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Kubota, S., Yang, J. T. (1984) Bis[cyclo(histidylhistidine)]copper(II) complex that mimicks the active center of superoxide dismutase has its catalytic activity. Proceedings of the National Academy of Sciences, 81 (11) 3283-3286 doi:10.1073/pnas.81.11.3283

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Reference TypeJournal (article/letter/editorial)
TitleBis[cyclo(histidylhistidine)]copper(II) complex that mimicks the active center of superoxide dismutase has its catalytic activity.
JournalProceedings of the National Academy of Sciences
AuthorsKubota, S.Author
Yang, J. T.Author
Year1984 (June 1)Volume81
Issue11
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.81.11.3283Search in ResearchGate
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Mindat Ref. ID1434626Long-form Identifiermindat:1:5:1434626:8
GUID0
Full ReferenceKubota, S., Yang, J. T. (1984) Bis[cyclo(histidylhistidine)]copper(II) complex that mimicks the active center of superoxide dismutase has its catalytic activity. Proceedings of the National Academy of Sciences, 81 (11) 3283-3286 doi:10.1073/pnas.81.11.3283
Plain TextKubota, S., Yang, J. T. (1984) Bis[cyclo(histidylhistidine)]copper(II) complex that mimicks the active center of superoxide dismutase has its catalytic activity. Proceedings of the National Academy of Sciences, 81 (11) 3283-3286 doi:10.1073/pnas.81.11.3283
In(1984, June) Proceedings of the National Academy of Sciences Vol. 81 (11) Proceedings of the National Academy of Sciences

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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
Marklund, S. L. (1982) Human copper-containing superoxide dismutase of high molecular weight. Proceedings of the National Academy of Sciences, 79 (24) 7634-7638 doi:10.1073/pnas.79.24.7634
Bermingham-McDonogh, O., Gralla, E. B., Valentine, J. S. (1988) The copper, zinc-superoxide dismutase gene of Saccharomyces cerevisiae: cloning, sequencing, and biological activity. Proceedings of the National Academy of Sciences, 85 (13) 4789-4793 doi:10.1073/pnas.85.13.4789
Tokunaga, C. (1972) Autonomy or Nonautonomy of Gene Effects in Mosaics. Proceedings of the National Academy of Sciences, 69 (11) 3283-3286 doi:10.1073/pnas.69.11.3283
Nakanishi, S., Kita, T., Taii, S., Imura, H., Numa, S. (1977) Glucocorticoid effect on the level of corticotropin messenger RNA activity in rat pituitary. Proceedings of the National Academy of Sciences, 74 (8) 3283-3286 doi:10.1073/pnas.74.8.3283
Pope, L. E., Sigman, D. S. (1984) Secondary structure specificity of the nuclease activity of the 1,10-phenanthroline-copper complex. Proceedings of the National Academy of Sciences, 81 (1) 3-7 doi:10.1073/pnas.81.1.3
Pinto, A. L., Hellinga, H. W., Caradonna, J. P. (1997) Construction of a catalytically active iron superoxide dismutase by rational protein design. Proceedings of the National Academy of Sciences, 94 (11) 5562-5567 doi:10.1073/pnas.94.11.5562
Gralla, E. B., Thiele, D. J., Silar, P., Valentine, J. S. (1991) ACE1, a copper-dependent transcription factor, activates expression of the yeast copper, zinc superoxide dismutase gene. Proceedings of the National Academy of Sciences, 88 (19) 8558-8562 doi:10.1073/pnas.88.19.8558
Tamai, K. T., Gralla, E. B., Ellerby, L. M., Valentine, J. S., Thiele, D. J. (1993) Yeast and mammalian metallothioneins functionally substitute for yeast copper-zinc superoxide dismutase. Proceedings of the National Academy of Sciences, 90 (17) 8013-8017 doi:10.1073/pnas.90.17.8013
Tegoni, M., Yu, F., Bersellini, M., Penner-Hahn, J. E., Pecoraro, V. L. (2012) Designing a functional type 2 copper center that has nitrite reductase activity within  -helical coiled coils. Proceedings of the National Academy of Sciences, 109 (52) 21234-21239 doi:10.1073/pnas.1212893110
Liochev, S. I., Fridovich, I. (1997) Lucigenin luminescence as a measure of intracellular superoxide dismutase activity in Escherichia coli. Proceedings of the National Academy of Sciences, 94 (7) 2891-2896 doi:10.1073/pnas.94.7.2891
 
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