ArticleNucleic acids research2005
Target-dependent on/off switch increases ribozyme fidelity.
Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Programming anti-ribozymes to sense trigger RNAs for modulating gene expression in mammalian cells.Synthetic and systems biotechnology · 2025Article
- Design and testing of Hepatitis Delta Ribozymes for suppression of Chikungunya virus infection in cell cultures.Medical research archives · 2024Article
- Topological constraints of structural elements in regulation of catalytic activity in HDV-like self-cleaving ribozymes.Scientific reports · 2016Article
- Effective inhibition of HIV-1 production by short hairpin RNAs and small interfering RNAs targeting a highly conserved site in HIV-1 Gag RNA is optimized by evaluating alternative length formats.Antimicrobial agents and chemotherapy · 2015Article
- A Conserved Target Site in HIV-1 Gag RNA is Accessible to Inhibition by Both an HDV Ribozyme and a Short Hairpin RNA.Molecular therapy. Nucleic acids · 2014Article
- Prospects for nucleic acid-based therapeutics against hepatitis C virus.World journal of gastroenterology · 2013Review
- Silencing of amyloid precursor protein expression using a new engineered delta ribozyme.International journal of Alzheimer's disease · 2012Article
- Selection of the most potent specific on/off adaptor-hepatitis delta virus ribozymes for use in gene targeting.Nucleic acid therapeutics · 2011Article
- Molecular Validation of PACE4 as a Target in Prostate Cancer.Translational oncology · 2011Article
- A novel ribozyme-based prophylaxis inhibits influenza A virus replication and protects from severe disease.PloS one · 2011Article
- Article
- Modulating RNA structure and catalysis: lessons from small cleaving ribozymes.Cellular and molecular life sciences : CMLS · 2009Review
- Development of an isoform-specific gene suppression system: the study of the human Pax-5B transcriptional element.Nucleic acids research · 2008Article
- A modern mode of activation for nucleic acid enzymes.PloS one · 2007Article
- RiboSubstrates: a web application addressing the cleavage specificities of ribozymes in designated genomes.BMC bioinformatics · 2006Article
- Gene targeting in the Gram-Positive bacterium Lactococcus lactis, using various delta ribozymes.Applied and environmental microbiology · 2006Article
- Controlling the rate of organic reactions: rational design of allosteric Diels-Alderase ribozymes.Nucleic acids research · 2006Article
- Functional characterization of the SOFA delta ribozyme.RNA (New York, N.Y.) · 2005Article
- Bis-aptazyme sensors for hepatitis C virus replicase and helicase without blank signal.Nucleic acids research · 2005Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Ribozymes, RNA molecules that catalyze the cleavage of RNA substrates, provide an interesting alternative to the RNA interference (RNAi) approach to gene inactivation, especially given the fact that RNAi seems to trigger an immunological response. Unfortunately, the limited substrate specificity of ribozymes is considered to be a significant hurdle in their development as molecular tools. Here, we report the molecular engineering of a ribozyme possessing a new biosensor module that switches the cleavage activity from 'off' (a 'safety lock') to 'on' solely in the presence of the appropriate RNA target substrate. Both proof-of-concept and the mechanism of action of this man-made riboswitch are demonstrated using hepatitis delta virus ribozymes that cleave RNA transcripts derived from the hepatitis B and C viruses. To our knowledge, this is the first report of a ribozyme bearing a target-dependent module that is activated by its RNA substrate, an arrangement which greatly diminishes non-specific effects. This new approach provides a highly specific and improved tool with significant potential for application in the fields of both functional genomics and gene therapy.
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