A Nine-transmembrane Domain Topology for Presenilin 1

Presenilin (PS) provides the catalytic core of the γ-secretase complex. γ-Secretase activity leads to generation of the amyloid β-peptide, a key event implicated in the pathogenesis of Alzheimer disease. PS has ten hydrophobic regions, which can all theoretically form membrane-spanning domains. Vari...

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Veröffentlicht in:	The Journal of biological chemistry 2005-10, Vol.280 (42), p.35352-35360
Hauptverfasser:	Laudon, Hanna, Hansson, Emil M., Melén, Karin, Bergman, Anna, Farmery, Mark R., Winblad, Bengt, Lendahl, Urban, von Heijne, Gunnar, Näslund, Jan
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amyloid Precursor Protein Secretases Animals Aspartic Acid Endopeptidases Aspartic Endopeptidases Binding Sites Biotinylation Cell Membrane - metabolism Cytosol - chemistry Cytosol - metabolism Cytosol/chemistry/metabolism Endopeptidases - chemistry Endoplasmic Reticulum - metabolism Extracellular Matrix - metabolism Gene Deletion Genes, Reporter Glycoside Hydrolases - pharmacology Glycosylation Humans Immunoblotting Immunohistochemistry Immunoprecipitation Luciferases - metabolism Membrane Proteins - chemistry Mice Molecular Sequence Data Presenilin-1 Protein Binding Protein Structure, Tertiary Sequence Homology, Amino Acid Streptavidin - chemistry
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