Arai T, Hasegawa M, Akiyama H, Ikeda K, Nonaka T, Mori H, Mann D, Tsuchiya K, Yoshida M, Hashizume Y et al (2006) TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem Biophys Res Commun 351:602–611. https://doi.org/10.1016/j.bbrc.2006.10.093
Article CAS PubMed Google Scholar
Ferrari R, Kapogiannis D, Huey ED, Momeni P (2011) FTD and ALS: a tale of two diseases. Curr Alzheimer Res 8:273–294. https://doi.org/10.2174/156720511795563700
Article CAS PubMed PubMed Central Google Scholar
Ling SC, Polymenidou M, Cleveland DW (2013) Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis. Neuron 79:416–438. https://doi.org/10.1016/j.neuron.2013.07.033
Article CAS PubMed PubMed Central Google Scholar
Neumann M, Sampathu DM, Kwong LK, Truax AC, Micsenyi MC, Chou TT, Bruce J, Schuck T, Grossman M, Clark CM et al (2006) Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314:130–133. https://doi.org/10.1126/science.1134108
Article CAS PubMed Google Scholar
Mackenzie IR, Bigio EH, Ince PG, Geser F, Neumann M, Cairns NJ, Kwong LK, Forman MS, Ravits J, Stewart H et al (2007) Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations. Ann Neurol 61:427–434. https://doi.org/10.1002/ana.21147
Article CAS PubMed Google Scholar
Cairns NJ, Neumann M, Bigio EH, Holm IE, Troost D, Hatanpaa KJ, Foong C, White CL 3rd, Schneider JA, Kretzschmar HA et al (2007) TDP-43 in familial and sporadic frontotemporal lobar degeneration with ubiquitin inclusions. Am J Pathol 171:227–240. https://doi.org/10.2353/ajpath.2007.070182
Article CAS PubMed PubMed Central Google Scholar
Kabashi E, Valdmanis PN, Dion P, Spiegelman D, McConkey BJ, Vande Velde C, Bouchard JP, Lacomblez L, Pochigaeva K, Salachas F et al (2008) TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis. Nat Genet 40:572–574. https://doi.org/10.1038/ng.132
Article CAS PubMed Google Scholar
Rutherford NJ, Zhang YJ, Baker M, Gass JM, Finch NA, Xu YF, Stewart H, Kelley BJ, Kuntz K, Crook RJ et al (2008) Novel mutations in TARDBP (TDP-43) in patients with familial amyotrophic lateral sclerosis. PLoS Genet 4:e1000193. https://doi.org/10.1371/journal.pgen.1000193
Article CAS PubMed PubMed Central Google Scholar
Sreedharan J, Blair IP, Tripathi VB, Hu X, Vance C, Rogelj B, Ackerley S, Durnall JC, Williams KL, Buratti E et al (2008) TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 319:1668–1672. https://doi.org/10.1126/science.1154584
Article CAS PubMed PubMed Central Google Scholar
Borroni B, Bonvicini C, Alberici A, Buratti E, Agosti C, Archetti S, Papetti A, Stuani C, Di Luca M, Gennarelli M et al (2009) Mutation within TARDBP leads to Frontotemporal Dementia without motor neuron disease. Hum Mutat 30:E974–E983. https://doi.org/10.1002/humu.21100
Article CAS PubMed Google Scholar
Chen HJ, Topp SD, Hui HS, Zacco E, Katarya M, McLoughlin C, King A, Smith BN, Troakes C, Pastore A et al (2019) RRM adjacent TARDBP mutations disrupt RNA binding and enhance TDP-43 proteinopathy. Brain 142:3753–3770. https://doi.org/10.1093/brain/awz313
Article PubMed PubMed Central Google Scholar
Al-Chalabi A, Jones A, Troakes C, King A, Al-Sarraj S, van den Berg LH (2012) The genetics and neuropathology of amyotrophic lateral sclerosis. Acta Neuropathol 124:339–352. https://doi.org/10.1007/s00401-012-1022-4
Article CAS PubMed Google Scholar
Chang X-L, Tan M-S, Tan L, Yu J-T (2015) The Role of TDP-43 in Alzheimer’s Disease. Mol Neurobiol 53:3349–3359. https://doi.org/10.1007/s12035-015-9264-5
Article CAS PubMed Google Scholar
Josephs KA, Whitwell JL, Weigand SD, Murray ME, Tosakulwong N, Liesinger AM, Petrucelli L, Senjem ML, Knopman DS, Boeve BF et al (2014) TDP-43 is a key player in the clinical features associated with Alzheimer’s disease. Acta Neuropathol 127:811–824. https://doi.org/10.1007/s00401-014-1269-z
Article CAS PubMed PubMed Central Google Scholar
Rohn TT (2008) Caspase-cleaved TAR DNA-binding protein-43 is a major pathological finding in Alzheimer’s disease. Brain Res 1228:189–198. https://doi.org/10.1016/j.brainres.2008.06.094
Article CAS PubMed PubMed Central Google Scholar
McAleese KE, Walker L, Erskine D, Thomas AJ, McKeith IG, Attems J (2017) TDP-43 pathology in Alzheimer’s disease, dementia with Lewy bodies and ageing. Brain Pathol 27:472–479. https://doi.org/10.1111/bpa.12424
Article CAS PubMed Google Scholar
Hasegawa M, Arai T, Akiyama H, Nonaka T, Mori H, Hashimoto T, Yamazaki M, Oyanagi K (2007) TDP-43 is deposited in the Guam parkinsonism-dementia complex brains. Brain 130:1386–1394. https://doi.org/10.1093/brain/awm065
Amador-Ortiz C, Lin WL, Ahmed Z, Personett D, Davies P, Duara R, Graff-Radford NR, Hutton ML, Dickson DW (2007) TDP-43 immunoreactivity in hippocampal sclerosis and Alzheimer’s disease. Ann Neurol 61:435–445. https://doi.org/10.1002/ana.21154
Article CAS PubMed PubMed Central Google Scholar
Josephs KA, Murray ME, Whitwell JL, Parisi JE, Petrucelli L, Jack CR, Petersen RC, Dickson DW (2014) Staging TDP-43 pathology in Alzheimer’s disease. Acta Neuropathol 127:441–450. https://doi.org/10.1007/s00401-013-1211-9
Article CAS PubMed Google Scholar
Meneses A, Koga S, O’Leary J, Dickson DW, Bu G, Zhao N (2021) TDP-43 pathology in Alzheimer’s disease. Mol Neurodegener 16:84. https://doi.org/10.1186/s13024-021-00503-x
Article CAS PubMed PubMed Central Google Scholar
Mackenzie IR, Neumann M, Baborie A, Sampathu DM, Du Plessis D, Jaros E, Perry RH, Trojanowski JQ, Mann DM, Lee VM (2011) A harmonized classification system for FTLD-TDP pathology. Acta Neuropathol 122:111–113. https://doi.org/10.1007/s00401-011-0845-8
Article PubMed PubMed Central Google Scholar
Gao J, Wang L, Huntley ML, Perry G, Wang X (2018) Pathomechanisms of TDP-43 in neurodegeneration. J Neurochem. https://doi.org/10.1111/jnc.14327
Article PubMed PubMed Central Google Scholar
Jo M, Lee S, Jeon YM, Kim S, Kwon Y, Kim HJ (2020) The role of TDP-43 propagation in neurodegenerative diseases: integrating insights from clinical and experimental studies. Exp Mol Med 52:1652–1662. https://doi.org/10.1038/s12276-020-00513-7
Article CAS PubMed PubMed Central Google Scholar
Swain A, Misulovin Z, Pherson M, Gause M, Mihindukulasuriya K, Rickels RA, Shilatifard A, Dorsett D (2016) Drosophila TDP-43 RNA-binding protein facilitates association of sister chromatid cohesion proteins with genes, enhancers and polycomb response elements. PLoS Genet 12:e1006331. https://doi.org/10.1371/journal.pgen.1006331
Article CAS PubMed PubMed Central Google Scholar
Fiesel FC, Weber SS, Supper J, Zell A, Kahle PJ (2012) TDP-43 regulates global translational yield by splicing of exon junction complex component SKAR. Nucl Acids Res 40:2668–2682. https://doi.org/10.1093/nar/gkr1082
Article CAS PubMed Google Scholar
Freibaum BD, Chitta RK, High AA, Taylor JP (2010) Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery. J Proteome Res 9:1104–1120. https://doi.org/10.1021/pr901076y
Article CAS PubMed PubMed Central Google Scholar
Ling JP, Pletnikova O, Troncoso JC, Wong PC (2015) TDP-43 repression of nonconserved cryptic exons is compromised in ALS-FTD. Science 349:650–655. https://doi.org/10.1126/science.aab0983
Article CAS PubMed PubMed Central Google Scholar
Polymenidou M, Lagier-Tourenne C, Hutt KR, Huelga SC, Moran J, Liang TY, Ling S-C, Sun E, Wancewicz E, Mazur C et al (2011) Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43. Nat Neurosci 14:459–468. https://doi.org/10.1038/nn.2779
Article CAS PubMed PubMed Central Google Scholar
Tollervey JR, Curk T, Rogelj B, Briese M, Cereda M, Kayikci M, König J, Hortobágyi T, Nishimura AL, Župunski V et al (2011) Characterizing the RNA targets and position-dependent splicing regulation by TDP-43. Nat Neurosci 14:452–458. https://doi.org/10.1038/nn.2778
Article CAS PubMed PubMed Central Google Scholar
Alami NH, Smith RB, Carrasco MA, Williams LA, Winborn CS, Han SS, Kiskinis E, Winborn B, Freibaum BD, Kanagaraj A et al (2014) Axonal transport of TDP-43 mRNA granules is impaired by ALS-causing mutations. Neuron 81:536–543. https://doi.org/10.1016/j.neuron.2013.12.018
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