Aβ42 oligomers, but not fibrils, simultaneously bind to and cause damage to ganglioside-containing lipid membranes

Biochemical Journal

Volumn 439, Issue 1, 2011, Pages 67-77

  William, Thomas L ^a,c   Johnson, Benjamin R G ^b   Urbanc, Brigita ^c   Jenkins, A Toby A ^d   Connell, Simon D A ^b   Serpell, Louise C ^a  

^a UNIVERSITY OF SUSSEX   (United Kingdom)

^b UNIVERSITY OF LEEDS   (United Kingdom)

^c DREXEL UNIVERSITY   (United States)

^d University of Bath Claverton Down   (United Kingdom)

Author keywords

Alzheimer's disease; Amyloid peptide; Atomic force microscopy; GM1 ganglioside; Membrane bilayer; Protein misfolding; Surface plasmon field enhanced fluorescence spectroscopy

Indexed keywords

AMYLOID BETA PROTEIN; GANGLIOSIDE; OLIGOMER;

ALZHEIMER DISEASE; ARTICLE; BIOMIMETICS; CELL VACUOLE; CONTROLLED STUDY; CYTOTOXICITY; FIBER; FLUORESCENCE SPECTROSCOPY; IN VITRO STUDY; LIPID BILAYER; LIPID MEMBRANE; MEMBRANE DAMAGE; MEMBRANE TRANSPORT; PRIORITY JOURNAL; PROTEIN AGGREGATION;

AMYLOID BETA-PEPTIDES; LIPID BILAYERS; MICROSCOPY, ATOMIC FORCE; MICROSCOPY, ELECTRON, TRANSMISSION; PROTEIN BINDING; SPECTROMETRY, FLUORESCENCE;

EID: 80052747064     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20110750     Document Type: Article

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