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

Mfold web server for nucleic acid folding and hybridization prediction

Zuker, M. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg595 · Cited by 13,404 · see citing works

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

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

Increasing the precision of comparative models with YASARA NOVA—a self‐parameterizing force field

Krieger, E., Koraimann, G., & Vriend, G. (2002) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10104 · Cited by 1,519 · see citing works

Spatiotemporal Rescue of Memory Dysfunction in Drosophila

McGuire, S. E., Le, P. T., Osborn, A. J., Matsumoto, K., & Davis, R. L. (2003) · Science · doi:10.1126/science.1089035 · Cited by 1,318 · 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

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

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

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

ALS‐associated fused in sarcoma (FUS) mutations disrupt Transportin‐mediated nuclear import

Dormann, D., Rodde, R., Edbauer, D., Bentmann, E., Fischer, I., Hruscha, A., Than, M. E., Mackenzie, I. R. A., Capell, A., Schmid, B., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.143 · Cited by 836 · 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

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

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

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

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

Prediction of water and metal binding sites and their affinities by using the Fold-X force field

Schymkowitz, J. W. H., Rousseau, F., Martins, I. C., Ferkinghoff‐Borg, J., Stricher, F., & Serrano, L. G. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501980102 · Cited by 340 · see citing works

Arginine methylation next to the PY‐NLS modulates Transportin binding and nuclear import of FUS

Dormann, D., Madl, T., Valori, C. F., Bentmann, E., Tahirovic, S., Abou‐Ajram, C., Kremmer, E., Ansorge, O., Mackenzie, I. R. A., Neumann, M., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.261 · Cited by 326 · 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

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

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

Co-aggregation of RNA binding proteins in ALS spinal motor neurons: evidence of a common pathogenic mechanism

Keller, B. A., Volkening, K., Droppelmann, C. A., Ang, L. C., Rademakers, R., & Strong, M. J. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-1035-z · Cited by 130 · see citing works

Protein Arginine Methyltransferase 1 and 8 Interact with FUS to Modify Its Sub-Cellular Distribution and Toxicity In Vitro and In Vivo

Scaramuzzino, C., Monaghan, J., Milioto, C., Lanson, N. A., Maltare, A., Aggarwal, T., Casci, I., Fackelmayer, F. O., Pennuto, M., & Pandey, U. B. (2013) · PLoS ONE · doi:10.1371/journal.pone.0061576 · Cited by 106 · see citing works

Transportin 1 accumulates specifically with FET proteins but no other transportin cargos in FTLD-FUS and is absent in FUS inclusions in ALS with FUS mutations

Neumann, M., Valori, C. F., Ansorge, O., Kretzschmar, H. A., Muñoz, D. G., Kusaka, H., Yokota, O., Ishihara, K., Ang, L.-C., Bilbao, J. M., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-1020-6 · Cited by 88 · 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

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

Fifty Years of Nuclear Pores and Nucleocytoplasmic Transport Studies

Floch, A. G., Palancade, B., & Doye, V. (2014) · Methods in cell biology · doi:10.1016/b978-0-12-417160-2.00001-1 · Cited by 59 · see citing works

[Clinico-pathological correlation].

Carvalhal, S. D. S., Bittencourt, L. A., & Jorge, P. A. (1972) · PubMed · Cited by 23 · see citing works

Protein Phase Separation: A New Phase in Cell Biology

Boeynaems, S., Alberti, S., Fawzi, N. L., Mittag, T., Polymenidou, M., Rousseau, F., Schymkowitz, J. W. H., Shorter, J., Wolozin, B. L., Bosch, L. V. D., et al. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.004 · Cited by 1,954 · see citing works

C9orf72-mediated ALS and FTD: multiple pathways to disease

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

Amyotrophic lateral sclerosis: a neurodegenerative disorder poised for successful therapeutic translation

Mead, R. J., Shan, N., Reiser, H. J., Marshall, F., & Shaw, P. J. (2023) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00612-2 · Cited by 505 · 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

The role of TDP-43 mislocalization in amyotrophic lateral sclerosis

Suk, T. R., & Rousseaux, M. W. C. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00397-1 · Cited by 456 · 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

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

Molecular mechanisms underlying nucleotide repeat expansion disorders

Malik, I., Kelley, C. P., Wang, E. T., & Todd, P. K. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00382-6 · Cited by 363 · see citing works

Poly(GR) impairs protein translation and stress granule dynamics in C9orf72-associated frontotemporal dementia and amyotrophic lateral sclerosis

Zhang, Y., Gendron, T. F., Ebbert, M., O’Raw, A. D., Yue, M., Jansen‐West, K. R., Zhang, X., Prudencio, M., Chew, J., Cook, C. N., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0071-1 · Cited by 307 · see citing works

Lost in Transportation: Nucleocytoplasmic Transport Defects in ALS and Other Neurodegenerative Diseases

Kim, H. J., & Taylor, J. P. (2017) · Neuron · doi:10.1016/j.neuron.2017.07.029 · Cited by 267 · see citing works

Disruption of RNA Metabolism in Neurological Diseases and Emerging Therapeutic Interventions

Nussbacher, J. K., Tabet, R., Yeo, G. W.-M., & Lagier‐Tourenne, C. (2019) · Neuron · doi:10.1016/j.neuron.2019.03.014 · Cited by 264 · see citing works

Triad of TDP43 control in neurodegeneration: autoregulation, localization and aggregation

Tziortzouda, P., Bosch, L. V. D., & Hirth, F. (2021) · Nature reviews. Neuroscience · doi:10.1038/s41583-021-00431-1 · Cited by 270 · see citing works

The Role of Dipeptide Repeats in C9ORF72-Related ALS-FTD

Freibaum, B. D., & Taylor, J. P. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00035 · Cited by 251 · 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

Dysregulated molecular pathways in amyotrophic lateral sclerosis–frontotemporal dementia spectrum disorder

Gao, F., Almeida, S., & Lopez‐Gonzalez, R. (2017) · The EMBO Journal · doi:10.15252/embj.201797568 · Cited by 218 · see citing works

Modelling amyotrophic lateral sclerosis: progress and possibilities

Damme, P. V., Robberecht, W., & Bosch, L. V. D. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.029058 · Cited by 203 · see citing works

Regulation of mRNA Translation in Neurons—A Matter of Life and Death

Kapur, M., Monaghan, C. E., & Ackerman, S. L. (2017) · Neuron · doi:10.1016/j.neuron.2017.09.057 · Cited by 200 · 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

ALS: A bucket of genes, environment, metabolism and unknown ingredients

Zufiría, M., Gil-Bea, F. J., Fernández‐Torrón, R., Poza, J. J., Muñoz-Blanco, J. L., Rojas‐García, R., Riancho, J., & de Munaín, A. L. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.05.004 · Cited by 192 · see citing works

TDP ‐43 and FUS en route from the nucleus to the cytoplasm

Ederle, H., & Dormann, D. (2017) · FEBS Letters · doi:10.1002/1873-3468.12646 · Cited by 169 · see citing works

RNA toxicity in non‐coding repeat expansion disorders

Swinnen, B., Robberecht, W., & Bosch, L. V. D. (2019) · The EMBO Journal · doi:10.15252/embj.2018101112 · Cited by 163 · see citing works

Nuclear egress of TDP-43 and FUS occurs independently of Exportin-1/CRM1

Ederle, H., Funk, C., Abou‐Ajram, C., Hutten, S., Funk, E. B. E., Kehlenbach, R. H., Bailer, S. M., & Dormann, D. (2018) · Scientific Reports · doi:10.1038/s41598-018-25007-5 · Cited by 159 · see citing works

There has been an awakening: Emerging mechanisms of C9orf72 mutations in FTD/ALS

Gitler, A. D., & Tsuiji, H. (2016) · Brain Research · doi:10.1016/j.brainres.2016.04.004 · Cited by 152 · see citing works

TDP43 nuclear export and neurodegeneration in models of amyotrophic lateral sclerosis and frontotemporal dementia

Archbold, H. C., Jackson, K. L., Arora, A., Weskamp, K., Tank, E. M. H., Li, X., Miguez, R., Dayton, R. D., Tamir, S., Klein, R. L., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-22858-w · Cited by 151 · 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

Mechanisms of protein toxicity in neurodegenerative diseases

Chung, C. G., Lee, H., & Lee, S. B. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2854-4 · Cited by 142 · see citing works

TCF4-mediated Fuchs endothelial corneal dystrophy: Insights into a common trinucleotide repeat-associated disease

Fautsch, M. P., Wieben, E. D., Baratz, K. H., Bhattacharyya, N., Sadan, A. N., Hafford‐Tear, N. J., Tuft, S. J., & Davidson, A. E. (2020) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2020.100883 · Cited by 141 · see citing works

Reduced autophagy upon C9ORF72 loss synergizes with dipeptide repeat protein toxicity in G4C2 repeat expansion disorders

Boivin, M., Pfister, V., Gaucherot, A., Ruffenach, F., Negroni, L., Sellier, C., & Charlet‐Berguerand, N. (2020) · The EMBO Journal · doi:10.15252/embj.2018100574 · Cited by 137 · 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

C9orf72 arginine-rich dipeptide repeat proteins disrupt karyopherin-mediated nuclear import

Hayes, L. R., Duan, L., Bowen, K., Kaláb, P., & Rothstein, J. D. (2020) · eLife · doi:10.7554/elife.51685 · Cited by 133 · see citing works

Inside out: the role of nucleocytoplasmic transport in ALS and FTLD

Boeynaems, S., Bogaert, E., Damme, P. V., & Bosch, L. V. D. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1586-5 · Cited by 128 · see citing works

Nuclear Import Receptors Directly Bind to Arginine-Rich Dipeptide Repeat Proteins and Suppress Their Pathological Interactions

Hutten, S., Usluer, S., Bourgeois, B. M. R., Simonetti, F., Odeh, H. M., Fare, C. M., Czuppa, M., Hruška-Plocháň, M., Hofweber, M., Polymenidou, M., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108538 · Cited by 107 · see citing works

Biomolecular condensates in neurodegeneration and cancer

Spannl, S., Tereshchenko, M., Mastromarco, G. J., Ihn, S. J., & Lee, H. O. (2019) · Traffic · doi:10.1111/tra.12704 · Cited by 112 · 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

C9orf72 arginine-rich dipeptide proteins interact with ribosomal proteins in vivo to induce a toxic translational arrest that is rescued by eIF1A

Moens, T. G., Niccoli, T., Wilson, K. M., Atilano, M. L., Birsa, N., Gittings, L. M., Hölbling, B. V., Dyson, M. C., Thoeng, A., Neeves, J., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-018-1946-4 · Cited by 110 · see citing works

Proteomics and C9orf72 neuropathology identify ribosomes as poly-GR/PR interactors driving toxicity

Hartmann, H., Hornburg, D., Czuppa, M., Bader, J. M., Michaelsen, M., Farny, D., Arzberger, T., Mann, M., Meissner, F., & Edbauer, D. (2018) · Life Science Alliance · doi:10.26508/lsa.201800070 · Cited by 106 · see citing works

Ageing as a risk factor for ALS/FTD

Niccoli, T., Partridge, L., & Isaacs, A. M. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx247 · Cited by 102 · see citing works

Poly-GR dipeptide repeat polymers correlate with neurodegeneration and Clinicopathological subtypes in C9ORF72-related brain disease

Sakae, N., Bieniek, K. F., Zhang, Y., Ross, K., Gendron, T. F., Murray, M. E., Rademakers, R., Petrucelli, L., & Dickson, D. W. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0564-7 · Cited by 103 · see citing works

A feedback loop between dipeptide-repeat protein, TDP-43 and karyopherin-α mediates C9orf72-related neurodegeneration

Solomon, D. A., Stepto, A., Au, W. H., Adachi, Y., Diaper, D. C., Hall, R., Rekhi, A., Boudi, A., Tziortzouda, P., Lee, Y., et al. (2018) · Brain · doi:10.1093/brain/awy241 · Cited by 100 · see citing works

Nuclear pore complexes — a doorway to neural injury in neurodegeneration

Coyne, A. N., & Rothstein, J. D. (2022) · Nature Reviews Neurology · doi:10.1038/s41582-022-00653-6 · Cited by 96 · see citing works

Repeat-associated non-ATG (RAN) translation

Cleary, J. D., Pattamatta, A., & Ranum, L. P. W. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.r118.003237 · Cited by 95 · see citing works

C9orf72 -derived arginine-containing dipeptide repeats associate with axonal transport machinery and impede microtubule-based motility

Fumagalli, L., Young, F. L., Boeynaems, S., Decker, M. D., Mehta, A. R., Swijsen, A., Fazal, R., Guo, W., Moisse, M., Beckers, J., et al. (2021) · Science Advances · doi:10.1126/sciadv.abg3013 · Cited by 89 · see citing works

Interactions between ALS-linked FUS and nucleoporins are associated with defects in the nucleocytoplasmic transport pathway

Lin, Y., Kumar, M. S., Ramesh, N., Anderson, E. N., Nguyen, A. T., Kim, B., Cheung, S., McDonough, J. A., Skarnes, W. C., Lopez-Gonzalez, R., et al. (2021) · Nature Neuroscience · doi:10.1038/s41593-021-00859-9 · Cited by 92 · see citing works

An Intramolecular Salt Bridge Linking TDP43 RNA Binding, Protein Stability, and TDP43-Dependent Neurodegeneration

Flores, B. N., Li, X., Malik, A. M., Martinez, J., Beg, A. A., & Barmada, S. J. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.03.093 · Cited by 92 · see citing works

Nucleocytoplasmic transport defects in neurodegeneration — Cause or consequence?

Hutten, S., & Dormann, D. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.05.020 · Cited by 82 · see citing works

Pooled CRISPR screens with imaging on microraft arrays reveals stress granule-regulatory factors

Wheeler, E. C., Vu, A. Q., Einstein, J. M., DiSalvo, M., Ahmed, N., Nostrand, E. L. V., Shishkin, A. A., Jin, W., Allbritton, N. L., & Yeo, G. W.-M. (2020) · Nature Methods · doi:10.1038/s41592-020-0826-8 · Cited by 87 · see citing works

New developments in RAN translation: insights from multiple diseases

Cleary, J. D., & Ranum, L. P. W. (2017) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2017.03.006 · Cited by 83 · see citing works

C9orf72-FTD/ALS pathogenesis: evidence from human neuropathological studies

Vatsavayai, S. C., Nana, A. L., Yokoyama, J. S., & Seeley, W. W. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1921-0 · Cited by 78 · see citing works

New pathologic mechanisms in nucleotide repeat expansion disorders

Rodriguez, C. M., & Todd, P. K. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104515 · Cited by 79 · see citing works

Synaptic dysfunction and altered excitability in C9ORF72 ALS/FTD

Starr, A., & Sattler, R. (2018) · Brain Research · doi:10.1016/j.brainres.2018.02.011 · Cited by 78 · see citing works

TFEB/Mitf links impaired nuclear import to autophagolysosomal dysfunction in C9-ALS

Cunningham, K. M., Maulding, K., Ruan, K., Şentürk, M., Grima, J. C., Sung, H., Zuo, Z., Song, H., Gao, J., Dubey, S. K., et al. (2020) · eLife · doi:10.7554/elife.59419 · Cited by 75 · 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

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

Cell‐to‐cell transmission of C9orf72 poly‐(Gly‐Ala) triggers key features of ALS/FTD

Khosravi, B., LaClair, K. D., Riemenschneider, H., Zhou, Q., Frottin, F., Mareljic, N., Czuppa, M., Farny, D., Hartmann, H., Michaelsen, M., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019102811 · Cited by 70 · see citing works

Traffic jam at the nuclear pore: All roads lead to nucleocytoplasmic transport defects in ALS/FTD

Fallini, C., Khalil, B., Smith, C. L., & Rossoll, W. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.104835 · Cited by 68 · see citing works

NUP62 localizes to ALS/FTLD pathological assemblies and contributes to TDP-43 insolubility

Gleixner, A. M., Verdone, B. M., Otte, C. G., Anderson, E. N., Ramesh, N., Shapiro, O. R., Gale, J. R., Mauna, J. C., Mann, J. R., Copley, K. E., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31098-6 · Cited by 68 · see citing works

Understanding Amyotrophic Lateral Sclerosis: Pathophysiology, Diagnosis, and Therapeutic Advances

Rizea, R. E., Corlatescu, A.-D., Costin, H. P., Dumitru, A. V., & Ciurea, A. V. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25189966 · Cited by 76 · see citing works

Genetic strategies to tackle neurological diseases in fruit flies

Şentürk, M., & Bellen, H. J. (2017) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2017.10.017 · 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

Molecular Mechanisms of Neurodegeneration Related to C9orf72 Hexanucleotide Repeat Expansion

Leko, M. B., Župunski, V., Kirincich, J., Smilović, D., Hortobágyi, T., Hof, P. R., & Šimić, G. (2019) · Behavioural Neurology · doi:10.1155/2019/2909168 · Cited by 70 · see citing works

Therapeutic Dissolution of Aberrant Phases by Nuclear-Import Receptors

Guo, L. E., Fare, C. M., & Shorter, J. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.12.004 · Cited by 66 · see citing works

Stable transgenic C9orf72 zebrafish model key aspects of the ALS/FTD phenotype and reveal novel pathological features

Shaw, M. P., Higginbottom, A., McGown, A., Castelli, L. M., James, E. G., Hautbergue, G. M., Shaw, P. J., & Ramesh, T. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0629-7 · Cited by 68 · see citing works

C9orf72-generated poly-GR and poly-PR do not directly interfere with nucleocytoplasmic transport

Vanneste, J., Vercruysse, T., Boeynaems, S., Sicart, A., Damme, P. V., Daelemans, D., & Bosch, L. V. D. (2019) · Scientific Reports · doi:10.1038/s41598-019-52035-6 · Cited by 68 · see citing works

ADAR2 mislocalization and widespread RNA editing aberrations in C9orf72-mediated ALS/FTD

Moore, S. R., Alsop, E. B., Lorenzini, I., Starr, A., Rabichow, B. E., Mendez, E. F., Levy, J. L., Burciu, C., Reiman, R. A., Chew, J., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-01999-w · Cited by 68 · see citing works

Congenic expression of poly-GA but not poly-PR in mice triggers selective neuron loss and interferon responses found in C9orf72 ALS

LaClair, K. D., Zhou, Q., Michaelsen, M., Wefers, B., Brill, M. S., Janjic, A., Rathkolb, B., Farny, D., Cygan, M., de Angelis, M. H., et al. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02176-0 · Cited by 68 · see citing works

C9orf72 loss-of-function: a trivial, stand-alone or additive mechanism in C9 ALS/FTD?

Braems, E., Swinnen, B., & Bosch, L. V. D. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02214-x · Cited by 68 · see citing works

Focus on the heterogeneity of amyotrophic lateral sclerosis

Bendotti, C., Bonetto, V., Pupillo, E., Logroscino, G., Al‐Chalabi, A., Lunetta, C., Riva, N., Mora, G., Lauria, G., Weishaupt, J. H., et al. (2020) · Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration · doi:10.1080/21678421.2020.1779298 · Cited by 67 · 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

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

Nucleo–cytoplasmic transport defects and protein aggregates in neurodegeneration

Bitetto, G., & Fonzo, A. D. (2020) · Translational Neurodegeneration · doi:10.1186/s40035-020-00205-2 · Cited by 66 · see citing works

Quality-control mechanisms targeting translationally stalled and C-terminally extended poly(GR) associated with ALS/FTD

Li, S., Wu, Z., Tantray, I., Li, Y., Chen, S., Dong, J., Glynn, S. E., Vogel, H. S., Snyder, M. P., & Lu, B. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2005506117 · Cited by 61 · see citing works

ALS and FTD: Where RNA metabolism meets protein quality control

Mandrioli, J., Mediani, L., Alberti, S., & Carra, S. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.06.003 · Cited by 58 · 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

Failure to Deliver and Translate—New Insights into RNA Dysregulation in ALS

Coyne, A. N., Zaepfel, B. L., & Zarnescu, D. C. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00243 · Cited by 57 · see citing works

Repeat-associated non-AUG (RAN) translation: insights from pathology

Báñez-Coronel, M., & Ranum, L. P. W. (2019) · Laboratory Investigation · doi:10.1038/s41374-019-0241-x · Cited by 57 · see citing works

Prion-Like Proteins in Phase Separation and Their Link to Disease

Sprunger, M. L., & Jackrel, M. E. (2021) · Biomolecules · doi:10.3390/biom11071014 · Cited by 57 · see citing works

Nuclear transport dysfunction: a common theme in amyotrophic lateral sclerosis and frontotemporal dementia

Jovičić, A., Paul, J. W., & Gitler, A. D. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13642 · Cited by 53 · see citing works

Insights into C9ORF72-Related ALS/FTD from Drosophila and iPSC Models

Yuva-Aydemir, Y., Almeida, S., & Gao, F. (2018) · Trends in Neurosciences · doi:10.1016/j.tins.2018.04.002 · Cited by 55 · see citing works

C9orf72 dipeptides disrupt the nucleocytoplasmic transport machinery and cause TDP-43 mislocalisation to the cytoplasm

Ryan, S., Rollinson, S. J., Hobbs, E., & Pickering-Brown, S. M. (2022) · Scientific Reports · doi:10.1038/s41598-022-08724-w · Cited by 49 · see citing works

ATXN1 repeat expansions confer risk for amyotrophic lateral sclerosis and contribute to TDP-43 mislocalization

Tazelaar, G. H. P., Boeynaems, S., Decker, M. D., van Vugt, J. J. F. A., Kool, L., Goedee, H. S., McLaughlin, R. L., Sproviero, W., Iacoangeli, A., Moisse, M., et al. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa064 · Cited by 53 · see citing works

Suppression of C9orf72 RNA repeat-induced neurotoxicity by the ALS-associated RNA-binding protein Zfp106

Celona, B., Dollen, J. V., Vatsavayai, S. C., Kashima, R., Johnson, J. R., Tang, A. A., Hata, A., Miller, B. L., Huang, E. J., Krogan, N. J., et al. (2017) · eLife · doi:10.7554/elife.19032 · Cited by 49 · see citing works

C9orf72 Dipeptide Repeats Cause Selective Neurodegeneration and Cell-Autonomous Excitotoxicity in Drosophila Glutamatergic Neurons

Xu, W., & Xu, J. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.0908-18.2018 · Cited by 49 · see citing works

Karyopherin abnormalities in neurodegenerative proteinopathies

Pasha, T., Zatorska, A., Sharipov, D., Rogelj, B., Hortobágyi, T., & Hirth, F. (2021) · Brain · doi:10.1093/brain/awab201 · Cited by 46 · see citing works

Phase Separation of Toxic Dipeptide Repeat Proteins Related to C9orf72 ALS/FTD

Jafarinia, H., der Giessen, E. V., & Onck, P. R. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2020.07.005 · Cited by 46 · see citing works

Role and therapeutic potential of liquid–liquid phase separation in amyotrophic lateral sclerosis

Pakravan, D., Orlando, G., Bercier, V., & Bosch, L. V. D. (2020) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjaa049 · Cited by 46 · see citing works

Integrative genetic analysis illuminates ALS heritability and identifies risk genes

Megat, S., Mora, N., Sanogo, J., Roman, O., Catanese, A., Alami, N. O., Freischmidt, A., Mingaj, X., de Calbiac, H., Muratet, F., et al. (2023) · Nature Communications · doi:10.1038/s41467-022-35724-1 · Cited by 52 · see citing works

Synaptic dysfunction induced by glycine‐alanine dipeptides in C9orf72‐ALS/FTD is rescued by SV2 replenishment

Jensen, B. K., Schuldi, M. H., McAvoy, K. J., Russell, K. A., Boehringer, A. V., Curran, B. M., Krishnamurthy, K., Wen, X., Westergard, T., Ma, L., et al. (2020) · EMBO Molecular Medicine · doi:10.15252/emmm.201910722 · Cited by 45 · see citing works

C9orf72 isoforms in Amyotrophic Lateral Sclerosis and Frontotemporal Lobar Degeneration

Xiao, S., MacNair, L., McLean, J. R., McGoldrick, P., McKeever, P. M., Soleimani, S., Keith, J. L., Zinman, L. H., Rogaeva, E. A., & Robertson, J. (2016) · Brain Research · doi:10.1016/j.brainres.2016.04.062 · Cited by 44 · see citing works

Pathogenic determinants and mechanisms of ALS/FTD linked to hexanucleotide repeat expansions in the C9orf72 gene

Wen, X., Westergard, T., Pasinelli, P., & Trotti, D. (2016) · Neuroscience Letters · doi:10.1016/j.neulet.2016.09.007 · Cited by 43 · see citing works

Distinct C9orf72-Associated Dipeptide Repeat Structures Correlate with Neuronal Toxicity

Flores, B. N., Dulchavsky, M. E., Krans, A., Sawaya, M. R., Paulson, H. L., Todd, P. K., Barmada, S. J., & Ivanova, M. I. (2016) · PLoS ONE · doi:10.1371/journal.pone.0165084 · Cited by 42 · see citing works

Loss of Ranbp2 in motor neurons causes the disruption of nucleocytoplasmic and chemokine signaling and proteostasis of hnRNPH3 and Mmp28, and the development of amyotrophic lateral sclerosis (ALS)-like syndromes

Cho, K., Yoon, D., Qiu, S., Danziger, Z. C., Grill, W. M., Wetsel, W. C., & Ferreira, P. A. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.027730 · Cited by 42 · see citing works

The Genetics of C9orf72 ExpansionsPreprint

Gijselinck, I., Cruts, M., & Broeckhoven, C. V. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026757 · Cited by 40 · see citing works

FUS-induced neurotoxicity in Drosophila is prevented by downregulating nucleocytoplasmic transport proteins

Steyaert, J., Scheveneels, W., Vanneste, J., Damme, P. V., Robberecht, W., Callaerts, P., Bogaert, E., & Bosch, L. V. D. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy303 · Cited by 42 · see citing works

Arginine-rich dipeptide-repeat proteins as phase disruptors in C9-ALS/FTD

Odeh, H. M., & Shorter, J. (2020) · Emerging Topics in Life Sciences · doi:10.1042/etls20190167 · Cited by 38 · see citing works

Nuclear Transport Deficits in Tau-Related Neurodegenerative Diseases

Diez, L., & Wegmann, S. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.01056 · Cited by 40 · see citing works

RAN Translation of the Expanded CAG Repeats in the SCA3 Disease Context

Jazurek, M., Ciesiołka, A., Komur, A. A., Urbanek-Trzeciak, M. O., Krzyżosiak, W. J., & Fiszer, A. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.10.033 · Cited by 40 · see citing works

Pathogenic Mechanisms and Therapy Development for C9orf72 Amyotrophic Lateral Sclerosis/Frontotemporal Dementia

Jiang, J., & Ravits, J. (2019) · Neurotherapeutics · doi:10.1007/s13311-019-00797-2 · Cited by 42 · see citing works

The Development of C9orf72-Related Amyotrophic Lateral Sclerosis and Frontotemporal Dementia Disorders

Yang, Q., Jiao, B., & Shen, L. H. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.562758 · Cited by 40 · see citing works

Sigma-1 receptor chaperones rescue nucleocytoplasmic transport deficit seen in cellular and Drosophila ALS/FTD models

Lee, P.-T., Liévens, J.-C., Wang, S., Chuang, J., Khalil, B., Wu, H.-E., Chang, W., Maurice, T., & Su, T. (2020) · Nature Communications · doi:10.1038/s41467-020-19396-3 · Cited by 39 · see citing works

De role van het nucleair-cytoplasmatisch transport in C9orf72 amyotrofe laterale sclerose

Vanneste, J. (2021) · Lirias

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

Epigenetic Small Molecules Rescue Nucleocytoplasmic Transport and DNA Damage Phenotypes in C9ORF72 ALS/FTD

Ramic, M., Andrade, N. S., Rybin, M. J., Esanov, R., Wahlestedt, C., Benatar, M. G., & Zeier, Z. R. (2021) · Brain Sciences · doi:10.3390/brainsci11111543 · Cited by 12 · see citing works

[P1–203]: C9ORF72 DIPEPTIDE REPEAT PROTEINS DISRUPT NUCLEOCYTOPLASMIC TRANSPORT

Ryan, S., Rollinson, S. J., Callister, J. B., Hobbs, E., & Pickering-Brown, S. M. (2017) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2017.06.023

[P1–024]: C9ORF72 DIPEPTIDE REPEAT PROTEINS DISRUPT NUCLEOCYTOPLASMIC TRANSPORT

Ryan, S., Rollinson, S. J., Callister, J. B., Hobbs, E., & Pickering-Brown, S. M. (2017) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2017.06.091