Alzheimer's Disease Amyloid-β Binds Copper and Zinc to Generate an Allosterically Ordered Membrane-penetrating Structure Containing Superoxide Dismutase-like Subunits
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Open Access
- 1 January 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (23) , 20466-20473
- https://doi.org/10.1074/jbc.m100175200
Abstract
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This publication has 62 references indexed in Scilit:
- Aqueous Dissolution of Alzheimer's Disease Aβ Amyloid Deposits by Biometal DepletionJournal of Biological Chemistry, 1999
- DiscussionNeurobiology of Aging, 1999
- Solution structures of micelle-bound amyloid β-(1-40) and β-(1-42) peptides of Alzheimer’s disease 1 1Edited by P. E. WrightJournal of Molecular Biology, 1999
- Oxidative Stress Hypothesis in Alzheimer's DiseasePublished by Elsevier ,1998
- Zinc-induced Alzheimer's Aβ1–40 Aggregation Is Mediated by Conformational FactorsJournal of Biological Chemistry, 1997
- The Soluble Form of Alzheimer′s Amyloid β Protein Is Complexed to High Density Lipoprotein 3 and Very High Density Lipoprotein in Normal Human PlasmaBiochemical and Biophysical Research Communications, 1994
- Rapid induction of Alzheimer A beta amyloid formation by zincScience, 1994
- Reversible Random Coil-.beta.-Sheet Transition of the Alzheimer .beta.-Amyloid Fragment (25-35)Biochemistry, 1994
- Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin NeuropeptidesScience, 1990
- Vesicles of variable sizes produced by a rapid extrusion procedureBiochimica et Biophysica Acta (BBA) - Biomembranes, 1986