Loss of function of C9orf72 causes motor deficits in a zebrafish model of amyotrophic lateral sclerosis

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

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

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TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia

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Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration

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A C9orf72 promoter repeat expansion in a Flanders-Belgian cohort with disorders of the frontotemporal lobar degeneration-amyotrophic lateral sclerosis spectrum: a gene identification study

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Distinct clinical and pathological characteristics of frontotemporal dementia associated with C9ORF72 mutations

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Gain and loss of function of ALS-related mutations of TARDBP (TDP-43) cause motor deficits in vivo

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Advances in understanding the molecular basis of frontotemporal dementia

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Large C9orf72 Hexanucleotide Repeat Expansions Are Seen in Multiple Neurodegenerative Syndromes and Are More Frequent Than Expected in the UK Population

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Motor Neuron dysfunction in frontotemporal dementia

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

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EPHA4 is a disease modifier of amyotrophic lateral sclerosis in animal models and in humans

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FUS and TARDBP but Not SOD1 Interact in Genetic Models of Amyotrophic Lateral Sclerosis

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Phenotype difference between ALS patients with expanded repeats in C9ORF72 and patients with mutations in other ALS-related genes

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Repeat Associated Non-ATG Translation Initiation: One DNA, Two Transcripts, Seven Reading Frames, Potentially Nine Toxic Entities!

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C9ORF72 Repeat Expansions in the Frontotemporal Dementias Spectrum of Diseases: A Flow-chart for Genetic Testing

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Methylene Blue Protects against TDP-43 and FUS Neuronal Toxicity in C. elegans and D. rerio

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

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Early interneuron dysfunction in ALS: Insights from a mutant sod1 zebrafish model

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Calcium Channel Agonists Protect against Neuromuscular Dysfunction in a Genetic Model of TDP-43 Mutation in ALS

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In the swim of things: recent insights to neurogenetic disorders from zebrafish

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RNA That Gets RAN in Neurodegeneration

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Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis

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

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C9orf72-mediated ALS and FTD: multiple pathways to disease

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Targeting RNA Foci in iPSC-Derived Motor Neurons from ALS Patients with a <i>C9ORF72</i> Repeat Expansion

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Targeted degradation of sense and antisense C9orf72 RNA foci as therapy for ALS and frontotemporal degeneration

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Gain of toxicity from ALS/FTD-linked repeat expansions in C9ORF72 is alleviated by antisense oligonucleotides targeting GGGGCC-containing RNAs

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Antisense Proline-Arginine RAN Dipeptides Linked to C9ORF72-ALS/FTD Form Toxic Nuclear Aggregates that Initiate In Vitro and In Vivo Neuronal Death

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CpG and non-CpG methylation in epigenetic gene regulation and brain function

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Loss of C9ORF72 impairs autophagy and synergizes with polyQ Ataxin‐2 to induce motor neuron dysfunction and cell death

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The C9orf72 protein interacts with Rab1a and the ULK1 complex to regulate initiation of autophagy

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C9orf72 BAC Mouse Model with Motor Deficits and Neurodegenerative Features of ALS/FTD

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The frontotemporal dementia-motor neuron disease continuum

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Inflammation in ALS/FTD pathogenesis

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

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C9orf72 BAC Transgenic Mice Display Typical Pathologic Features of ALS/FTD

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

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Neuroinflammation in frontotemporal dementia

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

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

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C 9orf72 ablation in mice does not cause motor neuron degeneration or motor deficits

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

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Human C9ORF72 Hexanucleotide Expansion Reproduces RNA Foci and Dipeptide Repeat Proteins but Not Neurodegeneration in BAC Transgenic Mice

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The C9orf72 repeat size correlates with onset age of disease, DNA methylation and transcriptional downregulation of the promoter

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Lysosome dysfunction as a cause of neurodegenerative diseases: Lessons from frontotemporal dementia and amyotrophic lateral sclerosis

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

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C9orf72 expansions in frontotemporal dementia and amyotrophic lateral sclerosis

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Zebrafish models of human motor neuron diseases: Advantages and limitations

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R Loops and Links to Human Disease

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Advances in treating amyotrophic lateral sclerosis: insights from pathophysiological studies

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

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The role of survival motor neuron protein (SMN) in protein homeostasis

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The neuropathology associated with repeat expansions in the C9ORF72 gene

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The expanding biology of the C9orf72 nucleotide repeat expansion in neurodegenerative disease

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Zebrafish models in neuropsychopharmacology and CNS drug discovery

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Modelling amyotrophic lateral sclerosis: progress and possibilities

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Cell-to-Cell Transmission of Dipeptide Repeat Proteins Linked to C9orf72-ALS/FTD

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RNA Dysregulation in Amyotrophic Lateral Sclerosis

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Autophagy and ALS: mechanistic insights and therapeutic implications

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Distribution of dipeptide repeat proteins in cellular models and C9orf72 mutation cases suggests link to transcriptional silencing

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Loss of C9orf72 Enhances Autophagic Activity via Deregulated mTOR and TFEB Signaling

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Deletion of C9ORF72 Results in Motor Neuron Degeneration and Stress Sensitivity in C. elegans

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C9orf72 hypermethylation protects against repeat expansion-associated pathology in ALS/FTD

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Microglia and C9orf72 in neuroinflammation and ALS and frontotemporal dementia

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C9ORF72: What It Is, What It Does, and Why It Matters

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Dissection of genetic factors associated with amyotrophic lateral sclerosis

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Poly-dipeptides encoded by the C9ORF72 repeats block global protein translation

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

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From animal models to human disease: a genetic approach for personalized medicine in ALS

Picher‐Martel, V., Valdmanis, P. N., Gould, P. V., Julien, J., & Dupré, N. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0340-5 · Cited by 150 · see citing works

C9ORF72 interaction with cofilin modulates actin dynamics in motor neurons

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

Genetics of <scp>FTLD</scp> : overview and what else we can expect from genetic studies

Pottier, C., Ravenscroft, T. A., Sanchez‐Contreras, M., & Rademakers, R. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13622 · Cited by 148 · see citing works

Characterization of the dipeptide repeat protein in the molecular pathogenesis of c9FTD/ALS

Yamakawa, M., Ito, D., Honda, T., Kubo, K., Noda, M., Nakajima, K., & Suzuki, N. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu576 · Cited by 145 · see citing works

Molecular and Cellular Mechanisms Affected in ALS

Gall, L. L., Anakor, E., Connolly, O., Vijayakumar, U. G., Duddy, W. J., & Duguez, S. (2020) · Journal of Personalized Medicine · doi:10.3390/jpm10030101 · Cited by 147 · see citing works

Mechanisms of toxicity in C9FTLD/ALS

Gendron, T. F., Belzil, V., Zhang, Y., & Petrucelli, L. (2014) · Acta Neuropathologica · doi:10.1007/s00401-013-1237-z · Cited by 144 · see citing works

TMEM106B is a genetic modifier of frontotemporal lobar degeneration with C9orf72 hexanucleotide repeat expansions

Gallagher, M. D., Suh, E. R., Grossman, M., Elman, L. B., McCluskey, L. F., Swieten, J. C. V., Al‐Sarraj, S., Neumann, M., Gelpí, E., Ghetti, B. F., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-013-1239-x · Cited by 143 · 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

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

RNA metabolism in neurodegenerative disease

Liu, E. Y., Cali, C. P., & Lee, E. B. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.028613 · Cited by 137 · see citing works

Amyotrophic lateral sclerosis: Problems and prospects

Sreedharan, J., & Brown, R. H. (2013) · Annals of Neurology · doi:10.1002/ana.24012 · Cited by 138 · 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

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

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

Zebrafish as a model organism for neurodegenerative disease

Chia, K., Klingseisen, A., Sieger, D., & Priller, J. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.940484 · Cited by 134 · see citing works

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

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

Antisense oligonucleotides in neurological disorders

Wurster, C. D., & Ludolph, A. C. (2018) · Therapeutic Advances in Neurological Disorders · doi:10.1177/1756286418776932 · Cited by 131 · see citing works

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

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

Defining the genetic connection linking amyotrophic lateral sclerosis (ALS) with frontotemporal dementia (FTD)

Lattante, S., Ciura, S., Rouleau, G. A., & Kabashi, E. (2015) · Trends in Genetics · doi:10.1016/j.tig.2015.03.005 · Cited by 125 · see citing works

Neurotheranostics as Personalized Medicines

Kevadiya, B. D., Ottemann, B. M., Thomas, M. B., Mukadam, I., Nigam, S., McMillan, J., Gorantla, S., Bronich, T. K., Edagwa, B., & Gendelman, H. E. (2019) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2018.10.011 · Cited by 124 · see citing works

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

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

Zebrafish: A Marvel of High-Throughput Biology for 21st Century Toxicology

Bugel, S. M., Tanguay, R. L., & Planchart, A. (2014) · Current Environmental Health Reports · doi:10.1007/s40572-014-0029-5 · Cited by 121 · see citing works

Amyotrophic lateral sclerosis: Current perspectives from basic research to the clinic

Mancuso, R., & Navarro, X. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.07.004 · Cited by 116 · see citing works

Novel antibodies reveal presynaptic localization of C9orf72 protein and reduced protein levels in C9orf72 mutation carriers

Frick, P., Sellier, C., Mackenzie, I., Cheng, C.-Y., Tahraoui-Bories, J., Martinat, C., Pasterkamp, R., Prudlo, J., Edbauer, D., Oulad-Abdelghani, M., et al. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0579-0 · Cited by 107 · see citing works

The genetics of amyotrophic lateral sclerosis: current insights

Kirby, J., Sultan, A. A., Waller, R., & Heath, P. R. (2016) · Degenerative Neurological and Neuromuscular Disease · doi:10.2147/dnnd.s84956 · Cited by 107 · see citing works

Disease Mechanisms ofC9ORF72Repeat ExpansionsPreprint

Gendron, T. F., & Petrucelli, L. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024224 · Cited by 101 · see citing works

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

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

Genetics insight into the amyotrophic lateral sclerosis/frontotemporal dementia spectrum

Ji, A.-L., Zhang, X., Chen, W., & Huang, W. (2017) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2016-104271 · Cited by 95 · see citing works

Sqstm1 knock-down causes a locomotor phenotype ameliorated by rapamycin in a zebrafish model of ALS/FTLD

Lattante, S., de Calbiac, H., Le Ber, I., Brice, A., Ciura, S., & Kabashi, E. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddu580 · Cited by 90 · see citing works

Cortical Function in Asymptomatic Carriers and Patients WithC9orf72Amyotrophic Lateral Sclerosis

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

Hypermethylation of the CpG-island near the C9orf72 G₄C₂-repeat expansion in FTLD patients.

Xi, Z., Rainero, I., Rubino, E., Pinessi, L., Bruni, A., Maletta, R., Nacmias, B., Sorbi, S., Galimberti, D., Surace, E., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu279 · Cited by 85 · see citing works

A C9orf72 ALS/FTD Ortholog Acts in Endolysosomal Degradation and Lysosomal Homeostasis

Corrionero, A., & Horvitz, H. R. (2018) · Current Biology · doi:10.1016/j.cub.2018.03.063 · Cited by 86 · see citing works

Animal models of amyotrophic lateral sclerosis: a comparison of model validity

Morrice, J. R., Gregory, C. Y., & Shaw, C. (2018) · Neural Regeneration Research · doi:10.4103/1673-5374.241445 · Cited by 88 · see citing works

A C9orf72–CARM1 axis regulates lipid metabolism under glucose starvation-induced nutrient stressPreprint

Liu, Y., Wang, T., Ji, Y. J., Johnson, K., Liu, H., Johnson, K., Bailey, S., Suk, Y., Lu, Y., Liu, M., et al. (2018) · Genes & Development · doi:10.1101/gad.315564.118 · 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

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

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

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

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

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

Nearly 30 Years of Animal Models to Study Amyotrophic Lateral Sclerosis: A Historical Overview and Future Perspectives

Bonifacino, T., Zerbo, R. A., Balbi, M., Torazza, C., Frumento, G., Fedele, E., Bonanno, G., & Milanese, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212236 · Cited by 78 · see citing works

Proteostatic imbalance and protein spreading in amyotrophic lateral sclerosis

Cicardi, M. E., Marrone, L., Azzouz, M., & Trotti, D. (2021) · The EMBO Journal · doi:10.15252/embj.2020106389 · Cited by 73 · see citing works

Insights into the pathogenic mechanisms of chromosome 9 open reading frame 72 (C9orf72) repeat expansions

Todd, T. W., & Petrucelli, L. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13623 · Cited by 73 · see citing works

Intrinsic Disorder in Proteins with Pathogenic Repeat Expansions

Darling, A. L., & Uversky, V. N. (2017) · Molecules · doi:10.3390/molecules22122027 · Cited by 72 · see citing works

The ALS-FTD-linked gene product, C9orf72, regulates neuronal morphogenesis via autophagy

Ho, W. Y., Tai, Y. K., Chang, J., Liang, J., Tyan, S.-H., Chen, S., Guan, J., Zhou, H., Shen, H., Koo, E. H., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1569441 · Cited by 70 · 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

C9orf72 amyotrophic lateral sclerosis and frontotemporal dementia

Mizielinska, S., & Isaacs, A. M. (2014) · Current Opinion in Neurology · doi:10.1097/wco.0000000000000130 · 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

Neuromuscular Junction Impairment in Amyotrophic Lateral Sclerosis: Reassessing the Role of Acetylcholinesterase

Campanari, M.-L., García-Ayllón, M.-S., Ciura, S., Sáez-Valero, J., & Kabashi, E. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00160 · Cited by 69 · see citing works

ALS and FTD: an epigenetic perspective

Belzil, V., Katzman, R. B., & Petrucelli, L. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1587-4 · Cited by 69 · see citing works

Reduced C9orf72 function leads to defective synaptic vesicle release and neuromuscular dysfunction in zebrafish

Butti, Z., Pan, Y. E., Giacomotto, J., & Patten, S. A. (2021) · Communications Biology · doi:10.1038/s42003-021-02302-y · Cited by 69 · see citing works

The C9orf72-interacting protein Smcr8 is a negative regulator of autoimmunity and lysosomal exocytosisPreprint

Zhang, Y., Burberry, A., Wang, J., Sandoe, J., Ghosh, S. D., Udeshi, N. D., Svinkina, T., Mordes, D. A., Mok, J., Charlton, M. E., et al. (2018) · Genes & Development · doi:10.1101/gad.313932.118 · Cited by 69 · 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

Emerging Perspectives on Dipeptide Repeat Proteins in C9ORF72 ALS/FTD

Schmitz, A., Marques, J. P., Oertig, I., Maharjan, N., & Saxena, S. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.637548 · Cited by 67 · see citing works

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

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

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

ALS gene, C9orf72, loss of function Zebrafish model \nshows motor and synaptic defects

Butti, Z., Giacomotto, J., & Patten, S. A. (2020) · EspaceINRS (National Institute for Scientific Research (Canada))

Zebrafish C9orf72 loss-of-function models of Amyotrophic Lateral Sclerosis and Frontotemporal Dementia

Rounding, N. (2018) · White Rose eTheses Online (University of Leeds, The University of Sheffield, University of York) · Cited by 2 · see citing works

ALS gene, C9orf72, loss of function Zebrafish model shows motor and synaptic defects

Butti, Z., Giacomotto, J., & Patten, S. A. (2020) · EspaceINRS (National Institute for Scientific Research (Canada))

Characterization of a C9orf72 Knockout Danio rerio model for ALS and cross-species validation of potential therapeutics screened in Caenorhabditis elegans

Emond, A., Laflamme, C., Therrien, M., Liao, M., Maios, C., Labarre, A., Drapeau, P., & Parker, J. A. (2026) · PLoS ONE · doi:10.1371/journal.pone.0346613

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