C9orf72-mediated ALS and FTD: multiple pathways to disease

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

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

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Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice

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Loss of autophagy in the central nervous system causes neurodegeneration in mice

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Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse

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A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation

Patel, A., Lee, H. O., Jawerth, L. M., Maharana, S., Jahnel, M., Hein, M. Y., Stoynov, S., Mahamid, J., Saha, S., Franzmann, T. M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.047 · Cited by 2,927

TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

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Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological Fibrillization

Molliex, A., Temirov, J. P., Lee, J., Coughlin, M., Kanagaraj, A., Kim, H. J., Mittag, T., & Taylor, J. P. (2015) · Cell · doi:10.1016/j.cell.2015.09.015 · Cited by 2,690

Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis

Ling, S.-C., Polymenidou, M., & Cleveland, D. W. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.033 · Cited by 1,811

State of play in amyotrophic lateral sclerosis genetics

Renton, A. E., Chiò, A., & Traynor, B. J. (2013) · Nature Neuroscience · doi:10.1038/nn.3584 · Cited by 1,626

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

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

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

Kinesin Transports RNA

Kanai, Y., Dohmae, N., & Hirokawa, N. (2004) · Neuron · doi:10.1016/j.neuron.2004.07.022 · Cited by 1,109

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

TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration

Lagier-Tourenne, C., Polymenidou, M., & Cleveland, D. W. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq137 · Cited by 1,021

The C9orf72 repeat expansion disrupts nucleocytoplasmic transport.

Zhang, K., Donnelly, C. J., Haeusler, A. R., Grima, J. C., Machamer, J. B., Steinwald, P., Daley, E. L., Miller, S. J., Cunningham, K. M., Vidensky, S., et al. (2015) · Nature · doi:10.1038/nature14973 · Cited by 982

C9orf72 nucleotide repeat structures initiate molecular cascades of disease

Haeusler, A. R., Donnelly, C. J., Periz, G., Simko, E. A. J., Shaw, P. G., Kim, M.-S., Maragakis, N. J., Troncoso, J. C., Pandey, A., Sattler, R., et al. (2014) · Nature · doi:10.1038/nature13124 · Cited by 978

The changing scene of amyotrophic lateral sclerosis

Robberecht, W., & Philips, T. (2013) · Nature Reviews Neuroscience · doi:10.1038/nrn3430 · Cited by 957

RNA phase transitions in repeat expansion disorders

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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

ALS/FTD Mutation-Induced Phase Transition of FUS Liquid Droplets and Reversible Hydrogels into Irreversible Hydrogels Impairs RNP Granule Function

Murakami, T., Qamar, S., Lin, J. Q., Schierle, G. S. K., Rees, E. J., Miyashita, A., Costa, A. R., Dodd, R. B., Chan, F. T. S., Michel, C. H., et al. (2015) · Neuron · doi:10.1016/j.neuron.2015.10.030 · Cited by 872

GGGGCC repeat expansion in C9orf72 compromises nucleocytoplasmic transport

Freibaum, B. D., Lu, Y., Lopez-Gonzalez, R., Kim, N. C., Almeida, S., Lee, K.-H., Badders, N., Valentine, M., Miller, B. L., Wong, P. C., et al. (2015) · Nature · doi:10.1038/nature14974 · Cited by 841

Haploinsufficiency of TBK1 causes familial ALS and fronto-temporal dementia

Freischmidt, A., Wieland, T., Richter, B., Ruf, W., Schaeffer, V., Müller, K., Marroquin, N., Nordin, F., Hübers, A., Weydt, P., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4000 · Cited by 786

RAN proteins and RNA foci from antisense transcripts in C9ORF72 ALS and frontotemporal dementia

Zu, T., Liu, Y., Báñez-Coronel, M., Reid, T. S., Pletniková, O., Lewis, J. M., Miller, T. M., Harms, M. B., Falchook, A. E., Subramony, S. H., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1315438110 · Cited by 777

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

C9orf72 Dipeptide Repeats Impair the Assembly, Dynamics, and Function of Membrane-Less Organelles

Lee, K., Zhang, P., Kim, H. J., Mitrea, D. M., Sarkar, M., Freibaum, B. D., Cika, J., Coughlin, M., Messing, J., Molliex, A., et al. (2016) · Cell · doi:10.1016/j.cell.2016.10.002 · Cited by 691

Intrinsic Membrane Hyperexcitability of Amyotrophic Lateral Sclerosis Patient-Derived Motor Neurons

Wainger, B. J., Kiskinis, E., Mellin, C., Wiskow, O., Han, S. S. W., Sandoe, J., Perez, N. P., Williams, L. A., Lee, S., Boulting, G. L., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.03.019 · Cited by 676

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

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

A C9orf72 promoter repeat expansion in a Flanders-Belgian cohort with disorders of the frontotemporal lobar degeneration-amyotrophic lateral sclerosis spectrum: a gene identification study

Gijselinck, I., Langenhove, T. V., van der Zee, J., Sleegers, K., Philtjens, S., Kleinberger, G., Janssens, J., Bettens, K., Cauwenberghe, C. V., Pereson, S., et al. (2011) · The Lancet Neurology · doi:10.1016/s1474-4422(11)70261-7 · Cited by 655

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

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

Modifiers of C9orf72 dipeptide repeat toxicity connect nucleocytoplasmic transport defects to FTD/ALS

Jovičić, A., Mertens, J., Boeynaems, S., Bogaert, E., Chai, N., Yamada, S. B., Paul, J. W., Sun, S., Herdy, J. R., Bieri, G., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4085 · Cited by 598

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

Haploinsufficiency leads to neurodegeneration in C9ORF72 ALS/FTD human induced motor neurons

Shi, Y., Lin, S., Staats, K. A., Li, Y., Chang, W.-H., Hung, S.-T., Hendricks, E., Linares, G. R., Wang, Y., Son, E. Y., et al. (2018) · Nature Medicine · doi:10.1038/nm.4490 · Cited by 566

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

Effects of α-Synuclein Immunization in a Mouse Model of Parkinson’s Disease

Masliah, E., Rockenstein, E., Adame, A., Alford, M., Crews, L., Hashimoto, M., Seubert, P., Lee, M., Goldstein, J., Chilcote, T., et al. (2005) · Neuron · doi:10.1016/j.neuron.2005.05.010 · Cited by 542

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

Antisense Proline-Arginine RAN Dipeptides Linked to C9ORF72-ALS/FTD Form Toxic Nuclear Aggregates that Initiate In Vitro and In Vivo Neuronal Death

Wen, X., Tan, W., Westergard, T., Krishnamurthy, K., Markandaiah, S. S., Shi, Y., Lin, S., Shneider, N. A., Monaghan, J., Pandey, U. B., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.12.010 · Cited by 533

Immunotherapy Targeting Pathological Tau Conformers in a Tangle Mouse Model Reduces Brain Pathology with Associated Functional Improvements

Asuni, A. A., Boutajangout, A., Quartermain, D., & Sigurdsson, E. M. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.2361-07.2007 · Cited by 506

Phase Separation of C9orf72 Dipeptide Repeats Perturbs Stress Granule Dynamics

Boeynaems, S., Bogaert, E., Kovács, D., Konijnenberg, A., Timmerman, E., Volkov, A. N., Guharoy, M., Decker, M. D., Jaspers, T., Ryan, V. H., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.02.013 · Cited by 502

Hexanucleotide Repeats in ALS/FTD Form Length-Dependent RNA Foci, Sequester RNA Binding Proteins, and Are Neurotoxic

Lee, Y., Chen, H.-J., Peres, J., Gómez-Deza, J., Attig, J., Štalekar, M., Troakes, C., Nishimura, A. L., Scotter, E. L., Vance, C. A., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.10.049 · Cited by 487

Bidirectional transcripts of the expanded C9orf72 hexanucleotide repeat are translated into aggregating dipeptide repeat proteins

Mori, K., Arzberger, T., Grässer, F. A., Gijselinck, I., May, S., Rentzsch, K., Weng, S., Schludi, M. H., van der Zee, J., Cruts, M., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1189-3 · Cited by 482

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

Frontotemporal dementia with the C9ORF72 hexanucleotide repeat expansion: clinical, neuroanatomical and neuropathological features

Mahoney, C., Beck, J. A., Rohrer, J. D., Lashley, T., Mok, K. Y., Shakespeare, T. J., Yeatman, T., Warrington, E. K., Schott, J. M., Fox, N. C., et al. (2012) · Brain · doi:10.1093/brain/awr361 · Cited by 452

Poly(GR) in C9ORF72 -Related ALS/FTD Compromises Mitochondrial Function and Increases Oxidative Stress and DNA Damage in iPSC-Derived Motor Neurons

Lopez-Gonzalez, R., Lu, Y., Gendron, T. F., Karydas, A., Tran, H., Yang, D., Petrucelli, L., Miller, B. L., Almeida, S., & Gao, F. (2016) · Neuron · doi:10.1016/j.neuron.2016.09.015 · Cited by 429

C9ORF72 repeat expansions in mice cause TDP-43 pathology, neuronal loss, and behavioral deficits

Chew, J., Gendron, T. F., Prudencio, M., Sasaguri, H., Zhang, Y., Castanedes‐Casey, M., Lee, C. W., Jansen‐West, K. R., Kurti, A., Murray, M. E., et al. (2015) · Science · doi:10.1126/science.aaa9344 · Cited by 426

Toxic PR Poly-Dipeptides Encoded by the C9orf72 Repeat Expansion Target LC Domain Polymers

Lin, Y., Mori, E., Kato, M., Xiang, S., Wu, L. C., Kwon, I., & McKnight, S. L. (2016) · Cell · doi:10.1016/j.cell.2016.10.003 · Cited by 423

Stress Granule Assembly Disrupts Nucleocytoplasmic Transport

Zhang, K., Daigle, J. G., Cunningham, K. M., Coyne, A. N., Ruan, K., Grima, J. C., Bowen, K., Wadhwa, H., Yang, P., Rigo, F., et al. (2018) · Cell · doi:10.1016/j.cell.2018.03.025 · Cited by 420

Loss of C9ORF72 impairs autophagy and synergizes with polyQ Ataxin‐2 to induce motor neuron dysfunction and cell death

Sellier, C., Campanari, M., Julie Corbier, C., Gaucherot, A., Kolb‐Cheynel, I., Oulad‐Abdelghani, M., Ruffenach, F., Page, A., Ciura, S., Kabashi, E., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593350 · Cited by 414

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

In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment

Guo, Q., Lehmer, C., Martínez-Sánchez, A., Rudack, T., Beck, F., Hartmann, H., Pérez‐Berlanga, M., Frottin, F., Hipp, M. S., Hartl, F. U., et al. (2018) · Cell · doi:10.1016/j.cell.2017.12.030 · Cited by 404

Distinct brain transcriptome profiles in C9orf72-associated and sporadic ALS

Prudencio, M., Belzil, V., Batra, R., Ross, C. A., Gendron, T. F., Pregent, L., Murray, M. E., Overstreet, K., Johnston, A., Desaro, P., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4065 · Cited by 396

C9orf72 BAC Mouse Model with Motor Deficits and Neurodegenerative Features of ALS/FTD

Liu, Y., Pattamatta, A., Zu, T., Reid, T. S., Bardhi, O., Borchelt, D., Yachnis, A. T., & Ranum, L. P. W. (2016) · Neuron · doi:10.1016/j.neuron.2016.04.005 · Cited by 368

Discovery of a Biomarker and Lead Small Molecules to Target r(GGGGCC)-Associated Defects in c9FTD/ALS

Su, Z., Zhang, Y., Gendron, T. F., Bauer, P. O., Chew, J., Yang, W.-Y., Fostvedt, E., Jansen‐West, K. R., Belzil, V., Desaro, P., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.07.041 · Cited by 365

hnRNP A3 binds to GGGGCC repeats and is a constituent of p62-positive/TDP43-negative inclusions in the hippocampus of patients with C9orf72 mutations

Mori, K., Lammich, S., Mackenzie, I. R., Forné, I., Zilow, S., Kretzschmar, H. A., Edbauer, D., Janssens, J., Kleinberger, G., Cruts, M., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1088-7 · Cited by 348

Aggregation-prone c9FTD/ALS poly(GA) RAN-translated proteins cause neurotoxicity by inducing ER stress

Zhang, Y., Jansen‐West, K. R., Xu, Y.-F., Gendron, T. F., Bieniek, K. F., Lin, W.-L., Sasaguri, H., Caulfield, T. R., Hubbard, J., Daughrity, L. M., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1336-5 · Cited by 346

Large C9orf72 Hexanucleotide Repeat Expansions Are Seen in Multiple Neurodegenerative Syndromes and Are More Frequent Than Expected in the UK Population

Beck, J., Poulter, M., Hensman, D., Rohrer, J. D., Mahoney, C. J., Adamson, G., Campbell, T., Uphill, J., Borg, A., Fratta, P., et al. (2013) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2013.01.011 · Cited by 345

Dipeptide repeat protein pathology in C9ORF72 mutation cases: clinico-pathological correlations

Mackenzie, I. R., Arzberger, T., Kremmer, E., Troost, D., Lorenzl, S., Mori, K., Weng, S.-M., Haass, C., Kretzschmar, H. A., Edbauer, D., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1181-y · Cited by 345

C9orf72 hexanucleotide repeat associated with amyotrophic lateral sclerosis and frontotemporal dementia forms RNA G-quadruplexes

Fratta, P., Mizielinska, S., Nicoll, A. J., Zloh, M., Fisher, E., Parkinson, G. N., & Isaacs, A. M. (2012) · Scientific Reports · doi:10.1038/srep01016 · Cited by 345

Sequestration of multiple RNA recognition motif-containing proteins by C9orf72 repeat expansions

Cooper‐Knock, J., Walsh, M. J., Higginbottom, A., Highley, J. R., Dickman, M. J., Edbauer, D., Ince, P. G., Wharton, S. B., Wilson, S. A., Kirby, J., et al. (2014) · Brain · doi:10.1093/brain/awu120 · Cited by 335

Expanded GGGGCC repeat RNA associated with amyotrophic lateral sclerosis and frontotemporal dementia causes neurodegeneration

Xu, Z., Poidevin, M., Li, X., Li, Y., Shu, L., Nelson, D. L., Li, H., Hales, C. M., Gearing, M., Wingo, T. S., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1219643110 · Cited by 334

Loss of function of C9orf72 causes motor deficits in a zebrafish model of amyotrophic lateral sclerosis

Ciura, S., Lattante, S., Le Ber, I., Latouche, M., Tostivint, H., Brice, A., & Kabashi, E. (2013) · Annals of Neurology · doi:10.1002/ana.23946 · Cited by 333

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

Zhang, Y., Gendron, T. F., Grima, J. C., Sasaguri, H., Jansen‐West, K. R., Xu, Y.-F., Katzman, R. B., Gass, J. M., Murray, M. E., Shinohara, M., et al. (2016) · Nature Neuroscience · doi:10.1038/nn.4272 · Cited by 324

Modeling key pathological features of frontotemporal dementia with C9ORF72 repeat expansion in iPSC-derived human neurons

Almeida, S., Gascon, E., Tran, H., Chou, H. J., Gendron, T. F., DeGroot, S., Tapper, A. R., Sellier, C., Charlet-Berguerand, N., Karydas, A., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1149-y · 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

The Disease-associated r(GGGGCC) Repeat from the C9orf72 Gene Forms Tract Length-dependent Uni- and Multimolecular RNA G-quadruplex Structures

Reddy, K., Zamiri, B., Stanley, S. Y., Macgregor, R. B., & Pearson, C. E. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.c113.452532 · Cited by 318

C9orf72 frontotemporal lobar degeneration is characterised by frequent neuronal sense and antisense RNA foci

Mizielinska, S., Lashley, T., Norona, F. E., Clayton, E. L., Ridler, C. E., Fratta, P., & Isaacs, A. M. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1200-z · Cited by 317

C9orf72 FTLD/ALS-associated Gly-Ala dipeptide repeat proteins cause neuronal toxicity and Unc119 sequestration

May, S., Hornburg, D., Schludi, M. H., Arzberger, T., Rentzsch, K., Schwenk, B. M., Grässer, F. A., Mori, K., Kremmer, E., Banzhaf‐Strathmann, J., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1329-4 · Cited by 317

A Small Molecule Screen in Stem-Cell-Derived Motor Neurons Identifies a Kinase Inhibitor as a Candidate Therapeutic for ALS

Yang, Y. M., Gupta, S. K., Kim, K. J., Powers, B. E., Cerqueira, A., Wainger, B. J., Ngo, H. D., Rosowski, K. A., Schein, P. A., Ackeifi, C. A., et al. (2013) · Cell stem cell · doi:10.1016/j.stem.2013.04.003 · Cited by 312

Reduced C9orf72 gene expression in c9FTD/ALS is caused by histone trimethylation, an epigenetic event detectable in blood

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Human iPSC-derived motoneurons harbouring TARDBP or C9ORF72 ALS mutations are dysfunctional despite maintaining viability

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Passive immunization targeting pathological phospho‐tau protein in a mouse model reduces functional decline and clears tau aggregates from the brain

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C 9orf72 ablation in mice does not cause motor neuron degeneration or motor deficits

Koppers, M., Blokhuis, A. M., Westeneng, H., Terpstra, M. L., Zundel, C. A. C., de Sá, R. V., Schellevis, R. D., Waite, A. J., Blake, D. J., Veldink, J. H., et al. (2015) · Annals of Neurology · doi:10.1002/ana.24453 · Cited by 301

Clinical and neuropathologic heterogeneity of c9FTD/ALS associated with hexanucleotide repeat expansion in C9ORF72

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Reduced C9orf72 protein levels in frontal cortex of amyotrophic lateral sclerosis and frontotemporal degeneration brain with the C9ORF72 hexanucleotide repeat expansion

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C9orf72 BAC Transgenic Mice Display Typical Pathologic Features of ALS/FTD

O’Rourke, J. G., Bogdanik, L., Muhammad, A. K. M. G., Gendron, T. F., Kim, K. J., Austin, A., Cady, J., Liu, E. Y., Zarrow, J., Grant, S., et al. (2015) · Neuron · doi:10.1016/j.neuron.2015.10.027 · Cited by 298

The ALS/FTLD associated protein C9orf72 associates with SMCR8 and WDR41 to regulate the autophagy-lysosome pathway

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Hypermethylation of the CpG Island Near the G4C2 Repeat in ALS with a C9orf72 Expansion

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Human C9ORF72 Hexanucleotide Expansion Reproduces RNA Foci and Dipeptide Repeat Proteins but Not Neurodegeneration in BAC Transgenic Mice

Peters, O. M., Cabrera, G. T., Tran, H., Gendron, T. F., McKeon, J. E., Metterville, J., Weiss, A., Wightman, N., Salameh, J. S., Kim, J., et al. (2015) · Neuron · doi:10.1016/j.neuron.2015.11.018 · Cited by 278

A Pan‐ E uropean Study of the C9orf72 Repeat Associated with FTLD : Geographic Prevalence, Genomic Instability, and Intermediate Repeats

van der Zee, J., Gijselinck, I., Dillen, L., Langenhove, T. V., Theuns, J., Engelborghs, S., Philtjens, S., Vandenbulcke, M., Sleegers, K., Sieben, A., et al. (2012) · Human Mutation · doi:10.1002/humu.22244 · Cited by 277

The C9ORF72 GGGGCC expansion forms RNA G-quadruplex inclusions and sequesters hnRNP H to disrupt splicing in ALS brains

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The clinical and pathological phenotype of C9ORF72 hexanucleotide repeat expansions

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Loss-of-function mutations in the C9ORF72 mouse ortholog cause fatal autoimmune disease

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Association between repeat sizes and clinical and pathological characteristics in carriers of C9ORF72 repeat expansions (Xpansize-72): a cross-sectional cohort study

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Poly(GP) proteins are a useful pharmacodynamic marker for C9ORF72 -associated amyotrophic lateral sclerosis

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C9orf72 ablation causes immune dysregulation characterized by leukocyte expansion, autoantibody production and glomerulonephropathy in mice

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The Src/c-Abl pathway is a potential therapeutic target in amyotrophic lateral sclerosis

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Drosophila screen connects nuclear transport genes to DPR pathology in c9ALS/FTD

Boeynaems, S., Bogaert, E., Michiels, E., Gijselinck, I., Sieben, A., Jovičić, A., De Baets, G., Scheveneels, W., Steyaert, J., Cuijt, I., et al. (2016) · Scientific Reports · doi:10.1038/srep20877 · Cited by 262

Elimination of Toxic Microsatellite Repeat Expansion RNA by RNA-Targeting Cas9

Batra, R., Nelles, D. A., PIRIE, E. C., Blue, S. M., Marina, R. J., Wang, H., Chaim, I. A., Thomas, J. D., Zhang, N., Nguyen, V., et al. (2017) · Cell · doi:10.1016/j.cell.2017.07.010 · Cited by 262

C9orf72 expansions in frontotemporal dementia and amyotrophic lateral sclerosis

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Nucleolar stress and impaired stress granule formation contribute to C9orf72 RAN translation-induced cytotoxicity

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Discovery of Novel DENN Proteins: Implications for the Evolution of Eukaryotic Intracellular Membrane Structures and Human Disease

Zhang, D., Iyer, L. M., He, F., & Aravind, L. (2012) · Frontiers in Genetics · doi:10.3389/fgene.2012.00283 · Cited by 244

C9orf72 Hexanucleotide Expansions Are Associated with Altered Endoplasmic Reticulum Calcium Homeostasis and Stress Granule Formation in Induced Pluripotent Stem Cell-Derived Neurons from Patients with Amyotrophic Lateral Sclerosis and Frontotemporal Dementia

Dafinca, R., Scaber, J., Ababneh, N. A., Lalic, T., Weir, G. A., Christian, H., Vowles, J., Douglas, A. G. L., Fletcher-Jones, A., Browne, C., et al. (2016) · Stem Cells · doi:10.1002/stem.2388 · Cited by 243

The C9orf72 repeat size correlates with onset age of disease, DNA methylation and transcriptional downregulation of the promoter

on behalf of the BELNEU CONSORTIUM, Gijselinck, I., Van Mossevelde, S., van der Zee, J., Sieben, A., Engelborghs, S., De Bleecker, J., Ivanoiu, A., Deryck, O., Edbauer, D., et al. (2016) · Molecular Psychiatry · doi:10.1038/mp.2015.159 · Cited by 242

Toxic PR n poly-dipeptides encoded by the C9orf72 repeat expansion block nuclear import and export

Shi, K. Y., Mori, E., Nizami, Z. F., Lin, Y., Kato, M., Xiang, S., Wu, L. C., Ding, M., Yu, Y., Gall, J. G., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1620293114 · Cited by 242

A C9ORF72/SMCR8-containing complex regulates ULK1 and plays a dual role in autophagy

Yang, M., Liang, C., Swaminathan, K., Herrlinger, S., Lai, F., Shiekhattar, R., & Chen, J.-F. (2016) · Science Advances · doi:10.1126/sciadv.1601167 · Cited by 238

Alzheimer's Disease Brain-Derived Amyloid-β-Mediated Inhibition of LTP In Vivo Is Prevented by Immunotargeting Cellular Prion Protein

Barry, A. E., Klyubin, I., Mc Donald, J. M., Mably, A. J., Farrell, M. A., Scott, M., Walsh, D. M., & Rowan, M. J. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.6500-10.2011 · Cited by 237

Quantitative analysis and clinico-pathological correlations of different dipeptide repeat protein pathologies in C9ORF72 mutation carriers

Mackenzie, I. R. A., Frick, P., Grässer, F. A., Gendron, T. F., Petrucelli, L., Cashman, N. R., Edbauer, D., Kremmer, E., Prudlo, J., Troost, D., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1476-2 · Cited by 231

Clinical and pathological features of familial frontotemporal dementia caused by C9ORF72 mutation on chromosome 9p

Hsiung, G. R., DeJesus-Hernandez, M., Feldman, H., Sengdy, P., Bouchard‐Kerr, P., Dwosh, E., Butler, R. K., Leung, B., Fok, A., Rutherford, N. J., et al. (2012) · Brain · doi:10.1093/brain/awr354 · Cited by 229

CRISPR–Cas9 screens in human cells and primary neurons identify modifiers of C9ORF72 dipeptide-repeat-protein toxicity

Kramer, N. J., Haney, M. S., Morgens, D. W., Jovičić, A., Couthouis, J., Li, A., Ousey, J., Ma, R., Bieri, G., Tsui, C. K., et al. (2018) · Nature Genetics · doi:10.1038/s41588-018-0070-7 · Cited by 226

RAN translation at C9orf72-associated repeat expansions is selectively enhanced by the integrated stress response

Green, K. M., Glineburg, M. R., Kearse, M. G., Flores, B. N., Linsalata, A. E., Fedak, S., Goldstrohm, A. C., Barmada, S. J., & Todd, P. K. (2017) · Nature Communications · doi:10.1038/s41467-017-02200-0 · Cited by 221

TMPyP4 Porphyrin Distorts RNA G-quadruplex Structures of the Disease-associated r(GGGGCC)n Repeat of the C9orf72 Gene and Blocks Interaction of RNA-binding Proteins

Zamiri, B., Reddy, K., Macgregor, R. B., & Pearson, C. E. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.c113.502336 · Cited by 221

C9ORF72 repeat expansion causes vulnerability of motor neurons to Ca2+-permeable AMPA receptor-mediated excitotoxicity

Selvaraj, B. T., Livesey, M. R., Zhao, C., Gregory, J. M., James, O. T., Cleary, E. M., Chouhan, A. K., Gane, A. B., Perkins, E., Dando, O., et al. (2018) · Nature Communications · doi:10.1038/s41467-017-02729-0 · Cited by 214

G‐quadruplex‐binding small molecules ameliorate C9orf72 FTD/ALS pathology in vitro and in vivo

Simone, R., Balendra, R., Moens, T. G., Preza, E., Wilson, K. M., Heslegrave, A., Woodling, N. S., Niccoli, T., Gilbert‐Jaramillo, J., Abdelkarim, S., et al. (2017) · EMBO Molecular Medicine · doi:10.15252/emmm.201707850 · Cited by 212

The expanding biology of the C9orf72 nucleotide repeat expansion in neurodegenerative disease

Haeusler, A. R., Donnelly, C. J., & Rothstein, J. D. (2016) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.38 · Cited by 205

Oligodendrocytes contribute to motor neuron death in ALS via SOD1-dependent mechanism

Ferraiuolo, L., Meyer, K., Sherwood, T. W., Vick, J. S., Likhite, S. B., Frakes, A., Miranda, C. J., Braun, L., Heath, P. R., Pineda, R., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1607496113 · Cited by 205

Differential Toxicity of Nuclear RNA Foci versus Dipeptide Repeat Proteins in a Drosophila Model of C9ORF72 FTD/ALS

Tran, H., Almeida, S., Moore, J. E., Gendron, T. F., Chalasani, U., Lu, Y., Du, X., Nickerson, J. A., Petrucelli, L., Weng, Z., et al. (2015) · Neuron · doi:10.1016/j.neuron.2015.09.015 · Cited by 204

C9orf72 binds SMCR8, localizes to lysosomes, and regulates mTORC1 signaling

Amick, J., Roczniak-Ferguson, A., & Ferguson, S. M. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-01-0003 · Cited by 201

C9ORF72 GGGGCC repeat-associated non-AUG translation is upregulated by stress through eIF2α phosphorylation

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Distribution of dipeptide repeat proteins in cellular models and C9orf72 mutation cases suggests link to transcriptional silencing

Schludi, M. H., Bavarian Brain Banking Alliance, May, S., Grässer, F. A., Rentzsch, K., Kremmer, E., Küpper, C., Klopstock, T., Arzberger, T., & Edbauer, D. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1450-z · Cited by 195

Gene-specific mitochondria dysfunctions in human TARDBP and C9ORF72 fibroblasts

Onesto, E., Colombrita, C., Gumina, V., Borghi, M. O., Dusi, S., Doretti, A., Fagiolari, G., Invernizzi, F., Moggio, M. G., Tiranti, V., et al. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0316-5 · Cited by 195

C9orf72 expansion disrupts ATM-mediated chromosomal break repair

Walker, C., Herranz-Martín, S., Karyka, E., Liao, C., Lewis, K. E. A., Elsayed, W., Lukashchuk, V., Chiang, S., Ray, S., Mulcahy, P. J., et al. (2017) · Nature Neuroscience · doi:10.1038/nn.4604 · Cited by 194

ALS/FTD-Associated C9ORF72 Repeat RNA Promotes Phase Transitions In Vitro and in Cells

Fay, M. M., Anderson, P., & Ivanov, P. V. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.11.093 · Cited by 192

Sense-encoded poly-GR dipeptide repeat proteins correlate to neurodegeneration and uniquely co-localize with TDP-43 in dendrites of repeat-expanded C9orf72 amyotrophic lateral sclerosis

Saberi, S., Stauffer, J. E., Jiang, J., Díaz-García, S., Taylor, A. E., Schulte, D. J., Ohkubo, T., Schloffman, C. L., Maldonado, M., Baughn, M. W., et al. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1793-8 · Cited by 187

Loss of C9orf72 Enhances Autophagic Activity via Deregulated mTOR and TFEB Signaling

Ugolino, J., Ji, Y. J., Conchina, K., Chu, J., Nirujogi, R. S., Pandey, A., Brady, N. R., Hamacher-Brady, A., & Wang, J. (2016) · PLOS Genetics · doi:10.1371/journal.pgen.1006443 · Cited by 185

Dipeptide repeat proteins are present in the p62 positive inclusions in patients with frontotemporal lobar degeneration and motor neurone disease associated with expansions in C9ORF72

Mann, D. M., Rollinson, S., Robinson, A., Bennion Callister, J., Thompson, J. C., Snowden, J. S., Gendron, T., Petrucelli, L., Masuda-Suzukake, M., Hasegawa, M., et al. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-68 · Cited by 182

Antisense RNA foci in the motor neurons of C9ORF72-ALS patients are associated with TDP-43 proteinopathy

Cooper‐Knock, J., Higginbottom, A., Stopford, M. J., Highley, J. R., Ince, P. G., Wharton, S. B., Pickering-Brown, S. M., Kirby, J., Hautbergue, G. M., & Shaw, P. J. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1429-9 · Cited by 181

C9orf72 hypermethylation protects against repeat expansion-associated pathology in ALS/FTD

Liu, E. Y., Russ, J., Wu, K., Neal, D., Suh, E., McNally, A. G., Irwin, D. J., Van Deerlin, V. M., & Lee, E. B. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1286-y · Cited by 180

The DNA damage response (DDR) is induced by the C9orf72 repeat expansion in amyotrophic lateral sclerosis

Farg, M. A., Konopka, A., Soo, K. Y., Ito, D., & Atkin, J. D. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx170 · Cited by 173

Timing and significance of pathological features in C9orf72 expansion-associated frontotemporal dementia

Vatsavayai, S. C., Yoon, S. J., Gardner, R. C., Gendron, T. F., Vargas, J. N. S., Trujillo, A. J., Pribadi, M., Phillips, J. J., Gaus, S. E., Hixson, J., et al. (2016) · Brain · doi:10.1093/brain/aww250 · Cited by 169

C9orf72 and RAB7L1 regulate vesicle trafficking in amyotrophic lateral sclerosis and frontotemporal dementia

Aoki, Y., Manzano, R., Lee, Y., Dafinca, R., Aoki, M., Douglas, A. G. L., Varela, M. A., Sathyaprakash, C., Scaber, J., Barbagallo, P., et al. (2017) · Brain · doi:10.1093/brain/awx024 · Cited by 167

Poly-dipeptides encoded by the C9ORF72 repeats block global protein translation

Kanekura, K., Yagi, T., Cammack, A. J., Mahadevan, J., Kuroda, M., Harms, M. B., Miller, T. M., & Urano, F. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw052 · Cited by 165

Cognitive decline and reduced survival inC9orf72expansion frontotemporal degeneration and amyotrophic lateral sclerosis

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C9ORF72 interaction with cofilin modulates actin dynamics in motor neurons

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Isoform‐specific antibodies reveal distinct subcellular localizations of C 9orf72 in amyotrophic lateral sclerosis

Xiao, S., MacNair, L., McGoldrick, P., McKeever, P. M., McLean, J. R., Zhang, M., Keith, J. L., Zinman, L. H., Rogaeva, E. A., & Robertson, J. (2015) · Annals of Neurology · doi:10.1002/ana.24469 · Cited by 154

Characterization of the dipeptide repeat protein in the molecular pathogenesis of c9FTD/ALS

Yamakawa, M., Ito, D., Honda, T., Kubo, K., Noda, M., Nakajima, K., & Suzuki, N. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu576 · Cited by 154

Homozygosity for the C9orf72 GGGGCC repeat expansion in frontotemporal dementia

Fratta, P., Poulter, M., Lashley, T., Rohrer, J. D., Polke, J. M., Beck, J. A., Ryan, N. S., Moss, D. J. H., Mizielinska, S., Waite, A. J., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1147-0 · Cited by 144

CUG initiation and frameshifting enable production of dipeptide repeat proteins from ALS/FTD C9ORF72 transcripts

Tabet, R., Schaeffer, L., Freyermuth, F., Jambeau, M., Workman, M. J., Lee, C.-Z., Lin, C.-C., Jiang, J., Jansen‐West, K. R., Hamdan, H. A., et al. (2018) · Nature Communications · doi:10.1038/s41467-017-02643-5 · Cited by 144

The C9orf72 repeat expansion itself is methylated in ALS and FTLD patients

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Comparative interactomics analysis of different ALS-associated proteins identifies converging molecular pathways

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SRSF1-dependent nuclear export inhibition of C9ORF72 repeat transcripts prevents neurodegeneration and associated motor deficits

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SURVEY AND SUMMARY: Puralpha: a multifunctional single-stranded DNA- and RNA-binding protein

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FTD/ALS-associated poly(GR) protein impairs the Notch pathway and is recruited by poly(GA) into cytoplasmic inclusions

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Spinal poly-GA inclusions in a C9orf72 mouse model trigger motor deficits and inflammation without neuron loss

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A zebrafish model for C9orf72 ALS reveals RNA toxicity as a pathogenic mechanism

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Full ablation of C9orf72 in mice causes immune system-related pathology and neoplastic events but no motor neuron defects

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Impeding Transcription of Expanded Microsatellite Repeats by Deactivated Cas9

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Extensive size variability of the GGGGCC expansion in C9orf72 in both neuronal and non-neuronal tissues in 18 patients with ALS or FTD

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Axonal transport defects are a common phenotype in Drosophila models of ALS

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Increased expression of the frontotemporal dementia risk factor TMEM106B causes C9orf72-dependent alterations in lysosomes

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