The catalytic redox activity of prion protein-Cu(II) is controlled by metal exchange with the Zn(II) -thiolate clusters of Zn(7) metallothionein-3.
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Mammalian Metallothionein-3: New Functional and Structural InsightsAdvances in the molecular understanding of biological zinc transport.Metallothioneins in Prion- and Amyloid-Related Diseases.Copper metallothioneins.Mutual interference of Cu and Zn ions in Alzheimer's disease: perspectives at the molecular level.Chemistry of mammalian metallothioneins and their interaction with amyloidogenic peptides and proteins.Resistance of Cu(Aβ4-16) to Copper Capture by Metallothionein-3 Supports a Function for the Aβ4-42 Peptide as a Synaptic Cu(II) Scavenger.In vivo-folded metal-metallothionein 3 complexes reveal the Cu-thionein rather than Zn-thionein character of this brain-specific mammalian metallothionein.
P2860
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P2860
The catalytic redox activity of prion protein-Cu(II) is controlled by metal exchange with the Zn(II) -thiolate clusters of Zn(7) metallothionein-3.
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name
The catalytic redox activity of prion protein-Cu
@nl
The catalytic redox activity o ...... rs of Zn(7) metallothionein-3.
@en
type
label
The catalytic redox activity of prion protein-Cu
@nl
The catalytic redox activity o ...... rs of Zn(7) metallothionein-3.
@en
prefLabel
The catalytic redox activity of prion protein-Cu
@nl
The catalytic redox activity o ...... rs of Zn(7) metallothionein-3.
@en
P2093
P2860
P356
P1433
P1476
The catalytic redox activity o ...... ers of Zn(7) metallothionein-3
@en
P2093
Andrea Crameri
David R Brown
Milan Vašák
Paul Davies
Peter M H Kroneck
P2860
P304
P356
10.1002/CBIC.201200198
P577
2012-05-21T00:00:00Z