Presenilin-1 differentially facilitates endoproteolysis of the beta-amyloid precursor protein and Notch.

Capell, A; Steiner, H; Romig, H; Keck, S; Baader, M; Grim, M G; Baumeister, R; Haass, C

Capell, A; Steiner, H; Romig, H; Keck, S; Baader, M; Grim, M G; Baumeister, R; Haass, C.

Affiliation

Capell A; Adolf Butenandt-Institute, Department of Biochemistry, Laboratory for Alzheimer's Disease Research, Ludwig-Maximilians-University, 80336 Munich, Germany.

Nat Cell Biol ; 2(4): 205-11, 2000 Apr.

Article in En | MEDLINE | ID: mdl-10783238

Subject(s)

Amyloid beta-Protein Precursor/metabolism; Membrane Proteins/genetics; Membrane Proteins/metabolism; Point Mutation; Alternative Splicing/physiology; Antibodies, Monoclonal; Aspartic Acid; Cell Line; Cell Membrane/chemistry; Cell Membrane/metabolism; Epitopes/genetics; Exons; Gene Expression/physiology; Humans; Kidney/cytology; Membrane Proteins/immunology; Presenilin-1; Receptors, Notch; Signal Transduction/physiology

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Collection: 01-internacional Database: MEDLINE Main subject: Amyloid beta-Protein Precursor / Point Mutation / Membrane Proteins Limits: Humans Language: En Journal: Nat Cell Biol Year: 2000 Document type: Article Affiliation country: Germany Country of publication: United kingdom

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