The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Structural relationship between an iron-regulated RNA-binding protein (IRE-BP) and aconitase: Functional implications
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Iron-Responsive Elements: Regulatory RNA Sequences That Control mRNA Levels and Translation
Casey, J. L., Hentze, M. W., Koeller, D. M., Caughman, S. W., Rouault, T. A., Klausner, R. D., & Harford, J. B. (1988) · Science · doi:10.1126/science.2452485 · Cited by 709
Self-citationBinding of a Cytosolic Protein to the Iron-Responsive Element of Human Ferritin Messenger RNA
Rouault, T. A., Hentze, M. W., Caughman, S. W., Harford, J. B., & Klausner, R. D. (1988) · Science · doi:10.1126/science.3413484 · Cited by 351
Self-citation
Cited by
The ferritins: molecular properties, iron storage function and cellular regulation
Harrison, P. M., & Arosio, P. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(96)00022-9 · Cited by 2,667
Insights into RNA Biology from an Atlas of Mammalian mRNA-Binding Proteins
Castello, A., Fischer, B., Eichelbaum, K., Horos, R., Beckmann, B. M., Strein, C., Davey, N. E., Humphreys, D. T., Preiss, T., Steinmetz, L. M., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.031 · Cited by 2,132
A brave new world of RNA-binding proteins
Hentze, M. W., Castello, A., Schwarzl, T., & Preiss, T. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.130 · Cited by 1,821
Fueling Immunity: Insights into Metabolism and Lymphocyte Function
Pearce, E. L., Poffenberger, M. C., Chang, C.-H., & Jones, R. G. (2013) · Science · doi:10.1126/science.1242454 · Cited by 1,363
Hentze, M. W., & Kühn, L. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.16.8175 · Cited by 1,292
Regulating 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-citationAconitase as iron–sulfur protein, enzyme, and iron-regulatory protein
Beinert, H., Kennedy, M. C., & Stout, C. D. (1996) · Chemical Reviews · doi:10.1021/cr950040z · Cited by 606
Self-citationIron Homeostasis, Oxidative Stress, and DNA Damage
Meneghini, R. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00016-6 · Cited by 578
Intracellular iron transport and storage: from molecular mechanisms to health implications
Mackenzie, E. L., Iwasaki, K., & Tsuji, Y. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1893 · Cited by 526
Nitric oxide and iron proteins
Cooper, C. E. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00021-3 · Cited by 510
Biosynthesis of nitric oxide activates iron regulatory factor in macrophages.
Drapier, J. C., Hirling, H., Wietzerbin, J., Kaldy, P., & Kühn, L. C. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06038.x · Cited by 401
Meyron‐Holtz, E. G., Ghosh, M. C., Iwai, K., LaVaute, T., Brazzolotto, X., Berger, U. V., Land, W., Ollivierre‐Wilson, H., Grinberg, A., Love, P., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600041 · Cited by 408
Self-citationTranslational regulation via iron‐responsive elements by the nitric oxide/NO‐synthase pathway.
Weiss, G., Goossen, B., Doppler, W., Fuchs, D., Pantopoulos, K., Werner‐Felmayer, G., Wachter, H., & Hentze, M. W. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06039.x · Cited by 389
Oexle, H., Gnaiger, E., & Weiss, G. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00088-2 · Cited by 307
Devireddy, L. R., Hart, D. O., Goetz, D. H., & Green, M. R. (2010) · Cell · doi:10.1016/j.cell.2010.04.040 · Cited by 295
Rogers, J. T., Leiter, L. M., McPhee, J., Cahill, C. M., Zhan, S.-S., Potter, H., & Nilsson, L. N. G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.10.6421 · Cited by 290
Molecular control of vertebrate iron homeostasis by iron regulatory proteins
Wallander, M. L., Leibold, E. A., & Eisenstein, R. S. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.004 · Cited by 287
Iron–sulfur proteins with nonredox functions
Flint, D. H., & Allen, R. M. (1996) · Chemical Reviews · doi:10.1021/cr950041r · Cited by 280
Iron regulatory proteins and their role in controlling iron metabolism
Kühn, L. C. (2015) · Metallomics · doi:10.1039/c4mt00164h · Cited by 242
Yogev, O., Yogev, O., Singer, E., Shaulian, E., Goldberg, M., Fox, T. D., & Pines, O. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000328 · Cited by 220
“other cellular activities, as for example aconitase in nucleoid binding and stabilization of mitochondrial DNA [34,35], aconitase as a regulator of iron metabolism [35], and more recently pyruvate kinase M2 as a phospho-tyrosine binding protein that is critical for a”
Wang, X., Kiledjian, M., Weiss, I. M., & Liebhaber, S. A. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.3.1769 · Cited by 192
Byrd, T. F., & Horwitz, M. A. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116318 · Cited by 149
Kiledjian, M., DeMaria, C. T., Brewer, G., & Novick, K. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.8.4870 · Cited by 145
Iron metabolism-new perspectives in view
Crichton, R. R., & Ward, R. J. (1992) · Biochemistry · doi:10.1021/bi00161a001 · Cited by 138
The Pathophysiology of Transfusional Iron Overload
Porter, J. B., & Garbowski, M. (2014) · Hematology/Oncology Clinics of North America · doi:10.1016/j.hoc.2014.04.003 · Cited by 120
The REM phase of gene regulation
Hentze, M. W., & Preiss, T. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.05.009 · Cited by 115
Rychtarcikova, Z., Lettlova, S., Tomkova, V., Korenkova, V., Langerova, L., Simonova, E., Zjablovskaja, P., Alberich-Jorda, M., Neuzil, J., & Truksa, J. (2017) · Oncotarget · doi:10.18632/oncotarget.14093 · Cited by 100
Metadata
- Authors
- Rouault, T. A., Stout, C. D., Kaptain, S., Harford, J. B., & Klausner, R. D.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1991-03
- Volume
- 64
- Issue
- 5
- Pages
- 881-883
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2070009162
- Cited by
- 296
- References
- 2
- FWCI
- 22.24
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
