C9orf72 poly(GR) aggregation induces TDP-43 proteinopathy

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

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

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

TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

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

Neurofilament light chain as a biomarker in neurological disorders

Gaetani, L., Blennow, K., Calabresi, P., Di Filippo, M., Parnetti, L., & Zetterberg, H. (2019) · Journal of Neurology, Neurosurgery & Psychiatry · doi:10.1136/jnnp-2018-320106 · Cited by 1,334 · see citing works

Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS

Elden, A. C., Kim, H.-J., Hart, M. P., Chen‐Plotkin, A. S., Johnson, B. S., Fang, X., Armakola, M., Geser, F., Greene, R. A., Lu, M. M., et al. (2010) · Nature · doi:10.1038/nature09320 · Cited by 1,327 · see citing works

The C9orf72 GGGGCC Repeat Is Translated into Aggregating Dipeptide-Repeat Proteins in FTLD/ALS

Mori, K., Weng, S., Arzberger, T., May, S., Rentzsch, K., Kremmer, E., Schmid, B., Kretzschmar, H. A., Cruts, M., Broeckhoven, C. V., et al. (2013) · Science · doi:10.1126/science.1232927 · Cited by 1,248 · see citing works

Unconventional Translation of C9ORF72 GGGGCC Expansion Generates Insoluble Polypeptides Specific to c9FTD/ALS

Ash, P. E. A., Bieniek, K. F., Gendron, T. F., Caulfield, T. R., Lin, W.-L., DeJesus‐Hernandez, M., van Blitterswijk, M., Jansen‐West, K. R., Paul, J. W., Rademakers, R., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.02.004 · Cited by 1,079 · 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

GGGGCC repeat expansion in C9orf72 compromises nucleocytoplasmic transport

Freibaum, B. D., Lu, Y., Lopez-Gonzalez, R., Kim, N. C., Almeida, S., Lee, K.-H., Badders, N., Valentine, M., Miller, B. L., Wong, P. C., et al. (2015) · Nature · doi:10.1038/nature14974 · Cited by 841 · see citing works

TDP-43 Is Intrinsically Aggregation-prone, and Amyotrophic Lateral Sclerosis-linked Mutations Accelerate Aggregation and Increase Toxicity

Johnson, B. S., Snead, D., Lee, J. J., McCaffery, J. M., Shorter, J., & Gitler, A. D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.010264 · Cited by 790 · see citing works

RAN proteins and RNA foci from antisense transcripts in C9ORF72 ALS and frontotemporal dementia

Zu, T., Liu, Y., Báñez-Coronel, M., Reid, T. S., Pletniková, O., Lewis, J. M., Miller, T. M., Harms, M. B., Falchook, A. E., Subramony, S. H., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1315438110 · Cited by 748 · see citing works

Characterization and Functional Implications of the RNA Binding Properties of Nuclear Factor TDP-43, a Novel Splicing Regulator ofCFTR Exon 9

Buratti, E., & Baralle, F. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104236200 · Cited by 697 · see citing works

C9orf72 Dipeptide Repeats Impair the Assembly, Dynamics, and Function of Membrane-Less Organelles

Lee, K., Zhang, P., Kim, H. J., Mitrea, D. M., Sarkar, M., Freibaum, B. D., Cika, J., Coughlin, M., Messing, J. A., Molliex, A., et al. (2016) · Cell · doi:10.1016/j.cell.2016.10.002 · Cited by 687 · see citing works

Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity

Zhang, Y., Xu, Y.-F., Cook, C. N., Gendron, T. F., Roettges, P. S., Link, C. D., Lin, W.-L., Tong, J., Castanedes‐Casey, M., Ash, P. E. A., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900688106 · Cited by 604 · see citing works

Modifiers of C9orf72 dipeptide repeat toxicity connect nucleocytoplasmic transport defects to FTD/ALS

Jovičić, A., Mertens, J., Boeynaems, S., Bogaert, E., Chai, N., Yamada, S. B., Paul, J. W., Sun, S., Herdy, J. R., Bieri, G., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4085 · Cited by 598 · see citing works

Antisense transcripts of the expanded C9ORF72 hexanucleotide repeat form nuclear RNA foci and undergo repeat-associated non-ATG translation in c9FTD/ALS

Gendron, T. F., Bieniek, K. F., Zhang, Y., Jansen‐West, K. R., Ash, P. E. A., Caulfield, T. R., Daughrity, L. M., Dunmore, J., Castanedes‐Casey, M., Chew, J., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1192-8 · Cited by 569 · see citing works

Targeted degradation of sense and antisense C9orf72 RNA foci as therapy for ALS and frontotemporal degeneration

Lagier‐Tourenne, C., Baughn, M. W., Rigo, F., Sun, S., Liu, P., Li, H., Jiang, J., Watt, A. T., Chun, S. J., Katz, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1318835110 · Cited by 555 · see citing works

Gain of toxicity from ALS/FTD-linked repeat expansions in C9ORF72 is alleviated by antisense oligonucleotides targeting GGGGCC-containing RNAs

Jiang, J., Zhu, Q., Gendron, T. F., Saberi, S., McAlonis-Downes, M., Seelman, A., Stauffer, J. E., Jafar-nejad, P., Drenner, K., Schulte, D., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.04.006 · Cited by 536 · see citing works

RNA Binding Antagonizes Neurotoxic Phase Transitions of TDP-43

Mann, J. R., Gleixner, A. M., Mauna, J. C., Gomes, E., DeChellis-Marks, M. R., Needham, P. G., Copley, K. E., Hurtle, B. T., Portz, B., Pyles, N. J., et al. (2019) · Neuron · doi:10.1016/j.neuron.2019.01.048 · Cited by 528 · see citing works

Cytoplasmic TDP-43 De-mixing Independent of Stress Granules Drives Inhibition of Nuclear Import, Loss of Nuclear TDP-43, and Cell Death

Gasset-Rosa, F., Lu, S., Yu, H., Chen, C., Melamed, Z., Guo, L. E., Shorter, J., Cruz, S. D., & Cleveland, D. W. (2019) · Neuron · doi:10.1016/j.neuron.2019.02.038 · Cited by 506 · see citing works

Phase Separation of C9orf72 Dipeptide Repeats Perturbs Stress Granule Dynamics

Boeynaems, S., Bogaert, E., Kovács, D., Konijnenberg, A., Timmerman, E., Volkov, A. N., Guharoy, M., Decker, M. D., Jaspers, T., Ryan, V. H., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.02.013 · Cited by 502 · see citing works

Bidirectional transcripts of the expanded C9orf72 hexanucleotide repeat are translated into aggregating dipeptide repeat proteins

Mori, K., Arzberger, T., Grässer, F. A., Gijselinck, I., May, S., Rentzsch, K., Weng, S., Schludi, M. H., van der Zee, J., Cruts, M., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1189-3 · Cited by 482 · see citing works

Nuclear-Import Receptors Reverse Aberrant Phase Transitions of RNA-Binding Proteins with Prion-like Domains

Guo, L. E., Kim, H. J., Wang, H. H., Monaghan, J., Freyermuth, F., Sung, J. C., O’Donovan, K., Fare, C. M., Diaz, Z., Singh, N., et al. (2018) · Cell · doi:10.1016/j.cell.2018.03.002 · Cited by 467 · see citing works

A single N‐terminal phosphomimic disrupts TDP‐43 polymerization, phase separation, and RNA splicing

Wang, A., Conicella, A. E., Schmidt, H. B., Martin, E. W., Rhoads, S. N., Reeb, A. N., Nourse, A., Montero, D. R., Ryan, V. H., Rohatgi, R., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201797452 · Cited by 445 · see citing works

Stress Granule Assembly Disrupts Nucleocytoplasmic Transport

Zhang, K., Daigle, J. G., Cunningham, K. M., Coyne, A. N., Ruan, K., Grima, J. C., Bowen, K., Wadhwa, H., Yang, P., Rigo, F., et al. (2018) · Cell · doi:10.1016/j.cell.2018.03.025 · Cited by 423 · see citing works

C9ORF72 repeat expansions in mice cause TDP-43 pathology, neuronal loss, and behavioral deficits

Chew, J., Gendron, T. F., Prudencio, M., Sasaguri, H., Zhang, Y., Castanedes‐Casey, M., Lee, C. W., Jansen‐West, K. R., Kurti, A., Murray, M. E., et al. (2015) · Science · doi:10.1126/science.aaa9344 · Cited by 410 · see citing works

C9orf72 BAC Mouse Model with Motor Deficits and Neurodegenerative Features of ALS/FTD

Liu, Y., Pattamatta, A., Zu, T., Reid, T. S., Bardhi, O., Borchelt, D., Yachnis, A. T., & Ranum, L. P. W. (2016) · Neuron · doi:10.1016/j.neuron.2016.04.005 · Cited by 368 · 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

Serum neurofilament light as a biomarker for mild traumatic brain injury in contact sports

Shahim, P., Zetterberg, H., Tegner, Y., & Blennow, K. (2017) · Neurology · doi:10.1212/wnl.0000000000003912 · Cited by 332 · see citing works

C9orf72 frontotemporal lobar degeneration is characterised by frequent neuronal sense and antisense RNA foci

Mizielinska, S., Lashley, T., Norona, F. E., Clayton, E. L., Ridler, C. E., Fratta, P., & Isaacs, A. M. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1200-z · Cited by 317 · see citing works

C9ORF72 poly(GA) aggregates sequester and impair HR23 and nucleocytoplasmic transport proteins

Zhang, Y., Gendron, T. F., Grima, J. C., Sasaguri, H., Jansen‐West, K. R., Xu, Y.-F., Katzman, R. B., Gass, J. M., Murray, M. E., Shinohara, M., et al. (2016) · Nature Neuroscience · doi:10.1038/nn.4272 · Cited by 315 · see citing works

Poly(GR) impairs protein translation and stress granule dynamics in C9orf72-associated frontotemporal dementia and amyotrophic lateral sclerosis

Zhang, Y., Gendron, T. F., Ebbert, M., O’Raw, A. D., Yue, M., Jansen‐West, K. R., Zhang, X., Prudencio, M., Chew, J., Cook, C. N., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0071-1 · Cited by 307 · see citing works

C 9orf72 ablation in mice does not cause motor neuron degeneration or motor deficits

Koppers, M., Blokhuis, A. M., Westeneng, H., Terpstra, M. L., Zundel, C. A. C., de Sá, R. V., Schellevis, R. D., Waite, A. J., Blake, D. J., Veldink, J. H., et al. (2015) · Annals of Neurology · doi:10.1002/ana.24453 · Cited by 268 · see citing works

Poly(GP) proteins are a useful pharmacodynamic marker for <i>C9ORF72</i> -associated amyotrophic lateral sclerosis

Gendron, T. F., Chew, J., Stankowski, J. N., Hayes, L. R., Zhang, Y.-J., Prudencio, M., Carlomagno, Y., Daughrity, L. M., Jansen-West, K., Perkerson, E. A., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aai7866 · Cited by 265 · see citing works

Quantitative analysis and clinico-pathological correlations of different dipeptide repeat protein pathologies in C9ORF72 mutation carriers

Mackenzie, I. R. A., Frick, P., Grässer, F. A., Gendron, T. F., Petrucelli, L., Cashman, N. R., Edbauer, D., Kremmer, E., Prudlo, J., Troost, D., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1476-2 · Cited by 231 · see citing works

RAN translation at C9orf72-associated repeat expansions is selectively enhanced by the integrated stress response

Green, K. M., Glineburg, M. R., Kearse, M. G., Flores, B. N., Linsalata, A. E., Fedak, S., Goldstrohm, A. C., Barmada, S. J., & Todd, P. K. (2017) · Nature Communications · doi:10.1038/s41467-017-02200-0 · Cited by 222 · see citing works

C9ORF72 GGGGCC repeat-associated non-AUG translation is upregulated by stress through eIF2α phosphorylation

Cheng, W., Wang, S., Mestre, A. A., Fu, C., Makarem, A. O., Xian, F., Hayes, L. R., Lopez-Gonzalez, R., Drenner, K., Jiang, J., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-02495-z · Cited by 203 · see citing works

Heterochromatin anomalies and double-stranded RNA accumulation underlie C9orf72 poly(PR) toxicity

Zhang, Y., Guo, L. E., Gonzales, P. K., Gendron, T. F., Wu, Y., Jansen‐West, K. R., O’Raw, A. D., Pickles, S. R., Prudencio, M., Carlomagno, Y., et al. (2019) · Science · doi:10.1126/science.aav2606 · Cited by 202 · see citing works

Nuclear import impairment causes cytoplasmic trans-activation response DNA-binding protein accumulation and is associated with frontotemporal lobar degeneration

Nishimura, A. L., Župunski, V., Troakes, C., Kathe, C., Fratta, P., Howell, M. T., Gallo, J., Hortobágyi, T., Shaw, C. E., & Rogelj, B. (2010) · Brain · doi:10.1093/brain/awq111 · Cited by 198 · see citing works

The dual functions of the extreme N-terminus of TDP-43 in regulating its biological activity and inclusion formation

Zhang, Y., Caulfield, T. R., Xu, Y., Gendron, T. F., Hubbard, J., Stetler, C. T., Sasaguri, H., Whitelaw, E. C., Cai, S., Lee, C. W., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt166 · Cited by 185 · see citing works

Sense-encoded poly-GR dipeptide repeat proteins correlate to neurodegeneration and uniquely co-localize with TDP-43 in dendrites of repeat-expanded C9orf72 amyotrophic lateral sclerosis

Saberi, S., Stauffer, J. E., Jiang, J., Díaz-García, S., Taylor, A. E., Schulte, D. J., Ohkubo, T., Schloffman, C. L., Maldonado, M., Baughn, M. W., et al. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1793-8 · Cited by 178 · see citing works

Aberrant deposition of stress granule-resident proteins linked to C9orf72-associated TDP-43 proteinopathy

Chew, J., Cook, C. N., Gendron, T. F., Jansen‐West, K. R., del Rosso, G., Daughrity, L. M., Castanedes‐Casey, M., Kurti, A., Stankowski, J. N., Disney, M. D., et al. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0310-z · Cited by 158 · see citing works

C9orf72 arginine-rich dipeptide repeat proteins disrupt karyopherin-mediated nuclear import

Hayes, L. R., Duan, L., Bowen, K., Kaláb, P., & Rothstein, J. D. (2020) · eLife · doi:10.7554/elife.51685 · Cited by 133 · see citing works

Cerebellar c9RAN proteins associate with clinical and neuropathological characteristics of C9ORF72 repeat expansion carriers

Gendron, T. F., van Blitterswijk, M., Bieniek, K. F., Daughrity, L. M., Jiang, J., Rush, B. K., Pedraza, O., Lucas, J. A., Murray, M. E., Desaro, P., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1474-4 · Cited by 106 · see citing works

Poly-GR dipeptide repeat polymers correlate with neurodegeneration and Clinicopathological subtypes in C9ORF72-related brain disease

Sakae, N., Bieniek, K. F., Zhang, Y., Ross, K., Gendron, T. F., Murray, M. E., Rademakers, R., Petrucelli, L., & Dickson, D. W. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0564-7 · Cited by 103 · see citing works

Misregulation of human sortilin splicing leads to the generation of a nonfunctional progranulin receptor

Prudencio, M., Jansen‐West, K. R., Lee, C. W., Gendron, T. F., Zhang, Y., Xu, Y.-F., Gass, J. M., Stuani, C., Stetler, C. T., Rademakers, R., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1211577110 · Cited by 95 · see citing works

Dipeptide repeat protein inclusions are rare in the spinal cord and almost absent from motor neurons in C9ORF72 mutant amyotrophic lateral sclerosis and are unlikely to cause their degeneration

Gomez-Deza, J., Lee, Y.-B., Troakes, C., Nolan, M., Al-Sarraj, S., Gallo, J.-M., & Shaw, C. E. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0218-y · Cited by 93 · see citing works

Poly(GP), neurofilament and grey matter deficits in <i>C9orf72</i> expansion carriers

Meeter, L. H. H., Gendron, T. F., Sias, A. C., Jiskoot, L. C., Russo, S. P., Donker Kaat, L., Papma, J. M., Panman, J. L., van der Ende, E. L., Dopper, E. G., et al. (2018) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.559 · Cited by 61 · see citing works

Amyotrophic lateral sclerosis

Feldman, E. L., Goutman, S. A., Petri, S., Mazzini, L., Savelieff, M. G., Shaw, P. J., & Sobue, G. (2022) · The Lancet · doi:10.1016/s0140-6736(22)01272-7 · Cited by 1,179 · see citing works

Emerging insights into the complex genetics and pathophysiology of amyotrophic lateral sclerosis

Goutman, S. A., Hardiman, O. M., Al‐Chalabi, A., Chiò, A., Savelieff, M. G., Kiernan, M. C., & Feldman, E. L. (2022) · The Lancet Neurology · doi:10.1016/s1474-4422(21)00414-2 · Cited by 413 · see citing works

Suppression of mutant C9orf72 expression by a potent mixed backbone antisense oligonucleotide

Tran, H., Moazami, M. P., Yang, H., McKenna-Yasek, D., Douthwright, C. L., Pinto, C., Metterville, J., Shin, M., Sanil, N., Dooley, C., et al. (2022) · Nature Medicine · doi:10.1038/s41591-021-01557-6 · Cited by 174 · see citing works

Intra-condensate demixing of TDP-43 inside stress granules generates pathological aggregates

Yan, X., Kuster, D., Mohanty, P., Nijssen, J., García, K. P., Morato, J. G., Rizuan, A., Franzmann, T. M., Sergeeva, A. V., Ly, A. M., et al. (2025) · Cell · doi:10.1016/j.cell.2025.04.039 · Cited by 172 · see citing works

Higher-order organization of biomolecular condensates

Fare, C. M., Villani, A., Drake, L. E., & Shorter, J. (2021) · Open Biology · doi:10.1098/rsob.210137 · Cited by 170 · see citing works

Axonal TDP-43 condensates drive neuromuscular junction disruption through inhibition of local synthesis of nuclear encoded mitochondrial proteins

Altman, T., Ionescu, A., Ibraheem, A., Priesmann, D., Gradus, T., Farberov, L., Alexandra, G., Shelestovich, N., Dafinca, R., Shomron, N., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-27221-8 · Cited by 140 · see citing works

Mitochondrial bioenergetic deficits in C9orf72 amyotrophic lateral sclerosis motor neurons cause dysfunctional axonal homeostasis

Mehta, A. R., Gregory, J. M., Dando, O., Carter, R. N., Burr, K., Nanda, J., Story, D., McDade, K., Smith, C., Morton, N. M., et al. (2021) · Acta Neuropathologica · doi:10.1007/s00401-020-02252-5 · Cited by 122 · see citing works

A New Phase of Networking: The Molecular Composition and Regulatory Dynamics of Mammalian Stress Granules

Millar, S. R., Huang, J. Q., Schreiber, K. J., Tsai, Y.-C., Won, J., Zhang, J., Moses, A. M., & Youn, J. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.2c00608 · Cited by 120 · see citing works

Nuclear Import Receptors Directly Bind to Arginine-Rich Dipeptide Repeat Proteins and Suppress Their Pathological Interactions

Hutten, S., Usluer, S., Bourgeois, B. M. R., Simonetti, F., Odeh, H. M., Fare, C. M., Czuppa, M., Hruška-Plocháň, M., Hofweber, M., Polymenidou, M., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108538 · Cited by 107 · see citing works

Nuclear pore complexes — a doorway to neural injury in neurodegeneration

Coyne, A. N., & Rothstein, J. D. (2022) · Nature Reviews Neurology · doi:10.1038/s41582-022-00653-6 · Cited by 96 · see citing works

Biological importance of arginine: A comprehensive review of the roles in structure, disorder, and functionality of peptides and proteins

Gupta, M. N., & Uversky, V. N. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.128646 · Cited by 92 · see citing works

C9orf72 -derived arginine-containing dipeptide repeats associate with axonal transport machinery and impede microtubule-based motility

Fumagalli, L., Young, F. L., Boeynaems, S., Decker, M. D., Mehta, A. R., Swijsen, A., Fazal, R., Guo, W., Moisse, M., Beckers, J., et al. (2021) · Science Advances · doi:10.1126/sciadv.abg3013 · Cited by 89 · see citing works

Cellular and physiological functions of C9ORF72 and implications for ALS/FTD

Pang, W., & Hu, F. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15255 · Cited by 87 · see citing works

Combating deleterious phase transitions in neurodegenerative disease

Darling, A. L., & Shorter, J. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.118984 · Cited by 85 · see citing works

Friend or foe: The role of stress granule in neurodegenerative disease

Cui, Q., Liu, Z., & Bai, G. (2024) · Neuron · doi:10.1016/j.neuron.2024.04.025 · Cited by 82 · see citing works

Two FTD-ALS genes converge on the endosomal pathway to induce TDP-43 pathology and degeneration

Shao, W., Todd, T. W., Wu, Y., Jones, C. Y., Tong, J., Jansen‐West, K. R., Daughrity, L. M., Park, J., Koike, Y. M., Kurti, A., et al. (2022) · Science · doi:10.1126/science.abq7860 · Cited by 79 · see citing works

TDP-43 pathology: From noxious assembly to therapeutic removal

Keating, S. S., Gil, R. S., Swanson, M. E. V., Scotter, E. L., & Walker, A. K. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2022.102229 · Cited by 74 · see citing works

The role of inflammation in neurodegeneration: novel insights into the role of the immune system in C9orf72 HRE-mediated ALS/FTD

Masrori, P., Beckers, J., Gossye, H., & Damme, P. V. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00525-z · Cited by 72 · see citing works

TDP-43 and Inflammation: Implications for Amyotrophic Lateral Sclerosis and Frontotemporal Dementia

Bright, F., Chan, G., van Hummel, A., Ittner, L. M., & Ke, Y. D. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22157781 · Cited by 71 · see citing works

NUP62 localizes to ALS/FTLD pathological assemblies and contributes to TDP-43 insolubility

Gleixner, A. M., Verdone, B. M., Otte, C. G., Anderson, E. N., Ramesh, N., Shapiro, O. R., Gale, J. R., Mauna, J. C., Mann, J. R., Copley, K. E., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31098-6 · Cited by 68 · see citing works

Emerging Perspectives on Dipeptide Repeat Proteins in C9ORF72 ALS/FTD

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Connecting TDP-43 Pathology with Neuropathy

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