SIREs: searching for iron-responsive elements

Cloning and characterization of a mammalian proton-coupled metal-ion transporter

Gunshin, H., Mackenzie, B., Berger, U. V., Gunshin, Y., Romero, M. F., Boron, W. F., Nussberger, S., Gollan, J. L., & Hediger, M. A. (1997) · Nature · doi:10.1038/41343 · Cited by 3,166 · see citing works

The Vienna RNA Websuite

Gruber, A. R., Lorenz, R., Bernhart, S. H., Neuböck, R., & Hofacker, I. L. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn188 · Cited by 2,717 · see citing works

A Novel Duodenal Iron-Regulated Transporter, IREG1, Implicated in the Basolateral Transfer of Iron to the Circulation

McKie, A. T., Marciani, P., Rolfs, A., Brennan, K., Wehr, K., Barrow, D., Miret, S., Bomford, A., Peters, T. J., Farzaneh, F., et al. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80425-6 · Cited by 1,422 · see citing works

Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network

Muckenthaler, M. U., Galy, B., & Hentze, M. W. (2008) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.28.061807.155521 · Cited by 701 · see citing works

An iron-responsive element type II in the 5'-untranslated region of the Alzheimer's amyloid precursor protein transcript

Rogers, J. T., Randall, J. D., Cahill, C. M., Eder, P. S., Huang, X., Gunshin, H., Leiter, L., McPhee, J., Sarang, S. S., Utsuki, T., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207435200 · Cited by 551 · see citing works

RNAMotif, an RNA secondary structure definition and search algorithm

Macke, T. J. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.22.4724 · Cited by 469 · see citing works

Identification of a novel iron‐responsive element in murine and human erythroid delta‐aminolevulinic acid synthase mRNA.

Dandekar, T., Stripecke, R., Gray, N. K., Goossen, B., Constable, A., Johansson, H. E., & Hentze, M. W. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07716.x · Cited by 347 · see citing works

IRP-1 binding to ferritin mRNA prevents the recruitment of the small ribosomal subunit by the cap-binding complex eIF4F.

Muckenthaler, M., Gray, N. K., & Hentze, M. W. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80282-8 · Cited by 297 · see citing works

Iron-regulatory proteins limit hypoxia-inducible factor-2α expression in iron deficiency

Sanchez, M., Galy, B., Muckenthaler, M. U., & Hentze, M. W. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1222 · Cited by 294 · see citing works

Mutation in the iron responsive element of the L ferritin mRNA in a family with dominant hyperferritinaemia and cataract

Beaumont, C., Leneuve, P., Devaux, I., Scoazec, J.-Y., Berthier, M., Loiseau, M.-N., Grandchamp, B., & Bonneau, D. (1995) · Nature Genetics · doi:10.1038/ng1295-444 · Cited by 293 · see citing works

Evidence that the pathway of transferrin receptor mRNA degradation involves an endonucleolytic cleavage within the 3′ UTR and does not involve poly(A) tail shortening.

Binder, R., Horowitz, J. A., Basilion, J. P., Koeller, D. M., Klausner, R. D., & Harford, J. B. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06466.x · Cited by 289 · see citing works

Post-transcriptional control of gene expression: a genome-wide perspective

Mata, J., Marguerat, S., & Bähler, J. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.07.005 · Cited by 288 · see citing works

A cis-acting element is necessary and sufficient for translational regulation of human ferritin expression in response to iron.

Hentze, M. W., Rouault, T. A., Caughman, S. W., Dancis, A., Harford, J. B., & Klausner, R. D. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.19.6730 · Cited by 249 · see citing works

A cytosolic protein binds to structural elements within the iron regulatory region of the transferrin receptor mRNA.

Koeller, D. M., Casey, J. L., Hentze, M. W., Gerhardt, E. M., Chan, L.-N. L., Klausner, R. D., & Harford, J. B. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.10.3574 · Cited by 242 · see citing works

A mutation, in the iron-responsive element of H ferritin mRNA, causing autosomal dominant iron overload.

Kato, J., Fujikawa, K., Kanda, M., Fukuda, N., Sasaki, K., Takayama, T., Kobune, M., Takada, K., Takimoto, R., Hamada, H., et al. (2001) · The American Journal of Human Genetics · doi:10.1086/321261 · Cited by 211 · see citing works

Iron regulatory proteins are essential for intestinal function and control key iron absorption molecules in the duodenum

Galy, B., Ferring-Appel, D., Kaden, S., Gröne, H.-J., & Hentze, M. W. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.10.006 · Cited by 195 · see citing works

Translational regulation of mammalian and Drosophila citric acid cycle enzymes via iron-responsive elements.

Gray, N. K., Pantopoulos, K., Dandekar, T., Ackrell, B. A. C., & Hentze, M. W. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.10.4925 · Cited by 187 · see citing works

Combinatorial mRNA Regulation: Iron Regulatory Proteins and Iso-iron-responsive Elements (Iso-IREs)

Theil, E. C., & Eisenstein, R. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.r000019200 · Cited by 162 · see citing works

UTRdb and UTRsite: a collection of sequences and regulatory motifs of the untranslated regions of eukaryotic mRNAs

Mignone, F. (2004) · Nucleic Acids Research · doi:10.1093/nar/gki021 · Cited by 160 · see citing works

Optimal sequence and structure of iron-responsive elements. Selection of RNA stem-loops with high affinity for iron regulatory factor

Henderson, B. R., Menotti, E., Bonnard, C., & Kühn, L. C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32466-3 · Cited by 151 · see citing works

Differences in the RNA binding sites of iron regulatory proteins and potential target diversity.

Butt, J., Kim, H. Y., Basilion, J. P., Cohen, S., Iwaï, K., Philpott, C. C., Altschul, S. F., Klausner, R. D., & Rouault, T. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.9.4345 · Cited by 139 · see citing works

Complete loss of iron regulatory proteins 1 and 2 prevents viability of murine zygotes beyond the blastocyst stage of embryonic development

Smith, S., Ghosh, M. C., Ollivierre, H., Tong, W. H., & Rouault, T. A. (2006) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2005.12.006 · Cited by 123 · see citing works

A model for the structure and functions of iron-responsive elements

Hentze, M. W., Caughman, S. W., Casey, J. L., Kodier, D. M., Rouault, T. A., Harford, J. B., & Klausner, R. D. (1988) · Gene · doi:10.1016/0378-1119(88)90145-x · Cited by 116 · see citing works

Iron Regulatory Proteins 1 and 2 Bind Distinct Sets of RNA Target Sequences

Henderson, B. R., Menotti, E., & Kühn, L. C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.9.4900 · Cited by 112 · see citing works

Iron Regulation and the Cell Cycle

Sánchez, M., Galy, B., Dandekar, T., Bengert, P., Vainshtein, Y., Stolte, J., Muckenthaler, M. U., & Hentze, M. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603876200 · Cited by 112 · see citing works

Combining SELEX with quantitative assays to rapidly obtain accurate models of protein-DNA interactions

Liu, J. (2005) · Nucleic Acids Research · doi:10.1093/nar/gni139 · Cited by 100 · see citing works

A cytosolic protein binds to structural elements within the iron regulatory region of the transferrin receptor mRNA

Koeller, K. M. (1989) · Medical Entomology and Zoology · Cited by 72 · see citing works

Multiple determinants within iron-responsive elements dictate iron regulatory protein binding and regulatory hierarchy

Goforth, J. B., Anderson, S. A., Nizzi, C. P., & Eisenstein, R. S. (2010) · RNA · doi:10.1261/rna.1857210 · Cited by 71 · see citing works

A novel iron responsive element in the 3′UTR of human MRCKα

Čmejla, R., Petrák, J., & Čmejlová, J. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.12.155 · Cited by 68 · see citing works

Molecular Cloning of Mouse Glycolate Oxidase

Kohler, S. A., Menotti, E., & Kühn, L. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.4.2401 · Cited by 56 · see citing works

A software tool-box for analysis of regulatory RNA elements

Bengert, P. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg568 · Cited by 40 · see citing works

CD63 is regulated by iron via the IRE-IRP system and is important for ferritin secretion by extracellular vesicles

Yanatori, I., Richardson, D. R., Dhekne, H. S., Toyokuni, S., & Kishi, F. (2021) · Blood · doi:10.1182/blood.2021010995 · Cited by 148 · see citing works

Iron regulatory protein-1 and -2: transcriptome-wide definition of binding mRNAs and shaping of the cellular proteome by iron regulatory proteins

Sánchez, M., Galy, B., Schwanhaeusser, B., Blake, J., Bähr-Ivacevic, T., Beneš, V., Selbach, M., Muckenthaler, M. U., & Hentze, M. W. (2011) · Blood · doi:10.1182/blood-2011-04-343541 · Cited by 132 · see citing works

Snx3 Regulates Recycling of the Transferrin Receptor and Iron Assimilation

Chen, C., Garcia‐Santos, D., Ishikawa, Y., Seguin, A., Li, L., Fegan, K. H., Hildick-Smith, G. J., Shah, D. I., Cooney, J. D., Chen, W., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.01.013 · Cited by 124 · see citing works

Low serum iron levels are associated with elevated plasma levels of coagulation factor VIII and pulmonary emboli/deep venous thromboses in replicate cohorts of patients with hereditary haemorrhagic telangiectasia

Livesey, J. A., Manning, R. A., MEEK, J. H., Jackson, J. E., Kulinskaya, E., Laffan, M., & Shovlin, C. L. (2011) · Thorax · doi:10.1136/thoraxjnl-2011-201076 · Cited by 121 · see citing works

Iron Regulatory Proteins Mediate Host Resistance to Salmonella Infection

Nairz, M., Ferring-Appel, D., Casarrubea, D., Sonnweber, T., Viatte, L., Schroll, A., Haschka, D., Fang, F. C., Hentze, M. W., Weiss, G., et al. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.06.017 · Cited by 103 · see citing works

Genome-Wide Identification of Fas/CD95 Alternative Splicing Regulators Reveals Links with Iron Homeostasis

Tejedor, J. R., Papasaikas, P., & Valcárcel, J. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.10.029 · Cited by 91 · see citing works

The Importance of the Stem Cell Marker Prominin-1/CD133 in the Uptake of Transferrin and in Iron Metabolism in Human Colon Cancer Caco-2 Cells

Bourseau-Guilmain, E., Griveau, A., Benoît, J., & Garcion, E. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025515 · Cited by 80 · see citing works

Thrombopoietin receptor–independent stimulation of hematopoietic stem cells by eltrombopag

Kao, Y.-R., Chen, J., Narayanagari, S.-R., Todorova, T. I., Aivalioti, M. M., Ferreira, M. D. S., Ramos, P. M., Pallaud, C., Mantzaris, I., Shastri, A., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aas9563 · Cited by 69 · see citing works

FTH1 Pseudogenes in Cancer and Cell Metabolism

Sanzo, M. D., Quaresima, B., Biamonte, F., Palmieri, C., & Faniello, M. C. (2020) · Cells · doi:10.3390/cells9122554 · Cited by 61 · see citing works

The Role of Butyrylcholinesterase and Iron in the Regulation of Cholinergic Network and Cognitive Dysfunction in Alzheimer’s Disease Pathogenesis

Jasiecki, J., Targońska, M., & Wasąg, B. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22042033 · Cited by 64 · see citing works

The Iron-Responsive Genome of the Chiton Acanthopleura granulata

Varney, R., Speiser, D. I., McDougall, C., Degnan, B. M., & Kocot, K. M. (2020) · Genome Biology and Evolution · doi:10.1093/gbe/evaa263 · Cited by 59 · see citing works

Overexpression of the MRI Reporter Genes Ferritin and Transferrin Receptor Affect Iron Homeostasis and Produce Limited Contrast in Mesenchymal Stem Cells

Pereira, S. M., Moss, D., Williams, S. R., Murray, P. A., & Taylor, A. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160715481 · Cited by 51 · see citing works

Identification and characterization of four ferritin subunits involved in immune defense of the Yesso scallop (Patinopecten yessoensis)

Zhang, Y., Zhang, R., Zou, J., Hu, X., Wang, S., Zhang, L., & Bao, Z. (2013) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2013.01.023 · Cited by 51 · see citing works

Novel mutations in the ferritin-L iron-responsive element that only mildly impair IRP binding cause hereditary hyperferritinaemia cataract syndrome

Luscieti, S., Tolle, G., Aranda, J., Campos, C. B., Risse, F., Morán, É., Muckenthaler, M. U., & Sánchez, M. (2013) · Orphanet Journal of Rare Diseases · doi:10.1186/1750-1172-8-30 · Cited by 49 · see citing works

Genome-wide characterization of the NRAMP gene family in Phaseolus vulgaris provides insights into functional implications during common bean development

Ishida, J. K., Caldas, D. G. G., Oliveira, L. R., Frederici, G. C., Leite, L. M. P., & Mui, T. S. (2018) · Genetics and Molecular Biology · doi:10.1590/1678-4685-gmb-2017-0272 · Cited by 46 · see citing works

Human STEAP3 maintains tumor growth under hypoferric condition

Isobe, T., Baba, E., Arita, S., Komoda, M., Tamura, S., Shirakawa, T., Ariyama, H., Takaishi, S., Kusaba, H., Ueki, T., et al. (2011) · Experimental Cell Research · doi:10.1016/j.yexcr.2011.07.022 · Cited by 42 · see citing works

The Causal Effects of Blood Iron and Copper on Lipid Metabolism Diseases: Evidence from Phenome-Wide Mendelian Randomization Study

Zhou, J.-Q., Liu, C., Francis, M., Sun, Y.-T., Ryu, M.-S., Grider, A., & Ye, K. (2020) · medRxiv · doi:10.3390/nu12103174 · Cited by 31 · see citing works

The actin-binding protein profilin 2 is a novel regulator of iron homeostasis

Luscieti, S., Galy, B., Gutiérrez, L., Reinke, M., Couso, J., Shvartsman, M., Pascale, A. D., Witke, W., Hentze, M. W., Boyl, P. P., et al. (2017) · Blood · doi:10.1182/blood-2016-11-754382 · Cited by 32 · see citing works

Trace Elements and Healthcare: A Bioinformatics Perspective

Zhang, Y. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-5717-5_4 · Cited by 33 · see citing works

Appetite and ghrelin levels in iron deficiency anemia and the effect of parenteral iron therapy: A longitudinal study

Ghrayeb, H., Elias, M. S., Nashashibi, J., Awni, Y., Manal, M. A., Mahagna, L., Masalha, R., Schwartz, N., & Elias, A. (2020) · PLoS ONE · doi:10.1371/journal.pone.0234209 · Cited by 31 · see citing works

Multiple ferritin subunit genes of the Pacific oyster Crassostrea gigas and their distinct expression patterns during early development

Huan, P., Liu, G., Wang, H., & Liu, B. (2014) · Gene · doi:10.1016/j.gene.2014.05.027 · Cited by 28 · see citing works

L-Ferritin: One Gene, Five Diseases; from Hereditary Hyperferritinemia to Hypoferritinemia—Report of New Cases

Cadenas, B., Fita‐Torró, J., Cortés, M. B., Hernández‐Rodríguez, I., Fuster, J. L., Llinares, M. E., Galera, A., Romero, J., Pérez-Montero, S., Tornador, C., et al. (2019) · Pharmaceuticals · doi:10.3390/ph12010017 · Cited by 28 · see citing works

Siderophore-mediated iron trafficking in humans is regulated by iron

Liu, Z., Lanford, R. E., Mueller, S., Gerhard, G. S., Luscieti, S., Sánchez, M., & Devireddy, L. R. (2012) · Journal of Molecular Medicine · doi:10.1007/s00109-012-0899-7 · Cited by 27 · see citing works

Conservation in the Iron Responsive Element Family

Volz, K. W. (2021) · Genes · doi:10.3390/genes12091365 · Cited by 26 · see citing works

Iron Responsive Element-Mediated Responses to Iron Dyshomeostasis in Alzheimer’s Disease

Hin, N., Newman, M., Pederson, S., & Lardelli, M. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210200 · Cited by 28 · see citing works

Silencing of Iron and Heme-Related Genes Revealed a Paramount Role of Iron in the Physiology of the Hematophagous Vector Rhodnius prolixus

Walter‐Nuno, A. B., Taracena, M. L., Mesquita, R. D., de Oliveira, P. L., & Paiva‐Silva, G. O. (2018) · Frontiers in Genetics · doi:10.3389/fgene.2018.00019 · Cited by 25 · see citing works

Insights into the Roles of the Sideroflexins/SLC56 Family in Iron Homeostasis and Iron-Sulfur Biogenesis

Tifoun, N., Heras, J. M. D. L., Guillaume, A., Bouleau, S., Mignotte, B., & Floch, N. L. (2021) · Biomedicines · doi:10.3390/biomedicines9020103 · Cited by 24 · see citing works

Cloning and Characterisation of Multiple Ferritin Isoforms in the Atlantic Salmon (Salmo salar)

Lee, J.-H., Pooley, N. J., Mohd-Adnan, A., & Martín, S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103729 · Cited by 24 · see citing works

Molecular characterization of two ferritins of the scallop Argopecten purpuratus and gene expressions in association with early development, immune response and growth rate

de la Peña, T. C., Cárcamo, C. B., Díaz, M. I., Brokordt, K., & Winkler, F. M. (2016) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2016.03.007 · Cited by 24 · see citing works

Gene Expression Profiling in Entamoeba histolytica Identifies Key Components in Iron Uptake and Metabolism

Hernández‐Cuevas, N. A., Weber, C., Hon, C.-C., & Guillén, N. (2014) · PLoS ONE · doi:10.1371/journal.pone.0107102 · Cited by 22 · see citing works

Mining Functional Elements in Messenger RNAs: Overview, Challenges, and Perspectives

Ahmed, F., Benedito, V. A., & Zhao, P. X. (2011) · Frontiers in Plant Science · doi:10.3389/fpls.2011.00084 · Cited by 22 · see citing works

Indicators of iron status are correlated with adiponectin expression in adipose tissue of patients with morbid obesity

Bars, F. P., Bonnet, F., Loréal, O., Loupp, A.-G. L., Ropert, M., Letessier, E., Prieur, X., Bach‐Ngohou, K., Deugnier, Y., Fromenty, B., et al. (2015) · Diabetes & Metabolism · doi:10.1016/j.diabet.2015.10.007 · Cited by 22 · see citing works

Transcriptome analyses of 7-day-old zebrafish larvae possessing a familial Alzheimer’s disease-like mutation in psen1 indicate effects on oxidative phosphorylation, ECM and MCM functions, and iron homeostasis

Dong, Y., Newman, M., Pederson, S., Barthelson, K., Hin, N., & Lardelli, M. T. (2021) · BMC Genomics · doi:10.1186/s12864-021-07509-1 · Cited by 21 · see citing works

A mutation in the iron-responsive element of ALAS2 is a modifier of disease severity in a patient suffering from CLPX associated erythropoietic protoporphyria

Ducamp, S., Luscieti, S., Ferrer-Cortés, X., Nicolas, G., Manceau, H., Peoc’h, K., Yien, Y. Y., Kannengiesser, C., Gouya, L., Puy, H., et al. (2021) · Haematologica · doi:10.3324/haematol.2020.272450 · Cited by 21 · see citing works

Ironing Out the Mechanism of gp130 Signaling

Osman, E. E. A., & Neamati, N. (2024) · Pharmacological Reviews · doi:10.1124/pharmrev.124.001245 · Cited by 20 · see citing works

Iron metabolic pathways in the processes of sponge plasticity

Finoshin, A. D., Adameyko, K. I., Mikhailov, K. V., Кравчук, О. И., Georgiev, A., Горностаев, Н. Г., Kosevich, I. A., Mikhailov, V. S., Gazizova, G. R., Shagimardanova, E. I., et al. (2020) · PLoS ONE · doi:10.1371/journal.pone.0228722 · Cited by 20 · see citing works

Ferroptosis in Alzheimer’s Disease: The Regulatory Role of Glial Cells

Xu, J., Shen, R., Qian, M., Zhou, Z., Xie, B., Jiang, Y. Q., Yu, Y., & Dong, W. (2025) · Journal of Integrative Neuroscience · doi:10.31083/jin25845 · Cited by 19 · see citing works

Heavy and light chain homologs of ferritin are essential for blood-feeding and egg production of the ectoparasitic copepod Lepeophtheirus salmonis

Heggland, E. I., Tröße, C., Eichner, C., & Nilsen, F. (2019) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2019.111197 · Cited by 19 · see citing works

Conservative and Atypical Ferritins of Sponges

Adameyko, K. I., Burakov, A. V., Finoshin, A. D., Mikhailov, K. V., Кравчук, О. И., Kozlova, O., Горностаев, Н. Г., Cherkasov, A. V., Erokhov, P. A., Indeykina, M. I., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168635 · Cited by 19 · see citing works

Cloning, expression, and function of ferritins in the tick Haemaphysalis flava

Zhao, Y., Liu, L., Liu, J.-B., Wu, C., Duan, D.-Y., & Cheng, T. (2021) · Ticks and Tick-borne Diseases · doi:10.1016/j.ttbdis.2021.101892 · Cited by 18 · see citing works

Effect of iron on cholesterol 7α-hydroxylase expression in alcohol-induced hepatic steatosis in mice

Liang, H., Huang, H., Tan, P., Liu, Y., Nie, J., Zhang, Y., Zhang, K.-L., Diao, Y., He, Q., Hou, B., et al. (2017) · Journal of Lipid Research · doi:10.1194/jlr.m074534 · Cited by 18 · see citing works

Yolk proteins of the schistosomiasis vector snail Biomphalaria glabrata revealed by multi-omics analysis

Habib, M. R., Bu, L., Posavi, M., Zhong, D., Yan, G., & Zhang, S. (2024) · Scientific Reports · doi:10.1038/s41598-024-52392-x · Cited by 17 · see citing works

Iron inhibits glioblastoma cell migration and polarization

Shenoy, G., Kheirabadi, S., Ataie, Z., Sahu, A. P., Palsa, K., Wade, Q. W., Khunsriraksakul, C., Khristov, V., Slagle‐Webb, B., Lathia, J. D., et al. (2023) · The FASEB Journal · doi:10.1096/fj.202202157rr · Cited by 16 · see citing works

Iron-mediated post-transcriptional regulation in Toxoplasma gondii

Sloan, M. A., Scott, A., Aghabi, D., Mrvova, L., & Harding, C. R. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1012857 · Cited by 12 · see citing works

Regulatory Multidimensionality of Gas Vesicle Biogenesis inHalobacterium salinarumNRC-1

Yao, A. I., & Facciotti, M. T. (2011) · Archaea · doi:10.1155/2011/716456 · Cited by 12 · see citing works

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 · see citing works

Tuning the engine

Dassi, E., & Quattrone, A. (2012) · RNA Biology · doi:10.4161/rna.22035 · Cited by 12 · see citing works

Molecular Evolution of Multiple-Level Control of Heme Biosynthesis Pathway in Animal Kingdom

Tzou, W., Chu, Y., Lin, T., Hu, C., Pai, T., Liu, H., Lin, H. ‐., Cases, I., Rojas, A. M., Sánchez, M., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0086718 · Cited by 11 · see citing works

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 · see citing works

Evaluation of the iron regulatory protein-1 interactome

Connell, G. J., Danial, J. S., & Haastruthers, C. X. (2018) · BioMetals · doi:10.1007/s10534-018-0076-8 · Cited by 11 · see citing works

Diurnal control of iron responsive element containing mRNAs through iron regulatory proteins IRP1 and IRP2 is mediated by feeding rhythms

Nadimpalli, H. P., Katsioudi, G., Arpa, E. S., Chikhaoui, L., Arpat, A. B., Liechti, A., Palais, G., Tessmer, C., Hofmann, I., Galy, B., et al. (2024) · Genome biology · doi:10.1186/s13059-024-03270-2 · Cited by 11 · see citing works

Intravenous iron treatment reduces coagulability in patients with iron deficiency anaemia: a longitudinal study

Nashashibi, J., Avraham, G. R., Schwartz, N., Awni, Y., & Elias, M. S. (2019) · British Journal of Haematology · doi:10.1111/bjh.15765 · Cited by 10 · see citing works

Cloning and molecular characterization of two ferritins from red abalone Haliotis rufescens and their expressions in response to bacterial challenge at juvenile and adult life stages

de la Peña, T. C., Cárcamo, C. B., Díaz, M. I., Winkler, F. M., Lange, B. M., Mercado, L. A., & Brokordt, K. (2018) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2018.08.030 · Cited by 10 · see citing works

Characterisation of iron regulatory protein 1A and 1B in the blood-feeding copepod Lepeophtheirus salmonis

Tröße, C., Kongshaug, H., Dondrup, M., & Nilsen, F. (2015) · Experimental Parasitology · doi:10.1016/j.exppara.2015.06.010 · Cited by 9 · see citing works

Evolution of the ferritin family in vertebrates

Lee, J.-H., Wan, K., Mohd-Adnan, A., & Gabaldón, T. (2012) · Trends in Evolutionary Biology · doi:10.4081/eb.2012.e3 · Cited by 9 · see citing works

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 · see citing works

The Use of Zebrafish in Transcriptome Analysis of the Early Effects of Mutations Causing Early Onset Familial Alzheimer’s Disease and Other Inherited Neurodegenerative Conditions

Lardelli, M. T., Baer, L., Hin, N., Allen, A. G., Pederson, S., & Barthelson, K. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-230522 · Cited by 8 · see citing works

Iron excess upregulates SPNS2 mRNA levels but reduces sphingosine-1-phosphate export in human osteoblastic MG-63 cells

Peltier, L., Bendavid, C., Cavey, T., Island, M., Doyard, M., Leroyer, P., Allain, C., de Tayrac, M., Ropert, M., Loréal, O., et al. (2018) · Osteoporosis International · doi:10.1007/s00198-018-4531-8 · Cited by 8 · see citing works

Molecular evolution and gene expression of ferritin family involved in immune defense of lampreys

Guo, J., Lyu, S., Qi, Y., Chen, X., Yang, L., Zhao, C., & Wang, H. (2023) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2023.104729 · Cited by 8 · see citing works

Characteristics of the Iron-responsive Element (IRE) Stems in the Untranslated Regions of Animal mRNAs

Wang, B., Thompson, M. S., & Adkins, K. M. (2021) · The Open Biochemistry Journal · doi:10.2174/1874091x02115010026 · Cited by 7 · see citing works

Expression of four new ferritins from grooved carpet shell clam Ruditapes decussatus challenged with Perkinsus olseni and metals (Cd, Cu and Zn)

Simão, M., Leite, R. B., & Cancela, M. L. (2020) · Aquatic Toxicology · doi:10.1016/j.aquatox.2020.105675 · Cited by 6 · see citing works

New Players in Neuronal Iron Homeostasis: Insights from CRISPRi Studies

Bórquez, D. A., Castro, F. B. D., Núñez, M. T., & Urrutia, P. J. (2022) · Antioxidants · doi:10.3390/antiox11091807 · Cited by 6 · see citing works

Cellular Iron Metabolism – The IRP/IRE Regulatory Network

Joshi, R. S., Moran, E. L., & Sánchez, M. (2012) · BiblioBoard Library Catalog (Open Research Library) · doi:10.5772/34987 · Cited by 6 · see citing works

Mapping the genetic landscape of iron metabolism uncovers the SETD2 methyltransferase as a modulator of iron flux

Martinelli, A. W., Wu, C.-P., Vornbäumen, T., Coates, H. W., Jordon, L., Wit, N., Sia, J. J., Speak, A. O., & Nathan, J. A. (2025) · Science Advances · doi:10.1126/sciadv.adw9095 · Cited by 5 · see citing works

RTN4IP1 Contributes to ESCC via Regulation of Amino Acid Transporters

Wei, H., Zhao, D., Zhi, Y., Wu, Q., Ma, J., Xu, J., Liu, T., Zhang, J., Wang, P., Hu, Y., et al. (2025) · Advanced Science · doi:10.1002/advs.202406220 · Cited by 5 · see citing works

Polymorphisms in SHISA3 and RFC3 genes and their association with feed conversion ratio in Hu sheep

Lin, C., Wang, W., Zhang, D., Huang, K., Li, X., Zhang, Y., Zhao, Y., Wang, J., Zhou, B., Cheng, J., et al. (2023) · Frontiers in Veterinary Science · doi:10.3389/fvets.2022.1010045 · Cited by 5 · see citing works

Three ferritin subunit analogs in Chinese giant salamander (Andrias davidianus) and their response to microbial stimulation

You, X., Sheng, J., Liu, L., Nie, D., & Liao, Z. (2015) · Molecular Immunology · doi:10.1016/j.molimm.2015.07.020 · Cited by 4 · see citing works

Computational characterization of Iron metabolism in the Tsetse disease vector, Glossina morsitans: IRE stem-loops

Dashti, Z. J. S., Gamieldien, J., & Christoffels, A. G. (2016) · BMC Genomics · doi:10.1186/s12864-016-2932-7 · Cited by 4 · see citing works

Fifty shades of iron: Unorthodox mechanisms of iron acquisition and utilization in blood-stage Plasmodium parasites

Loveridge, K. M., & Sigala, P. A. (2026) · PLoS Pathogens · doi:10.1371/journal.ppat.1014030 · Cited by 3 · see citing works

Iron overload regulates cognitive function in rats with minimal hepatic encephalopathy by inducing an increase in frontal butyrylcholinesterase activity

Lan, H., Yang, X., Wang, M., Wang, M., Huang, X., & Wang, X. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1447965 · Cited by 3 · see citing works

Calcium as a nutrient involved in the synthesis and localization of proteins that facilitate iron uptake and efflux in enterocytes

Julián Herrera, M., Parra-Sosa, B. E., Vanessa Corrales, A., Manuel Olivares, G., Fernando Pizarro, A., & Gaitán, D. (2015) · Revista chilena de nutrición · doi:10.4067/s0717-75182015000400011 · Cited by 3 · see citing works

Introduction to Bioinformatics Resources for Post-transcriptional Regulation of Gene Expression

Quattrone, A., & Dassi, E. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-3067-8_1 · Cited by 3 · see citing works

Cytoplasmic labile iron accumulates in aging stem cells perturbing a key rheostat for identity controlPreprint

Kao, Y.-R., Chen, J., Kumari, R., Tatiparthy, M., Ma, Y., Aivalioti, M. M., Zintiridou, A., Thiruthuvanathan, V. J., Reisz, J. A., Stransky, S., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.08.03.454947 · Cited by 3 · see citing works

SIREs 3.0, an improved RNA prediction tool for iron-responsive elements

Suárez-Quintana, C., Navarro-Padilla, M., Chorostecki, U., & Sánchez, M. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf390 · Cited by 2 · see citing works

Proteínas relacionadas con el metabolismo del hierro corporal

Nutresa, G. E., Corrales-Agudelo, V., Parra-Sosa, B. E., de Antioquia, U., Herrera, L. C. B., & de Antioquia, U. (2017) · Perspectivas en Nutrición Humana · doi:10.17161/to.vi.25067 · Cited by 2 · see citing works

BEAGLE 2.0: A Web Server for RNA Secondary Structure Similarity Detection Leveraging SHAPE-directed RNA Structure Determination

Ballesio, F., Teofani, A., Carrino, C., Catalano, M., Nicolaeasa, M. L., Ausiello, G., Helmer‐Citterich, M., & Gherardini, P. F. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169154 · Cited by 2 · see citing works

Iron Neurotoxicity in Parkinson’s Disease

Urrutia, P. J., Bórquez, D. A., & Núñez, M. T. (2021) · Springer eBooks · doi:10.1007/978-3-030-71519-9_11-1 · Cited by 2 · see citing works

Iron Neurotoxicity in Parkinson’s Disease

Núñez, M. T., Urrutia, P. J., Mena, N. P., & Aguirre, P. (2014) · Springer eBooks · doi:10.1007/978-1-4614-5836-4_11 · Cited by 2 · see citing works

The iron-responsive genome of the chiton Acanthopleura granulataPreprint

Varney, R., Speiser, D. I., McDougall, C., Degnan, B. M., & Kocot, K. M. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.19.102897 · Cited by 2 · see citing works

An iron-regulated methionine redox axis governs adipose browning and cancer cachexia

Nam, J. S., Ahn, S. S., Shin, Y., Vargas‐Castillo, A., Dixon, M. S., Ahmadi, P., Schilling, K., Zandkarimi, F., Chen, A., Yoon, N. A., et al. (2026) · Nature Cancer · doi:10.1038/s43018-026-01234-y · Cited by 1 · see citing works

The Functional RNA Identification (FRID) Pipeline: Identification of Potential Pseudoknot-Containing RNA Elements as Therapeutic Targets for SARS-CoV-2Preprint

Forstmeier, P. C., Meyer, M. O., & Bevilacqua, P. C. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.03.535424 · Cited by 1 · see citing works

Keeping FIT: Iron-mediated post-transcriptional regulation in Toxoplasma gondiiPreprint

Sloan, M. A., Scott, A., & Harding, C. R. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.08.565792 · Cited by 1 · see citing works

An Iron-regulated Signalling Pathway Controls Adipose Browning and Cancer CachexiaPreprint

Nam, J. S., Dixon, M. S., Ahmadi, P., Schilling, K., Pan, S. S., Chen, Y., Yoon, N. A., Sun, Y., Lu, J., Ichimiya, S., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.16.664180 · Cited by 1 · see citing works

Investigations of Potential Modifier Genes in Hereditary Haemochromatosis

Brew, J. (2010) · ANU Open Research (Australian National University) · doi:10.25911/5d7a265387fd8

Effects of Fe3O4 nanoparticles on the transcription of genes with iron-responsive elements

Liu, Y., & Wang, J. (2012) · IEEE International Conference on Nanotechnology (IEEE-NANO) · doi:10.1109/nano.2012.6321938

De la compréhension du comportement des cellules initiatrices de cancer dans les glioblastomes au développement d'une nanomédecine adaptée. Focalisation sur le marqueur de cellules souches cancéreuses AC133 / CD133

Bourseau, E. (2011) · OpenGrey (Institut de l'Information Scientifique et Technique)

Mapping of Post-Transcriptional Regulatory Networks by Means of Mechanistic and High Throughput Data

Dassi, E. (2012) · Unitn-eprints PhD (University of Trento) · doi:10.15168/11572_368833

Bioavailability and Modes of Action of Novel Metal Based Phenanthroline Drugs

O’Leary, T. (2021) · Arrow - TU Dublin (Technological University Dublin) · doi:10.21427/7sw6-vk06

Introduction to Bioinformatics Resources for Post-transcriptional Regulation of Gene Expression

Destefanis, E., & Dassi, E. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1851-6_1

Thrombin generation assay in platelet‐poor plasma in children with iron deficiency anemia

Özdöl, U., Özdemir, Z. C., Töret, E., Özen, H., & Bör, Ö. (2023) · International Journal of Laboratory Hematology · doi:10.1111/ijlh.14206

Additional file 2 of Transcriptome analyses of 7-day-old zebrafish larvae possessing a familial Alzheimer’s disease-like mutation in psen1 indicate effects on oxidative phosphorylation, ECM and MCM functions, and iron homeostasis

Dong, Y., Newman, M., Pederson, S., Barthelson, K., Hin, N., & Lardelli, M. T. (2021) · Figshare · doi:10.6084/m9.figshare.14299320

Iron triggers Tv PI4P5K proteostasis and Arf-mediated cell membrane trafficking to regulate PIP 2 signaling crucial for multiple pathogenic activities of the parasitic protozoan Trichomonas vaginalis

Wu, K.-Y., Chen, Y., Lin, S.-F., & Hsu, H. (2024) · mBio · doi:10.1128/mbio.01864-24

Additional file 6 of Transcriptome analyses of 7-day-old zebrafish larvae possessing a familial Alzheimer’s disease-like mutation in psen1 indicate effects on oxidative phosphorylation, ECM and MCM functions, and iron homeostasis

Dong, Y., Newman, M., Pederson, S., Barthelson, K., Hin, N., & Lardelli, M. T. (2021) · Figshare · doi:10.6084/m9.figshare.14299332

Additional file 2 of Diurnal control of iron responsive element containing mRNAs through iron regulatory proteins IRP1 and IRP2 is mediated by feeding rhythms

Nadimpalli, H. P., Katsioudi, G., Arpa, E. S., Chikhaoui, L., Arpat, A. B., Liechti, A., Palais, G., Tessmer, C., Hofmann, I., Galy, B., et al. (2024) · Figshare · doi:10.6084/m9.figshare.25876315

Additional file 4 of Diurnal control of iron responsive element containing mRNAs through iron regulatory proteins IRP1 and IRP2 is mediated by feeding rhythms

Nadimpalli, H. P., Katsioudi, G., Arpa, E. S., Chikhaoui, L., Arpat, A. B., Liechti, A., Palais, G., Tessmer, C., Hofmann, I., Galy, B., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26723735

Additional file 5 of Transcriptome analyses of 7-day-old zebrafish larvae possessing a familial Alzheimer’s disease-like mutation in psen1 indicate effects on oxidative phosphorylation, ECM and MCM functions, and iron homeostasis

Dong, Y., Newman, M., Pederson, S., Barthelson, K., Hin, N., & Lardelli, M. T. (2021) · Figshare · doi:10.6084/m9.figshare.14299329

Additional file 4 of Transcriptome analyses of 7-day-old zebrafish larvae possessing a familial Alzheimer’s disease-like mutation in psen1 indicate effects on oxidative phosphorylation, ECM and MCM functions, and iron homeostasis

Dong, Y., Newman, M., Pederson, S., Barthelson, K., Hin, N., & Lardelli, M. T. (2021) · Figshare · doi:10.6084/m9.figshare.14299326

Additional file 1 of Diurnal control of iron responsive element containing mRNAs through iron regulatory proteins IRP1 and IRP2 is mediated by feeding rhythms

Nadimpalli, H. P., Katsioudi, G., Arpa, E. S., Chikhaoui, L., Arpat, A. B., Liechti, A., Palais, G., Tessmer, C., Hofmann, I., Galy, B., et al. (2024) · Figshare · doi:10.6084/m9.figshare.25876187

Additional file 3 of Transcriptome analyses of 7-day-old zebrafish larvae possessing a familial Alzheimer’s disease-like mutation in psen1 indicate effects on oxidative phosphorylation, ECM and MCM functions, and iron homeostasis

Dong, Y., Newman, M., Pederson, S., Barthelson, K., Hin, N., & Lardelli, M. T. (2021) · Figshare · doi:10.6084/m9.figshare.14299323

Additional file 3 of Diurnal control of iron responsive element containing mRNAs through iron regulatory proteins IRP1 and IRP2 is mediated by feeding rhythms

Nadimpalli, H. P., Katsioudi, G., Arpa, E. S., Chikhaoui, L., Arpat, A. B., Liechti, A., Palais, G., Tessmer, C., Hofmann, I., Galy, B., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26723732

doi:10.1093/nar/gkq371 SIREs: searching for iron-responsive elements

Campillos, M., Hentze, M. W., & Sanchez, M. (2010)

SIREs 3.0, an improved RNA prediction tool for iron-responsive elements

Suárez-Quintana, C., Navarro-Padilla, M., Chorostecki, U., & Sánchez, M. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf390 · Cited by 2 · see citing works

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 · see citing works

The Iron Regulatory Protein/Iron Responsive Element (IRP/IRE) system: functional studies of new target mRNAs and pathological implications for novel IRE mutations

Luscieti, S. (2016) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas)

Conservation in the Iron Responsive Element Family

Volz, K. W. (2021) · Genes · doi:10.3390/genes12091365 · Cited by 26 · see citing works