Metal swap between Zn7-metallothionein-3 and amyloid-beta-Cu protects against amyloid-beta toxicity. (Q50335544)

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6 January 2020

title

Metal swap between Zn7-metallothionein-3 and amyloid-beta-Cu protects against amyloid-beta toxicity (English)

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6 January 2020

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7

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6 January 2020

Gabriele Meloni

1

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6 January 2020

Justin Teissie

6

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6 January 2020

author name string

Vanessa Sonois

2

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6 January 2020

Tamara Delaine

3

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6 January 2020

Luc Guilloreau

4

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Audrey Gillet

5

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6 January 2020

Milan Vasák

8

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publication date

4 May 2008

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6 January 2020

published in

Nature Chemical Biology

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6 January 2020

volume

4

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issue

6

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6 January 2020

page(s)

366-372

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https://scigraph.springernature.com/pub.10.1038/nchembio.89

6 January 2020

exact match

0 references

1 reference

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Rapid induction of Alzheimer A beta amyloid formation by zinc.

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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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Evidence that the beta-amyloid plaques of Alzheimer's disease represent the redox-silencing and entombment of abeta by zinc

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Cupric-amyloid beta peptide complex stimulates oxidation of ascorbate and generation of hydroxyl radical

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Metalloenzyme-like activity of Alzheimer's disease beta-amyloid. Cu-dependent catalytic conversion of dopamine, cholesterol, and biological reducing agents to neurotoxic H(2)O(2).

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Metals in our minds: therapeutic implications for neurodegenerative disorders

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Metallothioneins: new functional and structural insights

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The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein

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Three-dimensional structure and dynamics of a brain specific growth inhibitory factor: metallothionein-3

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Evidence for a dynamic structure of human neuronal growth inhibitory factor and for major rearrangements of its metal-thiolate clusters

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Solution structure and dynamics of human metallothionein-3 (MT-3).

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Growth inhibitory factor prevents neurite extension and the death of cortical neurons caused by high oxygen exposure through hydroxyl radical scavenging

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Metallothionein III is reduced in Alzheimer's disease.

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Metallothionein-III antagonizes the neurotoxic and neurotrophic effects of amyloid beta peptides

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Redox silencing of copper in metal-linked neurodegenerative disorders: reaction of Zn7metallothionein-3 with Cu2+ ions.

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7 January 2021

NMR reveals anomalous copper(II) binding to the amyloid Abeta peptide of Alzheimer's disease.

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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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7 January 2021

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

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Formation of mammalian Cu8-metallothionein in vitro: evidence for the existence of two Cu(I)4-thiolate clusters

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7 January 2021

Molecular structure of amyloid fibrils: insights from solid-state NMR.

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7 January 2021

Aluminium, iron, zinc and copper influence the in vitro formation of amyloid fibrils of Abeta42 in a manner which may have consequences for metal chelation therapy in Alzheimer's disease.

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7 January 2021

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

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7 January 2021

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

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7 January 2021

Metal binding and oxidation of amyloid-beta within isolated senile plaque cores: Raman microscopic evidence

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7 January 2021

Amyloid-beta peptide forms monomeric complexes with Cu(II) and Zn(II) prior to aggregation

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7 January 2021

Characterization of the ZnII binding to the peptide amyloid-beta1-16 linked to Alzheimer's disease.

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7 January 2021

The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics

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7 January 2021

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

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7 January 2021

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

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7 January 2021

Concentration dependent Cu2+ induced aggregation and dityrosine formation of the Alzheimer's disease amyloid-beta peptide.

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7 January 2021

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7 January 2021

Protective effect of zinc on amyloid-beta 25-35 and 1-40 mediated toxicity.

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Evidence of oxidative damage in Alzheimer's disease brain: central role for amyloid beta-peptide

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Ascorbate regulation and its neuroprotective role in the brain

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Characterization of Copper Interactions with Alzheimer Amyloid β Peptides

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Effect of the two conserved prolines of human growth inhibitory factor (metallothionein-3) on its biological activity and structure fluctuation: comparison with a mutant protein.

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Sulfur ligation in copper enzymes and models.

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Synthesis, structure, and H2O2-dependent catalytic functions of disulfide-bridged dicopper(I) and related thioether-copper(I) and thioether-copper(II) complexes

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The redox chemistry of the Alzheimer's disease amyloid beta peptide.

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New insights on how metals disrupt amyloid beta-aggregation and their effects on amyloid-beta cytotoxicity

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A Novel Function of Monomeric Amyloid β-Protein Serving as an Antioxidant Molecule against Metal-Induced Oxidative Damage

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Amyloid-beta: an antioxidant that becomes a pro-oxidant and critically contributes to Alzheimer's disease

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Solution NMR studies of the A beta(1-40) and A beta(1-42) peptides establish that the Met35 oxidation state affects the mechanism of amyloid formation

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Coumarin-3-carboxylic acid as a detector for hydroxyl radicals generated chemically and by gamma radiation

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7 January 2021

Identifiers

DOI

10.1038/NCHEMBIO.89

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18454142%20AND%20SRC:MED&resulttype=core&format=json

6 January 2020

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