Antisense Oligonucleotide Therapies for Neurodegenerative Diseases

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

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

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

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

A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group.

Shah, M. A., Datson, N. A., Srinidhi, L., Stanton, V. P., MacDonald, M. E., Allard, M. W., Youngman, S., Am, F., Mott, R., Draths, K., et al. (1993) · Cell · Cited by 3,055

Mechanisms of gene silencing by double-stranded RNA

Meister, G., & Tuschl, T. (2004) · Nature · doi:10.1038/nature02873 · Cited by 2,539

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

Amyotrophic lateral sclerosis

Hardiman, O. M., Al‐Chalabi, A., Chiò, A., Corr, E. M., Logroscino, G., Robberecht, W., Shaw, P. J., Simmons, Z., & van den Berg, L. H. (2017) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2017.71 · Cited by 2,237

miR-122 regulation of lipid metabolism revealed by in vivo antisense targeting

Esau, C., Davis, S., Murray, S. F., Yu, X. X., Pandey, S. K., Pear, M., Watts, L., Booten, S. L., Graham, M., McKay, R., et al. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.01.005 · Cited by 2,082

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

A single nucleotide in the SMN gene regulates splicing and is responsible for spinal muscular atrophy

Lorson, C. L., Hahnen, E., Androphy, E. J., & Wirth, B. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.11.6307 · Cited by 1,536

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 1,428

Propagation of Tau Pathology in a Model of Early Alzheimer's Disease

de Calignon, A., Polydoro, M., Suárez-Calvet, M., William, C., Adamowicz, D. H., Kopeikina, K. J., Pitstick, R., Sahara, N., Ashe, K. H., Carlson, G. A., et al. (2012) · Neuron · doi:10.1016/j.neuron.2011.11.033 · Cited by 1,427

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 1,353

Frequency of the C9orf72 hexanucleotide repeat expansion in patients with amyotrophic lateral sclerosis and frontotemporal dementia: a cross-sectional study

Majounie, E., Renton, A. E., Mok, K., Dopper, E. G., Waite, A., Rollinson, S., Chiò, A., Restagno, G., Nicolaou, N., Simon-Sanchez, J., et al. (2012) · The Lancet Neurology · doi:10.1016/s1474-4422(12)70043-1 · Cited by 1,210

RNA and Disease

Cooper, T. A., Wan, L., & Dreyfuss, G. (2009) · Cell · doi:10.1016/j.cell.2009.02.011 · Cited by 1,191

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

RNA therapeutics: beyond RNA interference and antisense oligonucleotides

Kole, R., Krainer, A. R., & Altman, S. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3625 · Cited by 1,152

Astrocytes as determinants of disease progression in inherited amyotrophic lateral sclerosis

Yamanaka, K., Chun, S. J., Boillee, S., Fujimori-Tonou, N., Yamashita, H., Gutmann, D. H., Takahashi, R., Misawa, H., & Cleveland, D. W. (2008) · Nature Neuroscience · doi:10.1038/nn2047 · Cited by 1,140

Unconventional Translation of C9ORF72 GGGGCC Expansion Generates Insoluble Polypeptides Specific to c9FTD/ALS

Ash, P. E. A., Bieniek, K. F., Gendron, T. F., Caulfield, T. R., Lin, W.-L., DeJesus‐Hernandez, M., van Blitterswijk, M., Jansen‐West, K. R., Paul, J. W., Rademakers, R., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.02.004 · Cited by 1,079

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

A single nucleotide difference that alters splicing patterns distinguishes the SMA gene SMN1 from the copy gene SMN2

Monani, U. R. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.7.1177 · Cited by 951

Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin

Cleveland, D. W., Hwo, S.-Y., & Kirschner, M. W. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90213-3 · Cited by 915

Non-ATG–initiated translation directed by microsatellite expansions

Zu, T., Gibbens, B. B., Doty, N. S., Gomes-Pereira, M., Huguet-Lachon, A., Stone, M. D., Margolis, J., Peterson, M., Markowski, T. W., Ingram, M. A. C., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1013343108 · Cited by 904

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

Pharmacokinetics, biodistribution and cell uptake of antisense oligonucleotides

Geary, R. S., Norris, D. A., Yu, R. Z., & Bennett, C. F. (2015) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.01.008 · Cited by 866

Molecular Mechanisms and Potential Therapeutical Targets in Huntington's Disease

Zuccato, C., Valenza, M., & Cattaneo, E. (2010) · Physiological Reviews · doi:10.1152/physrev.00041.2009 · Cited by 848

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

Neuronal activity enhances tau propagation and tau pathology in vivo

Wu, J. W., Hussaini, S. A., Bastille, I. M., Rodriguez, G. A., Mrejeru, A., Rilett, K., Sanders, D. W., Cook, C., Fu, H., Boonen, R. A. C. M., et al. (2016) · Nature Neuroscience · doi:10.1038/nn.4328 · Cited by 820

Increased apoptosis and early embryonic lethality in mice nullizygous for the Huntington's disease gene homologue

Zeitlin, S. O., Liu, J.-P., Chapman, D. L., Papaioannou, V. E., & Efstratiadis, A. (1995) · Nature Genetics · doi:10.1038/ng1095-155 · Cited by 807

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

C9orf72 repeat expansions cause neurodegeneration in Drosophila through arginine-rich proteins

Mizielinska, S., Grönke, S., Niccoli, T., Ridler, C. E., Clayton, E. L., Devoy, A., Moens, T., Norona, F. E., Woollacott, I. O. C., Pietrzyk, J., et al. (2014) · Science · doi:10.1126/science.1256800 · Cited by 740

Disruption of an SF2/ASF-dependent exonic splicing enhancer in SMN2 causes spinal muscular atrophy in the absence of SMN1

Cartegni, L., & Krainer, A. R. (2002) · Nature Genetics · doi:10.1038/ng854 · Cited by 730

Inactivation of the Mouse Huntington's Disease Gene Homolog Hdh

Duyao, M. P., Auerbach, A. B., Ryan, A., Persichetti, F., Barnes, G. T., McNeil, S. M., Ge, P., Vonsattel, J.-P., Gusella, J. F., Joyner, A. L., et al. (1995) · Science · doi:10.1126/science.7618107 · Cited by 723

C9orf72-mediated ALS and FTD: multiple pathways to disease

Balendra, R., & Isaacs, A. M. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0047-2 · Cited by 715

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

Clinical genetics of amyotrophic lateral sclerosis: what do we really know?

Andersen, P. M., & Al-Chalabi, A. (2011) · Nature Reviews Neurology · doi:10.1038/nrneurol.2011.150 · Cited by 687

RNA interference improves motor and neuropathological abnormalities in a Huntington's disease mouse model

Harper, S. Q., Staber, P. D., He, X., Eliason, S. L., Martins, I. H., Mao, Q., Yang, L., Kotin, R. M., Paulson, H. L., & Davidson, B. L. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501507102 · Cited by 682

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

Pan-ethnic carrier screening and prenatal diagnosis for spinal muscular atrophy: clinical laboratory analysis of >72 400 specimens

Sugarman, E. A., Nagan, N., Zhu, H., Akmaev, V. R., Zhou, Z., Rohlfs, E. M., Flynn, K., Hendrickson, B. C., Scholl, T., Sirko-Osadsa, D. A., et al. (2012) · European Journal of Human Genetics · doi:10.1038/ejhg.2011.134 · Cited by 661

Poly-dipeptides encoded by the C9orf72 repeats bind nucleoli, impede RNA biogenesis, and kill cells

Kwon, I., Xiang, S., Kato, M., Wu, L. C., Theodoropoulos, P., Wang, T., Kim, J., Yun, J., Xie, Y., & McKnight, S. L. (2014) · Science · doi:10.1126/science.1254917 · Cited by 656

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

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

Antisense transcripts of the expanded C9ORF72 hexanucleotide repeat form nuclear RNA foci and undergo repeat-associated non-ATG translation in c9FTD/ALS

Gendron, T. F., Bieniek, K. F., Zhang, Y., Jansen‐West, K. R., Ash, P. E. A., Caulfield, T. R., Daughrity, L. M., Dunmore, J., Castanedes‐Casey, M., Chew, J., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1192-8 · Cited by 569

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 559

C9orf72 is required for proper macrophage and microglial function in mice

O’Rourke, J. G., Bogdanik, L., Yáñez, A., Lall, D., Wolf, A. J., Muhammad, A. K. M. G., Ho, R., Carmona, S., Vit, J. P., Zarrow, J., et al. (2016) · Science · doi:10.1126/science.aaf1064 · Cited by 550

A negative element in SMN2 exon 7 inhibits splicing in spinal muscular atrophy

Kashima, T., & Manley, J. L. (2003) · Nature Genetics · doi:10.1038/ng1207 · Cited by 540

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

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

SMN2 splicing modifiers improve motor function and longevity in mice with spinal muscular atrophy

Naryshkin, N. A., Weetall, M., Dakka, A., Narasimhan, J., Zhao, X., Feng, Z., Ling, K. K. Y., Karp, G. M., Qi, H., Woll, M. G., et al. (2014) · Science · doi:10.1126/science.1250127 · Cited by 524 · cited 1×

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

C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal dementia, regulates endosomal trafficking

Farg, M. A., Sundaramoorthy, V., Sultana, J. M., Yang, S., Atkinson, R. A. K., Levina, V., Halloran, M. A., Gleeson, P. A., Blair, I. P., Soo, K. Y., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu068 · Cited by 478

Lentiviral-mediated silencing of SOD1 through RNA interference retards disease onset and progression in a mouse model of ALS

Raoul, C., Abbas‐Terki, T., Bensadoun, J., Guillot, S., Haase, G., Szulc, J., Henderson, C. E., & Aebischer, P. (2005) · Nature Medicine · doi:10.1038/nm1207 · Cited by 464

Splicing of a Critical Exon of Human Survival Motor Neuron Is Regulated by a Unique Silencer Element Located in the Last Intron

Singh, N. K., Singh, N. N., Androphy, E. J., & Singh, R. N. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.4.1333-1346.2006 · Cited by 452

Tau prion strains dictate patterns of cell pathology, progression rate, and regional vulnerability in vivo

Kaufman, S. K., Sanders, D. W., Thomas, T. L., Ruchinskas, A. J., Vaquer-Alicea, J., Sharma, A. M., Miller, T. M., & Diamond, M. I. (2016) · Neuron · doi:10.1016/j.neuron.2016.09.055 · Cited by 450

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 442

Therapeutic silencing of mutant huntingtin with siRNA attenuates striatal and cortical neuropathology and behavioral deficits

DiFiglia, M., Sena‐Esteves, M., Chase, K. O., Sapp, E., Pfister, E., Sass, M., Yoder, J., Reeves, P., Pandey, R. K., Rajeev, K. G., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708285104 · Cited by 432

SMN2 splice modulators enhance U1–pre-mRNA association and rescue SMA mice

Palacino, J., Swalley, S. E., Song, C., Cheung, A. K., Shu, L., Zhang, X., Van Hoosear, M., Shin, Y., Chin, D. N., Keller, C. G., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1837 · Cited by 432

Targeting protein aggregation for the treatment of degenerative diseases

Eisele, Y. S., Monteiro, C., Fearns, C., Encalada, S. E., Wiseman, R. L., Powers, E. T., & Kelly, J. W. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4593 · Cited by 426

Molecular Mechanisms of Antisense Oligonucleotides

Crooke, S. T. (2017) · Nucleic Acid Therapeutics · doi:10.1089/nat.2016.0656 · Cited by 415

Quantitative Analysis of Survival Motor Neuron Copies: Identification of Subtle SMN1 Mutations in Patients with Spinal Muscular Atrophy, Genotype-Phenotype Correlation, and Implications for Genetic Counseling

Wirth, B., Herz, M., Wetter, A., Moskau, S., Hahnen, E., Rudnik‐Schöneborn, S., Wienker, T. F., & Zerres, K. (1999) · The American Journal of Human Genetics · doi:10.1086/302369 · Cited by 368

Mildly affected patients with spinal muscular atrophy are partially protected by an increased SMN2 copy number

Wirth, B., Brichta, L., Schrank, B., Lochmüller, H., Blick, S., Baasner, A.-L., & Heller, R. (2006) · Human Genetics · doi:10.1007/s00439-006-0156-7 · Cited by 355

Nonallele-specific Silencing of Mutant and Wild-type Huntingtin Demonstrates Therapeutic Efficacy in Huntington's Disease Mice

Boudreau, R. L., McBride, J. L., Martins, I., Shen, S., Xing, Y., Carter, B. J., & Davidson, B. L. (2009) · Molecular Therapy · doi:10.1038/mt.2009.17 · Cited by 340

Enhancement of SMN2 Exon 7 Inclusion by Antisense Oligonucleotides Targeting the Exon

Hua, Y., Vickers, T. A., Baker, B. F., Bennett, C. F., & Krainer, A. R. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050073 · Cited by 340

A Positive Modifier of Spinal Muscular Atrophy in the SMN2 Gene

Prior, T. W., Krainer, A. R., Hua, Y., Swoboda, K. J., Snyder, P. C., Bridgeman, S. J., Burghes, A. H. M., & Kissel, J. T. (2009) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2009.08.002 · Cited by 321

The product of C9orf72, a gene strongly implicated in neurodegeneration, is structurally related to DENN Rab-GEFs

Levine, T. P., Daniels, R. D., Gatta, A. T., Wong, L. H., & Hayes, M. J. (2013) · Bioinformatics · doi:10.1093/bioinformatics/bts725 · Cited by 321

Antisense oligonucleotide therapy for spinocerebellar ataxia type 2

Scoles, D. R., Meera, P., Schneider, M. D., Paul, S., Dansithong, W., Figueroa, K. P., Hung, G., Rigo, F., Bennett, C. F., Otis, T. S., et al. (2017) · Nature · doi:10.1038/nature22044 · Cited by 319

Longitudinal cognitive and biomarker changes in dominantly inherited Alzheimer disease

McDade, E., Wang, G., Gordon, B. A., Hassenstab, J., Benzinger, T. L. S., Buckles, V., Fagan, A. M., Holtzman, D. M., Cairns, N. J., Goate, A. M., et al. (2018) · Neurology · doi:10.1212/wnl.0000000000006277 · Cited by 314

Antisense Reduction of Tau in Adult Mice Protects against Seizures

DeVos, S. L., Goncharoff, D. K., Chen, G., Kebodeaux, C. S., Yamada, K., Stewart, F. R., Schuler, D. R., Maloney, S. E., Wozniak, D. F., Rigo, F., et al. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.2107-13.2013 · Cited by 311

Determinants of Exon 7 Splicing in the Spinal Muscular Atrophy Genes, SMN1 and SMN2

Cartegni, L., Hastings, M. L., Calarco, J. A., de Stanchina, E., & Krainer, A. R. (2005) · The American Journal of Human Genetics · doi:10.1086/498853 · Cited by 302

Correction of disease-associated exon skipping by synthetic exon-specific activators

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Potent and Selective Antisense Oligonucleotides Targeting Single-Nucleotide Polymorphisms in the Huntington Disease Gene / Allele-Specific Silencing of Mutant Huntingtin

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