RNA targeting therapeutics: molecular mechanisms of antisense oligonucleotides as a therapeutic platform.
By C. Bennett, E. Swayze. Annual Review of Pharmacology and Toxicology, 2010
1,307 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/4647a7540cdbc682c44564669e9d1ab76c4d84fc
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Citations in the corpus
- Pharmacokinetics, biodistribution and cell uptake of antisense oligonucleotides. (2015, background): “C metabolism such as splicing and (2) double-stranded synthetic oligonucleotides that work through an RNA-induced silencing complex (RISC) to promote degradation of the target RNA [2].”
- Remodeling of the enhancer landscape during macrophage activation is coupled to enhancer transcription (2013, methodology): “We used locked nucleic acid antisense oligos (ASOs), which mediate nuclear RNA degradation via an RNase H pathway (Bennett and Swayze, 2010), to knock down the eRNAs for Irg1 and Ifnar2 enhancers (Figure S5F).”
- RNA Phase Transitions in Repeat Expansion Disorders (2017, neutral): “ASOs may disrupt cellular RNA foci either by inhibiting intermolecular base-pairing or by degrading RNA via the RNase H machinery 34 .”
- RNA-based Therapeutics- Current Progress and Future Prospects (2012, background): “However, recent reviews have addressed the current status of clinical antisense drugs (Bennett and Swayze, 2010; Sanghvi, 2011).”
- Sustained therapeutic reversal of Huntington’s disease by transient repression of huntingtin synthesis (2012, neutral): “nervous system, a 20-mer phosphorothioate modified oligonucleotide complementary to human huntingtin mRNA (HuASO) and containing 20-O-(-2-methoxy) ethyl modifications on the five nucleotides on the 30 and 50 ends to increase its stability, tolerability and potency (Bennett and Swayze, 2010; Henry et”
- The delivery of therapeutic oligonucleotides (2016, background): “Although ASOs can also act by translation arrest, they are currently primarily used as ‘gapmers’, having a central region that supports RNase H activity flanked by chemically modified ends that increase affinity and reduce susceptibility to nucleases (19).”