Comparison of the aggregation properties, secondary structure and apoptotic effects of wild-type, Flemish and Dutch N-terminally truncated amyloid β peptides

European Journal of Neuroscience

Volumn 13, Issue 11, 2001, Pages 2015-2024

  Demeester, N ^a   Mertens, C ^a   Caster, H ^a   Goethals, M ^a   Vandekerckhove, J ^a   Rosseneu, M ^a   Labeur, C ^a  

^a GHENT UNIVERSITY   (Belgium)

Author keywords

Alzheimer's disease; Caspase 3; DNA laddering; Secondary structure

Indexed keywords

AMYLOID BETA PROTEIN; BUFFER; CASPASE 3; DNA; MUTANT PROTEIN; PROPIDIUM IODIDE; TRIFLUOROETHANOL;

ALPHA HELIX; ALZHEIMER DISEASE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; APOPTOSIS; ARTICLE; BETA SHEET; CANCER CELL CULTURE; CIRCULAR DICHROISM; CONCENTRATION RESPONSE; CONTROLLED STUDY; CYTOTOXICITY; DNA DAMAGE; ENZYME ACTIVITY; INCUBATION TIME; NERVE CELL CULTURE; NONHUMAN; PHEOCHROMOCYTOMA CELL; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN SECONDARY STRUCTURE; RAT;

ALZHEIMER DISEASE; AMYLOID BETA-PROTEIN; APOPTOSIS; BRAIN CHEMISTRY; CASPASE 3; CASPASES; CEREBRAL CORTEX; CIRCULAR DICHROISM; DNA FRAGMENTATION; DNA MUTATIONAL ANALYSIS; DOSE-RESPONSE RELATIONSHIP, DRUG; HUMANS; MUTATION; NEPHELOMETRY AND TURBIDIMETRY; NEURONS; PEPTIDE FRAGMENTS; PROPIDIUM; PROTEIN STRUCTURE, SECONDARY; TRIFLUOROETHANOL;

EID: 0034954544     PISSN: 0953816X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.0953-816X.2001.01579.x     Document Type: Article

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