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Initiation and Synergistic Fibrillization of Tau and Alpha-Synuclein
Abstract
Alpha-synuclein (alpha-syn) and tau polymerize into amyloid fibrils and form intraneuronal filamentous inclusions characteristic of neurodegenerative diseases. We demonstrate that alpha-syn induces fibrillization of tau and that coincubation of tau and alpha-syn synergistically promotes fibrillization of both proteins. The in vivo relevance of these findings is grounded in the co-occurrence of alpha-syn and tau filamentous amyloid inclusions in humans, in single transgenic mice that express A53T human alpha-syn in neurons, and in oligodendrocytes of bigenic mice that express wild-type human alpha-syn plus P301L mutant tau. This suggests that interactions between alpha-syn and tau can promote their fibrillization and drive the formation of pathological inclusions in human neurodegenerative diseases.
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“Evidence suggests that Aβ can directly affect α-synuclein toxicity, and it is also known that tau protein and α-synuclein can directly interact promoting their co-assembly [124–126].”
From The neuropathological diagnosis of Alzheimer's disease (2019) · cites this paper as [125]
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“Although -syn and tau pathology can localize and intermingle within the same aggregate in vivo, most Lewy pathology and NFTs coexist in the same brain region, but in different neurons (Giasson et al., 2003; Lee et al., 2004).”
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Genetics of Parkinsonʼs disease
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BackgroundConfluence of α-Synuclein, Tau, and β-Amyloid Pathologies in Dementia With Lewy Bodies
Colom‐Cadena, M., Gelpí, E., Charif, S., Belbin, O., Blesa, R., Martí, M. J., Clarimón, J., & Lleó, A. (2013) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000018 · Cited by 188
“A synergistic relationship between >-synuclein and tau aggregates has been described (33, 34, 36), and a common entrance mechanism for both has been suggested (70).”
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Self-citationVasconcelos, B., Stancu, I.-C., Buist, A., Bird, M., Wang, P., Vanoosthuyse, A., Van Kolen, K., Verheyen, A., Kienlen-Campard, P., Octave, J.-N., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-015-1525-x · Cited by 192
“Heterotypic seeding or cross-seeding has been demonstrated for Tau and alpha-synuclein, and for different combinations of amyloidogenic proteins in vitro [11, 14, 15, 35].”
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“The prominent protein associated with PD and DLB is α-synuclein (αSyn; encoded by SNCA), which is intrinsically disordered and forms amyloid inclusions called Lewy bodies (LB) (Bossy-Wetzel et al., 2004; Chu and Kordower, 2010; Giasson et al., 2003b; Spillantini et al., 1997).”
BackgroundInfluentialEffects of in vivo conditions on amyloid aggregation
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Pathological Interface Between Oligomeric Alpha-Synuclein and Tau in Synucleinopathies
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AV‐1451 tau and β‐amyloid positron emission tomography imaging in dementia with Lewy bodies
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Self-citationCerebrospinal Fluid Biomarkers in Parkinson's Disease with Dementia and Dementia with Lewy Bodies
Parnetti, L., Tiraboschi, P., Lanari, A., Peducci, M., Padiglioni, C., D’Amore, C., Pierguidi, L., Tambasco, N., Rossi, A., & Calabresi, P. (2008) · Biological Psychiatry · doi:10.1016/j.biopsych.2008.02.016 · Cited by 173
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“The likely mechanism underlying this ‘crosstalk’ between -synuclein and tau is explained by in vitro Wndings indicating that -synuclein protein can directly promote aggregation and Wbrillization of tau, possibly by acting as amyloidogenic seeds for tau or as amyloidogenic chaperones that can induce the abnormal confor…”
BackgroundIrwin, 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 172
“Despite the relative stability of PrP, it is still probable that most forms of these non-PrP NDAPs observed herein could also survive the relatively crude sequential extraction process used to purify c-hGH prior to 1977 in the United States,(31) because the pathological species of NDAPs in AD and related proteinopathi…”
Self-citationMethionine oxidation, α-synuclein and Parkinson's disease
Glaser, C. B., Yamin, G., Uversky, V. N., & Fink, A. L. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.10.008 · Cited by 180
α-Synuclein Overexpression Increases Cytosolic Catecholamine Concentration
Mosharov, E. V., Staal, R. G. W., Bové, J., Prou, D., Hananiya, A., Markov, D., Poulsen, N., Larsen, K. E., Moore, C. M. H., Troyer, M. D., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.0519-06.2006 · Cited by 165
“Monomeric -synuclein is mainly unfolded in solution (Eliezer et al., 2001); however, both WT and mutant -synuclein can form oligomeric protofibrils and amyloid fibrils that resemble those in Lewy bodies (Conway et al., 1998; Giasson et al., 2003).”
BackgroundAssociation analysis of MAPT H1 haplotype and subhaplotypes in Parkinson's disease
Zabetian, C. P., Hutter, C. M., Factor, S. A., Nutt, J. G., Higgins, D. S., Griffith, A., Roberts, J. W., Leis, B. C., Kay, D. M., Yearout, D., et al. (2007) · Annals of Neurology · doi:10.1002/ana.21157 · Cited by 165
“lated that a direct interaction between tau and -synuclein might be involved.(44) Further mapping of the H1 clade in PD patients and control subjects from both isolated and outbred populations is now necessary to locate the underlying risk allele(s).”
BackgroundIrwin, D. J., & Hurtig, H. I. (2018) · Journal of Alzheimer’s Disease & Parkinsonism · doi:10.4172/2161-0460.1000444 · Cited by 177
“An in vitro cell model [85,86] and transgenic SYN murine models [86] suggest that tau and SYN pathology can accelerate co-polymerization of tau.”
BackgroundLimorenko, G., & Lashuel, H. A. (2021) · Chemical Society Reviews · doi:10.1039/d1cs00127b · Cited by 168
The cell biology of Parkinson’s disease
Panicker, N., Ge, P., Dawson, V. L., & Dawson, T. M. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202012095 · Cited by 179
Tau haplotypes regulate transcription and are associated with Parkinson's disease
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“tively charged microtubule region of Tau in vitro.(32) Our study suggests that an increase in expression of MAPT, in subjects with the H1/H1 genotype, may indirectly cause Lewy bodies by increasing the propensity of -synuclein to aggregate in PD brains.”
BackgroundMolecular motors implicated in the axonal transport of tau and α-synuclein
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“…in neurodegenerative diseases (Spillantini et al., 1998; Iwai, 2000; Mukaetova-Ladinska et al., 2000; Hamilton, 2000; Masliah et al., 2001; Popescu et al., 2004), and enhancement of tau pathology by -synuclein (Giasson et al., 2003), suggests that there may be a link between these two pathologies.”
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Self-citationA deadly spread: cellular mechanisms of α-synuclein transfer
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Impairment of microtubule‐dependent trafficking by overexpression of α‐synuclein
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“Alpha-synuclein aggregates in Parkinson’s disease (Spillantini et al., 1998b) and it has been reported to interact with tau (Giasson et al., 2003; Goris et al., 2007; Satake et al., 2009; Simón-Sánchez et al., 2009).”
Kroksveen, A. C., Opsahl, J. A., Aye, T. T., Ulvik, R. J., & Berven, F. S. (2010) · Journal of Proteomics · doi:10.1016/j.jprot.2010.11.010 · Cited by 154
Tau accelerates α-synuclein aggregation and spreading in Parkinson’s disease
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“…interaction with other proteins, such as tau, that leads to an ordered coassembly of the two proteins primarily to homopolymeric fibrils (Giasson et al., 2003); post-translational modifications such as phosphorylation at Ser 129 (Fujiwara et al., 2002; Chen and Feany, 2005; Smith et…”
BackgroundSelf-citationTau Enhances α-Synuclein Aggregation and Toxicity in Cellular Models of Synucleinopathy
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“co-incubation with tau in a concentration-dependent manner [14].”
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“Some MSA patients showed an overlap of α-synucleinopathy and tauopathy [ 11 , 37].”
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“Recent studies have also found that alpha-synuclein and tau proteins polymerize to amyloid fibrils, which subsequently form intraneuronal inclusions typically found in many neurodegenerative diseases (58).”
BackgroundPrion-like Mechanisms in the Pathogenesis of Tauopathies and Synucleinopathies
Goedert, M., Falcon, B., Clavaguera, F., & Tolnay, M. (2014) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-014-0495-z · Cited by 152
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“Both SNCA and MAPT pathologies may act synergistically [9], and variants in genes encoding these 2 proteins are the most significant genetic PD risk factors known [10].”
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“Moreover, synergistic tau-a-syn interactions of pathologic relevance are indicated by experimental findings both in vitro and in animal models, including evidence of mutually enhanced protein fibrillation.(36,41,42) Mixed-aggregate pathology and synergistic injury underscore the relevance of therapeutics capable of ta…”
BackgroundCognitive and Pathological Influences of Tau Pathology in Lewy Body Disorders
Coughlin, D. G., Xie, S. X., Liang, M., Williams, A., Peterson, C. S., Weintraub, D. A., McMillan, C. T., Wolk, D. A., Akhtar, R. S., Hurtig, H. I., et al. (2018) · Annals of Neurology · doi:10.1002/ana.25392 · Cited by 150
“No differences in test scores were seen between median divisions of the cohort by %AO of Aβ or SYN.”
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“hypothesized that tau and α-synuclein promote each other's accumulation, a sign of co-morbidity (63).”
BackgroundNigrostriatal tau pathology in parkinsonism and Parkinson’s disease
Chu, Y., Hirst, W. D., Federoff, H. J., Harms, A. S., Stoessl, A. J., & Kordower, J. H. (2023) · Brain · doi:10.1093/brain/awad388 · Cited by 149
“56 Alpha-syn phosphorylation triggers tau pathogenicity and induces widespread phosphorylated tau with prion-like nature in various brain areas.”
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α-Synuclein Oligomers Impair Neuronal Microtubule-Kinesin Interplay
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“K18 Tau proteins were purified as previously described for Tau proteins (77).”
MethodSelf-citationFormation and Propagation of Tau Oligomeric Seeds
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Back to the tubule: microtubule dynamics in Parkinson’s disease
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The Central Theme of Parkinson’s Disease: α-Synuclein
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Challenges of multimorbidity of the aging brain: a critical update
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“The synergistic interaction between Ab, tau, aSyn and other pathological proteins, demonstrated in in vitro and in animal models (Giasson et al. 2003; Oddo et al. 2003) accelerating neuropathology and cognitive decline, and explaining overlap between synucleinopathies, tauopathies, and other…”
BackgroundStructure–activity relationship of amyloid fibrils
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Metal ions and oxidative protein modification in neurological disease.
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“One is the direct interaction between the protein as tau and a-synuclein promote the fibrillization of each other in vitro.(55) The other is that the misfolding and aggregation of a disease protein disrupt normal cellular functions, leading to predisposing”
BackgroundRETRACTED: Soluble α-Synuclein Is a Novel Modulator of Alzheimer's Disease Pathophysiology
Larson, M. E., Sherman, M. A., Greimel, S., Kuskowski, M., Schneider, J. A., Bennett, D. A., & Lesné, S. E. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.0581-12.2012 · Cited by 128
RetractedInteraction between pathogenic proteins in neurodegenerative disorders
Jellinger, K. A. (2011) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2011.01507.x · Cited by 132
“There is strong interaction between aSyn, tau and Ab, particularly in their oligomeric forms, which might synergistically promote their mutual aggregation and vice versa [30, 168, 180].”
BackgroundHiguchi, M., Zhang, B., Forman, M. S., Yoshiyama, Y., Trojanowski, J. Q., & Lee, V. M. ‐. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.2691-05.2005 · Cited by 133
“…Tg tau at the lowest level, did not develop OLG tau inclusions, although they did so when they were crossbred with OLG-directed -synuclein Tg mice (Giasson et al., 2003), thereby implying that cofactors such as -synuclein, when expressed in OLG, can lower the threshold at which tau pathologies…”
BackgroundSelf-citationPathological Influences on Clinical Heterogeneity in Lewy Body Diseases
Coughlin, D. G., Hurtig, H. I., & Irwin, D. J. (2019) · Movement Disorders · doi:10.1002/mds.27867 · Cited by 132
Parkinson’s disease treatment: past, present, and future
Elsworth, J. D. (2020) · Journal of Neural Transmission · doi:10.1007/s00702-020-02167-1 · Cited by 144
Nucleation-dependent Tau Filament Formation
Congdon, E. E., Kim, S., Bonchak, J., Songrug, T., Anastasios Matzavinos, A., & Kuret, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800247200 · Cited by 126
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
“Thus, a-Syn and Tau were shown to polymerize into amyloid fibrils, forming intraneuronal filamentous inclusions, and in vitro studies showed that co-incubation of Tau and a-Syn synergistically promoted the fibrilization of both proteins (Giasson et al., 2003), with the A53T mutation of a-Syn accelerating such fibriliz…”
BackgroundAmyloid-β pathology enhances pathological fibrillary tau seeding induced by Alzheimer PHF in vivo
Vergara, C., Houben, S., Suain, V., Yilmaz, Z., Decker, R. D., Dries, V. V., Boom, A., Mansour, S., Leroy, K., Ando, K., et al. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1953-5 · Cited by 131
α-Synucleinopathy models and human neuropathology: similarities and differences
Kahle, P. J. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0302-x · Cited by 132
Pankratz, N., & Foroud, T. (2007) · Genetics in Medicine · doi:10.1097/gim.0b013e31815bf97c · Cited by 129
Tau gene and Parkinson's disease: a case-control study and meta-analysis
Healy, D. G. (2004) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.2003.026203 · Cited by 125
Thinking laterally about neurodegenerative proteinopathies
Golde, T. E., Borchelt, D., Giasson, B. I., & Lewis, J. M. (2013) · Journal of Clinical Investigation · doi:10.1172/jci66029 · Cited by 126
“Further, some in vitro studies show that many amyloidogenic proteins prefer to form homopolymers (39, 88).”
BackgroundSelf-citationNishie, M., Mori, F., Yoshimoto, M., Takahashi, H., & Wakabayashi, K. (2004) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2004.00564.x · Cited by 123
Phosphorylated tau and the neurodegenerative foldopathies
Kosik, K. S., & Shimura, H. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.10.011 · Cited by 124
Lu, Y., Prudent, M., Fauvet, B., Lashuel, H. A., & Girault, H. H. (2011) · ACS Chemical Neuroscience · doi:10.1021/cn200074d · Cited by 122
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
“A growing body of evidence suggests that one pathologic protein promotes fibrillation of other abnormal proteins.(26) Herein, we focused on cases with tau as a primary aggregate.”
Self-citationChapter 6 Molecular and Cellular Biology of Synucleins
Surguchov, A. P. (2008) · International review of cytology · doi:10.1016/s1937-6448(08)01406-8 · Cited by 123
Amyloid-beta and tau protein beyond Alzheimer’s disease
Abyadeh, M., Gupta, V., Paulo, J. A., Mahmoudabad, A. G., Shadfar, S., Mirshahvaladi, S., Gupta, V. B., Nguyen, C. T. O., Finkelstein, D. I., You, Y., et al. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.386406 · Cited by 126
“This enhances its activity and in turn, increases tau phosphorylation at Ser396 leading to microtubular destabilization (Giasson et al., 2003; Gąssowska et al., 2014; Credle et al., 2015).”
BackgroundMishizen-Eberz, A. J., Norris, E. H., Giasson, B. I., Hodara, R., Ischiropoulos, H., Lee, V. M. ‐., Trojanowski, J. Q., & Lynch, D. R. (2005) · Biochemistry · doi:10.1021/bi047846q · Cited by 119
Self-citationThe role of ?-synuclein in the pathogenesis of multiple system atrophy
Wenning, G. K., & Jellinger, K. A. (2005) · Acta Neuropathologica · doi:10.1007/s00401-004-0935-y · Cited by 117
“Furthermore, co-occurrence of AS and tau filamentous inclusions has been reported in oligodendrocytes of bigenic mice expressing wild-type human AS plus P301L mutant tau [31].”
BackgroundAge-Dependent Effects of A53T Alpha-Synuclein on Behavior and Dopaminergic Function
Oaks, A. W., Frankfurt, M., Finkelstein, D. I., & Sidhu, A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060378 · Cited by 117
“Furthermore, we report age-dependent accumulation of phosphorylated Tau and activation of Tau kinases, which we and others have shown co-occur in several PD models [24-29].”
Inhibition of amyloid-β plaque formation by α-synuclein
Bachhuber, T., Katzmarski, N., McCarter, J. F., Loreth, D., Tahirović, S., Kamp, F., Abou‐Ajram, C., Nuscher, B., Serrano‐Pozo, A., Müller, A., et al. (2015) · Nature Medicine · doi:10.1038/nm.3885 · Cited by 120
Spreading of α-Synuclein and Tau: A Systematic Comparison of the Mechanisms Involved
Vasili, E., Dominguez‐Meijide, A., & Outeiro, T. F. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00107 · Cited by 121
“Furthermore, the interaction between aSyn and tau appear to promote the oligomerization and solubility of each other in vitro and in vivo, thereby disrupting cytoskeletal organization, impairing axonal transport, and compromising synaptic organization (Masliah et al., 2001; Giasson et al., 2003; Kotzbauer et al., 2004…”
BackgroundXia, Y., Prokop, S., Gorion, K.-M. M., Kim, J. D., Sorrentino, Z. A., Bell, B. M., Manaois, A. N., Chakrabarty, P., Davies, P., & Giasson, B. I. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-00967-w · Cited by 118
Self-citationSynaptic tau: A pathological or physiological phenomenon?
Robbins, M., Clayton, E. L., & Schierle, G. S. K. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01246-y · Cited by 128
Fibril growth and seeding capacity play key roles in α-synuclein-mediated apoptotic cell death
Mahul-Mellier, A.-L., Vercruysse, F., Maco, B., Ait‐Bouziad, N., Roo, M. D., Müller, D., & Lashuel, H. A. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.79 · Cited by 112
“Previous studies have suggested that α-syn fibril formation could be seeded by fibrils derived from other amyloid-forming proteins in vitro, in primary neurons and in transgenic mice.(38)”
BackgroundHejjaoui, M., Butterfield, S. M., Fauvet, B., Vercruysse, F., Cui, J., Dikiy, I., Prudent, M., Olschewski, D., Zhang, Y., Eliezer, D., et al. (2012) · Journal of the American Chemical Society · doi:10.1021/ja210866j · Cited by 115
A critical evaluation of the ubiquitin–proteasome system in Parkinson's disease
Cook, C. N., & Petrucelli, L. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.01.012 · Cited by 119
“Modulation of aggregation potential of α-synuclein—The precipitating basis of α-synuclein aggregation in synucleinopathies is controversial, though broadly speculated to arise from an increase in α-synuclein protein expression (either through gene triplication or altered transcriptional or translational activities), e…”
BackgroundAmyloid Fibril Formation of α-Synuclein Is Accelerated by Preformed Amyloid Seeds of Other Proteins
Yagi, H., Kusaka, E., Hongo, K., Mizobata, T., & Kawata, Y. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508623200 · Cited by 113
Alpha‐Synuclein induces hyperphosphorylation of Tau in the MPTP model of Parkinsonism
Duka, T., Rusnak, M., Drolet, R. E., Duka, V., Wersinger, C., Goudreau, J. L., & Sidhu, A. (2006) · The FASEB Journal · doi:10.1096/fj.06-6092com · Cited by 112
“Despite their codeposition in certain neurological disorders and their enormous potential to either directly or indirectly interact with one another and/or modulate the molecular properties of each other, few studies have been conducted in this regard ( 21 , 22).”
BackgroundBellucci, A., Zaltieri, M., Navarria, L., Grigoletto, J., Missale, C., & Spano, P. (2012) · Brain Research · doi:10.1016/j.brainres.2012.04.014 · Cited by 115
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 109
“Our findings strongly corroborate the previously reported interactions between tau and α-syn pathologies (Badiola et al., 2011; Clinton et al., 2010; Gerson et al., 2018; Giasson et al., 2003; Guo et al., 2013; Kaul et al., 2011; Sengupta et al., 2015).”
BackgroundResultSelf-citationTau in the Pathophysiology of Parkinson’s Disease
Pan, L., Meng, L., He, M., & Zhang, Z. (2021) · Journal of Molecular Neuroscience · doi:10.1007/s12031-020-01776-5 · Cited by 110
“Many in vitro studies have demonstrated that Tau and α-Syn can interact and promote aggregation of the other (Giasson 2003).”
BackgroundInterplay between tau and α‐synuclein liquid–liquid phase separation
Siegert, A., Rankovic, M., Favretto, F., Ukmar, T., Strohäker, T., Becker, S., & Zweckstetter, M. (2021) · Protein Science · doi:10.1002/pro.4025 · Cited by 106
“Several previous studies investigated the coaggregation of aSyn and tau both in vitro and in cells.3-11,38,39 The in vitro experiments by Giasson et al.3 are particularly interesting, because they used purified compounds and secondary effects can therefore be excluded.”
BackgroundInfluentialCharacterization of α‐synuclein aggregation and synergistic toxicity with protein tau in yeast
Zabrocki, P., Pellens, K., Vanhelmont, T., Vandebroek, T., Griffioen, G., Wera, S., LEUVEN, F. V., & Winderickx, J. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04571.x · Cited by 111
“This confirms most recent data obtained in vitro as well as in double-transgenic mice in vivo [ 19 ,21,22], demonstrating that tau promotes the fibrilization of a-synuclein.”
BackgroundResultInfluentialPharmacogenomics in Alzheimer's Disease
Cacabelos, R. (2008) · Methods in molecular biology · doi:10.1007/978-1-59745-205-2_10 · Cited by 109
Metadata
- Authors
- Giasson, B. I., Forman, M. S., Higuchi, M., Golbe, L. I., Graves, C. L., Kotzbauer, P. T., Trojanowski, J. Q., & Lee, V. M.-Y.
- Affiliations
- University of Medicine and Dentistry of New Jersey (US)
- Corresponding author
- Lee, Virginia M.-Y.
- ORCID
- Venue
- Science
- Published
- 2003-04-25
- Volume
- 300
- Issue
- 5619
- Pages
- 636-640
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2073893553
- Cited by
- 879
- References
- 27
- Citations by year
- 2026: 23 · 2025: 29 · 2024: 37 · 2023: 35 · 2022: 58 · 2021: 32 · 2020: 50 · 2019: 52 · 2018: 49 · 2017: 42 · 2016: 35 · 2015: 31 · 2014: 39 · 2013: 42 · 2012: 33
- FWCI
- 26.70
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- alpha-synuclein, tau protein, amyloid fibril formation, protein aggregation, neurodegenerative diseases, synucleinopathies, tauopathy, oligodendrocytes, P301L tau, A53T alpha-synuclein, transgenic mouse model, intraneuronal inclusions
- MeSH terms
- Amyloid, Animals, Biopolymers, Brain Chemistry, Humans, Mice, Inbred C3H, Mice, Inbred C57BL, Mice, Transgenic, Microscopy, Electron, Microscopy, Fluorescence, Nerve Tissue Proteins, Neurons, Oligodendroglia, Protein Conformation, Microscopy, Immunoelectron, tau Proteins, Neurodegenerative Diseases, Protein Isoforms, Tauopathies, Mice, Synucleins, alpha-Synuclein
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