Uptake and pathogenic effects of amyloid beta peptide 1–42 are enhanced by integrin antagonists and blocked by NMDA receptor antagonists
- 21 June 2002
- journal article
- Published by Elsevier in Neuroscience
- Vol. 112 (4) , 827-840
- https://doi.org/10.1016/s0306-4522(02)00132-x
Abstract
No abstract availableKeywords
This publication has 95 references indexed in Scilit:
- Peripherally administered antibodies against amyloid β-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer diseaseNature Medicine, 2000
- Inflammation and Alzheimer's diseaseNeurobiology of Aging, 2000
- Integrin-type signaling has a distinct influence on NMDA-induced cytoskeletal disassemblyJournal of Neuroscience Research, 2000
- Glycoprotein IIb/IIIa Antagonists Induce Apoptosis in Rat Cardiomyocytes by Caspase-3 ActivationPublished by Elsevier ,2000
- Amyloid ? protein is internalized selectively by hippocampal field CA1 and causes neurons to accumulate amyloidogenic carboxyterminal fragments of the amyloid precursor proteinJournal of Comparative Neurology, 1998
- Arg-Gly-Asp-Ser-Selective Adhesion and the Stabilization of Long-Term Potentiation: Pharmacological Studies and the Characterization of a Candidate Matrix ReceptorJournal of Neuroscience, 1997
- Matrix Metalloproteinase-9 (MMP-9) Is Synthesized in Neurons of the Human Hippocampus and Is Capable of Degrading the Amyloid-β Peptide (1–40)Journal of Neuroscience, 1996
- Stable maintenance of glutamate receptors and other synaptic components in long‐term hippocampal slicesHippocampus, 1995
- Purification of an Arg-Gly-Asp selective matrix receptor from brain synaptic plasma membranesBiochemical Journal, 1992
- Fibronectin binding by brain synaptosomal membranes may not involve conventional integrinsNeuroReport, 1991