Mechanism of the Cleavage Specificity of Alzheimer's Disease γ -secretase Identified by Phenylalanine-Scanning Mutagenesis of the Transmembrane Domain of the Amyloid Precursor Protein

Proteolytic processing of the amyloid precursor protein by β -secretase yields A4CT (C99), which is cleaved further by the as yet unknown γ -secretase, yielding the β -amyloid (Aβ) peptide with 40 (Aβ40) or 42 residues (Aβ42). Because the position of γ -secretase cleavage is crucial for the pathogen...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1999-03, Vol.96 (6), p.3053-3058
Hauptverfasser:	Lichtenthaler, Stefan F., Wang, Rong, Grimm, Heike, Uljon, Sacha N., Masters, Colin L., Beyreuther, Konrad
Format:	Artikel
Sprache:	eng
Schlagworte:	Alzheimer Disease - metabolism Alzheimer's disease Alzheimers disease Amino acids Amyloid beta-Protein Precursor - genetics Amyloid beta-Protein Precursor - metabolism Amyloid Precursor Protein Secretases Amyloids Animal models Animals Antibodies Aspartic Acid Endopeptidases Binding Sites - genetics Biological Sciences Cell culture techniques COS Cells Endopeptidases - metabolism Enzymes Humans Mass spectroscopy Membranes Mutagenesis, Site-Directed Mutation Peptides Phenylalanine Plasmids Proteins Substrate Specificity
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