期刊
FEBS LETTERS
卷 592, 期 14, 页码 2383-2391出版社
WILEY
DOI: 10.1002/1873-3468.13108
关键词
molecular conformers; ordered assembly; Tau isoforms; Tau protein
资金
- UK Medical Research Council [MC_U105184291]
- MRC [MC_U105184291] Funding Source: UKRI
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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