期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 19, 期 10, 页码 -出版社
MDPI
DOI: 10.3390/ijms19102910
关键词
tau amyloid; Alzheimer's disease; tauopathy
资金
- Jagiellonian University-Medical College [K/ZDS/006363, K/ZDS/006366]
- PLGrid Infrastructure-Cyfronet AGH
- University of Science and Technology, Poland
Abnormal filamentous aggregates that are formed by tangled tau protein turn out to be classic amyloid fibrils, meeting all the criteria defined under the fuzzy oil drop model in the context of amyloid characterization. The model recognizes amyloids as linear structures where local hydrophobicity minima and maxima propagate in an alternating manner along the fibril's long axis. This distribution of hydrophobicity differs greatly from the classic monocentric hydrophobic core observed in globular proteins. Rather than becoming a globule, the amyloid instead forms a ribbonlike (or cylindrical) structure.
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