Activation of carboplatin and nedaplatin by the N-terminus of human copper transporter 1 (hCTR1)

2012 ◽  
Vol 3 (11) ◽  
pp. 3206 ◽  
Author(s):  
Xinghao Wang ◽  
Hongyan Li ◽  
Xiubo Du ◽  
Jack Harris ◽  
Zijian Guo ◽  
...  
Keyword(s):  
Copper Transporter ◽  
N Terminus ◽  
Copper Transporter 1

Model Peptide Studies Reveal a Mixed Histidine-Methionine Cu(I) Binding Site at the N-Terminus of Human Copper Transporter 1

2015 ◽  
Vol 54 (17) ◽  
pp. 8544-8551 ◽  
Author(s):  
M. Jake Pushie ◽  
Katharine Shaw ◽  
Katherine J. Franz ◽  
Jason Shearer ◽  
Kathryn L. Haas
Keyword(s):  
Binding Site ◽  
Model Peptide ◽  
Copper Transporter ◽  
N Terminus ◽  
Copper Transporter 1

Corrigendum to “The role of the N-terminus of mammalian copper transporter 1 in the cellular accumulation of cisplatin” [Biochem. Pharmacol. 80 (2010) 448–454]

2010 ◽  
Vol 80 (11) ◽  
pp. 1768
Author(s):  
Christopher A. Larson ◽  
Preston L. Adams ◽  
Danielle D. Jandial ◽  
Brian G. Blair ◽  
Roohangiz Safaei ◽  
...  
Keyword(s):  
Copper Transporter ◽  
Cellular Accumulation ◽  
N Terminus ◽  
Copper Transporter 1

scholarly journals The role of the N-terminus of mammalian copper transporter 1 in the cellular accumulation of cisplatin

2010 ◽  
Vol 80 (4) ◽  
pp. 448-454 ◽  
Author(s):  
Christopher A. Larson ◽  
Preston L. Adams ◽  
Danielle D. Jandial ◽  
Brian G. Blair ◽  
Roohangiz Safaei ◽  
...  
Keyword(s):  
Copper Transporter ◽  
Cellular Accumulation ◽  
N Terminus ◽  
Copper Transporter 1

scholarly journals The N-terminus of the human copper transporter 1 (hCTR1) is localized extracellularly, and interacts with itself

2003 ◽  
Vol 370 (3) ◽  
pp. 881-889 ◽  
Author(s):  
Adriana E.M. KLOMP ◽  
Jenneke A. JUIJN ◽  
Linda T.M. van der GUN ◽  
Inge E.T. van den BERG ◽  
Ruud BERGER ◽  
...  
Keyword(s):  
Glycosylation Site ◽  
Media Analysis ◽  
Growth Media ◽  
Deletion Mapping ◽  
Copper Binding ◽  
Copper Transporter ◽  
C Terminus ◽  
N Terminus ◽  
Multiple Regions ◽  
Copper Transporter 1

We have used indirect immunofluorescense studies and glycosylation-site insertion and deletion mapping to characterize the topology of human copper transporter 1 (hCTR1), the putative human high-affinity copper-import protein. Both approaches indicated that hCTR1 contains three transmembrane domains and that the N-terminus of hCTR1, which contains several putative copper-binding sites, is localized extracellularly, whereas the C-terminus is exposed to the cytosol. Based on previous observations that CTR1 proteins form high-molecular-mass complexes, we investigated directly whether CTR1 proteins interact with themselves. Yeast two-hybrid studies showed that interaction of yeast, mouse, rat and human CTR1 occurs at the sites of their N-terminal domains, and is not dependent on the copper concentration in the growth media. Analysis of deletion constructs indicated that multiple regions in the N-terminus are essential for this self-interaction. In contrast, the N-terminal tail of the presumed low-affinity copper transporter, hCTR2, does not interact with itself. Taken together, these results suggest that CTR1 spans the membrane at least six times, permitting formation of a channel, which is consistent with its proposed role as a copper transporter.

scholarly journals Copper Promotes Tumorigenesis by Activating the PDK1‐AKT Oncogenic Pathway in a Copper Transporter 1 Dependent Manner

2021 ◽  
pp. 2004303
Author(s):  
Jianping Guo ◽  
Ji Cheng ◽  
Nana Zheng ◽  
Xiaomei Zhang ◽  
Xiaoming Dai ◽  
...  
Keyword(s):  
Dependent Manner ◽  
Copper Transporter ◽  
Oncogenic Pathway ◽  
Copper Transporter 1
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