40-nucleotide random sequences using in vitro selection techniques. The isolated RNAs were observed to very avidly bind the HCV helicase with an apparent Kd of 990 pM in contrast to original pool RNAs with a Kd of >1 microM. These RNA ligands appear to impede binding of substrate RNA to the HCV helicase and can act as potent decoys to competitively inhibit helicase activity with high efficiency compared with poly(U) or tRNA. The minimal binding domain of the ligands was determined to evaluate the structural features of the isolated RNA molecules. Interestingly, part of binding motif of the RNA aptamers consists of similar secondary structure to the 3'-end of HCV negative-strand RNA. Moreover, intracellular NS3 protein can be specifically detected in situ with the RNA aptamers, indicating that the selected RNAs are very specific to the HCV NS3 helicase. Furthermore, the RNA aptamers partially inhibited RNA synthesis of HCV subgenomic replicon in Huh-7 hepatoma cell lines. These results suggest that the RNA aptamers selected in vitro could be useful not only as therapeutic and diagnostic agents of HCV infection but also as a powerful tool for the study of HCV helicase mechanism.
Indexed as
Identifiers
What OpenQuestion holds
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.