Cited by 298Amyotrophic Lateral Sclerosis ResearchGenetic Neurodegenerative DiseasesHereditary Neurological Disorders

The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.

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

Open access

O’Rourke, Jacqueline G., Bogdanik, Laurent, Muhammad, A.K.M.G., Gendron, Tania F., Kim, Kevin J., Austin, Andrew, Cady, Janet, Liu, Elaine Y., Zarrow, Jonah, Grant, Sharday, Ho, Ritchie, Bell, Shaughn, Carmona, Sharon, Simpkinson, Megan, Lall, Deepti, Wu, Kathryn, Daughrity, Lillian, Dickson, Dennis W., Harms, Matthew B., Petrucelli, Leonard, Lee, Edward B., Lutz, Cathleen M., Baloh, Robert H.·2015·Neuron

DOI 10.1016/j.neuron.2015.10.027PMC PMC4672384

Open this paper in CoChat — free account Open PDF

Abstract

Noncoding expansions of a hexanucleotide repeat (GGGGCC) in the C9orf72 gene are the most common cause of familial amyotrophic lateral sclerosis and frontotemporal dementia. Here we report transgenic mice carrying a bacterial artificial chromosome (BAC) containing the full human C9orf72 gene with either a normal allele (15 repeats) or disease-associated expansion (∼100-1,000 repeats; C9-BACexp). C9-BACexp mice displayed pathologic features seen in C9orf72 expansion patients, including widespread RNA foci and repeat-associated non-ATG (RAN) translated dipeptides, which were suppressed by antisense oligonucleotides targeting human C9orf72. Nucleolin distribution was altered, supporting that either C9orf72 transcripts or RAN dipeptides promote nucleolar dysfunction. Despite early and widespread production of RNA foci and RAN dipeptides in C9-BACexp mice, behavioral abnormalities and neurodegeneration were not observed even at advanced ages, supporting the hypothesis that RNA foci and RAN dipeptides occur presymptomatically and are not sufficient to drive neurodegeneration in mice at levels seen in patients.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1016/j.neuron.2015.10.027

Cites

41 of 41 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Gene set enrichment analysis: A knowledge-based approach for interpreting genome-wide expression profiles
Subramanian, A., Tamayo, P., Mootha, V. K., Mukherjee, S., Ebert, B. L., Gillette, M. A., Paulovich, A., Pomeroy, S. L., Golub, T. R., Lander, E. S., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506580102 · Cited by 53,625
PGC-1α-responsive genes involved in oxidative phosphorylation are coordinately downregulated in human diabetes
Mootha, V. K., Lindgren, C. M., Eriksson, K.-F., Subramanian, A., Sihag, S., Lehar, J., Puigserver, P., Carlsson, E., Ridderstråle, M., Laurila, E., et al. (2003) · Nature Genetics · doi:10.1038/ng1180 · Cited by 10,197
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 4×
“Expansions of a GGGGCC hexanucleotide repeat in the first intron/promoter of the C9orf72 gene are the most commonly identified genetic cause of both familial and sporadic ALS and FTLD (DeJesus-Hernandez et al., 2011; Renton et al., 2011).”
BackgroundInfluentialSelf-citation
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
Sociability and preference for social novelty in five inbred strains: an approach to assess autistic‐like behavior in mice
Moy, S. S., Nadler, J. J., Perez, A., Barbaro, R. P., Johns, J. M., Magnuson, T. R., Piven, J., & Crawley, J. N. (2004) · Genes, Brain and Behavior · doi:10.1111/j.1601-1848.2004.00076.x · Cited by 1,522
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
Self-citation
C9orf72 nucleotide repeat structures initiate molecular cascades of disease
Haeusler, A. R., Donnelly, C. J., Periz, G., Simko, E. A. J., Shaw, P. G., Kim, M.-S., Maragakis, N. J., Troncoso, J. C., Pandey, A., Sattler, R., et al. (2014) · Nature · doi:10.1038/nature13124 · Cited by 978
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
Self-citation
C9orf72 repeat expansions cause neurodegeneration in Drosophila through arginine-rich proteins
Mizielinska, S., Grönke, S., Niccoli, T., Ridler, C. E., Clayton, E. L., Devoy, A., Moens, T., Norona, F. E., Woollacott, I. O. C., Pietrzyk, J., et al. (2014) · Science · doi:10.1126/science.1256800 · Cited by 740

Flagged first, then by citations

Show all 41 references

Sorted by citations

Items 101–200 of 298

Nuclear transport dysfunction: a common theme in amyotrophic lateral sclerosis and frontotemporal dementia
Jovičić, A., Paul, J. W., & Gitler, A. D. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13642 · Cited by 53
Insights into C9ORF72-Related ALS/FTD from Drosophila and iPSC Models
Yuva-Aydemir, Y., Almeida, S., & Gao, F. (2018) · Trends in Neurosciences · doi:10.1016/j.tins.2018.04.002 · Cited by 52
Absence of Survival and Motor Deficits in 500 Repeat C9ORF72 BAC Mice
Mordes, D. A., Morrison, B. M., Ament, X. H., Cantrell, C., Mok, J., Eggan, P., Xue, C., Wang, J., Eggan, K. C., & Rothstein, J. D. (2020) · Neuron · doi:10.1016/j.neuron.2020.08.009 · Cited by 60
Interplay between immunity and amyotrophic lateral sclerosis: Clinical impact
Marchi, F. D., Munitić, I., Amedei, A., Berry, J. D., Feldman, E. L., Aronica, E., Nardo, G., Weehaeghe, D. V., Niccolai, E., Prtenjača, N., et al. (2021) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2021.06.027 · Cited by 52
Altered blood–brain barrier and blood–spinal cord barrier dynamics in amyotrophic lateral sclerosis: Impact on medication efficacy and safety
Pan, Y., & Nicolazzo, J. A. (2022) · British Journal of Pharmacology · doi:10.1111/bph.15802 · Cited by 49
Preclinical evaluation of WVE-004, an investigational stereopure oligonucleotide for the treatment of C9orf72-associated ALS or FTD
Liu, Y., Andreucci, A., Iwamoto, N., Yin, Y., Yang, H., Liu, F., Bulychev, A., Hu, X. S., Lin, X., Lamore, S. D., et al. (2022) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2022.04.007 · Cited by 56
Microglia and Astrocytes in Amyotrophic Lateral Sclerosis: Disease-Associated States, Pathological Roles, and Therapeutic Potential
You, J., Youssef, M., Santos, J. R., Lee, J., & Park, J. (2023) · Biology · doi:10.3390/biology12101307 · Cited by 60
Mouse Models of C9orf72 Hexanucleotide Repeat Expansion in Amyotrophic Lateral Sclerosis/ Frontotemporal Dementia
Batra, R., & Lee, C. W. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00196 · Cited by 63
Evidence of Metabolic Dysfunction in Amyotrophic Lateral Sclerosis (ALS) Patients and Animal Models
Maksimovic, K., Youssef, M., You, J., Sung, H., & Park, J. (2023) · Biomolecules · doi:10.3390/biom13050863 · Cited by 51
Emerging understanding of the genotype–phenotype relationship in amyotrophic lateral sclerosis
Goutman, S. A., Chen, K. S., Paez-Colasante, X., & Feldman, E. L. (2018) · Handbook of clinical neurology · doi:10.1016/b978-0-444-64076-5.00039-9 · Cited by 50
C9orf72 Dipeptide Repeats Cause Selective Neurodegeneration and Cell-Autonomous Excitotoxicity in Drosophila Glutamatergic Neurons
Xu, W., & Xu, J. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.0908-18.2018 · Cited by 55
Modeling Protein Aggregation and the Heat Shock Response in ALS iPSC-Derived Motor Neurons
Seminary, E. R., Sison, S. L., & Ebert, A. D. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00086 · Cited by 45
Microglial Turnover in Ageing-Related Neurodegeneration: Therapeutic Avenue to Intervene in Disease Progression
Azam, S., Haque, M. E., Kim, I., & Choi, D. (2021) · Cells · doi:10.3390/cells10010150 · Cited by 46
Long non‐coding RNAs in motor neuron development and disease
Vangoor, V. R., Gomes‐Duarte, A., & Pasterkamp, R. J. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15198 · Cited by 43
Modelling C9orf72 dipeptide repeat proteins of a physiologically relevant size
Callister, J. B., Ryan, S., Sim, J. A., Rollinson, S. J., & Pickering-Brown, S. M. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw327 · Cited by 41
Neuronal VCP loss of function recapitulates FTLD-TDP pathology
Wani, A., Zhu, J., Ulrich, J. D., Eteleeb, A. M., Sauerbeck, A. D., Reitz, S. J., Arhzaouy, K., Ikenaga, C., Yuede, C. M., Pittman, S. K., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109399 · Cited by 39
Insulin-like growth factor 1 in diabetic neuropathy and amyotrophic lateral sclerosis
Rauskolb, S., Dombert, B., & Sendtner, M. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.04.007 · Cited by 45
Pathogenic determinants and mechanisms of ALS/FTD linked to hexanucleotide repeat expansions in the C9orf72 gene
Wen, X., Westergard, T., Pasinelli, P., & Trotti, D. (2016) · Neuroscience Letters · doi:10.1016/j.neulet.2016.09.007 · Cited by 45
Loss of Ranbp2 in motor neurons causes the disruption of nucleocytoplasmic and chemokine signaling and proteostasis of hnRNPH3 and Mmp28, and the development of amyotrophic lateral sclerosis (ALS)-like syndromes
Cho, K., Yoon, D., Qiu, S., Danziger, Z. C., Grill, W. M., Wetsel, W. C., & Ferreira, P. A. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.027730 · Cited by 42
RNA Binding Proteins and the Pathogenesis of Frontotemporal Lobar Degeneration
Hofmann, J. W., Seeley, W. W., & Huang, E. J. (2018) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-012418-012955 · Cited by 50
PolyGR and polyPR knock-in mice reveal a conserved neuroprotective extracellular matrix signature in C9orf72 ALS/FTD neurons
Milioto, C., Carcolé, M., Giblin, A., Coneys, R., Attrebi, O. N., Ahmed, M., Harris, S., Lee, B. I., Yang, M., Ellingford, R. A., et al. (2024) · Nature Neuroscience · doi:10.1038/s41593-024-01589-4 · Cited by 46
Modelling amyotrophic lateral sclerosis in rodents
Todd, T. W., & Petrucelli, L. (2022) · Nature reviews. Neuroscience · doi:10.1038/s41583-022-00564-x · Cited by 44
Self-citation
Repeat-Associated Non-ATG Translation in Neurological DiseasesPreprint
Zu, T., Pattamatta, A., & Ranum, L. P. W. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033019 · Cited by 43
Pathogenic Mechanisms and Therapy Development for C9orf72 Amyotrophic Lateral Sclerosis/Frontotemporal Dementia
Jiang, J., & Ravits, J. (2019) · Neurotherapeutics · doi:10.1007/s13311-019-00797-2 · Cited by 44
Amyotrophic lateral sclerosis: recent genetic highlights
White, M. A., & Sreedharan, J. (2016) · Current Opinion in Neurology · doi:10.1097/wco.0000000000000367 · Cited by 40
The C9ORF72 Gene, Implicated in Amyotrophic Lateral Sclerosis and Frontotemporal Dementia, Encodes a Protein That Functions in Control of Endothelin and Glutamate Signaling
Fomin, V., Richard, P., Hoque, M., Li, C., Gu, Z., Fissore-O'Leary, M., Tian, B., Prives, C. L., & Manley, J. L. (2018) · Molecular and Cellular Biology · doi:10.1128/mcb.00155-18 · Cited by 44
Approaches to gene modulation therapy for ALS
Meijboom, K. E., & Brown, R. H. (2022) · Neurotherapeutics · doi:10.1007/s13311-022-01285-w · Cited by 38
Functional Roles of Long Non-coding RNAs in Motor Neuron Development and Disease
Chen, K., & Chen, J. (2020) · Journal of Biomedical Science · doi:10.1186/s12929-020-00628-z · Cited by 41
Pathological insights from amyotrophic lateral sclerosis animal models: comparisons, limitations, and challenges
Zhu, L., Li, S., Li, X., & Yin, P. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00377-7 · Cited by 41
Complex Coacervate-Based Materials for Biomedicine: Recent Advancements and Future Prospects
Roy, P. S. (2024) · Industrial & Engineering Chemistry Research · doi:10.1021/acs.iecr.3c03830 · Cited by 36
Survival and Motor Phenotypes in FVB C9-500 ALS/FTD BAC Transgenic Mice Reproduced by Multiple Labs
Nguyen, L., Laboissonniere, L. A., Guo, S., Pilotto, F., Scheidegger, O., Oestmann, A., Hammond, J. W., Li, H., Hyysalo, A., Peltola, R., et al. (2020) · Neuron · doi:10.1016/j.neuron.2020.09.009 · Cited by 36
Viral delivery of C9ORF72 hexanucleotide repeat expansions in mice lead to repeat length dependent neuropathology and behavioral deficits.
Herranz-Martín, S., Chandran, J. S., Lewis, K. E. A., Mulcahy, P. J., Higginbottom, A., Walker, C., y Valenzuela, I. M.-P., Jones, R. A., Coldicott, I., Iannitti, T., et al. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.029892 · Cited by 39
A C9ORF72 BAC mouse model recapitulates key epigenetic perturbations of ALS/FTD
Esanov, R., Cabrera, G. T., Andrade, N. S., Gendron, T. F., Brown, R. H., Benatar, M. G., Wahlestedt, C., Mueller, C., & Zeier, Z. R. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0185-9 · Cited by 35
Self-citation
Widespread loss of the silencing epigenetic mark H3K9me3 in astrocytes and neurons along with hippocampal-dependent cognitive impairment in C9orf72 BAC transgenic mice
Jury, N., Abarzúa, S., Díaz, I. D. P., Guerra, M. V., Ampuero, E., Cubillos, P., Martínez, P., Herrera-Soto, A., Arredondo, C., Rojas, F., et al. (2020) · Clinical Epigenetics · doi:10.1186/s13148-020-0816-9 · Cited by 35
Nucleolar stress in C9orf72 and sporadic ALS spinal motor neurons precedes TDP-43 mislocalization
Arogundade, O. A., Nguyen, S., Leung, R., Wainio, D., Gómez-Rodríguez, M. J., & Ravits, J. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01125-6 · Cited by 35
Negative regulation of TREM2-mediated C9orf72 poly-GA clearance by the NLRP3 inflammasome
Shu, X., Chen, W., Tu, W.-Y., Zhong, K., Qi, S., Wang, A., Bai, L., Zhang, S.-X., Luo, B., Xu, Z., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112133 · Cited by 33
Mouse models of frontotemporal dementia: A comparison of phenotypes with clinical symptomatology
Ahmed, R. M., Irish, M., van Eersel, J., Ittner, A., Ke, Y. D., Volkerling, A. M., van der Hoven, J., Tanaka, K., Karl, T., Kassiou, M., et al. (2017) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2017.01.004 · Cited by 34
Roadmap for C9ORF72 in Frontotemporal Dementia and Amyotrophic Lateral Sclerosis: Report on the C9ORF72 FTD/ALS Summit
Sattler, R., Traynor, B. J., Robertson, J., Bosch, L. V. D., Barmada, S. J., Svendsen, C. N., Disney, M. D., Gendron, T. F., Wong, P. C., Turner, M. R., et al. (2023) · Neurology and Therapy · doi:10.1007/s40120-023-00548-8 · Cited by 33
Self-citation
Modelling amyotrophic lateral sclerosis in mice
Stephenson, J., & Amor, S. (2017) · Drug Discovery Today Disease Models · doi:10.1016/j.ddmod.2018.10.001 · Cited by 34
RNA Deregulation in Amyotrophic Lateral Sclerosis: The Noncoding Perspective
Laneve, P., Tollis, P., & Caffarelli, E. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910285 · Cited by 32
Divergence, Convergence, and Therapeutic Implications: A Cell Biology Perspective of C9ORF72-ALS/FTD
Tang, X., Toro, A., Sahana, T. G., Gao, J., Chalk, J. L., Oskarsson, B., & Zhang, K. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00383-7 · Cited by 34
The coming-of-age of nucleocytoplasmic transport in motor neuron disease and neurodegeneration
Ferreira, P. A. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03029-0 · Cited by 34
Dipeptide repeat proteins activate a heat shock response found in C9ORF72-ALS/FTLD patients
Mordes, D. A., Prudencio, M., Goodman, L. D., Klim, J. R., Moccia, R., Limone, F., Pietiläinen, O. P. H., Chowdhary, K., Dickson, D. W., Rademakers, R., et al. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0555-8 · Cited by 33
Self-citation
Altered Phase Separation and Cellular Impact in C9orf72-Linked ALS/FTD
Solomon, D. A., Smikle, R., Reid, M. J., & Mizielinska, S. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.664151 · Cited by 33
C9orf72-associated neurodegeneration in ALS-FTD: breaking new ground in ribosomal RNA and nucleolar dysfunction
Herrmann, D., & Parlato, R. (2018) · Cell and Tissue Research · doi:10.1007/s00441-018-2806-1 · Cited by 29
Targeted DNA methylation of neurodegenerative disease genes via homology directed repair
Cali, C. P., Park, D. S., & Lee, E. B. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz979 · Cited by 28
Self-citation
Development of a sensitive trial-ready poly(GP) CSF biomarker assay for C9orf72 -associated frontotemporal dementia and amyotrophic lateral sclerosis
Wilson, K. M., Katona, E., Glaria, I., Carcolé, M., Swift, I. J., Sogorb‐Esteve, A., Heller, C., Bouzigues, A., Heslegrave, A., Keshavan, A., et al. (2022) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2021-328710 · Cited by 31
Amyotrophic Lateral Sclerosis Pathogenesis Converges on Defects in Protein Homeostasis Associated with TDP-43 Mislocalization and Proteasome-Mediated Degradation Overload
Lin, G., Mao, D., & Bellen, H. J. (2016) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2016.07.004 · Cited by 29
C9ORF72 hexanucleotide repeat exerts toxicity in a stable, inducible motor neuronal cell model, which is rescued by partial depletion of Pten
Stopford, M. J., Higginbottom, A., Hautbergue, G. M., Cooper‐Knock, J., Mulcahy, P. J., Vos, K. J. D., Renton, A. E., Pliner, H. A., Calvo, A., Chiò, A., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx022 · Cited by 28
La accesibilidad de los portales web de las universidades públicas andaluzas
Balsells, L. A. C., González, J. C. G., Balsells, M. A. C., & Chamorro, V. A. P. (2017) · Revista española de Documentación Científica · doi:10.3989/redc.2017.2.1372 · Cited by 32
RNA-Binding Proteins and the Complex Pathophysiology of ALS
Kim, W., Kim, D., & Lee, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22052598 · Cited by 28
NEAT1 lncRNA and amyotrophic lateral sclerosis
Nishimoto, Y., Nakagawa, S., & Okano, H. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.105175 · Cited by 28
Loss of C9orf72 perturbs the Ran-GTPase gradient and nucleocytoplasmic transport, generating compositionally diverse Importin β-1 granules
McGoldrick, P., Lau, A., You, Z., Durcan, T. M., & Robertson, J. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112134 · Cited by 29
Recent advances in understanding amyotrophic lateral sclerosis and emerging therapies
Gittings, L. M., & Sattler, R. (2020) · Faculty Reviews · doi:10.12703/b/9-12 · Cited by 27
Mini-Review: Induced pluripotent stem cells and the search for new cell-specific ALS therapeutic targets
Ferraiuolo, L., & Maragakis, N. J. (2021) · Neuroscience Letters · doi:10.1016/j.neulet.2021.135911 · Cited by 28
Updates on Disease Mechanisms and Therapeutics for Amyotrophic Lateral Sclerosis
Nguyen, L. (2024) · Cells · doi:10.3390/cells13110888 · Cited by 29
Loss of Tmem106b is unable to ameliorate frontotemporal dementia-like phenotypes in an AAV mouse model of C9ORF72-repeat induced toxicity
Nicholson, A. M., Zhou, X., Perkerson, R. B., Parsons, T. M., Chew, J., Brooks, M., DeJesus‐Hernandez, M., Finch, N. A., Matchett, B. J., Kurti, A., et al. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0545-x · Cited by 24
Self-citation
A blood–brain penetrant RNA-targeted small molecule triggers elimination of r(G 4 C 2 ) exp in c9ALS/FTD via the nuclear RNA exosome
Bush, J. A., Meyer, S. M., Fuerst, R., Tong, Y., Li, Y., Benhamou, R. I., Aikawa, H., Zanon, P. R. A., Gibaut, Q. M. R., Angelbello, A. J., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2210532119 · Cited by 23
Self-citation
Moderate intrinsic phenotypic alterations in C9orf72 ALS/FTD iPSC-microglia despite the presence of C9orf72 pathological features
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. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1179796 · Cited by 34
Self-citation
Incorporating upper motor neuron health in ALS drug discovery
Dervishi, I., & Özdi̇nler, P. H. (2018) · Drug Discovery Today · doi:10.1016/j.drudis.2018.01.027 · Cited by 24
Ablation of C9orf72 together with excitotoxicity induces ALS in rats
Dong, W., Ma, Y., Guan, F., Zhang, X., Chen, W., Zhang, L., & Zhang, L. (2020) · FEBS Journal · doi:10.1111/febs.15501 · Cited by 25
From Mouse Models to Human Disease: An Approach for Amyotrophic Lateral Sclerosis
Alrafiah, A. (2018) · In Vivo · doi:10.21873/invivo.11339 · Cited by 28
Modern approaches in gene therapy of motor neuron diseases
Zakharova, M. N. (2020) · Medicinal Research Reviews · doi:10.1002/med.21705 · Cited by 23
RAN proteins in neurodegenerative disease: Repeating themes and unifying therapeutic strategies
Guo, S., Nguyen, L., & Ranum, L. P. W. (2021) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2021.11.001 · Cited by 22
Hyperexcitability in young iPSC-derived C9ORF72 mutant motor neurons is associated with increased intracellular calcium release
Burley, S., Beccano-Kelly, D. A., Talbot, K., Llana, O. C., & Wade‐Martins, R. (2022) · Scientific Reports · doi:10.1038/s41598-022-09751-3 · Cited by 26
Targeting 14-3-3θ-mediated TDP-43 pathology in amyotrophic lateral sclerosis and frontotemporal dementia mice
Ke, Y. D., van Hummel, A., Au, C. G., Chan, G., Lee, W. S., van der Hoven, J., Przybyla, M., Deng, Y., Sabale, M., Morey, N., et al. (2024) · Neuron · doi:10.1016/j.neuron.2024.01.022 · Cited by 21
Concomitant gain and loss of function pathomechanisms in C9ORF72 amyotrophic lateral sclerosis
Pal, A., Kretner, B., Abo-Rady, M., Glaβ, H., Dash, B. P., Naumann, M., Japtok, J., Kreiter, N., Dhingra, A., Heutink, P., et al. (2021) · Life Science Alliance · doi:10.26508/lsa.202000764 · Cited by 24
Dual-gRNA approach with limited off-target effect corrects C9ORF72 repeat expansion in vivo
Piao, X., Meng, D., Zhang, X., Song, Q., Lv, H., & Jia, Y. (2022) · Scientific Reports · doi:10.1038/s41598-022-07746-8 · Cited by 23
Biomarkers for C9orf7-ALS in Symptomatic and Pre-symptomatic Patients: State-of-the-art in the New Era of Clinical Trials
Querin, G., Biferi, M. G., & Pradat, P. (2021) · Journal of Neuromuscular Diseases · doi:10.3233/jnd-210754 · Cited by 20
C9ORF72 hexanucleotide repeat expansion: From ALS and FTD to a broader pathogenic role?
Sellier, C., Corcia, P., Vourc’h, P., & Dupuis, L. (2024) · Revue Neurologique · doi:10.1016/j.neurol.2024.03.008 · Cited by 24
Motor Neuron Abnormalities Correlate with Impaired Movement in Zebrafish that Express Mutant Superoxide Dismutase 1
Robinson, K. J., Yuan, K. C., Don, E. K., Hogan, A. L., Winnick, C. G., Tym, M. C., Lucas, C. W., Shahheydari, H., Watchon, M., Blair, I. P., et al. (2018) · Zebrafish · doi:10.1089/zeb.2018.1588 · Cited by 19
Repeat-associated non-AUG (RAN) translation mechanisms are running into focus for GGGGCC-repeat associated ALS/FTD
Goodman, L. D., & Bonini, N. M. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2019.101697 · Cited by 20
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. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz230 · Cited by 20
A high-fidelity CRISPR-Cas13 system improves abnormalities associated with C9ORF72-linked ALS/FTD
McCallister, T. X., Lim, C. K. W., Singh, M., Zhang, S., Ahsan, N. S., Terpstra, W. M., Xiong, A. Y., C., M. A. Z., Powell, J. E., Drnevich, J. M., et al. (2025) · Nature Communications · doi:10.1038/s41467-024-55548-5 · Cited by 19
Repeat length increases disease penetrance and severity in C9orf72 ALS/FTD BAC transgenic mice
Pattamatta, A., Nguyen, L., Olafson, H. R., Scotti, M. M., Laboissonniere, L. A., Richardson, J. I., Berglund, J. A., Zu, T., Wang, E. T., & Ranum, L. P. W. (2020) · Human Molecular Genetics · doi:10.1093/hmg/ddaa279 · Cited by 22
Drosophila models of amyotrophic lateral sclerosis with defects in RNA metabolism
Zhang, K., Coyne, A. N., & Lloyd, T. E. (2018) · Brain Research · doi:10.1016/j.brainres.2018.04.043 · Cited by 21
Drosophila as a Model for Assessing the Function of RNA-Binding Proteins during Neurogenesis and Neurological Disease
Olesnicky, E. C., & Wright, E. G. (2018) · Journal of Developmental Biology · doi:10.3390/jdb6030021 · Cited by 18
Nucleolin reorganization and nucleolar stress in Purkinje cells of mutant PCD mice
Baltanás, F. C., Berciano, M. T., Tapia, O., Narcís, J. O., Lafarga, V., Díaz, D., Weruaga, E., Santos, E., & Lafarga, M. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.03.017 · Cited by 18
Knock in of a hexanucleotide repeat expansion in the C9orf72 gene induces ALS in rats
Dong, W., Zhang, L., Sun, C., Gao, X., Guan, F., Li, J., Chen, W., Ma, Y., & Zhang, L. (2020) · Animal Models and Experimental Medicine · doi:10.1002/ame2.12129 · Cited by 18
Antisense Transcription across Nucleotide Repeat Expansions in Neurodegenerative and Neuromuscular Diseases: Progress and Mysteries
Castro, A. F., Loureiro, J. R., Bessa, J., & Silveira, I. (2020) · Genes · doi:10.3390/genes11121418 · Cited by 18
RNA Toxicity and Perturbation of rRNA Processing in Spinocerebellar Ataxia Type 2
Li, P. P., Moulick, R., Feng, H., Sun, X., Arbez, N., Jin, J., Marque, L. O., Hedglen, E., Chan, H. Y. E., Ross, C. A., et al. (2021) · Movement Disorders · doi:10.1002/mds.28729 · Cited by 19
Principles of brain aging: Status and challenges of modeling human molecular changes in mice
Kluever, V., & Fornasiero, E. F. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101465 · Cited by 18
Inducible expression of human C9ORF72 36× G4C2 hexanucleotide repeats is sufficient to cause RAN translation and rapid muscular atrophy in mice
Riemslagh, F. W., van der Toorn, E. C., Verhagen, R. F. M., Maas, A., Bosman, L. W. J., Hukema, R. K., & Willemsen, R. (2021) · Disease Models & Mechanisms · doi:10.1242/dmm.044842 · Cited by 16
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
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) · Clinical Epigenetics · doi:10.1186/s13148-021-01039-z · Cited by 17
MicroRNA expression in animal models of amyotrophic lateral sclerosis and potential therapeutic approaches
Peplow, P., & Martinez, B. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.322431 · Cited by 16
C9ORF72 -ALS/FTD: Transgenic Mice Make a Come-BAC
Hayes, L. R., & Rothstein, J. D. (2016) · Neuron · doi:10.1016/j.neuron.2016.04.026 · Cited by 17
Preclinical models of disease and multimorbidity with focus upon cardiovascular disease and dementia
Shabir, O., Moll, T., Matuszyk, M. M., Eyre, B., Dake, M. D., Berwick, J., & Francis, S. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111361 · Cited by 17
High content analysis in amyotrophic lateral sclerosis
Rinaldi, F., Motti, D., Ferraiuolo, L., & Kaspar, B. K. (2016) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2016.12.001 · Cited by 17
Small molecule inhibition of PIKFYVE kinase rescues gain- and loss-of-function C9ORF72 ALS/FTD disease processes in vivo
Staats, K. A., Seah, C., Sahimi, A., Wang, Y., Koutsodendris, N., Lin, S., Kim, D., Chang, W.-H., Gray, K. A., Shi, Y., et al. (2019) · doi:10.1101/685800 · Cited by 16
Breakdown of the central synapses in C9orf72-linked ALS/FTD
Ghaffari, L., Trotti, D., Haeusler, A. R., & Jensen, B. K. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.1005112 · 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
Modeling the C9ORF72 repeat expansion mutation using human induced pluripotent stem cells
Selvaraj, B. T., Livesey, M. R., & Chandran, S. (2017) · Brain Pathology · doi:10.1111/bpa.12520 · Cited by 14
Little Helpers or Mean Rogue—Role of Microglia in Animal Models of Amyotrophic Lateral Sclerosis
Cihankaya, H., Theiß, C., & Matschke, V. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22030993 · 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
Review: Modelling the pathology and behaviour of frontotemporal dementia
Solomon, D. A., Mitchell, J. C., Salcher-Konrad, M.-T., Vance, C. A., & Mizielinska, S. (2018) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12536 · Cited by 16
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
CRISPR-Cas9 targeted deletion of the C9orf72 repeat expansion mutation corrects cellular phenotypes in patient-derived iPS cellsPreprint
Pribadi, M., Yang, Z., Kim, T. S., Swartz, E. W., Huang, A., Chen, J., Dokuru, D. R., Baek, J., Gao, F., Fua, A., et al. (2016) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/051193 · Cited by 15
Promising animal models for amyotrophic lateral sclerosis drug discovery: a comprehensive update
Lescouzères, L., & Patten, S. A. (2024) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2024.2387791 · Cited by 16
Dysfunction of RNA/RNA-Binding Proteins in ALS Astrocytes and Microglia
Rossi, S., & Cozzolino, M. (2021) · Cells · doi:10.3390/cells10113005 · Cited by 15

Authors: O’Rourke, J. G., Bogdanik, L., Muhammad, A. K. M. G., Gendron, T. F., Kim, K. J., Austin, A., Cady, J., Liu, E. Y., Zarrow, J., Grant, S., Ho, R., Bell, S., Carmona, S., Simpkinson, M., Lall, D., Wu, K., Daughrity, L., Dickson, D. W., Harms, M. B., Petrucelli, L., Lee, E. B., Lutz, C. M., & Baloh, R. H.
Affiliations: Cedars-Sinai Medical Center (US)
Jackson Laboratory (US)
Mayo Clinic (US)
Washington University in St. Louis (US)
University of Pennsylvania (US)
Corresponding author: Baloh, Robert H.
ORCID: Bogdanik, Laurent
Gendron, Tania F.
Kim, Kevin J.
Zarrow, Jonah
Ho, Ritchie
Bell, Shaughn
Wu, Kathryn
Daughrity, Lillian
Dickson, Dennis W.
Harms, Matthew B.
Petrucelli, Leonard
Lee, Edward B.
Lutz, Cathleen M.
Baloh, Robert H.
Venue: Neuron
Publisher: Elsevier BV
Published: 2015-12
Volume: 88
Issue: 5
Pages: 892-901
ISSN: 0896-6273 (ISSN-L)
DOI: 10.1016/j.neuron.2015.10.027
PMC: PMC4672384
OpenAlex: W2187620259
Cited by: 298
References: 41
Citations by year: 2026: 6 · 2025: 15 · 2024: 23 · 2023: 12 · 2022: 22 · 2021: 42 · 2020: 36 · 2019: 27 · 2018: 41 · 2017: 31 · 2016: 40 · 2015: 2
FWCI: 26.79
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 367 d)
Locations: Neuron (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
The Mouseion at the JAXlibrary (Jackson Laboratory) (submittedVersion)
Funders: National Institutes of Health (NS055980, NS069669, AG039510, AG000255, NS089979, NS084528, NS063964, NS077402, NS084974, ES20395)
Department of Defense ALSRP (AL130125)
Mayo Clinic Foundation
Mayo Clinic Center for Individualized Medicine
ALS Association
Robert Packard Center for ALS Research at Johns Hopkins
Target ALS
Robert and Louise Schwab Family
Cedars-Sinai ALS Research Fund
National Center for Advancing Translational Sciences (UL1TR000124)
Topics: Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Hereditary Neurological Disorders
Keywords: C9orf72, hexanucleotide repeat expansion, amyotrophic lateral sclerosis, frontotemporal dementia, RNA foci, antisense oligonucleotides, nucleolin, neurodegeneration
MeSH terms: C9orf72 Protein, Age Factors, Amyotrophic Lateral Sclerosis, Animals, Brain, Cells, Cultured, Disease Models, Animal, Humans, Mice, Transgenic, Motor Activity, Neuromuscular Junction, Neurons, Proteins, Psychomotor Performance, Spinal Cord, Glutamic Acid, Chromosomes, Artificial, Bacterial, DNA Repeat Expansion, Mice, Muscle Strength, Frontotemporal Dementia

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks