A Loss of Function Mutant of the Presenilin Homologue SEL-12 Undergoes Aberrant Endoproteolysis in Caenorhabditis elegans and Increases Aβ42 Generation in Human Cells
Open Access
- 1 December 2000
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 275 (52) , 40925-40932
- https://doi.org/10.1074/jbc.m005254200
Abstract
No abstract availableKeywords
This publication has 75 references indexed in Scilit:
- Membrane-anchored aspartyl protease with Alzheimer's disease β-secretase activityNature, 1999
- Purification and cloning of amyloid precursor protein β-secretase from human brainNature, 1999
- Identification of a Novel Aspartic Protease (Asp 2) as β-SecretaseMolecular and Cellular Neuroscience, 1999
- β-Secretase Cleavage of Alzheimer's Amyloid Precursor Protein by the Transmembrane Aspartic Protease BACEScience, 1999
- Membrane Topology of Alzheimer's Disease-related Presenilin 1Journal of Biological Chemistry, 1999
- Translating cell biology into therapeutic advances in Alzheimer's diseaseNature, 1999
- Additional evidence for an eight-transmembrane-domain topology for Caenorhabditis elegans and human presenilinsProceedings of the National Academy of Sciences, 1998
- Protein Topology of Presenilin 1Neuron, 1996
- Membrane Topology of the C. elegans SEL-12 PresenilinNeuron, 1996
- Cellular processing of β-amyloid precursor protein and the genesis of amyloid β-peptidePublished by Elsevier ,1993