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Copper transporter 1 (CTR1) is a transmembrane protein that imports copper(i) into yeast and mammalian cells. Surprisingly, the protein also mediates the uptake of platinum anticancer drugs, e.g. cisplatin and carboplatin. To study the effects of several metal-binding residues/motifs of hCTR1 on the transport of both Cu(+) and cisplatin, we have constructed(More)
Alzheimer's disease is a devastating and invariably fatal neurodegenerative brain disorder with no cure. AD is characterized by two pathological protein deposits, the senile plaques composed mainly of amyloid-β (Aβ) peptide and the neurofibrillary tangles which are bundles of paired helical filaments (PHF) of protein tau. In addition, oxidative stress,(More)
Alzheimer’s disease (AD) is a progressive neurodegenerative disease which is clinically characterized by memory loss and cognitive decline caused by protein misfolding and aggregation. Imbalance between free radicals and the antioxidant system is a prominent and early feature in the neuropathology of AD. Selenium (Se), a vital trace element with excellent(More)
Alzheimer's disease (AD) is a neurodegenerative disorder that is characterized by peptide and protein misfolding and aggregation, in part due to the presence of excess metal ions such as copper. Aggregation and cytotoxicity of amyloid-β (Aβ) peptide with copper ion have been investigated extensively; however, the effects of metalation on tau are less known.(More)
Aggregation and cytotoxicity of the amyloid-β (Aβ) peptide with transition metal ions in neuronal cells have been suggested to be involved in the progression of Alzheimer's disease (AD). A therapeutic strategy to combat this incurable disease is to design chemical agents to target metal-Aβ species. Selenoproteins are a group of special proteins that contain(More)
The N-terminus of hCTR1 was demonstrated to bind three Cu(+) ions tightly (log K = 14.92) and reversibly via its Met-rich motifs. Ag(+) binds to the protein with the same stoichiometry but much lower affinities than Cu(+). The protein also coordinates two Cu(2+) ions through its ATCUN motif and His-rich motif with lower affinity. This study provides an(More)
Selenium (Se), an essential trace element for human health, mainly exerts its biological function via selenoproteins. Among the 25 selenoproteins identified in human, selenoprotein P (SelP) is the only one that contains multiple selenocysteines (Sec) in the sequence, and has been suggested to function as a Se transporter. Upon feeding a selenium-deficient(More)
It has been suggested that the aggregation and cytotoxicity of amyloid-β (Aβ) peptide with transition-metal ions in neuronal cells is involved in the progression of Alzheimer's disease (AD). Selenoproteins are a group of special proteins that contain the 21st amino acid selenocysteine in their sequence, and they are found to be involved in the onset and(More)
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