Cited by 475Amyotrophic Lateral Sclerosis ResearchGenetic Neurodegenerative DiseasesAlzheimer's disease research and treatments

The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.

p62 positive, TDP-43 negative, neuronal cytoplasmic and intranuclear inclusions in the cerebellum and hippocampus define the pathology of C9orf72-linked FTLD and MND/ALS

Open access

Al-Sarraj, Safa, King, Andrew, Troakes, Claire, Smith, Bradley, Maekawa, Satomi, Bodi, Istvan, Rogelj, Boris, Al-Chalabi, Ammar, Hortobágyi, Tibor, Shaw, Christopher E.·2011·Acta Neuropathologica

DOI 10.1007/s00401-011-0911-2

Open this paper in CoChat — free account

Abstract

Neuronal cytoplasmic inclusions (NCIs) containing phosphorylated TDP-43 (p-TDP-43) are the pathological hallmarks of motor neuron disease/amyotrophic lateral sclerosis (MND/ALS) and FTLD-TDP. The vast majority of NCIs in the brain and spinal cord also label for ubiquitin and p62, however, we have previously reported a subset of TDP-43 proteinopathy patients who have unusual and abundant p62 positive, TDP-43 negative inclusions in the cerebellum and hippocampus. Here we sought to determine whether these cases carry the hexanucleotide repeat expansion in C9orf72. Repeat primer PCR was performed in 36 MND/ALS, FTLD-MND/ALS and FTLD-TDP cases and four controls. Fourteen individuals with the repeat expansion were detected. In all the 14 expansion mutation cases there were abundant globular and star-shaped p62 positive NCIs in the pyramidal cell layer of the hippocampus, the vast majority of which were p-TDP-43 negative. p62 positive NCIs were also abundant in the cerebellar granular and molecular layers in all cases and in Purkinje cells in 12/14 cases but they were only positive for p-TDP-43 in the granular layer of one case. Abundant p62 positive, p-TDP-43 negative neuronal intranuclear inclusions (NIIs) were seen in 12/14 cases in the pyramidal cell layer of the hippocampus and in 6/14 cases in the cerebellar granular layer. This unusual combination of inclusions appears pathognomonic for C9orf72 repeat expansion positive MND/ALS and FTLD-TDP which we believe form a pathologically distinct subset of TDP-43 proteinopathies. Our results suggest that proteins other than TDP-43 are binding p62 and aggregating in response to the mutation which may play a mechanistic role in neurodegeneration.

Integrity signals

Registry

Crossref · 10.1007/s00401-011-0911-2

Cites

35 of 35 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis
Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576
Expanded GGGGCC Hexanucleotide Repeat in Noncoding Region of C9ORF72 Causes Chromosome 9p-Linked FTD and ALS
DeJesus-Hernandez, M., Mackenzie, I. R., Boeve, B. F., Boxer, A. L., Baker, M., Rutherford, N. J., Nicholson, A. M., Finch, N. A., Flynn, H., Adamson, J., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.011 · Cited by 4,936
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
TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
Arai, T., Hasegawa, M., Akiyama, H., Ikeda, K., Nonaka, T., Mori, H., Mann, D., Tsuchiya, K., Yoshida, M., Hashizume, Y., et al. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.10.093 · Cited by 2,732
TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis
Sreedharan, J., Blair, I. P., Tripathi, V. B., Hu, X., Vance, C., Rogelj, B., Ackerley, S., Durnall, J. C., Williams, K. L., Buratti, E., et al. (2008) · Science · doi:10.1126/science.1154584 · Cited by 2,630
Self-citation
Mutations of optineurin in amyotrophic lateral sclerosis
Maruyama, H., Morino, H., Ito, H., Izumi, Y., Kato, H., Watanabe, Y., Kinoshita, Y., Kamada, M., Nodera, H., Suzuki, H., et al. (2010) · Nature · doi:10.1038/nature08971 · Cited by 1,265
Exome Sequencing Reveals VCP Mutations as a Cause of Familial ALS
Johnson, J. O., Mandrioli, J., Benatar, M., Abramzon, Y., Van Deerlin, V. M., Trojanowski, J. Q., Gibbs, J. R., Brunetti, M., Gronka, S., Wuu, J., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.036 · Cited by 1,235
Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia
Deng, H.-X., Chen, W., Hong, S.-T., Boycott, K. M., Gorrie, G. H., Siddique, N., Yang, Y., Fecto, F., Shi, Y., Zhai, H., et al. (2011) · Nature · doi:10.1038/nature10353 · Cited by 1,174
Neuropathologic diagnostic and nosologic criteria for frontotemporal lobar degeneration: consensus of the Consortium for Frontotemporal Lobar Degeneration
Cairns, N. J., Bigio, E. H., Mackenzie, I. R. A., Neumann, M., Lee, V. M.-Y., Hatanpaa, K. J., White, C. L., Schneider, J. A., Grinberg, L. T., Halliday, G., et al. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0237-2 · Cited by 1,110
Nomenclature and nosology for neuropathologic subtypes of frontotemporal lobar degeneration: an update
Mackenzie, I. R. A., Neumann, M., Bigio, E. H., Cairns, N. J., Alafuzoff, I., Kril, J., Kovacs, G. G., Ghetti, B., Halliday, G., Holm, I. E., et al. (2010) · Acta Neuropathologica · doi:10.1007/s00401-009-0612-2 · Cited by 1,012

Show all 35 references

Sorted by citations

Items 201–300 of 472

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
Looking beneath the surface: the importance of subcortical structures in frontotemporal dementia
Bocchetta, M., Malpetti, M., Todd, E. G., Rowe, J. B., & Rohrer, J. D. (2021) · Brain Communications · doi:10.1093/braincomms/fcab158 · Cited by 53
High frequency of the expanded C9ORF72 hexanucleotide repeat in familial and sporadic Greek ALS patients
Mok, K. Y., Koutsis, G., Schottlaender, L., Polke, J. M., Πάνας, Μ., & Houlden, H. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.02.021 · Cited by 50
An insoluble frontotemporal lobar degeneration-associated TDP-43 C-terminal fragment causes neurodegeneration and hippocampus pathology in transgenic mice
Walker, A. K., Tripathy, K., Restrepo, C. R., Ge, G., Xu, Y., Kwong, L. K., Trojanowski, J. Q., & Lee, V. M. ‐. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv424 · Cited by 50
C9ORF72 dipeptide repeat poly-GA inclusions promote intracellular aggregation of phosphorylated TDP-43
Nonaka, T., Masuda‐Suzukake, M., Hosokawa, M., Shimozawa, A., Hirai, S., Okado, H., & Hasegawa, M. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy174 · Cited by 53
Synaptic localization of C9orf72 regulates post-synaptic glutamate receptor 1 levels
Xiao, S., McKeever, P. M., Lau, A., & Robertson, J. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0812-5 · Cited by 50
Frontotemporal lobar degeneration with TDP‐43 proteinopathy and chromosome 9p repeat expansion in C9ORF72: clinicopathologic correlation
Bigio, E. H., Weıntraub, S., Rademakers, R., Baker, M. C., Ahmadian, S. S., RADEMAKER, A. W., Weitner, B. B., Mao, Q., Lee, K. ‐., Mishra, M., et al. (2012) · Neuropathology · doi:10.1111/j.1440-1789.2012.01332.x · Cited by 47
Matrin 3 Is a Component of Neuronal Cytoplasmic Inclusions of Motor Neurons in Sporadic Amyotrophic Lateral Sclerosis
Tada, M., Doi, H., Koyano, S., Kubota, S., Fukai, R., Hashiguchi, S., Hayashi, N., Kawamoto, Y., Kunii, M., Tanaka, K., et al. (2017) · American Journal Of Pathology · doi:10.1016/j.ajpath.2017.10.007 · Cited by 47
Motor Neuron Gene Therapy: Lessons from Spinal Muscular Atrophy for Amyotrophic Lateral Sclerosis
Tosolini, A. P., & Sleigh, J. N. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00405 · Cited by 48
Karyopherin abnormalities in neurodegenerative proteinopathies
Pasha, T., Zatorska, A., Sharipov, D., Rogelj, B., Hortobágyi, T., & Hirth, F. (2021) · Brain · doi:10.1093/brain/awab201 · Cited by 51
Self-citation
Ubiquilin immunoreactivity in cytoplasmic and nuclear inclusions in synucleinopathies, polyglutamine diseases and intranuclear inclusion body disease
Mori, F., Tanji, K., Odagiri, S., Toyoshima, Y., Yoshida, M., Ikeda, T., Sasaki, H., Kakita, A., Takahashi, H., & Wakabayashi, K. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0999-z · Cited by 47
The Role of Retrotransposons and Endogenous Retroviruses in Age-Dependent Neurodegenerative Disorders
Frost, B., & Dubnau, J. (2024) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-082823-020615 · Cited by 45
Systemic overexpression of SQSTM1/p62 accelerates disease onset in a SOD1H46R-expressing ALS mouse model
Mitsui, S., Otomo, A., Nozaki, M., Ono, S., Sato, K., Shirakawa, R., Adachi, H., Aoki, M., Sobue, G., Shang, H., et al. (2018) · Molecular Brain · doi:10.1186/s13041-018-0373-8 · Cited by 48
Astrocytes and Microglia as Potential Contributors to the Pathogenesis of C9orf72 Repeat Expansion-Associated FTLD and ALS
Rostalski, H., Leskelä, S., Huber, N., Katisko, K., Cajanus, A., Solje, E., Marttinen, M., Natunen, T., Remes, A. M., Hiltunen, M. O., et al. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00486 · Cited by 47
All Roads Lead to Rome: Different Molecular Players Converge to Common Toxic Pathways in Neurodegeneration
Argueti-Ostrovsky, S., Alfahel, L., Kahn, J., & Israelson, A. (2021) · Cells · doi:10.3390/cells10092438 · Cited by 46
Oligogenic inheritance of optineurin (OPTN) and C9ORF72 mutations in ALS highlights localisation of OPTN in the TDP‐43‐negative inclusions of C9ORF72‐ALS
Bury, J. J., Highley, J. R., Cooper‐Knock, J., Goodall, G., Higginbottom, A., McDermott, C. J., Ince, P. G., Shaw, P. J., & Kirby, J. (2015) · Neuropathology · doi:10.1111/neup.12240 · Cited by 47
Genetics of frontotemporal lobar degeneration: An up-date and diagnosis algorithm
Ber, I. L. (2013) · Revue Neurologique · doi:10.1016/j.neurol.2013.07.014 · Cited by 52
Evidence that the presynaptic vesicle protein CSPalpha is a key player in synaptic degeneration and protection in Alzheimer’s disease
Tiwari, S. S., d’Orange, M., Troakes, C., Shurovi, B. N., Engmann, O., Noble, W. J., Hortobágyi, T., & Giese, K.-P. (2015) · Molecular Brain · doi:10.1186/s13041-015-0096-z · Cited by 47
Self-citation
Microstructural Changes across Different Clinical Milestones of Disease in Amyotrophic Lateral Sclerosis
Trojsi, F., Caiazzo, G., Corbo, D., Piccirillo, G., Cristillo, V., Femiano, C., Ferrantino, T., Cirillo, M., Monsurrò, M. R., Esposito, F., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0119045 · Cited by 43
Genetic counseling for FTD/ALS caused by the C9ORF72 hexanucleotide expansion
Fong, J. C., Karydas, A. M., & Goldman, J. S. (2012) · Alzheimer s Research & Therapy · doi:10.1186/alzrt130 · Cited by 46
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
Survival and Prognostic Factors in C9orf72 Repeat Expansion Carriers
Glasmacher, S. A., Wong, C., Pearson, I., & Pal, S. (2019) · JAMA Neurology · doi:10.1001/jamaneurol.2019.3924 · Cited by 43
A pathogenic progranulin mutation and C9orf72 repeat expansion in a family with frontotemporal dementia
Lashley, T., Rohrer, J. D., Mahoney, C., Gordón, E., Beck, J. A., Mead, S., Warren, J. D., Rossor, M. N., & Révész, T. (2013) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12100 · Cited by 42
Frequency of C9orf72 repeat expansions in amyotrophic lateral sclerosis: a Belgian cohort study
Debray, S., Race, V., Crabbé, V., Herdewyn, S., Matthijs, G., Goris, A., Dubois, B., Thijs, V., Robberecht, W., & Damme, P. V. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.06.009 · Cited by 42
Molecular Network Analysis Suggests a Logical Hypothesis for the Pathological Role of C9orf72 in Amyotrophic Lateral Sclerosis/Frontotemporal Dementia
Satoh, J., Yamamoto, Y., Kitano, S., Takitani, M., Asahina, N., & Kino, Y. (2014) · Journal of Central Nervous System Disease · doi:10.4137/jcnsd.s18103 · Cited by 44
The imaging signature of C9orf72 hexanucleotide repeat expansions: implications for clinical trials and therapy development
Shing, S. L. H., McKenna, M. C., Siah, W. F., Chipika, R. H., Hardiman, O. M., & Bede, P. (2021) · Brain Imaging and Behavior · doi:10.1007/s11682-020-00429-w · Cited by 43
Distinct TDP-43 pathology in ALS patients with ataxin 2 intermediate-length polyQ expansions
Hart, M. P., Brettschneider, J., Lee, V. M. ‐., Trojanowski, J. Q., & Gitler, A. D. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0985-5 · Cited by 44
Prevalence of brain and spinal cord inclusions, including dipeptide repeat proteins, in patients with the C 9 ORF 72 hexanucleotide repeat expansion: a systematic neuropathological review
Schipper, L. J., Raaphorst, J., Aronica, E., Baas, F., de Haan, R. J., de Visser, M., & Troost, D. (2015) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12284 · Cited by 51
Clinicopathologic report of ocular involvement in ALS patients with C9orf72 mutation
Fawzi, A. A., Simonett, J. M., Purta, P., Moss, H. E., Lowry, J., Deng, H., Siddique, N., Sufit, R. L., Bigio, E. H., Volpe, N. J., et al. (2014) · Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration · doi:10.3109/21678421.2014.951941 · Cited by 41
Spatial transcriptomics identifies spatially dysregulated expression of GRM3 and USP47 in amyotrophic lateral sclerosis
Gregory, J. M., McDade, K., Livesey, M. R., Croy, I., de Procé, S. M., Aitman, T. J., Chandran, S., & Smith, C. (2020) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12597 · Cited by 41
Selective neuronal degeneration in MATR3 S85C knock-in mouse model of early-stage ALS
Kao, C. S., van Bruggen, R., Kim, J. R., Chen, X. X., Chan, C., Lee, J., Cho, W. I., Zhao, M., Arndt, C., Maksimovic, K., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-18949-w · Cited by 41
ALS-related misfolded protein management in motor neurons and muscle cells
Galbiati, M., Crippa, V., Rusmini, P., Cristofani, R., Cicardi, M. E., Giorgetti, E., Onesto, E., Messi, E., & Poletti, A. (2014) · Neurochemistry International · doi:10.1016/j.neuint.2014.10.007 · Cited by 42
Macular sub-layer thinning and association with pulmonary function tests in Amyotrophic Lateral Sclerosis
Simonett, J. M., Huang, R., Siddique, N., Farsiu, S., Siddique, T., Volpe, N. J., & Fawzi, A. A. (2016) · Scientific Reports · doi:10.1038/srep29187 · Cited by 42
Soluble and insoluble dipeptide repeat protein measurements in C9orf72-frontotemporal dementia brains show regional differential solubility and correlation of poly-GR with clinical severity
Quaegebeur, A., Glaria, I., Lashley, T., & Isaacs, A. M. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01036-y · Cited by 46
The Genetics of C9orf72 ExpansionsPreprint
Gijselinck, I., Cruts, M., & Broeckhoven, C. V. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026757 · Cited by 43
Detection of a novel frameshift mutation and regions with homozygosis within ARHGEF28 gene in familial amyotrophic lateral sclerosis
Droppelmann, C. A., Wang, J., Campos‐Melo, D., Keller, B. A., Volkening, K., Hegele, R. A., & Strong, M. J. (2013) · Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration · doi:10.3109/21678421.2012.758288 · Cited by 39
Brain functional connectome abnormalities in amyotrophic lateral sclerosis are associated with disability and cortical hyperexcitability
Geevasinga, N., Korgaonkar, M. S., Menon, P., van den Bos, M. A. J., Gomes, L., Foster, S., Kiernan, M. C., & Vucic, S. (2017) · European Journal of Neurology · doi:10.1111/ene.13461 · Cited by 39
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
Highly Immunoreactive IgG Antibodies Directed against a Set of Twenty Human Proteins in the Sera of Patients with Amyotrophic Lateral Sclerosis Identified by Protein Array
May, C., Nordhoff, E., Casjens, S., Turewicz, M., Eisenacher, M., Gold, R., Brüning, T., Pesch, B., Stephan, C., Woitalla, D., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089596 · Cited by 40
Motoneuronal and muscle-selective removal of ALS-related misfolded proteins
Crippa, V., Galbiati, M., Boncoraglio, A., Rusmini, P., Onesto, E., Giorgetti, E., Cristofani, R., Zito, A., & Poletti, A. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130118 · Cited by 41
Sporadic ALS with compound heterozygous mutations in the SQSTM1 gene
Shimizu, H., Toyoshima, Y., Shiga, A., Yokoseki, A., Arakawa, K., Sekine, Y., Shimohata, T., Ikeuchi, T., Nishizawa, M., Kakita, A., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1150-5 · Cited by 42
TDP-43 cytoplasmic inclusion formation is disrupted in C9orf72-associated amyotrophic lateral sclerosis/frontotemporal lobar degeneration
Lee, S. M., Asress, S., Hales, C. M., Gearing, M., Vizcarra, J. C., Fournier, C. N., Gutman, D. A., Chin, L., Li, L., & Glass, J. D. (2019) · Brain Communications · doi:10.1093/braincomms/fcz014 · Cited by 41
Upregulation of ATG7 attenuates motor neuron dysfunction associated with depletion of TARDBP/TDP-43
Donde, A., Sun, M., Jeong, Y. H., Wen, X., Ling, J. P., Lin, S. Z., Braunstein, K. E., Nie, S., Wang, S., Chen, L., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1635379 · Cited by 39
Neuropathological spectrum of anti-IgLON5 disease and stages of brainstem tau pathology: updated neuropathological research criteria of the disease-related tauopathy
Gelpí, E., Reinecke, R., Gaig, C., Iranzo, Á., Sabater, L., Molina‐Porcel, L., Aldecoa, I., Endmayr, V., Högl, B., Schmutzhard, E., et al. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02805-y · Cited by 36
A new Drosophila model of Ubiquilin knockdown shows the effect of impaired proteostasis on locomotive and learning abilities
Jantrapirom, S., Piccolo, L. L., Yoshida, H., & Yamaguchi, M. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.12.010 · Cited by 36
Potential benefits of medium chain fatty acids in aging and neurodegenerative disease
Dunn, E., Zhang, B., Sahota, V. K., & Augustin, H. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1230467 · Cited by 38
C9orf72-catalyzed GTP loading of Rab39A enables HOPS-mediated membrane tethering and fusion in mammalian autophagy
Zhang, S., Tong, M., Zheng, D., Huang, H., Li, L., Ungermann, C., Pan, Y., Luo, H., Lei, M., Tang, Z., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42003-0 · Cited by 36
Heavy metals in locus ceruleus and motor neurons in motor neuron disease
Pamphlett, R., & Jew, S. K. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-81 · Cited by 36
Pathogenic mutations in the ALS gene CCNF cause cytoplasmic mislocalization of Cyclin F and elevated VCP ATPase activity
Yu, Y., Nakagawa, T., Morohoshi, A., Nakagawa, M., Ishida, N., Suzuki, N., Aoki, M., & Nakayama, K. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz119 · Cited by 38
An interaction between synapsin and C9orf72 regulates excitatory synapses and is impaired in ALS/FTD
Bauer, C. S., Cohen, R. N., Sironi, F. M., Livesey, M. R., Gillingwater, T. H., Highley, J. R., Fillingham, D. J., Coldicott, I., Smith, E. F., Gibson, Y., et al. (2022) · Acta Neuropathologica · doi:10.1007/s00401-022-02470-z · Cited by 37
Advances and challenges in understanding the multifaceted pathogenesis of amyotrophic lateral sclerosis
Laferrière, F., & Polymenidou, M. (2015) · Swiss Medical Weekly · doi:10.4414/smw.2015.14054 · Cited by 43
Progressive amnestic dementia, hippocampal sclerosis, and mutation in C9ORF72
Murray, M. E., Bieniek, K. F., Greenberg, M. B., DeJesus‐Hernandez, M., Rutherford, N. J., van Blitterswijk, M., Niemantsverdriet, E., Ash, P. E. A., Gendron, T. F., Kouri, N., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1161-2 · Cited by 34
ExpandedC9ORF72Hexanucleotide Repeat in Depressive Pseudodementia
Bieniek, K. F., van Blitterswijk, M., Baker, M., Petrucelli, L., Rademakers, R., & Dickson, D. W. (2014) · JAMA Neurology · doi:10.1001/jamaneurol.2013.6368 · Cited by 36
Altered body schema processing in frontotemporal dementia with C9ORF72 mutations
Downey, L. E., Fletcher, P. D., Golden, H. L., Mahoney, C. J., Agustus, J. L., Schott, J. M., Rohrer, J. D., Beck, J., Mead, S., Rossor, M. N., et al. (2014) · Journal of Neurology, Neurosurgery & Psychiatry · doi:10.1136/jnnp-2013-306995 · Cited by 34
Recent advances in the molecular genetics of frontotemporal lobar degeneration
Rainero, I. (2017) · Functional Neurology · doi:10.11138/fneur/2017.32.1.007 · Cited by 34
TDP-43 pathology in a case of hereditary spastic paraplegia with a NIPA1/SPG6 mutation
Martinez‐Lage, M., Molina‐Porcel, L., Falcone, D., McCluskey, L. F., Lee, V. M. ‐., Deerlin, V. M. V., & Trojanowski, J. Q. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0947-y · Cited by 34
Amyotrophic lateral sclerosis
Younger, D. S., & Brown, R. H. (2023) · Handbook of clinical neurology · doi:10.1016/b978-0-323-98817-9.00031-4 · Cited by 35
Mitochondria: A Promising Convergent Target for the Treatment of Amyotrophic Lateral Sclerosis
Cunha‐Oliveira, T., Montezinho, L., Simões, R. F., de Carvalho, M., Ferreiro, E. B., & Silva, F. S. G. (2024) · Cells · doi:10.3390/cells13030248 · Cited by 34
Molecular hallmarks of ageing in amyotrophic lateral sclerosis
Jagaraj, C. J., Shadfar, S., Kashani, S. A., Saravanabavan, S., Farzana, F., & Atkin, J. D. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05164-9 · Cited by 39
C9ORF72 Mutations in Neurodegenerative Diseases
Liu, Y., Yu, J., Zong, Y., Zhou, J., & Tan, L. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8528-1 · Cited by 36
Pathophysiology and Treatment of Non-motor Dysfunction in Amyotrophic Lateral Sclerosis
Mahoney, C., Ahmed, R. M., Huynh, W., Tu, S., Rohrer, J. D., Bedlack, R., Hardiman, O. M., & Kiernan, M. C. (2021) · CNS Drugs · doi:10.1007/s40263-021-00820-1 · Cited by 38
RNA-Binding Protein Misregulation in Microsatellite Expansion Disorders
Goodwin, M., & Swanson, M. S. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-1-4939-1221-6_10 · Cited by 33
Frontotemporal dementia
Devenney, E. M., Ahmed, R. M., & Hodges, J. R. (2019) · Handbook of clinical neurology · doi:10.1016/b978-0-12-804766-8.00015-7 · Cited by 40
Neuroimaging features of C9ORF72 expansion
Yokoyama, J. S., & Rosen, H. J. (2012) · Alzheimer s Research & Therapy · doi:10.1186/alzrt148 · Cited by 35
Clinical Characteristics of C9ORF72-Linked Frontotemporal Lobar Degeneration
Kaivorinne, A.-L., Bode, M. K., Paavola, L. E., Tuominen, H. J., Kallio, M., Renton, A. E., Traynor, B. J., Moilanen, V., & Remes, A. M. (2013) · Dementia and Geriatric Cognitive Disorders Extra · doi:10.1159/000351859 · Cited by 33
Drosha Inclusions Are New Components of Dipeptide-Repeat Protein Aggregates in FTLD-TDP and ALSC9orf72Expansion Cases
Porta, S., Kwong, L. K., Trojanowski, J. Q., & Lee, V. M. ‐. (2015) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000182 · Cited by 34
Systematic Screening of Ubiquitin/p62 Aggregates in Cerebellar Cortex Expands the Neuropathological Phenotype of the C9orf72 Expansion Mutation
Ramos‐Campoy, O., Polo, R. Á., Grau‐Rivera, O., Antonell, A., Clarimón, J., Rojas‐García, R., Charif, S., Santiago-Valera, V., Hernandez, I., Aguilar, M., et al. (2018) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nly047 · Cited by 32
Molecular Pathology of ALS: What We Currently Know and What Important Information Is Still Missing
Jankovská, N., & Matěj, R. (2021) · Diagnostics · doi:10.3390/diagnostics11081365 · Cited by 36
Staufen Impairs Autophagy in Neurodegeneration
Paul, S., Dansithong, W., Gandelman, M., Figueroa, K. P., Zu, T., Ranum, L. P. W., Scoles, D. R., & Pulst, S. M. (2022) · Annals of Neurology · doi:10.1002/ana.26515 · Cited by 32
Autophagy and lysosomal pathways in nervous system disorders
Bingol, B. (2018) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2018.04.009 · Cited by 32
Glial Cell Dysfunction in C9orf72-Related Amyotrophic Lateral Sclerosis and Frontotemporal Dementia
Ghasemi, M., Keyhanian, K., & Douthwright, C. L. (2021) · Cells · doi:10.3390/cells10020249 · Cited by 35
Multiple pathways of toxicity induced by C9orf72 dipeptide repeat aggregates and G4C2 RNA in a cellular model
Frottin, F., Pérez‐Berlanga, M., Hartl, F. U., & Hipp, M. S. (2021) · eLife · doi:10.7554/elife.62718 · Cited by 33
Progressive Cerebrocerebellar Uncoupling in Sporadic and Genetic Forms of Amyotrophic Lateral Sclerosis
Tahedl, M., Tan, E. L., Kleinerová, J., Delaney, S., Hengeveld, J. C., Doherty, M. A., McLaughlin, R. L., Pradat, P., Raoul, C., Ango, F., et al. (2024) · Neurology · doi:10.1212/wnl.0000000000209623 · Cited by 30
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
ALS-FUS pathology revisited: singleton FUS mutations and an unusual case with both a FUS and TARDBP mutation
King, A., Troakes, C., Smith, B. N., Nolan, M., Curran, O. E., Vance, C. A., Shaw, C. E., & Al‐Sarraj, S. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0235-x · Cited by 32
Self-citation
The emerging role of minor intron splicing in neurological disorders
Jutzi, D., Akinyi, M. V., Mechtersheimer, J., Frilander, M. J., & Ruepp, M. (2018) · Cell Stress · doi:10.15698/cst2018.03.126 · Cited by 30
Cerebrospinal fluid Aβ40 is similarly reduced in patients with Frontotemporal Lobar Degeneration and Alzheimer's Disease
Baldeiras, I., Santana, I. J., Leitão, M. J., Ribeiro, M. H., Pascoal, R., Duro, D., Lemos, R., Santiago, B., Almeida, M. R., & Oliveira, C. R. (2015) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2015.09.022 · Cited by 30
Proteomic profiling of the spinal cord in ALS: decreased ATP5D levels suggest synaptic dysfunction in ALS pathogenesis
Engelen-Lee, J.-Y., Blokhuis, A. M., Spliet, W. G. M., Pasterkamp, R. J., Aronica, E., Demmers, J., Broekhuizen, R., Nardo, G., Bovenschen, N., & van den Berg, L. H. (2016) · Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration · doi:10.1080/21678421.2016.1245757 · Cited by 31
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
Detection of TDP‐43 oligomers in frontotemporal lobar degeneration–TDP
Kao, P. F., Chen, Y., Liu, X., DeCarli, C. S., Seeley, W. W., & Jin, L. (2015) · Annals of Neurology · doi:10.1002/ana.24431 · Cited by 28
Frontotemporal lobar degeneration and amyotrophic lateral sclerosis: Molecular similarities and differences
Neumann, M. (2013) · Revue Neurologique · doi:10.1016/j.neurol.2013.07.019 · Cited by 30
Monocytes of patients with amyotrophic lateral sclerosis linked to gene mutations display altered TDP‐43 subcellular distribution
Marco, G. D., Lomartire, A., Calvo, A., Risso, A., Luca, E. D., Mostert, M., Mandrioli, J., Caponnetto, C., Borghero, G., Manera, U., et al. (2016) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12328 · Cited by 30
Biological Spectrum of Amyotrophic Lateral Sclerosis PrionsPreprint
Polymenidou, M., & Cleveland, D. W. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024133 · Cited by 29
RETRACTED ARTICLE: A new inducible transgenic mouse model for C9orf72-associated GGGGCC repeat expansion supports a gain-of-function mechanism in C9orf72-associated ALS and FTD
Hukema, R. K., Riemslagh, F. W., Melhem, S., van der Linde, H. C., Severijnen, L.-A. W. F. M., Edbauer, D., Maas, A., Charlet‐Berguerand, N., Willemsen, R., & Swieten, J. C. V. (2014) · Acta Neuropathologica Communications · doi:10.1186/s40478-014-0166-y · Cited by 27
Retracted
Activation of the Nrf2 Pathway as a Therapeutic Strategy for ALS Treatment
Arslanbaeva, L. R., & Bisaglia, M. (2022) · Molecules · doi:10.3390/molecules27051471 · Cited by 27
Current advances in neuronal intranuclear inclusion disease
Bao, L., Zuo, D., Li, Q., Chen, H., & Cui, G. (2023) · Neurological Sciences · doi:10.1007/s10072-023-06677-0 · Cited by 27
ALS-Associated KIF5A Mutation Causes Locomotor Deficits Associated with Cytoplasmic Inclusions, Alterations of Neuromuscular Junctions, and Motor Neuron Loss
Soustelle, L., Aimond, F., López-Andrés, C., Brugioti, V., Raoul, C., & Layalle, S. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.0562-23.2023 · Cited by 27
Convergent molecular defects underpin diverse neurodegenerative diseases
Tofaris, G. K., & Buckley, N. J. (2018) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2017-316988 · Cited by 30
The converging roles of sequestosome-1/p62 in the molecular pathways of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD)
Davidson, J. M., Chung, R. S., & Lee, A. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105653 · Cited by 29
The pathogenesis of amyotrophic lateral sclerosis: Mitochondrial dysfunction, protein misfolding and epigenetics
Chen, W., Guo, L., Li, M., Wei, C., Li, S., & Xu, R. (2022) · Brain Research · doi:10.1016/j.brainres.2022.147904 · Cited by 26
Cognitive and behavioral features of c9FTD/ALS
Boeve, B. F., & Graff‐Radford, N. R. (2012) · Alzheimer s Research & Therapy · doi:10.1186/alzrt132 · Cited by 26
Increased prevalence of granulovacuolar degeneration in C9orf72 mutation
Brainbank NeuroCEB Neuropathology Network, Riku, Y., Duyckaerts, C. J., Boluda, S., Plu, I., Ber, I. L., Millecamps, S., Salachas, F., Yoshida, M., Ando, T., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02028-6 · Cited by 25
Cerebellum in neurodegenerative diseases: Advances, challenges, and prospects
Liu, G., Yang, C., Wang, X., Chen, X., Cai, H., & Le, W. (2024) · iScience · doi:10.1016/j.isci.2024.111194 · Cited by 25
The clinical and pathological phenotypes of frontotemporal dementia with C9ORF72 mutations
Liu, Y., Yu, J., Sun, F.-R., Ou, J.-R., Qu, S.-B., & Tan, L. (2013) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2013.09.013 · Cited by 27
Autophagy‐Mediated Inflammatory Cytokine Secretion in Sporadic ALS Patient iPSC‐Derived Astrocytes
BaofengFeng, Amponsah, A. E., Guo, R., Liu, X., Zhang, J., Du, X., Zhou, Z., He, J., Ma, J., & Cui, H. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/6483582 · Cited by 24
C9ORF72 hexanucleotide repeats in behavioral and motor neuron disease: clinical heterogeneity and pathological diversity.
Yokoyama, J. S., Sirkis, D. W., & Miller, B. L. (2014) · Europe PMC (PubMed Central) · Cited by 24
Genetic Testing for Amyotrophic Lateral Sclerosis and Frontotemporal Dementia
Roggenbuck, J., & Fong, J. C. (2020) · Clinics in Laboratory Medicine · doi:10.1016/j.cll.2020.05.002 · Cited by 24
Distinct neuroinflammatory signatures exist across genetic and sporadic amyotrophic lateral sclerosis cohorts
Rifai, O. M., O’Shaughnessy, J., Dando, O., Munro, A. F., Sewell, M. D. E., Abrahams, S., Waldron, F. M., Sibley, C. R., & Gregory, J. M. (2023) · Brain · doi:10.1093/brain/awad243 · Cited by 23
First-in-class thyrotropin-releasing hormone (TRH)-based compound binds to a pharmacologically distinct TRH receptor subtype in human brain and is effective in neurodegenerative models
Kelly, J., Boyle, N. T., Cole, N., Slator, G. R., Colivicchi, M. A., Stefanini, C., Gobbo, O. L., Scalabrino, G., Ryan, S. M., Elamin, M., et al. (2014) · Neuropharmacology · doi:10.1016/j.neuropharm.2014.09.024 · Cited by 23
Clinical heterogeneity of the C9orf72 genetic mutation in frontotemporal dementia
Devenney, E. M., Foxe, D., Dobson‐Stone, C., Kwok, J. B., Kiernan, M. C., & Hodges, J. R. (2014) · Neurocase · doi:10.1080/13554794.2014.951058 · Cited by 24

Authors: Al-Sarraj, S., King, A., Troakes, C., Smith, B., Maekawa, S., Bodi, I., Rogelj, B., Al-Chalabi, A., Hortobágyi, T., & Shaw, C. E.
Affiliations: King's College London (GB)
Corresponding author: King, Andrew
ORCID: King, Andrew
Troakes, Claire
Smith, Bradley
Rogelj, Boris
Hortobágyi, Tibor
Shaw, Christopher E.
Venue: Acta Neuropathologica
Publisher: Springer Science and Business Media LLC
Published: 2011-11-19
Volume: 122
Issue: 6
Pages: 691-702
ISSN: 0001-6322 (ISSN-L)
1432-0533
DOI: 10.1007/s00401-011-0911-2
OpenAlex: W2066002405
Cited by: 475
References: 35
Citations by year: 2026: 9 · 2025: 9 · 2024: 22 · 2023: 24 · 2022: 23 · 2021: 23 · 2020: 40 · 2019: 27 · 2018: 24 · 2017: 39 · 2016: 38 · 2015: 41 · 2014: 42 · 2013: 63 · 2012: 45
FWCI: 31.22
Type: journal article
Language: en
Open access: green
hdl.handle.net
Licence: other-oa
www.springer.com/tdm (tdm)
Locations: Acta Neuropathologica (publishedVersion)
PubMed (publishedVersion)
University of Debrecen Electronic Archive (University of Debrecen) (submittedVersion, other-oa)
Research Portal (King's College London) (submittedVersion)
Funders: Wellcome Trust (089701)
Medical Research Council (MC_G1000733)
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 › Alzheimer's disease research and treatments
Keywords: p62, TDP-43, C9orf72, hexanucleotide repeat expansion, amyotrophic lateral sclerosis, motor neuron disease, frontotemporal lobar degeneration, FTLD-TDP, neuronal cytoplasmic inclusions, neuronal intranuclear inclusions, cerebellum, hippocampus, Purkinje cells, neurodegeneration, protein aggregation
MeSH terms: Sequestosome-1 Protein, C9orf72 Protein, Adult, Aged, Aged, 80 and over, Amyotrophic Lateral Sclerosis, Inclusion Bodies, Cerebellum, DNA, DNA-Binding Proteins, Female, Hippocampus, Humans, Male, Middle Aged, Mutation, Neurons, Proteins, Purkinje Cells, Case-Control Studies, Pyramidal Cells, DNA Repeat Expansion, Intranuclear Inclusion Bodies, Adaptor Proteins, Signal Transducing, Frontotemporal Lobar Degeneration

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

p62 positive, TDP-43 negative, neuronal cytoplasmic and intranuclear inclusions in the cerebellum and hippocampus define the pathology of C9orf72-linked FTLD and MND/ALS

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks