Coordinated and widespread expression of γ-secretase in vivo: evidence for size and molecular heterogeneity
- 30 November 2004
- journal article
- Published by Elsevier BV in Neurobiology of Disease
- Vol. 17 (2), 260-272
- https://doi.org/10.1016/j.nbd.2004.08.002
Abstract
No abstract availableThis publication has 62 references indexed in Scilit:
- Signal Peptide Peptidase Forms a Homodimer That Is Labeled by an Active Site-directed γ-Secretase InhibitorOnline Journal of Public Health Informatics, 2004
- Membrane Topology and Nicastrin-enhanced Endoproteolysis of APH-1, a Component of the γ-Secretase ComplexOnline Journal of Public Health Informatics, 2004
- Detergent-Dependent Dissociation of Active γ-Secretase Reveals an Interaction between Pen-2 and PS1-NTF and Offers a Model for Subunit Organization within the ComplexBiochemistry, 2003
- Presenilins Mutated at Asp-257 or Asp-385 Restore Pen-2 Expression and Nicastrin Glycosylation but Remain Catalytically Inactive in the Absence of Wild Type PresenilinOnline Journal of Public Health Informatics, 2003
- Presenilin-1 and Presenilin-2 Exhibit Distinct yet Overlapping γ-Secretase ActivitiesJournal of Biological Chemistry, 2003
- Reconstitution of γ-secretase activityNature, 2003
- APH-1 Interacts with Mature and Immature Forms of Presenilins and Nicastrin and May Play a Role in Maturation of Presenilin·Nicastrin ComplexesOnline Journal of Public Health Informatics, 2003
- Molecular Analysis of the Presenilin 1 (S182) Gene in “Sporadic” Cases of Alzheimer's Disease: Identification and Characterisation of Unusual Splice VariantsJournal of Neurochemistry, 2002
- A γ‐secretase inhibitor blocks Notch signaling in vivo and causes a severe neurogenic phenotype in zebrafishEMBO Reports, 2002
- Regulated Intramembrane Proteolysis: A Control Mechanism Conserved from Bacteria to HumansCell, 2000