Copper-mediated amyloid-beta toxicity is associated with an intermolecular histidine bridge. (Q53378253)

13 May 2018

title

Copper-mediated amyloid-beta toxicity is associated with an intermolecular histidine bridge. (English)

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3

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Ashley I. Bush

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Frances Šeparović

13

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Roberto Cappai

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David Smith

David P Smith

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John D Wade

John D Wade

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Simon C Drew

Simon C Drew

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Colin L. Masters

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Colin L Masters

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Keyla Perez

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Giuseppe Donato Ciccotosto

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Giuseppe D Ciccotosto

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Kevin J Barnham

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Kevin J Barnham

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Deborah J Tew

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Deborah J Tew

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author name string

Danielle G Smith

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John F Boas

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John R Pilbrow

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Tong-Lay Lau

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language of work or name

English

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publication date

4 April 2006

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13 May 2018

Journal of Biological Chemistry

number of pages

10

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based on heuristic

inferred from page(s)

published in

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volume

281

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issue

22

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page(s)

15145-15154

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The metallobiology of Alzheimer's disease

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Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits

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Metal ions, pH, and cholesterol regulate the interactions of Alzheimer's disease amyloid-beta peptide with membrane lipid

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Methylation of the imidazole side chains of the Alzheimer disease amyloid-beta peptide results in abolition of superoxide dismutase-like structures and inhibition of neurotoxicity

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Cu(II) potentiation of alzheimer abeta neurotoxicity. Correlation with cell-free hydrogen peroxide production and metal reduction.

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Copper binding to the amyloid-beta (Abeta) peptide associated with Alzheimer's disease: folding, coordination geometry, pH dependence, stoichiometry, and affinity of Abeta-(1-28): insights from a range of complementary spectroscopic techniques

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N-Terminal deletions modify the Cu2+ binding site in amyloid-beta

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Structural changes of region 1-16 of the Alzheimer disease amyloid beta-peptide upon zinc binding and in vitro aging

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The channel hypothesis of Alzheimer's disease: current status

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Disruption of calcium homeostasis in the pathogenesis of Alzheimer's disease and other conformational diseases

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Alzheimer disease beta-amyloid activity mimics cholesterol oxidase

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Improved preparation of amyloid-beta peptides using DBU as Nalpha-Fmoc deprotection reagent.

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Copper mediates dityrosine cross-linking of Alzheimer's amyloid-beta

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Structural implications derived from the analysis of electron paramagnetic resonance spectra of natural and artificial copper proteins.

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Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice.

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Metal-protein attenuation with iodochlorhydroxyquin (clioquinol) targeting Abeta amyloid deposition and toxicity in Alzheimer disease: a pilot phase 2 clinical trial

21 January 2018

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Clioquinol, a drug for Alzheimer's disease specifically interfering with brain metal metabolism: structural characterization of its zinc(II) and copper(II) complexes

21 January 2018

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Zinc-induced Alzheimer's Abeta1-40 aggregation is mediated by conformational factors.

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Hydrogen peroxide mediates amyloid beta protein toxicity

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Two types of Alzheimer's beta-amyloid (1-40) peptide membrane interactions: aggregation preventing transmembrane anchoring versus accelerated surface fibril formation.

21 January 2018

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Cholesterol is necessary both for the toxic effect of Abeta peptides on vascular smooth muscle cells and for Abeta binding to vascular smooth muscle cell membranes

21 January 2018

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Metal ion-dependent effects of clioquinol on the fibril growth of an amyloid {beta} peptide

21 January 2018

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Cholesterol is an important factor affecting the membrane insertion of beta-amyloid peptide (A beta 1-40), which may potentially inhibit the fibril formation

21 January 2018

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The Aβ Peptide of Alzheimer's Disease Directly Produces Hydrogen Peroxide through Metal Ion Reduction†

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M600417200

1 reference

13 May 2018

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13 May 2018