ArticleNucleic acids research2003
Selective inhibitory DNA aptamers of the human RNase H1.
Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 72 citations in OpenAlex.
- G-Quadruplex-Based Fluorescent Turn-On Ligands and Aptamers: From Development to Applications.Molecules (Basel, Switzerland) · 2019Review
- Cross-protection of influenza A virus infection by a DNA aptamer targeting the PA endonuclease domain.Antimicrobial agents and chemotherapy · 2015Article
- Selection and Characterization of DNA Aptamers Targeting All Four Serotypes of Dengue Viruses.PloS one · 2015Article
- d(CGGTGGT) forms an octameric parallel G-quadruplex via stacking of unusual G(:C):G(:C):G(:C):G(:C) octads.Nucleic acids research · 2011Article
- The evolving world of protein-G-quadruplex recognition: a medicinal chemist's perspective.Biochimie · 2011Review
- siRNA-like double-stranded RNAs are specifically protected against degradation in human cell extract.PloS one · 2011Article
- Applications of isothermal titration calorimetry in biophysical studies of G-quadruplexes.International journal of molecular sciences · 2009Review
- A mathematical analysis of SELEX.Computational biology and chemistry · 2007Article
- High-affinity aptamers to subtype 3a hepatitis C virus polymerase display genotypic specificity.Antimicrobial agents and chemotherapy · 2006Article
- Combinatorial selection, inhibition, and antiviral activity of DNA thioaptamers targeting the RNase H domain of HIV-1 reverse transcriptase.Biochemistry · 2005Article
- Selective inhibition of HIV-1 reverse transcriptase-associated ribonuclease H activity by hydroxylated tropolones.Nucleic acids research · 2005Article
- Selection of genomic sequences that bind tightly to Ff gene 5 protein: primer-free genomic SELEX.Nucleic acids research · 2004Article
- Colorimetric biosensors based on DNAzyme-assembled gold nanoparticles.Journal of fluorescence · 2004Review
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
Human RNase H1 binds double-stranded RNA via its N-terminal domain and RNA-DNA hybrid via its C-terminal RNase H domain, the latter being closely related to Escherichia coli RNase HI. Using SELEX, we have generated a set of DNA sequences that can bind efficiently (K(d) values ranging from 10 to 80 nM) to the human RNase H1. None of them could fold into a simple perfect double-stranded DNA hairpin confirming that double-stranded DNA does not constitute a trivial ligand for the enzyme. Only two of the 37 DNA aptamers selected were inhibitors of human RNase H1 activity. The two inhibitory oligomers, V-2 and VI-2, were quite different in structure with V-2 folding into a large, imperfect but stable hairpin loop. The VI-2 structure consists of a central region unimolecular quadruplex formed by stacking of two guanine quartets flanked by the 5' and 3' tails that form a stem of six base pairs. Base pairing between the 5' and 3' tails appears crucial for conferring the inhibitory properties to the aptamer. Finally, the inhibitory aptamers were capable of completely abolishing the action of an antisense oligonucleotide in a rabbit reticulocyte lysate supplemented with human RNase H1, with IC50 ranging from 50 to 100 nM.
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