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 · see citing works

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 · see citing works

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 · see citing works

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

Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882 · see citing works

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

Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500 · see citing works

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

Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160 · see citing works

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 · see citing works

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

Arai, T., Hasegawa, M., Akiyama, H., Ikeda, K., Nonaka, T., Mori, H., Mann, D., Tsuchiya, K., Yoshida, M., Hashizume, Y., et al. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.10.093 · Cited by 2,732 · see citing works

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 2,658 · see citing works

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 · see citing works

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 1,546 · see citing works

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 1,327 · see citing works

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 · see citing works

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 · see citing works

Kinesin Transports RNA

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

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

The changing scene of amyotrophic lateral sclerosis

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

RNA phase transitions in repeat expansion disorders

(2017) · doi:10.1038/nature22386 · Cited by 911 · see citing works

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 · see citing works

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 848 · see citing works

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 · see citing works

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 · see citing works

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 748 · see citing works

<i>C9orf72</i> repeat expansions cause neurodegeneration in <i>Drosophila</i> 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 · see citing works

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. A., Molliex, A., et al. (2016) · Cell · doi:10.1016/j.cell.2016.10.002 · Cited by 687 · see citing works

Targeting RNA Foci in iPSC-Derived Motor Neurons from ALS Patients with a <i>C9ORF72</i> 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 · see citing works

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 652 · see citing works

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 648 · see citing works

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 635 · see citing works

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 · see citing works

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 · see citing works

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 583 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 555 · see citing works

<i>C9orf72</i> 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 · see citing works

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 · see citing works

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 · see citing works

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 513 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 431 · see citing works

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 423 · see citing works

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 416 · see citing works

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 · see citing works

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 410 · see citing works

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 410 · see citing works

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 · see citing works

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 393 · see citing works

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 381 · see citing works

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 · see citing works

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 358 · see citing works

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 · see citing works

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 · see citing works

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 339 · see citing works

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 335 · see citing works

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 · see citing works

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 · see citing works

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 328 · see citing works

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 · see citing works

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 · see citing works

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 320 · see citing works

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 · see citing works

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 315 · see citing works

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 314 · see citing works

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

Belzil, V., Bauer, P., Prudencio, M., Gendron, T. F., Stetler, C. T., Yan, I. K., Pregent, L., Daughrity, L. M., Baker, M., Rademakers, R., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1199-1 · Cited by 309 · see citing works

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

Boutajangout, A., Ingadottir, J., Davies, P., & Sigurdsson, E. M. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07337.x · Cited by 306 · see citing works

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 305 · see citing works

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 302 · see citing works

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 · see citing works

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

Murray, M. E., DeJesus‐Hernandez, M., Rutherford, N. J., Baker, M. C., Duara, R., Graff‐Radford, N. R., Wszołek, Z. K., Ferman, T. J., Josephs, K. A., Boylan, K., et al. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0907-y · Cited by 295 · see citing works

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

Devlin, A., Burr, K., Borooah, S., Foster, J. D., Cleary, E. M., Geti, I., Vallier, L., Shaw, C. E., Chandran, S., & Miles, G. B. (2015) · Nature Communications · doi:10.1038/ncomms6999 · Cited by 295 · see citing works

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

Sullivan, P. M., Zhou, X., Robins, A. M., Paushter, D. H., Kim, D., Smolka, M. B., & Hu, F. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0324-5 · Cited by 295 · see citing works

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

Conlon, E. G., Lü, L., Sharma, A., Yamazaki, T., Tang, T. K. K., Shneider, N. A., & Manley, J. L. (2016) · eLife · doi:10.7554/elife.17820 · Cited by 279 · see citing works

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

Waite, A. J., Bäumer, D., East, S. Z., Neal, J., Morris, H. R., Ansorge, O., & Blake, D. J. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.01.016 · Cited by 277 · see citing works

The clinical and pathological phenotype of C9ORF72 hexanucleotide repeat expansions

Simón‐Sánchez, J., Dopper, E. G. P., Cohn‐Hokke, P. E., Hukema, R. K., Nicolaou, N., Seelaar, H., de Graaf, J. R. A., de Koning, I., van Schoor, N. M., Deeg, D. J. H., et al. (2012) · Brain · doi:10.1093/brain/awr353 · Cited by 270 · see citing works

Loss-of-function mutations in the <i>C9ORF72</i> mouse ortholog cause fatal autoimmune disease

Burberry, A., Suzuki, N., Wang, J.-Y., Moccia, R., Mordes, D. A., Stewart, M. H., Suzuki-Uematsu, S., Ghosh, S., Singh, A., Merkle, F. T., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf6038 · Cited by 269 · see citing works

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 268 · see citing works

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

Xi, Z., Zinman, L. H., Moreno, D., Schymick, J. C., Liang, Y., Sato, C., Zheng, Y., Ghani, M., Dib, S., Keith, J. L., et al. (2013) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2013.04.017 · Cited by 267 · see citing works

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

van Blitterswijk, M., DeJesus‐Hernandez, M., Niemantsverdriet, E., Murray, M. E., Heckman, M. G., Diehl, N. N., Brown, P. H., Baker, M., Finch, N. A., Bauer, P. O., et al. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(13)70210-2 · Cited by 266 · see citing works

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 266 · see citing works

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

Gendron, T. F., Chew, J., Stankowski, J. N., Hayes, L. R., Zhang, Y.-J., Prudencio, M., Carlomagno, Y., Daughrity, L. M., Jansen-West, K., Perkerson, E. A., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aai7866 · Cited by 265 · see citing works

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

Atanasio, A., Decman, V., White, D., Ramos, M., Ikiz, B., Lee, H.-C., Siao, C.-J., Brydges, S., LaRosa, E., Bai, Y., et al. (2016) · Scientific Reports · doi:10.1038/srep23204 · Cited by 263 · see citing works

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 · see citing works

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

Imamura, K., Izumi, Y., Watanabe, A., Tsukita, K., Woltjen, K., Yamamoto, T., Hotta, A., Kondo, T., Kitaoka, S., Ohta, A., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf3962 · Cited by 260 · see citing works

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 259 · see citing works

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 252 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Alzheimer's Disease Brain-Derived Amyloid-β-Mediated Inhibition of LTP<i>In Vivo</i>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 · see citing works

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

Tao, Z., Wang, H., Qin, X., Li, K., Li, K., Jiang, X., Xu, G., Wang, G., & Ying, Z. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv005 · Cited by 237 · see citing works

C9orf72 expansions in frontotemporal dementia and amyotrophic lateral sclerosis

Rohrer, J. D., Isaacs, A. M., Mizielinska, S., Mead, S., Lashley, T., Wray, S., Sidle, K. C. L., Fratta, P., Orrell, R. W., Hardy, J., et al. (2015) · The Lancet Neurology · doi:10.1016/s1474-4422(14)70233-9 · Cited by 234 · see citing works

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 234 · see citing works

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 · see citing works

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 · see citing works

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 222 · see citing works

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 220 · see citing works

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 220 · see citing works

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 215 · see citing works

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 · see citing works

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

Cheng, W., Wang, S., Mestre, A. A., Fu, C., Makarem, A. O., Xian, F., Hayes, L. R., Lopez-Gonzalez, R., Drenner, K., Jiang, J., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-02495-z · Cited by 203 · see citing works

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 200 · see citing works

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 197 · see citing works

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 195 · see citing works

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 190 · see citing works

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 189 · see citing works

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 187 · see citing works

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 · see citing works

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 · see citing works

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 181 · see citing works

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 181 · see citing works

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 · see citing works

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 178 · see citing works

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 175 · see citing works

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 163 · see citing works

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 163 · see citing works

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 163 · see citing works

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 159 · see citing works

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

Irwin, D. J., McMillan, C. T., Brettschneider, J., Libon, D. J., Powers, J., Rascovsky, K., Toledo, J. B., Boller, A., Bekisz, J. M., Chandrasekaran, K., et al. (2012) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2012-303507 · Cited by 153 · see citing works

C9ORF72 interaction with cofilin modulates actin dynamics in motor neurons

Sivadasan, R., Hornburg, D., Drepper, C., Frank, N., Jablonka, S., Hansel, A., Lojewski, X., Sterneckert, J. L., Hermann, A., Shaw, P. J., et al. (2016) · Nature Neuroscience · doi:10.1038/nn.4407 · Cited by 148 · see citing works

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 145 · see citing works

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., Abou‐Hamdan, H., et al. (2018) · Nature Communications · doi:10.1038/s41467-017-02643-5 · Cited by 143 · see citing works

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 139 · see citing works

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

Gallia, G. L. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.17.3197 · Cited by 139 · see citing works

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

Blokhuis, A. M., Koppers, M., Groen, E. J. N., van den Heuvel, D. M. A., Modigliani, S. D., Anink, J. J., Fumoto, K., van Diggelen, F., Snelting, A., Sodaar, P., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1575-8 · Cited by 139 · see citing works

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

Hautbergue, G. M., Castelli, L. M., Ferraiuolo, L., Sánchez-Martínez, Á., Cooper‐Knock, J., Higginbottom, A., Lin, Y.-H., Bauer, C. S., Dodd, J. E., Myszczynska, M. A., et al. (2017) · Nature Communications · doi:10.1038/ncomms16063 · Cited by 138 · see citing works

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

Xi, Z., Zhang, M., Bruni, A. C., Maletta, R., Colao, R., Fratta, P., Polke, J. M., Sweeney, M. G., Mudanohwo, E. E., Nacmias, B., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1401-8 · Cited by 136 · see citing works

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

Yang, D., Abdallah, A., Li, Z., Lu, Y., Almeida, S., & Gao, F. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1448-6 · Cited by 134 · see citing works

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 134 · see citing works

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

Swinnen, B., Bento‐Abreu, A., Gendron, T. F., Boeynaems, S., Bogaert, E., Nuyts, R., Timmers, M., Scheveneels, W., Hersmus, N., Wang, J., et al. (2018) · Acta Neuropathologica · doi:10.1007/s00401-017-1796-5 · Cited by 133 · see citing works

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

Schludi, M. H., Becker, L., Garrett, L., Gendron, T. F., Zhou, Q., Schreiber, F., Popper, B., Dimou, L., Strom, T. M., Winkelmann, J., et al. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1711-0 · Cited by 131 · see citing works

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

Sudria-Lopez, E., Koppers, M., de Wit, M., van der Meer, C., Westeneng, H.-J., Zundel, C. A. C., Youssef, S. A., Harkema, L., de Bruin, A., Veldink, J. H., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1581-x · Cited by 130 · see citing works

Impeding Transcription of Expanded Microsatellite Repeats by Deactivated Cas9

Pinto, B. S., Saxena, T., Oliveira, R., Méndez‐Gómez, H. R., Cleary, J. D., Denes, L. T., McConnell, O. L., Arboleda, J. D., Xia, G., Swanson, M. S., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.09.033 · Cited by 130 · see citing works

Hypermethylation of repeat expanded C9orf72 is a clinical and molecular disease modifier

Russ, J., Liu, E. Y., Wu, K., Neal, D., Suh, E. R., Irwin, D. J., McMillan, C. T., Harms, M. B., Cairns, N. J., Wood, E. M., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1365-0 · Cited by 128 · see citing works

Novel clinical associations with specific C9ORF72 transcripts in patients with repeat expansions in C9ORF72

van Blitterswijk, M., Gendron, T. F., Baker, M., DeJesus‐Hernandez, M., Finch, N. A., Brown, P. H., Daughrity, L. M., Murray, M. E., Heckman, M. G., Jiang, J., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1480-6 · Cited by 123 · see citing works

Spt4 selectively regulates the expression of C9orf72 sense and antisense mutant transcripts

Kramer, N. J., Carlomagno, Y., Zhang, Y., Almeida, S., Cook, C. N., Gendron, T. F., Prudencio, M., van Blitterswijk, M., Belzil, V., Couthouis, J., et al. (2016) · Science · doi:10.1126/science.aaf7791 · Cited by 122 · see citing works

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

Nordin, A., Akimoto, C., Wuolikainen, A., Alstermark, H., Jonsson, P., Birve, A., Marklund, S. L., Graffmo, K. S., Forsberg, K., Brännström, T., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv064 · Cited by 120 · see citing works

TDP ‐43 binds and transports G ‐quadruplex‐containing m RNA s into neurites for local translation

Ishiguro, A., Kimura, N., Watanabe, Y., Watanabe, S., & Ishihama, A. (2016) · Genes to Cells · doi:10.1111/gtc.12352 · Cited by 120 · see citing works

Poly‐GP in cerebrospinal fluid links C9orf72‐associated dipeptide repeat expression to the asymptomatic phase of ALS/FTD

Lehmer, C., Oeckl, P., Weishaupt, J. H., Volk, A. E., Diehl‐Schmid, J., Schroeter, M. L., Lauer, M., Kornhuber, J., Levin, J., Fassbender, K., et al. (2017) · EMBO Molecular Medicine · doi:10.15252/emmm.201607486 · Cited by 118 · see citing works

Brain distribution of dipeptide repeat proteins in frontotemporal lobar degeneration and motor neurone disease associated with expansions in C9ORF72

Davidson, Y. S., Barker, H., Robinson, A., Thompson, J. C., Harris, J., Troakes, C., Smith, B. N., Al‐Saraj, S., Shaw, C. E., Rollinson, S. J., et al. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-70 · Cited by 115 · see citing works

Nuclear accumulation of mRNAs underlies G4C2 repeat-induced translational repression in a cellular model of C9orf72 ALS

Rossi, S., Serrano, A., Gerbino, V., Giorgi, A., Francesco, L. D., Nencini, M., Bozzo, F., Schininà, M. E., Bagni, C., Cestra, G., et al. (2015) · Journal of Cell Science · doi:10.1242/jcs.165332 · Cited by 113 · see citing works

Cytoplasmic poly-GA aggregates impair nuclear import of TDP-43 in C9orf72 ALS/FTLD

Khosravi, B., Hartmann, H., May, S., Möhl, C., Ederle, H., Michaelsen, M., Schludi, M. H., Dormann, D., & Edbauer, D. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw432 · Cited by 113 · see citing works

Cerebellar c9RAN proteins associate with clinical and neuropathological characteristics of C9ORF72 repeat expansion carriers

Gendron, T. F., van Blitterswijk, M., Bieniek, K. F., Daughrity, L. M., Jiang, J., Rush, B. K., Pedraza, O., Lucas, J. A., Murray, M. E., Desaro, P., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1474-4 · Cited by 106 · see citing works

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

Baldwin, K. R., Godena, V. K., Hewitt, V. L., & Whitworth, A. J. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw105 · Cited by 105 · see citing works

Post-transcriptional Inhibition of Hsc70-4/HSPA8 Expression Leads to Synaptic Vesicle Cycling Defects in Multiple Models of ALS

Coyne, A. N., Lorenzini, I., Chou, C., Torvund, M., Rogers, R. S., Starr, A., Zaepfel, B. L., Levy, J., Johannesmeyer, J., Schwartz, J. C., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.09.028 · Cited by 102 · see citing works

Length of normal alleles of C9ORF72 GGGGCC repeat do not influence disease phenotype

Rutherford, N. J., Heckman, M. G., DeJesus‐Hernandez, M., Baker, M. C., Soto‐Ortolaza, A. I., Rayaprolu, S., Stewart, H. G., Finger, E. C., Volkening, K., Seeley, W. W., et al. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.07.005 · Cited by 100 · see citing works

Evidence that C9ORF72 Dipeptide Repeat Proteins Associate with U2 snRNP to Cause Mis-splicing in ALS/FTD Patients

Yin, S., Lopez-Gonzalez, R., Kunz, R. C., Gangopadhyay, J. P., Borufka, C., Gygi, S. P., Gao, F., & Reed, R. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.05.056 · Cited by 100 · see citing works

Pathophysiological insights into ALS with C9ORF72 expansions

Williams, K. L., Fifita, J. A., Vucic, S., Durnall, J. C., Kiernan, M. C., Blair, I. P., & Nicholson, G. A. (2013) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2012-304529 · Cited by 99 · see citing works

C9ORF72 Regulates Stress Granule Formation and Its Deficiency Impairs Stress Granule Assembly, Hypersensitizing Cells to Stress

Maharjan, N., Künzli, C., Buthey, K., & Saxena, S. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9850-1 · Cited by 99 · see citing works

The small heat shock protein B8 (HSPB8) efficiently removes aggregating species of dipeptides produced in C9ORF72-related neurodegenerative diseases

Cristofani, R., Crippa, V., Vezzoli, G., Rusmini, P., Galbiati, M., Cicardi, M. E., Meroni, M., Ferrari, V., Tedesco, B., Piccolella, M., et al. (2017) · Cell Stress and Chaperones · doi:10.1007/s12192-017-0806-9 · Cited by 96 · see citing works

GGGGCC microsatellite RNA is neuritically localized, induces branching defects, and perturbs transport granule function

Burguete, A. S., Almeida, S., Gao, F., Kalb, R. G., Akins, M. R., & Bonini, N. M. (2015) · eLife · doi:10.7554/elife.08881 · Cited by 94 · see citing works

A 39-kD DNA-binding protein from mouse brain stimulates transcription of myelin basic protein gene in oligodendrocytic cells.

Haas, S., Thatikunta, P., Steplewski, A., et al. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.130.5.1171 · Cited by 93 · see citing works

Dipeptide repeat protein inclusions are rare in the spinal cord and almost absent from motor neurons in C9ORF72 mutant amyotrophic lateral sclerosis and are unlikely to cause their degeneration

Gomez-Deza, J., Lee, Y.-B., Troakes, C., Nolan, M., Al-Sarraj, S., Gallo, J.-M., & Shaw, C. E. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0218-y · Cited by 93 · see citing works

In-depth clinico-pathological examination of RNA foci in a large cohort of C9ORF72 expansion carriers

DeJesus‐Hernandez, M., Finch, N. A., Wang, X., Gendron, T. F., Bieniek, K. F., Heckman, M. G., Vasilevich, A. S., Murray, M. E., Rousseau, L., Weesner, R. E., et al. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1725-7 · Cited by 92 · see citing works

Cortical Function in Asymptomatic Carriers and Patients WithC9orf72Amyotrophic Lateral Sclerosis

Geevasinga, N., Menon, P., Nicholson, G. A., Ng, K., Howells, J., Kril, J. J., Yiannikas, C., Kiernan, M. C., & Vucic, S. (2015) · JAMA Neurology · doi:10.1001/jamaneurol.2015.1872 · Cited by 88 · see citing works

Antibodies inhibit transmission and aggregation of C9orf72 poly‐GA dipeptide repeat proteins

Zhou, Q., Lehmer, C., Michaelsen, M., Mori, K., Alterauge, D., Baumjohann, D., Schludi, M. H., Greiling, J., Farny, D., Flatley, A., et al. (2017) · EMBO Molecular Medicine · doi:10.15252/emmm.201607054 · Cited by 87 · see citing works

Review: Modulating the unfolded protein response to prevent neurodegeneration and enhance memory

Halliday, M., & Mallucci, G. R. (2014) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12211 · Cited by 85 · see citing works

Activation of HIPK2 Promotes ER Stress-Mediated Neurodegeneration in Amyotrophic Lateral Sclerosis

Lee, S., Shang, Y., Redmond, S., Urisman, A., Tang, A. A., Li, K. H., Burlingame, A. L., Pak, R. A., Jovičić, A., Gitler, A. D., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.05.021 · Cited by 85 · see citing works

The Glycine-Alanine Dipeptide Repeat from C9orf72 Hexanucleotide Expansions Forms Toxic Amyloids Possessing Cell-to-Cell Transmission Properties

Chang, Y., Jeng, U., Chiang, Y., Hwang, I., & Chen, Y. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.694273 · Cited by 84 · see citing works

Characterization of DNA hypermethylation in the cerebellum of c9FTD/ALS patients

Belzil, V., Bauer, P. O., Gendron, T. F., Murray, M. E., Dickson, D. W., & Petrucelli, L. (2014) · Brain Research · doi:10.1016/j.brainres.2014.02.015 · Cited by 82 · see citing works

Anti-sense DNA d(GGCCCC)n expansions in C9ORF72 form i-motifs and protonated hairpins

Kovanda, A., Zalar, M., Šket, P., Plavec, J., & Rogelj, B. (2015) · Scientific Reports · doi:10.1038/srep17944 · Cited by 82 · see citing works

C9orf72 is differentially expressed in the central nervous system and myeloid cells and consistently reduced in C9orf72, MAPT and GRN mutation carriers

Rizzu, P., Blauwendraat, C., Heetveld, S., Lynes, E. M., Castillo-Lizardo, M., Dhingra, A., Pyż, E., Hobert, M. A., Synofzik, M., Simón‐Sánchez, J., et al. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0306-7 · Cited by 79 · see citing works

Neurodegeneration in frontotemporal lobar degeneration and motor neurone disease associated with expansions in <i>C9orf72</i> is linked to TDP‐43 pathology and not associated with aggregated forms of dipeptide repeat proteins

Davidson, Y., Robinson, A. C., Liu, X., Wu, D., Troakes, C., Rollinson, S., Masuda‐Suzukake, M., Suzuki, G., Nonaka, T., Shi, J., et al. (2016) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12292 · Cited by 77 · see citing works

Early dipeptide repeat pathology in a frontotemporal dementia kindred with C9ORF72 mutation and intellectual disability

Proudfoot, M. J., Gutowski, N. J., Edbauer, D., Hilton, D. A., Stephens, M., Rankin, J., & Mackenzie, I. R. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1245-7 · Cited by 77 · see citing works

The mouse C9ORF72 ortholog is enriched in neurons known to degenerate in ALS and FTD

Suzuki, N., Maroof, A. M., Merkle, F. T., Koszka, K., Intoh, A., Armstrong, I. K. G., Moccia, R., Davis‐Dusenbery, B. N., & Eggan, K. C. (2013) · Nature Neuroscience · doi:10.1038/nn.3566 · Cited by 77 · see citing works

Lack of C9ORF72 coding mutations supports a gain of function for repeat expansions in amyotrophic lateral sclerosis

Harms, M. B., Cady, J., Zaidman, C. M., Cooper, P., Bali, T., Allred, P., Cruchaga, C., Baughn, M. W., Libby, R. T., Pestronk, A., et al. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.03.006 · Cited by 76 · see citing works

Inhibition of retrograde transport modulates misfolded protein accumulation and clearance in motoneuron diseases

Cristofani, R., Crippa, V., Rusmini, P., Cicardi, M. E., Meroni, M., Licata, N. V., Sala, G., Giorgetti, E., Grunseich, C., Galbiati, M., et al. (2017) · Autophagy · doi:10.1080/15548627.2017.1308985 · Cited by 75 · see citing works

Semi-automated quantification of C9orf72 expansion size reveals inverse correlation between hexanucleotide repeat number and disease duration in frontotemporal degeneration

Suh, E. R., Lee, E. B., Neal, D., Wood, E. M., Toledo, J. B., Rennert, L., Irwin, D. J., McMillan, C. T., Krock, B. L., Elman, L. B., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1445-9 · Cited by 75 · see citing works

Multiplex image-based autophagy RNAi screening identifies SMCR8 as ULK1 kinase activity and gene expression regulator

Jung, J., Nayak, A., Schaeffer, V., Starzetz, T., Kirsch, A. K., Müller, S. P., Đikić, I., Mittelbronn, M. G. A., & Behrends, C. (2017) · eLife · doi:10.7554/elife.23063 · Cited by 74 · see citing works

Glycine-alanine dipeptide repeat protein contributes to toxicity in a zebrafish model of C9orf72 associated neurodegeneration

Ohki, Y., Wenninger-Weinzierl, A., Hruscha, A., Asakawa, K., Kawakami, K., Haass, C., Edbauer, D., & Schmid, B. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0146-8 · Cited by 73 · see citing works

Altered mRNP granule dynamics in FTLD pathogenesis

Bowden, H. A., & Dormann, D. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13601 · Cited by 72 · see citing works

C9orf72 promoter hypermethylation is neuroprotective

McMillan, C. T., Russ, J., Wood, E. M., Irwin, D. J., Grossman, M., McCluskey, L. F., Elman, L. B., Deerlin, V. M. V., & Lee, E. B. (2015) · Neurology · doi:10.1212/wnl.0000000000001495 · Cited by 71 · see citing works

Highly Efficient Targeted Mutagenesis in Mice Using TALENs

Panda, S. K., Wefers, B., Ortiz, O., Floß, T., Schmid, B., Haass, C., Wurst, W., & Kühn, R. (2013) · Genetics · doi:10.1534/genetics.113.156570 · Cited by 71 · see citing works

Selective vulnerability in neurodegeneration: insights from clinical variants of Alzheimer's disease

Mattsson, N., Schott, J. M., Hardy, J., Turner, M. R., & Zetterberg, H. (2016) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2015-311321 · Cited by 71 · see citing works

Sense and antisense RNA are not toxic in Drosophila models of C9orf72-associated ALS/FTD

Moens, T. G., Mizielinska, S., Niccoli, T., Mitchell, J. S., Thoeng, A., Ridler, C. E., Grönke, S., Eßer, J., Heslegrave, A., Zetterberg, H., et al. (2018) · Acta Neuropathologica · doi:10.1007/s00401-017-1798-3 · Cited by 70 · see citing works

Accumulation of dipeptide repeat proteins predates that of TDP ‐43 in frontotemporal lobar degeneration associated with hexanucleotide repeat expansions in C9ORF72 gene

Baborie, A., Griffiths, T. D., Jaros, E., Perry, R., McKeith, I. G., Burn, D. J., Masuda‐Suzukake, M., Hasegawa, M., Rollinson, S. J., Pickering-Brown, S. M., et al. (2014) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12178 · Cited by 69 · see citing works

Pur-alpha regulates cytoplasmic stress granule dynamics and ameliorates FUS toxicity

Daigle, J. G., Krishnamurthy, K., Ramesh, N., Casci, I., Monaghan, J., McAvoy, K. J., Godfrey, E. W., Daniel, D. C., Johnson, E. M., Monahan, Z. T., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-015-1530-0 · Cited by 69 · see citing works

The Proline/Arginine Dipeptide from Hexanucleotide Repeat Expanded C9ORF72 Inhibits the Proteasome

Gupta, R., Lan, M., Mojsilovic‐Petrovic, J., Choi, W. H., Safren, N., Barmada, S. J., Lee, M. J., & Kalb, R. G. (2017) · eNeuro · doi:10.1523/eneuro.0249-16.2017 · Cited by 69 · see citing works

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

Busch, J. I., Unger, T. L., Jain, N., Skrinak, R. T., Charan, R. A., & Chen‐Plotkin, A. S. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw127 · Cited by 68 · see citing works

Expression of C9orf72-related dipeptides impairs motor function in a vertebrate model

Swaminathan, A., Bouffard, M., Liao, M., Ryan, S., Callister, J. B., Pickering-Brown, S. M., Armstrong, G. A. B., & Drapeau, P. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy083 · Cited by 66 · see citing works

Retention of hexanucleotide repeat-containing intron in C9orf72 mRNA: implications for the pathogenesis of ALS/FTD

Niblock, M., Smith, B. N., Lee, Y., Sardone, V., Topp, S. D., Troakes, C., Al‐Sarraj, S., Leblond, C. S., Dion, P. A., Rouleau, G. A., et al. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0289-4 · Cited by 64 · see citing works

The C9ORF72 expansion mutation: gene structure, phenotypic and diagnostic issues

Woollacott, I., & Mead, S. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1253-7 · Cited by 63 · see citing works

Screening a UK amyotrophic lateral sclerosis cohort provides evidence of multiple origins of the C9orf72 expansion

Fratta, P., Polke, J. M., Newcombe, J., Mizielinska, S., Lashley, T., Poulter, M., Beck, J. A., Preza, E., Devoy, A., Sidle, K. C. L., et al. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.07.037 · Cited by 61 · see citing works

Impaired long‐term potentiation–like cortical plasticity in presymptomatic genetic frontotemporal dementia

Benussi, A., Cosseddu, M., Filareto, I., Dell’Era, V., Archetti, S., Cotelli, M. S., Micheli, A., Padovani, A., & Borroni, B. (2016) · Annals of Neurology · doi:10.1002/ana.24731 · Cited by 61 · see citing works

Bidirectional nucleolar dysfunction in C9orf72 frontotemporal lobar degeneration

Mizielinska, S., Ridler, C. E., Balendra, R., Thoeng, A., Woodling, N. S., Grässer, F. A., Plagnol, V., Lashley, T., Partridge, L., & Isaacs, A. M. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0432-x · Cited by 61 · see citing works

Nuclear trafficking in amyotrophic lateral sclerosis and frontotemporal lobar degeneration

Mihevc, S. P., Darovic, S., Kovanda, A., Česnik, A. B., Župunski, V., & Rogelj, B. (2016) · Brain · doi:10.1093/brain/aww197 · Cited by 59 · see citing works

Genetic models of C9orf72: what is toxic?

Moens, T. G., Partridge, L., & Isaacs, A. M. (2017) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2017.01.006 · Cited by 57 · see citing works

Poly-A Binding Protein-1 Localization to a Subset of TDP-43 Inclusions in Amyotrophic Lateral Sclerosis Occurs More Frequently in Patients Harboring an Expansion inC9orf72

McGurk, L., Lee, V. M., Trojanowksi, J. Q., Deerlin, V. M. V., Lee, E. B., & Bonini, N. M. (2014) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000102 · Cited by 57 · see citing works

The Single‐Stranded DNA‐ and RNA‐Binding Proteins Pur α and Pur β Link BC1 RNA to Microtubules Through Binding to the Dendrite‐Targeting RNA Motifs

Ohashi, S., Kobayashi, S., Omori, A., Ohara, S., Omae, A., Muramatsu, T., Li, Y., & Anzai, K. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0751781.x · Cited by 56 · see citing works

Jump from Pre-mutation to Pathologic Expansion in C9orf72

Xi, Z., van Blitterswijk, M., Zhang, M., McGoldrick, P., McLean, J. R., Yunusova, Y., Knock, E., Moreno, D., Sato, C., McKeever, P. M., et al. (2015) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2015.04.016 · Cited by 53 · see citing works

Amyotrophic lateral sclerosis: translating genetic discoveries into therapies

Akçimen, F., Lopez, E. R., Landers, J. E., Nath, A., Chiò, A., Chia, R., & Traynor, B. J. (2023) · Nature Reviews Genetics · doi:10.1038/s41576-023-00592-y · Cited by 234 · see citing works

Reduced C9ORF72 function exacerbates gain of toxicity from ALS/FTD-causing repeat expansion in C9orf72

Zhu, Q., Jiang, J., Gendron, T. F., McAlonis-Downes, M., Jiang, L., Taylor, A., Diaz Garcia, S., Ghosh Dastidar, S., Rodriguez, M. J., King, P., et al. (2020) · Nature Neuroscience · doi:10.1038/s41593-020-0619-5 · Cited by 220 · see citing works

CRISPR-based functional genomics for neurological disease

Kampmann, M. (2020) · Nature Reviews Neurology · doi:10.1038/s41582-020-0373-z · Cited by 163 · see citing works

Selective Autophagy Receptors in Neuronal Health and Disease

Conway, O., Akpinar, H. A., Rogov, V. V., & Kirkin, V. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.10.013 · Cited by 75 · see citing works

Review: Fluid biomarkers for frontotemporal dementias

Zetterberg, H., van Swieten, J. C., Boxer, A. L., & Rohrer, J. D. (2019) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12530 · Cited by 48 · see citing works

Targeted Screening of the C9orf72 Gene in Bulgarian Amyotrophic Lateral Sclerosis Patients

Ormandzhiev, S., Тодоров, Т., Angelov, T., et al. (2022) · Acta Medica Bulgarica · doi:10.2478/amb-2022-0002

Amyotrophic Lateral Sclerosis with Frontotemporal Dementia in the Presence of C9orf72 Repeat Expansion-A Case Report.

Bonda, C., Kolikonda, M. K., Brown, M. E., & Lippmann, S. (2016) · PubMed Central · Cited by 1 · see citing works

Analysis of C9orf72 hexanucleotide repeat expansions in SOD1 negative patients with amyotrophic lateral sclerosis

Chan, C. Y. (2015) · Pathology · doi:10.1097/01.pat.0000461401.06779.80

[ 18 F]AV‐1451 binding is increased in frontotemporal dementia due to C9orf72 expansion

Bevan-Jones, W. R., Cope, T., Jones, S. P., Passamonti, L., Hong, Y. T., Fryer, T. D., Arnold, R. J., Coles, J., Aigbirhio, F. A., Patterson, K. E., et al. (2018) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.631 · Cited by 23 · see citing works

Clinico-pathological features in amyotrophic lateral sclerosis with expansions in C9ORF72

Cooper‐Knock, J., Hewitt, C., Highley, J. R., Brockington, A., Milano, A., Man, S., Martindale, J. E., Hartley, J. A., Walsh, T., Gelsthorpe, C., et al. (2012) · Brain · doi:10.1093/brain/awr365 · Cited by 329 · see citing works