The Proteolytic Fragments of the Alzheimer's Disease-associated Presenilin-1 Form Heterodimers and Occur as a 100–150-kDa Molecular Mass Complex-Reference-Cited by-同舟云学术

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The Proteolytic Fragments of the Alzheimer's Disease-associated Presenilin-1 Form Heterodimers and Occur as a 100–150-kDa Molecular Mass Complex

Published:1998-02 Issue:6 Volume:273 Page:3205-3211
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Capell Anja,Grünberg Jürgen,Pesold Brigitte,Diehlmann Anke,Citron Martin,Nixon Ralph,Beyreuther Konrad,Selkoe Dennis J.,Haass Christian

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference45 articles.

1. Endoproteolysis of Presenilin 1 and Accumulation of Processed Derivatives In Vivo

2. Human presenilin-1, but not familial Alzheimer’s disease (FAD) mutants, facilitate Caenorhabditis elegans Notch signalling independently of proteolytic processing

3. Assessment of normal and mutant human presenilin function in Caenorhabditis elegans

4. Hyperaccumulation of FAD-linked presenilin 1 variants in vivo

5. Amyloid β-Protein and the Genetics of Alzheimer's Disease

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