Significant structural differences between transient amyloid-β oligomers and less-toxic fibrils in regions known to harbor familial Alzheimer's mutations

Angewandte Chemie - International Edition

Volumn 53, Issue 27, 2014, Pages 6888-6892

  Sarkar, Bidyut ^a   Mithu, Venus Singh ^a   Chandra, Bappaditya ^a   Mandal, Arghya ^a   Chandrakesan, Muralidharan ^b   Bhowmik, Debanjan ^a   Madhu, Perunthiruthy K ^a,c   Maiti, Sudipta ^a  

^a TATA INSTITUTE OF FUNDAMENTAL RESEARCH   (India)

^b KEM HOSPITAL   (India)

^c TATA INSTITUTE OF FUNDAMENTAL RESEARCH   (India)

Author keywords

amyloid peptides; NMR spectroscopy; protein folding; toxic oligomers; transient structures

Indexed keywords

CELL MEMBRANES; CYTOLOGY; FLUORESCENCE; GLYCOPROTEINS; NEURODEGENERATIVE DISEASES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDES; PROTEIN FOLDING; SOLID STATE PHYSICS; TOXICITY;

ALZHEIMER'S DISEASE; FLUORESCENCE TECHNIQUE; HYDROPHOBIC REGIONS; PHYSIOLOGICAL CONDITION; PROTEIN STRUCTURES; STRUCTURAL DIFFERENCES; STRUCTURAL INVESTIGATION; TRANSIENT STRUCTURE;

OLIGOMERS;

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; PEPTIDE FRAGMENT;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; CELL MEMBRANE; CHEMICAL PHENOMENA; DRUG EFFECTS; GENETICS; HUMAN; METABOLISM; MUTATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PATHOLOGY; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AMYLOID BETA-PEPTIDES; CELL MEMBRANE; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MAGNETIC RESONANCE SPECTROSCOPY; MUTATION; PEPTIDE FRAGMENTS; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY;

EID: 84903267298     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201402636     Document Type: Article

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