FAD Mutations in Presenilin-1 or Amyloid Precursor Protein Decrease the Efficacy of a γ-Secretase Inhibitor: Evidence for Direct Involvement of PS1 in the γ-Secretase Cleavage Complex
- 31 December 2000
- journal article
- Published by Elsevier in Neurobiology of Disease
- Vol. 7 (6) , 673-681
- https://doi.org/10.1006/nbdi.2000.0322
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- The Transmembrane Aspartates in Presenilin 1 and 2 Are Obligatory for γ-Secretase Activity and Amyloid β-Protein GenerationJournal of Biological Chemistry, 2000
- A Role for Presenilin-1 in Nuclear Accumulation of Ire1 Fragments and Induction of the Mammalian Unfolded Protein ResponseCell, 1999
- Presenilin-1 mutations downregulate the signalling pathway of the unfolded-protein responseNature Cell Biology, 1999
- A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domainNature, 1999
- Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor proteinNature, 1998
- Amyloid precursor protein processing and Aβ 42 deposition in a transgenic mouse model of Alzheimer diseaseProceedings of the National Academy of Sciences, 1997
- Candidate .gamma.-Secretases in the Generation of the Carboxyl Terminus of the Alzheimer's Disease .beta.A4 Amyloid: Possible Involvement of Cathepsin DBiochemistry, 1995
- Cleavage at the amino and carboxyl termini of Alzheimer's amyloid-beta by cathepsin DJournal of Biological Chemistry, 1994
- Rat Ovarian Renin: Characterization and Changes during the Estrous Cycle*Endocrinology, 1988
- Rat kidney renin and cathepsin D: purification and comparison of propertiesBiochemistry, 1983