Mechanisms of protein toxicity in neurodegenerative diseases
Open accessAbstract
Protein toxicity can be defined as all the pathological changes that ensue from accumulation, mis-localization, and/or multimerization of disease-specific proteins. Most neurodegenerative diseases manifest protein toxicity as one of their key pathogenic mechanisms, the details of which remain unclear. By systematically deconstructing the nature of toxic proteins, we aim to elucidate and illuminate some of the key mechanisms of protein toxicity from which therapeutic insights may be drawn. In this review, we focus specifically on protein toxicity from the point of view of various cellular compartments such as the nucleus and the mitochondria. We also discuss the cell-to-cell propagation of toxic disease proteins that complicates the mechanistic understanding of the disease progression as well as the spatiotemporal point at which to therapeutically intervene. Finally, we discuss selective neuronal vulnerability, which still remains largely enigmatic.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
The buildup of neurotoxic agents causes neuronal damage and death, which can lead to neurological dysfunction including cognitive decline, motor abnormalities, mental disorders, and loss of inhibition.
“The buildup of neurotoxic agents is believed to cause neuronal damage and death, which can ultimately lead to various forms of neurological dysfunction that include cognitive decline, motor abnormalities, mental disorders, and loss of inhibition (Chung et al., 2018; Taylor et al., 2002; Vickers et al., 2009).”
From SYK coordinates neuroprotective microglial responses in neurodegenerative disease (2022) · cites this paper as Chung et al., 2018
The Introduction describes toxic protein accumulation as contributing to neurodegenerative disease and identifies memory impairment, motor problems, neuronal dysfunction, and eventual cell death. The Discussion and future perspectives section also notes psychiatric symptoms, but says their molecular link to neurodegeneration remains undefined. The paper does not substantiate loss of inhibition, and its account concerns toxic proteins rather than neurotoxic agents generally. (LLM, conf=0.85)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351 · see citing works
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · see citing works
Valadi, H., Ekström, K., Bossios, A., Sjöstrand, M., Lee, J. J., & Lötvall, J. O. (2007) · Nature Cell Biology · doi:10.1038/ncb1596 · Cited by 12,834 · see citing works
Staging of brain pathology related to sporadic Parkinson’s disease
Braak, H., Tredici, K. D., Rüb, U., de Vos, R. A. I., Jansen Steur, E. N. H., & Braak, E. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00065-9 · Cited by 10,777 · see citing works
Jaenisch, R., & Bird, A. (2003) · Nature Genetics · doi:10.1038/ng1089 · Cited by 6,325 · see citing works
Cui, C., Cui, J., Jin, F., Cui, Y., Li, R., Jiang, X., Tian, Y., Wang, R. C., Jiang, P., & Gao, J. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479571 · Cited by 5,214 · see citing works
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064 · see citing works
Liquid-Liquid Phase Separation in Biology
Hyman, A. A., Weber, C. A., & Jülicher, F. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100913-013325 · Cited by 3,155 · see citing works
The antibody aducanumab reduces Aβ plaques in Alzheimer’s disease
Sevigny, J., Chiao, P., Bussière, T., Weinreb, P. H., Williams, L., Maier, M., Dunstan, R., Salloway, S., Chen, T., Ling, Y., et al. (2016) · Nature · doi:10.1038/nature19323 · Cited by 3,059 · see citing works
Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · Science · doi:10.1126/science.1227157 · Cited by 2,563 · see citing works
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434 · see citing works
The role of autophagy in neurodegenerative disease
Nixon, R. A. (2013) · Nature Medicine · doi:10.1038/nm.3232 · Cited by 2,059 · see citing works
Decoding ALS: from genes to mechanism
Taylor, J. P., Brown, R. H., & Cleveland, D. W. (2016) · Nature · doi:10.1038/nature20413 · Cited by 2,047 · see citing works
Impaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy
Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T., & Sulzer, D. (2004) · Science · doi:10.1126/science.1101738 · Cited by 2,024 · see citing works
Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
Arrasate, M., Mitra, S., Schweitzer, E. S., Segal, M. R., & Finkbeiner, S. (2004) · Nature · doi:10.1038/nature02998 · Cited by 1,979 · see citing works
Li, J.-Y., Englund, E., Holton, J. L., Soulet, D., Hagell, P., Lees, A. J., Lashley, T., Quinn, N. P., Rehncrona, S., Björklund, A., et al. (2008) · Nature Medicine · doi:10.1038/nm1746 · Cited by 1,845 · see citing works
5′ UTR m6A Promotes Cap-Independent Translation
Meyer, K. D., Patil, D. P., Zhou, J. L., Zinoviev, A., Skabkin, M. A., Elemento, O., Pestova, T. V., Qian, S., & Jaffrey, S. R. (2015) · Cell · doi:10.1016/j.cell.2015.10.012 · Cited by 1,812 · see citing works
Transmission and spreading of tauopathy in transgenic mouse brain
Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1901 · Cited by 1,803 · see citing works
Alzheimer’s disease drug-development pipeline: Few candidates, frequent failures
Cummings, J. L., Morstorf, T., & Zhong, K. (2014) · Alzheimer's Research & Therapy · doi:10.1186/alzrt269 · Cited by 1,744 · see citing works
Principles and Properties of Stress Granules
Protter, D. S. W., & Parker, R. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.05.004 · Cited by 1,738 · see citing works
Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
Jucker, M., & Walker, L. C. (2013) · Nature · doi:10.1038/nature12481 · Cited by 1,663 · see citing works
Depletion of microglia and inhibition of exosome synthesis halt tau propagation
Asai, H., Ikezu, S., Tsunoda, S., Medalla, M., Luebke, J., Haydar, T., Wolozin, B., Butovsky, O., Kügler, S., & Ikezu, T. (2015) · Nature Neuroscience · doi:10.1038/nn.4132 · Cited by 1,591 · see citing works
Stabilization of α-Synuclein Secondary Structure upon Binding to Synthetic Membranes
Davidson, W. S., Jonas, A., Clayton, D. F., & George, J. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.9443 · Cited by 1,588 · see citing works
Inclusion formation and neuronal cell death through neuron-to-neuron transmission of α-synuclein
Desplats, P., Lee, H.-J., Bae, E.-J., Patrick, C., Rockenstein, E., Crews, L., Spencer, B., Masliah, E., & Lee, S.-J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903691106 · Cited by 1,485 · see citing works
Self-citationMutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS
Kim, H. J., Kim, N. C., Wang, Y., Scarborough, E. A., Moore, J., Diaz, Z., MacLea, K. S., Freibaum, B. D., Li, S., Molliex, A., et al. (2013) · Nature · doi:10.1038/nature11922 · Cited by 1,476 · see citing works
Genetics of Parkinson's DiseasePreprint
Klein, C., & Westenberger, A. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a008888 · Cited by 1,370 · see citing works
Alzheimer’s disease β-amyloid peptides are released in association with exosomes
Rajendran, L., Honsho, M., Zahn, T. R., Keller, P., Geiger, K. D., Verkade, P., & Simons, K. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603838103 · Cited by 1,343 · see citing works
ABAD Directly Links Aß to Mitochondrial Toxicity in Alzheimer's Disease
Lustbader, J. W., Cirilli, M., Lin, C., Xu, H. W., Takuma, K., Wang, N., Caspersen, C., Chen, X., Pollak, S., Chaney, M., et al. (2004) · Science · doi:10.1126/science.1091230 · Cited by 1,303 · see citing works
Toxic Proteins in Neurodegenerative Disease
Taylor, J. P., Hardy, J., & Fischbeck, K. H. (2002) · Science · doi:10.1126/science.1067122 · Cited by 1,251 · 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
Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in Drosophila
Steffan, J. S., Bodai, L., Pallos, J., Poelman, M., McCampbell, A., Apostol, B. L., Kazantsev, A., Schmidt, E., Zhu, Y.-Z., Greenwald, M., et al. (2001) · Nature · doi:10.1038/35099568 · Cited by 1,228 · see citing works
Gauthier, L. R., Charrin, B. C., Borrell-Pagès, M., Dompierre, J. P., Rangone, H., Cordelières, F. P., De Mey, J., MacDonald, M. E., Leßmann, V., Humbert, S., et al. (2004) · Cell · doi:10.1016/j.cell.2004.06.018 · Cited by 1,178 · see citing works
α-Synuclein strains cause distinct synucleinopathies after local and systemic administration
Peelaerts, W., Bousset, L., Van der Perren, A., Moskalyuk, A., Pulizzi, R., Giugliano, M., Van den Haute, C., Melki, R., & Baekelandt, V. (2015) · Nature · doi:10.1038/nature14547 · Cited by 1,130 · see citing works
Selective neuronal vulnerability in Parkinson disease
Surmeier, D. J., Obeso, J. A., & Halliday, G. M. (2017) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.178 · Cited by 1,120 · see citing works
Emmanouilidou, E., Melachroinou, K., Roumeliotis, T., Garbis, S. D., Ntzouni, M., Margaritis, L. H., Stefanis, L., & Vekrellis, K. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.5699-09.2010 · Cited by 1,115 · see citing works
Nucifora, F. C., Sasaki, M., Peters, M. F., Huang, H., Cooper, J. K., Yamada, M., Takahashi, H., Tsuji, S., Troncoso, J. C., Dawson, V. L., et al. (2001) · Science · doi:10.1126/science.1056784 · Cited by 1,095 · see citing works
Luk, K. C., Kehm, V. M., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M. ‐. (2012) · The Journal of Experimental Medicine · doi:10.1084/jem.20112457 · Cited by 1,087 · see citing works
Steffan, J. S., Kazantsev, A. G., Spasić-Bošković, O., Greenwald, M., Zhu, Y., Goehler, H., Wanker, E. E., Bates, G. P., Housman, D. E., & Thompson, L. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.100110097 · Cited by 1,057 · see citing works
Trial of Solanezumab for Mild Dementia Due to Alzheimer’s Disease
Honig, L. S., Vellas, B., Woodward, M., Boada, M., Bullock, R., Borrie, M., Hager, K., Andreasen, N., Scarpini, E., Liu-Seifert, H., et al. (2018) · New England Journal of Medicine · doi:10.1056/nejmoa1705971 · Cited by 1,049 · see citing works
Early mitochondrial calcium defects in Huntington's disease are a direct effect of polyglutamines
Panov, A. V., Gutekunst, C.-A., Leavitt, B. R., Hayden, M. R., Burke, J. R., Strittmatter, W. J., & Greenamyre, J. T. (2002) · Nature Neuroscience · doi:10.1038/nn884 · Cited by 1,030 · see citing works
Review Article: Genetics of Alzheimer Disease
Bekris, L. M., Yu, C.-E., Bird, T. D., & Tsuang, D. W. (2010) · Journal of Geriatric Psychiatry and Neurology · doi:10.1177/0891988710383571 · Cited by 1,029 · see citing works
Blalock, E. M., Geddes, J. W., Chen, K. C., Porter, N. M., Markesbery, W. R., & Landfield, P. W. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308512100 · Cited by 1,025 · see citing works
Cui, L., Jeong, H., Borovecki, F., Parkhurst, C. N., Tanese, N., & Krainc, D. (2006) · Cell · doi:10.1016/j.cell.2006.09.015 · Cited by 1,012 · see citing works
Trans-Synaptic Spread of Tau Pathology In Vivo
Liu, L., Drouet, V., Wu, J., Witter, M. P., Small, S. A., Clelland, C. L. T., & Duff, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031302 · Cited by 994 · see citing works
Saman, S., Kim, W., Raya, M., Visnick, Y., Miro, S., Saman, S., Jackson, B., McKee, A. C., Alvarez, V. E., Lee, N. C. Y., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.277061 · Cited by 985 · 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
Goedert, M. (2015) · Science · doi:10.1126/science.1255555 · Cited by 977 · 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
Du, H., Guo, L., Fang, F., Chen, D., Sosunov, A. A., McKhann, G. M., Yan, Y., Wang, C., Zhang, H., Molkentin, J. D., et al. (2008) · Nature Medicine · doi:10.1038/nm.1868 · Cited by 935 · see citing works
Direct evidence of Parkinson pathology spread from the gastrointestinal tract to the brain in rats
Holmqvist, S., Chutna, O., Bousset, L., Aldrin-Kirk, P., Li, W., Björklund, T., Wang, Z.-Y., Roybon, L., Melki, R., & Li, J.-Y. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1343-6 · Cited by 925 · see citing works
Degradation of misfolded proteins in neurodegenerative diseases: Therapeutic targets and strategies
Ciechanover, A., & Kwon, Y. T. (2015) · Experimental & Molecular Medicine · doi:10.1038/emm.2014.117 · Cited by 898 · see citing works
Browne, S. E., Bowling, A. C., Macgarvey, U., Baik, M. J., Berger, S. C., Muquit, M. M. K., Bird, E. D., & Beal, M. F. (1997) · Annals of Neurology · doi:10.1002/ana.410410514 · Cited by 885 · see citing works
Cargo recognition failure is responsible for inefficient autophagy in Huntington’s disease
Martinez-Vicente, M., Talloczy, Z., Wong, E., Tang, G., Koga, H., Kaushik, S., de Vries, R., Arias, E., Harris, S., Sulzer, D., et al. (2010) · Nature Neuroscience · doi:10.1038/nn.2528 · Cited by 885 · see citing works
Prion-like spreading of pathological α-synuclein in brain
Masuda-Suzukake, M., Nonaka, T., Hosokawa, M., Oikawa, T., Arai, T., Akiyama, H., Mann, D. M. A., & Hasegawa, M. (2013) · Brain · doi:10.1093/brain/awt037 · Cited by 867 · see citing works
Mitochondria and Mitochondrial Cascades in Alzheimer’s disease
Swerdlow, R. H. (2018) · Journal of Alzheimer’s Disease · doi:10.3233/jad-170585 · Cited by 850 · see citing works
Hockly, E., Richon, V. M., Woodman, B., Smith, D. L., Zhou, X., Rosa, E., Sathasivam, K., Ghazi‐Noori, S., Mahal, A., Lowden, P. A. S., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0437870100 · Cited by 847 · see citing works
Hansen, C., Angot, E., Bergström, A.-L., Steiner, J. A., Pieri, L., Paul, G., Outeiro, T. F., Melki, R., Kallunki, P., Fog, K., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci43366 · Cited by 842 · 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
Huntingtin interacts with REST/NRSF to modulate the transcription of NRSE-controlled neuronal genes
Zuccato, C., Tartari, M., Crotti, A., Goffredo, D., Valenza, M., Conti, L., Cataudella, T., Leavitt, B. R., Hayden, M. R., Timmusk, T., et al. (2003) · Nature Genetics · doi:10.1038/ng1219 · Cited by 814 · see citing works
Role of Stress Granules and RNA-Binding Proteins in Neurodegeneration: A Mini-Review
Vanderweyde, T. E., Youmans, K., Liu‐Yesucevitz, L., & Wolozin, B. L. (2013) · Gerontology · doi:10.1159/000354170 · Cited by 806 · see citing works
Intravesicular Localization and Exocytosis of α-Synuclein and its Aggregates
Lee, H.-J., Patel, S. S., & Lee, S. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0692-05.2005 · Cited by 798 · see citing works
Self-citationDevi, L., Prabhu, B. M., Galati, D. F., Avadhani, N. G., & Anandatheerthavarada, H. K. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1469-06.2006 · Cited by 792 · see citing works
The Stress Granule Transcriptome Reveals Principles of mRNA Accumulation in Stress Granules
Khong, A., Matheny, T., Jain, S., Mitchell, S. F., Wheeler, J., & Parker, R. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.10.015 · Cited by 760 · see citing works
Next generation antibody drugs: pursuit of the 'high-hanging fruit'
Carter, P. J., & Lazar, G. A. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.227 · Cited by 760 · see citing works
Eukaryotic Stress Granules Are Cleared by Autophagy and Cdc48/VCP Function
Buchan, J. R., Kolaitis, R.-M., Taylor, J. P., & Parker, R. (2013) · Cell · doi:10.1016/j.cell.2013.05.037 · Cited by 737 · see citing works
Ferrante, R. J., Kubilus, J. K., Lee, J.-H., Ryu, H., Beesen, A. A., Zucker, B., Smith, K., Kowall, N. W., Ratan, R. R., Luthi‐Carter, R., et al. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-28-09418.2003 · Cited by 694 · see citing works
Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS
Bosco, D. A., Morfini, G. A., Karabacak, M., Song, Y., Gros‐Louis, F., Pasinelli, P., Goolsby, H., Fontaine, B. A., Lemay, N., McKenna-Yasek, D. M., et al. (2010) · Nature Neuroscience · doi:10.1038/nn.2660 · Cited by 685 · see citing works
G3BP–Caprin1–USP10 complexes mediate stress granule condensation and associate with 40S subunits
Kedersha, N., Panas, M. D., Achorn, C. A., Lyons, S. M., Tisdale, S., Hickman, T. T., Thomas, M., Lieberman, J., McInerney, G. M., Ivanov, P. V., et al. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201508028 · Cited by 663 · see citing works
Identification of Genetic Factors that Modify Clinical Onset of Huntington’s Disease
Lee, J.-M., Wheeler, V. C., Chao, M. J., Vonsattel, J. P. G., Pinto, R. M., Lucente, D., Abu-Elneel, K., Ramos, E. M., Mysore, J. S., Gillis, T., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.003 · Cited by 655 · see citing works
Gunawardena, S., Her, L.-S., Brusch, R. G., Laymon, R. A., Niesman, I. R., Gordesky-Gold, B., Sintasath, L., Bonini, N. M., & Goldstein, L. S. B. (2003) · Neuron · doi:10.1016/s0896-6273(03)00594-4 · Cited by 648 · see citing works
Mackenzie, I. R., Nicholson, A. M., Sarkar, M., Messing, J. A., Purice, M. D., Pottier, C. P., Annu, K., Baker, M. C., Perkerson, R. B., Kurti, A., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.07.025 · Cited by 642 · see citing works
Williamson, T. L., & Cleveland, D. W. (1999) · Nature Neuroscience · doi:10.1038/4553 · Cited by 638 · see citing works
Waelter, S., Boeddrich, A., Lurz, R., Scherzinger, E., Lüder, G., Lehrach, H. R., & Wanker, E. E. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.5.1393 · Cited by 632 · see citing works
Enhancing mitochondrial proteostasis reduces amyloid-β proteotoxicity
Sorrentino, V., Romani, M., Mouchiroud, L., Beck, J. S., Zhang, H., D’Amico, D., Moullan, N., Potenza, F., Schmid, A. W., Rietsch, S., et al. (2017) · Nature · doi:10.1038/nature25143 · Cited by 630 · see citing works
α-Synuclein binds to TOM20 and inhibits mitochondrial protein import in Parkinson’s disease
Di Maio, R., Barrett, P. J., Hoffman, E. K., Barrett, C. W., Zharikov, A., Borah, A., Hu, X., McCoy, J., Chu, C. T., Burton, E. A., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf3634 · Cited by 619 · see citing works
Dual Specificity Kinase DYRK3 Couples Stress Granule Condensation/Dissolution to mTORC1 Signaling
Wippich, F., Bodenmiller, B., Trajkovska, M., Wanka, S., Aebersold, R. H., & Pelkmans, L. (2013) · Cell · doi:10.1016/j.cell.2013.01.033 · Cited by 597 · see citing works
Interplay of LRRK2 with chaperone-mediated autophagy
Orenstein, S. J., Kuo, S.-H., Tasset, I., Arias, E., Koga, H., Fernandez-Carasa, I., Cortes, E., Honig, L. S., Dauer, W., Consiglio, A., et al. (2013) · Nature Neuroscience · doi:10.1038/nn.3350 · Cited by 588 · see citing works
Anandatheerthavarada, H. K., Biswas, G., Robin, M.-A., & Avadhani, N. G. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200207030 · Cited by 571 · see citing works
Peripherally Applied Aβ-Containing Inoculates Induce Cerebral β-Amyloidosis
Eisele, Y. S., Obermüller, U., Heilbronner, G., Baumann, F., Kaeser, S. A., Wolburg, H., Walker, L. C., Staufenbiel, M., Heikenwalder, M., & Jucker, M. (2010) · Science · doi:10.1126/science.1194516 · Cited by 568 · see citing works
Saxena, S., & Caroni, P. (2011) · Neuron · doi:10.1016/j.neuron.2011.06.031 · Cited by 561 · see citing works
CREB-binding protein sequestration by expanded polyglutamine
McCampbell, A. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.14.2197 · Cited by 547 · see citing works
Choo, Y. S. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh162 · Cited by 515 · see citing works
Dinkins, M. B., Dasgupta, S., Wang, G., Zhu, G., & Bieberich, E. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.02.012 · Cited by 494 · see citing works
Human endogenous retrovirus-K contributes to motor neuron disease
Li, W., Lee, M.-H., Henderson, L., Tyagi, R., Bachani, M., Steiner, J., Campanac, E., Hoffman, D. A., von Geldern, G., Johnson, K., et al. (2015) · Science Translational Medicine · doi:10.1126/scitranslmed.aac8201 · Cited by 482 · see citing works
Matějů, D., Franzmann, T. M., Patel, A., Kopach, A., Boczek, E. E., Maharana, S., Lee, H. O., Carra, S., Hyman, A. A., & Alberti, S. (2017) · The EMBO Journal · doi:10.15252/embj.201695957 · Cited by 480 · see citing works
Self-citationCytosolic proteostasis through importing of misfolded proteins into mitochondria
Ruan, L., Zhou, C., Jin, E., Kucharavy, A., Zhang, Y., Wen, Z., Florens, L. A., & Li, R. (2017) · Nature · doi:10.1038/nature21695 · Cited by 474 · see citing works
Axonal Transport Defects in Neurodegenerative Diseases
Morfini, G. A., Burns, M. R., Binder, L. I., Kanaan, N. M., LaPointe, N. E., Bosco, D. A., Brown, R. H., Brown, H. E., Tiwari, A., Hayward, L. J., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.3463-09.2009 · Cited by 464 · see citing works
The inhibition of TDP-43 mitochondrial localization blocks its neuronal toxicity
Wang, W., Wang, L., Lu, J., Siedlak, S. L., Fujioka, H., Liang, J., Jiang, S., Ma, X., Jiang, Z., da Rocha, E. L., et al. (2016) · Nature Medicine · doi:10.1038/nm.4130 · Cited by 462 · see citing works
Tai, H., Serrano‐Pozo, A., Hashimoto, T., Frosch, M. P., Spires‐Jones, T. L., & Hyman, B. T. (2012) · American Journal Of Pathology · doi:10.1016/j.ajpath.2012.06.033 · Cited by 456 · see citing works
Gárdián, G., Browne, S. E., Choi, D., Klivènyi, P., Gregorio, J., Kubilus, J. K., Ryu, H., Langley, B. C., Ratan, R. R., Ferrante, R. J., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410210200 · Cited by 456 · see citing works
Mendez, I. M., Viñuela, Á., Astradsson, A., Mukhida, K., Hallett, P. J., Robertson, H. A., Tierney, T. S., Holness, R. O., Dagher, A., Trojanowski, J. Q., et al. (2008) · Nature Medicine · doi:10.1038/nm1752 · Cited by 442 · see citing works
Axonal transport and neurodegenerative disease
Chevalier-Larsen, E. S., & Holzbaur, E. L. F. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.04.002 · Cited by 438 · see citing works
N-Terminal Mutant Huntingtin Associates with Mitochondria and Impairs Mitochondrial Trafficking
Orr, A. L., Li, S., Wang, C.-E., Li, H., Wang, J., Rong, J., Xu, X., Mastroberardino, P. G., Greenamyre, J. T., & Li, X. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0106-08.2008 · Cited by 429 · see citing works
Stuendl, A., Kunadt, M., Kruse, N., Bartels, C., Moebius, W., Danzer, K. M., Mollenhauer, B., & Schneider, A. (2016) · Brain · doi:10.1093/brain/awv346 · Cited by 428 · see citing works
Deficits in axonal transport precede ALS symptoms in vivo
Bilsland, L. G., Sahai, E. A., Kelly, G. P., Golding, M., Greensmith, L., & Schiavo, G. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1006869107 · Cited by 418 · see citing works
Molecular Mechanisms of Amyloid Oligomers Toxicity
Kayed, R., & Lasagna‐Reeves, C. A. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129001 · Cited by 417 · see citing works
Tunneling nanotubes spread fibrillar α-synuclein by intercellular trafficking of lysosomes
Abounit, S., Bousset, L., Loria, F., Zhu, S., de Chaumont, F., Pieri, L., Olivo‐Marin, J., Melki, R., & Zurzolo, C. (2016) · The EMBO Journal · doi:10.15252/embj.201593411 · Cited by 414 · see citing works
Lopez-Gonzalez, R., Lu, Y., Gendron, T. F., Karydas, A., Tran, H., Yang, D., Petrucelli, L., Miller, B. L., Almeida, S., & Gao, F. (2016) · Neuron · doi:10.1016/j.neuron.2016.09.015 · Cited by 410 · see citing works
Gould, T. W., Buss, R. R., Vinsant, S. L., Prevette, D. M., Sun, W., Knudson, C. M., Milligan, C., & Oppenheim, R. W. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.2315-06.2006 · Cited by 397 · see citing works
McDonald, K. K., Aulas, A., Destroismaisons, L., Pickles, S. R., Beleac, E., Camu, W., Rouleau, G. A., & Velde, C. V. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr021 · Cited by 394 · see citing works
Kane, M. D., Lipinski, W. J., Callahan, M. J., Bian, F., Durham, R. A., Schwarz, R. D., Roher, A. E., & Walker, L. C. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-10-03606.2000 · Cited by 394 · see citing works
Rey, N. L., Steiner, J. A., Maroof, N., Luk, K. C., Madaj, Z., Trojanowski, J. Q., Lee, V. M. ‐., & Brundin, P. (2016) · The Journal of Experimental Medicine · doi:10.1084/jem.20160368 · Cited by 389 · see citing works
Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA
Woerner, A. C., Frottin, F., Hornburg, D., Feng, L., Meissner, F., Patra, M., Tatzelt, J., Mann, M., Winklhofer, K. F., Hartl, F. U., et al. (2015) · Science · doi:10.1126/science.aad2033 · Cited by 386 · see citing works
Polyglutamine spinocerebellar ataxias — from genes to potential treatments
Paulson, H. L., Shakkottai, V. G., Clark, H. B., & Orr, H. T. (2017) · Nature reviews. Neuroscience · doi:10.1038/nrn.2017.92 · Cited by 376 · see citing works
Axonal transport defects: a common theme in neurodegenerative diseases
Roy, S., Zhang, B., Lee, V. M. ‐., & Trojanowski, J. Q. (2005) · Acta Neuropathologica · doi:10.1007/s00401-004-0952-x · Cited by 372 · see citing works
Braak, H., & Del Tredici, K. (2017) · Journal of Parkinson’s Disease · doi:10.3233/jpd-179001 · Cited by 372 · see citing works
Grünblatt, E., Mandel, S. A., Jacob‐Hirsch, J., Zeligson, S., Amariglo, N., Rechavi, G., Li, J., Ravid, R., Roggendorf, W., Riederer, P. F., et al. (2004) · Journal of Neural Transmission · doi:10.1007/s00702-004-0212-1 · Cited by 358 · see citing works
Mutant Huntingtin Disrupts the Nuclear Pore Complex
Grima, J. C., Daigle, J. G., Arbez, N., Cunningham, K. M., Zhang, K., Ochaba, J., Smith-Geater, C., Morozko, E. L., Stocksdale, J. T., Glatzer, J. C., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.03.023 · Cited by 358 · see citing works
Choosing an animal model for the study of Huntington's disease
Pouladi, M. A., Morton, A. J., & Hayden, M. R. (2013) · Nature reviews. Neuroscience · doi:10.1038/nrn3570 · Cited by 350 · see citing works
Dantuma, N. P., & Bott, L. C. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00070 · Cited by 336 · see citing works
Huynh, D. P., Figueroa, K. P., Hoang, N., & Pulst, S.-M. (2000) · Nature Genetics · doi:10.1038/79162 · Cited by 330 · see citing works
Sacino, A. N., Brooks, M., Thomas, M. A., McKinney, A. B., Lee, S., Regenhardt, R. W., McGarvey, N. H., Ayers, J. I., Notterpek, L. M., Borchelt, D., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321785111 · Cited by 328 · see citing works
Self-citationNeuropathogenic Forms of Huntingtin and Androgen Receptor Inhibit Fast Axonal Transport
Szebenyi, G., Morfini, G. A., Babcock, A., Gould, M., Selkoe, K. A., Stenoien, D. L., Young, M., Faber, P. W., MacDonald, M. E., McPhaul, M. J., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00569-5 · Cited by 326 · see citing works
Flagmeier, P., Meisl, G., Vendruscolo, M., Knowles, T. P. J., Dobson, C. M., Buell, A. K., & Galvagnion, C. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1604645113 · Cited by 323 · see citing works
Harris, J. A., Devidze, N., Verret, L., Ho, K., Halabisky, B., Thwin, M. T., Kim, D., Hamto, P., Lo, I., Yu, G.-Q., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.10.020 · Cited by 319 · see citing works
Boutell, J. M., Thomas, P., Neal, J. W., Weston, V. J., Duce, J., Harper, P. S., & Lesley Jones, A. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.9.1647 · Cited by 310 · see citing works
Impaired ERAD and ER stress are early and specific events in polyglutamine toxicityPreprint
Duennwald, M. L., & Lindquist, S. L. (2008) · Genes & Development · doi:10.1101/gad.1673408 · Cited by 296 · see citing works
Cytoplasmic stress granules: Dynamic modulators of cell signaling and disease
Mahboubi, H., & Stochaj, U. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.12.022 · Cited by 288 · see citing works
Polyglutamine diseases: emerging concepts in pathogenesis and therapy
Shao, J., & Diamond, M. I. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm213 · Cited by 284 · see citing works
Huang, C. C., Faber, P. W., Persichetti, F., Mittal, V., Vonsattel, J., MacDonald, M. E., & Gusella, J. F. (1998) · Somatic Cell and Molecular Genetics · doi:10.1023/b:scam.0000007124.19463.e5 · Cited by 273 · see citing works
Polanco, J. C., Scicluna, B. J., Hill, A. F., & Götz, J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.709485 · Cited by 271 · see citing works
Alpha-synuclein cell-to-cell transfer and seeding in grafted dopaminergic neurons in vivo
Angot, E., Steiner, J. A., Lema Tomé, C. M., Ekström, P., Mattsson, B., Björklund, A., & Brundin, P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039465 · Cited by 270 · see citing works
Transient Sequestration of TORC1 into Stress Granules during Heat Stress
Takahara, T., & Maeda, T. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.019 · Cited by 268 · see citing works
Kim, H. J., & Taylor, J. P. (2017) · Neuron · doi:10.1016/j.neuron.2017.07.029 · Cited by 267 · 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
Dujardin, S., Lécolle, K., Caillierez, R., Bégard, S., Zommer, N., Lachaud, C., Carrier, S., Dufour, N., Aurégan, G., Winderickx, J., et al. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-14 · Cited by 259 · see citing works
Hirabayashi, M., Inoue, K., Tanaka, K., Nakadate, K., Ohsawa, Y., Kamei, Y., Popiel, A. H., Shinohara, A., Iwamatsu, A., Kimura, Y., et al. (2001) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400907 · Cited by 258 · see citing works
The Role of Dipeptide Repeats in C9ORF72-Related ALS-FTD
Freibaum, B. D., & Taylor, J. P. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00035 · Cited by 251 · see citing works
Pathological alpha-synuclein propagates through neural networks
Masuda‐Suzukake, M., Nonaka, T., Hosokawa, M., Kubo, M., Shimozawa, A., Akiyama, H., & Hasegawa, M. (2014) · Acta Neuropathologica Communications · doi:10.1186/s40478-014-0088-8 · Cited by 249 · see citing works
Toxic PR n poly-dipeptides encoded by the C9orf72 repeat expansion block nuclear import and export
Shi, K. Y., Mori, E., Nizami, Z. F., Lin, Y., Kato, M., Xiang, S., Wu, L. C., Ding, M., Yu, Y., Gall, J. G., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1620293114 · Cited by 242 · see citing works
CHIP Suppresses Polyglutamine Aggregation and ToxicityIn VitroandIn Vivo
Miller, V. M., Nelson, R. F., Gouvion, C. M., Williams, A. J., Rodríguez-Lebrón, E., Harper, S. Q., Davidson, B. L., Rebagliati, M. R., & Paulson, H. L. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3001-05.2005 · Cited by 236 · see citing works
Leitman, J., Hartl, F. U., & Lederkremer, G. Z. (2013) · Nature Communications · doi:10.1038/ncomms3753 · Cited by 233 · see citing works
Gasset-Rosa, F., Chillón-Marinas, C., Goginashvili, A., Atwal, R. S., Artates, J. W., Tabet, R., Wheeler, V. C., Bang, A. G., Cleveland, D. W., & Lagier‐Tourenne, C. (2017) · Neuron · doi:10.1016/j.neuron.2017.03.027 · Cited by 231 · see citing works
Soluble Oligomers of PolyQ-Expanded Huntingtin Target a Multiplicity of Key Cellular Factors
Kim, Y., Hosp, F., Frottin, F., Ge, H., Mann, M., Hayer-Hartl, M. K., & Hartl, F. U. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.07.022 · Cited by 229 · see citing works
Kabuta, T., Furuta, A., Aoki, S., Furuta, K., & Wada, K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801918200 · Cited by 227 · see citing works
Inhibition of mitochondrial protein import by mutant huntingtin
Yano, H., Baranov, S. V., Baranova, O. V., Kim, J., Pan, Y., Yablonska, S., Carlisle, D. L., Ferrante, R. J., Kim, A. H., & Friedlander, R. M. (2014) · Nature Neuroscience · doi:10.1038/nn.3721 · Cited by 226 · see citing works
Iba, M., McBride, J. D., Guo, J. L., Zhang, B., Trojanowski, J. Q., & Lee, V. M.-Y. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1458-4 · Cited by 223 · see citing works
Ataxin-3 Is a Histone-binding Protein with Two Independent Transcriptional Corepressor Activities
Li, F., Macfarlan, T. S., Pittman, R. N., & Chakravarti, D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205259200 · Cited by 212 · see citing works
Bowman, A. B., Yoo, S.-Y., Dantuma, N. P., & Zoghbi, H. Y. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi064 · Cited by 212 · see citing works
Song, Y., Kirkpatrick, L., Schilling, A. B., Helseth, D. L., Chabot, N., Keillor, J. W., Johnson, G. V. W., & Brady, S. T. (2013) · Neuron · doi:10.1016/j.neuron.2013.01.036 · Cited by 209 · see citing works
Kanaan, N. M., Pigino, G. F., Brady, S. T., Lazarov, O., Binder, L. I., & Morfini, G. A. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.06.003 · Cited by 208 · see citing works
CHIP regulates leucine-rich repeat kinase-2 ubiquitination, degradation, and toxicity
Ko, H. S., Bailey, R. M., Smith, W. W., Liu, Z., Shin, J., Lee, Y.-I., Zhang, Y., Jiang, H., Ross, C. A., Moore, D. J., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810123106 · Cited by 208 · see citing works
Rostovtseva, T. K., Gurnev, P. A., Protchenko, O. V., Hoogerheide, D. P., Yap, T. L., Philpott, C. C., Lee, J. C., & Bezrukov, S. M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.641746 · Cited by 195 · see citing works
The cytoskeleton in neurodegenerative diseases
Cairns, N. J., Lee, V. M. ‐., & Trojanowski, J. Q. (2004) · The Journal of Pathology · doi:10.1002/path.1650 · Cited by 193 · see citing works
Alpha-synuclein release by neurons activates the inflammatory response in a microglial cell line
Alvarez‐Erviti, L., Couch, Y., Richardson, J. C., Cooper, J. A. D., & Wood, M. J. A. (2011) · Neuroscience Research · doi:10.1016/j.neures.2010.12.020 · Cited by 193 · see citing works
Human-to-mouse prion-like propagation of mutant huntingtin protein
Jeon, I., Cicchetti, F., Cisbani, G., Lee, S., Li, E., Bae, J., Lee, N., Li, L., Im, W., Kim, M., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1582-9 · Cited by 193 · see citing works
Self-citationBiophysics of α-synuclein membrane interactions
Pfefferkorn, C. M., Jiang, Z., & Lee, J. C. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.07.032 · Cited by 190 · see citing works
Depressive symptoms in neurodegenerative diseases
Baquero, M. (2015) · World Journal of Clinical Cases · doi:10.12998/wjcc.v3.i8.682 · Cited by 178 · see citing works
Extensive changes in DNA methylation are associated with expression of mutant huntingtin
Ng, C., Yildirim, F., Yap, Y. S., Dalin, S., Matthews, B. J., Vélez, P., Labadorf, A. T., Housman, D. E., & Fraenkel, E. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1221292110 · Cited by 178 · see citing works
ADF/Cofilin-Actin Rods in Neurodegenerative Diseases
Bamburg, J. R., Bernstein, B. W., Davis, R. C., Flynn, K. C., Goldsbury, C., Jensen, J. R., Maloney, M. T., Marsden, I. T., Minamide, L. S., Pak, C. W., et al. (2010) · Current Alzheimer Research · doi:10.2174/156720510791050902 · Cited by 173 · see citing works
Transfer of host-derived alpha synuclein to grafted dopaminergic neurons in rat
Kordower, J. H., Dodiya, H. B., Kordower, A. M., Terpstra, B. T., Paumier, K. L., Madhavan, L., Sortwell, C. E., Steece‐Collier, K., & Collier, T. J. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.05.001 · Cited by 170 · see citing works
Molecular Neuropathology of TDP-43 Proteinopathies
Neumann, M. (2009) · International Journal of Molecular Sciences · doi:10.3390/ijms10010232 · Cited by 169 · see citing works
Cytoskeletal pathologies of Alzheimer disease
Bamburg, J. R., & Bloom, G. S. (2009) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.20388 · Cited by 168 · see citing works
Irwin, D. J., Abrams, J. Y., Schonberger, L. B., Leschek, E., Mills, J. L., Lee, V. M. ‐., & Trojanowski, J. Q. (2013) · JAMA Neurology · doi:10.1001/jamaneurol.2013.1933 · Cited by 167 · see citing works
Exercise and Genetic Rescue of SCA1 via the Transcriptional Repressor Capicua
Fryer, J. D., Yu, P., Kang, H., Mandel-Brehm, C., Carter, A. N., Crespo-Barreto, J., Gao, Y., Flora, A., Shaw, C., Orr, H. T., et al. (2011) · Science · doi:10.1126/science.1212673 · Cited by 162 · see citing works
Prion-like transmission of neuronal huntingtin aggregates to phagocytic glia in the Drosophila brain
Pearce, M. M. P., Spartz, E. J., Hong, W., Luo, L., & Kopito, R. R. (2015) · Nature Communications · doi:10.1038/ncomms7768 · Cited by 159 · see citing works
Dieriks, B. V., Park, T. I.-H., Fourie, C., Faull, R. L. M., Dragunow, M., & Curtis, M. A. (2017) · Scientific Reports · doi:10.1038/srep42984 · Cited by 158 · see citing works
Autophagy, a guardian against neurodegeneration
Garcı́a-Arencibia, M., Hochfeld, W. E., Toh, P. P. C., & Rubinsztein, D. C. (2010) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2010.02.008 · Cited by 157 · see citing works
Adachi, H., Waza, M., Tokui, K., Katsuno, M., Minamiyama, M., Tanaka, F., Doyu, M., & Sobue, G. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.1242-07.2007 · Cited by 156 · see citing works
Long-Term Health of Dopaminergic Neuron Transplants in Parkinson's Disease Patients
Hallett, P. J., Cooper, O., Sadi, D., Robertson, H. A., Mendez, I. M., & Ole Isacson, A. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.05.027 · Cited by 156 · see citing works
Amyotrophic lateral sclerosis-linked FUS/TLS alters stress granule assembly and dynamics
Baron, D. M., Kaushansky, L. J., Ward, C. L., Sama, R. R. K., Chian, R.-J., Boggio, K. J., Quaresma, A. J. C., Nickerson, J. A., & Bosco, D. A. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-30 · Cited by 154 · see citing works
Regulation of motor proteins, axonal transport deficits and adult-onset neurodegenerative diseases
Brady, S. T., & Morfini, G. A. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.04.010 · Cited by 152 · see citing works
Huntington’s Disease and Mitochondria
Farshbaf, M. J., & Ghaedi, K. (2017) · Neurotoxicity Research · doi:10.1007/s12640-017-9766-1 · Cited by 148 · see citing works
Granulostasis: Protein Quality Control of RNP Granules
Alberti, S., Matějů, D., Mediani, L., & Carra, S. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00084 · Cited by 147 · see citing works
Peripheral administration of tau aggregates triggers intracerebral tauopathy in transgenic mice
Clavaguera, F., Hench, J., Lavenir, I., Schweighauser, G., Frank, S., Goedert, M., & Tolnay, M. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1231-5 · Cited by 143 · see citing works
Jia, H., Kast, R. J., Steffan, J. S., & Thomas, E. A. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds379 · Cited by 143 · see citing works
Bhat, K. P., Yan, S., Wang, C.-E., Li, S., & Li, X. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402215111 · Cited by 142 · see citing works
Ju, J.-S., Miller, S., Hanson, P. I., & Weihl, C. C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805517200 · Cited by 140 · see citing works
Profilin 1 Associates with Stress Granules and ALS-Linked Mutations Alter Stress Granule Dynamics
Figley, M. D., Bieri, G., Kolaitis, R., Taylor, J. P., & Gitler, A. D. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.0543-14.2014 · Cited by 139 · see citing works
A Mitocentric View of Parkinson's Disease
Haelterman, N. A. T., Yoon, W. H., Sandoval, H., Jaiswal, M., Shulman, J. M., & Bellen, H. J. (2014) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071013-014317 · Cited by 138 · see citing works
Autophagy and misfolded proteins in neurodegeneration
Metcalf, D. J., García-Arencibia, M., Hochfeld, W. E., & Rubinsztein, D. C. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2010.11.003 · Cited by 138 · see citing works
Culver, B. P., Savas, J. N., Park, S. K., Choi, J. H., Zheng, S., Zeitlin, S. O., Yates, J. R., & Tanese, N. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.359307 · Cited by 137 · see citing works
Walters, R. W., Muhlrad, D., Garcia, J. F., & Parker, R. (2015) · RNA · doi:10.1261/rna.053116.115 · Cited by 137 · see citing works
Ubiquitin pathways in neurodegenerative disease
Atkin, G., & Paulson, H. L. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00063 · Cited by 136 · see citing works
The Role of Chaperone-Mediated Autophagy in Huntingtin Degradation
Qi, L., Zhang, X., Wu, J.-C., Lin, F., Wang, J., DiFiglia, M., & Qin, Z.-H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046834 · Cited by 136 · see citing works
Harris, J. A., Koyama, A., Maeda, S., Ho, K., Devidze, N., Dubal, D. B., Yu, G.-Q., Masliah, E., & Mucke, L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045881 · Cited by 135 · see citing works
Ratovitski, T., Chighladze, E., Arbez, N., Boronina, T. N., Herbrich, S. M., Cole, R. N., & Ross, C. A. (2012) · Cell Cycle · doi:10.4161/cc.20423 · Cited by 134 · see citing works
Rouaux, C., Loeffler, J., & Boutillier, A. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.05.035 · Cited by 129 · see citing works
Inside out: the role of nucleocytoplasmic transport in ALS and FTLD
Boeynaems, S., Bogaert, E., Damme, P. V., & Bosch, L. V. D. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1586-5 · Cited by 128 · see citing works
Ramdzan, Y. M., Trubetskov, M. M., Ormsby, A. R., Newcombe, E. A., Sui, X., Tobin, M. J., Bongiovanni, M. N., Gras, S. L., Dewson, G., Miller, J. M. L., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.04.029 · Cited by 124 · see citing works
Deriziotis, P., André, R., Smith, D. M., Goold, R., Kinghorn, K. J., Kristiansen, M., Nathan, J. A., Rosenzweig, R., Krutauz, D., Glickman, M. H., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.224 · Cited by 122 · see citing works
Transcellular spreading of huntingtin aggregates in the Drosophila brain
Babcock, D. T., & Ganetzky, B. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1516217112 · Cited by 122 · see citing works
New Insights in the Amyloid-Beta Interaction with Mitochondria
Spuch, C., Ortolano, S., & Fernández-Balbuena, C. N. (2012) · Journal of Aging Research · doi:10.1155/2012/324968 · Cited by 117 · see citing works
From Intrinsic Firing Properties to Selective Neuronal Vulnerability in Neurodegenerative Diseases
Roselli, F., & Caroni, P. (2015) · Neuron · doi:10.1016/j.neuron.2014.12.063 · Cited by 117 · see citing works
Hosp, F., Gutiérrez-Ángel, S., Schaefer, M. H., Cox, J., Meissner, F., Hipp, M. S., Hartl, F. U., Klein, R., Dudanova, I., & Mann, M. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.10.097 · Cited by 117 · see citing works
Physiological Phenotype and Vulnerability in Parkinson's DiseasePreprint
Surmeier, D. J., Guzmán, J. N., Sánchez, J. A., & Schumacker, P. T. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009290 · Cited by 115 · see citing works
Exosomes and nanotubes: Control of immune cell communication
McCoy-Simandle, K., Hanna, S. J., & Cox, D. (2015) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2015.12.006 · Cited by 113 · see citing works
Axonal transport defects are a common phenotype in Drosophila models of ALS
Baldwin, K. R., Godena, V. K., Hewitt, V. L., & Whitworth, A. J. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw105 · Cited by 105 · see citing works
Interaction of misfolded proteins and mitochondria in neurodegenerative disorders
Abramov, A. Y., Berezhnov, A. V., Fedotova, E. I., Зинченко, В. П., & Долгачева, Л. П. (2017) · Biochemical Society Transactions · doi:10.1042/bst20170024 · Cited by 105 · see citing works
Williams, A. J., Knutson, T. M., Gould, V. F. C., & Paulson, H. L. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.10.016 · Cited by 103 · see citing works
Yang, H., Li, J., Liu, S., Zhao, J., Jiang, Y., Song, A.-X., & Hu, H. (2014) · Scientific Reports · doi:10.1038/srep06410 · Cited by 103 · see citing works
Ying, M., Xu, R., Wu, X., Zhu, H., Zhuang, Y., Han, M., & Xu, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m511677200 · Cited by 103 · see citing works
Ho, L. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01753-5 · Cited by 103 · see citing works
Hamaguchi, T., Eisele, Y. S., Varvel, N. H., Lamb, B. T., Walker, L. C., & Jucker, M. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0912-1 · Cited by 100 · see citing works
Chiesa, R., Piccardo, P., Dossena, S., Akhtar, L. N., Roth, K. A., Ghetti, B. F., & Harris, D. A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406173102 · Cited by 99 · see citing works
Identification of NUB1 as a suppressor of mutant Huntingtin toxicity via enhanced protein clearance
Lu, B., Al‐Ramahi, I., Valencia, A., Wang, Q., Berenshteyn, F., Yang, H., Gallego‐Flores, T., Ichcho, S., Lacoste, A., Hild, M., et al. (2013) · Nature Neuroscience · doi:10.1038/nn.3367 · Cited by 99 · see citing works
Guo, W., Crossey, E. L., Zhang, L., Zucca, S., George, O. L., Valenzuela, C. F., & Zhao, X. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019351 · Cited by 99 · see citing works
Neurodegeneration: diseases of the cytoskeleton?
McMurray, C. T. (2000) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400764 · Cited by 99 · see citing works
Enteroviral Infection: The Forgotten Link to Amyotrophic Lateral Sclerosis?
Xue, Y. C., Feuer, R., Cashman, N. R., & Luo, H. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00063 · Cited by 97 · see citing works
Helwig, M., Klinkenberg, M., Rusconi, R., Musgrove, R. E., Majbour, N. K., El‐Agnaf, O. M. A., Ulusoy, A., & Monte, D. A. D. (2015) · Brain · doi:10.1093/brain/awv376 · Cited by 96 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
SYK coordinates neuroprotective microglial responses in neurodegenerative disease
Ennerfelt, H., Frost, E. L., Shapiro, D. A., Holliday, C., Zengeler, K. E., Voithofer, G., Bolte, A. C., Lammert, C. R., Kulas, J. A., Ulland, T. K., et al. (2022) · Cell · doi:10.1016/j.cell.2022.09.030 · Cited by 329 · see citing works
“The buildup of neurotoxic agents is believed to cause neuronal damage and death, which can ultimately lead to various forms of neurological dysfunction that include cognitive decline, motor abnormalities, mental disorders, and loss of inhibition (Chung et al., 2018; Taylor et al., 2002; Vickers et al., 2009).”
- Authors
- Chung, C. G., Lee, H., & Lee, S. B.
- Affiliations
- Daegu Gyeongbuk Institute of Science and Technology (KR)
- Corresponding author
- Lee, Hyosang
- Lee, Sung Bae
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2018-06-12
- Volume
- 75
- Issue
- 17
- Pages
- 3159-3180
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- PMC
- PMC6063327
- OpenAlex
- W2807962932
- Cited by
- 142
- References
- 246
- Citations by year
- 2026: 7 · 2025: 20 · 2024: 13 · 2023: 18 · 2022: 21 · 2021: 30 · 2020: 23 · 2019: 8 · 2018: 1 · 2015: 1
- FWCI
- 2.03
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Cellular and Molecular Life Sciences (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Ministry of Science and ICT (18-BD-0402, 18-BT-02, 18-01-HRSS-02, 18-BR-04-03)
- Ministry of Science, ICT and Future Planning (2017R1A2B4003351, 2016M3C7A1947307, 2016M3C7A1904148)
- Korea Research Institute of Standards and Science (KRISS-2018-GP2018-0018)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Keywords
- protein toxicity, neurodegenerative diseases, protein aggregation, protein mislocalization, protein oligomerization, mitochondrial toxicity, cell-to-cell transmission, selective neuronal vulnerability, disease progression, therapeutic interventions
- MeSH terms
- Animals, Cell Nucleus, Humans, Mitochondria, Neurons, Proteins, Disease Progression, Neurodegenerative Diseases
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
