α-Helix targeting reduces amyloid-β peptide toxicity

Proceedings of the National Academy of Sciences of the United States of America

Volumn 106, Issue 23, 2009, Pages 9191-9196

  Nerelius, C ^a   Sandegren, A ^a   Sargsyan, H ^b   Raunak, R ^b   Leijonmarck, H ^b   Chatterjee, U ^a   Fisahn, A ^b   Imarisio, S ^c   Lomas, D A ^c,d   Crowther, D C ^c   Stromberg R ^b   Johansson, J ^a  

^a SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

^b KAROLINSKA INSTITUTE   (Sweden)

^c UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^d UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Alzheimer's disease; Amyloid fibrils; Neurodegenerative disease; Protein misfolding

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; DECANOIC ACID DERIVATIVE; DIETHYLENETRIAMINE; OLIGOMER;

ALPHA HELIX; ANIMAL TISSUE; ARTICLE; CENTRAL NERVOUS SYSTEM; CONTROLLED STUDY; CYTOTOXICITY; DROSOPHILA MELANOGASTER; HIPPOCAMPUS; HISTOPATHOLOGY; LIFESPAN; LIGAND BINDING; LOCOMOTION; NERVE DEGENERATION; NEUROPATHOLOGY; NEUROPROTECTION; NONHUMAN; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN TARGETING; TRANSGENIC ORGANISM;

AMYLOID; AMYLOID BETA-PROTEIN; ANIMALS; ANIMALS, GENETICALLY MODIFIED; DROSOPHILA MELANOGASTER; HUMANS; MODELS, MOLECULAR; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY;

DROSOPHILA MELANOGASTER;

EID: 67249117859     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0810364106     Document Type: Article

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