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Advances in oligonucleotide drug delivery
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“To unbiasedly evaluate the transcriptomic impact of NRXN1+/− deletions, and their unique splicing patterns, we utilized differential expression analysis27 in iGLUT and iGABA neurons, which revealed overlap of FDR-corrected differentially expressed genes (DEGs) across cell types/genotypes (e.g., FAM66D, TTC34, GALNT9), and represented gene sets related to synaptic function (via SynapseGO28) (Fig. 2”
From Phenotypic complexities of rare heterozygous neurexin-1 deletions (2025) · cites this paper as [28]
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Research works printed but not linked: 263
- Kim, J. et al. Patient-customized oligonucleotide therapy for a rare genetic disease. N. Engl. J. Med. 381, 1644–1652 (2019). This is the first study to utilize an oligonucleotide therapy tailored to a single patient. · DOI
- Giorgio, E. et al. Allele-specific silencing as treatment for gene duplication disorders: proof-of-principle in autosomal dominant leukodystrophy. Brain 142, 1905–1920 (2019). · DOI
- Southwell, A. L. et al. In vivo evaluation of candidate allele-specific mutant huntingtin gene silencing antisense oligonucleotides. Mol. Ther. 22, 2093–2106 (2014). · DOI
- Miller, V. M. et al. Allele-specific silencing of dominant disease genes. Proc. Natl Acad. Sci. USA 100, 7195–7200 (2003). · DOI
- Klein, A. F. et al. Peptide-conjugated oligonucleotides evoke long-lasting myotonic dystrophy correction in patient-derived cells and mice. J. Clin. Invest. 129, 4739–4744 (2019). · DOI
- Crnković-Mertens, I., Semzow, J., Hoppe-Seyler, F. & Butz, K. Isoform-specific silencing of the Livin gene by RNA interference defines Livin β as key mediator of apoptosis inhibition in HeLa cells. J. Mol. Med. 84, 232–240 (2006). · DOI
- Valencia-Serna, J. et al. siRNA-mediated BCR–ABL silencing in primary chronic myeloid leukemia cells using lipopolymers. J. Controlled Rel. 310, 141–154 (2019). · DOI
- Wu, S. Y., Lopez-Berestein, G., Calin, G. A. & Sood, A. K. RNAi therapies: drugging the undruggable. Sci. Transl. Med. 6, 240ps7 (2014).
- Tushir-Singh, J. Antibody–siRNA conjugates: drugging the undruggable for anti-leukemic therapy. Expert Opin. Biol. Ther. 17, 325–338 (2017). · DOI
- Bobbin, M. L., Burnett, J. C. & Rossi, J. J. RNA interference approaches for treatment of HIV-1 infection. Genome Med. 7, 50 (2015). · DOI
- Hermann, T. & Patel, D. J. Adaptive recognition by nucleic acid aptamers. Science 287, 820–825 (2000). · DOI · Paper page
- Jackson, A. L. et al. Widespread siRNA ‘off-target’ transcript silencing mediated by seed region sequence complementarity. RNA 12, 1179–1187 (2006). · DOI
- Scacheri, P. C. et al. Short interfering RNAs can induce unexpected and divergent changes in the levels of untargeted proteins in mammalian cells. Proc. Natl Acad. Sci. USA 101, 1892–1897 (2004). · DOI
- Persengiev, S. P., Zhu, X. & Green, M. R. Nonspecific, concentration-dependent stimulation and repression of mammalian gene expression by small interfering RNAs (siRNAs). RNA 10, 12–18 (2004). · DOI
- Doench, J. G., Petersen, C. P. & Sharp, P. A. siRNAs can function as miRNAs. Genes Dev. 17, 438–442 (2003). · DOI
- Wu, H. et al. Determination of the role of the human RNase H1 in the pharmacology of DNA-like antisense drugs. J. Biol. Chem. 279, 17181–17189 (2004). · DOI
- Crooke, S. T. Molecular mechanisms of antisense oligonucleotides. Nucleic Acid. Ther. 27, 70–77 (2017). · DOI
- Monia, B. P. et al. Evaluation of 2′-modified oligonucleotides containing 2′-deoxy gaps as antisense inhibitors of gene expression. J. Biol. Chem. 268, 14514–14522 (1993). · DOI
- Liang, X.-H., Sun, H., Nichols, J. G. & Crooke, S. T. RNase H1-dependent antisense oligonucleotides are robustly active in directing RNA cleavage in both the cytoplasm and the nucleus. Mol. Ther. 25, 2075–2092 (2017). · DOI
- Lennox, K. A. & Behlke, M. A. Cellular localization of long non-coding RNAs affects silencing by RNAi more than by antisense oligonucleotides. Nucleic Acids Res. 44, 863–877 (2016). · DOI
- Dominski, Z. & Kole, R. Restoration of correct splicing in thalassemic pre-mRNA by antisense oligonucleotides. Proc. Natl Acad. Sci. USA 90, 8673–8677 (1993). · DOI
- Singh, R. N. & Singh, N. N. Mechanism of splicing regulation of spinal muscular atrophy genes. Adv. Neurobiol. 20, 31–61 (2018). · DOI
- Aartsma-Rus, A. et al. Development of exon skipping therapies for Duchenne muscular dystrophy: a critical review and a perspective on the outstanding issues. Nucleic Acid. Ther. 27, 251–259 (2017). · DOI
- Wan, L. & Dreyfuss, G. Splicing-correcting therapy for SMA. Cell 170, 5 (2017). · DOI
- Ward, A. J., Norrbom, M., Chun, S., Bennett, C. F. & Rigo, F. Nonsense-mediated decay as a terminating mechanism for antisense oligonucleotides. Nucleic Acids Res. 42, 5871–5879 (2014). · DOI
- Boiziau, C. et al. Inhibition of translation initiation by antisense oligonucleotides via an RNase-H independent mechanism. Nucleic Acids Res. 19, 1113–1119 (1991). · DOI
- Baker, B. F. et al. 2′-O-(2-methoxy)ethyl-modified anti-intercellular adhesion molecule 1 (ICAM-1) oligonucleotides selectively increase the ICAM-1 mRNA level and inhibit formation of the ICAM-1 translation initiation complex in human umbilical vein endothelial cells. J. Biol. Chem. 272, 11994–12000 (1997). · DOI
- Liang, X.-H. et al. Translation efficiency of mRNAs is increased by antisense oligonucleotides targeting upstream open reading frames. Nat. Biotechnol. 34, 875–880 (2016). · DOI
- Nomakuchi, T. T., Rigo, F., Aznarez, I. & Krainer, A. R. Antisense oligonucleotide-directed inhibition of nonsense-mediated mRNA decay. Nat. Biotechnol. 34, 164–166 (2016). · DOI
- Vickers, T. A., Wyatt, J. R., Burckin, T., Bennett, C. F. & Freier, S. M. Fully modified 2′ MOE oligonucleotides redirect polyadenylation. Nucleic Acids Res. 29, 1293–1299 (2001). · DOI
- Elbashir, S. M. et al. Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411, 494–498 (2001). · DOI · Paper page
- Liu, J. et al. Argonaute2 is the catalytic engine of mammalian RNAi. Science 305, 1437–1441 (2004). · DOI · Paper page
- Roberts, T. C. The microRNA machinery. Adv. Exp. Med. Biol. 887, 15–30 (2015). · DOI
- Schürmann, N., Trabuco, L. G., Bender, C., Russell, R. B. & Grimm, D. Molecular dissection of human Argonaute proteins by DNA shuffling. Nat. Struct. Mol. Biol. 20, 818–826 (2013). · DOI
- Kim, D.-H. et al. Synthetic dsRNA Dicer substrates enhance RNAi potency and efficacy. Nat. Biotechnol. 23, 222–226 (2005). · DOI
- Bramsen, J. B. et al. Improved silencing properties using small internally segmented interfering RNAs. Nucleic Acids Res. 35, 5886–5897 (2007). · DOI
- Byrne, M. et al. Novel hydrophobically modified asymmetric RNAi compounds (sd-rxRNA) demonstrate robust efficacy in the eye. J. Ocul. Pharmacol. Ther. 29, 855–864 (2013). · DOI
- Yu, D. et al. Single-stranded RNAs use RNAi to potently and allele-selectively inhibit mutant huntingtin expression. Cell 150, 895–908 (2012). · DOI
- Lima, W. F. et al. Single-stranded siRNAs activate RNAi in animals. Cell 150, 883–894 (2012). · DOI
- Svoronos, A. A., Engelman, D. M. & Slack, F. J. OncomiR or tumor suppressor? The duplicity of microRNAs in cancer. Cancer Res. 76, 3666–3670 (2016). · DOI
- Okada, N. et al. A positive feedback between p53 and miR-34 miRNAs mediates tumor suppression. Genes Dev. 28, 438–450 (2014). · DOI
- Bueno, M. J. & Malumbres, M. MicroRNAs and the cell cycle. Biochim. Biophys. Acta 1812, 592–601 (2011). · DOI
- Shimakami, T. et al. Stabilization of hepatitis C virus RNA by an Ago2–miR-122 complex. Proc. Natl Acad. Sci. USA 109, 941–946 (2012). · DOI
- Balasubramaniam, M., Pandhare, J. & Dash, C. Are microRNAs important players in HIV-1 infection? An update. Viruses 10, 110 (2018). · DOI
- Xu, S. J., Hu, H. T., Li, H. L. & Chang, S. The role of miRNAs in immune cell development, immune cell activation, and tumor immunity: with a focus on macrophages and natural killer cells. Cells 8, 1140 (2019). · DOI
- Wendt, A., Esguerra, J. L. & Eliasson, L. Islet microRNAs in health and type-2 diabetes. Curr. Opin. Pharmacol. 43, 46–52 (2018). · DOI
- Vienberg, S., Geiger, J., Madsen, S. & Dalgaard, L. T. MicroRNAs in metabolism. Acta Physiol. 219, 346–361 (2017). · DOI
- van Rooij, E., Liu, N. & Olson, E. N. MicroRNAs flex their muscles. Trends Genet. 24, 159–166 (2008). · DOI
- Chen, J.-F. et al. microRNA-1 and microRNA-206 regulate skeletal muscle satellite cell proliferation and differentiation by repressing Pax7. J. Cell Biol. 190, 867–879 (2010). · DOI
- Roberts, T. C. et al. Expression analysis in multiple muscle groups and serum reveals complexity in the microRNA transcriptome of the MDX mouse with implications for therapy. Mol. Ther. Nucleic Acids 1, e39 (2012).
- Cacchiarelli, D. et al. MicroRNAs involved in molecular circuitries relevant for the Duchenne muscular dystrophy pathogenesis are controlled by the dystrophin/nNOS pathway. Cell Metab. 12, 341–351 (2010). · DOI
- Provost, P. et al. Ribonuclease activity and RNA binding of recombinant human Dicer. EMBO J. 21, 5864–5874 (2002). · DOI
- Lee, Y. et al. The nuclear RNase III Drosha initiates microRNA processing. Nature 425, 415–419 (2003). · DOI
- Filipowicz, W., Bhattacharyya, S. N. & Sonenberg, N. Mechanisms of post-transcriptional regulation by microRNAs: are the answers in sight? Nat. Rev. Genet. 9, 102–114 (2008). · DOI
- Roberts, T. C. & Wood, M. J. A. Therapeutic targeting of non-coding RNAs. Essays Biochem. 54, 127–145 (2013). · DOI
- Lindow, M. & Kauppinen, S. Discovering the first microRNA-targeted drug. J. Cell Biol. 199, 407–412 (2012). · DOI
- Jopling, C. L., Yi, M., Lancaster, A. M., Lemon, S. M. & Sarnow, P. Modulation of hepatitis C virus RNA abundance by a liver-specific microRNA. Science 309, 1577–1581 (2005). · DOI
- Jopling, C. L., Schütz, S. & Sarnow, P. Position-dependent function for a tandem microRNA miR-122-binding site located in the hepatitis C virus RNA genome. Cell Host Microbe 4, 77–85 (2008). · DOI
- Jopling, C. L. Targeting microRNA-122 to treat hepatitis C virus infection. Viruses 2, 1382–1393 (2010). · DOI
- Janssen, H. L. A. et al. Treatment of HCV infection by targeting microRNA. N. Engl. J. Med. 368, 1685–1694 (2013). · DOI
- Machlin, E. S., Sarnow, P. & Sagan, S. M. Masking the 5′ terminal nucleotides of the hepatitis C virus genome by an unconventional microRNA–target RNA complex. Proc. Natl Acad. Sci. USA 108, 3193–3198 (2011). · DOI
- Ottosen, S. et al. In vitro antiviral activity and preclinical and clinical resistance profile of miravirsen, a novel anti-hepatitis C virus therapeutic targeting the human factor miR-122. Antimicrob. Agents Chemother. 59, 599–608 (2015). · DOI
- Gomez, I. G. et al. Anti-microRNA-21 oligonucleotides prevent Alport nephropathy progression by stimulating metabolic pathways. J. Clin. Invest. 125, 141–156 (2015). · DOI
- Seto, A. G. et al. Cobomarsen, an oligonucleotide inhibitor of miR-155, co-ordinately regulates multiple survival pathways to reduce cellular proliferation and survival in cutaneous T-cell lymphoma. Br. J. Haematol. 183, 428–444 (2018). · DOI
- Gallant-Behm, C. L. et al. A microRNA-29 mimic (remlarsen) represses extracellular matrix expression and fibroplasia in the skin. J. Invest. Dermatol. 139, 1073–1081 (2019). · DOI
- Choi, W.-Y., Giraldez, A. J. & Schier, A. F. Target protectors reveal dampening and balancing of Nodal agonist and antagonist by miR-430. Science 318, 271–274 (2007). · DOI
- Wang, Z. The principles of miRNA-masking antisense oligonucleotides technology. Methods Mol. Biol. 676, 43–49 (2011). · DOI
- Roberts, T. C., Morris, K. V. & Wood, M. J. A. The role of long non-coding RNAs in neurodevelopment, brain function and neurological disease. Philos. Trans. R. Soc. Lond. B Biol. Sci. 369, (2014). · DOI
- Wahlestedt, C. Targeting long non-coding RNA to therapeutically upregulate gene expression. Nat. Rev. Drug Discov. 12, 433–446 (2013). · DOI
- Yoon, S. & Rossi, J. J. Therapeutic potential of small activating RNAs (saRNAs) in human cancers. Curr. Pharm. Biotechnol. 19, 604–610 (2018). · DOI
- Modarresi, F. et al. Inhibition of natural antisense transcripts in vivo results in gene-specific transcriptional upregulation. Nat. Biotechnol. 30, 453–459 (2012). · DOI
- Meng, L. et al. Towards a therapy for Angelman syndrome by targeting a long non-coding RNA. Nature 518, 409–412 (2015). · DOI
- Hsiao, J. et al. Upregulation of haploinsufficient gene expression in the brain by targeting a long non-coding RNA improves seizure phenotype in a model of Dravet syndrome. EBioMedicine 9, 257–277 (2016). · DOI
- Schwartz, J. C. et al. Antisense transcripts are targets for activating small RNAs. Nat. Struct. Mol. Biol. 15, 842–848 (2008). · DOI
- Matsui, M. et al. Promoter RNA links transcriptional regulation of inflammatory pathway genes. Nucleic Acids Res. 41, 10086–10109 (2013). · DOI
- Turunen, T. A. et al. Changes in nuclear and cytoplasmic microRNA distribution in response to hypoxic stress. Sci. Rep. 9, 10332 (2019).
- Gagnon, K. T., Li, L., Chu, Y., Janowski, B. A. & Corey, D. R. RNAi factors are present and active in human cell nuclei. Cell Rep. 6, 211–221 (2014). · DOI · Paper page
- Voutila, J. et al. Development and mechanism of small activating RNA targeting CEBPA, a novel therapeutic in clinical trials for liver cancer. Mol. Ther. 25, 2705–2714 (2017). · DOI
- Reebye, V. et al. Gene activation of CEBPA using saRNA: preclinical studies of the first in human saRNA drug candidate for liver cancer. Oncogene 37, 3216–3228 (2018). · DOI
- Sarker, D. et al. MTL-CEBPA, a small activating RNA therapeutic up-regulating C/EBP-α, in patients with advanced liver cancer: a first-in-human, multi-centre, open-label, phase I trial. Clin. Cancer Res. https://doi.org/10.1158/1078-0432.CCR-20-0414 (2020). This paper presents the currently most advanced oligonucleotide therapy aimed at upregulating a target gene. · DOI
- Tsui, N. B. Y., Ng, E. K. O. & Lo, Y. M. D. Stability of endogenous and added RNA in blood specimens, serum, and plasma. Clin. Chem. 48, 1647–1653 (2002). · DOI
- Iversen, F. et al. Optimized siRNA–PEG conjugates for extended blood circulation and reduced urine excretion in mice. Theranostics 3, 201–209 (2013). · DOI
- Geary, R. S., Norris, D., Yu, R. & Bennett, C. F. Pharmacokinetics, biodistribution and cell uptake of antisense oligonucleotides. Adv. Drug Deliv. Rev. 87, 46–51 (2015). · DOI
- Shemesh, C. S. et al. Pharmacokinetic and pharmacodynamic investigations of ION-353382, a model antisense oligonucleotide: using α2-macroglobulin and murinoglobulin double-knockout mice. Nucleic Acid. Ther. 26, 223–235 (2016). · DOI
- Allen, T. M. The use of glycolipids and hydrophilic polymers in avoiding rapid uptake of liposomes by the mononuclear phagocyte system. Adv. Drug Delivery Rev. 13, 285–309 (1994). · DOI
- Sahay, G. et al. Efficiency of siRNA delivery by lipid nanoparticles is limited by endocytic recycling. Nat. Biotechnol. 31, 653–658 (2013). · DOI · Paper page
- Finkel, R. S. et al. Treatment of infantile-onset spinal muscular atrophy with nusinersen: a phase 2, open-label, dose-escalation study. Lancet 388, 3017–3026 (2016). This landmark study shows efficacy of an oligonucleotide therapy for spinal muscular atrophy. · DOI
- Wan, W. B. & Seth, P. P. The medicinal chemistry of therapeutic oligonucleotides. J. Med. Chem. 59, 9645–9667 (2016). · DOI
- Hung, G. et al. Characterization of target mRNA reduction through in situ RNA hybridization in multiple organ systems following systemic antisense treatment in animals. Nucleic Acid. Ther. 23, 369–378 (2013). · DOI
- Hall, A. H. S., Wan, J., Shaughnessy, E. E., Ramsay Shaw, B. & Alexander, K. A. RNA interference using boranophosphate siRNAs: structure–activity relationships. Nucleic Acids Res. 32, 5991–6000 (2004). · DOI
- Braasch, D. A. et al. RNA interference in mammalian cells by chemically-modified RNA. Biochemistry 42, 7967–7975 (2003). · DOI
- Bijsterbosch, M. K. et al. In vivo fate of phosphorothioate antisense oligodeoxynucleotides: predominant uptake by scavenger receptors on endothelial liver cells. Nucleic Acids Res. 25, 3290–3296 (1997). · DOI
- Ezzat, K. et al. Self-assembly into nanoparticles is essential for receptor mediated uptake of therapeutic antisense oligonucleotides. Nano Lett. 15, 4364–4373 (2015). · DOI
- Miller, C. M. et al. Stabilin-1 and Stabilin-2 are specific receptors for the cellular internalization of phosphorothioate-modified antisense oligonucleotides (ASOs) in the liver. Nucleic Acids Res. 44, 2782–2794 (2016). · DOI
- Gaus, H. J. et al. Characterization of the interactions of chemically-modified therapeutic nucleic acids with plasma proteins using a fluorescence polarization assay. Nucleic Acids Res. 47, 1110–1122 (2019). · DOI
- Brown, D. A. et al. Effect of phosphorothioate modification of oligodeoxynucleotides on specific protein binding. J. Biol. Chem. 269, 26801–26805 (1994). · DOI
- Liang, X., Sun, H., Shen, W. & Crooke, S. T. Identification and characterization of intracellular proteins that bind oligonucleotides with phosphorothioate linkages. Nucleic Acids Res. 43, 2927–2945 (2015). · DOI
- Weidner, D. A., Valdez, B. C., Henning, D., Greenberg, S. & Busch, H. Phosphorothioate oligonucleotides bind in a non sequence-specific manner to the nucleolar protein C23/nucleolin. FEBS Lett. 366, 146–150 (1995). · DOI
- Shen, W., Liang, X. & Crooke, S. T. Phosphorothioate oligonucleotides can displace NEAT1 RNA and form nuclear paraspeckle-like structures. Nucleic Acids Res. 42, 8648–8662 (2014). · DOI
- Liang, X., Shen, W., Sun, H., Prakash, T. P. & Crooke, S. T. TCP1 complex proteins interact with phosphorothioate oligonucleotides and can co-localize in oligonucleotide-induced nuclear bodies in mammalian cells. Nucleic Acids Res. 42, 7819–7832 (2014). · DOI
- Monia, B. P., Johnston, J. F., Sasmor, H. & Cummins, L. L. Nuclease resistance and antisense activity of modified oligonucleotides targeted to Ha-ras. J. Biol. Chem. 271, 14533–14540 (1996). · DOI
- Iwamoto, N. et al. Control of phosphorothioate stereochemistry substantially increases the efficacy of antisense oligonucleotides. Nat. Biotechnol. 35, 845–851 (2017). This study demonstrates the influence of phosphorothioate stereochemistry on the properties of gapmer ASOs. · DOI
- Wan, W. B. et al. Synthesis, biophysical properties and biological activity of second generation antisense oligonucleotides containing chiral phosphorothioate linkages. Nucleic Acids Res. 42, 13456–13468 (2014). · DOI
- Lee, H.-S. et al. Abasic pivot substitution harnesses target specificity of RNA interference. Nat. Commun. 6, 10154 (2015).
- Liu, J. et al. RNA duplexes with abasic substitutions are potent and allele-selective inhibitors of huntingtin and ataxin-3 expression. Nucleic Acids Res. 41, 8788–8801 (2013). · DOI
- Schirle, N. T. & MacRae, I. J. The crystal structure of human Argonaute2. Science 336, 1037–1040 (2012). · DOI
- Frank, F., Sonenberg, N. & Nagar, B. Structural basis for 5′-nucleotide base-specific recognition of guide RNA by human AGO2. Nature 465, 818–822 (2010). · DOI · Paper page
- Haraszti, R. A. et al. 5′-Vinylphosphonate improves tissue accumulation and efficacy of conjugated siRNAs in vivo. Nucleic Acids Res. 45, 7581–7592 (2017). · DOI
- Behlke, M. A. Chemical modification of siRNAs for in vivo use. Oligonucleotides 18, 305–319 (2008). · DOI
- Southwell, A. L., Skotte, N. H., Bennett, C. F. & Hayden, M. R. Antisense oligonucleotide therapeutics for inherited neurodegenerative diseases. Trends Mol. Med. 18, 634–643 (2012). · DOI
- Manoharan, M. 2′-Carbohydrate modifications in antisense oligonucleotide therapy: importance of conformation, configuration and conjugation. Biochim. Biophys. Acta 1489, 117–130 (1999). · DOI
- Roberts, T. C., Ezzat, K., El Andaloussi, S. & Weinberg, M. S. Synthetic siRNA delivery: progress and prospects. Methods Mol. Biol. 1364, 291–310 (2016). · DOI
- Prakash, T. P. et al. Positional effect of chemical modifications on short interference RNA activity in mammalian cells. J. Med. Chem. 48, 4247–4253 (2005). · DOI
- Allerson, C. R. et al. Fully 2′-modified oligonucleotide duplexes with improved in vitro potency and stability compared to unmodified small interfering RNA. J. Med. Chem. 48, 901–904 (2005). · DOI
- Hassler, M. R. et al. Comparison of partially and fully chemically-modified siRNA in conjugate-mediated delivery in vivo. Nucleic Acids Res. 46, 2185–2196 (2018). · DOI · Paper page
- Jackson, A. L. et al. Position-specific chemical modification of siRNAs reduces ‘off-target’ transcript silencing. RNA 12, 1197–1205 (2006). · DOI
- Garber, K. Alnylam terminates revusiran program, stock plunges. Nat. Biotechnol. 34, 1213–1214 (2016). · DOI
- Nair, J. K. et al. Impact of enhanced metabolic stability on pharmacokinetics and pharmacodynamics of GalNAc–siRNA conjugates. Nucleic Acids Res. 45, 10969–10977 (2017). · DOI · Paper page
- Judge, A. D. et al. Sequence-dependent stimulation of the mammalian innate immune response by synthetic siRNA. Nat. Biotechnol. 23, 457–462 (2005). · DOI
- Shen, W., Liang, X.-H., Sun, H. & Crooke, S. T. 2′-Fluoro-modified phosphorothioate oligonucleotide can cause rapid degradation of P54nrb and PSF. Nucleic Acids Res. 43, 4569–4578 (2015). · DOI
- Iwasaki, A. & Medzhitov, R. Toll-like receptor control of the adaptive immune responses. Nat. Immunol. 5, 987–995 (2004). · DOI
- Hornung, V. et al. Sequence-specific potent induction of IFN-α by short interfering RNA in plasmacytoid dendritic cells through TLR7. Nat. Med. 11, 263–270 (2005). · DOI
- Morrissey, D. V. et al. Potent and persistent in vivo anti-HBV activity of chemically modified siRNAs. Nat. Biotechnol. 23, 1002–1007 (2005). This landmark study demonstrates enhanced RNAi-mediated gene silencing using chemically modified siRNA in vivo. · DOI
- Judge, A. D., Bola, G., Lee, A. C. H. & MacLachlan, I. Design of noninflammatory synthetic siRNA mediating potent gene silencing in vivo. Mol. Ther. 13, 494–505 (2006). · DOI
- Poeck, H. et al. 5′-Triphosphate-siRNA: turning gene silencing and Rig-I activation against melanoma. Nat. Med. 14, 1256–1263 (2008). · DOI · Paper page
- Kortylewski, M. et al. In vivo delivery of siRNA to immune cells by conjugation to a TLR9 agonist enhances antitumor immune responses. Nat. Biotechnol. 27, 925–932 (2009). · DOI
- Kandimalla, E. R. et al. Design, synthesis and biological evaluation of novel antagonist compounds of Toll-like receptors 7, 8 and 9. Nucleic Acids Res. 41, 3947–3961 (2013). · DOI
- Veedu, R. N. & Wengel, J. Locked nucleic acid as a novel class of therapeutic agents. RNA Biol. 6, 321–323 (2009). · DOI
- Morita, K. et al. 2′-O,4′-C-ethylene-bridged nucleic acids (ENA): highly nuclease-resistant and thermodynamically stable oligonucleotides for antisense drug. Bioorg. Med. Chem. Lett. 12, 73–76 (2002). · DOI
- Koshkin, A. A. et al. LNA (locked nucleic acids): synthesis of the adenine, cytosine, guanine, 5-methylcytosine, thymine and uracil bicyclonucleoside monomers, oligomerisation, and unprecedented nucleic acid recognition. Tetrahedron 54, 3607–3630 (1998). · DOI
- Obad, S. et al. Silencing of microRNA families by seed-targeting tiny LNAs. Nat. Genet. 43, 371–378 (2011). · DOI
- Moulton, J. D. Using morpholinos to control gene expression. Curr. Protoc. Nucleic Acid. Chem. 68, 4.30.1–4.30.29 (2017). · DOI
- Iversen, P. L. Phosphorodiamidate morpholino oligomers: favorable properties for sequence-specific gene inactivation. Curr. Opin. Mol. Ther. 3, 235–238 (2001).
- Komaki, H. et al. Systemic administration of the antisense oligonucleotide NS-065/NCNP-01 for skipping of exon 53 in patients with Duchenne muscular dystrophy. Sci. Transl Med. 10, eaan0713 (2018). · DOI
- Larsen, H. J., Bentin, T. & Nielsen, P. E. Antisense properties of peptide nucleic acid. Biochim. Biophys. Acta 1489, 159–166 (1999). · DOI
- Saarbach, J., Sabale, P. M. & Winssinger, N. Peptide nucleic acid (PNA) and its applications in chemical biology, diagnostics, and therapeutics. Curr. Opin. Chem. Biol. 52, 112–124 (2019). · DOI
- Renneberg, D. & Leumann, C. J. Watson–Crick base-pairing properties of tricyclo-DNA. J. Am. Chem. Soc. 124, 5993–6002 (2002). · DOI
- Goyenvalle, A. et al. Functional correction in mouse models of muscular dystrophy using exon-skipping tricyclo-DNA oligomers. Nat. Med. 21, 270–275 (2015). · DOI
- Dowling, J. J. Eteplirsen therapy for Duchenne muscular dystrophy: skipping to the front of the line. Nat. Rev. Neurol. 12, 675–676 (2016). · DOI
- Yin, H. et al. Optimization of peptide nucleic acid antisense oligonucleotides for local and systemic dystrophin splice correction in the MDX mouse. Mol. Ther. 18, 819–827 (2010). · DOI
- Imbert, M., Blandel, F., Leumann, C., Garcia, L. & Goyenvalle, A. Lowering mutant huntingtin using tricyclo-DNA antisense oligonucleotides as a therapeutic approach for Huntington’s disease. Nucleic Acid. Ther. 29, 256–265 (2019). · DOI
- Meade, B. R. et al. Efficient delivery of RNAi prodrugs containing reversible charge-neutralizing phosphotriester backbone modifications. Nat. Biotechnol. 32, 1256–1261 (2014). · DOI
- Wolfrum, C. et al. Mechanisms and optimization of in vivo delivery of lipophilic siRNAs. Nat. Biotechnol. 25, 1149–1157 (2007). · DOI · Paper page
- Soutschek, J. et al. Therapeutic silencing of an endogenous gene by systemic administration of modified siRNAs. Nature 432, 173–178 (2004). · DOI
- Lorenz, C., Hadwiger, P., John, M., Vornlocher, H.-P. & Unverzagt, C. Steroid and lipid conjugates of siRNAs to enhance cellular uptake and gene silencing in liver cells. Bioorg. Med. Chem. Lett. 14, 4975–4977 (2004). · DOI
- Eguchi, A. et al. Efficient siRNA delivery into primary cells by a peptide transduction domain–dsRNA binding domain fusion protein. Nat. Biotechnol. 27, 567–571 (2009). · DOI
- Betts, C. et al. Pip6–PMO, a new generation of peptide–oligonucleotide conjugates with improved cardiac exon skipping activity for DMD treatment. Mol. Ther. Nucleic Acids 1, e38 (2012). · DOI
- Alam, Md. R. et al. Multivalent cyclic RGD conjugates for targeted delivery of small interfering RNA. Bioconjugate Chem. 22, 1673–1681 (2011). · DOI
- Ämmälä, C. et al. Targeted deliivery of antisense oligonucleotides to pancreatic β-cells. Sci. Adv. 4, eaat3386 (2018). · DOI
- Liu, X. et al. Tumor-targeted in vivo gene silencing via systemic delivery of cRGD-conjugated siRNA. Nucleic Acids Res. 42, 11805–11817 (2014). · DOI
- McNamara, J. O. et al. Cell type-specific delivery of siRNAs with aptamer–siRNA chimeras. Nat. Biotechnol. 24, 1005–1015 (2006). · DOI
- Song, E. et al. Antibody mediated in vivo delivery of small interfering RNAs via cell-surface receptors. Nat. Biotechnol. 23, 709–717 (2005). This paper demonstrates antibody–siRNA conjugates for gene silencing in mice. · DOI
- Matsuda, S. et al. siRNA conjugates carrying sequentially assembled trivalent N-acetylgalactosamine linked through nucleosides elicit robust gene silencing in vivo in hepatocytes. ACS Chem. Biol. 10, 1181–1187 (2015). · DOI
- Tai, W. Current aspects of siRNA bioconjugate for in vitro and in vivo delivery. Molecules 24, 2211 (2019). · DOI
- Juliano, R. L. The delivery of therapeutic oligonucleotides. Nucleic Acids Res. 44, 6518–6548 (2016). · DOI
- Khan, T. et al. Silencing myostatin using cholesterol-conjugated siRNAs induces muscle growth. Mol. Ther. Nucleic Acids 5, e342 (2016). · DOI
- Nishina, K. et al. Efficient in vivo delivery of siRNA to the liver by conjugation of α-tocopherol. Mol. Ther. 16, 734–740 (2008). · DOI
- Osborn, M. F. et al. Hydrophobicity drives the systemic distribution of lipid-conjugated siRNAs via lipid transport pathways. Nucleic Acids Res. 47, 1070–1081 (2019). · DOI
- Spiess, M. The asialoglycoprotein receptor: a model for endocytic transport receptors. Biochemistry 29, 10009–10018 (1990). · DOI
- Tanowitz, M. et al. Asialoglycoprotein receptor 1 mediates productive uptake of N-acetylgalactosamine-conjugated and unconjugated phosphorothioate antisense oligonucleotides into liver hepatocytes. Nucleic Acids Res. 45, 12388–12400 (2017). · DOI
- Prakash, T. P. et al. Targeted delivery of antisense oligonucleotides to hepatocytes using triantennary N-acetyl galactosamine improves potency 10-fold in mice. Nucleic Acids Res. 42, 8796–8807 (2014). · DOI
- Zimmermann, T. S. et al. Clinical proof of concept for a novel hepatocyte-targeting GalNAc–siRNA conjugate. Mol. Ther. 25, 71–78 (2017). · DOI
- Sardh, E. et al. Phase 1 trial of an RNA interference therapy for acute intermittent porphyria. N. Engl. J. Med. 380, 549–558 (2019). · DOI
- Hooper, A. J. & Burnett, J. R. Anti-PCSK9 therapies for the treatment of hypercholesterolemia. Expert Opin. Biol. Ther. 13, 429–435 (2013). · DOI
- Mousavi, S. A., Berge, K. E. & Leren, T. P. The unique role of proprotein convertase subtilisin/kexin 9 in cholesterol homeostasis. J. Intern. Med. 266, 507–519 (2009). · DOI
- Sievers, E. L. & Senter, P. D. Antibody–drug conjugates in cancer therapy. Annu. Rev. Med. 64, 15–29 (2013). · DOI
- Yao, Y. et al. Targeted delivery of PLK1–siRNA by ScFv suppresses Her2+ breast cancer growth and metastasis. Sci. Transl Med. 4, 130ra48 (2012).
- Kumar, P. et al. T cell-specific siRNA delivery suppresses HIV-1 infection in humanized mice. Cell 134, 577–586 (2008). · DOI
- Sugo, T. et al. Development of antibody–siRNA conjugate targeted to cardiac and skeletal muscles. J. Control. Rel. 237, 1–13 (2016). · DOI
- Cuellar, T. L. et al. Systematic evaluation of antibody-mediated siRNA delivery using an industrial platform of THIOMAB–siRNA conjugates. Nucleic Acids Res. 43, 1189–1203 (2015). · DOI
- Arnold, A. E. et al. Antibody–antisense oligonucleotide conjugate downregulates a key gene in glioblastoma stem cells. Mol. Ther. Nucleic Acids 11, 518–527 (2018). · DOI
- Astriab-Fisher, A., Fisher, M. H., Juliano, R. & Herdewijn, P. Increased uptake of antisense oligonucleotides by delivery as double stranded complexes. Biochem. Pharmacol. 68, 403–407 (2004). · DOI
- Nuzzo, S. et al. Potential and challenges of aptamers as specific carriers of therapeutic oligonucleotides for precision medicine in cancer. Cancers 11, 1521 (2019). · DOI
- Hong, S., Sun, N., Liu, M., Wang, J. & Pei, R. Building a chimera of aptamer–antisense oligonucleotide for silencing galectin-1 gene. RSC Adv. 6, 112445–112450 (2016). · DOI
- White, R. R., Sullenger, B. A. & Rusconi, C. P. Developing aptamers into therapeutics. J. Clin. Invest. 106, 929–934 (2000). · DOI
- McClorey, G. & Banerjee, S. Cell-penetrating peptides to enhance delivery of oligonucleotide-based therapeutics. Biomedicines 6, 51 (2018). · DOI
- Yin H. et al. Cell-penetrating peptide-conjugated antisense oligonucleotides restore systemic muscle and cardiac dystrophin expression and function. Hum. Mol. Genet. 17, 3909–3918 (2008). · DOI
- McClorey, G., Moulton, H. M., Iversen, P. L., Fletcher, S. & Wilton, S. D. Antisense oligonucleotide-induced exon skipping restores dystrophin expression in vitro in a canine model of DMD. Gene Ther. 13, 1373–1381 (2006). · DOI
- Wu, B. et al. Effective rescue of dystrophin improves cardiac function in dystrophin-deficient mice by a modified morpholino oligomer. Proc. Natl Acad. Sci. USA 105, 14814–14819 (2008). · DOI
- Abes, R. et al. Delivery of steric block morpholino oligomers by (R-X-R)4 peptides: structure–activity studies. Nucleic Acids Res. 36, 6343–6354 (2008). · DOI
- Wender, P. A. et al. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. Proc. Natl Acad. Sci. USA 97, 13003–13008 (2000). · DOI
- Yin, H. et al. A fusion peptide directs enhanced systemic dystrophin exon skipping and functional restoration in dystrophin-deficient mdx mice. Hum. Mol. Genet. 18, 4405–4414 (2009). · DOI
- Yin, H. et al. Context dependent effects of chimeric peptide morpholino conjugates contribute to dystrophin exon-skipping efficiency. Mol. Ther. Nucleic Acids 2, e124 (2013).
- Gao, X. et al. Effective dystrophin restoration by a novel muscle-homing peptide–morpholino conjugate in dystrophin-deficient MDX mice. Mol. Ther. 22, 1333–1341 (2014). · DOI
- Yin, H. et al. Pip5 transduction peptides direct high efficiency oligonucleotide-mediated dystrophin exon skipping in heart and phenotypic correction in MDX mice. Mol. Ther. 19, 1295–1303 (2011). · DOI
- van Westering, T. L. E. et al. Uniform sarcolemmal dystrophin expression is required to prevent extracellular microRNA release and improve dystrophic pathology. J. Cachexia Sarcopenia Muscle 11, 578–593 (2019). · DOI
- Gait, M. J. et al. Cell-penetrating peptide conjugates of steric blocking oligonucleotides as therapeutics for neuromuscular diseases from a historical perspective to current prospects of treatment. Nucleic Acid. Ther. 29, 1–12 (2019). · DOI
- Betts, C. A. et al. Prevention of exercised induced cardiomyopathy following Pip–PMO treatment in dystrophic mdx mice. Sci. Rep. 5, 8986 (2015).
- Hammond, S. M. et al. Systemic peptide-mediated oligonucleotide therapy improves long-term survival in spinal muscular atrophy. Proc. Natl Acad. Sci. USA 113, 10962–10967 (2016). · DOI
- Amantana, A. et al. Pharmacokinetics, biodistribution, stability and toxicity of a cell-penetrating peptide–morpholino oligomer conjugate. Bioconjug. Chem. 18, 1325–1331 (2007). · DOI
- Moulton, H. M. & Moulton, J. D. Morpholinos and their peptide conjugates: therapeutic promise and challenge for Duchenne muscular dystrophy. Biochim. Biophys. Acta 1798, 2296–2303 (2010). · DOI
- Lehto, T. et al. Cellular trafficking determines the exon skipping activity of Pip6a–PMO in MDX skeletal and cardiac muscle cells. Nucleic Acids Res. 42, 3207–3217 (2014). · DOI
- Abes, S. et al. Vectorization of morpholino oligomers by the (R-Ahx-R)4 peptide allows efficient splicing correction in the absence of endosomolytic agents. J. Control. Rel. 116, 304–313 (2006). · DOI
- Bestas, B. et al. Splice-correcting oligonucleotides restore BTK function in X-linked agammaglobulinemia model. J. Clin. Invest. 124, 4067–4081 (2014). · DOI
- Du, L. et al. Arginine-rich cell-penetrating peptide dramatically enhances AMO-mediated ATM aberrant splicing correction and enables delivery to brain and cerebellum. Hum. Mol. Genet. 20, 3151–3160 (2011). · DOI
- Geller, B. L. et al. Gene-silencing antisense oligomers inhibit acinetobacter growth in vitro and in vivo. J. Infect. Dis. 208, 1553–1560 (2013). · DOI
- Burrer, R. et al. Antiviral effects of antisense morpholino oligomers in murine coronavirus infection models. J. Virol. 81, 5637–5648 (2007). · DOI
- Neuman, B. W. et al. Inhibition and escape of SARS-CoV treated with antisense morpholino oligomers. Adv. Exp. Med. Biol. 581, 567–571 (2006). · DOI
- Enterlein, S. et al. VP35 knockdown inhibits Ebola virus amplification and protects against lethal infection in mice. Antimicrob. Agents Chemother. 50, 984–993 (2006). · DOI
- Moschos, S. A. et al. Lung delivery studies using siRNA conjugated to TAT(48–60) and penetratin reveal peptide induced reduction in gene expression and induction of innate immunity. Bioconjug. Chem. 18, 1450–1459 (2007). · DOI
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“Finally, emerging therapeutic modalities such as antisense oligonucleotides or siRNA could be developed to directly target and degrade PPP1R18 mRNA, thereby reducing its protein levels [64].”
Metadata
- Authors
- Roberts, T. C., Langer, R., & Wood, M. J. A.
- Venue
- Nature Reviews Drug Discovery
- Published
- 2020-08-11
- Volume
- 19
- Issue
- 10
- Pages
- 673-694
- ISSN
- 1474-1776
- 1474-1784
- PMC
- PMC7419031
- Cited by
- 2,027
- References
- 37
- Language
- en
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