Antisense Drugs Make Sense for Neurological Diseases

Staging of brain pathology related to sporadic Parkinson’s disease

Braak, H., Tredici, K. D., Rüb, U., de Vos, R. A. I., Jansen Steur, E. N. H., & Braak, E. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00065-9 · Cited by 10,777

Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy

Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359

Copper-Zinc Superoxide Dismutase (SOD1) Is Released by Microglial Cells and Confers Neuroprotection against 6-OHDA Neurotoxicity

Polazzi, E., Mengoni, I., Caprini, M., Peña‐Altamira, E., Kurtys, E., & Monti, B. (2012) · Neurosignals · doi:10.1159/000337115 · Cited by 9,023

A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes

MACDONALD, M. (1993) · Cell · doi:10.1016/0092-8674(93)90585-e · Cited by 8,366

Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis

Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062

Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576

A Paravascular Pathway Facilitates CSF Flow Through the Brain Parenchyma and the Clearance of Interstitial Solutes, Including Amyloid β

Iliff, J. J., Wang, M., Liao, Y., Plogg, B. A., Peng, W., Gundersen, G. A., Benveniste, H., Vates, G. E., Deane, R., Goldman, S. A., et al. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3003748 · Cited by 5,824 · cited 1×

Parkinson disease

Poewe, W., Seppi, K., Tanner, C. M., Halliday, G. M., Brundin, P., Volkmann, J., Schrag, A.-E., & Lang, A. E. (2017) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2017.13 · Cited by 5,415

Expanded GGGGCC Hexanucleotide Repeat in Noncoding Region of C9ORF72 Causes Chromosome 9p-Linked FTD and ALS

DeJesus-Hernandez, M., Mackenzie, I. R., Boeve, B. F., Boxer, A. L., Baker, M., Rutherford, N. J., Nicholson, A. M., Finch, N. A., Flynn, H., Adamson, J., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.011 · Cited by 4,936 · cited 9×

A Hexanucleotide Repeat Expansion in C9ORF72 Is the Cause of Chromosome 9p21-Linked ALS-FTD

Renton, A. E., Majounie, E., Waite, A., Simón-Sánchez, J., Rollinson, S., Gibbs, J. R., Schymick, J. C., Laaksovirta, H., van Swieten, J. C., Myllykangas, L., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.010 · Cited by 4,409

Motor Neuron Degeneration in Mice that Express a Human Cu,Zn Superoxide Dismutase Mutation

Gurney, M. E., Pu, H., Chiu, A. Y., Dal Canto, M. C., Polchow, C. Y., Alexander, D. D., Caliendo, J., Hentati, A., Kwon, Y. W., Deng, H.-X., et al. (1994) · Science · doi:10.1126/science.8209258 · Cited by 4,143

Identification and characterization of a spinal muscular atrophy-determining gene

Lefebvre, S., Bürglen, L., Reboullet, S., Clermont, O., Burlet, P., Viollet, L., Bénichou, B., Cruaud, C., Millasseau, P., Zeviani, M., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90460-3 · Cited by 3,995

Alzheimer Disease: An Update on Pathobiology and Treatment Strategies

Long, J. M., & Holtzman, D. M. (2019) · Cell · doi:10.1016/j.cell.2019.09.001 · Cited by 3,204

Patisiran, an RNAi Therapeutic, for Hereditary Transthyretin Amyloidosis

Adams, D., Gonzalez-Duarte, A., O’Riordan, W. D., Yang, C.-C., Ueda, M., Kristen, A. V., Tournev, I., Schmidt, H. H., Coelho, T., Berk, J. L., et al. (2018) · New England Journal of Medicine · doi:10.1056/nejmoa1716153 · Cited by 3,047

Amyotrophic Lateral Sclerosis

Brown, R. H., & Al‐Chalabi, A. (2017) · New England Journal of Medicine · doi:10.1056/nejmra1603471 · Cited by 2,580

Pathological α-Synuclein Transmission Initiates Parkinson-like Neurodegeneration in Nontransgenic Mice

Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · Science · doi:10.1126/science.1227157 · Cited by 2,563

Nusinersen versus Sham Control in Infantile-Onset Spinal Muscular Atrophy

Finkel, R. S., Mercuri, E., Darras, B. T., Connolly, A. M., Kuntz, N. L., Kirschner, J., Chiriboga, C. A., Saito, K., Servais, L., Tizzano, E., et al. (2017) · New England Journal of Medicine · doi:10.1056/nejmoa1702752 · Cited by 2,337

Decoding ALS: from genes to mechanism

Taylor, J. P., Brown, R. H., & Cleveland, D. W. (2016) · Nature · doi:10.1038/nature20413 · Cited by 2,120

The glymphatic system: a beginner's guide

Jessen, N. A., Munk, A. S. F., Lundgaard, I., & Nedergaard, M. (2015) · Neurochemical Research · doi:10.1007/s11064-015-1581-6 · Cited by 2,075

Reducing Endogenous Tau Ameliorates Amyloid ß-Induced Deficits in an Alzheimer's Disease Mouse Model

Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., Gerstein, H., Yu, G.-Q., & Mucke, L. (2007) · Science · doi:10.1126/science.1141736 · Cited by 1,892

Onset and Progression in Inherited ALS Determined by Motor Neurons and Microglia

Boillée, S., Yamanaka, K., Lobsiger, C. S., Copeland, N. G., Jenkins, N. A., Kassiotis, G., Kollias, G., & Cleveland, D. W. (2006) · Science · doi:10.1126/science.1123511 · Cited by 1,623

Inotersen Treatment for Patients with Hereditary Transthyretin Amyloidosis

Benson, M. D., Waddington‐Cruz, M., Berk, J. L., Polydefkis, M. J., Dyck, P. J. B., Wang, A. K., Planté‐Bordeneuve, V., Barroso, F. A., Merlini, G., Obici, L. P., et al. (2018) · New England Journal of Medicine · doi:10.1056/nejmoa1716793 · Cited by 1,483

Nusinersen versus Sham Control in Later-Onset Spinal Muscular Atrophy

Mercuri, E., Darras, B. T., Chiriboga, C. A., Day, J. W., Campbell, C., Connolly, A. M., Iannaccone, S. T., Kirschner, J., Kuntz, N. L., Saito, K., et al. (2018) · New England Journal of Medicine · doi:10.1056/nejmoa1710504 · Cited by 1,433

RNA Targeting Therapeutics: Molecular Mechanisms of Antisense Oligonucleotides as a Therapeutic Platform

Bennett, C. F., & Swayze, E. E. (2010) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.010909.105654 · Cited by 1,431

Trinucleotide Repeat Disorders

Orr, H. T., & Zoghbi, H. Y. (2007) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.29.051605.113042 · Cited by 1,394

Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS

Elden, A. C., Kim, H.-J., Hart, M. P., Chen‐Plotkin, A. S., Johnson, B. S., Fang, X., Armakola, M., Geser, F., Greene, R. A., Lu, M. M., et al. (2010) · Nature · doi:10.1038/nature09320 · Cited by 1,361

ALS-Linked SOD1 Mutant G85R Mediates Damage to Astrocytes and Promotes Rapidly Progressive Disease with SOD1-Containing Inclusions

Bruijn, L. I., Becher, M. W., Lee, M. K., Anderson, K. L., Jenkins, N. A., Copeland, N. G., Sisodia, S. S., Rothstein, J. D., Borchelt, D. R., Price, D. L., et al. (1997) · Neuron · doi:10.1016/s0896-6273(00)80272-x · Cited by 1,341

Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43

Polymenidou, M., Lagier-Tourenne, C., Hutt, K. R., Huelga, S. C., Moran, J., Liang, T. Y., Ling, S.-C., Sun, E., Wancewicz, E., Mazur, C., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2779 · Cited by 1,335

Aggregation and Motor Neuron Toxicity of an ALS-Linked SOD1 Mutant Independent from Wild-Type SOD1

Bruijn, L. I., Houseweart, M. K., Kato, S., Anderson, K. L., Anderson, S., Ohama, E., Reaume, A. G., Scott, R. W., & Cleveland, D. W. (1998) · Science · doi:10.1126/science.281.5384.1851 · Cited by 1,250

The C9orf72 GGGGCC Repeat Is Translated into Aggregating Dipeptide-Repeat Proteins in FTLD/ALS

Mori, K., Weng, S., Arzberger, T., May, S., Rentzsch, K., Kremmer, E., Schmid, B., Kretzschmar, H. A., Cruts, M., Broeckhoven, C. V., et al. (2013) · Science · doi:10.1126/science.1232927 · Cited by 1,248

UNRAVELING THE MECHANISMS INVOLVED IN MOTOR NEURON DEGENERATION IN ALS

Bruijn, L. I., Miller, T. M., & Cleveland, D. W. (2004) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.27.070203.144244 · Cited by 1,185

Correlation between severity and SMN protein level in spinal muscular atrophy

Lefebvre, S., Burlet, P., Liu, Q., Bertrandy, S., Clermont, O., Münnich, A., Dreyfuss, G., & Melki, J. (1997) · Nature Genetics · doi:10.1038/ng0797-265 · Cited by 1,100

Treatment of infantile-onset spinal muscular atrophy with nusinersen: a phase 2, open-label, dose-escalation study

Finkel, R. S., Chiriboga, C. A., Vajsar, J., Day, J., Montes, J., Vivo, D. C. D., Yamashita, M., Rigo, F., Hung, G., Schneider, E., et al. (2016) · The Lancet · doi:10.1016/s0140-6736(16)31408-8 · Cited by 1,039

MicroRNA-143 Regulates Adipocyte Differentiation

Esau, C., Kang, X., Peralta, E. R., Hanson, E. M., Marcusson, E. G., Ravichandran, L. V., Sun, Y., Koo, S., Perera, R. J., Jain, R., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400438200 · Cited by 1,023

The Biology of Huntingtin

Saudou, F., & Humbert, S. (2016) · Neuron · doi:10.1016/j.neuron.2016.02.003 · Cited by 945

RNA Toxicity from the ALS/FTD C9ORF72 Expansion Is Mitigated by Antisense Intervention

Donnelly, C. J., Zhang, P.-W., Pham, J. T., Haeusler, A. R., Mistry, N. A., Vidensky, S., Daley, E. L., Poth, E. M., Hoover, B., Fines, D. M., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.10.015 · Cited by 877

Patient-Customized Oligonucleotide Therapy for a Rare Genetic Disease

Kim, J., Hu, C., Achkar, C. M. E., Black, L. E., Douville, J., Larson, A. A., Pendergast, M. K., Goldkind, S. F., Lee, E. A., Kuniholm, A., et al. (2019) · New England Journal of Medicine · doi:10.1056/nejmoa1813279 · Cited by 852

Ribonuclease H: the enzymes in eukaryotes

Cerritelli, S. M., & Crouch, R. J. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.06908.x · Cited by 845

RNA-Targeted Therapeutics

Crooke, S. T., Witztum, J. L., Bennett, C. F., & Baker, B. F. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.03.004 · Cited by 841

Eteplirsen for the treatment of Duchenne muscular dystrophy

Mendell, J. R., Rodino‐Klapac, L. R., Sahenk, Z., Roush, K., Bird, L., Lowes, L. P., Alfano, L. N., Gomez, A. M., Lewis, S., Kota, J., et al. (2013) · Annals of Neurology · doi:10.1002/ana.23982 · Cited by 827

A new look at cerebrospinal fluid circulation

Brinker, T., Stopa, E., Morrison, J., & Klinge, P. (2014) · Fluids and Barriers of the CNS · doi:10.1186/2045-8118-11-10 · Cited by 819

Sustained Therapeutic Reversal of Huntington's Disease by Transient Repression of Huntingtin Synthesis

Kordasiewicz, H. B., Stanek, L. M., Wancewicz, E. V., Mazur, C., McAlonis, M. M., Pytel, K. A., Artates, J. W., Weiss, A., Cheng, S. H., Shihabuddin, L. S., et al. (2012) · Neuron · doi:10.1016/j.neuron.2012.05.009 · Cited by 770

Peripheral SMN restoration is essential for long-term rescue of a severe spinal muscular atrophy mouse model

Hua, Y., Sahashi, K., Rigo, F., Hung, G., Horev, G., Bennett, C. F., & Krainer, A. R. (2011) · Nature · doi:10.1038/nature10485 · Cited by 744

Targeting Huntingtin Expression in Patients with Huntington’s Disease

Tabrizi, S. J., Leavitt, B. R., Landwehrmeyer, G. B., Wild, E. J., Saft, C., Barker, R. A., Blair, N. F., Craufurd, D., Priller, J., Rickards, H., et al. (2019) · New England Journal of Medicine · doi:10.1056/nejmoa1900907 · Cited by 708

Stability and structural features of the duplexes containing nucleoside analogues with a fixed N-type conformation, 2′-O,4′-C-methyleneribonucleosides

Obika, S., Nanbu, D., Hari, Y., Andoh, J., Morio, K., Doi, T., & Imanishi, T. (1998) · Tetrahedron Letters · doi:10.1016/s0040-4039(98)01084-3 · Cited by 701

TDP-43 repression of nonconserved cryptic exons is compromised in ALS-FTD

Ling, J. P., Pletniková, O., Troncoso, J. C., & Wong, P. C. (2015) · Science · doi:10.1126/science.aab0983 · Cited by 697

The ups and downs of nucleic acid duplex stability: structure-stability studies on chemically-modified DNA:RNA duplexes

Freier, S. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.22.4429 · Cited by 697

Antisense correction of SMN2 splicing in the CNS rescues necrosis in a type III SMA mouse modelPreprint

Hua, Y., Sahashi, K., Hung, G., Rigo, F., Passini, M. A., Bennett, C. F., & Krainer, A. R. (2010) · Genes & Development · doi:10.1101/gad.1941310 · Cited by 680

Targeting RNA Foci in iPSC-Derived Motor Neurons from ALS Patients with a C9ORF72 Repeat Expansion

Sareen, D., O’Rourke, J. G., Meera, P., Muhammad, A. K. M. G., Grant, S., Simpkinson, M., Bell, S., Carmona, S., Ornelas, L., Sahabian, A., et al. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3007529 · Cited by 670

Nusinersen initiated in infants during the presymptomatic stage of spinal muscular atrophy: Interim efficacy and safety results from the Phase 2 NURTURE study

Vivo, D. C. D., Bertini, E., Swoboda, K. J., Hwu, W., Crawford, T. O., Finkel, R. S., Kirschner, J., Kuntz, N. L., Parsons, J. A., Ryan, M. M., et al. (2019) · Neuromuscular Disorders · doi:10.1016/j.nmd.2019.09.007 · Cited by 669

ALS-implicated protein TDP-43 sustains levels of STMN2, a mediator of motor neuron growth and repair

Klim, J. R., Williams, L. A., Limone, F., Guerra San Juan, I., Davis-Dusenbery, B. N., Mordes, D. A., Burberry, A., Steinbaugh, M. J., Gamage, K. K., Kirchner, R., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-018-0300-4 · Cited by 653

Premature polyadenylation-mediated loss of stathmin-2 is a hallmark of TDP-43-dependent neurodegeneration

Melamed, Z., López-Erauskin, J., Baughn, M. W., Zhang, O., Drenner, K., Sun, Y., Freyermuth, F., McMahon, M. A., Beccari, M. S., Artates, J. W., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-018-0293-z · Cited by 635

An antisense oligonucleotide against SOD1 delivered intrathecally for patients with SOD1 familial amyotrophic lateral sclerosis: a phase 1, randomised, first-in-man study

Miller, T. M., Pestronk, A., David, W., Rothstein, J., Simpson, E., Appel, S. H., Andres, P. L., Mahoney, K., Allred, P., Alexander, K., et al. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(13)70061-9 · Cited by 617

Results from a phase 1 study of nusinersen (ISIS-SMN Rx ) in children with spinal muscular atrophy

Chiriboga, C. A., Swoboda, K. J., Darras, B. T., Iannaccone, S. T., Montes, J., Vivo, D. C. D., Norris, D. A., Bennett, C. F., & Bishop, K. M. (2016) · Neurology · doi:10.1212/wnl.0000000000002445 · Cited by 613

Therapeutic Antisense Oligonucleotides Are Coming of Age

Bennett, C. F. (2019) · Annual Review of Medicine · doi:10.1146/annurev-med-041217-010829 · Cited by 609

TDP-43 pathology disrupts nuclear pore complexes and nucleocytoplasmic transport in ALS/FTD

Chou, C., Zhang, Y., Umoh, M. E., Vaughan, S. W., Lorenzini, I., Liu, F., Sayegh, M., Donlin-Asp, P., Chen, Y. H., Duong, D. M., et al. (2018) · Nature Neuroscience · doi:10.1038/s41593-017-0047-3 · Cited by 606

Antisense Masking of an hnRNP A1/A2 Intronic Splicing Silencer Corrects SMN2 Splicing in Transgenic Mice

Hua, Y., Vickers, T. A., Okunola, H. L., Bennett, C. F., & Krainer, A. R. (2008) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2008.01.014 · Cited by 591

Targeted degradation of sense and antisense C9orf72 RNA foci as therapy for ALS and frontotemporal degeneration

Lagier‐Tourenne, C., Baughn, M. W., Rigo, F., Sun, S., Liu, P., Li, H., Jiang, J., Watt, A. T., Chun, S. J., Katz, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1318835110 · Cited by 585

Therapeutic reduction of ataxin-2 extends lifespan and reduces pathology in TDP-43 mice

Becker, L. A., Huang, B., Bieri, G., Ma, R., Knowles, D. A., Jafar-Nejad, P., Messing, J., Kim, H. J., Soriano, A., Auburger, G., et al. (2017) · Nature · doi:10.1038/nature22038 · Cited by 571

Phase 1–2 Trial of Antisense Oligonucleotide Tofersen for SOD1 ALS

Miller, T., Cudkowicz, M., Shaw, P. J., Andersen, P. M., Atassi, N., Bucelli, R. C., Genge, A., Glass, J., Ladha, S., Ludolph, A. L., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2003715 · Cited by 565

Antisense Oligonucleotides Delivered to the Mouse CNS Ameliorate Symptoms of Severe Spinal Muscular Atrophy

Passini, M. A., Bu, J., Richards, A. M., Kinnecom, C., Sardi, S. P., Stanek, L. M., Hua, Y., Rigo, F., Matson, J. E., Hung, G., et al. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3001777 · Cited by 560

Towards a therapy for Angelman syndrome by targeting a long non-coding RNA

Meng, L., Ward, A. J., Chun, S. J., Bennett, C. F., Beaudet, A. L., & Rigo, F. (2014) · Nature · doi:10.1038/nature13975 · Cited by 537

Gain of toxicity from ALS/FTD-linked repeat expansions in C9ORF72 is alleviated by antisense oligonucleotides targeting GGGGCC-containing RNAs

Jiang, J., Zhu, Q., Gendron, T. F., Saberi, S., McAlonis-Downes, M., Seelman, A., Stauffer, J. E., Jafar-nejad, P., Drenner, K., Schulte, D., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.04.006 · Cited by 536

Epidemiology of mutations in superoxide dismutase in amyotrophic lateal sclerosis

Cudkowicz, M., McKenna‐Yasek, D., Sapp, P. C., Chin, W., Geller, B. A., Hayden, D. L., Schoenfeld, D., Hosler, B. A., Horvitz, H. R., & Brown, R. H. (1997) · Annals of Neurology · doi:10.1002/ana.410410212 · Cited by 533

Observational study of spinal muscular atrophy type I and implications for clinical trials

Finkel, R. S., McDermott, M., Kaufmann, P., Darras, B. T., Chung, W. K., Sproule, D. M., Kang, P. B., Foley, A. R., Yang, M. L., Martens, W. B., et al. (2014) · Neurology · doi:10.1212/wnl.0000000000000741 · Cited by 530

Target Protectors Reveal Dampening and Balancing of Nodal Agonist and Antagonist by miR-430

Choi, W.-Y., Giráldez, A. J., & Schier, A. F. (2007) · Science · doi:10.1126/science.1147535 · Cited by 517

Tau reduction prevents neuronal loss and reverses pathological tau deposition and seeding in mice with tauopathy

DeVos, S. L., Miller, R. L., Schoch, K. M., Holmes, B. B., Kebodeaux, C. S., Wegener, A. J., Chen, G., Shen, T., Tran, H., Nichols, B., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aag0481 · Cited by 516

Antisense oligonucleotide therapy for neurodegenerative disease

Smith, R. A. (2006) · Journal of Clinical Investigation · doi:10.1172/jci25424 · Cited by 506

Pharmacology of Antisense Drugs

Bennett, C. F., Baker, B. F., Pham, N. C., Swayze, E. E., & Geary, R. S. (2016) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104846 · Cited by 445

Inhibition of axonal growth by SNAP-25 antisense oligonucleotides in vitro and in vivo

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Givosiran: First Approval

Scott, L. J. (2020) · Drugs · doi:10.1007/s40265-020-01269-0 · Cited by 441

Restoration of correct splicing in thalassemic pre-mRNA by antisense oligonucleotides.

Domiński, Z., & Kole, R. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.18.8673 · Cited by 426

The C9orf72 protein interacts with Rab1a and the ULK1 complex to regulate initiation of autophagy

Webster, C. P., Smith, E. F., Bauer, C. S., Moller, A., Hautbergue, G. M., Ferraiuolo, L., Myszczynska, M. A., Higginbottom, A., Walsh, M. J., Whitworth, A. J., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201694401 · Cited by 404

Therapeutic developments for Duchenne muscular dystrophy

Verhaart, I. E. C., & Aartsma-Rus, A. M. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-019-0203-3 · Cited by 391

Phosphorothioate Oligodeoxynucleotides: What Is Their Origin and What Is Unique About Them?

Eckstein, F. (2000) · Antisense and Nucleic Acid Drug Development · doi:10.1089/oli.1.2000.10.117 · Cited by 383

Antisense oligodeoxynucleotides to NMDA-R1 receptor channel protect cortical neurons from excitotoxicity and reduce focal ischaemic infarctions

Wahlestedt, C., Golanov, E. V., Yamamoto, S., Yee, F., Ericson, H., Yoo, H., Inturrisi, C. E., & Reis, D. J. (1993) · Nature · doi:10.1038/363260a0 · Cited by 373

Spinocerebellar ataxia: an update

Sullivan, R., Yau, W. Y., O’Connor, E., & Houlden, H. (2018) · Journal of Neurology · doi:10.1007/s00415-018-9076-4 · Cited by 368

LNA (Locked Nucleic Acid): An RNA Mimic Forming Exceedingly Stable LNA:LNA Duplexes

Koshkin, A. A., Nielsen, P., Meldgaard, M., Rajwanshi, V. K., Singh, S. K., & Wengel, J. (1998) · Journal of the American Chemical Society · doi:10.1021/ja9822862 · Cited by 343

Increased dystrophin production with golodirsen in patients with Duchenne muscular dystrophy

Frank, D. E., Schnell, F. J., Akana, C., El-Husayni, S. H., Desjardins, C. A., Morgan, J. E., Charleston, J. S., Sardone, V., Domingos, J., Dickson, G., et al. (2020) · Neurology · doi:10.1212/wnl.0000000000009233 · Cited by 332

C9ORF72 poly(GA) aggregates sequester and impair HR23 and nucleocytoplasmic transport proteins

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Antisense oligonucleotide therapy for spinocerebellar ataxia type 2

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