TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
Abstract
Ubiquitin-positive tau-negative neuronal cytoplasmic inclusions and dystrophic neurites are common pathological features in frontotemporal lobar degeneration (FTLD) with or without symptoms of motor neuron disease and in amyotrophic lateral sclerosis (ALS). Using biochemical and immunohistochemical analyses, we have identified a TAR DNA-binding protein of 43 kDa (TDP-43), a nuclear factor that functions in regulating transcription and alternative splicing, as a component of these structures in FTLD. Furthermore, skein-like inclusions, neuronal intranuclear inclusions, and glial inclusions in the spinal cord of ALS patients are also positive for TDP-43. Dephosphorylation treatment of the sarkosyl insoluble fraction has shown that abnormal phosphorylation takes place in accumulated TDP-43. The common occurrence of intracellular accumulations of TDP-43 supports the hypothesis that these disorders represent a clinicopathological entity of a single disease, and suggests that they can be newly classified as a proteinopathy of TDP-43.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
Biochemical and histopathologic examination of frontotemporal cortex and spinal cord in sALS patients reveals that ubiquitin-positive inclusions contain TARDBP.
“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 [274]
Cites
Mutations 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 · see citing works
Self-citationα-Synuclein is phosphorylated in synucleinopathy lesions
Fujiwara, H., Hasegawa, M., Dohmae, N., Kawashima, A., Masliah, E., Goldberg, M., Shen, J., Takio, K., & Iwatsubo, T. (2002) · Nature Cell Biology · doi:10.1038/ncb748 · Cited by 1,906 · see citing works
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 · see citing works
Clinical and Pathological Diagnosis of Frontotemporal Dementia
McKhann, G. M. (2001) · Archives of Neurology · doi:10.1001/archneur.58.11.1803 · Cited by 1,475 · see citing works
Watts, G. D. J., Wymer, J., Kovach, M. J., Mehta, S. G., Mumm, S., Darvish, D., Pestronk, A., Whyte, M. P., & Kimonis, V. E. (2004) · Nature Genetics · doi:10.1038/ng1332 · Cited by 1,391 · see citing works
Goedert, M., Spillantini, M. G., Cairns, N. J., & Crowther, R. A. (1992) · Neuron · doi:10.1016/0896-6273(92)90117-v · Cited by 1,114 · see citing works
Ubiquitin Is a Component of Paired Helical Filaments in Alzheimer's Disease
Mori, H., Kondo, J., & Ihara, Y. (1987) · Science · doi:10.1126/science.3029875 · Cited by 843 · see citing works
Self-citationOu, 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 · see citing works
The 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 · see citing works
Mutations in progranulin are a major cause of ubiquitin-positive frontotemporal lobar degeneration
Gass, J. M., Cannon, A. D., Mackenzie, I. R., Boeve, B. F., Baker, M. C., Adamson, J. L., Crook, R., Melquist, S., Kuntz, K., Petersen, R. C., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl241 · Cited by 574 · see citing works
TDP-43 Binds Heterogeneous Nuclear Ribonucleoprotein A/B through Its C-terminal Tail
Buratti, E., Brindisi, A., Giombi, M., Tisminetzky, S. G., Ayala, Y. M., & Baralle, F. E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505557200 · Cited by 455 · see citing works
Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain
Hasegawa, M., Morishima-Kawashima, M., Takio, K., Suzuki, M., Titani, K., & Ihara, Y. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41890-x · Cited by 430 · see citing works
Self-citationVance, C. A., Al‐Chalabi, A., Ruddy, D., Smith, B. N., Hu, X., Sreedharan, J., Siddique, T., Schelhaas, H. J., Küsters, B., Troost, D., et al. (2006) · Brain · doi:10.1093/brain/awl030 · Cited by 392 · see citing works
Dementia lacking distinctive histologie features
Knopman, D. S., Mastri, A. R., Frey, W. H., Sung, J. H., & Rustan, T. D. (1990) · Neurology · doi:10.1212/wnl.40.2.251 · Cited by 377 · see citing works
Hudson, A. J. (1981) · Brain · doi:10.1093/brain/104.2.217 · Cited by 369 · see citing works
A locus on chromosome 9p confers susceptibility to ALS and frontotemporal dementia
Morita, M., Al‐Chalabi, A., Andersen, P. M., Hosler, B. A., Sapp, P. C., Englund, E. M., Mitchell, J. E., Habgood, J., de Belleroche, J., Xi, J., et al. (2006) · Neurology · doi:10.1212/01.wnl.0000200048.53766.b4 · Cited by 356 · see citing works
Kuusisto, E., Salminen, A., & Alafuzoff, I. I. (2001) · Neuroreport · doi:10.1097/00001756-200107200-00009 · Cited by 347 · see citing works
UBIQUITIN-IMMUNOREACTIVE INTRANEURONAL INCLUSIONS IN AMYOTROPHIC LATERAL SCLEROSIS
Leigh, P. N., Whitwell, H., Garofalo, O., Buller, J., Swash, M., Martin, J., Gallo, J., Weller, R. O., & Anderton, B. H. (1991) · Brain · doi:10.1093/brain/114.2.775 · Cited by 331 · see citing works
Hosler, B. A. (2000) · JAMA · doi:10.1001/jama.284.13.1664 · Cited by 314 · see citing works
Structural diversity and functional implications of the eukaryotic TDP gene family
Wang, H., Wang, I., Bose, J. K., & Shen, C. ‐. J. (2003) · Genomics · doi:10.1016/s0888-7543(03)00214-3 · Cited by 306 · see citing works
Antibodies to paired helical filaments in Alzheimer's disease do not recognize normal brain proteins
Ihara, Y., Abraham, C. R., & Selkoe, D. J. (1983) · Nature · doi:10.1038/304727a0 · Cited by 254 · see citing works
Wightman, G., Anderson, V., Martin, J., Swash, M., Anderton, B. H., Neary, D., Mann, D. M. A., Luthert, P. J., & Leigh, P. N. (1992) · Neuroscience Letters · doi:10.1016/0304-3940(92)90569-s · Cited by 233 · see citing works
Self-citationLowe, J. S., Lennox, G. G., Jefferson, D., Morrell, K., McQuire, D., Gray, T. B., Landon, M., DOHERTY, F. J., & Mayer, R. J. (1988) · Neuroscience Letters · doi:10.1016/0304-3940(88)90296-0 · Cited by 227 · see citing works
Forman, M. S., Mackenzie, I. R., Cairns, N. J., Swanson, E., Boyer, P. J., Drachman, D. A., Jhaveri, B. S., Karlawish, J. H., Pestronk, A., Smith, T. W., et al. (2006) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-200606000-00005 · Cited by 226 · see citing works
Okamoto, K., Hirai, S., Yamazaki, T., Sun, X., & Nakazato, Y. (1991) · Neuroscience Letters · doi:10.1016/0304-3940(91)90469-a · Cited by 226 · see citing works
Motor Neurone Disease-inclusion Dementia
Jackson, M., Lennox, G. G., & Lowe, J. S. (1996) · Neurodegeneration · doi:10.1006/neur.1996.0046 · Cited by 222 · see citing works
Higher order arrangement of the eukaryotic nuclear bodies
Wang, I., Reddy, N. M., & Shen, C.-K. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.212483099 · Cited by 190 · see citing works
Lipton, A. M., White, C. L., & Bigio, E. H. (2004) · Acta Neuropathologica · doi:10.1007/s00401-004-0900-9 · Cited by 188 · see citing works
Mukherjee, O., Pástor, P., Cairns, N. J., Chakraverty, S., Kauwe, J. S. K., Shears, S., Behrens, M. I., Budde, J., Hinrichs, A. L., Norton, J. B., et al. (2006) · Annals of Neurology · doi:10.1002/ana.20963 · Cited by 187 · see citing works
Cognitive function in bulbar– and spinal–onset amyotrophic lateral sclerosis
Schreiber, H., Gaigalat, T., Wiedemuth-Catrinescu, U., Graf, M., Uttner, I., Muche, R., & Ludolph, A. C. (2005) · Journal of Neurology · doi:10.1007/s00415-005-0739-6 · Cited by 172 · see citing works
Protein kinase and protein phosphatase expression in amyotrophic lateral sclerosis spinal cord
Hu, J. H., Zhang, H., Wagey, R. T. E., et al. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01670.x · Cited by 165 · see citing works
Mackenzie, I. R., & Feldman, H. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000174335.27708.0a · Cited by 162 · see citing works
Familial frontotemporal dementia with ubiquitin-positive inclusions is linked to chromosome 17q21-22
Rosso, S. M. (2001) · Brain · doi:10.1093/brain/124.10.1948 · Cited by 158 · see citing works
Okamoto, K., Murakami, N., Kusaka, H., Yoshida, M., Hashizume, Y., Nakazato, Y., Matsubara, E., & Hirai, S. (1992) · Journal of Neurology · doi:10.1007/bf00856806 · Cited by 122 · see citing works
Self-citationAccumulation of NEDD8 in neuronal and glial inclusions of neurodegenerative disorders
Mori, F., Nishie, M., Piao, Y., Kito, K., Kamitani, T., Takahashi, H., & Wakabayashi, K. (2004) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2004.00603.x · Cited by 121 · see citing works
Deamidation and Isoaspartate Formation in Smeared Tau in Paired Helical Filaments
Watanabe, A., Takio, K., & Ihara, Y. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.11.7368 · Cited by 120 · see citing works
Presenile Dementia With Motor Neuron Disease in Japan
Mitsuyama, Y. (1979) · Archives of Neurology · doi:10.1001/archneur.1979.00500450086021 · Cited by 114 · see citing works
Bendotti, C., Atzori, C., Piva, R., Tortarolo, M., Strong, M. J., Debiasi, S., & Migheli, A. (2004) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/63.2.113 · Cited by 103 · see citing works
Frontotemporal dementia with ubiquitinated cytoplasmic and intranuclear inclusions
Woulfe, J., KERTESZ, A. E., & Muñoz, D. G. (2001) · Acta Neuropathologica · doi:10.1007/s004010000346 · Cited by 96 · see citing works
Arai, T., Nonaka, T., Hasegawa, M., Akiyama, H., Yoshida, M., Hashizume, Y., Tsuchiya, K., Oda, T., & Ikeda, K. (2003) · Neuroscience Letters · doi:10.1016/s0304-3940(03)00216-7 · Cited by 92 · see citing works
Self-citationCognitive impairment in motor neuron disease with bulbar onset
Portet, F., Cadilhac, C., Touchon, J., & Camu, W. (2001) · Amyotrophic Lateral Sclerosis and Other Motor Neuron Disorders · doi:10.1080/146608201300079382 · Cited by 89 · see citing works
Lack of the carboxyl terminal sequence of tau in ghost tangles of Alzheimer's disease.
Endoh, R., Ogawara, M., Iwatsubo, T., Nakano, I., & Mori, H. (1993) · Brain Research · doi:10.1016/0006-8993(93)91707-y · Cited by 87 · see citing works
Self-citationMicrotubule-associated tau protein positive neuronal and glial inclusions in ALS
Yang, W., Sopper, M. M., Leystra‐Lantz, C., et al. (2003) · Neurology · doi:10.1212/01.wnl.0000099372.75786.f8 · Cited by 83 · see citing works
Different variants of frontotemporal dementia: a neuropathological and immunohistochemical study
Bergmann, M., Kuchelmeister, K., Schmid, K. W., Kretzschmar, H. A., & Schröder, R. (1996) · Acta Neuropathologica · doi:10.1007/s004010050505 · Cited by 78 · see citing works
Amyotrophic lateral sclerosis with neuronal intranuclear protein inclusions
Seilhean, D., Takahashi, J., Hachimi, K. H. E., Fujigasaki, H., Lèbre, A.-S., Biancalana, V., Dürr, A., Salachas, F., Hogenhuis, J., de Thé, H., et al. (2004) · Acta Neuropathologica · doi:10.1007/s00401-004-0855-x · Cited by 57 · see citing works
Arai, T., Ikeda, K., Akiyama, H., Tsuchiya, K., Iritani, S., Ishiguro, K., Yagishita, S., Oda, T., Odawara, T., & Iseki, E. (2003) · Acta Neuropathologica · doi:10.1007/s00401-003-0671-8 · Cited by 54 · see citing works
Self-citationUbiquitin-immunohistochemical investigation of atypical Pick's disease without Pick bodies
Iseki, E., Feng, L., Odawara, T., Hino, H., Suzuki, K., Kosaka, K., Akiyama, H., Ikeda, K., & Kato, M. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00168-3 · Cited by 39 · see citing works
Self-citationIkeda, K., Akiyama, H., Arai, T., Ueno, H., Tsuchiya, K., & Kosaka, K. (2002) · Acta Neuropathologica · doi:10.1007/s00401-001-0513-5 · Cited by 35 · see citing works
Self-citationKakita, A., Oyanagi, K., Nagai, H., & Takahashi, H. (1997) · Acta Neuropathologica · doi:10.1007/s004010050649 · Cited by 28 · see citing works
Forno, L. S., Langston, J. W., Herrick, M. K., Wilson, J. D., & Murayama, S. (2002) · Acta Neuropathologica · doi:10.1007/s00401-001-0509-1 · Cited by 25 · see citing works
Gallyas- and tau-positive glial structures in motor neuron disease with dementia.
Noda, K., Katayama, S., Watanabe, C., Yamamura, Y., & Nakamura, S. (1999) · PubMed · Cited by 22 · see citing works
Ikeda, K. (2000) · Neuropathology · doi:10.1046/j.1440-1789.2000.00270.x · Cited by 20 · see citing works
Self-citationGallyas- and tau-positive glial structures in motor neuron disease with dementia
野田, 公. (1999) · Hiroshima University Institutional Repository · Cited by 9 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis
Sreedharan, J., Blair, I. P., Tripathi, V. B., Hu, X., Vance, C., Rogelj, B., Ackerley, S., Durnall, J. C., Williams, K. L., Buratti, E., et al. (2008) · Science · doi:10.1126/science.1154584 · Cited by 2,630 · see citing works
Nelson, P. T., Alafuzoff, I., Bigio, E. H., Bouras, C., Braak, H., Cairns, N. J., Castellani, R. J., Crain, B. J., Davies, P., Tredici, K. D., et al. (2012) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31825018f7 · Cited by 2,050 · see citing works
Self-citationConverging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis
Ling, S.-C., Polymenidou, M., & Cleveland, D. W. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.033 · Cited by 1,811 · see citing works
TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis
Kabashi, E., Valdmanis, P. N., Dion, P., Spiegelman, D., McConkey, B. J., Velde, C. V., Bouchard, J.-P., Lacomblez, L., Pochigaeva, K., Salachas, F., et al. (2008) · Nature Genetics · doi:10.1038/ng.132 · Cited by 1,544 · see citing works
Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43
Polymenidou, M., Lagier-Tourenne, C., Hutt, K. R., Huelga, S. C., Moran, J., Liang, T. Y., Ling, S.-C., Sun, E., Wancewicz, E., Mazur, C., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2779 · Cited by 1,335 · see citing works
Cairns, N. J., Bigio, E. H., Mackenzie, I. R. A., Neumann, M., Lee, V. M.-Y., Hatanpaa, K. J., White, C. L., Schneider, J. A., Grinberg, L. T., Halliday, G., et al. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0237-2 · Cited by 1,110 · see citing works
Self-citationTDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration
Lagier-Tourenne, C., Polymenidou, M., & Cleveland, D. W. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq137 · Cited by 1,021 · see citing works
Mackenzie, I. R. A., Bigio, E. H., Ince, P. G., Geser, F., Neumann, M., Cairns, N. J., Kwong, L. K., Forman, M. S., Ravits, J., Stewart, H., et al. (2007) · Annals of Neurology · doi:10.1002/ana.21147 · Cited by 992 · see citing works
The neuropathology of probable Alzheimer disease and mild cognitive impairment
Schneider, J. A., Arvanitakis, Z., Leurgans, S. E., & Bennett, D. A. (2009) · Annals of Neurology · doi:10.1002/ana.21706 · Cited by 935 · 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
C9orf72-mediated ALS and FTD: multiple pathways to disease
Balendra, R., & Isaacs, A. M. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0047-2 · Cited by 715 · see citing works
Van Deerlin, V. M., Leverenz, J. B., Bekris, L. M., Bird, T. D., Yuan, W., Elman, L. B., Clay, D., Wood, E. M., Chen-Plotkin, A. S., Martinez-Lage, M., et al. (2008) · The Lancet Neurology · doi:10.1016/s1474-4422(08)70071-1 · Cited by 723 · see citing works
A new subtype of frontotemporal lobar degeneration with FUS pathology
Neumann, M., Rademakers, R., Roeber, S., Baker, M., Kretzschmar, H. A., & Mackenzie, I. R. A. (2009) · Brain · doi:10.1093/brain/awp214 · Cited by 722 · see citing works
Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration
Lee, E. B., Lee, V. M.-Y., & Trojanowski, J. Q. (2012) · Nature Reviews Neuroscience · doi:10.1038/nrn3121 · Cited by 659 · see citing works
Arendt, T., Stieler, J. T., & Holzer, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.018 · Cited by 609 · see citing works
TDP-43 proteinopathy and motor neuron disease in chronic traumatic encephalopathy
McKee, A. C., Gavett, B. E., Stern, R. A., Nowinski, C. J., Cantu, R. C., Kowall, N. W., Perl, D. P., Hedley-Whyte, E. T., Price, B., Sullivan, C., et al. (2010) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181ee7d85 · Cited by 659 · see citing works
Filimonenko, M., Stuffers, S., Raiborg, C., Yamamoto, A., Malerød, L., Fisher, E. M. C., Isaacs, A., Brech, A., Stenmark, H., & Simonsen, A. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200702115 · Cited by 626 · see citing works
Barmada, S. J., Skibinski, G., Korb, E., Rao, E. J., Wu, J. Y., & Finkbeiner, S. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4988-09.2010 · Cited by 554 · see citing works
Modeling sporadic ALS in iPSC-derived motor neurons identifies a potential therapeutic agent
Fujimori, K., Ishikawa, M., Otomo, A., Atsuta, N., Nakamura, R., Akiyama, T., Hadano, S., Aoki, M., Saya, H., Sobue, G., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0140-5 · Cited by 494 · see citing works
Exaggerated inflammation, impaired host defense, and neuropathology in progranulin-deficient mice
Yin, F., Banerjee, R., Thomas, B., Zhou, P., Qian, L., Jia, T., Ma, X., Ma, Y., Iadecola, C., Beal, M. F., et al. (2010) · Journal of Experimental Medicine · doi:10.1084/jem.20091568 · Cited by 480 · see citing works
Al-Sarraj, S., King, A., Troakes, C., Smith, B., Maekawa, S., Bodi, I., Rogelj, B., Al-Chalabi, A., Hortobágyi, T., & Shaw, C. E. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0911-2 · Cited by 475 · see citing works
NLRP3 inflammasome in neurological diseases, from functions to therapies
Song, L., Pei, L., Yao, S., Wu, Y., & Shang, Y. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00063 · Cited by 467 · see citing works
Extracellular vesicles in neurodegenerative disease — pathogenesis to biomarkers
Thompson, A. G., Gray, E., Heman-Ackah, S. M., Mäger, I., Talbot, K., Andaloussi, S. E., Wood, M. J., & Turner, M. R. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2016.68 · Cited by 431 · see citing works
TDP-43 stage, mixed pathologies, and clinical Alzheimer’s-type dementia
James, B. D., Wilson, R. S., Boyle, P. A., Trojanowski, J. Q., Bennett, D. A., & Schneider, J. A. (2016) · Brain · doi:10.1093/brain/aww224 · Cited by 407 · see citing works
Sellier, C., Campanari, M., Julie Corbier, C., Gaucherot, A., Kolb‐Cheynel, I., Oulad‐Abdelghani, M., Ruffenach, F., Page, A., Ciura, S., Kabashi, E., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593350 · Cited by 414 · see citing works
ALS Genetics: Gains, Losses, and Implications for Future Therapies
Kim, G., Gautier, O., Tassoni-Tsuchida, E., Ma, X. R., & Gitler, A. D. (2020) · Neuron · doi:10.1016/j.neuron.2020.08.022 · Cited by 370 · see citing works
Uryu, K., Nakashima-Yasuda, H., Forman, M. S., Kwong, L. K., Clark, C. M., Grossman, M., Miller, B. L., Kretzschmar, H. A., Lee, V. M.-Y., Trojanowski, J. Q., et al. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31817713b5 · Cited by 382 · see citing works
Wang, I.-F., Guo, B.-S., Liu, Y.-C., Wu, C.-C., Yang, C.-H., Tsai, K.-J., & Shen, C.-K. J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206362109 · Cited by 377 · see citing works
<i>TDP</i> ‐ <i>43</i> mutation in familial amyotrophic lateral sclerosis
Yokoseki, A., Shiga, A., Tan, C., Tagawa, A., Kaneko, H., Koyama, A., Eguchi, H., Tsujino, A., Ikeuchi, T., Kakita, A., et al. (2008) · Annals of Neurology · doi:10.1002/ana.21392 · Cited by 373 · see citing works
Serio, A., Bilican, B., Barmada, S. J., Ando, D. M., Zhao, C., Siller, R., Burr, K., Haghi, G., Story, D., Nishimura, A. L., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300398110 · Cited by 345 · see citing works
Understanding the role of TDP-43 and FUS/TLS in ALS and beyond
Da Cruz, S., & Cleveland, D. W. (2011) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2011.05.029 · Cited by 351 · see citing works
Tam, O. H., Rozhkov, N. V., Shaw, R., Kim, D., Hubbard, I., Fennessey, S., Propp, N., Phatnani, H., Kwan, J., Sareen, D., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.09.066 · Cited by 327 · see citing works
Bilican, B., Serio, A., Barmada, S. J., Nishimura, A. L., Sullivan, G. J., Carrasco, M., Phatnani, H. P., Puddifoot, C. A., Story, D., Fletcher, J., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1202922109 · Cited by 328 · see citing works
Almeida, S., Gascon, E., Tran, H., Chou, H. J., Gendron, T. F., DeGroot, S., Tapper, A. R., Sellier, C., Charlet-Berguerand, N., Karydas, A., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1149-y · Cited by 321 · see citing works
Pottier, C., Bieniek, K. F., Finch, N., van de Vorst, M., Baker, M., Perkersen, R., Brown, P., Ravenscroft, T., van Blitterswijk, M., Nicholson, A. M., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1436-x · Cited by 312 · see citing works
Mitra, J., Guerrero, E. N., Hegde, P. M., Liachko, N. F., Wang, H., Vasquez, V., Gao, J., Pandey, A., Taylor, J. P., Kraemer, B. C., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1818415116 · Cited by 305 · see citing works
The genetics and neuropathology of frontotemporal lobar degeneration
Sieben, A., Van Langenhove, T., Engelborghs, S., Martin, J.-J., Boon, P., Cras, P., De Deyn, P.-P., Santens, P., Van Broeckhoven, C., & Cruts, M. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-1029-x · Cited by 280 · see citing works
Mutations in CHMP2B in Lower Motor Neuron Predominant Amyotrophic Lateral Sclerosis (ALS)
Cox, L. E., Ferraiuolo, L., Goodall, E. F., Heath, P. R., Higginbottom, A., Mortiboys, H., Hollinger, H. C., Hartley, J. A., Brockington, A., Burness, C. E., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009872 · Cited by 262 · see citing works
Truncated stathmin-2 is a marker of TDP-43 pathology in frontotemporal dementia
Prudencio, M., Humphrey, J., Pickles, S., Brown, A.-L., Hill, S. E., Kachergus, J. M., Shi, J., Heckman, M. G., Spiegel, M. R., Cook, C., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci139741 · Cited by 231 · see citing works
Cellular senescence and Alzheimer disease: the egg and the chicken scenario
Saez-Atienzar, S., & Masliah, E. (2020) · Nature Reviews Neuroscience · doi:10.1038/s41583-020-0325-z · Cited by 257 · see citing works
TDP‐43, a neuro‐pathosignature factor, is essential for early mouse embryogenesis
Wu, L., Cheng, W., Hou, S., Yan, Y., Jiang, S., & Shen, C. ‐. J. (2010) · genesis · doi:10.1002/dvg.20584 · Cited by 256 · see citing works
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 · see citing works
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 · see citing works
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 · 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
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 · see citing works
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 · see citing works
Self-citationRetrotransposon activation contributes to neurodegeneration in a Drosophila TDP-43 model of ALS
Krug, L., Chatterjee, N., Borges-Monroy, R., Hearn, S., Liao, W.-W., Morrill, K., Prazak, L., Rozhkov, N., Theodorou, D., Hammell, M., et al. (2017) · PLOS Genetics · doi:10.1371/journal.pgen.1006635 · Cited by 201 · see citing works
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 · see citing works
“[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 · see citing works
Tashiro, 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 · see citing works
Geser, F., Lee, V. M.-Y., & Trojanowski, J. Q. (2010) · Neuropathology · doi:10.1111/j.1440-1789.2009.01091.x · Cited by 195 · see citing works
<i>C9orf72</i> 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 · see citing works
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 · see citing works
Misregulated 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 · see citing works
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 · see citing works
Frontotemporal dementia and related disorders: Deciphering the enigma
Josephs, K. A. (2008) · Annals of Neurology · doi:10.1002/ana.21426 · Cited by 166 · see citing works
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 · see citing works
<i>Progranulin</i> 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 · see citing works
“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 · see citing works
Amyotrophic Lateral Sclerosis: From Current Developments in the Laboratory to Clinical Implications
Cozzolino, M., Ferri, A., & Teresa Carrì, M. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1760 · Cited by 156 · see citing works
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 · see citing works
SQSTM1 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 · see citing works
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 · see citing works
Self-citationProgranulin: 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 · see citing works
Chen-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 · see citing works
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 · see citing works
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 · 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
Sasaki, S. (2010) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181d44992 · Cited by 121 · see citing works
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 · see citing works
Risk genotypes at TMEM106B are associated with cognitive impairment in amyotrophic lateral sclerosis
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 · see citing works
Synergistic effect between proteasome and autophagosome in the clearance of polyubiquitinated TDP‐43
Urushitani, M., Sato, T., Bamba, H., Hisa, Y., & Tooyama, I. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22243 · Cited by 114 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Risk factors and emerging therapies in amyotrophic lateral sclerosis
Nowicka, N., Juranek, J., Juranek, J. K., & Wojtkiewicz, J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20112616 · Cited by 106 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Genetics of Amyotrophic Lateral Sclerosis
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 · see citing works
Proteomics Approaches for Biomarker and Drug Target Discovery in ALS and FTD
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 · see citing works
Modeling cell-autonomous motor neuron phenotypes in ALS using iPSCs
Hawrot, J., Imhof, S., & Wainger, B. J. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104680 · Cited by 74 · see citing works
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 · see citing works
ALS and frontotemporal dysfunction: a review
Achi, E. Y., & Rudnicki, S. A. (2012) · Neurology Research International · doi:10.1155/2012/806306 · Cited by 74 · see citing works
Rising Stars: Astrocytes as a Therapeutic Target for ALS Disease
Izrael, M., Slutsky, S. G., & Revel, M. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00824 · Cited by 73 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Self-citationAxonal ligation induces transient redistribution of TDP-43 in brainstem motor neurons
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 · see citing works
Koga, S., Sanchez‐Contreras, M., Josephs, K. A., Uitti, R. J., Graff‐Radford, N., van Gerpen, J. A., Cheshire, W. P., Wszolek, Z. K., Rademakers, R., & Dickson, D. W. (2017) · Movement Disorders · doi:10.1002/mds.26809 · Cited by 63 · see citing works
Biomarkers for diseases with TDP-43 pathology
Steinacker, P., Barschke, P., & Otto, M. (2019) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2018.10.003 · Cited by 57 · see citing works
Chang, Y.-H., & Dubnau, J. (2023) · Nature Communications · doi:10.1038/s41467-023-36649-z · Cited by 49 · see citing works
The 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 · see citing works
Approaches to gene modulation therapy for ALS
Meijboom, K. E., & Brown, R. H. (2022) · Neurotherapeutics · doi:10.1007/s13311-022-01285-w · Cited by 38 · see citing works
Concurrent tau pathologies in frontotemporal lobar degeneration with TDP‐43 pathology
Koga, S., Zhou, X., Murakami, A., Fernandez De Castro, C., Baker, M. C., Rademakers, R., & Dickson, D. W. (2022) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12778 · Cited by 30 · see citing works
Could sirtuin activities modify ALS onset and progression?
Tang, B. L. (2017) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-016-0452-2 · Cited by 24 · see citing works
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 · see citing works
“In the case of amyotrophic sclerosis (ALS), cytoplasmic inclusions of transactive response DNA binding protein 43 kDa (TDP-43) are observed in approximately 97% of all patients, including patients with sporadic ALS (sALS) or familial ALS (fALS) (1-3), as well as in subsets of patients with frontotemporal dementia (FTD…”
BackgroundInfluentialChallenges in Therapeutically Targeting the <scp>RNA</scp>‐Recognition Motif
Schmeing, S., & Hart, P. '. (2024) · WIREs RNA · doi:10.1002/wrna.1877 · Cited by 11 · see citing works
- Authors
- Arai, T., Hasegawa, M., Akiyama, H., Ikeda, K., Nonaka, T., Mori, H., Mann, D., Tsuchiya, K., Yoshida, M., Hashizume, Y., & Oda, T.
- Affiliations
- Tokyo Institute of Psychiatry (JP)
- Osaka City University (JP)
- University of Manchester (GB)
- Tokyo Metropolitan Matsuzawa Hospital (JP)
- Aichi Medical University (JP)
- Corresponding author
- Arai, Tetsuaki
- Hasegawa, Masato
- ORCID
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 2006-12
- Volume
- 351
- Issue
- 3
- Pages
- 602-611
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W2031964319
- Cited by
- 2,732
- References
- 53
- Citations by year
- 2026: 122 · 2025: 181 · 2024: 182 · 2023: 168 · 2022: 181 · 2021: 191 · 2020: 177 · 2019: 133 · 2018: 153 · 2017: 124 · 2016: 132 · 2015: 94 · 2014: 106 · 2013: 136 · 2012: 134
- FWCI
- 57.53
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion)
- PubMed (publishedVersion)
- Research Explorer (The University of Manchester) (publishedVersion)
- Topics
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Health Sciences › Medicine › Physiology › 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, dystrophic neurites, neuronal intranuclear inclusions, glial inclusions, TDP-43 phosphorylation, proteinopathies, motor neuron disease, neurodegeneration
- MeSH terms
- Aged, Aged, 80 and over, Amyotrophic Lateral Sclerosis, Brain, Inclusion Bodies, Dementia, DNA-Binding Proteins, Female, Humans, Male, Middle Aged, Tissue Distribution, tau Proteins, Ubiquitin
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