The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Ferric reductase of Saccharomyces cerevisiae: molecular characterization, role in iron uptake, and transcriptional control by iron.
Open accessAbstract
The principal iron uptake system of Saccharomyces cerevisiae utilizes a reductase activity that acts on ferric iron chelates external to the cell. The FRE1 gene product is required for this activity. The deduced amino acid sequence of the FRE1 protein exhibits hydrophobic regions compatible with transmembrane domains and has significant similarity to the sequence of the plasma membrane cytochrome b558 (the X-CGD protein), a critical component of a human phagocyte oxidoreductase, suggesting that FRE1 is a structural component of the yeast ferric reductase. FRE1 mRNA levels are repressed by iron. Fusion of 977 base pairs of FRE1 DNA upstream from the translation start site of an Escherichia coli lacZ reporter gene confers iron-dependent regulation on expression of beta-galactosidase in yeast. An 85-base-pair segment of FRE1 5' noncoding sequence contains a RAP1 binding site and a repeated sequence, TTTTTGCTCAYC; this segment is sufficient to confer iron-repressible transcriptional activity on heterologous downstream promoter elements.
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Cites
Improved tools for biological sequence comparison.
Pearson, W. R., & Lipman, D. J. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.8.2444 · Cited by 11,227
Cited by
The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989
“However, at least in yeast, the FRE homologs within the NOX family reduce metal ions, particularly trivalent iron (182, 183).”
BackgroundRegulating the fate of mRNA: the control of cellular iron metabolism
Klausner, R. D., Rouault, T. A., & Harford, J. B. (1993) · Cell · doi:10.1016/0092-8674(93)90046-s · Cited by 1,210
Self-citationAn iron-regulated ferric reductase associated with the absorption of dietary iron
McKie, A. T., Barrow, D., Latunde-Dada, G. O., Rolfs, A., Sager, G., Mudaly, E., Mudaly, M., Richardson, C., Barlow, D., Bomford, A., et al. (2001) · Science · doi:10.1126/science.1057206 · Cited by 1,101
Chemistry and biology of eukaryotic iron metabolism
Aisen, P. (2001) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(01)00063-2 · Cited by 804
The Steap proteins are metalloreductases
Ohgami, R. S., Campagna, D. R., McDonald, A., & Fleming, M. D. (2006) · Blood · doi:10.1182/blood-2006-02-003681 · Cited by 744
Metadata
- Authors
- Dancis, A., Roman, D. G., Anderson, G. J., Hinnebusch, A. G., & Klausner, R. D.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1992-05
- Volume
- 89
- Issue
- 9
- Pages
- 3869-3873
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2050742607
- Cited by
- 357
- References
- 1
- FWCI
- 6.74
- Type
- journal article
- Language
- en
- Open access
- green
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- Dancis, A., Roman, D. G., Anderson, G. J., Hinnebusch, A. G., & Klausner, R. D. (1992). Ferric reductase of Saccharomyces cerevisiae: molecular characterization, role in iron uptake, and transcriptional control by iron. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.89.9.3869
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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