Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases

Journal of Biological Chemistry

Volumn 279, Issue 45, 2004, Pages 46363-46366

  Kayed, Rakez ^a   Sokolov, Yuri ^b   Edmonds, Brian ^a   McIntire, Theresa M ^a   Milton, Saskia C ^a   Hall, James E ^b   Glabe, Charles G ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; DISEASES; HYDRAULIC CONDUCTIVITY; OLIGOMERS; PATHOLOGY; PROTEINS; TOXICITY;

AMYLOID FIBRILLIZATION; GENERIC STRUCTURES; PROTOFIBRILS;

LIPIDS;

AMYLOID; OLIGOMER;

AMINO ACID SEQUENCE; ARTICLE; CELL MEMBRANE DEPOLARIZATION; CHANNEL GATING; DEGENERATIVE DISEASE; FIBER; HUMAN; LIPID BILAYER; MEMBRANE CONDUCTANCE; MOLECULAR WEIGHT; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN CONFORMATION;

AMYLOID; AMYLOID BETA-PROTEIN; CELL MEMBRANE; CHROMATOGRAPHY; ELECTROPHYSIOLOGY; HUMANS; IONS; LIPID BILAYERS; MICROSCOPY, ELECTRON; NEURODEGENERATIVE DISEASES; PEPTIDES; PROTEIN CONFORMATION; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; THIAZOLES; TIME FACTORS; TRANSFECTION;

EID: 8744220663     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.C400260200     Document Type: Article

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