The amyloid-cell membrane system. The interplay between the biophysical features of oligomers/fibrils and cell membrane defines amyloid toxicity

Biophysical Chemistry

Volumn 182, Issue , 2013, Pages 30-43

  Cecchi, Cristina ^a   Stefani, Massimo ^a  

^a UNIVERSITY OF FLORENCE   (Italy)

Author keywords

Amyloid; Amyloid oligomers; Amyloid toxicity; Protein aggregation; Protein misfolding

Indexed keywords

ALPHA CRYSTALLIN; AMYLOID; BETA CRYSTALLIN; MEMBRANE LIPID; OLIGOMER;

ARTICLE; CELL MEMBRANE; CELL VIABILITY; CYTOTOXICITY; HYDROPHOBICITY; LIPID BILAYER; LIPID COMPOSITION; LIPID RAFT; MOLECULAR DYNAMICS; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN STRUCTURE; STATIC ELECTRICITY;

AMYLOID; AMYLOID OLIGOMERS; AMYLOID TOXICITY; PROTEIN AGGREGATION; PROTEIN MISFOLDING;

AMYLOID; CELL MEMBRANE; ENDOCYTOSIS; PROTEIN CONFORMATION; PROTEIN FOLDING; SURFACE PROPERTIES;

EID: 84885176987     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2013.06.003     Document Type: Article

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