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Pantopoulos, K., Hentze, M. W. (1995) Nitric oxide signaling to iron-regulatory protein: direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts. Proceedings of the National Academy of Sciences, 92 (5) 1267-1271 doi:10.1073/pnas.92.5.1267

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Reference TypeJournal (article/letter/editorial)
TitleNitric oxide signaling to iron-regulatory protein: direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts.
JournalProceedings of the National Academy of Sciences
AuthorsPantopoulos, K.Author
Hentze, M. W.Author
Year1995 (February 28)Volume92
Issue5
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.92.5.1267Search in ResearchGate
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Mindat Ref. ID1567193Long-form Identifiermindat:1:5:1567193:0
GUID0
Full ReferencePantopoulos, K., Hentze, M. W. (1995) Nitric oxide signaling to iron-regulatory protein: direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts. Proceedings of the National Academy of Sciences, 92 (5) 1267-1271 doi:10.1073/pnas.92.5.1267
Plain TextPantopoulos, K., Hentze, M. W. (1995) Nitric oxide signaling to iron-regulatory protein: direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts. Proceedings of the National Academy of Sciences, 92 (5) 1267-1271 doi:10.1073/pnas.92.5.1267
In(1995, February) Proceedings of the National Academy of Sciences Vol. 92 (5) Proceedings of the National Academy of Sciences

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Hentze, M. W., Kuhn, L. C. (1996) Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proceedings of the National Academy of Sciences, 93 (16) 8175-8182 doi:10.1073/pnas.93.16.8175
Pantopoulos, K., Hentze, M. W. (1998) Activation of iron regulatory protein-1 by oxidative stress in vitro. Proceedings of the National Academy of Sciences, 95 (18) 10559-10563 doi:10.1073/pnas.95.18.10559
Koeller, D. M., Casey, J. L., Hentze, M. W., Gerhardt, E. M., Chan, L. N., Klausner, R. D., Harford, J. B. (1989) A cytosolic protein binds to structural elements within the iron regulatory region of the transferrin receptor mRNA. Proceedings of the National Academy of Sciences, 86 (10) 3574-3578 doi:10.1073/pnas.86.10.3574
Aziz, N., Munro, H. N. (1987) Iron regulates ferritin mRNA translation through a segment of its 5' untranslated region. Proceedings of the National Academy of Sciences, 84 (23) 8478-8482 doi:10.1073/pnas.84.23.8478
Hintze, K. J., Theil, E. C. (2005) DNA and mRNA elements with complementary responses to hemin, antioxidant inducers, and iron control ferritin-L expression. Proceedings of the National Academy of Sciences, 102 (42) 15048-15052 doi:10.1073/pnas.0505148102
Schalinske, K. L., Blemings, K. P., Steffen, D. W., Chen, O. S., Eisenstein, R. S. (1997) Iron regulatory protein 1 is not required for the modulation of ferritin and transferrin receptor expression by iron in a murine pro-B lymphocyte cell line. Proceedings of the National Academy of Sciences, 94 (20) 10681-10686 doi:10.1073/pnas.94.20.10681
Gay, D. A., Sisodia, S. S., Cleveland, D. W. (1989) Autoregulatory control of beta-tubulin mRNA stability is linked to translation elongation. Proceedings of the National Academy of Sciences, 86 (15) 5763-5767 doi:10.1073/pnas.86.15.5763
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Harrell, C. M., McKenzie, A. R., Patino, M. M., Walden, W. E., Theil, E. C. (1991) Ferritin mRNA: interactions of iron regulatory element with translational regulator protein P-90 and the effect on base-paired flanking regions. Proceedings of the National Academy of Sciences, 88 (10) 4166-4170 doi:10.1073/pnas.88.10.4166
Fajardo, J. E., Shatkin, A. J. (1990) Translation of bicistronic viral mRNA in transfected cells: regulation at the level of elongation. Proceedings of the National Academy of Sciences, 87 (1) 328-332 doi:10.1073/pnas.87.1.328
Liang, S. (1995) Correction: Adenoviral E1B-55kDa Protein Inhibits Yeast mRNA Export and Perturbs Nuclear Structure. Proceedings of the National Academy of Sciences, 92 (23) 10815 doi:10.1073/pnas.92.23.10815d
 
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