2010
DOI: 10.1016/j.jtemb.2010.01.009
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Ctr1 transports silver into mammalian cells

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Cited by 68 publications
(60 citation statements)
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“…Moreover, recently, it has been demonstrated that CTR1 is an important Ag transporter. Cells over-expressing Ctr1 accumulated Ag and cells lacking Ctr1 had a 50% reduction in Ag content compared with wild-type [104]. In addition, the evidence that Ag þ inhibit Cu uptake suggests that monovalent Cu is the favourite substrate for CTR1.…”
Section: Molecular Mechanisms Of Ag Uptakementioning
confidence: 99%
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“…Moreover, recently, it has been demonstrated that CTR1 is an important Ag transporter. Cells over-expressing Ctr1 accumulated Ag and cells lacking Ctr1 had a 50% reduction in Ag content compared with wild-type [104]. In addition, the evidence that Ag þ inhibit Cu uptake suggests that monovalent Cu is the favourite substrate for CTR1.…”
Section: Molecular Mechanisms Of Ag Uptakementioning
confidence: 99%
“…Both excess and deficiency of Cu is deleterious for the cell, thus Cu intracellular concentration is tightly regulated by Cu transporter proteins [102]. Notably, some of these proteins have been shown to transport Ag as well as Cu [103,104].…”
Section: Molecular Mechanisms Of Ag Uptakementioning
confidence: 99%
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“…It is generally thought that cuprous (Cu ϩ ), rather than cupric (Cu 2ϩ ) copper ions are transported by hCTR1 (40). Of numerous metals tested, only monovalent silver (Ag ϩ ) inhibits or competes with 64 Cu uptake (27), and it was subsequently shown that hCTR1 transports Ag ϩ (8). Furthermore, using spectroscopic techniques, De Feo et al (13) showed that purified recombinant hCTR1 bound two Cu ϩ ions per trimer (13).…”
mentioning
confidence: 99%
“…CTR/COPT proteins are highly specific for Cu + transport (and the isoelectric Ag + ), but not for Cu 2+ [13,36,37]. Consequently, they function in coordination with membrane metalloreductases that catalyze Cu 2+ reduction to Cu + before transport [38,39].…”
Section: Introductionmentioning
confidence: 99%