Asparagine residue 368 is involved in Alzheimer's disease tau strain–specific aggregation

In tauopathies, tau forms pathogenic fibrils with distinct conformations (termed “tau strains”) and acts as an aggregation “seed” templating the conversion of normal tau into isomorphic fibrils. Previous research showed that the aggregation core of tau fibril covers the C-terminal region (243–406 am...

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Veröffentlicht in:	The Journal of biological chemistry 2020-10, Vol.295 (41), p.13996-14014
Hauptverfasser:	Shimonaka, Shotaro, Matsumoto, Shin-Ei, Elahi, Montasir, Ishiguro, Koichi, Hasegawa, Masato, Hattori, Nobutaka, Motoi, Yumiko
Format:	Artikel
Sprache:	eng
Schlagworte:	Alzheimer Disease - genetics Alzheimer Disease - metabolism Amino Acid Sequence Asparagine - chemistry Asparagine - genetics Asparagine - metabolism Cell Line, Tumor Humans Molecular Bases of Disease neurodegenerative disease prion protein aggregation Protein Aggregation, Pathological - genetics Protein Aggregation, Pathological - metabolism protein misfolding seed Sequence Deletion tau protein tau Proteins - chemistry tau Proteins - genetics tau Proteins - metabolism tau strain tauopathy
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