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Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis
Abstract
Ubiquitin-positive, tau- and α-synuclein–negative inclusions are hallmarks of frontotemporal lobar degeneration with ubiquitin-positive inclusions and amyotrophic lateral sclerosis. Although the identity of the ubiquitinated protein specific to either disorder was unknown, we showed that TDP-43 is the major disease protein in both disorders. Pathologic TDP-43 was hyper-phosphorylated, ubiquitinated, and cleaved to generate C-terminal fragments and was recovered only from affected central nervous system regions, including hippocampus, neocortex, and spinal cord. TDP-43 represents the common pathologic substrate linking these neurodegenerative disorders.
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In the citing paper
“In 2006, hyperphosphorylated and ubiquitinated TDP-43 (encoded by TARDBP) cytoplasmic inclusions were identified as the most common (at about 97%) pathological hallmark of ALS.79”
From Role of neuroinflammation in neurodegeneration development (2023) · cites this paper as [79]
In the citing paper
“Degenerating motor neurons in ALS patients commonly display cytoplasmic aggregates containing the DNA/RNA-binding protein TDP-43 (Neumann et al. 2006).”
From Emerging complexity of the HuD/ELAVl4 gene; implications for neuronal development, function, and dysfunction (2013) · cites this paper as Neumann et al. 2006
In the citing paper
“Cytoplasmic TDP43 mislocalization and aggregation are pathological hallmarks of amyotrophic lateral sclerosis (ALS).”
From Nemo-like kinase disrupts nuclear import and drives TDP43 mislocalization in ALS (2025) · cites this paper as [2]
In the citing paper
“TDP‐43 inclusions are also observed in > 95% of ALS, 22 supporting the notion that FTLD‐TDP and ALS are part of a clinicopathological continuum.”
From New developments of biofluid‐based biomarkers for routine diagnosis and disease trajectories in frontotemporal dementia (2022) · cites this paper as [22]
In the citing paper
“The scarcity of these samples has prompted efforts to enrich cohorts with FTD syndromes that are highly correlated with a specific underlying neuropathology (e.g., FTD‐ALS for FTLD‐TDP 22 or PSP and CBS for FTLD‐tau 119 , 120 ) and/or to jointly analyze data from both combined cohorts of sporadic and familial cases with the same neuropathology background.”
From New developments of biofluid‐based biomarkers for routine diagnosis and disease trajectories in frontotemporal dementia (2022) · cites this paper as [22]
In the citing paper
“biochemical and histopathologic examination of frontotemporal cortex and spinal cord in sALS patients reveals that ubiquitin-positive inclusions contain TARDBP [274,275]”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [275]
Citations
Cites
Frontotemporal lobar degeneration: A consensus on clinical diagnostic criteria
Neary, D., Snowden, J. S., Gustafson, L., Passant, U., Stuss, D., Black, S., Freedman, M., Kertesz, A., Robert, P. H., Albert, M., et al. (1998) · Neurology · doi:10.1212/wnl.51.6.1546 · Cited by 5,047
Self-citationAssociation of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498
Self-citationMutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17
Baker, M., Mackenzie, I. R., Pickering-Brown, S. M., Gass, J., Rademakers, R., Lindholm, C., Snowden, J., Adamson, J., Sadovnick, A. D., Rollinson, S., et al. (2006) · Nature · doi:10.1038/nature05016 · Cited by 2,058
Self-citationCruts, M., Gijselinck, I., van der Zee, J., Engelborghs, S., Wils, H., Pirici, D., Rademakers, R., Vandenberghe, R., Dermaut, B., Martin, J.-J., et al. (2006) · Nature · doi:10.1038/nature05017 · Cited by 1,512
Clinical and Pathological Diagnosis of Frontotemporal Dementia
McKhann, G. M. (2001) · Archives of Neurology · doi:10.1001/archneur.58.11.1803 · Cited by 1,478
Tau is a candidate gene for chromosome 17 frontotemporal dementia
Poorkaj, P., Bird, T. D., Wijsman, E., Nemens, E., Garruto, R. M., Anderson, L., Andreadis, A., Wiederholt, W. C., Raskind, M., & Schellenberg, G. D. (1998) · Annals of Neurology · doi:10.1002/ana.410430617 · Cited by 1,374
Ou, S.-H. I., Wu, F. K., Harrich, D., Garcı́a-Martı́nez, L. F., & Gaynor, R. B. (1995) · Journal of Virology · doi:10.1128/jvi.69.6.3584-3596.1995 · Cited by 762
Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs
Forman, M. S., Trojanowski, J. Q., & Lee, V. M.-Y. (2004) · Nature Medicine · doi:10.1038/nm1113 · Cited by 715
Self-citationThe overlap of amyotrophic lateral sclerosis and frontotemporal dementia
Lomen, C. E., Anderson, T. T., & Miller, B. L. (2002) · Neurology · doi:10.1212/wnl.59.7.1077 · Cited by 699
Self-citationNuclear factor TDP‐43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping
Buratti, E., Dörk, T., Zuccato, E., Pagani, F., Romano, M., & Baralle, F. E. (2001) · The EMBO Journal · doi:10.1093/emboj/20.7.1774 · Cited by 633
Research works printed but not linked: 3
- J. K. Johnson et al., Arch. Neurol.62, 925 (2005).
- D. M. Sampathu et al. Am. J. Pathol. in press.
- Z. He, A. Bateman, J. Mol. Med.1, 600 (2003).
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Items 201–279 of 279
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Gregory, J. M., Fagegaltier, D., Phatnani, H., & Harms, M. B. (2020) · Current Genetic Medicine Reports · doi:10.1007/s40142-020-00194-8 · Cited by 83
Brenowitz, W. D., Keene, C. D., Hawes, S. E., Hubbard, R. A., Longstreth, W. T., Woltjer, R. L., Crane, P. K., Larson, E. B., & Kukull, W. A. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.01.017 · Cited by 88
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Huey, E. D., Ferrari, R., Moreno, J. H., Jensen, C., Morris, C. M., Potocnik, F., Kalaria, R. N., Tierney, M., Wassermann, E. M., Hardy, J., et al. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.08.004 · Cited by 82
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BackgroundJohnson, V. E., Stewart, W., Trojanowski, J. Q., & Smith, D. H. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0909-9 · Cited by 87
Sephton, C. F., Cenik, B., Cenik, B. K., Herz, J., & Yu, G. (2012) · bchm · doi:10.1515/hsz-2012-0115 · Cited by 86
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Hedl, T. J., San Gil, R., Cheng, F., Rayner, S. L., Davidson, J. M., De Luca, A., Villalva, M. D., Ecroyd, H., Walker, A. K., & Lee, A. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00548 · Cited by 87
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Wennberg, A. M., Whitwell, J. L., Tosakulwong, N., Weigand, S. D., Murray, M. E., Machulda, M. M., Petrucelli, L., Mielke, M. M., Jack, C. R., Knopman, D. S., et al. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2019.01.008 · Cited by 79
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Hawrot, J., Imhof, S., & Wainger, B. J. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104680 · Cited by 74
Tanji, K., Maruyama, A., Odagiri, S., Mori, F., Itoh, K., Kakita, A., Takahashi, H., & Wakabayashi, K. (2013) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31827b5713 · Cited by 80
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Cooper-Knock, J., Green, C., Altschuler, G., Wei, W., Bury, J. J., Heath, P. R., Wyles, M., Gelsthorpe, C., Highley, J. R., Lorente-Pons, A., et al. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0424-x · Cited by 80
Verstraete, E., Veldink, J. H., Huisman, M. H. B., Draak, T., Uijtendaal, E. V., van der Kooi, A. J., Schelhaas, H. J., de Visser, M., van der Tweel, I., & van den Berg, L. H. (2012) · Journal of Neurology, Neurosurgery & Psychiatry · doi:10.1136/jnnp-2011-302021 · Cited by 78
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Grossman, M., Xie, S. X., Libon, D. J., Wang, X., Massimo, L., Moore, P., Vesely, L., Berkowitz, R., Chatterjee, A., Coslett, H. B., et al. (2008) · Neurology · doi:10.1212/01.wnl.0000303816.25065.bc · Cited by 77
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A systematic review of behavioural changes in motor neuron disease
Raaphorst, J., Beeldman, E., De Visser, M., De Haan, R. J., & Schmand, B. (2012) · Amyotrophic Lateral Sclerosis · doi:10.3109/17482968.2012.656652 · Cited by 75
Neuron Enriched Nuclear Proteome Isolated from Human Brain
Dammer, E. B., Duong, D. M., Diner, I., Gearing, M., Feng, Y., Lah, J. J., Levey, A. I., & Seyfried, N. T. (2013) · Journal of Proteome Research · doi:10.1021/pr400246t · Cited by 70
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Izrael, M., Slutsky, S. G., & Revel, M. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00824 · Cited by 73
Boeve, B. F. (2007) · Alzheimer Disease & Associated Disorders · doi:10.1097/wad.0b013e31815bf454 · Cited by 73
TDP-43 and Inflammation: Implications for Amyotrophic Lateral Sclerosis and Frontotemporal Dementia
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Seyfried, N. T., Gozal, Y. M., Donovan, L. E., Herskowitz, J. H., Dammer, E. B., Xia, Q., Ku, L., Chang, J., Duong, D. M., Rees, H. D., et al. (2012) · Journal of Proteome Research · doi:10.1021/pr2010814 · Cited by 64
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Vickers, J. C., King, A. E., Woodhouse, A., Kirkcaldie, M. T., Staal, J. A., McCormack, G. H., Blizzard, C. A., Musgrove, R. E. J., Mitew, S., Liu, Y., et al. (2009) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2009.08.004 · Cited by 69
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Corcia, P., Couratier, P., Blasco, H., Andres, C. R., Beltran, S., Meininger, V., & Vourc’h, P. (2017) · Revue Neurologique · doi:10.1016/j.neurol.2017.03.030 · Cited by 68
Guerrero, E. N., Mitra, J., Wang, H., Rangaswamy, S., Hegde, P. M., Basu, P., Rao, K. S., & Hegde, M. L. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz062 · Cited by 68
Hiji, M., Takahashi, T., Fukuba, H., Yamashita, H., Kohriyama, T., & Matsumoto, M. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0402-2 · Cited by 68
Josephs, K. A., Mackenzie, I., Frosch, M. P., Bigio, E. H., Neumann, M., Arai, T., Dugger, B. N., Ghetti, B., Grossman, M., Hasegawa, M., et al. (2019) · Brain · doi:10.1093/brain/awz224 · Cited by 66
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Elahi, F. M., Marx, G., Cobigo, Y., Staffaroni, A. M., Kornak, J., Tosun, D., Boxer, A. L., Kramer, J. H., Miller, B. L., & Rosen, H. J. (2017) · NeuroImage: Clinical · doi:10.1016/j.nicl.2017.09.007 · Cited by 59
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Crippa, V., Boncoraglio, A., Galbiati, M., Aggarwal, T., Rusmini, P., Giorgetti, E., Cristofani, R., Carra, S., Pennuto, M., & Poletti, A. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00234 · Cited by 63
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Diner, I., Hales, C. M., Bishof, I., Rabenold, L., Duong, D. M., Yi, H., Laur, O., Gearing, M., Troncoso, J., Thambisetty, M., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.562959 · Cited by 63
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Sato, T., Takeuchi, S., Saito, A., Ding, W., Bamba, H., Matsuura, H., Hisa, Y., Tooyama, I., & Urushitani, M. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.09.050 · Cited by 63
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Sporadic inclusion body myositis: possible pathogenesis inferred from biomarkers.
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Self-citationThe Frontotemporal Syndromes of ALS. Clinicopathological Correlates
Strong, M. J., & Yang, W. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9609-0 · Cited by 41
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Frings, L., Mader, I., Landwehrmeyer, B. G., Weiller, C., Hüll, M., & Huppertz, H. (2012) · Human Brain Mapping · doi:10.1002/hbm.21304 · Cited by 38
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Caccamo, A., Shaw, D. M., Guarino, F., Messina, A., Walker, A. W., & Oddo, S. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv193 · Cited by 35
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BackgroundCristofani, R., Rusmini, P., Galbiati, M., Cicardi, M. E., Ferrari, V., Tedesco, B., Casarotto, E., Chierichetti, M., Messi, E., Piccolella, M., et al. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00796 · Cited by 35
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Cykowski, M. D., Powell, S. Z., Schulz, P. E., Takei, H., Rivera, A. L., Jackson, R. E., Roman, G., Jicha, G. A., & Nelson, P. T. (2017) · Archives of Pathology & Laboratory Medicine · doi:10.5858/arpa.2016-0469-sa · Cited by 33
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Lutz, B. M., & Peng, J. (2018) · Proteomes · doi:10.3390/proteomes6040046 · Cited by 27
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Bajc Česnik, A., Motaln, H., & Rogelj, B. (2020) · Cells · doi:10.3390/cells9081791 · Cited by 17
Gal, J., Katsumata, Y., Zhu, H., Srinivasan, S., Chen, J., Johnson, L. A., Wang, W.-X., Golden, L. R., Wilcock, D. M., Jicha, G. A., et al. (2022) · The American Journal of Pathology · doi:10.1016/j.ajpath.2021.11.013 · Cited by 17
Tejwani, L., Jung, Y., Kokubu, H., Sowmithra, S., Ni, L., Lee, C., Sanders, B., Lee, P. J., Xiang, Y., Luttik, K., et al. (2023) · Journal of Clinical Investigation · doi:10.1172/jci138207 · Cited by 17
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Copley, K. E., Mauna, J. C., Danielson, H. L., Chen, Q., Ozguney, B., Ngo, M., Xie, L., Smirnov, A., Davis, M., Mayne, L., et al. (2026) · Science · doi:10.1126/science.adv3301 · Cited by 16
Moussa, C. E.-H. (2015) · Neurodegenerative Diseases · doi:10.1159/000430888 · Cited by 13
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Schmeing, S., & Hart, P. '. (2024) · WIREs RNA · doi:10.1002/wrna.1877 · Cited by 11
Kim, E.-J., Vatsavayai, S., & Seeley, W. W. (2016) · The Behavioral Neurology of Dementia · doi:10.1017/9781139924771.008 · Cited by 7
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Bekier, M. E., Pinarbasi, E., Krishnan, G., Mesojedec, J. J., Hurley, M., Harikumar Sheela, H., Collins, C. A., Ghaffari, L., de Majo, M., Ullian, E. M., et al. (2025) · Journal of Clinical Investigation · doi:10.1172/jci188138 · Cited by 2
“Despite this, a single pathological hallmark — mislocalization and aggregation of the RNA-binding protein trans-active response DNA-binding protein 43 (TDP43) — is found in more than 95% of individuals with ALS (2).”
InfluentialJami, K. M., Corbett, K. E., Farb, D. C., Osumi, K. M., Shafer, C. C., Criscione, S., & Murray, D. T. (2026) · Biophysical Chemistry · doi:10.1016/j.bpc.2026.107590 · Cited by 2
Metadata
- Authors
- 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., McCluskey, L. F., Miller, B. L., Masliah, E., Mackenzie, I. R., Feldman, H., Feiden, W., Kretzschmar, H. A., Trojanowski, J. Q., & Lee, V. M.-Y.
- Affiliations
- University of Pennsylvania (US)
- Corresponding author
- Neumann, Manuela
- Sampathu, Deepak M.
- Kwong, Linda K.
- Lee, Virginia M.-Y.
- ORCID
- Venue
- Science
- Published
- 2006-10-06
- Volume
- 314
- Issue
- 5796
- Pages
- 130-133
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2003618511
- Cited by
- 6,576
- References
- 25
- Citations by year
- 2026: 341 · 2025: 401 · 2024: 411 · 2023: 405 · 2022: 425 · 2021: 441 · 2020: 442 · 2019: 368 · 2018: 400 · 2017: 339 · 2016: 315 · 2015: 283 · 2014: 305 · 2013: 311 · 2012: 301
- FWCI
- 115.98
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (T32 AG 00255, P30AG010124, P01AG017586, AG17586, AG-10124, P01AG019724, T32AG000255)
- Topics
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Keywords
- TDP-43, frontotemporal lobar degeneration, amyotrophic lateral sclerosis, ubiquitination, C-terminal fragment, ubiquitin-positive inclusions, neurodegeneration, hippocampus, neocortex, spinal cord
- MeSH terms
- Amino Acid Sequence, Amyotrophic Lateral Sclerosis, Antibodies, Monoclonal, Brain Chemistry, Cerebral Cortex, Dementia, DNA-Binding Proteins, Fluorescent Antibody Technique, Hippocampus, Humans, Molecular Sequence Data, Motor Neurons, Neurons, Peptide Fragments, Phosphorylation, Spinal Cord, Immunoblotting, Ubiquitin
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