Aβ dimers differ from monomers in structural propensity, aggregation paths and population of synaptotoxic assemblies

Biochemical Journal

Volumn 461, Issue 3, 2014, Pages 413-426

  O'Malley, Tiernan T ^a,b   Oktaviani, Nur Alia ^c   Zhang, Dainan ^d   Lomakin, Aleksey ^e   O'Nuallain, Brian ^a   Linse, Sara ^f   Benedek, George B ^e   Rowan, Michael J ^d   Mulder, Frans A A ^c,g   Walsh, Dominic M ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b UNIVERSITY COLLEGE DUBLIN   (Ireland)

^c UNIVERSITY OF GRONINGEN   (Netherlands)

^d TRINITY COLLEGE DUBLIN   (Ireland)

^e MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^f LUND UNIVERSITY   (Sweden)

^g AARHUS UNIVERSITY   (Denmark)

Author keywords

Alzheimer's disease; Amyloid protein; Long term potentiation; Nuclear magnetic resonance (NMR); Synaptic plasticity

Indexed keywords

AMYLOID BETA PROTEIN(M1-40); AMYLOID BETA PROTEIN[1-40]; CYSTEINE; CYSTINE; DIMER; MONOMER; RECOMBINANT PROTEIN; SERINE; SYNTHETIC PEPTIDE; TYROSINE; UNCLASSIFIED DRUG; [AMYLOID BETA PROTEIN(M1-40)S26C]2; [AMYLOID BETA PROTEIN(M1-40)]DIY;

ALKALINITY; ALZHEIMER DISEASE; ANIMAL EXPERIMENT; ARTICLE; CELL DENSITY; CELL INCLUSION; CONTROLLED STUDY; CROSS LINKING; DIMERIZATION; ELECTRODE IMPLANT; ESCHERICHIA COLI; EXCITATORY POSTSYNAPTIC POTENTIAL; LIGHT SCATTERING; LONG TERM POTENTIATION; LOW TEMPERATURE; MALE; NERVE CELL PLASTICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; RAT; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; SIGNAL TRANSDUCTION; SYNAPTIC TRANSMISSION;

ALZHEIMER DISEASE; AMINO ACID SUBSTITUTION; AMYLOID BETA-PEPTIDES; ANIMALS; CEREBELLUM; DIMERIZATION; EVOKED POTENTIALS; HUMANS; INJECTIONS, INTRAVENTRICULAR; KINETICS; LONG-TERM POTENTIATION; MALE; NERVE TISSUE PROTEINS; NEURONS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; RATS; RATS, WISTAR; RECOMBINANT PROTEINS; SOLUBILITY; SYNAPSES;

EID: 84903174803     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20140219     Document Type: Article

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