Direct evidence for self-propagation of different amyloid-ß fibril conformations

Neurodegenerative Diseases

Volumn 14, Issue 3, 2014, Pages 151-159

  Spirig, Thomas ^a   Ovchinnikova, Oxana ^a   Vagt, Toni ^a   Glockshuber, Rudi ^a  

^a ETH ZURICH   (Switzerland)

Author keywords

Aggregation; Alzheimer's disease; Electron microscopy; Prion; Thioflavin T

Indexed keywords

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

ALZHEIMER DISEASE; ARTICLE; CONTROLLED STUDY; DISSOCIATION CONSTANT; ELECTRON MICROSCOPY; ENZYME LINKED IMMUNOSORBENT ASSAY; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; GENE MUTATION; MICROPLATE READER; OSAKA MUTATION; PROTEIN CONFORMATION; PROTEIN QUATERNARY STRUCTURE; SELF PROPAGATION; THERMODYNAMICS; THIOFLAVIN T FLUORESCENCE; WILD TYPE; ESCHERICHIA COLI; GENETICS; HUMAN; KINETICS; METABOLISM; MUTATION; SPECTROFLUOROMETRY; TRANSMISSION ELECTRON MICROSCOPY;

AMYLOID; AMYLOID BETA-PEPTIDES; ESCHERICHIA COLI; HUMANS; KINETICS; MICROSCOPY, ELECTRON, TRANSMISSION; MUTATION; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, QUATERNARY; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS;

EID: 84912128384     PISSN: 16602854     EISSN: 16602862     Source Type: Journal    
DOI: 10.1159/000363623     Document Type: Article

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