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

Mfold web server for nucleic acid folding and hybridization prediction

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

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

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

DeJesus-Hernandez, M., Mackenzie, I. R., Boeve, B. F., Boxer, A. L., Baker, M., Rutherford, N. J., Nicholson, A. M., Finch, N. A., Flynn, H., Adamson, J., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.011 · Cited by 4,936 · cited 2×

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

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

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

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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

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

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

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

Synthetic hydrogel mimics of the nuclear pore complex for the study of nucleocytoplasmic transport defects in C9orf72 ALS/FTD

Friedman, A. K., Boeynaems, S., & Baker, L. A. (2021) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-021-03478-2 · Cited by 6

Cellular and molecular phenotypes of C9orf72 ALS/FTD patient derived iPSC-microglia mono-culturesPreprint

Lorenzini, I., Alsop, E. B., Levy, J., Gittings, L. M., Lall, D., Rabichow, B. E., Moore, S. R., Pevey, R. S., Bustos, L. M., Burciu, C., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.03.277459 · Cited by 6

Loss of nucleoporin Nup50 is a risk factor for amyotrophic lateral sclerosisPreprint

Megat, S., Mora, N., Sanogo, J., Catanese, A., Alami, N. O., Freischmidt, A., Mingaj, X., de Calbiac, H., Muratet, F., Dirrig‐Grosch, S., et al. (2021) · medRxiv · doi:10.1101/2021.08.23.21262299 · Cited by 6

ERO1A inhibition mitigates neuronal ER stress and ameliorates UBQLN2ALS phenotypes in Drosophila melanogaster

Yeewa, R., Sangphukieo, A., Jantaree, P., Wongkummool, W., Yamsri, T., Poompouang, S., Chaiyawat, P., Piccolo, L. L., & Jantrapirom, S. (2024) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2024.102674 · Cited by 5

TDP-43 pathology in Drosophila induces glial-cell type specific toxicity that can be ameliorated by knock-down of SF2/SRSF1

Krupp, S., Hubbard, I., Tam, O. H., Hammell, M., & Dubnau, J. (2023) · PLoS Genetics · doi:10.1371/journal.pgen.1010973 · Cited by 6

Assay to Measure Nucleocytoplasmic Transport in Real Time within Motor Neuron-like NSC-34 Cells

Shani, T., Levy, M., & Israelson, A. (2017) · Journal of Visualized Experiments · doi:10.3791/55676 · Cited by 5

Frontotemporal dementia

Wauters, E., Sleegers, K., Cruts, M., & Broeckhoven, C. V. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-805120-7.00009-9 · Cited by 6

Neurodegenerative Diseases and RNA-Mediated Toxicity

Todd, T. W., & Petrucelli, L. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811304-2.00015-8 · Cited by 5

C9orf72 polyPR interaction with the nuclear pore complex

Jafarinia, H., der Giessen, E. V., & Onck, P. R. (2024) · Biophysical Journal · doi:10.1016/j.bpj.2024.08.024 · Cited by 4

Repeat length of C9orf72-associated glycine–alanine polypeptides affects their toxicity

Morón-Oset, J., Fischer, L. K., Jauré, N., Zhang, P., Jahn, A. J., Supèr, T., Pahl, A., Isaacs, A. M., Grönke, S., & Partridge, L. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01634-6 · Cited by 5

Nuclear Pore and Genome Organization and Gene Expression in Drosophila

Kuhn, T. M., & Capelson, M. (2018) · Springer eBooks · doi:10.1007/978-3-319-71614-5_5 · Cited by 4

Accumulation of TDP-43 causes karyopherin-α4 pathology that characterises amyotrophic lateral sclerosis

Atwal, M. S., Nimac, J., Čerček, U., Goesch, S. R., Goesch, H. R., Tziortzouda, P., Ercolani, T., Zatorska, A., Pasha, T., Carre, I., et al. (2025) · Frontiers in Neuroscience · doi:10.3389/fnins.2025.1558227 · Cited by 3

Cellular quiescence uncouples the proteome from the transcriptome in neural stem cells

Rossi, A., Coum, A., Madelenat, M., Harris, L., Strohbuecker, S., Chai, A., Fiaz, H., Chaouni, R., Faull, P. A., Heaven, N. C., et al. (2026) · The EMBO Journal · doi:10.1038/s44318-026-00693-4 · Cited by 3

The Fault in Our Astrocytes - cause or casualties of proteinopathies of ALS/FTD and other neurodegenerative diseases?

Bustos, L. M., & Sattler, R. (2023) · Frontiers in Molecular Medicine · doi:10.3389/fmmed.2023.1075805 · Cited by 4

CRISPR interference to evaluate modifiers of C9ORF72-mediated toxicity in FTD

Pickles, S. R., Alepuz, D. Z., Koike, Y. M., Yue, M., Tong, J., Liu, P., Zhou, Y., Jansen‐West, K. R., Daughrity, L. M., Song, Y., et al. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1251551 · Cited by 4

Biochemistry and Cell Biology of Ageing: Part III Biomedical Science

Harris, J. R., & Korolchuk, V. I. (2023) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-21410-3 · Cited by 4

The Effects of poly-GA and poly-PR C9orf72 Dipeptide Repeats on Sleep Patterns in Drosophila melanogaster

Uy, G., Farrell, L. N., Faheem, S. F., Kinne, L. E., Adore, M. G., Im, S. H., & Fairman, R. (2023) · PubMed Central · doi:10.17912/micropub.biology.000973 · Cited by 3

The Expanding Role of RNA-Binding Proteins in Neurodegeneration

Maurya, B., Surabhi, S., Pandey, P., Mukherjee, A., & Mutsuddi, M. (2019) · Springer eBooks · doi:10.1007/978-981-13-2218-1_13 · Cited by 3

CRISPR expands insight into the mechanisms of ALS and FTD

Pickles, S. R., & Petrucelli, L. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0005-z · Cited by 3

C9ORF72 dipeptide repeat proteins disrupt formation of GEM bodies and induce aberrant accumulation of survival of motor neuron proteinPreprint

Kato, Y., Yokogawa, M., Nakagawa, I., Onodera, K., Okano, H., Inoue, H., Hattori, M., Okada, Y., & Tsuiji, H. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.24.436890 · Cited by 3

Nemo-like kinase disrupts nuclear import and drives TDP43 mislocalization in ALS

Bekier, M. E., Pinarbasi, E., Krishnan, G., Mesojedec, J. J., Hurley, M., Harikumar Sheela, H., Collins, C. A., Ghaffari, L., de Majo, M., Ullian, E. M., et al. (2025) · Journal of Clinical Investigation · doi:10.1172/jci188138 · Cited by 2

C9orf72 polyPR directly binds to various nuclear transport components

Jafarinia, H., van der Giessen, E., & Onck, P. R. (2024) · eLife · doi:10.7554/elife.89694.3 · Cited by 2

Understanding the Pathogenicity of Noncoding RNA Expansion-Associated Neurodegenerative Disorders

Das, R., Chakraborty, M., Mukherjee, A., & Mutsuddi, M. (2019) · Springer eBooks · doi:10.1007/978-981-13-2218-1_12 · Cited by 2

The exocyst subunit EXOC2 regulates the toxicity of expanded GGGGCC repeats in C9ORF72-ALS/FTD

Halim, D. O., Krishnan, G., Hass, E. P., Lee, S., Verma, M., Almeida, S., Gu, Y., Kwon, D. Y., Fazzio, T. G., & Gao, F. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114375 · Cited by 1

Reversible ALKBH5 cytosolic aggregation accelerates cellular senescence

Chen, L., Chen, Z., Mo, J., Xie, Q., Lin, W., Zheng, H., Zou, Y., Chen, Y., Bian, X., Zhou, Z., et al. (2025) · Cell Death and Differentiation · doi:10.1038/s41418-025-01560-1 · Cited by 1

Impaired nucleocytoplasmic transport in SOD1-mediated ALS

Argueti-Ostrovsky, S., Lim, S. M., Arogundade, O. A., Díaz-García, S., Yunisova, G., Meng, A., Hermann, A., Ong, K., Eremenko, E., Bravo‐Hernández, M., et al. (2026) · Molecular Neurodegeneration · doi:10.1186/s13024-026-00930-8 · Cited by 1

Deficiency in KPNA4, but Not in KPNA3, Causes Attention Deficit/Hyperactivity Disorder like Symptoms in Mice

Rother, F., Parmar, A. R., Bodenhagen, J. S., Marvaldi, L., Hartmann, E., & Bäder, M. (2025) · Genes · doi:10.3390/genes16060690 · Cited by 1

Amyotrophic Lateral Sclerosis and Other TDP-43 Proteinopathies

Gómez-Deza, J., & Shaw, C. E. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811304-2.00005-5 · Cited by 1

Drosophila Models to Study Long Noncoding RNAs Related to Neurological Disorders

Muraoka, Y., & Yamaguchi, M. (2020) · RNA technologies · doi:10.1007/978-3-030-44743-4_16 · Cited by 1

An Intramolecular Salt Bridge Linking TDP43's RNA Recognition Motifs Dictates RNA Binding and TDP43-Dependent NeurodegenerationPreprint

Flores, B. N., Li, X., Martinez, J., Beg, A. A., & Barmada, S. J. (2018) · SSRN Electronic Journal · doi:10.2139/ssrn.3236488 · Cited by 1

Genome-wide RNA binding analysis of C9orf72 poly(PR) dipeptidesPreprint

Balendra, R., Mozos, I. R. D. L., Glaria, I., Milioto, C., Odeh, H. M., Wilson, K. M., Ule, A. M., Hallegger, M., Masino, L., Martin, S. R., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.10.10.511318 · Cited by 1

C9orf72 polyPR directly binds to various nuclear transport components

Jafarinia, H., Van der Giessen, E., & Onck, P. R. (2023) · doi:10.1101/2023.06.22.546068 · Cited by 1

C9ORF72-derived polyGR polypeptides disrupt passive nucleocytoplasmic transport by tuning protein affinity for the nuclear pore barrierPreprint

Solomon, D. A., Emenecker, R. J., Salcher-Konrad, M.-T., Konstantinidou, S. M., Houghton, O. H., Wycherley, E., Lee, S., O’Brien, N. L., Alcalde, J., Cabaco, I. L., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.03.16.711670 · Cited by 1

Identification of a Nuclear Localization Signal (NLS) within the Pleckstrin Homology (PH) domain of Rho Guanine Nucleotide Exchange Factor (RGNEF)

Tavolieri, M. V., & Strong, M. J. (2016) · Scholarship@Western (Western University) · doi:10.13140/rg.2.2.10647.21924

Arginine valency in C9ORF72 dipolypeptides mediates promiscuous proteome binding that stalls ribosomes, disable actin cytoskeleton assembly and impairs arginine methylation of endogenous proteinsPreprint

Radwan, M., Ang, C., Ormsby, A. R., Cox, D., Daly, J. C., Reid, G. E., & Hatters, D. M. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/749127

Understanding Motor Disorders Using Flies

Chaplot, K., Ratnaparkhi, A., & Ratnaparkhi, G. S. (2019) · Springer eBooks · doi:10.1007/978-981-13-2218-1_5

Unraveling molecular biology of C9ORF72 repeat expansions in amyotrophic lateral sclerosis-frontotemporal dementia: Implications for therapy

Arogundade, O. A., Jiang, J., & Ravits, J. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-816475-4.00009-4

RNA-Mediated Metabolic Defects in Microsatellite Expansion Diseases

Zhang, N. (2021) · Springer eBooks · doi:10.1007/978-3-030-76571-2_8

Loss of C9orf72 perturbs the Ran-GTPase gradient and generates compositionally diverse cytoplasmic Importin β-1 granules in motor and cortical neurons in vivoPreprint

McGoldrick, P., Lau, A., You, Z., Durcan, T. M., & Robertson, J. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.20.465148

Effect of G 4 C 2 Repeat Expansions on the Motion of Lysosomes Inside NeuritesPreprint

Mytiliniou, M., Wondergem, J. A. J., Feliksik, M., Schmidt, T., & Heinrich, D. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.29.466472

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

Houart, C., & Gordon, P. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.734473246.793554065

Faculty Opinions recommendation of Stress granule assembly disrupts nucleocytoplasmic transport.

Finkbeiner, S. M. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.732994586.793546070

Investigation of the role of prolyl isomerase A in protein misfolding associated with neurodegenerative diseases

Babu, M. (2023) · doi:10.53846/goediss-9950

C9orf72 polyPR directly binds to various nuclear transport componentsPreprint

Jafarinia, H., der Giessen, E. V., & Onck, P. R. (2023) · eLife · doi:10.7554/elife.89694.1

C9orf72 polyPR directly binds to various nuclear transport components

Jafarinia, H., Van der Giessen, E., & Onck, P. R. (2023) · doi:10.7554/elife.89694.2

Poly-GR Impairs PRMT1-Mediated Arginine Methylation of Disease-Linked RNA-Binding Proteins by Acting as a Substrate Sink

Hutten, S., Chen, J., Isaacs, A. M., & Dormann, D. (2024) · Biochemistry · doi:10.1021/acs.biochem.4c00308

Super‐Enhancer Protects Cells From Toxicity of C9orf72 Poly(proline–arginine) by Inducing the Expression of KPNA2/KPNB1

Chen, M., Cui, H., Zhang, X., Ma, S., Guo, J., Liu, Z., Gu, D., & Fan, Y. (2025) · Cell Biochemistry and Function · doi:10.1002/cbf.70053

Additional file 6 of Nucleolar stress in C9orf72 and sporadic ALS spinal motor neurons precedes TDP-43 mislocalization

Aladesuyi Arogundade, O., Nguyen, S., Leung, R., Wainio, D., Rodriguez, M., & Ravits, J. (2021) · Figshare · doi:10.6084/m9.figshare.14037392

Additional file 1 of Co-expression of C9orf72 related dipeptide-repeats over 1000 repeat units reveals age- and combination-specific phenotypic profiles in Drosophila

West, R. J. H., Sharpe, J. L., Voelzmann, A., Munro, A. L., Hahn, I., Baines, R., & Pickering-Brown, S. M. (2020) · Figshare · doi:10.6084/m9.figshare.12926309

Additional file 5 of Nucleolar stress in C9orf72 and sporadic ALS spinal motor neurons precedes TDP-43 mislocalization

Aladesuyi Arogundade, O., Nguyen, S., Leung, R., Wainio, D., Rodriguez, M., & Ravits, J. (2021) · Figshare · doi:10.6084/m9.figshare.14037389

Additional file 1 of Nucleolar stress in C9orf72 and sporadic ALS spinal motor neurons precedes TDP-43 mislocalization

Aladesuyi Arogundade, O., Nguyen, S., Leung, R., Wainio, D., Rodriguez, M., & Ravits, J. (2021) · Figshare · doi:10.6084/m9.figshare.14037377

Additional file 4 of Nucleolar stress in C9orf72 and sporadic ALS spinal motor neurons precedes TDP-43 mislocalization

Aladesuyi Arogundade, O., Nguyen, S., Leung, R., Wainio, D., Rodriguez, M., & Ravits, J. (2021) · Figshare · doi:10.6084/m9.figshare.14037386

Additional file 3 of Nucleolar stress in C9orf72 and sporadic ALS spinal motor neurons precedes TDP-43 mislocalization

Aladesuyi Arogundade, O., Nguyen, S., Leung, R., Wainio, D., Rodriguez, M., & Ravits, J. (2021) · Figshare · doi:10.6084/m9.figshare.14037383

Additional file 2 of Nucleolar stress in C9orf72 and sporadic ALS spinal motor neurons precedes TDP-43 mislocalization

Aladesuyi Arogundade, O., Nguyen, S., Leung, R., Wainio, D., Rodriguez, M., & Ravits, J. (2021) · Figshare · doi:10.6084/m9.figshare.14037380

Novel single molecule imaging approaches reveal structure-function alterations to the nuclear pore complex in early C9ORF72 -associated TDP-43 proteinopathyPreprint

Lee, S., & Mizielinska, S. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.17.706337

Effect of G 4 C 2 repeat expansions on the motion of lysosomes inside neurites

Mytiliniou, M., Wondergem, J. A. J., Feliksik, M., Schmidt, T., Fuhs, T., & Heinrich, D. (2026) · Physical Biology · doi:10.1088/1478-3975/ae5143

Modeling C9ORF72 loss-of-function : a knockdown mouse model

Lopez-Herdoiza, M.-B. (2016) · theses.fr (ABES) · doi:10.70675/dfc77570z827az4993z840dz21dfc54360de

Caractérisations biochimiques des protéines à répétitions de dipeptides et de leurs assemblages

Brasseur, L. (2019) · theses.fr (ABES) · doi:10.70675/9c659bfdz83dez45e5za549z64f5d270b2f9

Mechanisms of C9ORF72 pathogenicity and related autophagy impairment in amyotrophic lateral sclerosis

de Calbiac, H. (2019) · theses.fr (ABES) · doi:10.70675/bafe951fz8332z4b0azb55bzac8a4af1955b

Développement d’outils pour la caractérisation de la TDP-43 et exploration de marqueurs indirects dans un contexte de dégénérescence lobaire frontotemporale

Escal, J. (2021) · theses.fr (ABES) · doi:10.70675/c8b346f7zb4e3z43e0za63azb407baddab64

The C9orf72 dipeptide repeat protein poly-glycine-alanine sequesters nucleoporins and disrupts nuclear membranes

Richter, K. (2022) · theses.fr (ABES) · doi:10.70675/d4b295c1zf862z434dz9956z7eaa90a7d4a7

C9orf72-associated G4C2 hexanucleotide repeat expression in Drosophila mushroom bodies causes age-dependent TDP-43 pathology and dementia relevant phenotypes mediated in part by the glypican Dlp/GPC6

Chauhan, B. S., Brennan, M. A., Forstmeier, P. C., Han, Y., Godfrey, R. K., Keuren‐Jensen, K. R. V., Sattler, R., Ichida, J. K., & Zarnescu, D. C. (2026) · Acta Neuropathologica Communications · doi:10.64898/2026.05.08.723849

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

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

[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