The hairpin conformation of the amyloid β peptide is an important structural motif along the aggregation pathway Topical Issue in honor of Ivano Bertini Guest editors: Lucia Banci, Claudio Luchinat

Journal of Biological Inorganic Chemistry

Volumn 19, Issue 4-5, 2014, Pages 623-634

  Abelein, Axel ^a   Abrahams, Jan Pieter ^b   Danielsson, Jens ^a   Gräslund, Astrid ^a   Jarvet, Jüri ^a,c   Luo, Jinghui ^b   Tiiman, Ann ^a   Wärmländer, Sebastian K T S ^a  

^a STOCKHOLM UNIVERSITY   (Sweden)

^b LEIDEN UNIVERSITY   (Netherlands)

^c NATIONAL INSTITUTE OF CHEMICAL PHYSICS AND BIOPHYSICS   (Estonia)

Author keywords

Alzheimer's disease; Amyloid peptide; Hairpin; Neurotoxicity; Protein aggregation

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; COPPER ION; ZINC ION;

ALPHA HELIX; ALZHEIMER DISEASE; BINDING AFFINITY; ELECTRON MICROSCOPY; HYDROGEN BOND; METAL BINDING; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; REVIEW; ANIMAL; CHEMISTRY; HUMAN; METABOLISM; PROTEIN TERTIARY STRUCTURE;

ALZHEIMER DISEASE; AMYLOID BETA-PEPTIDES; ANIMALS; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 84901911159     PISSN: 09498257     EISSN: 14321327     Source Type: Journal    
DOI: 10.1007/s00775-014-1131-8     Document Type: Review

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