High resolution scanning tunnelling microscopy of the β-amyloid protein (Aβ1-40) of Alzheimer's disease suggests a novel mechanism of oligomer assembly

Journal of Structural Biology

Volumn 155, Issue 1, 2006, Pages 104-110

  Losic, Dusan ^a,b   Martin, Lisandra L ^a   Mechler, Adam ^a   Aguilar, Marie Isabel ^a   Small, David H ^a  

^a MONASH UNIVERSITY   (Australia)

^b FLINDERS UNIVERSITY   (Australia)

Author keywords

Alzheimer's disease; Amyloid; Fibril; Fibrillogenesis; Protofibril; Scanning tunnelling microscopy

Indexed keywords

AMYLOID BETA PROTEIN; POLYPEPTIDE;

ALZHEIMER DISEASE; ARTICLE; HUMAN; MOLECULAR WEIGHT; PATHOGENESIS; PRIORITY JOURNAL; SCANNING ELECTRON MICROSCOPY; SCANNING TUNNELING MICROSCOPY; SURFACE PROPERTY;

ALZHEIMER DISEASE; AMYLOID BETA-PROTEIN; HUMANS; MICROSCOPY, SCANNING TUNNELING; PEPTIDE FRAGMENTS; POLYMERS;

EID: 33744966120     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2006.02.013     Document Type: Article

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