The molecular assembly of amyloid Aβ controls its neurotoxicity and binding to cellular proteins

PLoS ONE

Volumn 6, Issue 9, 2011, Pages

  Manzoni, Claudia ^a,e   Colombo, Laura ^a   Bigini, Paolo ^a   Diana, Valentina ^a,f   Cagnotto, Alfredo ^a   Messa, Massimo ^a   Lupi, Monica ^a   Bonetto, Valentina ^a,b   Pignataro, Mauro ^a,b   Airoldi, Cristina ^c   Sironi, Erika ^c   Williams, Alun ^d   Salmona, Mario ^a  

^a MARIO NEGRI INSTITUTE FOR PHARMACOLOGICAL RESEARCH   (Italy)

^b DULBECCO TELETHON INSTITUTE   (Italy)

^c UNIVERSITY OF MILANO BICOCCA   (Italy)

^d UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^e UNIVERSITY COLLEGE LONDON   (United Kingdom)

^f ISTITUTO AUXOLOGICO ITALIANO   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID A PROTEIN; BINDING PROTEIN; CELL PROTEIN; MONOMER; NEUROTOXIN; OLIGOMER; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN (1 42); AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA-PROTEIN (1-42); CATHEPSIN D; HEAT SHOCK PROTEIN; MOLECULAR CHAPERONE GRP78; PEPTIDE FRAGMENT; VIMENTIN;

ANIMAL CELL; ARTICLE; CELL DEATH; CELL MEMBRANE; CELLULAR DISTRIBUTION; CONTROLLED STUDY; CYTOSKELETON; DENDRITIC SPINE; ENDOPLASMIC RETICULUM; IMMUNOHISTOCHEMISTRY; MOLECULAR MECHANICS; MOUSE; NEUROTOXICITY; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN MODIFICATION; STRUCTURE ACTIVITY RELATION; ANIMAL; CELL SURVIVAL; CHEMISTRY; CYTOPLASM; DRUG EFFECT; FAR WESTERN BLOTTING; FLUORESCENCE MICROSCOPY; HUMAN; LYSOSOME; METABOLISM; PROTEIN MULTIMERIZATION; TUMOR CELL LINE;

AMYLOID BETA-PEPTIDES; ANIMALS; BLOTTING, FAR-WESTERN; CATHEPSIN D; CELL LINE, TUMOR; CELL SURVIVAL; CYTOPLASM; CYTOSKELETON; ENDOPLASMIC RETICULUM; HEAT-SHOCK PROTEINS; HUMANS; IMMUNOHISTOCHEMISTRY; LYSOSOMES; MICROSCOPY, FLUORESCENCE; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN MULTIMERIZATION; VIMENTIN;

EID: 80053129900     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0024909     Document Type: Article

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