γ‐Secretase complexes containing N‐ and C‐terminal fragments of different presenilin origin retain normal γ‐secretase activity

The γ‐secretase complex processes substrate proteins within membranes and consists of four proteins: presenilin (PS), nicastrin, Aph‐1 and Pen‐2. PS harbours the enzymatic activity of the complex, and there are two mammalian PS homologues: PS1 and PS2. PS undergoes endoproteolysis, generating the N‐...

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Veröffentlicht in:	Journal of neurochemistry 2005-11, Vol.95 (3), p.880-890
Hauptverfasser:	Strömberg, Kia, Hansson, Emil M., Laudon, Hanna, Bergstedt, Susanne, Näslund, Jan, Lundkvist, Johan, Lendahl, Urban
Format:	Artikel
Sprache:	eng
Schlagworte:	Alzheimer's disease Amino Acid Sequence Amyloid Precursor Protein Secretases Aspartic Acid Endopeptidases Bacteriology Biological and medical sciences Cell Line Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases Endopeptidases - chemistry Endopeptidases - genetics Endopeptidases - metabolism Enzyme Activation - physiology Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Enzymologic Humans Medical sciences Membrane Proteins - genetics Membrane Proteins - metabolism Microbiology Molecular Sequence Data neurodegenerative disease Neurology nicastrin Notch signalling Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains Peptide Fragments - chemistry Peptide Fragments - genetics Peptide Fragments - metabolism presenilin Presenilin-1 Presenilin-2 Protein Structure, Tertiary Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism γ‐secretase
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