The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Iron regulates ferritin mRNA translation through a segment of its 5′-untranslated region.
Open accessAbstract
In previous studies, we showed that acute administration of iron to intact rats or to rat hepatoma cells in culture induces synthesis of the iron-storage protein ferritin by activating translation of inactive cytoplasmic ferritin mRNAs for both the heavy (H) and the light (L) subunits. In the course of activation, these ferritin mRNAs are recruited onto polysomes. To elucidate the structural features of these mRNAs involved in the translational response to iron, a chimera was constructed from the 5' and 3' untranslated regions (UTRs) of ferritin L subunit mRNA fused to the reading frame of the mRNA of bacterial chloramphenicol acetyltransferase (CAT). This chimera and deletion constructs derived from it were introduced into a rat hepatoma cell line by retrovirus-mediated gene transfer. The complete chimera showed increased CAT activity in response to iron enrichment of the medium, whereas deletion of the first 67 nucleotides of the 5' UTR, which contain a highly conserved sequence, caused loss of regulation by iron. Whereas cis-acting sequences located in the 5' flanking regions of many genes have been repeatedly implicated in modulating their transcriptional expression, we report here a specific regulatory translational sequence found within the 5' UTR of a eukaryotic mRNA.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“In 1987, investigators observed that conserved sequences in the 5Ј untranslated regions (UTRs) of both H-and L-ferritin mRNAs were needed to control a ready but quiescent pool of ferritin mRNA in the cell, which could quickly be mobilized to produce ferritin protein when iron was abundant.22,23”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [22]
Citations
Cites
Recombinant Genomes Which Express Chloramphenicol Acetyltransferase in Mammalian Cells
Gorman, C., Moffat, L. F., & Howard, B. H. (1982) · Molecular and Cellular Biology · doi:10.1128/mcb.2.9.1044 · Cited by 7,674
Radloff, R. J., Bauer, W. R., & Vinograd, J. R. (1967) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.57.5.1514 · Cited by 1,328
Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles
Kozak, M. (1983) · Microbiological Reviews · doi:10.1128/mr.47.1.1-45.1983 · Cited by 1,278
Construction and applications of a highly transmissible murine retrovirus shuttle vector
Cepko, C. L., Roberts, B. E., & Mulligan, R. C. (1984) · Cell · doi:10.1016/0092-8674(84)90440-9 · Cited by 974
Parker, B. A., & Stark, G. R. (1979) · Journal of Virology · doi:10.1128/jvi.31.2.360-369.1979 · Cited by 622
Pelletier, J., & Sonenberg, N. (1985) · Cell · doi:10.1016/0092-8674(85)90200-4 · Cited by 610
Novel mechanism for translational control in regulation of ferritin synthesis by iron.
Zähringer, J., Baliga, B. S., & Munro, H. N. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.3.857 · Cited by 318
The preferential translation of Drosophila hsp70 mRNA requires sequences in the untranslated leader
McGarry, T. J., & Lindquist, S. L. (1985) · Cell · doi:10.1016/0092-8674(85)90286-7 · Cited by 289
Jobling, S. A., & Gehrke, L. (1987) · Nature · doi:10.1038/325622a0 · Cited by 283
5' untranslated sequences are required for the translational control of a yeast regulatory gene.
Thireos, G., Penn, M. D., & Greer, H. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.16.5096 · Cited by 257
Flagged first, then by citations
Cited by
Sorted by citations
Items 201–300 of 367
Brock, J. H. (1989) · Acta Paediatrica · doi:10.1111/apa.1989.78.s361.31 · Cited by 33
Schreinemachers, D. M., & Ghio, A. J. (2016) · Environmental Health Insights · doi:10.4137/ehi.s36225 · Cited by 32
Puy, V., Darwiche, W., Trudel, S., Gomila, C., Lony, C., Puy, L., Lefèbvre, T., Vitry, S., Boullier, A., Karim, Z., et al. (2018) · Glia · doi:10.1002/glia.23335 · Cited by 32
Wu, C., Zhang, W., Mai, K., Xu, W., Wang, X., Ma, H., & Liufu, Z. (2010) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2010.07.002 · Cited by 32
Swenson, G. R., & Walden, W. E. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.13.2627 · Cited by 32
Huang, Y., & Hui, D. Y. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)89558-1 · Cited by 32
Santamaria, R., Fiorito, F., Irace, C., Martino, L. D., Maffettone, C., Granato, G. E., Pascale, A. D., Iovane, V., Pagnini, U., & Colonna, A. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.02.003 · Cited by 31
Iron, oxygen, and the pulmonary circulation
Frise, M. C., & Robbins, P. A. (2015) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00179.2015 · Cited by 31
Equal G and C contents in histone genes indicate selection pressures on mRNA secondary structure
Huynen, M. A., Konings, D. A. M., & Hogeweg, P. (1992) · Journal of Molecular Evolution · doi:10.1007/bf00160235 · Cited by 30
Gallic, D. R., Walbot, V., & Hershey, J. W. B. (1988) · Nucleic Acids Research · doi:10.1093/nar/16.17.8675 · Cited by 30
Coulson, R., & Cleveland, D. W. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.16.7613 · Cited by 30
A 40 kd protein binds specifically to the 5′‐untranslated regions of yeast mitochondrial mRNAs.
Papadopoulou, B., Dekker, P., Blom, J., & Grivell, L. A. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07636.x · Cited by 30
Distribution of PCP4 protein in the forebrain of adult mice
Renelt, M., Halbach, V. V. B. U., & Halbach, O. V. B. U. (2014) · Acta Histochemica · doi:10.1016/j.acthis.2014.04.012 · Cited by 29
On the origin of the yolk protein ferritin in snails
Bottke, W., Burschyk, M., & Volmer, J. (1988) · Development Genes and Evolution · doi:10.1007/bf00398988 · Cited by 29
Hsu, Y., & Guidotti, G. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)52452-2 · Cited by 29
The Ferritin Genes: Structure, Expression, and Regulation
Munro, H. N., Aziz, N., Leibold, E. A., Murray, M. T., Rogers, J. T., Vass, J. K., & White, K. (1988) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1988.tb55497.x · Cited by 29
Crosslinking of hemin to a specific site on the 90-kDa ferritin repressor protein.
Lin, J., Patiño, M. M., Gaffield, L., Walden, W. E., Smith, A., & Thach, R. E. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.14.6068 · Cited by 29
Chan, L.-N. L., Grammatikakis, N., Banks, J. M., & Gerhardt, E. M. (1989) · Nucleic Acids Research · doi:10.1093/nar/17.10.3763 · Cited by 29
Busfield, S. J., Tilbrook, P. A., Callus, B. A., Spadaccini, A., Kühn, L. C., & Klinken, S. P. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.t01-1-00077.x · Cited by 29
Kim, H., Elvitigala, D. A. S., Lee, Y., Lee, S., Whang, I., & Lee, J. (2012) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2012.08.007 · Cited by 28
Cloning and characterization of an unusual elongation factor-1α cDNA from Entamoeba histolytica
DEMEESTER, F., Bracha, R., HUBER, M., Keren, Z., Rozenblatt, S., & Mirelman, D. (1991) · Molecular and Biochemical Parasitology · doi:10.1016/0166-6851(91)90217-t · Cited by 28
PHOTOCONTROL OF ORGANELLE BIOGENESIS IN Euglena
Schwartzbach, S. D. (1990) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1990.tb01708.x · Cited by 28
NMR probing of invisible excited states using selectively labeled RNAs
LeBlanc, R. M., Longhini, A. P., Tugarinov, V., & Dayie, T. K. (2018) · Journal of Biomolecular NMR · doi:10.1007/s10858-018-0184-3 · Cited by 27
Conservation in the Iron Responsive Element Family
Volz, K. W. (2021) · Genes · doi:10.3390/genes12091365 · Cited by 26
Iron Responsive Element-Mediated Responses to Iron Dyshomeostasis in Alzheimer’s Disease
Hin, N., Newman, M., Pederson, S., & Lardelli, M. T. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210200 · Cited by 28
Iron metabolism in mammalian cells
Walker, B., Tiong, J., & Jefferies, W. A. (2001) · International review of cytology · doi:10.1016/s0074-7696(01)11020-x · Cited by 27
Air pollution particles and iron homeostasis
Ghio, A. J., Soukup, J. M., & Dailey, L. A. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.05.026 · Cited by 27
Bevilacqua, M. A., Faniello, M. C., Russo, T., Cimino, F., & Costanzo, F. S. (1994) · Gene · doi:10.1016/0378-1119(94)90587-8 · Cited by 26
Expression of iron‐related proteins during infection by bovine herpes virus type‐1
Maffettone, C., Martino, L. D., Irace, C., Santamaria, R., Pagnini, U., Iovane, G., & Colonna, A. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21618 · Cited by 25
Lin, S.-J., Lee, D., Wang, H., Kang, S.-T., Hwang, P., Kou, G., Huang, M.-F., Chang, G., & Lo, C. (2014) · Journal of Virology · doi:10.1128/jvi.02318-14 · Cited by 25
Habel, M., & Jung, D. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.01.097 · Cited by 25
Swenson, G. R., Patiño, M. M., Beck, M. M., Gaffield, L., & Walden, W. E. (1991) · BioMetals · doi:10.1007/bf01135557 · Cited by 25
Gegout, V., Schlegl, J., Schläger, B., Hentze, M. W., Reinbolt, J., Ehresmann, B., Ehresmann, C., & Romby, P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.21.15052 · Cited by 25
The impact of oxidative stress on eukaryotic iron metabolism
Rouault, T. A., & Klausner, R. D. (1996) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-9088-5_12 · Cited by 25
Lafuse, W. P., Alvarez, G. R., & Zwilling, B. S. (2000) · Biochemical Journal · doi:10.1042/bj3510687 · Cited by 25
Iron‐induced energy supply deficiency and mitochondrial fragmentation in neurons
Huang, X. T., Liu, X., Ye, C. Y., Tao, L.-X., Zhou, H., & Zhang, H. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14621 · Cited by 26
Cairo, G., Tacchini, L., Schiaffonati, L., Rappocciolo, E., Ventura, E., & Pietrangelo, A. (1989) · Biochemical Journal · doi:10.1042/bj2640925 · Cited by 24
Multifaceted interplays between the essential players and lipid peroxidation in ferroptosis
Liu, C., Liu, Z., Dong, Z., Liu, S., Kan, H., & Zhang, S. (2025) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2025.01.009 · Cited by 25
Li, X., Xu, K., Qiao, Y., Qu, S., Zhang, Z., & Dai, W. (2010) · Molecular Biology Reports · doi:10.1007/s11033-010-0568-2 · Cited by 23
Serrano‐Nascimento, C., Calil‐Silveira, J., Goulart-Silva, F., & Nunes, M. T. (2011) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.09.036 · Cited by 23
Regulation of ferritin H-chain expression in differentiating Friend leukemia cells
Coccia, E. M., Stellacci, E., Orsatti, R., Testa, U., & Battistini, A. (1995) · Blood · doi:10.1182/blood.v86.4.1570.bloodjournal8641570 · Cited by 23
Nucleotide sequence of cDNA encoding rabbit ferritin L chain
Daniels-McQueen, S., Ray, A., Walden, W. E., Ray, B. K., Brown, P. H., & Thach, R. E. (1988) · Nucleic Acids Research · doi:10.1093/nar/16.15.7741 · Cited by 23
Defective biliary copper excretion in Wilson's disease: the role of caeruloplasmin
DAVIS, W., Chowrimootoo, G., & Seymour, C. A. (1996) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.1996.tb02135.x · Cited by 22
Molecular and cellular biology of plant ferritins
Briat, J., Labouré, A., Laulhère, J. P., Lescure, A., Lobréaux, S., Pesey, H., Proudhon, D., & Wuytswinkel, O. V. (1995) · Springer eBooks · doi:10.1007/978-94-011-0503-3_39 · Cited by 22
Ferritin is a translationally regulated heat shock protein of avian reticulocytes.
Atkinson, B. G., Blaker, T. W., Tomlinson, J., & Dean, R. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)77281-5 · Cited by 21
Neupert, B., Menotti, E., & Kühn, L. C. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.14.2579 · Cited by 20
Murine ferritin heavy chain: isolation and characterization of a functional gene
Kwak, E. L., Torti, S. V., & Torti, F. M. (1990) · Gene · doi:10.1016/0378-1119(90)90396-9 · Cited by 20
WEISS, G., GRAZIADEI, I., URBANEK, M., GRÜNEWALD, K., & VOGEL, W. (1996) · Biochemical Journal · doi:10.1042/bj3190897 · Cited by 19
Chen, S.-C., & Olsthoorn, R. C. L. (2019) · Gene · doi:10.1016/j.gene.2019.06.012 · Cited by 19
Perng, V., Li, C., Klocke, C. R., Navazesh, S. E., Pinneles, D., Lein, P. J., & Ji, P. (2020) · Journal of Nutrition · doi:10.1093/jn/nxaa326 · Cited by 19
Iron-responsive element-binding protein in hemochromatosis liver and intestine
Flanagan, P. R., Hajdu, A., & Adams, P. C. (1995) · Hepatology · doi:10.1002/hep.1840220321 · Cited by 19
Zhou, Y., & Ragan, M. A. (1995) · Plant Molecular Biology · doi:10.1007/bf00021189 · Cited by 19
Thyrotropin and Adenosine 3′, 5′- Monophosphate Stimulate the Activity of the Ferritin-H Promoter
Chazenbalk, G. D., Wadsworth, H., FOTI, D. P., & Rapoport, B. (1990) · Molecular Endocrinology · doi:10.1210/mend-4-8-1117 · Cited by 19
Veyrune, J., Hesketh, J. E., & Blanchard, J. (1997) · Progress in molecular and subcellular biology · doi:10.1007/978-3-642-60471-3_3 · Cited by 19
Identification of proteins associating with poly(A)‐binding‐protein mRNA
Berger, L., Bag, J., & Sells, B. H. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb16688.x · Cited by 19
Xue, G., & Morris, R. J. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb09740.x · Cited by 18
Allele-specific quantification of TNFA transcripts in rheumatoid arthritis
Brinkman, B. M. N., Huizinga, T. W. J., Breedveld, F. C., & Verweij, C. L. (1996) · Human Genetics · doi:10.1007/bf02346195 · Cited by 18
Frise, M. C., Holdsworth, D., Johnson, A. W., Chung, Y. J., Curtis, M. K., Cox, P. J., Clarke, K., Tyler, D. J., Roberts, D. J., Ratcliffe, P. J., et al. (2022) · Scientific Reports · doi:10.1038/s41598-021-03968-4 · Cited by 21
Données récentes sur le métabolisme du fer : un état de transition
Cadet, E., Gadenne, M., Capron, D., & Rochette, J. (2004) · La Revue de Médecine Interne · doi:10.1016/j.revmed.2004.09.024 · Cited by 20
Induction of Ferritin Synthesis in Cells Infected with Mengo Virus
Mulvey, M. R., Kühn, L. C., & Scraba, D. G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.16.9851 · Cited by 17
Pantopoulos, K., Johansson, H. E., & Hentze, M. W. (1994) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)60856-9 · Cited by 17
Effects of alterations in the leader sequence of Rous sarcoma virus RNA on initiation of translation
Hensel, C. H., Petersen, R. B., & Hackett, P. B. (1989) · Journal of Virology · doi:10.1128/jvi.63.11.4986-4990.1989 · Cited by 17
Targeting mitochondria-regulated ferroptosis: A new frontier in Parkinson's disease therapy
Wang, W., Thomas, E. R., Xiao, R., Chen, T., Guo, Q., Liu, K., Yang, Y., & Li, X. (2025) · Neuropharmacology · doi:10.1016/j.neuropharm.2025.110439 · Cited by 18
Muckenthaler, M. U., & Hentze, M. W. (1997) · Progress in molecular and subcellular biology · doi:10.1007/978-3-642-60471-3_5 · Cited by 16
Borovská, I., Zhang, C., Dülk, S.-L., Morandi, E., Cardoso, M. F. S., Bourkia, B. M., van den Homberg, D. A. L., Wolfinger, M. T., Velema, W. A., & Incarnato, D. (2025) · Nature Biotechnology · doi:10.1038/s41587-025-02739-0 · Cited by 17
Bilateral cataract in a subject carrying a C to A transition in the L ferritin promoter region
Faniello, M. C., Sanzo, M. D., Quaresima, B., Nisticò, A., Fregola, A., Grosso, M., Cuda, G., & Costanzo, F. S. (2009) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2009.02.013 · Cited by 15
Differential translation of two distinct preprosomatostatin messenger RNAs.
Danoff, A., & Shields, D. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37614-2 · Cited by 15
Differential Processing of the Ferritin Heavy Chain mRNA in Human Liver and Adult Human Brain
Dhar, M. S., & Joshi, J. G. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb07452.x · Cited by 15
Murtagh, J. J., Moss, J., & Vaughan, M. M. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.5.842 · Cited by 14
Henderson, B. R., & Kühn, L. C. (1997) · Progress in molecular and subcellular biology · doi:10.1007/978-3-642-60471-3_6 · Cited by 15
Recent Advance in Molecular Iron Metabolism: Translational Disorders of Ferritin
Kato, J., & Niitsu, Y. (2002) · International Journal of Hematology · doi:10.1007/bf02982789 · Cited by 13
Faniello, M. C., Fregola, A., Nisticò, A., Quaresima, B., Crugliano, T., Faraonio, R., Puzzonia, P., Baudi, F., Parlato, G., Cuda, G., et al. (2006) · Gene · doi:10.1016/j.gene.2006.02.034 · Cited by 13
Characterization of an insect ferritin subunit synthesized in a cell-free system
Ketola-Pirie, C. A. (1990) · Biochemistry and Cell Biology · doi:10.1139/o90-148 · Cited by 13
Erythroid 5‐aminolaevulinate synthase activity during normal and iron deficient erythropoiesis
Houston, T. E., Moore, M. R., McColl, K. E. L., & Fitzsimons, E. J. (1991) · British Journal of Haematology · doi:10.1111/j.1365-2141.1991.tb04489.x · Cited by 13
Three novel and two recurrent mutations of the Norrie disease gene in patients with Norrie Syndrome
Fuchs, S., van de Pol, T. J. R., Beudt, U., Kellner, U., Meire, F., Berger, W., & Gal, A. (1996) · Radboud Repository (Radboud University) · doi:10.1002/(sici)1098-1004(1996)8:1<85::aid-humu15>3.3.co;2-r · Cited by 13
Iron Regulation of Transferrin Receptor mRNA Stability
Harford, J. B. (1993) · Elsevier eBooks · doi:10.1016/b978-0-08-091652-1.50015-3 · Cited by 13
The regulation of iron absorption: One more piece in the puzzle?
Halliday, J. W. (1992) · Gastroenterology · doi:10.1016/0016-5085(92)90201-9 · Cited by 13
Methods for Studying Iron Regulatory Protein 1: An Important Protein in Human Iron Metabolism
Holmes‐Hampton, G. P., Ghosh, M. C., & Rouault, T. A. (2017) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2017.09.006 · Cited by 13
Su, X., Du, L., Li, Y., Li, T., Li, D., Wang, M., & He, J. (2009) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2009.06.014 · Cited by 12
The Fate of Iron in The Organism and Its Regulatory Pathways
Mladěnka, P., Hrdina, R., Hübl, M., & Šimůnek, T. (2005) · Acta Medica (Hradec Kralove Czech Republic) · doi:10.14712/18059694.2018.40 · Cited by 12
Habel, M., Lemieux, R., & Jung, D. (2004) · Journal of Cellular Physiology · doi:10.1002/jcp.20229 · Cited by 12
Nichol, H., & Winzerling, J. J. (2002) · Insect Biochemistry and Molecular Biology · doi:10.1016/s0965-1748(02)00110-8 · Cited by 12
Schmidt, E. E., & Merrill, G. F. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.7.3726-3734.1991 · Cited by 12
Rethinking IRPs/IRE system in neurodegenerative disorders: Looking beyond iron metabolism
Yao, Z., Fu, L., Jia, F., Bi, M., Jiao, Q., Chen, X., Du, X., & Jiang, H. F. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101511 · Cited by 11
Iron–Sulfur Cluster Metabolism Impacts Iron Homeostasis, Ferroptosis Sensitivity, and Human Disease
Sviderskiy, V. O., Terzi, E. M., & Possemato, R. (2019) · Springer eBooks · doi:10.1007/978-3-030-26780-3_12 · Cited by 12
Two covariance models for iron-responsive elements
Stevens, S. G., Gardner, P. P., & Brown, C. M. (2011) · RNA Biology · doi:10.4161/rna.8.5.16037 · Cited by 11
Peffley, D. M., & Gayen, A. K. (1995) · Somatic Cell and Molecular Genetics · doi:10.1007/bf02254770 · Cited by 11
Infante, A. A., Infante, D., & Rimland, J. M. (1993) · Developmental Genetics · doi:10.1002/dvg.1020140108 · Cited by 11
Srai, S. K., & Sharp, P. (2011) · Humana Press eBooks · doi:10.1007/978-1-60327-485-2_1 · Cited by 11
Metabolic capacity regulates iron homeostasis in endothelial cells
Carraway, M. S., Suliman, H. B., Madden, M. C., Piantadosi, C. A., & Ghio, A. J. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.09.005 · Cited by 10
Translational Control by Iron-Responsive Elements
Hentze, M. W. (1994) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-2554-7_13 · Cited by 10
Wang, S. Y., & Rowe, J. W. (1988) · Endocrinology · doi:10.1210/endo-123-2-1008 · Cited by 10
Tip of the Iceberg: A New Wave of Iron–Sulfur Cluster Proteins Found in Viruses
Heffner, A. L., & Maio, N. (2024) · Inorganics · doi:10.3390/inorganics12010034 · Cited by 8
Iron Responsive Element (IRE)-mediated responses to iron dyshomeostasis in Alzheimer’s diseasePreprint
Hin, N., Newman, M., Pederson, S., & Lardelli, M. T. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.01.071498 · Cited by 9
Iron, Copper, and Selenium: Cancer's Thing for Redox BlingPreprint
Terzi, E. M., & Possemato, R. (2023) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a041545 · Cited by 9
The Re-Emerging Role of Iron in Infection and Immunity
Hamad, M. A., & Bajbouj, K. (2016) · Integrative Molecular Medicine · doi:10.15761/imm.1000251 · Cited by 8
Habel, M., & Jung, D. (2006) · Free Radical Research · doi:10.1080/10715760500484344 · Cited by 8
Shterman, N., Kupfer, B., & Moroz, C. (1989) · PubMed · Cited by 8
Daniels-McQueen, S., Goessling, L. S., & Thach, R. E. (1992) · Gene · doi:10.1016/0378-1119(92)90215-b · Cited by 8
Translational modulation in hepatitis B virus preS-S open reading frame expression
Gallina, A., Koning, A. D., Rossi, F., Calogero, R., Manservigi, R., & Milanesi, G. (1992) · Journal of General Virology · doi:10.1099/0022-1317-73-1-139 · Cited by 8
Metadata
- Authors
- Aziz, N., & Munro, H. N.
- Affiliations
- Massachusetts Institute of Technology (US)
- ORCID
- Aziz, N
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1987-12
- Volume
- 84
- Issue
- 23
- Pages
- 8478-8482
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC299567
- OpenAlex
- W2032558977
- Cited by
- 368
- References
- 28
- Citations by year
- 2026: 3 · 2025: 8 · 2024: 3 · 2023: 1 · 2022: 2 · 2021: 4 · 2020: 4 · 2019: 3 · 2018: 7 · 2017: 3 · 2016: 6 · 2015: 2 · 2014: 8 · 2013: 5 · 2012: 3
- FWCI
- 16.87
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- iron regulation, ferritin, mRNA translation, 5' untranslated region, translational regulation, polysome association, cis-regulatory elements, hepatoma cells, iron storage
- MeSH terms
- Animals, Cell Line, DNA Mutational Analysis, Ferritins, Gene Expression Regulation, Iron, Recombinant Fusion Proteins, Regulatory Sequences, Nucleic Acid, RNA, Messenger, Transfection, Protein Biosynthesis, Rats
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review