Tau aggregation is driven by a transition from random coil to beta sheet structure

Biochimica et Biophysica Acta - Molecular Basis of Disease

Volumn 1739, Issue 2, 2005, Pages 158-166

  Von Bergen, Martin ^a   Barghorn, Stefan ^a   Biernat, Jacek ^a   Mandelkow, Eva Maria ^a   Mandelkow, Eckhard ^a  

^a MAX PLANCK UNIT FOR STRUCTURAL MOLECULAR BIOLOGY   (Germany)

Author keywords

Alzheimer's disease; Cross beta structure; FTDP 17; Paired helical filament; Tau

Indexed keywords

AMYLOID PROTEIN; CONGO RED; HEXAPEPTIDE; TAU PROTEIN;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; BETA SHEET; CHROMOSOME 17; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; FRONTOTEMPORAL DEMENTIA; GENETIC LINKAGE; HUMAN; HUMAN TISSUE; INFRARED SPECTROSCOPY; MICROTUBULE; MISSENSE MUTATION; MORPHOLOGY; PAIRED HELICAL FILAMENT; PARKINSONISM; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN MOTIF; REVIEW; SOLUBILITY; X RAY DIFFRACTION;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; BRAIN CHEMISTRY; CIRCULAR DICHROISM; HUMANS; MODELS, CHEMICAL; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TAU PROTEINS; X-RAY DIFFRACTION;

EID: 10944258455     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2004.09.010     Document Type: Review

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