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Article

FTD-tau S320F mutation stabilizes local structure and allosterically promotes amyloid motif-dependent aggregation

2022-08-13

Abstract excerpt

Amyloid deposition of the microtubule-associated protein tau is a unifying theme in a multitude of neurodegenerative diseases. Disease-associated missense mutations in tau are associated with frontotemporal dementia (FTD) and enhance tau aggregation propensity. However, the molecular mechanism of how mutations in tau promote tau assembly into amyloids remains obscure. There is a need to understand how tau folds in...

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Identifiers and source

Literature Corpus work
7e2ba763-3550-5bb2-a0e4-0c7fbce979aa
DOI
10.1101/2022.08.11.503511
Open publication

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FTD-tau S320F mutation stabilizes local structure and allosterically promotes amyloid motif-dependent aggregationDOI 10.1101/2022.08.11.503511
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