The Notch Ligands, Delta1 and Jagged2, Are Substrates for Presenilin-dependent “γ-Secretase” Cleavage
Open Access
- 1 March 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (10) , 7751-7754
- https://doi.org/10.1074/jbc.c200711200
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Nectin-1α, an Immunoglobulin-like Receptor Involved in the Formation of Synapses, Is a Substrate for Presenilin/γ-Secretase-like CleavageJournal of Biological Chemistry, 2002
- Presenilin-dependent Intramembrane Proteolysis of CD44 Leads to the Liberation of Its Intracellular Domain and the Secretion of an Aβ-like PeptideJournal of Biological Chemistry, 2002
- Proteolytic Processing of Low Density Lipoprotein Receptor-related Protein Mediates Regulated Release of Its Intracellular DomainJournal of Biological Chemistry, 2002
- A presenilin-1/gamma-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctionsThe EMBO Journal, 2002
- γ-Secretase Cleavage and Nuclear Localization of ErbB-4 Receptor Tyrosine KinaseScience, 2001
- A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domainNature, 1999
- Presenilin is required for activity and nuclear access of Notch in DrosophilaNature, 1999
- ALZHEIMER'S DISEASE: Genetic Studies and Transgenic ModelsAnnual Review of Genetics, 1998
- Effects of PS1 Deficiency on Membrane Protein Trafficking in NeuronsNeuron, 1998
- Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor proteinNature, 1998