cupric ion binding

Known as: Cu(2+) binding, Cu(II) binding, copper(2+)binding 
Interacting selectively and non-covalently with cupric ion, copper(2+). [GO_REF:0000067, GOC:bf, GOC:PARL, GOC:TermGenie, PMID:24567322]

Topic mentions per year

Topic mentions per year

1967-2017
0102019672017

Papers overview

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2008
2008
The aggregation of alpha-synuclein (AS) is a critical step in the etiology of Parkinson's disease (PD) and other… (More)
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2005
2005
The function of human Sco1 and Sco2 is shown to be dependent on copper ion binding. Expression of soluble domains of human Sco1… (More)
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2004
2004
There is now direct evidence that copper is bound to amyloid-beta peptide (Abeta) in senile plaque of Alzheimer's disease. Copper… (More)
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2004
2004
The prion protein (PrP) is a Cu(2+) binding cell surface glycoprotein that can misfold into a beta-sheet-rich conformation to… (More)
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2004
2004
Alzheimer's disease is a neurodegenerative disorder associated with aging and cognitive decline. Amyloid beta peptide (1-42… (More)
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2003
2003
The prion protein (PrP) is a Cu(2+) binding cell surface glycoprotein. There is increasing evidence that PrP functions as a… (More)
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2002
2002
The solution structure of human beta2-microglobulin (beta2-m), the nonpolymorphic component of class I major histocompatibility… (More)
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Highly Cited
2000
Highly Cited
2000
Aggregation of the amyloid beta-peptide (Abeta) into insoluble fibrils is a key pathological event in Alzheimer's disease. Zn(II… (More)
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2000
2000
Recent evidence indicates that the prion protein (PrP) plays a role in copper metabolism in the central nervous system. The N… (More)
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Highly Cited
1999
Highly Cited
1999
Evidence is growing to support a functional role for the prion protein (PrP) in copper metabolism. Copper ions appear to bind to… (More)
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