Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

Frontotemporal lobar degeneration: A consensus on clinical diagnostic criteria

Neary, D., Snowden, J. S., Gustafson, L., Passant, U., Stuss, D., Black, S., Freedman, M., Kertesz, A., Robert, P. H., Albert, M., et al. (1998) · Neurology · doi:10.1212/wnl.51.6.1546 · Cited by 5,047 · see citing works

Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17

Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498 · see citing works

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

Null mutations in progranulin cause ubiquitin-positive frontotemporal dementia linked to chromosome 17q21

Cruts, 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

Tau is a candidate gene for chromosome 17 frontotemporal dementia

Poorkaj, P., Bird, T. D., Wijsman, E., Nemens, E., Garruto, R. M., Anderson, L., Andreadis, A., Wiederholt, W. C., Raskind, M., & Schellenberg, G. D. (1998) · Annals of Neurology · doi:10.1002/ana.410430617 · Cited by 1,374 · see citing works

Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs

Ou, S.-H. I., Wu, F. K., Harrich, D., Garcı́a-Martı́nez, L. F., & Gaynor, R. B. (1995) · Journal of Virology · doi:10.1128/jvi.69.6.3584-3596.1995 · Cited by 762 · see citing works

Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs

Forman, M. S., Trojanowski, J. Q., & Lee, V. M.-Y. (2004) · Nature Medicine · doi:10.1038/nm1113 · Cited by 715 · 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

Nuclear factor TDP‐43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping

Buratti, E., Dörk, T., Zuccato, E., Pagani, F., Romano, M., & Baralle, F. E. (2001) · The EMBO Journal · doi:10.1093/emboj/20.7.1774 · Cited by 633 · see citing works

Clinicopathological correlates in frontotemporal dementia

Hodges, J. R., Davies, R. R., Xuereb, J. H., Casey, B., Broe, M., Bak, T. H., Kril, J. J., & Halliday, G. M. (2004) · Annals of Neurology · doi:10.1002/ana.20203 · Cited by 580 · see citing works

Frontotemporal dementia: Clinicopathological correlations

Forman, M. S., Farmer, J., Johnson, J. K., Clark, C. M., Arnold, S. E., Coslett, H. B., Chatterjee, A., Hurtig, H. I., Karlawish, J. H., Rosen, H. J., et al. (2006) · Annals of Neurology · doi:10.1002/ana.20873 · Cited by 478 · see citing works

Frontotemporal Lobar Degeneration

Johnson, J. K., Diehl, J., Mendez, M. F., Neuhaus, J. M., Shapira, J. S., Forman, M. S., Chute, D. J., Roberson, E. D., Pace-Savitsky, C., Neumann, M., et al. (2005) · Archives of Neurology · doi:10.1001/archneur.62.6.925 · Cited by 423 · see citing works

Human, Drosophila, and C.elegans TDP43: Nucleic Acid Binding Properties and Splicing Regulatory Function

Ayala, Y. M., Pantano, S., D’Ambrogio, A., Buratti, E., Brindisi, A., Marchetti, C., Romano, M., & Baralle, F. E. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.02.038 · Cited by 375 · 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

Depletion of TDP 43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene

Mercado, P. A. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki897 · Cited by 226 · 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

Frontotemporal lobar degeneration with motor neuron disease-type inclusions predominates in 76 cases of frontotemporal degeneration

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

Nuclear Factor TDP-43 Binds to the Polymorphic TG Repeats in CFTR Intron 8 and Causes Skipping of Exon 9: A Functional Link with Disease Penetrance

Buratti, E., Brindisi, A., Pagani, F., & Baralle, F. E. (2004) · The American Journal of Human Genetics · doi:10.1086/420978 · Cited by 187 · see citing works

Frontotemporal dementia: A review

Grossman, M. (2002) · Journal of the International Neuropsychological Society · doi:10.1017/s1355617702814357 · Cited by 182 · see citing works

Ubiquitin Immunohistochemistry Suggests Classic Motor Neuron Disease, Motor Neuron Disease With Dementia, and Frontotemporal Dementia of the Motor Neuron Disease Type Represent a Clinicopathologic Spectrum

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

Hereditary dysphasic disinhibition dementia A frontotemporal dementia linked to 17 q21‐‐22

Lendon, C. L., Lynch, T., Norton, J. B., McKeel, D. W., Busfield, F., Craddock, N. J., Chakraverty, S., Gopalakrishnan, G., Shears, S., Grimmett, W., et al. (1998) · Neurology · doi:10.1212/wnl.50.6.1546 · Cited by 144 · see citing works

Histopathological changes underlying frontotemporal lobar degeneration with clinicopathological correlation

Shi, J., Shaw, C. L., du Plessis, D., Richardson, A. M. T., Bailey, K. L., Julien, C. L., Stopford, C. L., Thompson, J. C., Varma, A. R., Craufurd, D., et al. (2005) · Acta Neuropathologica · doi:10.1007/s00401-005-1079-4 · Cited by 139 · see citing works

Tau negative frontal lobe dementia at 17q21: significant finemapping of the candidate region to a 4.8 cM interval

Rademakers, R., Cruts, M., Dermaut, B., Sleegers, K., Rosso, S. M., den Broeck, M. V., Backhovens, H., Swieten, J. C. V., van Duijn, C. M., & Broeckhoven, C. V. (2002) · Molecular Psychiatry · doi:10.1038/sj.mp.4001198 · Cited by 104 · see citing works

A family with tau-negative frontotemporal dementia and neuronal intranuclear inclusions linked to chromosome 17

Mackenzie, I. R., Baker, M., West, G., Woulfe, J., Qadi, N., Gass, J. M., Cannon, A. D., Adamson, J. L., Feldman, H., Lindholm, C., et al. (2006) · Brain · doi:10.1093/brain/awh724 · Cited by 104 · see citing works

Expanded GGGGCC Hexanucleotide Repeat in Noncoding Region of C9ORF72 Causes Chromosome 9p-Linked FTD and ALS

DeJesus-Hernandez, M., Mackenzie, I. R., Boeve, B. F., Boxer, A. L., Baker, M., Rutherford, N. J., Nicholson, A. M., Finch, N. A., Flynn, H., Adamson, J., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.011 · Cited by 4,936 · see citing works

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide

Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744 · see citing works

A Hexanucleotide Repeat Expansion in C9ORF72 Is the Cause of Chromosome 9p21-Linked ALS-FTD

Renton, A. E., Majounie, E., Waite, A., Simón-Sánchez, J., Rollinson, S., Gibbs, J. R., Schymick, J. C., Laaksovirta, H., van Swieten, J. C., Myllykangas, L., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.010 · Cited by 4,409 · see citing works

Mechanisms underlying inflammation in neurodegeneration

Glass, C. K., Saijo, K., Winner, B., Marchetto, M. C., & Gage, F. H. (2010) · Cell · doi:10.1016/j.cell.2010.02.016 · Cited by 3,580 · 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

Amyotrophic lateral sclerosis

Kiernan, M. C., Vucic, S., Cheah, B. C., Turner, M. R., Eisen, A., Hardiman, O., Burrell, J. R., & Zoing, M. C. (2011) · The Lancet · doi:10.1016/s0140-6736(10)61156-7 · Cited by 2,603 · see citing works

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

Pathology of Neurodegenerative Diseases

Dugger, B. N., & Dickson, D. W. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a028035 · Cited by 1,665 · see citing works

Role of neuroinflammation in neurodegeneration development

Zhang, W., Xiao, D., Mao, Q., & Xia, H. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01486-5 · Cited by 1,668 · see citing works

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

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

Apolipoprotein E and Alzheimer disease: pathobiology and targeting strategies

Yamazaki, Y., Zhao, N., Caulfield, T. R., Liu, C.-C., & Bu, G. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-019-0228-7 · Cited by 1,425 · 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

Exome Sequencing Reveals VCP Mutations as a Cause of Familial ALS

Johnson, J. O., Mandrioli, J., Benatar, M., Abramzon, Y., Van Deerlin, V. M., Trojanowski, J. Q., Gibbs, J. R., Brunetti, M., Gronka, S., Wuu, J., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.036 · Cited by 1,235 · see citing works

Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia

Deng, H.-X., Chen, W., Hong, S.-T., Boycott, K. M., Gorrie, G. H., Siddique, N., Yang, Y., Fecto, F., Shi, Y., Zhai, H., et al. (2011) · Nature · doi:10.1038/nature10353 · Cited by 1,174 · see citing works

Characterizing the RNA targets and position-dependent splicing regulation by TDP-43

Tollervey, J. R., Curk, T., Rogelj, B., Briese, M., Cereda, M., Kayikci, M., König, J., Hortobágyi, T., Nishimura, A. L., Župunski, V., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2778 · Cited by 1,165 · see citing works

Neuropathologic diagnostic and nosologic criteria for frontotemporal lobar degeneration: consensus of the Consortium for Frontotemporal Lobar Degeneration

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

Autophagy and apoptosis dysfunction in neurodegenerative disorders

Ghavami, S., Shojaei, S., Yeganeh, B., Ande, S. R., Jangamreddy, J. R., Mehrpour, M., Christoffersson, J., Chaabane, W., Moghadam, A. R., Kashani, H. H., et al. (2014) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.10.004 · Cited by 1,039 · 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 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

Pathological TDP‐43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with <i>SOD1</i> mutations

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

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

Semantic dementia: a unique clinicopathological syndrome

Hodges, J. R., & Patterson, K. (2007) · The Lancet Neurology · doi:10.1016/s1474-4422(07)70266-1 · Cited by 772 · 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

TARDBP mutations in amyotrophic lateral sclerosis with TDP-43 neuropathology: a genetic and histopathological analysis

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

Neurodegenerative disease concomitant proteinopathies are prevalent, age-related and APOE4-associated

Robinson, J. L., Lee, E. B., Xie, S. X., Rennert, L., Suh, E., Bredenberg, C., Caswell, C., Van Deerlin, V. M., Yan, N., Yousef, A., et al. (2018) · Brain · doi:10.1093/brain/awy146 · Cited by 729 · see citing works

TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration

Wegorzewska, I., Bell, S., Cairns, N. J., Miller, T. M., & Baloh, R. H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908767106 · Cited by 706 · see citing works

Chronic neuropathologies of single and repetitive TBI: substrates of dementia?

Smith, D. H., Johnson, V. E., & Stewart, W. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2013.29 · Cited by 699 · see citing works

Cell-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

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

Tau and tauopathies

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 &amp; Experimental Neurology · doi:10.1097/nen.0b013e3181ee7d85 · Cited by 659 · see citing works

Targeting RNA Foci in iPSC-Derived Motor Neurons from ALS Patients with a <i>C9ORF72</i> Repeat Expansion

Sareen, D., O’Rourke, J. G., Meera, P., Muhammad, A. K. M. G., Grant, S., Simpkinson, M., Bell, S., Carmona, S., Ornelas, L., Sahabian, A., et al. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3007529 · Cited by 670 · see citing works

Protein 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

The bowel and beyond: The enteric nervous system in neurological disorders

Rao, M., & Gershon, M. D. (2016) · Nature Reviews Gastroenterology &amp; Hepatology · doi:10.1038/nrgastro.2016.107 · Cited by 629 · see citing works

Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease

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

Molecular pathways of motor neuron injury in amyotrophic lateral sclerosis

Ferraiuolo, L., Kirby, J., Grierson, A. J., Sendtner, M., & Shaw, P. J. (2011) · Nature Reviews Neurology · doi:10.1038/nrneurol.2011.152 · Cited by 615 · see citing works

Clinical, genetic and pathological heterogeneity of frontotemporal dementia: A review

Seelaar, H., Rohrer, J. D., Pijnenburg, Y. A. L., Fox, N. C., & van Swieten, J. C. (2011) · Journal of Neurology, Neurosurgery &amp; Psychiatry · doi:10.1136/jnnp.2010.212225 · Cited by 609 · see citing works

Animal models of neurodegenerative diseases

Dawson, T. M., Golde, T. E., & Lagier-Tourenne, C. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0236-8 · Cited by 576 · see citing works

TDP-43 represses cryptic exon inclusion in the FTD-ALS gene UNC13A

Ma, X. R., Prudencio, M., Koike, Y., Vatsavayai, S. C., Kim, G., Harbinski, F., Briner, A., Rodriguez, C. M., Guo, C., Akiyama, T., et al. (2022) · Nature · doi:10.1038/s41586-022-04424-7 · Cited by 574 · see citing works

Cytoplasmic Mislocalization of TDP-43 Is Toxic to Neurons and Enhanced by a Mutation Associated with Familial Amyotrophic Lateral Sclerosis

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

Current state of Alzheimer’s fluid biomarkers

Molinuevo, J. L., Ayton, S., Batrla, R., Bednar, M. M., Bittner, T., Cummings, J., Fagan, A. M., Hampel, H., Mielke, M. M., Mikulskis, A., et al. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1932-x · Cited by 518 · 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

Distinct clinical and pathological characteristics of frontotemporal dementia associated with C9ORF72 mutations

Snowden, J. S., Rollinson, S., Thompson, J. C., Harris, J. M., Stopford, C. L., Richardson, A. M. T., Jones, M., Gerhard, A., Davidson, Y. S., Robinson, A., et al. (2012) · Brain · doi:10.1093/brain/awr355 · Cited by 523 · see citing works

Amyotrophic lateral sclerosis: a neurodegenerative disorder poised for successful therapeutic translation

Mead, R. J., Shan, N., Reiser, H. J., Marshall, F., & Shaw, P. J. (2023) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00612-2 · Cited by 505 · see citing works

Valosin-containing protein (VCP) is required for autophagy and is disrupted in VCP disease

Ju, J.-S., Fuentealba, R. A., Miller, S. E., Jackson, E., Piwnica-Worms, D., Baloh, R. H., & Weihl, C. C. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200908115 · 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

TBK1 Suppresses RIPK1-Driven Apoptosis and Inflammation during Development and in Aging

Xu, D., Jin, T., Zhu, H., Chen, H., Ofengeim, D., Zou, C., Mifflin, L., Pan, L., Amin, P., Li, W., et al. (2018) · Cell · doi:10.1016/j.cell.2018.07.041 · Cited by 461 · see citing works

p62 positive, TDP-43 negative, neuronal cytoplasmic and intranuclear inclusions in the cerebellum and hippocampus define the pathology of C9orf72-linked FTLD and MND/ALS

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

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

Loss of C9ORF72 impairs autophagy and synergizes with polyQ Ataxin‐2 to induce motor neuron dysfunction and cell death

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

Concomitant TAR-DNA-Binding Protein 43 Pathology Is Present in Alzheimer Disease and Corticobasal Degeneration but Not in Other Tauopathies

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 &amp; Experimental Neurology · doi:10.1097/nen.0b013e31817713b5 · Cited by 382 · see citing works

Neuropathology of variants of progressive supranuclear palsy

Dickson, D. W., Ahmed, Z., Algom, A. A., Tsuboi, Y., & Josephs, K. A. (2010) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32833be924 · Cited by 386 · see citing works

Autophagy activators rescue and alleviate pathogenesis of a mouse model with proteinopathies of the TAR DNA-binding protein 43

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

Early frontotemporal dementia targets neurons unique to apes and humans

Seeley, W. W., Carlin, D. A., Allman, J. M., Macedo, M. N., Bush, C., Miller, B. L., & DeArmond, S. J. (2006) · Annals of Neurology · doi:10.1002/ana.21055 · Cited by 364 · see citing works

TDP-43 Is a Developmentally Regulated Protein Essential for Early Embryonic Development

Sephton, C. F., Good, S. K., Atkin, S., Dewey, C. M., Mayer, P., Herz, J., & Yu, G. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.061846 · Cited by 370 · see citing works

Astrocyte pathology and the absence of non-cell autonomy in an induced pluripotent stem cell model of TDP-43 proteinopathy

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

Antisense Oligonucleotide Therapies for Neurodegenerative Diseases

Bennett, C. F., Krainer, A. R., & Cleveland, D. W. (2019) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-070918-050501 · Cited by 353 · 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

Postmortem Cortex Samples Identify Distinct Molecular Subtypes of ALS: Retrotransposon Activation, Oxidative Stress, and Activated Glia

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

Loss of murine TDP-43 disrupts motor function and plays an essential role in embryogenesis

Kraemer, B. C., Schuck, T., Wheeler, J. M., Robinson, L. C., Trojanowski, J. Q., Lee, V. M. Y., & Schellenberg, G. D. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0659-0 · Cited by 350 · see citing works

Dipeptide repeat protein pathology in C9ORF72 mutation cases: clinico-pathological correlations

Mackenzie, I. R., Arzberger, T., Kremmer, E., Troost, D., Lorenzl, S., Mori, K., Weng, S.-M., Haass, C., Kretzschmar, H. A., Edbauer, D., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1181-y · Cited by 345 · see citing works

The small heat shock protein B8 (HspB8) promotes autophagic removal of misfolded proteins involved in amyotrophic lateral sclerosis (ALS)

Crippa, V., Sau, D., Rusmini, P., Boncoraglio, A., Onesto, E., Bolzoni, E., Galbiati, M., Fontana, E., Marino, M., Carra, S., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq257 · Cited by 330 · see citing works

U1 small nuclear ribonucleoprotein complex and RNA splicing alterations in Alzheimer’s disease

Bai, B., Hales, C. M., Chen, P.-C., Gozal, Y., Dammer, E. B., Fritz, J. J., Wang, X., Xia, Q., Duong, D. M., Street, C., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1310249110 · Cited by 335 · see citing works

Loss of function of C9orf72 causes motor deficits in a zebrafish model of amyotrophic lateral sclerosis

Ciura, S., Lattante, S., Le Ber, I., Latouche, M., Tostivint, H., Brice, A., & Kabashi, E. (2013) · Annals of Neurology · doi:10.1002/ana.23946 · Cited by 333 · see citing works

TDP-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

Mutant induced pluripotent stem cell lines recapitulate aspects of TDP-43 proteinopathies and reveal cell-specific vulnerability

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

Modeling key pathological features of frontotemporal dementia with C9ORF72 repeat expansion in iPSC-derived human neurons

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

Whole-genome sequencing reveals important role for TBK1 and OPTN mutations in frontotemporal lobar degeneration without motor neuron disease

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

Use of Caenorhabditis elegans as a model to study Alzheimer’s disease and other neurodegenerative diseases

Alexander, A. G., Marfil, V., & Li, C. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00279 · Cited by 310 · see citing works

Motor neuron disease-associated loss of nuclear TDP-43 is linked to DNA double-strand break repair defects

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

Microglia-mediated recovery from ALS-relevant motor neuron degeneration in a mouse model of TDP-43 proteinopathy

Spiller, K. J., Restrepo, C. R., Khan, T., Dominique, M. A., Fang, T. C., Canter, R. G., Roberts, C. J., Miller, K. R., Ransohoff, R. M., Trojanowski, J. Q., et al. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0083-7 · Cited by 301 · see citing works

Oxidative damage and the Nrf2-ARE pathway in neurodegenerative diseases

Gan, L., & Johnson, J. A. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.12.011 · Cited by 288 · 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

Hippocampal sclerosis in advanced age: clinical and pathological features

Nelson, P. T., Schmitt, F. A., Lin, Y., Abner, E. L., Jicha, G. A., Patel, E., Thomason, P. C., Neltner, J. H., Smith, C. D., Santacruz, K. S., et al. (2011) · Brain · doi:10.1093/brain/awr053 · Cited by 279 · see citing works

Widespread binding of FUS along nascent RNA regulates alternative splicing in the brain

Rogelj, B., Easton, L. E., Bogu, G. K., Stanton, L. W., Rot, G., Curk, T., Zupan, B., Sugimoto, Y., Modic, M., Haberman, N., et al. (2012) · Scientific Reports · doi:10.1038/srep00603 · Cited by 278 · see citing works

Microglial Activation Correlates with Disease Progression and Upper Motor Neuron Clinical Symptoms in Amyotrophic Lateral Sclerosis

Brettschneider, J., Toledo, J. B., Van Deerlin, V. M., Elman, L., McCluskey, L., Lee, V. M.-Y., & Trojanowski, J. Q. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039216 · Cited by 268 · see citing works

Clinical 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

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

Rates of hippocampal atrophy and presence of post-mortem TDP-43 in patients with Alzheimer’s disease: A longitudinal retrospective study

Josephs, K. A., Dickson, D. W., Tosakulwong, N., Weigand, S. D., Murray, M. E., Petrucelli, L., Liesinger, A. M., Senjem, M. L., Spychalla, A. J., Knopman, D. S., et al. (2017) · The Lancet Neurology · doi:10.1016/s1474-4422(17)30284-3 · Cited by 252 · 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

Drosophila screen connects nuclear transport genes to DPR pathology in c9ALS/FTD

Boeynaems, S., Bogaert, E., Michiels, E., Gijselinck, I., Sieben, A., Jovičić, A., De Baets, G., Scheveneels, W., Steyaert, J., Cuijt, I., et al. (2016) · Scientific Reports · doi:10.1038/srep20877 · Cited by 262 · see citing works

The olfactory bulb as the entry site for prion-like propagation in neurodegenerative diseases

Rey, N. L., Wesson, D. W., & Brundin, P. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.12.013 · 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

Analysis of alternative splicing associated with aging and neurodegeneration in the human brain

Tollervey, J. R., Wang, Z., Hortobágyi, T., Witten, J. T., Zarnack, K., Kayikci, M., Clark, T. A., Schweitzer, A. C., Rot, G., Curk, T., et al. (2011) · Genome Research · doi:10.1101/gr.122226.111 · Cited by 252 · see citing works

Abnormalities of Mitochondrial Dynamics in Neurodegenerative Diseases

Gao, J., Wang, L., Liu, J., Xie, F., Su, B., & Wang, X. (2017) · Antioxidants · doi:10.3390/antiox6020025 · Cited by 250 · see citing works

Patient-derived frontotemporal lobar degeneration brain extracts induce formation and spreading of TDP-43 pathology in vivo

Porta, S., Xu, Y., Restrepo, C. R., Kwong, L. K., Zhang, B., Brown, H. J., Lee, E. B., Trojanowski, J. Q., & Lee, V. M.-Y. (2018) · Nature Communications · doi:10.1038/s41467-018-06548-9 · Cited by 248 · see citing works

Mutations in SQSTM1 encoding p62 in amyotrophic lateral sclerosis: genetics and neuropathology

Teyssou, E., Takeda, T., Lebon, V., Boillée, S., Doukouré, B., Bataillon, G., Sazdovitch, V., Cazeneuve, C., Meininger, V., LeGuern, E., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1090-0 · Cited by 241 · see citing works

CRISPR–Cas9 screens in human cells and primary neurons identify modifiers of C9ORF72 dipeptide-repeat-protein toxicity

Kramer, N. J., Haney, M. S., Morgens, D. W., Jovičić, A., Couthouis, J., Li, A., Ousey, J., Ma, R., Bieri, G., Tsui, C. K., et al. (2018) · Nature Genetics · doi:10.1038/s41588-018-0070-7 · Cited by 226 · see citing works

The overlapping genetics of amyotrophic lateral sclerosis and frontotemporal dementia

Abramzon, Y. A., Fratta, P., Traynor, B. J., & Chia, R. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00042 · Cited by 244 · see citing works

The microglial NLRP3 inflammasome is activated by amyotrophic lateral sclerosis proteins

Deora, V., Lee, J. D., Albornoz, E. A., McAlary, L., Jagaraj, C. J., Robertson, A. A. B., Atkin, J. D., Cooper, M. A., Schroder, K., Yerbury, J. J., et al. (2020) · Glia · doi:10.1002/glia.23728 · Cited by 245 · 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

Modeling the Association between 43 Different Clinical and Pathological Variables and the Severity of Cognitive Impairment in a Large Autopsy Cohort of Elderly Persons

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

TARDBP mutations in motoneuron disease with frontotemporal lobar degeneration

Benajiba, L., Ber, I. L., Camuzat, A., Lacoste, M., Thomas-Antérion, C., Couratier, P., Legallic, S., Salachas, F., Hannequin, D., Décousus, M., et al. (2009) · Annals of Neurology · doi:10.1002/ana.21612 · Cited by 302 · see citing works

Pathogenic Genome Signatures That Damage Motor Neurons in Amyotrophic Lateral Sclerosis

Yousefian-Jazi, A., Seol, Y., Kim, J., Ryu, H. L., Lee, J.-H., & Ryu, H. (2020) · Cells · doi:10.3390/cells9122687 · Cited by 27 · see citing works

Rat model of TAR DNA binding protein 43 (TDP-43; TARDBP)-driven amyotrophic lateral sclerosis (ALS)

(2012) · Science-Business eXchange · doi:10.1038/scibx.2012.54

FUS Mutations in Frontotemporal Lobar Degeneration with Amyotrophic Lateral Sclerosis

Broustal, O., Camuzat, A., Guillot‐Noël, L., Guy, N., Millecamps, S., Deffond, D., Lacomblez, L., Golfier, V., Hannequin, D., Salachas, F., et al. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100837 · Cited by 100 · see citing works

Nutritional and metabolic status at diagnosis and survival of patients with Amyotrophic Lateral Sclerosis (ALS) and frontotemporal dementia (FTD) compared to patients with ALS alone

Jésus, P., Sourisseau, H., Lautrette, G., et al. (2020) · HAL (Le Centre pour la Communication Scientifique Directe)