The chaperone domain BRICHOS prevents CNS toxicity of amyloid-β peptide in Drosophila melanogaster

DMM Disease Models and Mechanisms

Volumn 7, Issue 6, 2014, Pages 659-665

  Hermansson, Erik ^a   Schultz, Sebastian ^b   Crowther, Damian ^c   Linse, Sara ^d   Winblad, Bengt ^a   Westermark, Gunilla ^e   Johansson, Jan ^a,f,g   Presto, Jenny ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

^b OSLO UNIVERSITY HOSPITAL   (Norway)

^c UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^d LUND UNIVERSITY   (Sweden)

^e UPPSALA UNIVERSITY   (Sweden)

^f SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

^g TALLINN UNIVERSITY   (Estonia)

Author keywords

Alzheimer's disease; Amyloid; Chaperone; Protein misfolding

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; CHAPERONE; PROTEIN BRICHOS; UNCLASSIFIED DRUG; AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DROSOPHILA MELANOGASTER; FEMALE; IN VITRO STUDY; LIFESPAN; LOCOMOTION; LONGEVITY; NEUROTOXICITY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; TRANSGENIC DROSOPHILA; ANIMAL; BRAIN; CENTRAL NERVOUS SYSTEM; DRUG EFFECTS; METABOLISM; MOTOR ACTIVITY; PHYSIOLOGY; TOXICITY; TRANSGENIC ANIMAL;

AMYLOID BETA-PEPTIDES; ANIMALS; ANIMALS, GENETICALLY MODIFIED; BRAIN; CENTRAL NERVOUS SYSTEM; DROSOPHILA MELANOGASTER; MOLECULAR CHAPERONES; MOTOR ACTIVITY; PEPTIDE FRAGMENTS;

EID: 84902267654     PISSN: 17548403     EISSN: 17548411     Source Type: Journal    
DOI: 10.1242/dmm.014787     Document Type: Article

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