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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
Flagged first, then by citations
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).
Cited by
Sorted by citations
Items 101–200 of 279
Porta, S., Xu, Y., Restrepo, C. R., Kwong, L. K., Zhang, B., Brown, H. J., Lee, E. B., Trojanowski, J. Q., & Lee, V. M.-Y. (2018) · Nature Communications · doi:10.1038/s41467-018-06548-9 · Cited by 248
Self-citationKramer, N. J., Haney, M. S., Morgens, D. W., Jovičić, A., Couthouis, J., Li, A., Ousey, J., Ma, R., Bieri, G., Tsui, C. K., et al. (2018) · Nature Genetics · doi:10.1038/s41588-018-0070-7 · Cited by 226
The overlapping genetics of amyotrophic lateral sclerosis and frontotemporal dementia
Abramzon, Y. A., Fratta, P., Traynor, B. J., & Chia, R. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00042 · Cited by 244
The microglial NLRP3 inflammasome is activated by amyotrophic lateral sclerosis proteins
Deora, V., Lee, J. D., Albornoz, E. A., McAlary, L., Jagaraj, C. J., Robertson, A. A. B., Atkin, J. D., Cooper, M. A., Schroder, K., Yerbury, J. J., et al. (2020) · Glia · doi:10.1002/glia.23728 · Cited by 245
TDP-43 activates microglia through NF-κB and NLRP3 inflammasome
Zhao, W., Beers, D. R., Bell, S., Wang, J., Wen, S., Baloh, R. H., & Appel, S. H. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.07.019 · Cited by 241
Mutations in SQSTM1 encoding p62 in amyotrophic lateral sclerosis: genetics and neuropathology
Teyssou, E., Takeda, T., Lebon, V., Boillée, S., Doukouré, B., Bataillon, G., Sazdovitch, V., Cazeneuve, C., Meininger, V., LeGuern, E., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1090-0 · Cited by 241
Nelson, P. T., Abner, E. L., Schmitt, F. A., Kryscio, R. J., Jicha, G. A., Smith, C. D., Davis, D. G., Poduska, J. W., Patel, E., Mendiondo, M. S., et al. (2010) · Brain Pathology · doi:10.1111/j.1750-3639.2008.00244.x · Cited by 239
Amyotrophic lateral sclerosis: translating genetic discoveries into therapies
Akçimen, F., Lopez, E. R., Landers, J. E., Nath, A., Chiò, A., Chia, R., & Traynor, B. J. (2023) · Nature Reviews Genetics · doi:10.1038/s41576-023-00592-y · Cited by 234
Mackenzie, I. R. A., Frick, P., Grässer, F. A., Gendron, T. F., Petrucelli, L., Cashman, N. R., Edbauer, D., Kremmer, E., Prudlo, J., Troost, D., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1476-2 · Cited by 231
Self-citationToledo, J. B., Van Deerlin, V. M., Lee, E. B., Suh, E., Baek, Y., Robinson, J. L., Xie, S. X., McBride, J., Wood, E. M., Schuck, T., et al. (2014) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2013.06.003 · Cited by 234
Self-citationLoss of Nuclear TDP-43 Is Associated with Decondensation of LINE Retrotransposons
Liu, E. Y., Russ, J., Cali, C. P., Phan, J. M., Amlie-Wolf, A., & Lee, E. B. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.04.003 · Cited by 231
“A key pathologic hallmark of both diseases is the loss of nuclear TAR DNA binding protein-43 (TDP-43) into cytoplasmic aggregates (Neumann et al., 2006).”
BackgroundHuman TBK1: A Gatekeeper of Neuroinflammation
Ahmad, L., Zhang, S.-Y., Casanova, J.-L., & Sancho-Shimizu, V. (2016) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.04.006 · Cited by 208
Diagnosis and management of motor neurone disease
McDermott, C. J., & Shaw, P. J. (2008) · BMJ · doi:10.1136/bmj.39493.511759.be · Cited by 220
Brady, O. A., Meng, P., Zheng, Y., Mao, Y., & Hu, F. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.07098.x · Cited by 215
Dendritic Spine Pathology in Neurodegenerative Diseases
Herms, J., & Dorostkar, M. M. (2016) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-012615-044216 · Cited by 201
Custer, S. K., Neumann, M., Lu, H., Wright, A. C., & Taylor, J. P. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq050 · Cited by 204
Self-citationMoisse, K., Volkening, K., Leystra-Lantz, C., Welch, I., Hill, T., & Strong, M. J. (2009) · Brain Research · doi:10.1016/j.brainres.2008.10.021 · Cited by 210
Sex: A Significant Risk Factor for Neurodevelopmental and Neurodegenerative Disorders
Pinares-Garcia, P., Stratikopoulos, M., Zagato, A., Loke, H., & Lee, J. (2018) · Brain Sciences · doi:10.3390/brainsci8080154 · Cited by 200
Increased TDP-43 protein in cerebrospinal fluid of patients with amyotrophic lateral sclerosis
Kasai, T., Tokuda, T., Ishigami, N., Sasayama, H., Foulds, P., Mitchell, D. J., Mann, D. M. A., Allsop, D., & Nakagawa, M. (2009) · Acta Neuropathologica · doi:10.1007/s00401-008-0456-1 · Cited by 211
Degradation of TDP-43 and its pathogenic form by autophagy and the ubiquitin-proteasome system
Wang, X., Fan, H., Ying, Z., Li, B., Wang, H., & Wang, G. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2009.11.055 · Cited by 207
The neuropathology associated with repeat expansions in the C9ORF72 gene
Mackenzie, I. R. A., Frick, P., & Neumann, M. (2014) · Acta Neuropathologica · doi:10.1007/s00401-013-1232-4 · Cited by 206
Self-citationAltered Proteins in the Aging Brain
Elobeid, A., Libard, S., Leino, M., Popova, S. N., & Alafuzoff, I. (2016) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlw002 · Cited by 202
Prevalence and clinical phenotype of quadruple misfolded proteins in older adults
Karanth, S., Nelson, P. T., Katsumata, Y., Kryscio, R. J., Schmitt, F. A., Fardo, D. W., Cykowski, M. D., Jicha, G. A., Van Eldik, L. J., & Abner, E. L. (2020) · JAMA Neurology · doi:10.1001/jamaneurol.2020.1741 · Cited by 206
Brkic, M., Balusu, S., Libert, C., & Vandenbroucke, R. E. (2015) · Mediators of Inflammation · doi:10.1155/2015/620581 · Cited by 205
Autophagy and ALS: mechanistic insights and therapeutic implications
Chua, J. P., De Calbiac, H., Kabashi, E., & Barmada, S. J. (2022) · Autophagy · doi:10.1080/15548627.2021.1926656 · Cited by 189
“[274,275], which is itself involved in the regulation of autophagy [276].”
BackgroundSteinacker, P., Hendrich, C., Sperfeld, A. D., Jesse, S., von Arnim, C. A. F., Lehnert, S., Pabst, A., Uttner, I., Tumani, H., Lee, V. M.-Y., et al. (2008) · Archives of Neurology · doi:10.1001/archneur.65.11.1481 · Cited by 199
Self-citationHsieh, Y.-C., Guo, C., Yalamanchili, H. K., Abreha, M., Al-Ouran, R., Li, Y., Dammer, E. B., Lah, J. J., Levey, A. I., Bennett, D. A., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.08.104 · Cited by 196
Geser, F., Lee, V. M.-Y., & Trojanowski, J. Q. (2010) · Neuropathology · doi:10.1111/j.1440-1789.2009.01091.x · Cited by 195
Self-citationTashiro, Y., Urushitani, M., Inoue, H., Koike, M., Uchiyama, Y., Komatsu, M., Tanaka, K., Yamazaki, M., Abe, M., Misawa, H., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.417600 · Cited by 194
TDP‐43 loss of function increases TFEB activity and blocks autophagosome–lysosome fusion
Xia, Q., Wang, H., Hao, Z., Fu, C., Hu, Q., Gao, F., Ren, H., Chen, D., Han, J., Ying, Z., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201591998 · Cited by 195
C9orf72 poly(GR) aggregation induces TDP-43 proteinopathy
Cook, C. N., Wu, Y., Odeh, H. M., Gendron, T. F., Jansen-West, K., del Rosso, G., Yue, M., Jiang, P., Gomes, E., Tong, J., et al. (2020) · Science Translational Medicine · doi:10.1126/scitranslmed.abb3774 · Cited by 193
Neurological consequences of traumatic brain injuries in sports
Ling, H., Hardy, J., & Zetterberg, H. (2015) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2015.03.012 · Cited by 197
Nishihira, Y., Tan, C.-F., Onodera, O., Toyoshima, Y., Yamada, M., Morita, T., Nishizawa, M., Kakita, A., & Takahashi, H. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0385-z · Cited by 187
Hall, C. E., Yao, Z., Choi, M., Tyzack, G. E., Serio, A., Luisier, R., Harley, J., Preza, E., Arber, C., Crisp, S. J., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.05.024 · Cited by 179
The Ubiquitin-Proteasome System and the Autophagic-Lysosomal System in Alzheimer Disease
Ihara, Y., Morishima-Kawashima, M., & Nixon, R. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006361 · Cited by 190
Yu, C.-E., Bird, T. D., Bekris, L. M., Montine, T. J., Leverenz, J. B., Steinbart, E., Galloway, N. M., Feldman, H., Woltjer, R., Miller, C. A., et al. (2010) · Archives of Neurology · doi:10.1001/archneurol.2009.328 · Cited by 190
Self-citationMisregulated RNA processing in amyotrophic lateral sclerosis
Polymenidou, M., Lagier-Tourenne, C., Hutt, K. R., Bennett, C. F., Cleveland, D. W., & Yeo, G. W. (2012) · Brain Research · doi:10.1016/j.brainres.2012.02.059 · Cited by 169
SQSTM1/p62: a potential target for neurodegenerative disease
Ma, S., Attarwala, I. Y., & Xie, X.-Q. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00516 · Cited by 185
CSF biomarkers cutoffs: The importance of coincident neuropathological diseases
Toledo, J. B., Brettschneider, J., Grossman, M., Arnold, S. E., Hu, W. T., Xie, S. X., Lee, V. M.-Y., Shaw, L. M., & Trojanowski, J. Q. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0983-7 · Cited by 182
Self-citationCaccamo, A., Majumder, S., Deng, J. J., Bai, Y., Thornton, F. B., & Oddo, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.031278 · Cited by 169
The Complex Molecular Biology of Amyotrophic Lateral Sclerosis (ALS)
Redler, R. L., & Dokholyan, N. V. (2012) · Progress in Molecular Biology and Translational Science · doi:10.1016/b978-0-12-385883-2.00002-3 · Cited by 172
Aging and Neurodegenerative Disease: Is the Adaptive Immune System a Friend or Foe?
Mayne, K., White, J. A., McMurran, C. E., Rivera, F. J., & de la Fuente, A. G. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.572090 · Cited by 167
Chronic traumatic encephalopathy - confusion and controversies
Smith, D. H., Johnson, V. E., Trojanowski, J. Q., & Stewart, W. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-018-0114-8 · Cited by 166
Self-citationFrontotemporal dementia and related disorders: Deciphering the enigma
Josephs, K. A. (2008) · Annals of Neurology · doi:10.1002/ana.21426 · Cited by 166
Regulation of Autophagy by Neuropathological Protein TDP-43
Bose, J. K., Huang, C.-C., & Shen, C.-K. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.237115 · Cited by 165
18F-flortaucipir (AV-1451) tau PET in frontotemporal dementia syndromes
Tsai, R. M., Bejanin, A., Lesman-Segev, O., LaJoie, R., Visani, A., Bourakova, V., O’Neil, J. P., Janabi, M., Baker, S., Lee, S. E., et al. (2019) · Alzheimer's Research & Therapy · doi:10.1186/s13195-019-0470-7 · Cited by 164
Self-citationProgranulin genetic variability contributes to amyotrophic lateral sclerosis
Sleegers, K., Brouwers, N., Maurer-Stroh, S., van Es, M. A., Damme, P. V., van Vught, P. W. J., van der Zee, J., Serneels, S., Pooter, T. D., Van den Broeck, M., et al. (2008) · Neurology · doi:10.1212/01.wnl.0000289191.54852.75 · Cited by 161
“New Old Pathologies”: AD, PART, and Cerebral Age-Related TDP-43 With Sclerosis (CARTS)
Nelson, P. T., Trojanowski, J. Q., Abner, E. L., Al-Janabi, O. M., Jicha, G. A., Schmitt, F. A., Smith, C. D., Fardo, D. W., Wang, W.-X., Kryscio, R. J., et al. (2016) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlw033 · Cited by 158
Self-citationXie, M., Liu, Y. U., Zhao, S., Zhang, L., Bosco, D. B., Pang, Y.-P., Zhong, J., Sheth, U., Martens, Y. A., Zhao, N., et al. (2022) · Nature Neuroscience · doi:10.1038/s41593-021-00975-6 · Cited by 157
Review: neuropathology of non-tau frontotemporal lobar degeneration
Neumann, M., & Mackenzie, I. R. A. (2019) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12526 · Cited by 144
Self-citationSQSTM1 mutations – Bridging Paget disease of bone and ALS/FTLD
Rea, S. L., Majcher, V., Searle, M. S., & Layfield, R. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.01.020 · Cited by 152
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
Incidence and extent of TDP-43 accumulation in aging human brain
Uchino, A., Takao, M., Hatsuta, H., Sumikura, H., Nakano, Y., Nogami, A., Saito, Y., Arai, T., Nishiyama, K., & Murayama, S. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0215-1 · Cited by 144
The advent of AAV9 expands applications for brain and spinal cord gene delivery
Dayton, R. D., Wang, D. B., & Klein, R. L. (2012) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2012.681463 · Cited by 144
Progranulin deficiency causes impairment of autophagy and TDP-43 accumulation
Chang, M. C., Srinivasan, K., Friedman, B. A., Suto, E., Modrusan, Z., Lee, W. P., Kaminker, J. S., Hansen, D. V., & Sheng, M. (2017) · Journal of Experimental Medicine · doi:10.1084/jem.20160999 · Cited by 141
ALS and other motor neuron diseases
Tiryaki, E., & Horak, H. A. (2014) · Continuum · doi:10.1212/01.con.0000455886.14298.a4 · Cited by 143
Maeda, J., Zhang, M.-R., Okauchi, T., Ji, B., Ono, M., Hattori, S., Kumata, K., Iwata, N., Saido, T. C., Trojanowski, J. Q., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.3076-10.2011 · Cited by 136
Self-citationDownregulation of MicroRNA-9 in iPSC-Derived Neurons of FTD/ALS Patients with TDP-43 Mutations
Zhang, Z., Almeida, S., Lu, Y., Nishimura, A. L., Peng, L., Sun, D., Wu, B., Karydas, A. M., Tartaglia, M. C., Fong, J. C., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076055 · Cited by 142
Self-citationIntercellular Spread of Protein Aggregates in Neurodegenerative Disease
Davis, A. A., Leyns, C. E. G., & Holtzman, D. M. (2018) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100617-062636 · Cited by 131
Progranulin: a new avenue towards the understanding and treatment of neurodegenerative disease
Chitramuthu, B. P., Bennett, H. P. J., & Bateman, A. (2017) · Brain · doi:10.1093/brain/awx198 · Cited by 138
Pottier, C., Zhou, X., Perkerson, R. B., Baker, M., Jenkins, G. D., Serie, D. J., Ghidoni, R., Benussi, L., Binetti, G., López de Munain, A., et al. (2018) · The Lancet Neurology · doi:10.1016/s1474-4422(18)30126-1 · Cited by 131
Self-citationChen-Plotkin, A. S., Geser, F., Plotkin, J. B., Clark, C. M., Kwong, L. K., Yuan, W., Grossman, M., Van Deerlin, V. M., Trojanowski, J. Q., & Lee, V. M.-Y. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn023 · Cited by 135
Self-citationHumphrey, J., Venkatesh, S., Hasan, R., Herb, J. T., de Paiva Lopes, K., Küçükali, F., Byrska-Bishop, M., Evani, U. S., Narzisi, G., Fagegaltier, D., et al. (2023) · Nature Neuroscience · doi:10.1038/s41593-022-01205-3 · Cited by 138
Frontotemporal Lobar Degeneration: Epidemiology, Pathology, Diagnosis and Management
Seltman, R. E., & Matthews, B. R. (2012) · CNS Drugs · doi:10.2165/11640070-000000000-00000 · Cited by 132
Cerebrospinal fluid macrophage biomarkers in amyotrophic lateral sclerosis
Thompson, A. G., Gray, E., Thézénas, M., Charles, P. D., Evetts, S., Hu, M. T., Talbot, K., Fischer, R., Kessler, B. M., & Turner, M. R. (2018) · Annals of Neurology · doi:10.1002/ana.25143 · Cited by 130
Cytoplasmic accumulation and aggregation of TDP-43 upon proteasome inhibition in cultured neurons.
van Eersel, J., Ke, Y. D., Gladbach, A., Bi, M., Götz, J., Kril, J. J., & Ittner, L. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022850 · Cited by 130
Leverenz, J. B., Yu, C. E., Montine, T. J., Steinbart, E., Bekris, L. M., Zabetian, C., Kwong, L. K., Lee, V. M.-Y., Schellenberg, G. D., & Bird, T. D. (2007) · Brain · doi:10.1093/brain/awm069 · Cited by 129
Self-citationFluid biomarkers in frontotemporal dementia: past, present and future
Swift, I. J., Sogorb-Esteve, A., Heller, C., Synofzik, M., Otto, M., Graff, C., Galimberti, D., Todd, E., Heslegrave, A. J., van der Ende, E. L., et al. (2021) · Journal of Neurology, Neurosurgery & Psychiatry · doi:10.1136/jnnp-2020-323520 · Cited by 122
Rosen, E. Y., Wexler, E. M., Versano, R., Coppola, G., Gao, F., Winden, K. D., Oldham, M. C., Martens, L. H., Zhou, P., Farese, R. V., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.07.021 · Cited by 128
Scialò, C., Tran, T. H., Salzano, G., Novi, G., Caponnetto, C., Chiò, A., Calvo, A., Canosa, A., Moda, F., Caroppo, P., et al. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa142 · Cited by 123
Cerebrospinal fluid neurofilament light chain protein levels in subtypes of frontotemporal dementia
Landqvist Waldö, M., Frizell Santillo, A., Passant, U., Zetterberg, H., Rosengren, L., Nilsson, C., & Englund, E. (2013) · BMC Neurology · doi:10.1186/1471-2377-13-54 · Cited by 127
Bronicki, L. M., & Jasmin, B. J. (2013) · RNA · doi:10.1261/rna.039164.113 · Cited by 126
Feng, T., Lacrampe, A., & Hu, F. (2021) · Acta Neuropathologica · doi:10.1007/s00401-020-02246-3 · Cited by 110
Troakes, C., Maekawa, S., Wijesekera, L., Rogelj, B., Siklós, L., Bell, C., Smith, B., Newhouse, S., Vance, C., Johnson, L., et al. (2012) · Neuropathology · doi:10.1111/j.1440-1789.2011.01286.x · Cited by 124
Repetitive element transcripts are elevated in the brain of C9orf72 ALS/FTLD patients
Prudencio, M., Gonzales, P. K., Cook, C. N., Gendron, T. F., Daughrity, L. M., Song, Y., Ebbert, M. T. W., van Blitterswijk, M., Zhang, Y.-J., Jansen-West, K., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx233 · Cited by 122
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Panza, F., Lozupone, M., Seripa, D., Daniele, A., Watling, M., Giannelli, G., & Imbimbo, B. P. (2020) · Nature Reviews Neurology · doi:10.1038/s41582-020-0330-x · Cited by 122
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Vass, R., Ashbridge, E., Geser, F., Hu, W. T., Grossman, M., Clay-Falcone, D., Elman, L., McCluskey, L., Lee, V. M. Y., Van Deerlin, V. M., et al. (2011) · Acta Neuropathologica · doi:10.1007/s00401-010-0782-y · Cited by 119
Self-citationIs synaptic loss a unique hallmark of Alzheimer’s disease?
Scheff, S. W., Neltner, J. H., & Nelson, P. T. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.12.028 · Cited by 118
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Toth, R. P., & Atkin, J. D. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01017 · Cited by 114
Reduced CSF p-Tau 181 to Tau ratio is a biomarker for FTLD-TDP
Hu, W. T., Watts, K., Grossman, M., Glass, J., Lah, J. J., Hales, C., Shelnutt, M., Van Deerlin, V., Trojanowski, J. Q., & Levey, A. I. (2013) · Neurology · doi:10.1212/01.wnl.0000436625.63650.27 · Cited by 113
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Urushitani, M., Sato, T., Bamba, H., Hisa, Y., & Tooyama, I. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22243 · Cited by 114
Inflammation Induces TDP-43 Mislocalization and Aggregation
Correia, A. S., Patel, P., Dutta, K., & Julien, J.-P. (2015) · PLOS ONE · doi:10.1371/journal.pone.0140248 · Cited by 114
Nelson, P. T., Abner, E. L., Schmitt, F. A., Kryscio, R. J., Jicha, G. A., Santacruz, K., Smith, C. D., Patel, E., & Markesbery, W. R. (2009) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181aacbe9 · Cited by 115
Zhang, H., Tan, C.-F., Mori, F., Tanji, K., Kakita, A., Takahashi, H., & Wakabayashi, K. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0285-7 · Cited by 111
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Fazal, R., Boeynaems, S., Swijsen, A., De Decker, M., Fumagalli, L., Moisse, M., Vanneste, J., Guo, W., Boon, R., Vercruysse, T., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2020106177 · Cited by 108
Natural Products as a Potential Modulator of Microglial Polarization in Neurodegenerative Diseases
Jin, X., Liu, M.-Y., Zhang, D.-F., Zhong, X., Du, K., Qian, P., Gao, H., & Wei, M.-J. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104253 · Cited by 109
Suárez‐Calvet, M., Capell, A., Araque Caballero, M. Á., Morenas‐Rodríguez, E., Fellerer, K., Franzmeier, N., Kleinberger, G., Eren, E., Deming, Y., Piccio, L., et al. (2018) · EMBO Molecular Medicine · doi:10.15252/emmm.201809712 · Cited by 109
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Pickford, F., Marcus, J., Camargo, L. M., Xiao, Q., Graham, D., Mo, J.-R., Burkhardt, M., Kulkarni, V., Crispino, J., Hering, H., et al. (2011) · The American Journal of Pathology · doi:10.1016/j.ajpath.2010.11.002 · Cited by 107
Crippa, V., D’Agostino, V. G., Cristofani, R., Rusmini, P., Cicardi, M. E., Messi, E., Loffredo, R., Pancher, M., Piccolella, M., Galbiati, M., et al. (2016) · Scientific Reports · doi:10.1038/srep22827 · Cited by 101
Svahn, A. J., Don, E. K., Badrock, A. P., Cole, N. J., Graeber, M. B., Yerbury, J. J., Chung, R., & Morsch, M. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1875-2 · Cited by 87
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Grossman, M., Elman, L., McCluskey, L., McMillan, C. T., Boller, A., Powers, J., Rascovsky, K., Hu, W., Shaw, L., Irwin, D. J., et al. (2014) · JAMA Neurology · doi:10.1001/jamaneurol.2013.6064 · Cited by 94
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Gomez-Deza, J., Lee, Y.-B., Troakes, C., Nolan, M., Al-Sarraj, S., Gallo, J.-M., & Shaw, C. E. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0218-y · Cited by 93
Garcia Morato, J., Hans, F., von Zweydorf, F., Feederle, R., Elsässer, S. J., Skodras, A. A., Gloeckner, C. J., Buratti, E., Neumann, M., & Kahle, P. J. (2022) · Nature Communications · doi:10.1038/s41467-022-28822-7 · Cited by 94
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Moisse, K., Mepham, J., Volkening, K., Welch, I., Hill, T., & Strong, M. J. (2009) · Brain Research · doi:10.1016/j.brainres.2009.07.023 · Cited by 93
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Shimonaka, S., Nonaka, T., Suzuki, G., Hisanaga, S.-I., & Hasegawa, M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.713552 · Cited by 93
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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