Structural and thermodynamical properties of CuII amyloid-beta16/28 complexes associated with Alzheimer's disease. (Q53280441)

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29 December 2019

title

Structural and thermodynamical properties of CuII amyloid-beta16/28 complexes associated with Alzheimer's disease (English)

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29 December 2019

5

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29 December 2019

Peter Faller

6

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29 December 2019

Yannick Coppel

3

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29 December 2019

author name string

Luc Guilloreau

1

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29 December 2019

Luminita Damian

2

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29 December 2019

Honoré Mazarguil

4

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29 December 2019

publication date

22 August 2006

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Journal of Biological Inorganic Chemistry

29 December 2019

published in

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29 December 2019

volume

11

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29 December 2019

issue

8

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29 December 2019

page(s)

1024-1038

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https://scigraph.springernature.com/pub.10.1007/s00775-006-0154-1

29 December 2019

exact match

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Coordination abilities of the 1-16 and 1-28 fragments of beta-amyloid peptide towards copper(II) ions: a combined potentiometric and spectroscopic study

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Products of Cu(II)-catalyzed oxidation in the presence of hydrogen peroxide of the 1-10, 1-16 fragments of human and mouse beta-amyloid peptide

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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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Cu2+ Inhibits the Aggregation of Amyloid β-Peptide(1-42) in vitro

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12 December 2020

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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Amyloid precursor protein, presenilins, and alpha-synuclein: molecular pathogenesis and pharmacological applications in Alzheimer's disease.

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The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor

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

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Dramatic aggregation of Alzheimer abeta by Cu(II) is induced by conditions representing physiological acidosis.

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Characterization of Copper Interactions with Alzheimer Amyloid β Peptides

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Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families

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A survey of diamagnetic probes for copper2+ binding to the prion protein. 1H NMR solution structure of the palladium2+ bound single octarepeat

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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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Amyloidosis of Alzheimer's Abeta peptides: solid-state nuclear magnetic resonance, electron paramagnetic resonance, transmission electron microscopy, scanning transmission electron microscopy and atomic force microscopy studies

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Cu(II)-catalyzed oxidation of beta-amyloid peptide targets His13 and His14 over His6: Detection of 2-Oxo-histidine by HPLC-MS/MS.

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Probing copper2+ binding to the prion protein using diamagnetic nickel2+ and 1H NMR: the unstructured N terminus facilitates the coordination of six copper2+ ions at physiological concentrations

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Rapid induction of Alzheimer A beta amyloid formation by zinc.

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Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein

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

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Alzheimer's disease: genes, proteins, and therapy

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Amyloid-beta binds Cu2+ in a mononuclear metal ion binding site

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Tyrosine gated electron transfer is key to the toxic mechanism of Alzheimer's disease beta-amyloid

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12 December 2020

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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12 December 2020

Structure and function of amyloid in Alzheimer's disease

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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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Binding of Zn(II), Cu(II), and Fe(II) ions to Alzheimer's A beta peptide studied by fluorescence

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Dietary Cu stabilizes brain superoxide dismutase 1 activity and reduces amyloid Abeta production in APP23 transgenic mice

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Anion binding to bovine erythrocyte superoxide dismutase. Evidence for multiple binding sites with qualitatively different properties

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12 December 2020

10.1007/S00775-006-0154-1

Identifiers

DOI

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release_njhw6o2rxzfazjzht5ibzjrdlu

29 December 2019

Fatcat ID

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Fatcat

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