FAQ

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
Site-specific interactions of Cu(II) with alpha and beta-synuclein: bridging the molecular gap between metal binding and aggregation.
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
Human Sco1 and Sco2 function as copper-binding proteins.
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
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…
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
Preferential Cu2+ coordination by His96 and His111 induces beta-sheet formation in the unstructured amyloidogenic region of the prion protein.
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
Rodent Abeta(1-42) exhibits oxidative stress properties similar to those of human Abeta(1-42): Implications for proposed mechanisms of toxicity.
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
Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity: insights from circular dichroism.
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 reveals the prodromes of its amyloid transition.
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
Metal binding modes of Alzheimer's amyloid beta-peptide in insoluble aggregates and soluble complexes.
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
Identification of the Cu2+ binding sites in the N-terminal domain of the prion protein by EPR and CD spectroscopy.
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
Copper binding to the prion protein: structural implications of four identical cooperative binding sites.
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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