Patient-derived frontotemporal lobar degeneration brain extracts induce formation and spreading of TDP-43 pathology in vivo
Open accessAbstract
Abstract The stereotypical distribution of TAR DNA-binding 43 protein (TDP-43) aggregates in frontotemporal lobar degeneration (FTLD-TDP) suggests that pathological TDP-43 spreads throughout the brain via cell-to-cell transmission and correlates with disease progression, but no in vivo experimental data support this hypothesis. We first develop a doxycycline-inducible cell line expressing GFP-tagged cytoplasmic TDP-43 protein (iGFP-NLSm) as a cell-based system to screen and identify seeding activity of human brain-derived pathological TDP-43 isolated from sporadic FTLD-TDP and familial cases with Granulin (FTLD-TDP-GRN) or C9orf72 repeat expansion mutations (FTLD-TDP-C9+). We demonstrate that intracerebral injections of biologically active pathogenic FTLD-TDP seeds into transgenic mice expressing cytoplasmic human TDP-43 (lines CamKIIa-hTDP-43 NLSm , rNLS8, and CamKIIa-208) and non-transgenic mice led to the induction of de-novo TDP-43 pathology. Moreover, TDP-43 pathology progressively spreads throughout the brain in a time-dependent manner via the neuroanatomic connectome. Our study suggests that the progression of FTLD-TDP reflects the templated cell-to-cell transneuronal spread of pathological TDP-43.
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
Cites
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?
Accumulation of pathological protein is detected in some pyramidal neurons in cortical regions contralateral to the site of injection.
“The accumulation of pathological protein is detected in some pyramidal neurons in cortical regions that are contralateral to the site of injection.”
From The Role of Retrotransposons and Endogenous Retroviruses in Age-Dependent Neurodegenerative Disorders (2024) · cites this paper as Porta et al. 2018
The Results section, “FTLD-TDP brain extracts seed cytoplasmic TDP-43 in vivo” (page unavailable), reports pTDP-43 inclusions in scattered cortical neurons contralateral to the injection site. It identifies pyramidal neurons with aggregates in hippocampal CA1, but does not identify the affected contralateral cortical neurons as pyramidal. (LLM, conf=0.86)
Experimental — accuracy not yet measuredNeuron-to-neuron transfer of pathological TDP-43 has been observed in vivo in response to injection of aggregated human TDP-43 into the cortex of mice that express pan-neuronal human TDP-43 that is already mislocalized to the cytoplasm.
“Neuron-to-neuron transfer has also been observed in vivo in response to injection of aggregated human TDP-43 into the cortex of mice that express pan-neuronal human TDP-43 that is already mislocalized to the cytoplasm (Porta et al. 2018).”
From The Role of Retrotransposons and Endogenous Retroviruses in Age-Dependent Neurodegenerative Disorders (2024) · cites this paper as Porta et al. 2018
The Results section ('FTLD-TDP brain extracts seed cytoplasmic TDP-43 in vivo'; page not provided) reports that patient-derived extracts containing pathological TDP-43 were injected into mice expressing cytoplasmic human TDP-43, with the neocortex among the injection sites. The Discussion describes the subsequent spread as consistent with transneuronal transmission, rather than direct observation of neuron-to-neuron transfer. The mice expressed the transgene in forebrain neurons, not pan-neuronally, and injections also targeted the hippocampus and thalamus. (LLM, conf=0.88)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
1 retracted
RETRACTED: The RasGAP-associated endoribonuclease G3BP assembles stress granules
Tourrière, H., Chébli, K., Zekri, L., Courselaud, B., Blanchard, J. M., Bertrand, É., & Tazi, J. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200212128 · Cited by 834 · see citing works
RetractedUbiquitinated 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 · see citing works
Self-citationA mesoscale connectome of the mouse brain
Oh, S. W., Harris, J. A., Ng, L., Winslow, B., Cain, N., Mihalas, S., Wang, Q., Lau, C., Kuan, L., Henry, A. M., et al. (2014) · Nature · doi:10.1038/nature13186 · Cited by 2,612 · see citing works
Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · Science · doi:10.1126/science.1227157 · Cited by 2,563 · see citing works
Self-citationThe three-dimensional organization of the hippocampal formation: A review of anatomical data
Amaral, D. G., & Witter, M. P. (1989) · Neuroscience · doi:10.1016/0306-4522(89)90424-7 · Cited by 2,180 · see citing works
Li, J.-Y., Englund, E., Holton, J. L., Soulet, D., Hagell, P., Lees, A. J., Lashley, T., Quinn, N. P., Rehncrona, S., Björklund, A., et al. (2008) · Nature Medicine · doi:10.1038/nm1746 · Cited by 1,845 · see citing works
Transmission and spreading of tauopathy in transgenic mouse brain
Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1901 · Cited by 1,803 · see citing works
Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils
Petkova, A. T., Leapman, R. D., Guo, Z., Yau, W.-M., Mattson, M. P., & Tycko, R. (2005) · Science · doi:10.1126/science.1105850 · Cited by 1,687 · see citing works
Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
Jucker, M., & Walker, L. C. (2013) · Nature · doi:10.1038/nature12481 · Cited by 1,663 · see citing works
Volpicelli-Daley, L. A., Luk, K. C., Patel, T. P., Tanik, S. A., Riddle, D. M., Stieber, A., Meaney, D. F., Trojanowski, J. Q., & Lee, V. M.-Y. (2011) · Neuron · doi:10.1016/j.neuron.2011.08.033 · Cited by 1,569 · see citing works
Self-citationLuk, K. C., Kehm, V. M., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M. ‐. (2012) · The Journal of Experimental Medicine · doi:10.1084/jem.20112457 · Cited by 1,087 · see citing works
Self-citationStages of pTDP‐43 pathology in amyotrophic lateral sclerosis
Brettschneider, J., Del Tredici, K., Toledo, J. B., Robinson, J. L., Irwin, D. J., Grossman, M., Suh, E., Van Deerlin, V. M., Wood, E. M., Baek, Y., et al. (2013) · Annals of Neurology · doi:10.1002/ana.23937 · Cited by 1,065 · see citing works
Self-citationA harmonized classification system for FTLD-TDP pathology
Mackenzie, I. R., Neumann, M., Baborie, A., Sampathu, D. M., du Plessis, D., Jaros, E., Perry, R. H., Trojanowski, J. Q., Mann, D. M. A., & Lee, V. M. ‐. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0845-8 · Cited by 1,013 · see citing works
Self-citationStress Granule Assembly Is Mediated by Prion-like Aggregation of TIA-1
Farny, N. G., Kedersha, N., Ayodele, M. O., Shen, L., Stoecklin, G., Dember, L. M., & Anderson, P. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-08-0715 · Cited by 1,000 · see citing works
The C9orf72 repeat expansion disrupts nucleocytoplasmic transport.
Zhang, K., Donnelly, C. J., Haeusler, A. R., Grima, J. C., Machamer, J. B., Steinwald, P., Daley, E. L., Miller, S. J., Cunningham, K. M., Vidensky, S., et al. (2015) · Nature · doi:10.1038/nature14973 · Cited by 982 · see citing works
TDP‐43 immunoreactivity in hippocampal sclerosis and Alzheimer's disease
Amador‐Ortiz, C., Lin, W., Ahmed, Z., Personett, D., Davies, P., Duara, R., Graff‐Radford, N. R., Hutton, M. L., & Dickson, D. W. (2007) · Annals of Neurology · doi:10.1002/ana.21154 · Cited by 916 · see citing works
GGGGCC repeat expansion in C9orf72 compromises nucleocytoplasmic transport
Freibaum, B. D., Lu, Y., Lopez-Gonzalez, R., Kim, N. C., Almeida, S., Lee, K.-H., Badders, N., Valentine, M., Miller, B. L., Wong, P. C., et al. (2015) · Nature · doi:10.1038/nature14974 · Cited by 841 · see citing works
ALS‐associated fused in sarcoma (FUS) mutations disrupt Transportin‐mediated nuclear import
Dormann, D., Rodde, R., Edbauer, D., Bentmann, E., Fischer, I., Hruscha, A., Than, M. E., Mackenzie, I. R. A., Capell, A., Schmid, B., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.143 · Cited by 836 · see citing works
Role of Stress Granules and RNA-Binding Proteins in Neurodegeneration: A Mini-Review
Vanderweyde, T. E., Youmans, K., Liu‐Yesucevitz, L., & Wolozin, B. L. (2013) · Gerontology · doi:10.1159/000354170 · Cited by 806 · see citing works
Spreading of pathology in neurodegenerative diseases: a focus on human studies
Brettschneider, J., Tredici, K. D., Lee, V. M.-Y., & Trojanowski, J. Q. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3887 · Cited by 790 · see citing works
Self-citationPhosphorylated TDP‐43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
Hasegawa, M., Arai, T., Nonaka, T., Kametani, F., Yoshida, M., Hashizume, Y., Beach, T. G., Buratti, E., Baralle, F., Morita, M., et al. (2008) · Annals of Neurology · doi:10.1002/ana.21425 · Cited by 777 · see citing works
Evidence for α-synuclein prions causing multiple system atrophy in humans with parkinsonism
Prusiner, S. B., Woerman, A. L., Mordes, D. A., Watts, J. C., Rampersaud, R., Berry, D. B., Patel, S. S., Oehler, A., Lowe, J. K., Kravitz, S. N., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1514475112 · Cited by 679 · see citing works
Iba, M., Guo, J. L., McBride, J. D., Zhang, B., Trojanowski, J. Q., & Lee, V. M.-Y. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.2642-12.2013 · Cited by 664 · see citing works
Self-citationWinton, M. J., Igaz, L. M., Wong, M. M., Kwong, L. K., Trojanowski, J. Q., & Lee, V. M. ‐. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800342200 · Cited by 660 · see citing works
Self-citationCell-to-cell transmission of pathogenic proteins in neurodegenerative diseases
Guo, J. L., & Lee, V. M. Y. (2014) · Nature Medicine · doi:10.1038/nm.3457 · Cited by 641 · see citing works
Self-citationLiu‐Yesucevitz, L., Bilgutay, A. N., Zhang, Y., Vanderwyde, T., Citro, A., Mehta, T., Zaarur, N., McKee, A. C., Bowser, R. P., Sherman, M. Y., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013250 · Cited by 623 · see citing works
TDP‐43 regulates its mRNA levels through a negative feedback loop
Ayala, Y. M., Conti, L. D., Avendaño-Vázquez, S. E., Dhir, A., Romano, M., D’Ambrogio, A., Tollervey, J. R., Ule, J., Baralle, M., Buratti, E., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.310 · Cited by 618 · see citing works
Jovičić, A., Mertens, J., Boeynaems, S., Bogaert, E., Chai, N., Yamada, S. B., Paul, J. W., Sun, S., Herdy, J. R., Bieri, G., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4085 · Cited by 598 · see citing works
TDP-43 pathology disrupts nuclear pore complexes and nucleocytoplasmic transport in ALS/FTD
Chou, C., Zhang, Y., Umoh, M. E., Vaughan, S. W., Lorenzini, I., Liu, F., Sayegh, M., Donlin-Asp, P., Chen, Y. H., Duong, D. M., et al. (2018) · Nature Neuroscience · doi:10.1038/s41593-017-0047-3 · Cited by 583 · see citing works
TDP‐43 is recruited to stress granules in conditions of oxidative insult
Colombrita, C., Zennaro, E., Fallini, C., Weber, M., Sommacal, A., Buratti, E., Silani, V., & Ratti, A. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06383.x · Cited by 542 · see citing works
Prion-like Properties of Pathological TDP-43 Aggregates from Diseased Brains
Nonaka, T., Masuda‐Suzukake, M., Arai, T., Hasegawa, Y., Akatsu, H., Obi, T., Yoshida, M., Murayama, S., Mann, D. M. A., Akiyama, H., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.06.007 · Cited by 520 · see citing works
Guo, J. L., Narasimhan, S., Changolkar, L., He, Z., Stieber, A., Zhang, B., Gathagan, R. J., Iba, M., McBride, J. D., Trojanowski, J. Q., et al. (2016) · Journal of Experimental Medicine · doi:10.1084/jem.20160833 · Cited by 440 · see citing works
Self-citationDysregulation of the ALS-associated gene TDP-43 leads to neuronal death and degeneration in mice
Igaz, L. M., Kwong, L. K., Lee, E. B., Chen‐Plotkin, A. S., Swanson, E., Unger, T. L., Malunda, J. A., Xu, Y., Winton, M. J., Trojanowski, J. Q., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44867 · Cited by 434 · see citing works
Self-citationMcDonald, K. K., Aulas, A., Destroismaisons, L., Pickles, S. R., Beleac, E., Camu, W., Rouleau, G. A., & Velde, C. V. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr021 · Cited by 394 · see citing works
Staging TDP-43 pathology in Alzheimer’s disease
Josephs, K. A., Murray, M. E., Whitwell, J. L., Parisi, J. E., Petrucelli, L., Jack, C. R., Petersen, R. C., & Dickson, D. W. (2014) · Acta Neuropathologica · doi:10.1007/s00401-013-1211-9 · Cited by 366 · see citing works
Walker, A. K., Spiller, K. J., Ge, G., Zheng, A., Xu, Y., Zhou, M. S., Tripathy, K., Kwong, L. K., Trojanowski, J. Q., & Lee, V. M. ‐. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1460-x · Cited by 338 · see citing works
Self-citationTDP-43 is intercellularly transmitted across axon terminals
Feiler, M. S., Strobel, B., Freischmidt, A., Helferich, A. M., Kappel, J., Brewer, B. M., Li, D., Thal, D. R., Walther, P., Ludolph, A. C., et al. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201504057 · Cited by 329 · see citing works
Igaz, L. M., Kwong, L. K., Xu, Y., Truax, A. C., Uryu, K., Neumann, M., Clark, C. M., Elman, L. B., Miller, B. L., Grossman, M., et al. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.080003 · Cited by 328 · see citing works
Self-citationSequential distribution of pTDP-43 pathology in behavioral variant frontotemporal dementia (bvFTD)
Brettschneider, J., Tredici, K. D., Irwin, D. J., Grossman, M., Robinson, J. L., Toledo, J. B., Fang, L., Deerlin, V. M. V., Ludolph, A. C., Lee, V. M. ‐., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-013-1238-y · Cited by 314 · see citing works
Self-citationALS Genes in the Genomic Era and their Implications for FTD
Nguyen, H. P., Broeckhoven, C. V., & van der Zee, J. (2018) · Trends in Genetics · doi:10.1016/j.tig.2018.03.001 · Cited by 308 · see citing works
TDP-43 pathology and neuronal loss in amyotrophic lateral sclerosis spinal cord
Brettschneider, J., Arai, K., Tredici, K. D., Toledo, J. B., Robinson, J. L., Lee, E. B., Kuwabara, S., Shibuya, K., Irwin, D. J., Fang, L., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1299-6 · Cited by 271 · see citing works
Self-citationClinical and Pathological Continuum of Multisystem TDP-43 Proteinopathies
Geser, F., Martinez-Lage, M., Robinson, J., Uryu, K., Neumann, M., Brandmeir, N. J., Xie, S. X., Kwong, L. K., Elman, L., McCluskey, L., et al. (2009) · Archives of Neurology · doi:10.1001/archneurol.2008.558 · Cited by 267 · see citing works
Self-citationFrontotemporal lobar degeneration: defining phenotypic diversity through personalized medicine
Irwin, D. J., Cairns, N. J., Grossman, M., McMillan, C. T., Lee, E. B., Deerlin, V. M. V., Lee, V. M. ‐., & Trojanowski, J. Q. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1380-1 · Cited by 262 · see citing works
Self-citationLee, E. B., Porta, S., Baer, G. M., Xu, Y., Suh, E. R., Kwong, L. K., Elman, L. B., Grossman, M., Lee, V. M. ‐., Irwin, D. J., et al. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1679-9 · Cited by 257 · see citing works
Self-citationPropagation of prions causing synucleinopathies in cultured cells
Woerman, A. L., Stöhr, J., Aoyagi, A., Rampersaud, R., Krejciova, Z., Watts, J. C., Ohyama, T., Patel, S. S., Widjaja, K., Oehler, A., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1513426112 · Cited by 241 · see citing works
Neumann, M., Kwong, L. K., Truax, A. C., Vanmassenhove, B., Kretzschmar, H. A., Deerlin, V. M. V., Clark, C. M., Grossman, M., Miller, B. L., Trojanowski, J. Q., et al. (2007) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000248554.45456.58 · Cited by 238 · see citing works
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 · see citing works
Self-citationContinuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes
Legname, G., Nguyen, H.-O. B., Peretz, D., Cohen, F. E., DeArmond, S. J., & Prusiner, S. B. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608970103 · Cited by 219 · see citing works
Moisse, 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 · see citing works
Zhang, Y., Caulfield, T. R., Xu, Y., Gendron, T. F., Hubbard, J., Stetler, C. T., Sasaguri, H., Whitelaw, E. C., Cai, S., Lee, C. W., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt166 · Cited by 185 · see citing works
Self-citationBrettschneider, J., Deerlin, V. M. V., Robinson, J. L., Kwong, L. K., Lee, E. B., Ali, Y., Safren, N., Monteiro, M. J., Toledo, J. B., Elman, L. B., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0970-z · Cited by 183 · see citing works
Self-citationThe N-terminus of TDP-43 promotes its oligomerization and enhances DNA binding affinity
Chang, C., Wu, T.-H., Wu, C.-Y., Chiang, M.-H., Toh, E. K.-W., Hsu, Y.-C., Lin, K.-F., Liao, Y.-H., Huang, T.-H., & Huang, J. J. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.07.071 · Cited by 142 · see citing works
Seeded strain‐like transmission of β‐amyloid morphotypes in APP transgenic mice
Heilbronner, G., Eisele, Y. S., Langer, F., Kaeser, S. A., Novotny, R., Nagarathinam, A., Åslund, A., Hammarström, P., Nilsson, K. P. R., & Jucker, M. (2013) · EMBO Reports · doi:10.1038/embor.2013.137 · Cited by 139 · see citing works
In vitro prion-like behaviour of TDP-43 in ALS
Smethurst, P., Newcombe, J., Troakes, C., Simone, R., Chen, Y., Patani, R., & Sidle, K. C. L. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.08.007 · Cited by 139 · see citing works
Reappraisal of TDP-43 pathology in FTLD-U subtypes
Mackenzie, I. R., & Neumann, M. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1716-8 · Cited by 116 · see citing works
Wang, Y.-T., Kuo, P. H., Chiang, C.-H., Liang, J.-R., Chen, Y., Wang, S., Shen, J., & Yuan, H. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.438564 · Cited by 116 · see citing works
Cytoplasmic poly-GA aggregates impair nuclear import of TDP-43 in C9orf72 ALS/FTLD
Khosravi, B., Hartmann, H., May, S., Möhl, C., Ederle, H., Michaelsen, M., Schludi, M. H., Dormann, D., & Edbauer, D. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw432 · Cited by 113 · see citing works
Molecular analysis and biochemical classification of TDP-43 proteinopathy
Tsuji, H., Arai, T., Kametani, F., Nonaka, T., Yamashita, M., Masuda‐Suzukake, M., Hosokawa, M., Yoshida, M., Hatsuta, H., Takao, M., et al. (2012) · Brain · doi:10.1093/brain/aws230 · Cited by 107 · see citing works
Stress granules at the intersection of autophagy and ALS
Monahan, Z. T., Shewmaker, F. P., & Pandey, U. B. (2016) · Brain Research · doi:10.1016/j.brainres.2016.05.022 · Cited by 105 · see citing works
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 · see citing works
Clinicopathological Staging of Frontotemporal Dementia Severity: Correlation with Regional Atrophy
Kril, J. J., & Halliday, G. M. (2004) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000077161 · Cited by 84 · see citing works
Astrocytic TDP-43 Pathology in Alexander Disease
Walker, A. K., Daniels, C. M. L., Goldman, J. E., Trojanowski, J. Q., Lee, V. M. ‐., & Messing, A. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.0248-14.2014 · Cited by 80 · see citing works
Self-citationConjoint pathologic cascades mediated by ALS/FTLD-U linked RNA-binding proteins TDP-43 and FUS
Ito, D., & Suzuki, N. (2011) · Neurology · doi:10.1212/wnl.0b013e3182343365 · Cited by 76 · see citing works
Semi-Automated Digital Image Analysis of Pick’s Disease and TDP-43 Proteinopathy
Irwin, D. J., Byrne, M. D., McMillan, C. T., Cooper, F. I., Arnold, S. E., Lee, E. B., Deerlin, V. M. V., Xie, S. X., Lee, V. M. ‐., Grossman, M., et al. (2015) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155415614303 · Cited by 64 · see citing works
Self-citationReversible Behavioral Phenotypes in a Conditional Mouse Model of TDP-43 Proteinopathies
Alfieri, J. A., Pino, N. S., & Igaz, L. M. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1918-14.2014 · Cited by 60 · see citing works
Jovičić, A., Paul, J. W., & Gitler, A. D. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13642 · Cited by 53 · see citing works
RNA Granules and Diseases: A Case Study of Stress Granules in ALS and FTLD
Fan, A. C., & Leung, A. K. L. (2016) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-29073-7_11 · Cited by 52 · see citing works
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 48 · see citing works
Self-citationMougenot, A.-L. J., Bencsik, A. A., Nicot, S., Vulin, J., Morignat, E., Verchère, J., Bétemps, D., Lakhdar, L., Legastelois, S., & Baron, T. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318217d95f · Cited by 34 · see citing works
Tsuji, H., Nonaka, T., Yamashita, M., Masuda‐Suzukake, M., Kametani, F., Akiyama, H., Mann, D. M. A., Tamaoka, A., & Hasegawa, M. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.11.066 · Cited by 34 · see citing works
Porta, S., Kwong, L. K., Trojanowski, J. Q., & Lee, V. M. ‐. (2015) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000182 · Cited by 32 · see citing works
Self-citationFamilial Frontotemporal Dementia: From Gene Discovery to Clinical Molecular Diagnostics
Deerlin, V. M. V., Gill, L. H., Farmer, J. M., Trojanowski, J. Q., & Lee, V. M. ‐. (2003) · Clinical Chemistry · doi:10.1373/49.10.1717 · Cited by 21 · see citing works
Self-citation
Flagged first, then by citations
Research works printed but not linked: 1
- [69]Paxinos, G. & Franklin, K. B. J. The Mouse Brain in Stereotaxic Coordinates 2nd edn (Academic Press, San Diego, CA, 2001).
Cited by
Sorted by citations
Limbic-predominant age-related TDP-43 encephalopathy (LATE): consensus working group report
Nelson, P. T., Dickson, D. W., Trojanowski, J. Q., Jack, C. R., Boyle, P. A., Arfanakis, K., Rademakers, R., Alafuzoff, I., Attems, J., Brayne, C., et al. (2019) · Brain · doi:10.1093/brain/awz099 · Cited by 1,547 · see citing works
Self-citationProtein transmission in neurodegenerative disease
Peng, C., Trojanowski, J. Q., & Lee, V. M.-Y. (2020) · Nature Reviews Neurology · doi:10.1038/s41582-020-0333-7 · Cited by 625 · see citing works
Self-citationPhase separation and neurodegenerative diseases: a disturbance in the force
Zbinden, A., Pérez-Berlanga, M., De Rossi, P., & Polymenidou, M. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.09.014 · Cited by 500 · see citing works
The role of TDP-43 mislocalization in amyotrophic lateral sclerosis
Suk, T. R., & Rousseaux, M. W. C. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00397-1 · Cited by 456 · see citing works
Propagation and spread of pathogenic protein assemblies in neurodegenerative diseases
Jucker, M., & Walker, L. C. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0238-6 · Cited by 450 · see citing works
Jo, M., Lee, S., Jeon, Y., Kim, S., Kwon, Y., & Kim, H. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-020-00513-7 · Cited by 405 · see citing works
TDP-43 proteinopathies: a new wave of neurodegenerative diseases
de Boer, E. M. J., Orie, V. K., Williams, T. L., Baker, M. R., Oliveira, H. M. D., Polvikoski, T. M., Silsby, M., Menon, P., van den Bos, M. A. J., Halliday, G. M., et al. (2020) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2020-322983 · Cited by 373 · see citing works
FUS and TDP-43 Phases in Health and Disease
Portz, B., Lee, B. L., & Shorter, J. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.12.005 · Cited by 323 · see citing works
Structure of pathological TDP-43 filaments from ALS with FTLD
Arseni, D., Hasegawa, M., Murzin, A. G., Kametani, F., Arai, M., Yoshida, M., & Falcon, B. (2021) · Nature · doi:10.1038/s41586-021-04199-3 · Cited by 303 · see citing works
Molecular pathology of neurodegenerative diseases by cryo-EM of amyloids
Scheres, S. H. W., Falcon, B., & Goedert, M. (2023) · Nature · doi:10.1038/s41586-023-06437-2 · Cited by 293 · see citing works
Cryo-EM structures of four polymorphic TDP-43 amyloid cores
Cao, Q., Boyer, D. R., Sawaya, M. R., Ge, P., & Eisenberg, D. S. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0248-4 · Cited by 253 · see citing works
Motor Neuron Susceptibility in ALS/FTD
Ragagnin, A., Shadfar, S., Vidal, M., Jamali, M. S., & Atkin, J. D. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00532 · Cited by 216 · see citing works
The Pathobiology of TDP-43 C-Terminal Fragments in ALS and FTLD
Berning, B. A., & Walker, A. K. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00335 · Cited by 183 · see citing works
Frontotemporal lobar degeneration
Grossman, M., Seeley, W. W., Boxer, A. L., Hillis, A. E., Knopman, D. S., Ljubenov, P. A., Miller, B., Piguet, O., Rademakers, R., Whitwell, J. L., et al. (2023) · Nature Reviews Disease Primers · doi:10.1038/s41572-023-00447-0 · Cited by 178 · see citing works
Lu, S., Hu, J., Arogundade, O. A., Goginashvili, A., Vazquez‐Sanchez, S., Diedrich, J. K., Gu, J., Blum, J. A., Oung, S., Ye, Q., et al. (2022) · Nature Cell Biology · doi:10.1038/s41556-022-00988-8 · Cited by 163 · see citing works
TDP-43 forms amyloid filaments with a distinct fold in type A FTLD-TDP
Arseni, D., Chen, R., Murzin, A. G., Peak‐Chew, S., Garringer, H. J., Newell, K. L., Kametani, F., Robinson, A., Vidal, R., Ghetti, B. F., et al. (2023) · Nature · doi:10.1038/s41586-023-06405-w · Cited by 159 · see citing works
Carey, J. L., & Guo, L. E. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.826719 · Cited by 157 · see citing works
Prion-Like Propagation of Protein Misfolding and Aggregation in Amyotrophic Lateral Sclerosis
McAlary, L., Plotkin, S. S., Yerbury, J. J., & Cashman, N. R. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00262 · Cited by 149 · see citing works
Invited Review: The role of prion‐like mechanisms in neurodegenerative diseases
Jaunmuktane, Z., & Brandner, S. (2019) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12592 · Cited by 147 · see citing works
Nanozyme scavenging ROS for prevention of pathologic α-synuclein transmission in Parkinson’s disease
Liu, Y., Mao, Y., Xu, E., Jia, H., Zhang, S., Dawson, V. L., Dawson, T. M., Li, Y., Zheng, Z. G., He, W., et al. (2020) · Nano Today · doi:10.1016/j.nantod.2020.101027 · Cited by 137 · see citing works
Genetics of amyotrophic lateral sclerosis: seeking therapeutic targets in the era of gene therapy
Suzuki, N., Nishiyama, A., Warita, H., & Aoki, M. (2022) · Journal of Human Genetics · doi:10.1038/s10038-022-01055-8 · Cited by 136 · see citing works
The basis of clinicopathological heterogeneity in TDP-43 proteinopathy
Kawakami, I., Arai, T., & Hasegawa, M. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02077-x · Cited by 128 · see citing works
French, R. L., Grese, Z. R., Aligireddy, H., Dhavale, D. D., Reeb, A. N., Kedia, N., Kotzbauer, P. T., Bieschke, J., & Ayala, Y. M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005889 · Cited by 125 · see citing works
Genetic Convergence Brings Clarity to the Enigmatic Red Line in ALS
Cook, C. N., & Petrucelli, L. (2019) · Neuron · doi:10.1016/j.neuron.2019.02.032 · Cited by 124 · see citing works
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 · see citing works
Patient-Tailored, Connectivity-Based Forecasts of Spreading Brain Atrophy
Brown, J. A., Deng, J., Neuhaus, J. M., Sible, I. J., Sias, A. C., Lee, S. E., Kornak, J., Marx, G. A., Karydas, A. M., Spina, S., et al. (2019) · Neuron · doi:10.1016/j.neuron.2019.08.037 · Cited by 112 · see citing works
Molecular Chaperones: A Double-Edged Sword in Neurodegenerative Diseases
Tittelmeier, J., Nachman, E., & Nussbaum-Krammer, C. I. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.581374 · Cited by 107 · see citing works
Neumann, M., Lee, E. B., & Mackenzie, I. R. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-51140-1_13 · Cited by 104 · see citing works
Self-citationMolecular Mechanisms Underlying TDP-43 Pathology in Cellular and Animal Models of ALS and FTLD
Wood, A., Gurfinkel, Y., Polain, N., Lamont, W. G., & Rea, S. L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094705 · Cited by 101 · see citing works
Hierarchical chemical determination of amyloid polymorphs in neurodegenerative disease
Li, D., & Liu, C. (2021) · Nature Chemical Biology · doi:10.1038/s41589-020-00708-z · Cited by 95 · see citing works
Tau and TDP-43 proteinopathies: kindred pathologic cascades and genetic pleiotropy
Chornenkyy, Y., Fardo, D. W., & Nelson, P. T. (2019) · Laboratory Investigation · doi:10.1038/s41374-019-0196-y · Cited by 93 · see citing works
Seeding the aggregation of TDP-43 requires post-fibrillization proteolytic cleavage
Kumar, S. T., Nazarov, S., Porta, S., Maharjan, N., Cendrowska, U., Kabani, M., Finamore, F., Xu, Y., Lee, V. M. ‐., & Lashuel, H. A. (2023) · Nature Neuroscience · doi:10.1038/s41593-023-01341-4 · Cited by 88 · see citing works
Self-citationDhakal, S., Wyant, C. E., George, H. E., Morgan, S. E., & Rangachari, V. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166953 · Cited by 87 · see citing works
Thal, D. R., & Tomé, S. O. (2022) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2022.10.006 · Cited by 85 · see citing works
The PERK-Dependent Molecular Mechanisms as a Novel Therapeutic Target for Neurodegenerative Diseases
Rozpędek-Kamińska, W., Siwecka, N., Wawrzynkiewicz, A., Wojtczak, R., Pytel, D., Diehl, J. A., & Majsterek, I. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21062108 · Cited by 84 · see citing works
Protein S-nitrosylation and oxidation contribute to protein misfolding in neurodegeneration
Nakamura, T., Oh, C.-K., Zhang, X., & Lipton, S. A. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.07.002 · Cited by 82 · see citing works
Emerging Therapies and Novel Targets for TDP-43 Proteinopathy in ALS/FTD
Hayes, L. R., & Kaláb, P. (2022) · Neurotherapeutics · doi:10.1007/s13311-022-01260-5 · Cited by 81 · see citing works
Sternburg, E. L., da Silva, L. A. G., & Dormann, D. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2021.07.004 · Cited by 72 · see citing works
TDP-43 pathology: From noxious assembly to therapeutic removal
Keating, S. S., Gil, R. S., Swanson, M. E. V., Scotter, E. L., & Walker, A. K. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2022.102229 · Cited by 74 · see citing works
Oiwa, K., Watanabe, S., Onodera, K., Iguchi, Y., Kinoshita, Y., Komine, O., Sobue, A., Okada, Y., Katsuno, M., & Yamanaka, K. (2023) · Science Advances · doi:10.1126/sciadv.adf6895 · Cited by 73 · see citing works
Proteostatic imbalance and protein spreading in amyotrophic lateral sclerosis
Cicardi, M. E., Marrone, L., Azzouz, M., & Trotti, D. (2021) · The EMBO Journal · doi:10.15252/embj.2020106389 · Cited by 73 · see citing works
α-synuclein strains that cause distinct pathologies differentially inhibit proteasome
Suzuki, G., Imura, S., Hosokawa, M., Katsumata, R., Nonaka, T., Hisanaga, S., Saeki, Y., & Hasegawa, M. (2020) · eLife · doi:10.7554/elife.56825 · Cited by 72 · see citing works
Ultrastructural and biochemical classification of pathogenic tau, α-synuclein and TDP-43
Tarutani, A., Adachi, T., Akatsu, H., Hashizume, Y., Hasegawa, K., Saito, Y., Robinson, A., Mann, D. M. A., Yoshida, M., Murayama, S., et al. (2022) · Acta Neuropathologica · doi:10.1007/s00401-022-02426-3 · Cited by 74 · see citing works
Li, Y., Liu, Y., Yu, X., Xu, Y., Pan, X., Sun, Y. E., Wang, Y., Song, Y.-H., & Shen, Z. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02013-w · Cited by 70 · see citing works
Self-citationScialò, C., Cecco, E. D., Manganotti, P., & Legname, G. (2019) · Viruses · doi:10.3390/v11030261 · Cited by 67 · see citing works
Chang, Y.-H., & Dubnau, J. (2019) · Current Biology · doi:10.1016/j.cub.2019.07.071 · Cited by 68 · see citing works
Zhuo, X.-F., Wang, J., Zhang, J., Jiang, L., Hu, H., & Lu, J. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.9b10736 · Cited by 66 · see citing works
Spinal cord extracts of amyotrophic lateral sclerosis spread TDP-43 pathology in cerebral organoids
Tamaki, Y., Ross, J. P., Alipour, P., Castonguay, C.-E., Li, B., Catoire, H., Rochefort, D. L., Urushitani, M., Takahashi, R., Sonnen, J. A., et al. (2023) · PLoS Genetics · doi:10.1371/journal.pgen.1010606 · Cited by 65 · see citing works
TDP-43 pathology is associated with increased tau burdens and seeding
Tomé, S. O., Tsaka, G., Ronisz, A., Ospitalieri, S., Gawor, K., Gomes, L. A., Otto, M., Arnim, C. A. F. V., Damme, P. V., Bosch, L. V. D., et al. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00653-0 · Cited by 67 · see citing works
Proteome Homeostasis Dysfunction: A Unifying Principle in ALS Pathogenesis
Yerbury, J. J., Farrawell, N. E., & McAlary, L. (2020) · Trends in Neurosciences · doi:10.1016/j.tins.2020.03.002 · Cited by 63 · see citing works
Research progress on the role of extracellular vesicles in neurodegenerative diseases
Li, Z., Wang, X., Wang, X., Yi, X., Wong, Y. K., Wu, J., Xie, F., Hu, D., Wang, Q., Wang, J., et al. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00375-9 · Cited by 65 · see citing works
Porta, S., Xu, Y., Lehr, T., Zhang, B., Meymand, E. S., Olufemi, M. F., Stieber, A., Lee, E. B., Trojanowski, J. Q., & Lee, V. M. ‐. (2021) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12732 · Cited by 62 · see citing works
Self-citationZamani, A., Walker, A., Rollo, B., Ayers, K., Farah, R., O'Brien, T., & Wright, D. K. (2022) · Translational Neurodegeneration · doi:10.1186/s40035-022-00291-4 · Cited by 54 · see citing works
Prion-Like Proteins in Phase Separation and Their Link to Disease
Sprunger, M. L., & Jackrel, M. E. (2021) · Biomolecules · doi:10.3390/biom11071014 · Cited by 57 · see citing works
Aggregation-prone TDP-43 sequesters and drives pathological transitions of free nuclear TDP-43
Keating, S. S., Bademosi, A. T., Gil, R. S., & Walker, A. K. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04739-2 · Cited by 56 · see citing works
Limone, F., Mordes, D. A., Couto, A., Joseph, B. J., Mitchell, J. M., Therrien, M., Ghosh, S. D., Meyer, D., Zhang, Y., Goldman, M., et al. (2024) · Nature Aging · doi:10.1038/s43587-024-00640-0 · Cited by 54 · see citing works
Quantitative patterns of motor cortex proteinopathy across ALS genotypes
Nolan, M., Scott, C., Pallebage‐Gamarallage, M. M., Lunn, D., Carpenter, K., McDonough, E., Meyer, D. E., Kaanumalle, S., Santamaría-Pang, A., Turner, M. R., et al. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-00961-2 · Cited by 51 · see citing works
Molecular Dissection of TDP-43 as a Leading Cause of ALS/FTLD
Tamaki, Y., & Urushitani, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012508 · Cited by 52 · see citing works
Spiller, K. J., Khan, T., Dominique, M. A., Restrepo, C. R., Cotton‐Samuel, D., Levitan, M., Jafar‐Nejad, P., Zhang, B., Soriano, A., Rigo, F., et al. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.11.013 · Cited by 52 · see citing works
Self-citationLiquid–Liquid Phase Separation Enhances TDP-43 LCD Aggregation but Delays Seeded Aggregation
Pakravan, D., Michiels, E., Bratek‐Skicki, A., Decker, M. D., Lindt, J. V., Alsteens, D., Derclaye, S., Damme, P. V., Schymkowitz, J. W. H., Rousseau, F., et al. (2021) · Biomolecules · doi:10.3390/biom11040548 · Cited by 51 · see citing works
RNA-binding proteins in ALS and FTD: from pathogenic mechanisms to therapeutic insights
Rummens, J., & Cruz, S. D. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00851-y · Cited by 52 · see citing works
Chang, Y.-H., & Dubnau, J. (2023) · Nature Communications · doi:10.1038/s41467-023-36649-z · Cited by 49 · see citing works
Frost, B., & Dubnau, J. (2024) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-082823-020615 · Cited by 45 · see citing works
Dhakal, S., Mondal, M., Mirzazadeh, A., Banerjee, S., Ghosh, A., & Rangachari, V. (2023) · Communications Biology · doi:10.1038/s42003-023-05608-1 · Cited by 45 · see citing works
TDP-43: A Key Therapeutic Target beyond Amyotrophic Lateral Sclerosis
Palomo, V., Tosat‐Bitrián, C., Nozal, V., Nagaraj, S., Martín‐Requero, Á., & Martı́nez, A. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00026 · Cited by 45 · see citing works
Katsinelos, T., Tuck, B. J., Mukadam, A. S., & McEwan, W. A. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01139 · Cited by 44 · see citing works
Amyotrophic Lateral Sclerosis: Proteins, Proteostasis, Prions, and Promises
McAlary, L., Chew, Y. L., Lum, J. S., Geraghty, N. J., Yerbury, J. J., & Cashman, N. R. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.581907 · Cited by 45 · see citing works
Opinion: more mouse models and more translation needed for ALS
Fisher, E., Greensmith, L., Malaspina, A., Fratta, P., Hanna, M. G., Schiavo, G., Isaacs, A. M., Orrell, R. W., Cunningham, T. J., & Acevedo‐Arozena, A. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00619-2 · Cited by 42 · see citing works
Annexin A11 aggregation in FTLD–TDP type C and related neurodegenerative disease proteinopathies
Robinson, J. L., Suh, E. R., Xu, Y., Hurtig, H. I., Elman, L. B., McMillan, C. T., Irwin, D. J., Porta, S., Deerlin, V. M. V., & Lee, E. B. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02753-7 · Cited by 44 · see citing works
Self-citationDing, X., Xiang, Z., Qin, C., Chen, Y., Tian, H., Lin, M., Xia, D., Liu, H., Song, J. T., Fu, J., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01112-3 · Cited by 42 · see citing works
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 44 · see citing works
TDP-43 Proteinopathy Specific Biomarker Development
Cordts, I., Wachinger, A., Scialò, C., Lingor, P., Polymenidou, M., Buratti, E., & Feneberg, E. (2023) · Cells · doi:10.3390/cells12040597 · Cited by 45 · see citing works
Omics Approach to Axonal Dysfunction of Motor Neurons in Amyotrophic Lateral Sclerosis (ALS)
Suzuki, N., Akiyama, T., Warita, H., & Aoki, M. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00194 · Cited by 42 · see citing works
PIRIE, E. C., Oh, C.-K., Zhang, X., Han, X., Cieplak, P., Scott, H. R., Deal, A. K., Ghatak, S., Martinez, F. J., Yeo, G. W.-M., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2021368118 · Cited by 41 · see citing works
VCP suppresses proteopathic seeding in neurons
Zhu, J., Pittman, S. K., Dhavale, D. D., French, R. L., Patterson, J. N., Kaleelurrrahuman, M. S., Sun, Y., Vaquer‐Alicea, J., Maggiore, G., Clemen, C. S., et al. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00532-0 · Cited by 41 · see citing works
Disrupting pathologic phase transitions in neurodegeneration
Hurtle, B. T., Xie, L., & Donnelly, C. J. (2023) · Journal of Clinical Investigation · doi:10.1172/jci168549 · Cited by 39 · see citing works
Neumann, M., Frick, P., Paron, F., Kosten, J., Buratti, E., & Mackenzie, I. R. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02207-w · Cited by 38 · see citing works
Giannini, L., Peterson, C. S., Ohm, D. T., Xie, S. X., McMillan, C. T., Raskovsky, K., Massimo, L. M., Suh, E. R., Deerlin, V. M. V., Wolk, D. A., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01129-2 · Cited by 36 · see citing works
Self-citationTDP-43 seeding induces cytoplasmic aggregation heterogeneity and nuclear loss of function of TDP-43
Rummens, J., Khalil, B., Yıldırım, G., Silva, P., Zorzini, V., Peredo, N., Wojno, M., Ramakers, M., Bosch, L. V. D., Damme, P. V., et al. (2025) · Neuron · doi:10.1016/j.neuron.2025.03.004 · Cited by 38 · see citing works
Evidence of corticofugal tau spreading in patients with frontotemporal dementia
Kim, E., Hwang, J., Gaus, S. E., Nana, A. L., Deng, J., Brown, J. A., Spina, S., Lee, M. J., Ramos, E. M., Grinberg, L. T., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02075-z · Cited by 32 · see citing works
Poly(ADP-Ribosylation) in Age-Related Neurological Disease
McGurk, L., Rifai, O. M., & Bonini, N. M. (2019) · Trends in Genetics · doi:10.1016/j.tig.2019.05.004 · Cited by 36 · see citing works
Jacquet, A. D. R., Denis, H. L., Cicchetti, F., & Alpaugh, M. (2021) · Molecular Psychiatry · doi:10.1038/s41380-020-00999-7 · Cited by 35 · see citing works
TDP-43 Proteinopathy and Tauopathy: Do They Have Pathomechanistic Links?
Riku, Y., Yoshida, M., Iwasaki, Y., Sobue, G., Katsuno, M., & Ishigaki, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232415755 · Cited by 35 · see citing works
Perturbations in Traffic: Aberrant Nucleocytoplasmic Transport at the Heart of Neurodegeneration
Fahrenkrog, B., & Harel, A. (2018) · Cells · doi:10.3390/cells7120232 · Cited by 35 · see citing works
Kinetics of α-synuclein prions preceding neuropathological inclusions in multiple system atrophy
Woerman, A. L., Patel, S. S., Kazmi, S. A., Oehler, A., Lee, J., Mordes, D. A., Olson, S. H., & Prusiner, S. B. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008222 · Cited by 35 · see citing works
The Role of Extracellular Matrix Components in the Spreading of Pathological Protein Aggregates
Moretto, E., Stuart, S., Surana, S., Vargas, J. N. S., & Schiavo, G. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.844211 · Cited by 32 · see citing works
Seeded aggregation of TDP-43 induces its loss of function and reveals early pathological signatures
Scialò, C., Zhong, W., Jagannath, S., Wilkins, O. G., Caredio, D., Hruška-Plocháň, M., Lurati, F., Peter, M., Cecco, E. D., Celauro, L., et al. (2025) · Neuron · doi:10.1016/j.neuron.2025.03.008 · Cited by 34 · see citing works
FTLD-TDP assemblies seed neoaggregates with subtype-specific features via a prion-like cascade
Rossi, P. D., Lewis, A. J., Furrer, J., Vos, L. D., Demeter, T., Zbinden, A., Zhong, W., Wiersma, V. I., Scialò, C., Weber, J., et al. (2021) · EMBO Reports · doi:10.15252/embr.202153877 · Cited by 33 · see citing works
The Cellular Prion Protein Increases the Uptake and Toxicity of TDP-43 Fibrils
Scialò, C., Celauro, L., Zattoni, M., Tran, T. H., Bistaffa, E., Moda, F., Kammerer, R., Buratti, E., & Legname, G. (2021) · Viruses · doi:10.3390/v13081625 · Cited by 32 · see citing works
Afroz, T., Chevalier, E., Audrain, M., Dumayne, C., Ziehm, T., Moser, R., Egesipe, A.-L., Mottier, L., Ratnam, M., Neumann, M., et al. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106050 · Cited by 33 · see citing works
Self-citationMolecular 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 33 · see citing works
Coudert, L., Nonaka, T., Bernard, E., Hasegawa, M., Schaeffer, L., & Leblanc, P. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03059-8 · Cited by 32 · see citing works
Riemenschneider, H., Simonetti, F., Sheth, U., Katona, E., Roth, S., Hutten, S., Farny, D., Michaelsen, M., Nuscher, B., Schmidt, M. K., et al. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01592-z · Cited by 29 · see citing works
TMEM106B modifies TDP-43 pathology in human ALS brain and cell-based models of TDP-43 proteinopathy
Mao, F., Robinson, J. L., Unger, T. L., Posavi, M., Amado, D. A., Elman, L. B., Grossman, M., Wolk, D. A., Lee, E. B., Deerlin, V. M. V., et al. (2021) · Acta Neuropathologica · doi:10.1007/s00401-021-02330-2 · Cited by 28 · see citing works
Self-citationReviewing the Potential Links between Viral Infections and TDP-43 Proteinopathies
Rahic, Z., Buratti, E., & Cappelli, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021581 · Cited by 28 · see citing works
Prionoids in amyotrophic lateral sclerosis
Gosset, P., Camu, W., Raoul, C., & Mezghrani, A. (2022) · Brain Communications · doi:10.1093/braincomms/fcac145 · Cited by 28 · see citing works
Intercellular transmission of pathogenic proteins in ALS: Exploring the pathogenic wave
Arnold, F. J., Nguyen, A., Bedlack, R., Bennett, C. L., & Spada, A. R. L. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106218 · Cited by 26 · see citing works
Prion-like properties of assembled TDP-43
Nonaka, T., & Hasegawa, M. (2019) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2019.11.018 · Cited by 26 · see citing works
The Cryo-EM Effect: Structural Biology of Neurodegenerative Disease Aggregates
Creekmore, B. C., Chang, Y., & Lee, E. B. (2021) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlab039 · Cited by 26 · see citing works
Self-citationSignature laminar distributions of pathology in frontotemporal lobar degeneration
Ohm, D. T., Cousins, K. A. Q., Xie, S. X., Peterson, C. S., McMillan, C. T., Massimo, L. M., Raskovsky, K., Wolk, D. A., Deerlin, V. M. V., Elman, L. B., et al. (2022) · Acta Neuropathologica · doi:10.1007/s00401-021-02402-3 · Cited by 25 · see citing works
Self-citation
- Authors
- 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.
- Affiliations
- University of Pennsylvania (US)
- Corresponding author
- Lee, Virginia M.-Y.
- ORCID
- Venue
- Nature Communications
- Published
- 2018-10-11
- Volume
- 9
- Issue
- 1
- Pages
- 4220-4220
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC6181940
- OpenAlex
- W2894965458
- Cited by
- 248
- References
- 72
- Citations by year
- 2026: 19 · 2025: 21 · 2024: 37 · 2023: 40 · 2022: 31 · 2021: 39 · 2020: 29 · 2019: 24 · 2018: 7
- FWCI
- 16.81
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- U.S. Department of Health & Human Services | NIH | National Institute on Aging (AG10124, AG17586)
- Wyncote Foundation Biogen
- Topics
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- frontotemporal lobar degeneration, TDP-43, FTLD-TDP, cell-to-cell transmission, transneuronal spread, seeding activity, prion-like propagation, granulin, C9orf72 repeat expansion, transgenic mouse model, disease progression
- MeSH terms
- Animals, Brain, Cytoplasm, DNA-Binding Proteins, Hippocampus, Humans, Neurons, Tissue Extracts, Mice, 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
