The N-terminal region of non-Aβ component of Alzheimer's disease amyloid is responsible for its tendency to assume β-sheet and aggregate to form fibrils

European Journal of Biochemistry

Volumn 258, Issue 1, 1998, Pages 157-163

  El Agnaf, Omar M A ^a   Bodles, Angela M ^a   Guthrie, David J S ^a   Harriott, Patrick ^a   Irvine, G Brent ^a  

^a QUEEN'S UNIVERSITY BELFAST   (United Kingdom)

Author keywords

synuclein; Alzheimer's; Amyloid; Circular dichroism; Non A component of Alzheimer's disease amyloid

Indexed keywords

ACETONITRILE; AMYLIN; AMYLOID BETA PROTEIN; AMYLOID PROTEIN; CONGO RED; PEPTIDE FRAGMENT; PRION PROTEIN; TRIFLUOROETHANOL;

ALPHA HELIX; ALZHEIMER DISEASE; AMINO TERMINAL SEQUENCE; ARTICLE; CIRCULAR DICHROISM; DEGENERATIVE DISEASE; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN SECONDARY STRUCTURE;

AGING; ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AMYLOID; CIRCULAR DICHROISM; HUMANS; MICROSCOPY, ELECTRON; MOLECULAR SEQUENCE DATA; NEUROFIBRILS; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY;

EID: 0032533733     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2580157.x     Document Type: Article

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