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Hassan, H. M., Sun, H. C. (1992) Regulatory roles of Fnr, Fur, and Arc in expression of manganese-containing superoxide dismutase in Escherichia coli. Proceedings of the National Academy of Sciences, 89 (8) 3217-3221 doi:10.1073/pnas.89.8.3217

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Reference TypeJournal (article/letter/editorial)
TitleRegulatory roles of Fnr, Fur, and Arc in expression of manganese-containing superoxide dismutase in Escherichia coli.
JournalProceedings of the National Academy of Sciences
AuthorsHassan, H. M.Author
Sun, H. C.Author
Year1992 (April 15)Volume89
Issue8
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.89.8.3217Search in ResearchGate
Generate Citation Formats
Mindat Ref. ID1520450Long-form Identifiermindat:1:5:1520450:7
GUID0
Full ReferenceHassan, H. M., Sun, H. C. (1992) Regulatory roles of Fnr, Fur, and Arc in expression of manganese-containing superoxide dismutase in Escherichia coli. Proceedings of the National Academy of Sciences, 89 (8) 3217-3221 doi:10.1073/pnas.89.8.3217
Plain TextHassan, H. M., Sun, H. C. (1992) Regulatory roles of Fnr, Fur, and Arc in expression of manganese-containing superoxide dismutase in Escherichia coli. Proceedings of the National Academy of Sciences, 89 (8) 3217-3221 doi:10.1073/pnas.89.8.3217
In(1992, April) Proceedings of the National Academy of Sciences Vol. 89 (8) Proceedings of the National Academy of Sciences

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Privalle, C. T., Kong, S. E., Fridovich, I. (1993) Induction of manganese-containing superoxide dismutase in anaerobic Escherichia coli by diamide and 1,10-phenanthroline: sites of transcriptional regulation. Proceedings of the National Academy of Sciences, 90 (6) 2310-2314 doi:10.1073/pnas.90.6.2310
Gruber, M. Y., Glick, B. R., Thompson, J. E. (1990) Cloned manganese superoxide dismutase reduces oxidative stress in Escherichia coli and Anacystis nidulans. Proceedings of the National Academy of Sciences, 87 (7) 2608-2612 doi:10.1073/pnas.87.7.2608
Hartman, J. R., Geller, T., Yavin, Z., Bartfeld, D., Kanner, D., Aviv, H., Gorecki, M. (1986) High-level expression of enzymatically active human Cu/Zn superoxide dismutase in Escherichia coli. Proceedings of the National Academy of Sciences, 83 (19) 7142-7146 doi:10.1073/pnas.83.19.7142
Eliasson, R., Jornvall, H., Reichard, P. (1986) Superoxide dismutase participates in the enzymatic formation of the tyrosine radical of ribonucleotide reductase from Escherichia coli. Proceedings of the National Academy of Sciences, 83 (8) 2373-2377 doi:10.1073/pnas.83.8.2373
Privalle, C. T., Fridovich, I. (1987) Induction of superoxide dismutase in Escherichia coli by heat shock. Proceedings of the National Academy of Sciences, 84 (9) 2723-2726 doi:10.1073/pnas.84.9.2723
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
Farr, S. B., D'Ari, R., Touati, D. (1986) Oxygen-dependent mutagenesis in Escherichia coli lacking superoxide dismutase. Proceedings of the National Academy of Sciences, 83 (21) 8268-8272 doi:10.1073/pnas.83.21.8268
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
Parge, H. E. (1992) Correction: Atomic Structures of Wild-Type and Thermostable Mutant Recombinant Human Cu,Zn Superoxide Dismutase. Proceedings of the National Academy of Sciences, 89 (22) 11106 doi:10.1073/pnas.89.22.11106
Parker, B. O., Marinus, M. G. (1992) Repair of DNA heteroduplexes containing small heterologous sequences in Escherichia coli. Proceedings of the National Academy of Sciences, 89 (5) 1730-1734 doi:10.1073/pnas.89.5.1730
Jasin, M., Zalamea, P. (1992) Analysis of Escherichia coli beta-galactosidase expression in transgenic mice by flow cytometry of sperm. Proceedings of the National Academy of Sciences, 89 (22) 10681-10685 doi:10.1073/pnas.89.22.10681
 
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