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

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

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

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

Renton, A. E., Majounie, E., Waite, A., Simón-Sánchez, J., Rollinson, S., Gibbs, J. R., Schymick, J. C., Laaksovirta, H., van Swieten, J. C., Myllykangas, L., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.010 · Cited by 4,409

The C9orf72 GGGGCC Repeat Is Translated into Aggregating Dipeptide-Repeat Proteins in FTLD/ALS

Mori, K., Weng, S., Arzberger, T., May, S., Rentzsch, K., Kremmer, E., Schmid, B., Kretzschmar, H. A., Cruts, M., Broeckhoven, C. V., et al. (2013) · Science · doi:10.1126/science.1232927 · Cited by 1,248

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

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

GAL4 system in drosophila: A fly geneticist's swiss army knife

Duffy, J. B. (2002) · genesis · doi:10.1002/gene.10150 · Cited by 1,099

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

A Cross-Sectional Study

Drozdzowska, B., Pluskiewicz, W., Halaba, Z. P., Misiołek, H., & Beck, B. R. (2005) · Cited by 984

Non-ATG–initiated translation directed by microsatellite expansions

Zu, T., Gibbens, B. B., Doty, N. S., Gomes-Pereira, M., Huguet-Lachon, A., Stone, M. D., Margolis, J., Peterson, M., Markowski, T. W., Ingram, M. A. C., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1013343108 · Cited by 928

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

A conditional tissue-specific transgene expression system using inducible GAL4

Osterwalder, T., Yoon, K. S., White, B. H., & Keshishian, H. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.221303298 · Cited by 804

Toxic PR poly-dipeptides encoded by the C9orf72 repeat expansion target Kapβ2 and dysregulate phase separation of low-complexity domainsPreprint

Nanaura, H., Kawamukai, H., Fujiwara, A., Uehara, T., Nakanishi, M., Shiota, T., Hibino, M., Aiba, Y., Wiriyasermkul, P., Kikuchi, S., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/812099 · Cited by 2

Surface glia predominantly contribute to the development of ALS/FTD in Drosophila modelPreprint

Snow, B. A., Stevenson, C. C., Kaur, J., Lee, S. G., Wei, Y., Miao, H., & Kim, W. J. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.10.07.511246 · Cited by 2

Surface glia predominantly contribute to the development of ALS/FTD in Drosophila modelPreprint

Snow, B. A., Stevenson, C. C., Kaur, J., Lee, S. G., Wei, Y., Miao, H., & Kim, W. J. (2022) · Research Square · doi:10.21203/rs.3.rs-2259679/v1 · Cited by 2

Generation of C9orf72 h370 mice, an intron 1 humanised C9orf72 repeat-expansion knock-in modelPreprint

Nair, R., Carcolé, M., Thompson, D., Tibbit, C., McLeod, R., Cammack, A. J., Jakubcova, T., Biggs, D., Wyles, M., Parker, M. T., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.06.636691 · Cited by 2

Aggregates associated with amyotrophic lateral sclerosis sequester the actin-binding protein profilin 2

Kubinski, S., Claus, L., Schüning, T., Zeug, A., Kalmbach, N., Staege, S., Gschwendtberger, T., Petri, S., Wegner, F., Claus, P., et al. (2025) · Human Molecular Genetics · doi:10.1093/hmg/ddaf020 · Cited by 1

Synaptic defects in adult drosophila motor neurons in a model of amyotrophic lateral sclerosis

Malik, T., Sidisky, J. M., Jones, S., Winters, A., Hocking, B., Rotay, J., Huhulea, E. N., Moran, S., Connors, B., & Babcock, D. T. (2025) · Human Molecular Genetics · doi:10.1093/hmg/ddaf068 · Cited by 1

Patient-derived induced pluripotent stem cells with a C9orf72 expansion as a model to study frontotemporal dementia pathologies

Infante-Tadeo, S., & Barber, D. L. (2025) · Molecular Biology of the Cell · doi:10.1091/mbc.e24-12-0539 · Cited by 2

The telomeric valine–arginine dipeptide repeat protein changes state to diffuse staining in mitosis and represses in vitro translation

Al-Turki, T. M., Mantri, V., Willcox, S., Mills, C. A., Herring, L. E., Cho, S.-J., Lee, H., Meyer, C., Anton, E. S., & Griffith, J. D. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2520441122 · Cited by 1

G-Quadruplexes Abet Neuronal Burnout in ALS and FTD

Herbert, A. G. (2025) · Antioxidants · doi:10.3390/antiox15010005 · Cited by 1

The intrinsic disorder challenge for AlphaFold: A case study of G3BP1 and pathogenic peptide

Li, Y., Yao, Z., Song, Z., Yang, P., Huang, J., Lei, K., & Xu, Y. C. (2026) · iScience · doi:10.1016/j.isci.2026.115737 · Cited by 1

Targeting the integrated stress response or Ataxin-2 alleviates neurodegeneration in PolyGR models of C9orf72 associated frontotemporal dementia and amyotrophic lateral sclerosis

Harper, N. S., Sharpe, J. L., Speranza, J., Gulia, R., Chen, J. X., Allen, S. P., Atwal, M. S., Pickering-Brown, S. M., Livesey, M. R., Bennett, C. L., et al. (2026) · Acta Neuropathologica Communications · doi:10.1186/s40478-026-02301-2 · Cited by 2

Molecular Pathways Leading to the Clinical Phenomenology of Frontotemporal Dementia

Yokoyama, J. S., & Lee, S. E. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-800105-9.00033-0 · Cited by 1

A human cellular model of amyotrophic lateral sclerosis

Marton, R. M., & Pașca, S. P. (2018) · Nature Medicine · doi:10.1038/nm.4509 · Cited by 1

Notch Signaling: From Neurogenesis to Neurodegeneration

Sachan, N., Mutsuddi, M., & Mukherjee, A. (2019) · Springer eBooks · doi:10.1007/978-981-13-2218-1_7 · Cited by 1

Antisense oligonucleotide drugs for neurological and neuromuscular disease

Lane, R. M., & Bennett, C. F. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-813955-4.00017-9 · Cited by 1

Intricate roles of spacers and stickers of Arg-rich C9ORF72 dipeptide repeat proteins; from toxicity to targeting to membraneless organelles

Miyagi, T., & Kanekura, K. (2023) · Organelle · doi:10.61747/0ifp.202311001 · Cited by 1

Mapping of repeat-associated non-AUG (RAN) translation knowledge: A bibliometric analysis

Zhao, T., Duan, S., Li, J., Zheng, H., Liu, C., Zhang, H., Luo, H., & Xu, Y. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e29141 · Cited by 1

A bacterial artificial chromosome mouse model of amyotrophic lateral sclerosis manifests ‘space cadet syndrome’ on two FVB backgrounds

Badger, S. E., Coldicott, I., Kyrgiou-Balli, E., Higginbottom, A., Moutin, C., Imran, K. M., Day, J. C. C., Cooper‐Knock, J., Mead, R. J., & Alix, J. J. P. (2025) · Disease Models & Mechanisms · doi:10.1242/dmm.052221 · Cited by 1

Antisense Oligonucleotides for Amyotrophic Lateral Sclerosis

Smith, S., & Miller, T. M. (2025) · Springer eBooks · doi:10.1007/978-3-031-89307-0_11 · 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

Amyotrophic Lateral Sclerosis

Osafo, N., Obiri, D. D., Yeboah, K. O., & Minkah, P. A. B. (2018) · Advances in medical diagnosis, treatment, and care (AMDTC) book series · doi:10.4018/978-1-5225-5282-6.ch015 · Cited by 1

Understanding Neurodegeneration and Neuroprotection Through Genetic Screens in Drosophila

Mandya, A. S., Cheramangalam, R. N., & Jaiswal, M. (2019) · Springer eBooks · doi:10.1007/978-981-13-2218-1_3 · 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

Intrinsic determinants of prion protein neurotoxicity in Drosophila: from sequence to (dys)function

Cembran, A., & Fernández-Fúnez, P. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1231079 · 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

Cellular Uptake Mechanisms of Arginine‐Rich Cell‐Penetrating Peptides

Nakase, I. (2022) · Wiley eBooks · doi:10.1002/9783527835997.ch9 · Cited by 1

CLIP-Seq Analysis Enables the Design of Ribosomal RNA Bait Oligonucleotides That Protect Against C9ORF72 ALS/FTD-Associated Poly-GR PathophysiologyPreprint

Ortega, J. A., Sasselli, I. R., Boccitto, M., Fleming, A. C., Fortuna, T. R., Li, Y., Sato, K., Clemons, T. D., Daley, E. L., Nguyen, T. P., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.12.30.522259 · 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

Pinpointing protein as the problem

Arnold, F. J., & Spada, A. R. L. (2026) · Science · doi:10.1126/science.aee6924 · Cited by 1

A Chemical Inducer of Ribophagy Limits the Toxicity of ALS-Related Arginine-Rich PeptidesPreprint

Porębski, B., Lafarga, V., Hansel, C. S., Haraldsson, M., Sáez-Mas, A., Sánchez-Molleda, Á., Moragón, S., Häggblad, M., Lidemalm, L., Rodrigo, S., et al. (2026) · SSRN Electronic Journal · doi:10.2139/ssrn.7284617 · 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

A new topical gene C9orf72 in neurodegenerative diseases

Asai, M. (2015) · Folia Pharmacologica Japonica · doi:10.1254/fpj.145.44

Modelling C9orf72-linked frontotemporal dementia and amyotrophic lateral sclerosis

Ryan, S. (2015) · Research Explorer (The University of Manchester)

Ny viten om nevrodegenerative mekanismer

Haugen, T. B. (2014) · Tidsskrift for Den norske legeforening · doi:10.4045/tidsskr.14.1015

C9orF72 RAN Proteins Detected in ALS CSF, Reduced In Vitro with Small Molecules

Robinson, R. (2014) · Neurology Today · doi:10.1097/01.nt.0000455664.13637.f2

The genetic basis of amyotrophic lateral sclerosis: recent breakthroughs

Leuven, K. (2015)

A survey of axonal transport function and motor behaviour in Drosophila models of amyotrophic lateral sclerosis

Baldwin, K. R. (2015) · White Rose eTheses Online (University of Leeds, The University of Sheffield, University of York)

Antisense Oligonucleotides for Amyotrophic Lateral Sclerosis

Self, W. K., & Miller, T. M. (2016) · Springer eBooks · doi:10.1007/978-1-4899-7654-3_6

The role of the nucleolus in neurodegeneration.

Hallgren, J. (2016) · doi:10.18297/etd/2547

Phosphorylation of tau protein at Thr175 is a toxic event associated with neurodegeneration

Moszczynski, A. J. (2017) · Scholarship@Western (Western University)

Repeat expansions in myoclonic epilepsy

van Blitterswijk, M., & Rademakers, R. (2018) · Nature Genetics · doi:10.1038/s41588-018-0093-0

C9orf72 expansions disrupt ATM-mediated DNA repair

Walker, C. (2018) · White Rose eTheses Online (University of Leeds, The University of Sheffield, University of York)

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

Presynaptic depression maintains stable synaptic strength in developmentally arrested Drosophila larvaePreprint

Perry, S., Goel, P., Miller, D. L., Ganetzky, B., & Dickman, D. K. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/840470

Understanding Motor Disorders Using Flies

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

Regulation of intracellular traffic by TBK1 and its relevance to ALS

Villarroel‐Campos, D. (2020) · UCL Discovery (University College London)

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

In vivo CGG repeat RNA binding protein capture identifies RAN translation modifiers and suppressors of repeat toxicityPreprint

Malik, I., Tseng, Y., Wright, S. E., Zheng, K., Ramaiyer, P., Green, K. M., & Todd, P. K. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.08.425998

Lost in Translation: Variations in WNT Signaling and Other Translational Changes in a Drosophila Model of ALS

Lehmkuhl, E. M. (2021) · UA Campus Repository (The University of Arizona)

Neurons undergo pathogenic metabolic reprograming in models of familial ALSPreprint

Riechers, S., Mojsilovic‐Petrovic, J., Garjani, M., Medvedeva, V., Dalton, C., Dienel, G. A., & Kalb, R. G. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.08.20.457111

C9orf72 -derived poly-GA DPRs undergo endocytic uptake in iNPC-derived astrocytes and spread to motor neuronsPreprint

Marchi, P. M., Marrone, L., Brasseur, L., Bousset, L., Webster, C. P., Destro, M., Smith, E. F., Walther, C. G., Alfred, V., Marroccella, R., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.11.463891

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

Theme 3 In vivo experimental models

(2018) · Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration · doi:10.1080/21678421.2018.1510570

Faculty Opinions recommendation of Novel antibodies reveal presynaptic localization of C9orf72 protein and reduced protein levels in C9orf72 mutation carriers.

Fisher, E. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733757974.793549156

FUS regulates RAN translation through modulating the G-quadruplex structure of GGGGCC repeat RNA in C9orf72-linked ALS/FTDPreprint

Fujino, Y., Ueyama, M., Ishiguro, T., Ozawa, D., Sugiki, T., Ito, H., Murata, A., Ishiguro, A., Gendron, T. F., Mori, K., et al. (2023) · eLife · doi:10.7554/elife.84338.1

Inhibiting toxicity of ALS-linked dipeptide repeat proteins by polystyrene sulfonate (PSS)Preprint

Bratek‐Skicki, A., Ahmed, J., Lindt, J. V., Jonckheere, K., Peeters, E., Heeren, K., Fakhri, F., Volkov, A., Hendrix, J., Batys, P., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.19.541518 · Cited by 1

Reconstitution of C9orf72 (GGGGCC) repeat-associated non-AUG translation with purified componentsPreprint

Ito, H., Machida, K., Ueyama, M., Nagai, Y., Imataka, H., & Taguchi, H. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.29.542719

FUS regulates RAN translation through modulating the G-quadruplex structure of GGGGCC repeat RNA in C9orf72-linked ALS/FTDPreprint

Fujino, Y., Ueyama, M., Ishiguro, T., Ozawa, D., Ito, H., Sugiki, T., Murata, A., Ishiguro, A., Gendron, T. F., Mori, K., et al. (2023) · eLife · doi:10.7554/elife.84338.2

G 2 C 4 targeting antisense oligonucleotides potently mitigate TDP-43 dysfunction in C9orf72 ALS/FTD human neuronsPreprint

Rothstein, J. D., Baskerville, V., Rapuri, S., Mehlhop, E., Jafar‐Nejad, P., Rigo, F., Bennett, F., Mizielinska, S., Isaacs, A. M., & Coyne, A. N. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.26.546581

PolyGR and polyPR knock-in mice reveal a conserved neuroprotective extracellular matrix signature in C9orf72 ALS/FTD neuronsPreprint

Milioto, C., Carcolé, M., Giblin, A., Coneys, R., Attrebi, O. N., Ahmed, M., Harris, S., Lee, B. I., Yang, M., Nirujogi, R. S., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.07.17.549331

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

Mitigation of TDP-43-induced toxic phenotype by expression of RGNEF N-terminal fragment in ALS modelsPreprint

Droppelmann, C. A., Campos‐Melo, D., Noches, V., McLellan, C., Szabla, R., Lyons, T. A., Amzil, H., Withers, B., Sonkar, K. S., Simon, A. F., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.29.560207

Antisense RNA C9orf72 Hexanucleotide Repeat Associated With Amyotrophic Lateral Sclerosis and Frontotemporal Dementia Forms A Triplex-Like Structure and Binds Small Synthetic LigandPreprint

Błaszczyk, L., Ryczek, M., Das, B., Mateja-Pluta, M., Bejger, M., Nakatani, K., & Kiliszek, A. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.10.10.561654

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

Editorial: Molecular mechanisms underlying C9orf72 neurodegeneration, volume II

Gallo, J., Nishimura, A. L., & Haapasalo, A. (2024) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1357319

Repeat-associated non-AUG (RAN) translation and Huntington's disease: Pathology, mechanistic and therapeutic perspectives

Báñez-Coronel, M., Cleary, J. D., & Ranum, L. P. W. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-95672-7.00011-x

Conserved loop of a phase modifier endows protein condensates with fluidityPreprint

Kawamukai, H., Matsusaki, M., Tanimoto, T., Watabe, M., Morishima, K., Tomita, S., Shinkai, Y., Niwa, T., Mannen, T., Kumeta, H., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.03.601791

The valine-arginine dipeptide repeat protein encoded by mammalian telomeric RNA appears highly expressed in mitosis and may repress global translationPreprint

Al-Turki, T. M., Mantri, V., Willcox, S., Mills, C. A., Herring, L. E., Cho, S.-J., Lee, H., Meyer, C., Anton, E. S., & Griffith, J. D. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.24.604971

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

A robust evaluation of TDP-43, poly GP, cellular pathology and behavior in a AAV-C9ORF72 (G 4 C 2 ) 66 mouse modelPreprint

Thompson, E. G., Spead, O., Åkerman, S., Curcio, C., Zaepfel, B. L., Kent, E. R., Philips, T., Vijayakumar, B. G., Zacco, A., Zhou, W., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.27.607409

Studying C9orf72 dipeptide repeat polypeptide aggregation using an analytical ultracentrifuge equipped with fluorescence detection

Kokona, B., Cunningham, N. R., Quinn, J. M., Jacobsen, D. R., Garcia, F. J., Galindo, S. M., Petrucelli, L., Stafford, W. F., Laue, T. M., & Fairman, R. (2024) · Analytical Biochemistry · doi:10.1016/j.ab.2024.115720

Patient-derived Induced Pluripotent Stem Cells as a Model to Study Frontotemporal Dementia PathologiesPreprint

Infante-Tadeo, S., & Barber, D. L. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.11.628042

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

C9orf72 polyGA knock-in mice exhibit mild motor and proteomic changes consistent with ALS/FTDPreprint

Milioto, C., Carcolé, M., Zanovello, M., Ahmed, M., Nirujogi, R. S., Biggs, D., Katona, E., Glaria, I., Santos, A., Devoy, A., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.30.656994

Membrane Disruption Properties of Poly-Glycine Arginine Dipeptide Repeats Affected by Peptide Repeats Continuity and Membrane Composition

Ho, C.-Y., Chang, Y., Yang, C.-W., Shih, O., Jeng, U., Hwang, I., Huang, W., & Chen, Y. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169296

Mechanistic insights into RAN translation within the Huntingtin coding sequencePreprint

Krans, A., Albertson, R. M., Maltby, C. J., & Todd, P. K. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.02.673827

Recent Advancements in 20S Proteasome Enhancement: Degradation of Undruggable Targets

Cobb, S. G., & Tepe, J. J. (2025) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5c00451

Protein tandem repeats that produce frameshifts can generate new structural states and functions

Osmanli, Z., Aldrian, G., Leclercq, J., Falgarone, T., Gómez Bergna, S. M., Prada Gori, D. N., Oleinikov, A. V., Shahmuradov, I., & Kajava, A. V. (2026) · The FEBS Journal · doi:10.1111/febs.70273

Glial cell-intrinsic and non-cell autonomous toxicity in a Drosophila C9orf72 neurodegeneration modelPreprint

Hubbard, I., & Dubnau, J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.07.680869

RNA regulates repeat-associated non-AUG (RAN) translation initiation in C9orf72 FTD/ALSPreprint

Grosely, R., Yamada, S. B., Puglisi, A. V., Palo, M. Z., Alvarado, C., Lapointe, C. P., Gitler, A. D., & Puglisi, J. D. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.09.681477 · Cited by 1

Genetically Modified Primate Models for Brain Disorder Research

Yang, Y., Lin, J., Li, M., Yang, L., Lu, Z., & Yan, T. (2025) · Neuroscience Bulletin · doi:10.1007/s12264-025-01529-7

CRISPR/Cas9-mediated generation of a de novo C9ORF72 knock-in isogenic iPSC cell bank to model ALS and FTDPreprint

O’Brien, N. L., Hedges, E. C., Nair, R., Cammack, A. J., Carcolé, M., Vaizoglu, D., Tacconelli, S., Sutherland, K., Fisher-Ward, C. L., Awan, A. R., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.12.687564

CANVAS causing AAGGG repeat expansions cause tissue-specific reduction in RFC1 expression and increase sensitivity to DNA damagePreprint

Curró, R., Dominik, N., Facchini, S., Schnekenberg, R. P., Perini, C., Ronco, R., Rugginini, B., Ghia, A., Bione, S., Tagliaferri, N., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.18.688292

The molecular mechanism of uptake and cell-to-cell transmission of arginine-containing dipeptide repeat proteinsPreprint

Sutter, A. B., Buksh, B. F., Mojsilovic‐Petrovic, J., Dalton, C., Till, N. A., Morgan, D. C., MacMillan, D. W. C., & Kalb, R. G. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.25.690484

A fly model of SCA36 reveals combinatorial neurotoxicity of hexanucleotide and dipeptide repeats

Hsiao, C.-T., Fu, S., Guo, T.-N., Lin, C., Tsao, Y.-J., Chang, W., Liao, Y., Hashimoto, M., Huang, S., Lee, Y., et al. (2025) · PLoS Genetics · doi:10.1371/journal.pgen.1011954

Physiological function of FUS: An RNA binding protein in motor neuron disease

Yang, L. (2015) · UKnowledge (University of Kentucky)

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 10 of SRSF1-dependent inhibition of C9ORF72-repeat RNA nuclear export: genome-wide mechanisms for neuroprotection in amyotrophic lateral sclerosis

Castelli, L. M., Cutillo, L., Souza, C. D. S., Sánchez-Martínez, Á., Granata, I., Lin, Y.-H., Myszczynska, M. A., Heath, P. R., Livesey, M. R., Ning, K., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15145929

Additional file 8 of SRSF1-dependent inhibition of C9ORF72-repeat RNA nuclear export: genome-wide mechanisms for neuroprotection in amyotrophic lateral sclerosis

Castelli, L. M., Cutillo, L., Souza, C. D. S., Sánchez-Martínez, Á., Granata, I., Lin, Y.-H., Myszczynska, M. A., Heath, P. R., Livesey, M. R., Ning, K., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15145995

Additional file 19 of SRSF1-dependent inhibition of C9ORF72-repeat RNA nuclear export: genome-wide mechanisms for neuroprotection in amyotrophic lateral sclerosis

Castelli, L. M., Cutillo, L., Souza, C. D. S., Sánchez-Martínez, Á., Granata, I., Lin, Y.-H., Myszczynska, M. A., Heath, P. R., Livesey, M. R., Ning, K., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15145956

Additional file 1 of SRSF1-dependent inhibition of C9ORF72-repeat RNA nuclear export: genome-wide mechanisms for neuroprotection in amyotrophic lateral sclerosis

Castelli, L. M., Cutillo, L., Souza, C. D. S., Sánchez-Martínez, Á., Granata, I., Lin, Y.-H., Myszczynska, M. A., Heath, P. R., Livesey, M. R., Ning, K., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15145959

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 22 of SRSF1-dependent inhibition of C9ORF72-repeat RNA nuclear export: genome-wide mechanisms for neuroprotection in amyotrophic lateral sclerosis

Castelli, L. M., Cutillo, L., Souza, C. D. S., Sánchez-Martínez, Á., Granata, I., Lin, Y.-H., Myszczynska, M. A., Heath, P. R., Livesey, M. R., Ning, K., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15145968

Additional file 1 of BET bromodomain inhibitors PFI-1 and JQ1 are identified in an epigenetic compound screen to enhance C9ORF72 gene expression and shown to ameliorate C9ORF72-associated pathological and behavioral abnormalities in a C9ALS/FTD model

Quezada, E. R., Cappelli, C., Díaz, I. D. P., Jury, N., Wightman, N., Brown, R. H., Montecino, M. A., & van Zundert, B. (2021) · Figshare · doi:10.6084/m9.figshare.14227789

Additional file 1 of Conformational dynamics in the disordered region of human CPEB3 linked to memory consolidation

de Mingo, D. R., Pantoja‐Uceda, D., Hervás, R., Carrión-Vázquez, M., & Laurents, D. V. (2022) · Figshare · doi:10.6084/m9.figshare.19993904

Additional file 12 of SRSF1-dependent inhibition of C9ORF72-repeat RNA nuclear export: genome-wide mechanisms for neuroprotection in amyotrophic lateral sclerosis

Castelli, L. M., Cutillo, L., Souza, C. D. S., Sánchez-Martínez, Á., Granata, I., Lin, Y.-H., Myszczynska, M. A., Heath, P. R., Livesey, M. R., Ning, K., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15145935

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 16 of SRSF1-dependent inhibition of C9ORF72-repeat RNA nuclear export: genome-wide mechanisms for neuroprotection in amyotrophic lateral sclerosis

Castelli, L. M., Cutillo, L., Souza, C. D. S., Sánchez-Martínez, Á., Granata, I., Lin, Y.-H., Myszczynska, M. A., Heath, P. R., Livesey, M. R., Ning, K., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15145947

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

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 72

Molecular mechanisms of pathogenesis in Drosophila models of C9orf72 mutation associated ALS/FTD

Moens, T. G. (2018) · UCL Discovery (University College London)

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 75

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 263

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