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Pope, C. R., De Feo, C. J., Unger, V. M. (2013) Cellular distribution of copper to superoxide dismutase involves scaffolding by membranes. Proceedings of the National Academy of Sciences, 110 (51) 20491-20496 doi:10.1073/pnas.1309820110

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Reference TypeJournal (article/letter/editorial)
TitleCellular distribution of copper to superoxide dismutase involves scaffolding by membranes
JournalProceedings of the National Academy of Sciences
AuthorsPope, C. R.Author
De Feo, C. J.Author
Unger, V. M.Author
Year2013 (December 17)Volume110
Issue51
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.1309820110Search in ResearchGate
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Mindat Ref. ID1823710Long-form Identifiermindat:1:5:1823710:8
GUID0
Full ReferencePope, C. R., De Feo, C. J., Unger, V. M. (2013) Cellular distribution of copper to superoxide dismutase involves scaffolding by membranes. Proceedings of the National Academy of Sciences, 110 (51) 20491-20496 doi:10.1073/pnas.1309820110
Plain TextPope, C. R., De Feo, C. J., Unger, V. M. (2013) Cellular distribution of copper to superoxide dismutase involves scaffolding by membranes. Proceedings of the National Academy of Sciences, 110 (51) 20491-20496 doi:10.1073/pnas.1309820110
In(2013, December) Proceedings of the National Academy of Sciences Vol. 110 (51) Proceedings of the National Academy of Sciences

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De Feo, C. J., Aller, S. G., Siluvai, G. S., Blackburn, N. J., Unger, V. M. (2009) Three-dimensional structure of the human copper transporter hCTR1. Proceedings of the National Academy of Sciences, 106 (11) 4237-4242 doi:10.1073/pnas.0810286106
Wong, P. C., Waggoner, D., Subramaniam, J. R., Tessarollo, L., Bartnikas, T. B., Culotta, V. C., Price, D. L., Rothstein, J., Gitlin, J. D. (2000) Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutase. Proceedings of the National Academy of Sciences, 97 (6) 2886-2891 doi:10.1073/pnas.040461197
Saez, J. C., Kessler, J. A., Bennett, M. V., Spray, D. C. (1987) Superoxide dismutase protects cultured neurons against death by starvation. Proceedings of the National Academy of Sciences, 84 (9) 3056-3059 doi:10.1073/pnas.84.9.3056
Kubisch, H. M., Wang, J., Luche, R., Carlson, E., Bray, T. M., Epstein, C. J., Phillips, J. P. (1994) Transgenic copper/zinc superoxide dismutase modulates susceptibility to type I diabetes. Proceedings of the National Academy of Sciences, 91 (21) 9956-9959 doi:10.1073/pnas.91.21.9956
Cheung, E. C., Ludwig, R. L., Vousden, K. H. (2012) Mitochondrial localization of TIGAR under hypoxia stimulates HK2 and lowers ROS and cell death. Proceedings of the National Academy of Sciences, 109 (50) 20491-20496 doi:10.1073/pnas.1206530109
Troy, C. M., Shelanski, M. L. (1994) Down-regulation of copper/zinc superoxide dismutase causes apoptotic death in PC12 neuronal cells. Proceedings of the National Academy of Sciences, 91 (14) 6384-6387 doi:10.1073/pnas.91.14.6384
Braun, N., Zacharias, M., Peschek, J., Kastenmuller, A., Zou, J., Hanzlik, M., Haslbeck, M., Rappsilber, J., Buchner, J., Weinkauf, S. (2011) Multiple molecular architectures of the eye lens chaperone  B-crystallin elucidated by a triple hybrid approach. Proceedings of the National Academy of Sciences, 108 (51) 20491-20496 doi:10.1073/pnas.1111014108
Viegas, J. (2013) Profile of Edward M. De Robertis. Proceedings of the National Academy of Sciences, 110 (51) 20349-20351 doi:10.1073/pnas.1320552110
Nishida, C. R., Gralla, E. B., Valentine, J. S. (1994) Characterization of three yeast copper-zinc superoxide dismutase mutants analogous to those coded for in familial amyotrophic lateral sclerosis. Proceedings of the National Academy of Sciences, 91 (21) 9906-9910 doi:10.1073/pnas.91.21.9906
Nguyen, M. D., Lariviere, R. C., Julien, J.-P. (2000) Reduction of axonal caliber does not alleviate motor neuron disease caused by mutant superoxide dismutase 1. Proceedings of the National Academy of Sciences, 97 (22) 12306-12311 doi:10.1073/pnas.97.22.12306
Nettleton, C. J., Bull, C., Baldwin, T. O., Fee, J. A. (1984) Isolation of the Escherichia coli iron superoxide dismutase gene: evidence that intracellular superoxide concentration does not regulate oxygen-dependent synthesis of the manganese superoxide dismutase. Proceedings of the National Academy of Sciences, 81 (15) 4970-4973 doi:10.1073/pnas.81.15.4970
 
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