α-Synuclein Oligomers Induce a Unique Toxic Tau Strain
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BACKGROUND: The coexistence of α-synuclein and tau aggregates in several neurodegenerative disorders, including Parkinson's disease and Alzheimer's disease, raises the possibility that a seeding mechanism is involved in disease progression. METHODS: To further investigate the role of α-synuclein in the tau aggregation pathway, we performed a set of experiments using both recombinant and brain-derived tau and α-synuclein oligomers to seed monomeric tau aggregation in vitro and in vivo. Brain-derived tau oligomers were isolated from well-characterized cases of progressive supranuclear palsy (n = 4) and complexes of brain-derived α-synuclein/tau oligomers isolated from patients with Parkinson's disease (n = 4). The isolated structures were purified and characterized by standard biochemical methods, then injected into Htau mice (n = 24) to assess their toxicity and role in tau aggregation. RESULTS: We found that α-synuclein induced a distinct toxic tau oligomeric strain that avoids fibril formation. In vivo, Parkinson's disease brain-derived α-synuclein/tau oligomers administered into Htau mouse brains accelerated endogenous tau oligomer formation concurrent with increasing cell loss. CONCLUSIONS: Our findings provide evidence, for the first time, that α-synuclein enhances the harmful effects of tau, thus contributing to disease progression.
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α-synuclein oligomers induce a distinct toxic strain of TauO that evades fibril formation.
“our previous study demonstrated that α‐synuclein oligomers induce a distinct toxic strain of TauO that evades fibril formation.”
From Senescence, brain inflammation, and oligomeric tau drive cognitive decline in Alzheimer's disease: Evidence from clinical and preclinical studies (2024) · cites this paper as [172]
Injection of α-synuclein/TauO into the brains of a tauopathy mouse model accelerates endogenous TauO formation and concurrent neurodegeneration, contributing to disease progression.
“Injection of α‐synuclein/TauO into the brains of a tauopathy mouse model accelerates endogenous TauO formation and concurrent neurodegeneration, thereby contributing to disease progression.”
From Senescence, brain inflammation, and oligomeric tau drive cognitive decline in Alzheimer's disease: Evidence from clinical and preclinical studies (2024) · cites this paper as [172]
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1 retracted
Accumulation of oligomer-prone α-synuclein exacerbates synaptic and neuronal degeneration in vivo.
Rockenstein, E., Nuber, S., Overk, C., Ubhi, K., Mante, M., Patrick, C., Adame, A., Trejo-Morales, M., Gerez, J., Picotti, P., et al. (2014) · Brain : a journal of neurology · doi:10.1093/brain/awu057 · Cited by 228 · see citing works
RetractedCommon 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
Self-citationLuk, 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
Initiation and Synergistic Fibrillization of Tau and Alpha-Synuclein
Giasson, B. I., Forman, M. S., Higuchi, M., Golbe, L. I., Graves, C. L., Kotzbauer, P. T., Trojanowski, J. Q., & Lee, V. M.-Y. (2003) · Science · doi:10.1126/science.1082324 · Cited by 879 · cited 2× · see citing works
“In addition, recombinant tau and a -synuclein are capable of inducing fi bril-lization of each other (12), and the exposure of cells in culture to exogenous fi brils of recombinant tau and a -synuclein leads to the development of large inclusions (14,15).”
Parkinson's disease dementia: convergence of α-synuclein, tau and amyloid-β pathologies
Irwin, D. J., Lee, V. M. ‐., & Trojanowski, J. Q. (2013) · Nature reviews. Neuroscience · doi:10.1038/nrn3549 · Cited by 875 · 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
Hamilton, R. L. (2000) · Brain Pathology · doi:10.1111/j.1750-3639.2000.tb00269.x · Cited by 754 · see citing works
Proteopathic tau seeding predicts tauopathy in vivo
Holmes, B. B., Furman, J. L., Mahan, T. E., Yamasaki, T. R., Mirbaha, H., Eades, W. C., Belaygorod, L., Cairns, N. J., Holtzman, D. M., & Diamond, M. I. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1411649111 · Cited by 696 · see citing works
Distinct α-Synuclein Strains Differentially Promote Tau Inclusions in Neurons
Guo, J. L., Covell, D. J., Daniels, J. P., Iba, M., Stieber, A., Zhang, B., Riddle, D. M., Kwong, L. K., Xu, Y., Trojanowski, J. Q., et al. (2013) · Cell · doi:10.1016/j.cell.2013.05.057 · Cited by 680 · see citing works
Iba, M., Guo, J. L., McBride, J. D., Zhang, B., Trojanowski, J. Q., & Lee, V. M.-Y. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.2642-12.2013 · Cited by 664 · see citing works
Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice
Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Sengupta, U., Clos, A. L., Jackson, G. R., & Kayed, R. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-39 · Cited by 633 · see citing works
Self-citationSharon, R., Bar-Joseph, I., Frosch, M. P., Walsh, D. M., Hamilton, J. A., & Selkoe, D. J. (2003) · Neuron · doi:10.1016/s0896-6273(03)00024-2 · Cited by 562 · see citing works
Lippa, C. F., Fujiwara, H., Mann, D. M. A., Giasson, B., Baba, M., Schmidt, M. L., Nee, L. E., O'Connell, B., Pollen, D. A., St. George-Hyslop, P., et al. (1998) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65722-7 · Cited by 533 · see citing works
Identification of oligomers at early stages of tau aggregation in Alzheimer's disease
Lasagna‐Reeves, C. A., Castillo‐Carranza, D. L., Sengupta, U., Sarmiento, J., Troncoso, J., Jackson, G. R., & Kayed, R. (2012) · The FASEB Journal · doi:10.1096/fj.11-199851 · Cited by 527 · see citing works
Self-citationAlzheimer brain-derived tau oligomers propagate pathology from endogenous tau
Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Sengupta, U., Guerrero-Munoz, M. J., Kiritoshi, T., Neugebauer, V., Jackson, G. R., & Kayed, R. (2012) · Scientific Reports · doi:10.1038/srep00700 · Cited by 502 · see citing works
Self-citationColocalization of Tau and Alpha-Synuclein Epitopes in Lewy Bodies
Ishizawa, T., Mattila, P. M., Davies, P., Wang, D., & Dickson, D. W. (2003) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/62.4.389 · Cited by 391 · see citing works
Prefibrillar Amyloid Protein Aggregates Share Common Features of Cytotoxicity
Bucciantini, M., Calloni, G., Chiti, F., Formigli, L., Nosi, D., Dobson, C. M., & Stefani, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400348200 · Cited by 369 · see citing works
Preparation and Characterization of Neurotoxic Tau Oligomers
Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Guerrero-Muñoz, M. J., Jackson, G. R., & Kayed, R. (2010) · Biochemistry · doi:10.1021/bi1016233 · Cited by 359 · see citing works
Self-citationCharacterization of Prefibrillar Tau Oligomers in Vitro and in Alzheimer Disease
Patterson, K. R., Remmers, C. L., Fu, Y., Brooker, S. M., Kanaan, N. M., Vana, L., Ward, S., Reyes, J. F., Philibert, K., Glucksman, M., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.237974 · Cited by 354 · see citing works
Seeded Aggregation and Toxicity of α-Synuclein and Tau
Nonaka, T., Watanabe, S., Iwatsubo, T., & Hasegawa, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.148460 · Cited by 330 · see citing works
Structural Organization of α-Synuclein Fibrils Studied by Site-directed Spin Labeling
Der-Sarkissian, A., Jao, C. C., Chen, J., & Langen, R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305266200 · Cited by 328 · see citing works
Tau Oligomers: Cytotoxicity, Propagation, and Mitochondrial Damage
Shafiei, S. S., Guerrero-Muñoz, M. J., & Castillo-Carranza, D. L. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00083 · Cited by 314 · see citing works
Self-citationSeeding induced by α‐synuclein oligomers provides evidence for spreading of α‐synuclein pathology
Danzer, K. M., Krebs, S. K., Wolff, M., Birk, G., & Hengerer, B. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06324.x · Cited by 303 · see citing works
Increased levels of granular tau oligomers: An early sign of brain aging and Alzheimer's disease
Maeda, S., Sahara, N., Saito, Y., Murayama, S., Ikai, A., & Takashima, A. (2006) · Neuroscience Research · doi:10.1016/j.neures.2005.11.009 · Cited by 301 · see citing works
Template-assisted filament growth by parallel stacking of tau
Margittai, M., & Langen, R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401911101 · Cited by 276 · see citing works
Paleologou, K. E., Kragh, C. L., Mann, D. M. A., Salem, S. A., Al‐Shami, R., Allsop, D., Hassan, A. H. M., Jensen, P. H., & El‐Agnaf, O. M. A. (2008) · Brain · doi:10.1093/brain/awn349 · Cited by 225 · see citing works
Tau-dependent microtubule disassembly initiated by prefibrillar β-amyloid
King, M. E., Kan, H.-M., Baas, P. W., Erişir, A., Glabe, C. G., & Bloom, G. S. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200605187 · Cited by 215 · see citing works
Fang, Y.-S., Tsai, K., Chang, Y.-J., Kao, P. F., Woods, R., Kuo, P. H., Wu, C., Liao, J., Chou, S.-C., Lin, V., et al. (2014) · Nature Communications · doi:10.1038/ncomms5824 · Cited by 211 · see citing works
Waxman, E. A., & Giasson, B. I. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.0297-11.2011 · Cited by 193 · see citing works
Confluence of α-Synuclein, Tau, and β-Amyloid Pathologies in Dementia With Lewy Bodies
Colom‐Cadena, M., Gelpí, E., Charif, S., Belbin, O., Blesa, R., Martı́, M. J., Clarimón, J., & Lleó, A. (2013) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000018 · Cited by 184 · see citing works
Pathological Interface Between Oligomeric Alpha-Synuclein and Tau in Synucleinopathies
Sengupta, U., Guerrero‐Munoz, M. J., Castillo‐Carranza, D. L., Lasagna‐Reeves, C. A., Gerson, J. E., Paulucci-Holthauzen, A. A., Krishnamurthy, S., Farhed, M., Jackson, G. R., & Kayed, R. (2015) · Biological Psychiatry · doi:10.1016/j.biopsych.2014.12.019 · Cited by 181 · see citing works
Self-citationTau Enhances α-Synuclein Aggregation and Toxicity in Cellular Models of Synucleinopathy
Badiola, N., de Oliveira, R. M., Herrera, F., Guardia‐Laguarta, C., Gonçalves, S. A., Pera, M., Suárez‐Calvet, M., Clarimón, J., Outeiro, T. F., & Lleó, A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026609 · Cited by 150 · see citing works
α-Synuclein Oligomers Impair Neuronal Microtubule-Kinesin Interplay
Prots, I., Veber, V., Brey, S., Campioni, S., Buder, K., Riek, R., Böhm, K. J., & Winner, B. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.451815 · Cited by 140 · see citing works
Tau and α-Synuclein Pathology in Amygdala of Parkinsonism-Dementia Complex Patients of Guam
Forman, M. S., Schmidt, M. L., Kasturi, S. S., Perl, D. P., Lee, V. M. ‐., & Trojanowski, J. Q. (2002) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)61119-4 · Cited by 127 · see citing works
Hyperphosphorylated Tau in an α-synuclein-overexpressing transgenic model of Parkinson’s disease
Haggerty, T., Credle, J. J., Rodriguez, O. C., Wills, J., Oaks, A. W., Masliah, E., & Sidhu, A. (2011) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2011.07660.x · Cited by 126 · see citing works
Popescu, A., Lippa, C. F., Lee, V. M. ‐., & Trojanowski, J. Q. (2004) · Archives of Neurology · doi:10.1001/archneur.61.12.1915 · Cited by 117 · see citing works
Guerrero‐Munoz, M. J., Castillo‐Carranza, D. L., & Kayed, R. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.12.023 · Cited by 103 · see citing works
Self-citationCharacterization of tau oligomeric seeds in progressive supranuclear palsy
Gerson, J. E., Sengupta, U., Lasagna‐Reeves, C. A., Guerrero‐Munoz, M. J., Troncoso, J. C., & Kayed, R. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-73 · Cited by 95 · see citing works
Self-citationObi, K., Akiyama, H., Kondo, H., Shimomura, Y., Hasegawa, M., Iwatsubo, T., Mizuno, Y., & Mochizuki, H. (2007) · Experimental Neurology · doi:10.1016/j.expneurol.2007.11.019 · Cited by 91 · see citing works
Chu, J., Lauretti, E., & Praticò, D. (2017) · Molecular Psychiatry · doi:10.1038/mp.2016.214 · Cited by 90 · see citing works
Morozova, O. A., March, Z. M., Robinson, A. S., & Colby, D. W. (2013) · Biochemistry · doi:10.1021/bi400866w · Cited by 87 · see citing works
Takeda, A., Hashimoto, M., Mallory, M., Sundsumo, M., Hansen, L., & Masliah, E. (2000) · Acta Neuropathologica · doi:10.1007/pl00007441 · Cited by 83 · see citing works
Roy, B., & Jackson, G. R. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu011 · Cited by 75 · see citing works
Arima, K., Mizutani, T., Alim, A., Tonozuka-Uehara, H., Izumiyama, Y., Hirai, S., & Uéda, K. (2000) · Acta Neuropathologica · doi:10.1007/s004010050002 · Cited by 71 · see citing works
Amyloid-β oligomers as a template for secondary amyloidosis in Alzheimer's disease
Guerrero‐Munoz, M. J., Castillo‐Carranza, D. L., Krishnamurthy, S., Paulucci-Holthauzen, A. A., Sengupta, U., Lasagna‐Reeves, C. A., Ahmad, Y., Jackson, G. R., & Kayed, R. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.08.008 · Cited by 67 · see citing works
Self-citationDetection of Lewy Bodies in Trisomy 21 (Down's Syndrome)
Raghavan, R., Khin-Nu, C., Brown, A., Irving, D., Ince, P. G., Day, K. A., Tyrer, S. P., & Perry, R. H. (1993) · Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques · doi:10.1017/s0317167100047405 · Cited by 54 · see citing works
MAPT H1 haplotype is associated with enhanced α-synuclein deposition in dementia with Lewy bodies
Colom‐Cadena, M., Gelpí, E., Martı́, M. J., Charif, S., Dols‐Icardo, O., Blesa, R., Clarimón, J., & Lleó, A. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.06.015 · Cited by 53 · see citing works
Price (1999) · doi:10.1002/1531-8249(199903)45:3
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Self-citationSengupta, U., & Kayed, R. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2022.102270 · Cited by 303 · see citing works
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Du, X.-Y., Xie, X.-X., & Liu, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228645 · Cited by 242 · see citing works
Limorenko, G., & Lashuel, H. A. (2021) · Chemical Society Reviews · doi:10.1039/d1cs00127b · Cited by 162 · see citing works
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Plotkin, S. S., & Cashman, N. R. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105010 · Cited by 156 · see citing works
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Pan, L., Li, C., Meng, L., Tian, Y., He, M., Yuan, X., Zhang, G., Zhang, Z., Xiong, J., Chen, G., et al. (2022) · Brain · doi:10.1093/brain/awac171 · Cited by 154 · see citing works
Ivanova, M. I., Lin, Y., Lee, Y., Zheng, J., & Ramamoorthy, A. (2020) · Biophysical Chemistry · doi:10.1016/j.bpc.2020.106507 · Cited by 155 · see citing works
An outline for the pharmacological effect of icariin in the nervous system
Jin, J., Wang, H., Hua, X., Chen, D., Huang, C., & Chen, Z. (2018) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2018.10.006 · Cited by 137 · see citing works
Fundamentals of cross-seeding of amyloid proteins: an introduction
Ren, B., Zhang, Y., Zhang, M., Liu, Y., Zhang, D., Gong, X., Feng, Z., Tang, J., Chang, Y., & Zheng, J. (2019) · Journal of Materials Chemistry B · doi:10.1039/c9tb01871a · Cited by 135 · see citing works
P53 aggregation, interactions with tau, and impaired DNA damage response in Alzheimer’s disease
Farmer, K. M., Ghag, G., Puangmalai, N., Montalbano, M., Bhatt, N. N., & Kayed, R. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01012-6 · Cited by 126 · see citing works
Self-citationGaikwad, S., Senapati, S., Haque, M. A., & Kayed, R. (2024) · Alzheimer's & Dementia · doi:10.1002/alz.13490 · Cited by 117 · see citing works
Self-citationAmyloid Cross-Seeding: Mechanism, Implication, and Inhibition
Subedi, S., Sasidharan, S., Nag, N., Saudagar, P., & Tripathi, T. (2022) · Molecules · doi:10.3390/molecules27061776 · Cited by 114 · see citing works
α-Synuclein modulates tau spreading in mouse brains
Bassil, F., Meymand, E. S., Brown, H. J., Xu, H. W., Cox, T. O., Pattabhiraman, S., Maghames, C. M., Wu, Q., Zhang, B., Trojanowski, J. Q., et al. (2020) · The Journal of Experimental Medicine · doi:10.1084/jem.20192193 · Cited by 111 · see citing works
Montalbano, M., McAllen, S., Cascio, F. L., Sengupta, U., García, S., Bhatt, N. N., Ellsworth, A., Heidelman, E. A., Johnson, O. D., Doskocil, S. D., et al. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105130 · Cited by 107 · see citing works
Self-citationTau in neurodegenerative diseases: molecular mechanisms, biomarkers, and therapeutic strategies
Zhang, X., Wang, J., Zhang, Z., & Ye, K. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00429-6 · Cited by 106 · see citing works
Immunotherapies for Aging-Related Neurodegenerative Diseases—Emerging Perspectives and New Targets
Kwon, S., Iba, M., Kim, C., & Masliah, E. (2020) · Neurotherapeutics · doi:10.1007/s13311-020-00853-2 · Cited by 92 · see citing works
Singh, B., Covelo, A., Martell-Martinez, H. A., Nanclares, C., Sherman, M. A., Okematti, E., Meints, J. P., Teravskis, P. J., Gallardo, C., Savonenko, A. V., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02032-w · Cited by 84 · see citing works
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Self-citationKayed, R., Dettmer, U., & Lesné, S. (2020) · Journal of Parkinson s Disease · doi:10.3233/jpd-201965 · Cited by 62 · see citing works
Self-citationModulating disease-relevant tau oligomeric strains by small molecules
Cascio, F. L., García, S., Montalbano, M., Puangmalai, N., McAllen, S., Pace, A., Piccionello, A. P., & Kayed, R. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014630 · Cited by 51 · see citing works
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Zhu, W., Zhang, W., Chen, J., Tong, Y., Xu, F., & Pang, J. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c01719 · Cited by 51 · see citing works
Lim, K. H. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00158 · Cited by 46 · see citing works
Feng, S., Wang, Z., Yuan, Y., Sun, H., Chen, N., & Zhang, Y. (2020) · European Journal of Neuroscience · doi:10.1111/ejn.14699 · Cited by 47 · see citing works
The prion-like transmission of tau oligomers via exosomes
Jackson, N. A., Guerrero‐Munoz, M. J., & Castillo‐Carranza, D. L. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.974414 · Cited by 44 · see citing works
Self-citationHill, E., Wall, M. J., Moffat, K. G., & Karikari, T. K. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00155 · Cited by 42 · see citing works
Advances in Proteasome Enhancement by Small Molecules
George, D. E., & Tepe, J. J. (2021) · Biomolecules · doi:10.3390/biom11121789 · Cited by 40 · see citing works
Sengupta, U., Puangmalai, N., Bhatt, N. N., García, S., Zhao, Y., & Kayed, R. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-01913-6 · Cited by 38 · see citing works
Self-citationWren, M. C., Lashley, T., Årstad, E., & Sander, K. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0535-z · Cited by 37 · see citing works
Bodily, T. A., Ramanathan, A., Wei, S., Karkisaval, A. G., Bhatt, N. N., Jerez, C., Haque, M. A., Ramil, A., Heda, P., Wang, Y., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2311565120 · Cited by 37 · see citing works
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Tian, Y., Meng, L., & Zhang, Z. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03298-9 · Cited by 37 · see citing works
Caligiore, D., Giocondo, F., & Silvetti, M. (2022) · IBRO Neuroscience Reports · doi:10.1016/j.ibneur.2022.09.007 · Cited by 36 · see citing works
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Hayakawa, H., Nakatani, R., Ikenaka, K., Aguirre, C., Choong, C., Tsuda, H., Nagano, S., Koike, M., Ikeuchi, T., Hasegawa, M., et al. (2019) · Movement Disorders · doi:10.1002/mds.27887 · Cited by 36 · see citing works
Cascio, F. L., Park, S., Sengupta, U., Puangmalai, N., Bhatt, N. N., Shchankin, N., Jerez, C., Moreno, N., Bittar, A., Xavier, R., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-07499-w · Cited by 35 · see citing works
Self-citationTau induces formation of α-synuclein filaments with distinct molecular conformations
Hojjatian, A., Dasari, A. K. R., Sengupta, U., Taylor, D. W., Daneshparvar, N., Yeganeh, F. A., Dillard, L. B., Michael, B. C., Griffin, R. G., Borgnia, M. J., et al. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.03.091 · Cited by 40 · see citing works
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“Prion-like” seeding and propagation of oligomeric protein assemblies in neurodegenerative disorders
Zampar, S., Gregorio, S. E. D., Grimmer, G., Watts, J. C., & Ingelsson, M. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1436262 · Cited by 34 · see citing works
Kumar, D., Sharma, A., & Sharma, L. K. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200203101828 · Cited by 33 · see citing works
Pharmacological Modulators of Tau Aggregation and Spreading
Dominguez‐Meijide, A., Vasili, E., & Outeiro, T. F. (2020) · Brain Sciences · doi:10.3390/brainsci10110858 · Cited by 34 · see citing works
Neuropathologic correlates of amyloid and dopamine transporter imaging in Lewy body disease
Shirvan, J. C., Clement, N. F., Ye, R., Katz, S. R., Schultz, A. P., Johnson, K. A., Gómez‐Isla, T., Frosch, M. P., Growdon, J. H., & Gomperts, S. N. (2019) · Neurology · doi:10.1212/wnl.0000000000007855 · Cited by 30 · see citing works
Guttuso, T. J., Andrzejewski, K. L., Lichter, D. G., & Andersen, J. K. (2019) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2019.05.016 · Cited by 29 · see citing works
Sekiya, H., Matsubara, T., Deture, M. A., & Dickson, D. W. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00900-6 · Cited by 30 · see citing works
Na, H., Gan, Q., Mcparland, L., Yang, J. B., Yao, H., Tian, H., Zhang, Z., & Qiu, W. Q. (2020) · Neuropharmacology · doi:10.1016/j.neuropharm.2020.108017 · Cited by 26 · see citing works
Open questions on the nature of Parkinson’s disease: from triggers to spreading pathology
Mou, L., Ding, W., & Fernández-Fúnez, P. (2019) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2019-106210 · Cited by 25 · see citing works
Amyloid Protein Cross-Seeding Provides a New Perspective on Multiple Diseases In Vivo
Ge, W., Deng, X., Shi, W., Lin, W.-J., Chen, L., Liang, H., Wang, X., Zhang, T., Zhao, F., Guo, W., et al. (2022) · Biomacromolecules · doi:10.1021/acs.biomac.2c01233 · Cited by 22 · see citing works
Takaichi, Y., CHAMBERS, J. K., Inoue, H., Ano, Y., Takashima, A., Nakayama, H., & Uchida, K. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-00969-8 · Cited by 20 · see citing works
Hadi, F., Akrami, H., Totonchi, M., Barzegar, A., Nabavi, S. M., & Shahpasand, K. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15257 · Cited by 20 · see citing works
Cehlár, O., Njemoga, S., Horvath, M., Cizmazia, E., Bednáriková, Z., & Barrera, E. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252313049 · Cited by 21 · see citing works
Shi, J., Wang, Y., Chen, D., Xu, X., Li, W., Li, K., He, J., Su, W., & Luo, Q. (2023) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-023-12410-w · Cited by 19 · see citing works
Lau, D., Magnan, C., Hill, K. J., Cooper, A. A., Gambin, Y., & Sierecki, E. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00553 · Cited by 18 · see citing works
Masuda‐Suzukake, M., Suzuki, G., Hosokawa, M., Nonaka, T., Goedert, M., & Hasegawa, M. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa091 · Cited by 16 · see citing works
Moore, K., Sengupta, U., Puangmalai, N., Bhatt, N. N., & Kayed, R. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03211-3 · Cited by 14 · see citing works
Self-citationZhan, X., Wen, G., Wu, X., & Li, J. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00490-9 · Cited by 14 · see citing works
The unique neuropathological vulnerability of the human brain to aging
Ferrer, I. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101916 · Cited by 14 · see citing works
The Strategies of Development of New Non-Toxic Inhibitors of Amyloid Formation
Galzitskaya, O. V., Grishin, S. Y., Glyakina, A. V., Dovidchenko, N. V., Konstantinova, A. V., Kravchenko, S. V., & Surin, A. K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043781 · Cited by 12 · see citing works
Relationship Between Tau, β Amyloid and α-Synuclein Pathologies
Walker, L., & Attems, J. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_14 · Cited by 12 · see citing works
Bhopatkar, A. A., Bhatt, N., Haque, M. A., Xavier, R., Fung, L., Jerez, C., & Kayed, R. (2024) · Protein Science · doi:10.1002/pro.5099 · Cited by 5 · see citing works
Self-citationIvanova, M. I., Rosa, C. L., & Ramamoorthy, A. (2026) · Protein Science · doi:10.1002/pro.70525 · Cited by 10 · see citing works
Zhan, X., Li, W., Hatterer, E., Courade, J., Piché, K., Klementieva, O. L., & Li, J. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c02811 · Cited by 10 · see citing works
Liang, J., Li, R., Wong, G., & Huang, X. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00879-0 · Cited by 13 · see citing works
Abulimiti, G., Zeng, J., Aimaiti, M., Lei, X., & Mi, N. (2022) · Food Science & Nutrition · doi:10.1002/fsn3.3031 · Cited by 9 · see citing works
Distinct cryo-EM Structure of α-synuclein Filaments derived by TauPreprint
Hojjatian, A., Dasari, A. K. R., Sengupta, U., Taylor, D. W., Daneshparvar, N., Yeganeh, F. A., Dillard, L. B., Michael, B. C., Griffin, R. G., Borgnia, M. J., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.12.31.424989 · Cited by 9 · see citing works
Self-citationCSF α-Synuclein and Tau as Biomarkers for Dementia With Lewy Bodies
Zhang, Q., Li, J., Quan, W., Liu, L., Qin, Y., Pei, X., Su, H., Xu, J., & Chen, J. (2022) · Alzheimer Disease & Associated Disorders · doi:10.1097/wad.0000000000000516 · Cited by 8 · see citing works
Sengupta, U., & Kayed, R. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3629-9_9 · Cited by 7 · see citing works
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Hinkle, J. T., & Pontone, G. M. (2020) · Psychiatric Clinics of North America · doi:10.1016/j.psc.2020.02.003 · Cited by 7 · see citing works
Mroczek, K. H., Fernando, S., Fisher, P. R., & Annesley, S. J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.741662 · Cited by 7 · see citing works
Electrochemical Aptasensors for Parkinson’s Disease Biomarkers Detection
Mikuła, E., Katrlı́k, J., & Rodrigues, L. R. (2022) · Current Medicinal Chemistry · doi:10.2174/0929867329666220520123337 · Cited by 5 · see citing works
Investigating key factors underlying neurodegeneration linked to alpha‐synuclein spread
Pang, C. C.-C., Sørensen, M. H., Lee, K., Luk, K. C., Trojanowski, J. Q., Lee, V. M. ‐., Noble, W. J., & Chang, R. C. (2022) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12829 · Cited by 4 · see citing works
Lim, M. J., Boschen, S. L., Kurti, A., Casey, M. C., Phillips, V. R., Fryer, J. D., Dickson, D. W., Jansen‐West, K. R., Petrucelli, L., Delenclos, M., et al. (2023) · Biomedicines · doi:10.3390/biomedicines11102863 · Cited by 4 · see citing works
Amyloid Cross-Interactions through the Lens of Simulations: The Case of Aβ–IAPP
Xenophontos, X., Vlachou, A., Hunt, R. K., & Tamamis, P. (2025) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5c04536 · Cited by 2 · see citing works
Lifestyles of a Toxic Twosome: A Novel Tau Strain Induced by α-Synuclein Oligomers
Jackson, G. R. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2018.08.003 · Cited by 2 · see citing works
Preclinical Model to Evaluate Outcomes of Amyloid Cross-Toxicity in the Rodent Brain
Henrı́quez, G., Méndez, L., Castañeda, E., Wagler, A. E., Jeon, S., & Narayan, M. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00419 · Cited by 2 · see citing works
Senapati, S., Sciortino, A., Samples, M., Shchankin, N., Aday, A., Zhao, Y., Montalbano, M., & Kayed, R. (2026) · Molecular Neurodegeneration Advances · doi:10.1186/s44477-026-00033-0 · Cited by 1 · see citing works
Self-citationSengupta, U., & Kayed, R. (2018) · Neuropsychopharmacology · doi:10.1038/s41386-018-0204-8 · Cited by 1 · see citing works
Self-citationA toxic subset of soluble α-synuclein species in dementia with Lewy body
Castillo‐Carranza, D. L. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa016
Self-citationManagement of Psychiatric Phenomena in Lewy Body Dementia
Hinkle, J. T., & Pontone, G. M. (2022) · Psychiatric Annals · doi:10.3928/00485713-20220908-01
Farmer, K. M., Ghag, G., Puangmalai, N., Montalbano, M., Bhatt, N. N., & Kayed, R. (2020) · Figshare · doi:10.6084/m9.figshare.12788590
Self-citationFarmer, K. M., Ghag, G., Puangmalai, N., Montalbano, M., Bhatt, N. N., & Kayed, R. (2020) · Figshare · doi:10.6084/m9.figshare.12788593
Self-citationFarmer, K. M., Ghag, G., Puangmalai, N., Montalbano, M., Bhatt, N. N., & Kayed, R. (2020) · Figshare · doi:10.6084/m9.figshare.12788602
Self-citationFarmer, K. M., Ghag, G., Puangmalai, N., Montalbano, M., Bhatt, N. N., & Kayed, R. (2020) · Figshare · doi:10.6084/m9.figshare.12788596
Self-citationNeurotoxic Tau Oligomers: Isolation, Preparation, and Characterization
Khan, S., Haque, M. A., & Kayed, R. (2026) · Neuromethods · doi:10.1007/978-1-0716-5234-3_9
Self-citationTargeting protein aggregate co-pathologies in neurodegeneration: a viable therapeutic strategy?
Buck, S. A., Madhavan, S. S., & Sanders, L. H. (2026) · Molecular Neurodegeneration Advances · doi:10.1186/s44477-026-00047-8
Differential Effects of α-Synuclein Monomers and Seeds on the Material Properties of Tau Condensates
Sharma, B., Wang, J., Chinchilla, P., Baum, J., & Shi, Z. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c07726
- Authors
- Castillo-Carranza, D. L., Guerrero-Muñoz, M. J., Sengupta, U., Gerson, J. E., & Kayed, R.
- Affiliations
- The University of Texas Medical Branch at Galveston (US)
- Corresponding author
- Kayed, Rakez
- Venue
- Biological Psychiatry
- Publisher
- Elsevier BV
- Published
- 2018-10
- Volume
- 84
- Issue
- 7
- Pages
- 499-508
- ISSN
- 0006-3223 (ISSN-L)
- PMC
- PMC6201292
- OpenAlex
- W2782823547
- Cited by
- 84
- References
- 48
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 7 · 2023: 7 · 2022: 13 · 2021: 6 · 2020: 24 · 2019: 10 · 2018: 5
- FWCI
- 7.71
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Biological Psychiatry (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion, other-oa)
- PubMed Central (acceptedVersion, cc-by-nc-nd)
- Funders
- Michael J. Fox Foundation for Parkinson's Research
- National Institutes of Health
- Mitchell Center for Neurodegenerative Diseases, University of Texas Medical Branch
- National Institute on Aging (RF1AG055771, R01AG054025)
- National Institute of Neurological Disorders and Stroke (R01NS094557)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- alpha-synuclein, tau oligomers, tau aggregation, Parkinson's disease, progressive supranuclear palsy, neurodegeneration, fibril formation, cell loss
- MeSH terms
- Animals, Brain, Humans, Parkinson Disease, Recombinant Proteins, Supranuclear Palsy, Progressive, tau Proteins, Disease Progression, Mice, alpha-Synuclein
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