Axonal ligation induces transient redistribution of TDP-43 in brainstem motor neurons
Abstract
Nuclear exclusion of TAR DNA binding protein 43 (TDP-43) and formation of cytosolic aggregates are a pathological characteristic of amyotrophic lateral sclerosis (ALS). However, the molecular basis of the aberrant distribution of TDP-43 remains elusive. Here, we show evidence that axonal ligation induced transient nuclear exclusion and peripheral accumulation of TDP-43, without apparent cytosolic aggregates in hypoglossal neurons in mice. Immunohistochemistry showed marked loss of nuclear TDP-43 7-14 days after ligation, which was accompanied by reduction of choline acetyltransferase (ChAT). TDP-43 staining was restored in the nucleus on day 28 exclusively in the neurons with normalized ChAT expression. We also showed that importin beta, which was shown to mediate nuclear transport of TDP-43 was downregulated transiently by nerve ligation. The analysis of the peripheral nerves proximal to the ligation revealed that TDP-43 markedly accumulated with a concomitant decrease in active autophagosome. Moreover, we showed that TDP-43 was present in the microsome fraction containing endoplasmic reticulum (ER) or autophagosomes in the brainstem section, indicating that TDP-43 is axonally transported with vesicles. These results indicate that axonal damage is associated with redistribution of TDP-43 through the combination of defective axonal autophagy periphery and the impaired nuclear transport system in the soma. Moreover, it was also shown that transient redistribution of TDP-43 does not prevent motor neurons from axonal regeneration. Therefore, our data suggest that the subcellular distribution of TDP-43 correlates to the innervation status of motor neurons, which may be governed by unidentified cause of ALS.
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?
TDP-43 binds to many cellular transcripts including tau and alpha synuclein, and its dysregulation may underlie some of the pathologies seen with these proteins; TDP-43 may influence tau isoform expression.
“TDP-43 binds to many cellular transcripts including tau and alpha synuclein, and its dysregulation may underlie some of the pathologies seen with these proteins [162]. In particular, TDP-43 may influence tau iso-form expression [136].”
From The neuropathology of sport (2014) · cites this paper as [162]
Cites
Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis
Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576 · see citing works
Arai, T., Hasegawa, M., Akiyama, H., Ikeda, K., Nonaka, T., Mori, H., Mann, D., Tsuchiya, K., Yoshida, M., Hashizume, Y., et al. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.10.093 · Cited by 2,732 · see citing works
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
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
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
Winton, 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
TDP‐43 A315T mutation in familial motor neuron disease
Gitcho, M. A., Baloh, R. H., Chakraverty, S., Mayo, K., Norton, J. B., Levitch, D., Hatanpaa, K. J., White, C. L., Bigio, E. H., Caselli, R. J., et al. (2008) · Annals of Neurology · doi:10.1002/ana.21344 · Cited by 619 · see citing works
Vimentin-Dependent Spatial Translocation of an Activated MAP Kinase in Injured Nerve
Perlson, E., Hanz, S., Ben‐Yaakov, K., Segal-Ruder, Y., Seger, R., & Fainzilber, M. (2005) · Neuron · doi:10.1016/j.neuron.2005.01.023 · Cited by 505 · see citing works
Axoplasmic Importins Enable Retrograde Injury Signaling in Lesioned Nerve
Hanz, S., Perlson, E., Willis, D. E., Zheng, J.-Q., Massarwa, R., Huerta, J. J., Koltzenburg, M., Köhler, M., van Minnen, J., Twiss, J. L., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00770-0 · Cited by 487 · see citing works
Co-morbidity of TDP-43 proteinopathy in Lewy body related diseases
Nakashima-Yasuda, H., Uryu, K., Robinson, J., Xie, S. X., Hurtig, H., Duda, J. E., Arnold, S. E., Siderowf, A., Grossman, M., Leverenz, J. B., et al. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0261-2 · Cited by 468 · see citing works
Julien, J. (2001) · Cell · doi:10.1016/s0092-8674(01)00244-6 · Cited by 435 · see citing works
Urushitani, M., Sik, A., Sakurai, T., Nukina, N., Takahashi, R., & Julien, J.-P. (2006) · Nature Neuroscience · doi:10.1038/nn1603 · Cited by 419 · see citing works
Self-citation<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
Progranulin Mediates Caspase-Dependent Cleavage of TAR DNA Binding Protein-43
Zhang, Y., Xu, Y.-F., Dickey, C. A., Buratti, E., Baralle, F. E., Bailey, R. M., Pickering-Brown, S. M., Dickson, D. W., & Petrucelli, L. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.3421-07.2007 · Cited by 371 · see citing works
Igaz, L. M., Kwong, L. K., Chen‐Plotkin, A. S., Winton, M. J., Unger, T. L., Xu, Y., Neumann, M., Trojanowski, J. Q., & Lee, V. M. ‐. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809462200 · Cited by 357 · see citing works
TDP43 is a human low molecular weight neurofilament (hNFL) mRNA-binding protein
Strong, M. J., Volkening, K., Hammond, R. R., Yang, W., Strong, W., Leystra‐Lantz, C., & Shoesmith, C. L. (2007) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2007.03.007 · Cited by 349 · see citing works
Targeted delivery to the nucleus☆
Pouton, C. W., Wagstaff, K. M., ROTH, D., Moseley, G. W., & Jans, D. A. (2007) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2007.06.010 · Cited by 246 · see citing works
Ayala, Y. M., Misteli, T., & Baralle, F. E. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800546105 · Cited by 232 · see citing works
Kwong, L. K., Neumann, M., Sampathu, D. M., Lee, V. M. ‐., & Trojanowski, J. Q. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0226-5 · Cited by 231 · 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
Steinacker, 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
Merianda, T. T., Lin, A. C., Lam, J. S. Y., Vuppalanchi, D., Willis, D. E., Karin, N. J., Holt, C. E., & Twiss, J. L. (2008) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2008.09.008 · Cited by 175 · see citing works
TDP-43 in differential diagnosis of motor neuron disorders
Dickson, D. W., Josephs, K. A., & Amador, C. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0234-5 · Cited by 143 · see citing works
Lams, B. E., Ole Isacson, A., & Sofroniew, M. V. (1988) · Brain Research · doi:10.1016/0006-8993(88)90635-x · Cited by 123 · see citing works
Nonaka, T., Arai, T., Buratti, E., Baralle, F. E., Akiyama, H., & Hasegawa, M. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.12.031 · Cited by 118 · see citing works
Kim, S. H., Shi, Y., Hanson, K. A., Williams, L. M., Sakasai, R., Bowler, M. J., & Tibbetts, R. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m808064200 · Cited by 117 · 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
Self-citationTAR-DNA Binding Protein 43 in Pick Disease
Freeman, S. H., Spires‐Jones, T. L., Hyman, B. T., Growdon, J. H., & Frosch, M. P. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181609361 · Cited by 81 · see citing works
TDP-43 immunoreactivity in anoxic, ischemic and neoplastic lesions of the central nervous system
Lee, E. B., Lee, V. M. ‐., Trojanowski, J. Q., & Neumann, M. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0331-5 · Cited by 66 · see citing works
McKerracher, L. J., Essagian, C., & Aguayo, A. (1993) · Journal of Neuroscience · doi:10.1523/jneurosci.13-12-05294.1993 · Cited by 58 · see citing works
Importin-mediated nuclear transport in neurons
Otis, K. O., Thompson, K. R., & Martin, K. C. (2006) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2006.05.001 · Cited by 54 · see citing works
Bussmann, K. A. V., & Sofroniew, M. V. (1999) · Neuroscience · doi:10.1016/s0306-4522(98)00562-4 · Cited by 45 · see citing works
Matsuura, J., Ajiki, K., Ichikawa, T., & Misawa, H. (1997) · Neuroscience Letters · doi:10.1016/s0304-3940(97)00763-5 · Cited by 25 · see citing works
Maeda, M., Ohba, N., Nakagomi, S., Suzuki, Y., Kiryu‐Seo, S., Namikawa, K., Kondoh, W., Tanaka, A., & Kiyama, H. (2004) · Neuroscience Research · doi:10.1016/j.neures.2003.11.008 · Cited by 23 · see citing works
Hypoglossal motoneurons in newborn mice receive respiratory drive from both sides of the medulla
Tarras-Wahlberg, S., & Rekling, J. C. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.02.064 · Cited by 14 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Converging 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
TDP-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
TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia
Mackenzie, I. R., Rademakers, R., & Neumann, M. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(10)70195-2 · Cited by 977 · see citing works
The Neuropathology and Neurobiology of Traumatic Brain Injury
Blennow, K., Hardy, J., & Zetterberg, H. (2012) · Neuron · doi:10.1016/j.neuron.2012.11.021 · Cited by 669 · 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
The Neuropathology of Chronic Traumatic Encephalopathy
McKee, A. C., Stein, T. D., Kiernan, P. T., & Alvarez, V. E. (2015) · Brain Pathology · doi:10.1111/bpa.12248 · Cited by 585 · see citing works
Sortilin-Mediated Endocytosis Determines Levels of the Frontotemporal Dementia Protein, Progranulin
Hu, F., Padukkavidana, T., Vægter, C. B., Brady, O. A., Zheng, Y., Mackenzie, I. R., Feldman, H., Nykjær, A., & Strittmatter, S. M. (2010) · Neuron · doi:10.1016/j.neuron.2010.09.034 · Cited by 545 · see citing works
McKee, A. C., Daneshvar, D. H., Alvarez, V. E., & Stein, T. D. (2014) · Acta Neuropathologica · doi:10.1007/s00401-013-1230-6 · Cited by 422 · see citing works
Castillo, K., Nassif, M., Valenzuela, V., Rojas, F., Matus, S., Mercado, G., Court, F. A., van Zundert, B., & Hetz, C. A. (2013) · Autophagy · doi:10.4161/auto.25188 · Cited by 338 · 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
Bentmann, E., Neumann, M., Tahirović, S., Rodde, R., Dormann, D., & Haass, C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.328757 · Cited by 277 · see citing works
Stein, T. D., Alvarez, V. E., & McKee, A. C. (2014) · Alzheimer s Research & Therapy · doi:10.1186/alzrt234 · Cited by 274 · see citing works
Chronic Traumatic Encephalopathy: The Neuropathological Legacy of Traumatic Brain Injury
Hay, J. R., Johnson, V. E., Smith, D. H., & Stewart, W. B., Jr. (2016) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-012615-044116 · Cited by 193 · see citing works
TDP-43-mediated neurodegeneration: towards a loss-of-function hypothesis?
Broeck, L. V., Callaerts, P., & Dermaut, B. (2013) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2013.11.003 · Cited by 130 · see citing works
Post-traumatic neurodegeneration and chronic traumatic encephalopathy
Daneshvar, D. H., Goldstein, L. E., Kiernan, P. T., Stein, T. D., & McKee, A. C. (2015) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2015.03.007 · Cited by 130 · see citing works
Iguchi, Y., Katsuno, M., Takagi, S., Ishigaki, S., Niwa, J., Hasegawa, M., Tanaka, F., & Sobue, G. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.002 · Cited by 101 · see citing works
Role of Transcription Factors in Peripheral Nerve Regeneration
Patodia, S., & Raivich, G. (2012) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2012.00008 · Cited by 103 · see citing works
Traumatic Brain Injury as a Trigger of Neurodegeneration
Johnson, V. E., Stewart, W. B., Jr., Arena, J. D., & Smith, D. H. (2017) · Advances in neurobiology · doi:10.1007/978-3-319-57193-5_15 · Cited by 97 · see citing works
Walker, A. K., & Atkin, J. D. (2011) · IUBMB Life · doi:10.1002/iub.520 · Cited by 100 · 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
Smethurst, P., Sidle, K. C. L., & Hardy, J. (2014) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12206 · Cited by 94 · see citing works
Does a loss of TDP-43 function cause neurodegeneration?
Xu, Z. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-27 · Cited by 91 · see citing works
Johnson, V. E., Stewart, W., Trojanowski, J. Q., & Smith, D. H. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0909-9 · Cited by 87 · see citing works
Sarm1 deletion suppresses TDP-43-linked motor neuron degeneration and cortical spine loss
White, M. A., Lin, Z., Kim, E., Henstridge, C. M., Peña‐Altamira, E., Hunt, C. K., Burchill, E., Callaghan, I., Loreto, A., Brown-Wright, H., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0800-9 · Cited by 86 · see citing works
Takeuchi, S., Fujiwara, N., Ido, A., Oono, M., Takeuchi, Y., Tateno, M., Suzuki, K., Takahashi, R., Tooyama, I., Taniguchi, N., et al. (2010) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181f4a90a · Cited by 85 · see citing works
Self-citationSynaptic Paths to Neurodegeneration: The Emerging Role of TDP-43 and FUS in Synaptic Functions
Ling, S. (2018) · Neural Plasticity · doi:10.1155/2018/8413496 · Cited by 81 · see citing works
Loss of mouse Stmn2 function causes motor neuropathy
Juan, I. G. S., Nash, L. A., Smith, K. S., Leyton-Jaimes, M. F., Qian, M., Klim, J. R., Limone, F., Dorr, A. B., Couto, A., Pintacuda, G., et al. (2022) · Neuron · doi:10.1016/j.neuron.2022.02.011 · Cited by 80 · see citing works
Connecting TDP-43 Pathology with Neuropathy
Klim, J. R., Pintacuda, G., Nash, L. A., Juan, I. G. S., & Eggan, K. C. (2021) · Trends in Neurosciences · doi:10.1016/j.tins.2021.02.008 · Cited by 65 · see citing works
Barmada, S. J., & Finkbeiner, S. M. (2010) · Reviews in the Neurosciences · doi:10.1515/revneuro.2010.21.4.251 · Cited by 62 · see citing works
Buratti, E., & Baralle, F. E. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08257.x · Cited by 56 · see citing works
TDP-43 dysregulation and neuromuscular junction disruption in amyotrophic lateral sclerosis
Lépine, S., Castellanos‐Montiel, M. J., & Durcan, T. M. (2022) · Translational Neurodegeneration · doi:10.1186/s40035-022-00331-z · Cited by 43 · see citing works
Goossens, J., Vanmechelen, E., Trojanowski, J. Q., Lee, V. M. ‐., Broeckhoven, C. V., van der Zee, J., & Engelborghs, S. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0195-1 · Cited by 43 · see citing works
Turner, B. J., Alfazema, N., Sheean, R. K., Sleigh, J. N., Davies, K. E., Horne, M. K., & Talbot, K. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.09.030 · Cited by 43 · see citing works
Li, Z., Lu, Y., Xu, X., & Gao, F. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds420 · Cited by 43 · see citing works
Bembich, S., Herzog, J. S., Conti, L. D., Stuani, C., Avendaño-Vázquez, S. E., Buratti, E., Baralle, M., & Baralle, F. E. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1343 · Cited by 41 · see citing works
Dysregulation of axonal transport and motorneuron diseases
Sau, D., Rusmini, P., Crippa, V., Onesto, E., Bolzoni, E., Ratti, A., & Poletti, A. (2011) · Biology of the Cell · doi:10.1042/bc20100093 · Cited by 36 · see citing works
Shodai, A., Ido, A., Fujiwara, N., Ayaki, T., Morimura, T., Oono, M., Uchida, T., Takahashi, R., Ito, H., & Urushitani, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0052776 · Cited by 35 · see citing works
Self-citationColombrita, C., Onesto, E., Tiloca, C., Ticozzi, N., Silani, V., & Ratti, A. (2011) · PubMed · doi:10.4449/aib.v149i1.1261 · Cited by 32 · see citing works
The long-term consequences of repetitive head impacts: Chronic traumatic encephalopathy
Alosco, M. L., & Stern, R. A. (2019) · Handbook of clinical neurology · doi:10.1016/b978-0-12-804766-8.00018-2 · Cited by 27 · see citing works
Furukawa, Y., & Nukina, N. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.04.011 · Cited by 25 · see citing works
Molecular Motor Proteins and Amyotrophic Lateral Sclerosis
Soo, K. Y., Farg, M. A., & Atkin, J. D. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12129057 · Cited by 23 · see citing works
RNA Dysregulation in Diseases of Motor Neurons
Ibrahim, F., Nakaya, T., & Mourelatos, Z. (2011) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-011110-130307 · Cited by 22 · see citing works
Jayakumar, A. R., Tong, X., Shamaladevi, N., Barcelona, S., Gaidosh, G., Agarwal, A. N., & Norenberg, M. D. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13867 · Cited by 21 · see citing works
TDP43 ribonucleoprotein granules: physiologic function to pathologic aggregates
Corbet, G. A., Wheeler, J., Parker, R., & Weskamp, K. (2021) · RNA Biology · doi:10.1080/15476286.2021.1963099 · Cited by 20 · see citing works
Ido, A., Fukuyama, H., & Urushitani, M. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12106980 · Cited by 20 · see citing works
Self-citationBumber, J. R., Pilipović, K., Janković, T., Dolenec, P., Gržeta, N., Križ, J., & Župan, G. (2020) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlaa130 · Cited by 16 · see citing works
Raivich, G. (2011) · Annals of Anatomy - Anatomischer Anzeiger · doi:10.1016/j.aanat.2011.01.010 · Cited by 13 · see citing works
Shindo, A., Yata, K., Sasaki, R., & Tomimoto, H. (2013) · Brain Research · doi:10.1016/j.brainres.2013.08.007 · Cited by 14 · see citing works
Scofield, M. D., Korutla, L., Jackson, T. G., Kalivas, P. W., & Mackler, S. A. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.09.043 · Cited by 13 · see citing works
Umahara, T., Uchihara, T., Shibata, N., Nakamura, A., & Hanyu, H. (2016) · Brain Research · doi:10.1016/j.brainres.2016.05.051 · Cited by 11 · see citing works
RNP2 of RNA Recognition Motif 1 Plays a Central Role in the Aberrant Modification of TDP-43
Takagi, S., Iguchi, Y., Katsuno, M., Ishigaki, S., Ikenaka, K., Fujioka, Y., Honda, D., Niwa, J.-I., Tanaka, F., Watanabe, H., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066966 · Cited by 5 · see citing works
Chronic traumatic encephalopathy and the nucleus basalis of Meynert.
Mufson, E., Kelley, C. M., & Perez, S. E. (2021) · Handbook of Clinical Neurology · doi:10.1016/b978-0-12-819973-2.00002-2 · Cited by 4 · see citing works
Messmer, M. L., Salapa, H. E., Popescu, B. F. G., & Levin, M. C. (2024) · Annals of Neurology · doi:10.1002/ana.27114 · Cited by 4 · see citing works
Frontotemporal Lobar Degeneration
Schlachetzki, J. C. M. (2011) · InTech eBooks · doi:10.5772/28174
Misfolded superoxide dismutase-1 in amyotrophic lateral sclerosis
Zetterström, P. (2011) · DiVA at Umeå University (Umeå University)
Involvement of endoplasmic reticulum stress in TDP-43-linked neurodegenerative disease
Walker, A. K. (2014) · Postdoc Journal · doi:10.14304/surya.jpr.v2n6.2
Conserved loop of a phase modifier endows protein condensates with fluidityPreprint
Kawamukai, H., Matsusaki, M., Tanimoto, T., Watabe, M., Morishima, K., Tomita, S., Shinkai, Y., Niwa, T., Mannen, T., Kumeta, H., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.03.601791
Mura, M. E. (2012) · UnissResearch (Università degli Studi di Sassari)
Modeling C9ORF72 loss-of-function : a knockdown mouse model
Lopez-Herdoiza, M.-B. (2016) · theses.fr (ABES) · doi:10.70675/dfc77570z827az4993z840dz21dfc54360de
de Calbiac, H. (2019) · theses.fr (ABES) · doi:10.70675/bafe951fz8332z4b0azb55bzac8a4af1955b
- Authors
- Sato, T., Takeuchi, S., Saito, A., Ding, W., Bamba, H., Matsuura, H., Hisa, Y., Tooyama, I., & Urushitani, M.
- Affiliations
- Shiga University of Medical Science (JP)
- Kyoto Prefectural University of Medicine (JP)
- Venue
- Neuroscience
- Publisher
- Elsevier BV
- Published
- 2009-12
- Volume
- 164
- Issue
- 4
- Pages
- 1565-1578
- ISSN
- 0306-4522 (ISSN-L)
- OpenAlex
- W1975640285
- Cited by
- 63
- References
- 36
- Citations by year
- 2024: 2 · 2022: 2 · 2021: 3 · 2020: 1 · 2019: 3 · 2018: 2 · 2017: 1 · 2016: 5 · 2015: 4 · 2014: 3 · 2013: 10 · 2012: 9
- FWCI
- 5.74
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Japan Society of Promotion of Science (JSPS
- Japan Health and Labour Science Research Grants
- Japan ALS Association
- Takeda Science Foundation
- Presidential Grant-in-Aid from SUMS
- Topics
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Hereditary Neurological Disorders
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Keywords
- TDP-43, amyotrophic lateral sclerosis, motor neurons, hypoglossal nucleus, nuclear exclusion, axonal transport, autophagy, importin beta, choline acetyltransferase, endoplasmic reticulum, axon regeneration, subcellular localization
- MeSH terms
- Animals, Autophagy, Axons, Axonal Transport, Brain Stem, Cell Nucleus, Choline O-Acetyltransferase, DNA-Binding Proteins, Hypoglossal Nerve, Ligation, Mice, Inbred C57BL, Motor Neurons, RNA, Messenger, Transcription, Genetic, Active Transport, Cell Nucleus, beta Karyopherins, Mice
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
