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

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

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

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

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

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Unconventional Translation of C9ORF72 GGGGCC Expansion Generates Insoluble Polypeptides Specific to c9FTD/ALS

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A Cross-Sectional Study

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Non-ATG–initiated translation directed by microsatellite expansions

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RNA Toxicity from the ALS/FTD C9ORF72 Expansion Is Mitigated by Antisense Intervention

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A conditional tissue-specific transgene expression system using inducible GAL4

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Type I PRMT Inhibition Protects Against C9ORF72 Arginine-Rich Dipeptide Repeat Toxicity

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Inducible expression of human C9ORF72 36× G4C2 hexanucleotide repeats is sufficient to cause RAN translation and rapid muscular atrophy in mice

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Disease Mechanisms and Therapeutic Approaches in C9orf72 ALS-FTD

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Exploring the alternative: Fish, flies and worms as preclinical models for ALS

Braems, E., Tziortzouda, P., & Bosch, L. V. D. (2021) · Neuroscience Letters · doi:10.1016/j.neulet.2021.136041 · Cited by 20

Synaptopathy Mechanisms in ALS Caused by C9orf72 Repeat Expansion

Nishimura, A. L., & Arias, N. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.660693 · Cited by 17

Aberrant splicing exonizes C9orf72 repeat expansion in ALS/FTD

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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

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Translation of the poly(GR) frame in C9ORF72-ALS/FTD is regulated by cis-elements involved in alternative splicing

Lampasona, A. A., Almeida, S., & Gao, F. (2021) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2021.04.030 · Cited by 16

Poly-dipeptides produced from C9orf72 hexanucleotide repeats cause selective motor neuron hyperexcitability in ALS

Jo, Y., Lee, J., Lee, S.-Y., Kwon, I., & Cho, H. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2113813119 · Cited by 16

A cell-penetrant peptide blocking C9ORF72 -repeat RNA nuclear export reduces the neurotoxic effects of dipeptide repeat proteins

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Mitigation of TDP-43 toxic phenotype by an RGNEF fragment in amyotrophic lateral sclerosis models

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Catastrophic cliffs: a partial suggestion for selective vulnerability in neurodegenerative diseases

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Epigenetic Regulation of ALS and CMT: A Lesson from Drosophila Models

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Metabolomics: A Tool to Understand the Impact of Genetic Mutations in Amyotrophic Lateral Sclerosis

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Chemical chaperones targeted to the endoplasmic reticulum (ER) and lysosome prevented neurodegeneration in a C9orf72 repeat expansion drosophila amyotrophic lateral sclerosis (ALS) model

Azoulay‐Ginsburg, S., Salvio, M. D., Weitman, M., Afri, M., Ribeiro, S. S., Ebbinghaus, S., Cestra, G., & Gruzman, A. (2021) · Pharmacological Reports · doi:10.1007/s43440-021-00226-2 · Cited by 16

Therapeutic reduction of GGGGCC repeat RNA levels by hnRNPA3 suppresses neurodegeneration in Drosophila models of C9orf72 -linked ALS/FTD

Taminato, T., Takeuchi, T., Ueyama, M., Mori, K., Ikeda, M., Mochizuki, H., & Nagai, Y. (2022) · Human Molecular Genetics · doi:10.1093/hmg/ddac298 · Cited by 14

Translation of dipeptide repeat proteins in C9ORF72 ALS/FTD through unique and redundant AUG initiation codons

Sonobe, Y., Lee, S., Krishnan, G., Gu, Y., Kwon, D. Y., Gao, F., Roos, R. P., & Kratsios, P. (2023) · eLife · doi:10.7554/elife.83189 · Cited by 15

A monocarboxylate transporter rescues frontotemporal dementia and Alzheimer’s disease models

Xu, D., Vincent, A. J., González‐Gutiérrez, A., Aleyakpo, B., Anoar, S., Giblin, A., Atilano, M. L., Adams, M. L., Shen, D., Thoeng, A., et al. (2023) · PLoS Genetics · doi:10.1371/journal.pgen.1010893 · Cited by 15

Interaction-Dependent Secondary Structure of Peptides in Biomolecular Condensates

Lorenz-Ochoa, K. A., Cho, M., Parekh, S. H., & Baiz, C. R. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.4c11226 · Cited by 15

Modelling C9orf72-Related Amyotrophic Lateral Sclerosis in Zebrafish

Fortier, G., Butti, Z., & Patten, S. A. (2020) · Biomedicines · doi:10.3390/biomedicines8100440 · Cited by 15

Measuring and Interpreting Nuclear Transport in Neurodegenerative Disease—The Example of C9orf72 ALS

Semmelink, M. F. W., Steen, A., & Veenhoff, L. M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179217 · Cited by 15

Neurons undergo pathogenic metabolic reprogramming in models of familial ALS

Riechers, S., Mojsilovic‐Petrovic, J., Belton, T. B., Chakrabarty, R. P., Garjani, M., Medvedeva, V., Dalton, C., Wong, Y. C., Chandel, N. S., Dienel, G. A., et al. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101468 · Cited by 16

Differential toxicity and localization of arginine-rich C9ORF72 dipeptide repeat proteins depend on de-clustering of positive charges

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Repeated repeat problems: Combinatorial effect of C9orf72-derived dipeptide repeat proteins

Darling, A. L., Breydo, L., Rivas, E. G., Gebru, N. T., Zheng, D., Baker, J. D., Blair, L. J., Dickey, C. A., Koren, J., & Uversky, V. N. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.01.035 · Cited by 16

Elucidating the Role of Cerebellar Synaptic Dysfunction in C9orf72-ALS/FTD — a Systematic Review and Meta-Analysis

Kaliszewska, A., Allison, J., Col, T.-T., Shaw, C. E., & Arias, N. (2021) · The Cerebellum · doi:10.1007/s12311-021-01320-0 · Cited by 15

C9orf72-linked arginine-rich dipeptide repeats aggravate pathological phase separation of G3BP1

Nerom, M. V., Ahmed, J., Lázár, T., Mészáros, A., Galand, Q., Malsche, W. D., Lindt, J. V., Pancsa, R., Maes, D., & Tompa, P. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2402847121 · Cited by 14

Amyotrophic Lateral Sclerosis Model

Azuma, Y., Mizuta, I., Tokuda, T., & Mizuno, T. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-0529-0_6 · Cited by 15

Review: Modelling the pathology and behaviour of frontotemporal dementia

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Smcr8 deficiency disrupts axonal transport-dependent lysosomal function and promotes axonal swellings and gain of toxicity in C9ALS/FTD mouse models

Chen, L., Shao, Q., Zhang, W., Yang, M., Chang, Q., Chen, R., & Chen, J. (2020) · Human Molecular Genetics · doi:10.1093/hmg/ddaa012 · Cited by 14

Primary Neurons and Differentiated NSC-34 Cells Are More Susceptible to Arginine-Rich ALS Dipeptide Repeat Protein-Associated Toxicity than Non-Differentiated NSC-34 and CHO Cells

Gill, A. L., Wang, M. Z., Levine, B. A., Premasiri, A. S., & Vieira, F. G. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20246238 · Cited by 14

Correlation between C9ORF72 mutation and neurodegenerative diseases: A comprehensive review of the literature

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Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry Imaging of Phospholipid Changes in a Drosophila Model of Early Amyotrophic Lateral Sclerosis

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Regulating Phase Transition in Neurodegenerative Diseases by Nuclear Import Receptors

Girdhar, A., & Guo, L. E. (2022) · Biology · doi:10.3390/biology11071009 · Cited by 15

Aberrant Rna Homeostasis in Amyotrophic Lateral Sclerosis: Potential for New Therapeutic targets?

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CRISPR-Cas9 targeted deletion of the C9orf72 repeat expansion mutation corrects cellular phenotypes in patient-derived iPS cellsPreprint

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Rapid cell type-specific nascent proteome labeling in Drosophila

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

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Drosophila melanogaster as a Tool for Amyotrophic Lateral Sclerosis Research

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Loss of TMEM106B exacerbates C9ALS/FTD DPR pathology by disrupting autophagosome maturation

Bauer, C. S., Webster, C. P., Shaw, A. C., Kok, J. R., Castelli, L. M., Lin, Y.-H., Smith, E. F., Illanes-Álvarez, F., Higginbottom, A., Shaw, P. J., et al. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.1061559 · Cited by 15

Promising animal models for amyotrophic lateral sclerosis drug discovery: a comprehensive update

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Tau Accumulation via Reduced Autophagy Mediates GGGGCC Repeat Expansion-Induced Neurodegeneration in Drosophila Model of ALS

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Drosophila as a Model to Gain Insight into the Role of lncRNAs in Neurological Disorders

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Molecular Dynamics Study of Structure, Folding, and Aggregation of Poly-PR and Poly-GR Proteins

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Heat-shock chaperone HSPB1 mitigates poly-glycine-induced neurodegeneration via restoration of autophagic flux

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Cryptic intronic transcriptional initiation generates efficient endogenous mRNA templates for C9orf72-associated RAN translation

Miller, S. L., Green, K. M., Crone, B., Switzenberg, J. A., Tank, E. M. H., Krans, A., Jansen‐West, K. R., Wieland, C. M., Ji, E. W., Petrucelli, L., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2507334122 · Cited by 12

Amyotrophic lateral sclerosis

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The Interplay Between Autophagy and RNA Homeostasis: Implications for Amyotrophic Lateral Sclerosis and Frontotemporal Dementia

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Comprehensive evaluation of human-derived anti-poly-GA antibodies in cellular and animal models of C9orf72 disease

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C9orf72 protein quality control by UBR5‐mediated heterotypic ubiquitin chains

Jülg, J., Edbauer, D., & Behrends, C. (2023) · EMBO Reports · doi:10.15252/embr.202255895 · Cited by 11

ALS’ Perfect Storm: C9orf72-Associated Toxic Dipeptide Repeats as Potential Multipotent Disruptors of Protein Homeostasis

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eIF5 stimulates the CUG initiation of RAN translation of poly-GA dipeptide repeat protein (DPR) in C9orf72 FTLD/ALS

Gotoh, S., Mori, K., Fujino, Y., Kawabe, Y., Yamashita, T., Omi, T., Nagata, K., Tagami, S., Nagai, Y., & Ikeda, M. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105703 · Cited by 12

Zfp106 binds to G-quadruplex RNAs and inhibits RAN translation and formation of RNA foci caused by G4C2 repeats

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Targeting EGLN2/PHD1 protects motor neurons and normalizes the astrocytic interferon response

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Problems at the nuclear pore

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Targeting RNA G‐quadruplexes as new treatment strategy for C9orf72 ALS/FTD

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Dissecting Motor Neuron Disease With Drosophila melanogaster

Walters, R., Manion, J., & Neely, G. G. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00331 · Cited by 12

The progress inC9orf72research: ALS/FTD pathogenesis, functions and structure

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Hypothesis and Theory: Roles of Arginine Methylation in C9orf72-Mediated ALS and FTD

Gill, A. L., Premasiri, A. S., & Vieira, F. G. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.633668 · Cited by 12

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

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C9ORF72 knockdown triggers FTD-like symptoms and cell pathology in mice

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CLIP-Seq analysis enables the design of protective ribosomal RNA bait oligonucleotides against C9ORF72 ALS/FTD poly-GR pathophysiology

Ortega, J. A., Sasselli, I. R., Boccitto, M., Fleming, A. C., Fortuna, T. R., Li, Y., Sato, K., Clemons, T. D., McKenna, E. D., Nguyen, T. P., et al. (2023) · Science Advances · doi:10.1126/sciadv.adf7997 · Cited by 15

Repeat Expansion Disease Models

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A synthetic Pur-based peptide binds and alters G-quadruplex secondary structure present in the expanded RNA repeat of C9orf72 ALS/FTD

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Reduction of oxidative stress suppresses poly-GR-mediated toxicity in zebrafish embryos

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C9ORF72-derived poly-GA DPRs undergo endocytic uptake in iAstrocytes and spread to motor neurons

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Clogging information flow in ALS

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NeuroLINCS Proteomics: Defining human-derived iPSC proteomes and protein signatures of pluripotency

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Disrupted endoplasmic reticulum-mediated autophagosomal biogenesis in a Drosophila model of C9-ALS-FTD

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C9orf72 dipeptides activate the NLRP3 inflammasome

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Distinct neurological disorders with C9orf72 mutations: genetics, pathogenesis, and therapy

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Amyotrophic Lateral Sclerosis-associated GGGGCC repeat expansion promotes Tau phosphorylation and toxicity

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The nuclear ubiquitin ligase adaptor SPOP is a conserved regulator of C9orf72 dipeptide toxicity

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Amyotrophic Lateral Sclerosis Risk Genes and Suppressor

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Dipeptide repeat protein toxicity in frontotemporal lobar degeneration and in motor neurone disease associated with expansions in C9ORF72—a cautionary note

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