Modulation of Amyloid Precursor Protein Metabolism by X11α/Mint-1
Open Access
- 1 December 2000
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 275 (50) , 39302-39306
- https://doi.org/10.1074/jbc.m008453200
Abstract
No abstract availableKeywords
This publication has 48 references indexed in Scilit:
- hFE65L Influences Amyloid Precursor Protein Maturation and SecretionJournal of Neurochemistry, 1999
- Translating cell biology into therapeutic advances in Alzheimer's diseaseNature, 1999
- Mint2/X11‐like colocalizes with the Alzheimer's disease amyloid precursor protein and is associated with neuritic plaques in Alzheimer's diseaseEuropean Journal of Neuroscience, 1999
- X11L2, a New Member of the X11 Protein Family, Interacts with Alzheimer's β-Amyloid Precursor ProteinBiochemical and Biophysical Research Communications, 1999
- Identification of an Evolutionarily Conserved Heterotrimeric Protein Complex Involved in Protein TargetingJournal of Biological Chemistry, 1998
- X11 Interaction with β-Amyloid Precursor Protein Modulates Its Cellular Stabilization and Reduces Amyloid β-Protein SecretionJournal of Biological Chemistry, 1998
- The X11α Protein Slows Cellular Amyloid Precursor Protein Processing and Reduces Aβ40 and Aβ42 SecretionJournal of Biological Chemistry, 1998
- The Phosphotyrosine Interaction Domains of X11 and FE65 Bind to Distinct Sites on the YENPTY Motif of Amyloid Precursor ProteinMolecular and Cellular Biology, 1996
- Association of a novel human FE65-like protein with the cytoplasmic domain of the beta-amyloid precursor protein.Proceedings of the National Academy of Sciences, 1996
- The Regions of the Fe65 Protein Homologous to the Phosphotyrosine Interaction/Phosphotyrosine Binding Domain of Shc Bind the Intracellular Domain of the Alzheimer's Amyloid Precursor ProteinJournal of Biological Chemistry, 1995