Prion diseases: copper deficiency states associated with impaired nitrogen monoxide or carbon monoxide transduction and translocation (Q34455039)

2 August 2017

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title

Prion diseases: copper deficiency states associated with impaired nitrogen monoxide or carbon monoxide transduction and translocation (English)

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2 August 2017

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Sorenson JR

1

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2 August 2017

publication date

1 December 2001

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Journal of Inorganic Biochemistry

2 August 2017

published in

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2 August 2017

volume

87

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2 August 2017

issue

3

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2 August 2017

page(s)

125-127

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Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein.

2 August 2017

cites work

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Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: structural studies using synthetic peptides

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B lymphocytes and neuroinvasion

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Prions are copper-binding proteins

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7 January 2021

Prion protein selectively binds copper(II) ions

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PrPSc-like prion protein peptide inhibits the function of cellular prion protein

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Antioxidant activity related to copper binding of native prion protein

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7 January 2021

Identification of the Cu2+ binding sites in the N-terminal domain of the prion protein by EPR and CD spectroscopy

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Metal-dependent alpha-helix formation promoted by the glycine-rich octapeptide region of prion protein

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Copper refolding of prion protein.

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A cellular form of prion protein (PrPC) exists in many non-neuronal tissues of sheep

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Effects of oxidative stress on prion protein expression in PC12 cells

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Prion diseases and the BSE crisis

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Copper stimulates endocytosis of the prion protein

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Prion protein expression and superoxide dismutase activity

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Normal prion protein has an activity like that of superoxide dismutase.

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7 January 2021

Evidence for oxidative stress in experimental prion disease

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Prion disease: A loss of antioxidant function?

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Hydroperoxide metabolism in mammalian organs

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Evidence of presynaptic location and function of the prion protein

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Signal transduction through prion protein

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Cu2+ is the active principle of an endogenous substance from porcine cerebral cortex which antagonizes the anticonvulsant effect of diazepam.

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Nerve endings from rat brain tissue release copper upon depolarization. A possible role in regulating neuronal excitability

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7 January 2021

High-affinity uptake of 67Cu into a veratridine-releasable pool in brain tissue

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7 January 2021

Prion protein is necessary for normal synaptic function

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7 January 2021

Prion protein expression aids cellular uptake and veratridine-induced release of copper

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7 January 2021

Dose-dependent, prion protein (PrP)-mediated facilitation of excitatory synaptic transmission in the mouse hippocampus

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7 January 2021

Differential expression of metallothioneins in human prion diseases

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7 January 2021

Prion proteins and the gut: une liaison dangereuse?

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Biochemistry of Nitric Oxide and Its Redox-Activated Forms

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7 January 2021

Carbon monoxide: a putative neural messenger

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7 January 2021

Ecosystems supporting clusters of sporadic TSEs demonstrate excesses of the radical-generating divalent cation manganese and deficiencies of antioxidant co factors Cu, Se, Fe, Zn. Does a foreign cation substitution at prion protein's Cu domain initi

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7 January 2021

Does an ultra violet photooxidation of the manganese-loaded/copper-depleted prion protein in the retina initiate the pathogenesis of TSE?

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7 January 2021

10.1016/S0162-0134(01)00303-8

Identifiers

DOI

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2 August 2017

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