The DOI matches its Crossref record; 66 of the 66 references it cites were found in a registry or an index.
Tau filaments in neurodegenerative diseases
Open accessAbstract
The ordered assembly of Tau protein into abnormal filamentous inclusions is a defining characteristic of many human neurodegenerative diseases. Thirty years ago, we reported that Tau is an integral component of the intraneuronal filaments of Alzheimer's disease. All six brain Tau isoforms make up those filaments. Twenty years ago, we and others showed that mutations in MAPT, the Tau gene, cause familial forms of frontotemporal dementia, thus proving that dysfunction of Tau protein is sufficient to cause neurodegeneration and dementia. More recently, we showed that high‐resolution structures of Tau filaments from human brain can be determined by electron cryo‐microscopy. These filaments may form the seeds that underlie the prion‐like properties of aggregated tau.
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“In AD, tau becomes truncated and hyperphosphorylated (3), which can increase the risk for tau to aggregate into the paired helical filaments (PHF) that are found in neurofibrillary tangles (NFT) and neuropil treads in the brains of patients with AD (1).”
From Aβ deposition is associated with increases in soluble and phosphorylated tau that precede a positive tau PET in Alzheimer's disease (2020) · cites this paper as [1]
In the citing paper
“Accumulation of Aβ fibrils is thought to be an initiating factor in AD and necessary for the formation of tau aggregates (1).”
From Aβ deposition is associated with increases in soluble and phosphorylated tau that precede a positive tau PET in Alzheimer's disease (2020) · cites this paper as [1]
Citations
Cites
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Self-citationImaging brain amyloid in Alzheimer's disease with Pittsburgh Compound‐B
Klunk, W. E., Engler, H., Nordberg, A., Wang, Y., Blomqvist, G., Holt, D. P., Bergström, M., Savitcheva, I., Huang, G., Estrada, S., et al. (2004) · Annals of Neurology · doi:10.1002/ana.20009 · Cited by 4,496
Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498
Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492
Self-citationCryo-EM structures of tau filaments from Alzheimer’s disease
Fitzpatrick, A. W. P., Falcon, B., He, S., Murzin, A. G., Murshudov, G., Garringer, H. J., Crowther, R. A., Ghetti, B., Goedert, M., & Scheres, S. H. W. (2017) · Nature · doi:10.1038/nature23002 · Cited by 2,061
Self-citationMutation in the tau gene in familial multiple system tauopathy with presenile dementia
Spillantini, M. G., Murrell, J. R., Goedert, M., Farlow, M. R., Klug, A., & Ghetti, B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7737 · Cited by 1,474
Self-citationTau is a candidate gene for chromosome 17 frontotemporal dementia
Poorkaj, P., Bird, T. D., Wijsman, E., Nemens, E., Garruto, R. M., Anderson, L., Andreadis, A., Wiederholt, W. C., Raskind, M., & Schellenberg, G. D. (1998) · Annals of Neurology · doi:10.1002/ana.410430617 · Cited by 1,374
Goedert, M., Wischik, C. M., Crowther, R. A., Walker, J. E., & Klug, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.11.4051 · Cited by 1,134
Self-citationGoedert, M., Spillantini, M. G., Cairns, N. J., & Crowther, R. A. (1992) · Neuron · doi:10.1016/0896-6273(92)90117-v · Cited by 1,122
Self-citationTau protein liquid–liquid phase separation can initiate tau aggregation
Wegmann, S., Eftekharzadeh, B., Tepper, K., Zoltowska, K. M., Bennett, R. E., Dujardin, S., Laskowski, P. R., MacKenzie, D., Kamath, T., Commins, C., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201798049 · Cited by 1,102
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Mattsson-Carlgren, N., Andersson, E., Janelidze, S., Ossenkoppele, R., Insel, P., Strandberg, O., Zetterberg, H., Rosen, H. J., Rabinovici, G., Chai, X., et al. (2020) · Science Advances · doi:10.1126/sciadv.aaz2387 · Cited by 359
“In AD, tau becomes truncated and hyperphosphorylated (3), which can increase the risk for tau to aggregate into the paired helical filaments (PHF) that are found in neurofibrillary tangles (NFT) and neuropil treads in the brains of patients with AD (1).”
Leuzy, A., Smith, R., Ossenkoppele, R., Santillo, A., Borroni, E., Klein, G., Ohlsson, T., Jögi, J., Palmqvist, S., Mattsson-Carlgren, N., et al. (2020) · JAMA Neurology · doi:10.1001/jamaneurol.2020.0989 · Cited by 222
Enzymatic Noncovalent Synthesis
He, H., Tan, W., Guo, J., Yi, M., Shy, A. N., & Xu, B. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00306 · Cited by 225
Autophagic and endo-lysosomal dysfunction in neurodegenerative disease
Malik, B. R., Maddison, D. C., Smith, G. A., & Peters, O. M. (2019) · Molecular Brain · doi:10.1186/s13041-019-0504-x · Cited by 187
Roles and Mechanisms of Gut Microbiota in Patients With Alzheimer’s Disease
Wu, S., Liu, X., Jiang, R., Yan, X., & Ling, Z. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.650047 · Cited by 150
Metadata
- Authors
- Goedert, M.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Corresponding author
- Goedert, Michel
- ORCID
- Goedert, Michel
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2018-07
- Volume
- 592
- Issue
- 14
- Pages
- 2383-2391
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2803767896
- Cited by
- 127
- References
- 66
- Citations by year
- 2026: 4 · 2025: 14 · 2024: 9 · 2023: 22 · 2022: 22 · 2021: 21 · 2020: 19 · 2019: 13 · 2018: 3
- FWCI
- 1.84
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- tau protein, tau filaments, neurodegenerative diseases, Alzheimer's disease, frontotemporal dementia, MAPT mutations, tau isoforms, protein aggregation, prion-like seeding
- MeSH terms
- Alzheimer Disease, Animals, Brain, Humans, tau Proteins, Neurodegenerative Diseases, Protein Isoforms, Protein Aggregation, Pathological, Protein Aggregates
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