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A nine-transmembrane domain topology for presenilin 1.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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2005 (English)In: J Biol Chem, ISSN 0021-9258, Vol. 280, no 42, 35352-60 p.Article in journal (Refereed) Published
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2005. Vol. 280, no 42, 35352-60 p.
Keyword [en]
Amino Acid Sequence, Amyloid Precursor Protein Secretases, Animals, Aspartic Endopeptidases, Binding Sites, Biotinylation, Cell Membrane/*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
URN: urn:nbn:se:su:diva-18894PubMedID: 16046406OAI: diva2:185417
Available from: 2007-12-27 Created: 2007-12-27 Last updated: 2011-01-12Bibliographically approved

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Melén, Karinvon Heijne, Gunnar
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Department of Biochemistry and Biophysics

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