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Bacterial iron homeostasis
Open accessAbstract
Iron is essential to virtually all organisms, but poses problems of toxicity and poor solubility. Bacteria have evolved various mechanisms to counter the problems imposed by their iron dependence, allowing them to achieve effective iron homeostasis under a range of iron regimes. Highly efficient iron acquisition systems are used to scavenge iron from the environment under iron-restricted conditions. In many cases, this involves the secretion and internalisation of extracellular ferric chelators called siderophores. Ferrous iron can also be directly imported by the G protein-like transporter, FeoB. For pathogens, host-iron complexes (transferrin, lactoferrin, haem, haemoglobin) are directly used as iron sources. Bacterial iron storage proteins (ferritin, bacterioferritin) provide intracellular iron reserves for use when external supplies are restricted, and iron detoxification proteins (Dps) are employed to protect the chromosome from iron-induced free radical damage. There is evidence that bacteria control their iron requirements in response to iron availability by down-regulating the expression of iron proteins during iron-restricted growth. And finally, the expression of the iron homeostatic machinery is subject to iron-dependent global control ensuring that iron acquisition, storage and consumption are geared to iron availability and that intracellular levels of free iron do not reach toxic levels.
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“For comparison, E. coli has an iron content of 10 5 -10 6 molecules per cell (Andrews et al., 2003).”
From Iron in infection and immunity (2020) · cites this paper as Andrews et al., 2003
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In the citing paper
“Bacterial pathogens store iron in one of three types of proteins: ferritin, bacterioferritins, and Dps proteins.”
From Iron in infection and immunity (2013) · cites this paper as Andrews et al., 2003
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In the citing paper
“In addition, several pathogens are able to acquire TF-bound iron [51–54].”
From Iron deficiency or anemia of inflammation?: Differential diagnosis and mechanisms of anemia of inflammation (2016) · cites this paper as [51]
In the citing paper
“Binding of Fur–Fe2+ and DtxR–Fe2+ upstream of iron uptake and storage operons/genes inhibits their transcription under iron‐replete conditions. 56 , 61”
From The battle for iron in enteric infections (2020) · cites this paper as [61]
In the citing paper
“Central to iron homeostasis in Salmonella is Fur, which controls essential mechanisms of iron uptake and storage. 61 , 62”
From The battle for iron in enteric infections (2020) · cites this paper as [61]
In the citing paper
“In the host, however, free iron is scarce, an innate immune defense strategy of the host known as “nutritional immunity” (Andrews et al., 2003; Schaible and Kaufmann, 2004; Weinberg, 1975).”
From Staphylococcus aureus Targets the Duffy Antigen Receptor for Chemokines (DARC) to Lyse Erythrocytes (2015) · cites this paper as Andrews et al., 2003
In the citing paper
“The four regulatory modes of Fur have been identified: apo-Fur activation, apo-Fur repression, holo-Fur activation, and holo-Fur repression ( 28 , 60 , 62 ).”
From YdiV regulates Escherichia coli ferric uptake by manipulating the DNA-binding ability of Fur in a SlyD-dependent manner (2020) · cites this paper as [60]
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Citations
Cites
Berman, H. M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.235 · Cited by 40,196
Superoxide radical and superoxide dismutases
Fridovich, I. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000525 · Cited by 3,455
Iron-sulfur clusters: nature's modular, multipurpose structures
Beinert, H., Holm, R. H., & Münck, E. (1997) · Science · doi:10.1126/science.277.5326.653 · Cited by 1,944
Iron Metabolism in Pathogenic Bacteria
Ratledge, C., & Dover, L. G. (2000) · Annual Review of Microbiology · doi:10.1146/annurev.micro.54.1.881 · Cited by 1,539
FERRITIN: STRUCTURE, GENE REGULATION, AND CELLULAR FUNCTION IN ANIMALS, PLANTS, AND MICROORGANISMS
Theil, E. C. (1987) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.56.070187.001445 · Cited by 1,337
A ferric-chelate reductase for iron uptake from soils
Robinson, N. J., Procter, C. M., Connolly, E. L., & Guerinot, M. L. (1999) · Nature · doi:10.1038/17800 · Cited by 1,271
A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli
Massé, E., & Gottesman, S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.032066599 · Cited by 1,154
An 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
Iron and Oxidative Stress in Bacteria
Touati, D. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1518 · Cited by 915
Superoxide accelerates DNA damage by elevating free-iron levels
Keyer, K., & Imlay, J. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.24.13635 · Cited by 841
Research works printed but not linked: 3
- Silver, S. (1996) Transport of inorganic cations. In: Escherichia coli and Salmonella. Cellular and Molecular Biology, 2nd edn. (Neidhardt, F.C., Ed.), pp. 1091–1102. ASM Press, Washington, DC.
- Earhart, C.F. (1996) Uptake and metabolism of iron and molybdenum. In: Escherichia coli and Salmonella. Cellular and Molecular Biology, 2nd edn. (Neidhardt, F.C., Ed.), pp. 1075–1090. ASM Press, Washington, DC.
- Hantke, K. and Braun, V. (2000) The art of keeping low and high iron concentrations in balance. In: Bacterial Stress Responses (Storz, G. and Hengge-Aronis, R., Eds.), pp 275–288. ASM Press, Washington, DC.
Cited by
Sorted by citations
Items 701–800 of 1,010
Contribution of the FeoB transporter to Streptococcus suis virulence.
Aranda, J., Cortés, P., Garrido, M. E., Fittipaldi, N., Llagostera, M., Gottschalk, M. G., & Barbé, J. (2009) · PubMed · Cited by 48
Kidarsa, T. A., Shaffer, B. T., Goebel, N. C., Roberts, D. P., Buyer, J. S., Johnson, A., Kobayashi, D. Y., Zabriskie, T. M., Paulsen, I. T., & Loper, J. E. (2012) · Environmental Microbiology · doi:10.1111/1462-2920.12066 · Cited by 48
Baumgart, M., & Frunzke, J. (2015) · FEMS Microbiology Letters · doi:10.1093/femsle/fnu001 · Cited by 47
Uptake mechanisms for inorganic iron and ferric citrate in Trichodesmium erythraeum IMS101
Roe, K., & Barbeau, K. A. (2014) · Metallomics · doi:10.1039/c4mt00026a · Cited by 48
Bernick, D. L., Dennis, P. P., Lui, L. M., & Lowe, T. M. (2012) · Frontiers in Microbiology · doi:10.3389/fmicb.2012.00231 · Cited by 48
Role of oxygen and the OxyR protein in the response to iron limitation in Rhodobacter sphaeroides
Remes, B., Berghoff, B. A., Förstner, K. U., & Klug, G. (2014) · BMC Genomics · doi:10.1186/1471-2164-15-794 · Cited by 48
Kvitko, B. H., Goodyear, A., Propst, K. L., DOW, S. W., & Schweizer, H. P. (2012) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0001715 · Cited by 48
González, A., Angarica, V. E., Sancho, J., & Fillat, M. F. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku123 · Cited by 48
Whole Genome Sequencing and Metabolomic Study of Cave Streptomyces Isolates ICC1 and ICC4
Gosse, J. T., Ghosh, S. B., Sproule, A., Overy, D. P., Cheeptham, N., & Boddy, C. N. C. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.01020 · Cited by 48
Siderophores for medical applications: Imaging, sensors, and therapeutics
Fan, D., & Fang, Q. (2021) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2021.120306 · Cited by 48
Iron nutrition and physiological responses to iron stress in Nitrosomonas europaea
Wei, X., Vajrala, N., Hauser, L., Sayavedra‐Soto, L. A., & Arp, D. J. (2006) · Archives of Microbiology · doi:10.1007/s00203-006-0126-4 · Cited by 48
Global Gene Expression Analysis of the Heat Shock Response in the Phytopathogen Xylella fastidiosa
Koide, T., Vêncio, R. Z. N., & Gomes, S. L. (2006) · Journal of Bacteriology · doi:10.1128/jb.00182-06 · Cited by 47
Editorial: Role of Iron in Bacterial Pathogenesis
Zughaier, S. M., & Cornélis, P. (2018) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2018.00344 · Cited by 48
Debeljak, P., Toulza, È., Beier, S., Blain, S., & Obernosterer, I. (2019) · Environmental Microbiology · doi:10.1111/1462-2920.14621 · Cited by 47
Robbel, L., Knappe, T. A., Linne, U., Xie, X., & Marahiel, M. A. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07512.x · Cited by 47
Sun, X., Xiao, C., Ge, R., Yin, X., Li, H., Li, N., Yang, X.-Y., Zhu, Y., He, X., & He, Q. (2011) · PROTEOMICS · doi:10.1002/pmic.201000396 · Cited by 47
Whole‐genome microarray analyses of Synechococcus – Vibrio interactions
Tai, V., Paulsen, I. T., Phillippy, K., Johnson, D. A., & Palenik, B. P. (2009) · Environmental Microbiology · doi:10.1111/j.1462-2920.2009.01997.x · Cited by 47
Ferric Uptake Regulator and Its Role in the Pathogenesis of Nontypeable Haemophilus influenzae
Harrison, A., Santana, E. A., Szelestey, B. R., Newsom, D. E., White, P., & Mason, K. M. (2013) · Infection and Immunity · doi:10.1128/iai.01227-12 · Cited by 47
Oyserman, B. O., Moya, F., Lawson, C. E., Garcia, A. L., Vogt, M., Heffernen, M., Noguera, D. R., & McMahon, K. D. (2016) · The ISME Journal · doi:10.1038/ismej.2016.67 · Cited by 47
Jacek, P., Ryngajłło, M., & Bielecki, S. (2019) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-019-09846-4 · Cited by 47
Proteomic Changes inEscherichia coliWhen Grown in Fresh Milk versus Laboratory Media
Lippolis, J. D., Bayles, D. O., & Reinhardt, T. A. (2008) · Journal of Proteome Research · doi:10.1021/pr800458v · Cited by 47
Todd, J. D., Sawers, R. G., & Johnston, A. W. B. (2005) · Molecular Genetics and Genomics · doi:10.1007/s00438-005-1127-8 · Cited by 47
Lin, X., Wu, L., Li, H., Wang, S., & Peng, X. (2008) · Journal of Proteome Research · doi:10.1021/pr7005928 · Cited by 47
Transcriptional regulation of the Bacteroides fragilis ferritin gene (ftnA) by redox stress
Rocha, E. R., & Smith, C. J. (2004) · Microbiology · doi:10.1099/mic.0.26948-0 · Cited by 47
Magnetic Resonance Imaging of Tumors Colonized with Bacterial Ferritin-Expressing Escherichia coli
Hill, P. J., Stritzker, J., Scadeng, M., Geissinger, U., Haddad, D., Basse-Lüsebrink, T. C., Gbureck, U., Jakob, P. M., & Szalay, A. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025409 · Cited by 47
Ferrophilic Characteristics of Vibrio vulnificus and Potential Usefulness of Iron Chelation Therapy
Kim, C., Park, R., Choi, M., Sun, H., & Shin, S. (2007) · The Journal of Infectious Diseases · doi:10.1086/509822 · Cited by 46
The vacuolar iron transporter mediates iron detoxification in Toxoplasma gondii
Aghabi, D., Sloan, M. A., Gill, G., Hartmann, E., Antipova, O. A., Dou, Z., Guerra, A. J., Carruthers, V. B., & Harding, C. R. (2023) · Nature Communications · doi:10.1038/s41467-023-39436-y · Cited by 47
Högbom, M. (2011) · Metallomics · doi:10.1039/c0mt00095g · Cited by 47
Ramakrishnan, G., Sen, B., & Johnson, R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.371856 · Cited by 46
Dang, T. C., Fujii, M., Rose, A. L., Bligh, M. W., & Waite, T. D. (2011) · Applied and Environmental Microbiology · doi:10.1128/aem.06908-11 · Cited by 46
Erythrocyte and Leukocyte: Two Partners in Bacteria Killing
Minasyan, H. A. (2014) · International Reviews of Immunology · doi:10.3109/08830185.2014.956359 · Cited by 46
Wang, S., Wu, Y., & Outten, F. W. (2010) · Journal of Bacteriology · doi:10.1128/jb.01062-10 · Cited by 45
Tam, J. C. H., & Jacques, D. A. (2014) · Journal of Leukocyte Biology · doi:10.1189/jlb.4ri0214-090r · Cited by 47
Lee, Y. S., & Park, W. (2019) · AMB Express · doi:10.1186/s13568-019-0773-x · Cited by 46
Liu, Z., Ma, X., He, N., Zhang, J., Wu, J., & Liu, C. (2020) · Applied Soil Ecology · doi:10.1016/j.apsoil.2020.103517 · Cited by 45
Vasileva, D. P., Janssen, H., Hönicke, D., Ehrenreich, A., & Bahl, H. (2012) · Microbiology · doi:10.1099/mic.0.056978-0 · Cited by 45
Lenčo, J., Hubálek, M., Larsson, P., Fučíková, A., Brychta, M., Macela, A., & Stulík, J. (2007) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2006.00595.x · Cited by 49
Distinct gene clusters drive formation of ferrosome organelles in bacteria
Grant, C. R., Amor, M., Trujillo, H. A., Krishnapura, S., Iavarone, A. T., & Komeili, A. (2022) · Nature · doi:10.1038/s41586-022-04741-x · Cited by 45
Nickel-responsive transcriptional regulators
Musiani, F., Zambelli, B., Bazzani, M., Mazzei, L., & Ciurli, S. (2015) · Metallomics · doi:10.1039/c5mt00072f · Cited by 44
Butcher, J., & Stintzi, A. P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0079475 · Cited by 45
Liu, Z., Guo, J., Li, T., & Xu, Y. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22002 · Cited by 45
López-Gomollón, S., Hernández, J. A., Wölk, C. P., Peleato, M. L., & Fillat, M. F. (2006) · Microbiology · doi:10.1099/mic.0.2006/000091-0 · Cited by 45
An iron detection system determines bacterial swarming initiation and biofilm formation
Lin, C.-S., Tsai, Y.-H., Chang, C., Tseng, S., Wu, T.-R., Lu, C., Wu, T., Lu, J., Horng, J., Martel, J., et al. (2016) · Scientific Reports · doi:10.1038/srep36747 · Cited by 46
Yamamoto, Y., Fukui, K., Koujin, N., Ohya, H., Kimura, K., & Kamio, Y. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.18.5997-6002.2004 · Cited by 45
Hanke, T., Richhardt, J., Polen, T., Sahm, H., Bringer, S., & Bott, M. H. (2011) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2011.12.020 · Cited by 45
A role for tumour necrosis factor α in human small bowel iron transport
Sharma, N., Laftah, A. H., Brookes, M., Cooper, B. T., Iqbal, T. H., & Tselepis, C. (2005) · Biochemical Journal · doi:10.1042/bj20050256 · Cited by 44
Transcriptional profiling of Mycoplasma hyopneumoniae during iron depletion using microarrays
Madsen, M. L., Nettleton, D. S., Thacker, E. L., & Minion, F. C. (2006) · Microbiology · doi:10.1099/mic.0.28674-0 · Cited by 45
Pandey, S. S., Patnana, P. K., Rai, R., & Chatterjee, S. (2016) · Molecular Plant Pathology · doi:10.1111/mpp.12451 · Cited by 45
Mioni, C. E., Poorvin, L., & Wilhelm, S. W. (2005) · Aquatic Microbial Ecology · doi:10.3354/ame041233 · Cited by 47
Utilization of Lactoferrin-Bound and Transferrin-Bound Iron by Campylobacter jejuni
Miller, C. E., Rock, J. D., Ridley, K. A., Williams, P. H., & Ketley, J. M. (2008) · Journal of Bacteriology · doi:10.1128/jb.01761-07 · Cited by 43
Wang, Y., Zhang, X., Zhong, X.-L., Huang, Y.-J., Lin, J., & Chen, W. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c02044 · Cited by 42
Huang, M., Wang, Z., Yao, L., Zhang, L., Gou, X., Mo, H., Li, H., Hu, L., & Zhou, X. (2023) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2023.106794 · Cited by 44
Iron Oxide Nanoparticles as Promising Antibacterial Agents of New Generation
Zhang, T.-G., & Miao, C. (2024) · Nanomaterials · doi:10.3390/nano14151311 · Cited by 49
Jeanjean, R., Talla, E., Latifi, A., Havaux, M., Janicki, A., & Zhang, C. (2008) · Environmental Microbiology · doi:10.1111/j.1462-2920.2008.01680.x · Cited by 44
Jittawuttipoka, T., Sallabhan, R., Vattanaviboon, P., Fuangthong, M., & Mongkolsuk, S. (2010) · Archives of Microbiology · doi:10.1007/s00203-010-0558-8 · Cited by 44
Systemic and cellular consequences of macrophage control of iron metabolism
Recalcati, S., Locati, M., & Cairo, G. (2012) · Seminars in Immunology · doi:10.1016/j.smim.2013.01.001 · Cited by 44
Kim, I. H., Wen, Y., Son, J. S., Lee, K., & Kim, K. (2013) · Infection and Immunity · doi:10.1128/iai.00375-13 · Cited by 44
Crozier, L., Hedley, P. E., Morris, J., Wagstaff, C., Andrews, S. C., Toth, I. K., Jackson, R. W., & Holden, N. J. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.01088 · Cited by 44
Self-citationMechanisms of iron- and O2-sensing by the [4Fe-4S] cluster of the global iron regulator RirA
Martinez, M. T. P., Crack, J. C., Stewart, M. Y., Bradley, J. M., Svistunenko, D. A., Johnston, A. W. B., Cheesman, M. R., Todd, J. D., & Brun, N. E. L. (2019) · eLife · doi:10.7554/elife.47804 · Cited by 45
Suryadi, Y., Susilowati, D. N., & Fauziah, F. (2019) · Microorganisms for sustainability · doi:10.1007/978-981-13-6986-5_4 · Cited by 46
Bacteria-induced crystallization of kaolinite
Fiore, S., Dumontet, S., Huertas, F. J., & Pasquale, V. (2011) · Applied Clay Science · doi:10.1016/j.clay.2011.05.005 · Cited by 44
Small, S. K., Puri, S., Sangwan, I., & O’Brian, M. R. (2008) · Journal of Bacteriology · doi:10.1128/jb.01571-08 · Cited by 44
Tanabe, T., Naka, A., Aso, H., Nakao, H., Narimatsu, S., Inoue, Y., Ono, T., & Yamamoto, S. (2005) · Microbiology and Immunology · doi:10.1111/j.1348-0421.2005.tb03671.x · Cited by 44
2.6 Å resolution crystal structure of the bacterioferritin from Azotobacter vinelandii
Liu, H., Zhou, H., Xing, W., Zhao, J., Li, S., Huang, J., & Bi, R. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.07.054 · Cited by 44
Antimicrobial Peptides as Potential Anti-Tubercular Leads: A Concise Review
Oliveira, G. S., Costa, R. P., Gomes, P. A. C., Gomes, M. S., Silva, T., & Teixeira, C. A. S. (2021) · Pharmaceuticals · doi:10.3390/ph14040323 · Cited by 46
Easy detection of siderophore production in diluted growth media using an improved CAS reagent
Murakami, C., Tanaka, A. R., Sato, Y. Z., Kimura, Y., & Morimoto, K. (2021) · Journal of Microbiological Methods · doi:10.1016/j.mimet.2021.106310 · Cited by 43
Jeske, A., Arce‐Rodríguez, A., Thöming, J. G., Tomasch, J., & Häußler, S. (2022) · npj Biofilms and Microbiomes · doi:10.1038/s41522-022-00268-1 · Cited by 43
Pulcherrimin protects Bacillus subtilis against oxidative stress during biofilm development
Angelini, L. L., Santos, R., Fox, G., Paruthiyil, S., Gozzi, K., Shemesh, M., & Chai, Y. (2023) · npj Biofilms and Microbiomes · doi:10.1038/s41522-023-00418-z · Cited by 42
A heritable iron memory enables decision-making in Escherichia coli
Bhattacharyya, S., Bhattarai, N., Pfannenstiel, D. M., Wilkins, B., Singh, A., & Harshey, R. M. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2309082120 · Cited by 42
The pearl jubilee of microcin J25: thirty years of research on an exceptional lasso peptide
Baquero, F., Beis, K., Craik, D. J., Li, Y., Link, A. J., Rebuffat, S., Salomón, R. A., Severinov, K., Zirah, S., & Hegemann, J. D. (2024) · Natural Product Reports · doi:10.1039/d3np00046j · Cited by 45
The role of iron uptake in pathogenicity and symbiosis in Photorhabdus luminescens TT01
Watson, R. J., Millichap, P. J., Joyce, S. A., Reynolds, S. E., & Clarke, D. J. (2010) · BMC Microbiology · doi:10.1186/1471-2180-10-177 · Cited by 43
McLaughlin, H. P., Xiao, Q., Rea, R. B., Pi, H., Casey, P. G., Darby, T. M., Charbit, A., Sleator, R. D., Joyce, S. A., Cowart, R. E., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0030928 · Cited by 42
Collins, A. J., Fullmer, M. S., Gogarten, J. P., & Nyholm, S. V. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00123 · Cited by 44
Streptococcus pneumoniae Invades Erythrocytes and Utilizes Them to Evade Human Innate Immunity
Yamaguchi, M., Terao, Y., Mori-Yamaguchi, Y., Domon, H., Sakaue, Y., Yagi, T., Nishino, K., Yamaguchi, A., Nizet, V., & Kawabata, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077282 · Cited by 42
Wang, Y., Yao, H., Cheng, Y., Lovell, S., Battaile, K. P., Middaugh, C. R., & Rivera, M. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00937 · Cited by 42
Martinez, M. T. P., Martínez, A. B., Crack, J. C., Holmes, J. D., Svistunenko, D. A., Johnston, A. W. B., Cheesman, M. R., Todd, J. D., & Brun, N. E. L. (2017) · Chemical Science · doi:10.1039/c7sc02801f · Cited by 43
Leaden, L., Silva, L. G., Ribeiro, R. A., dos Santos, N. M., Lorenzetti, A. P. R., Alegria, T. G. P., Schulz, M. L., de Medeiros, M. H. G., Koide, T., & Marques, M. V. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02014 · Cited by 39
Cheng, Y., Yang, R., Lyu, M., Wang, S., Liu, X., Wen, Y., Song, Y., Li, J., & Chen, Z. (2018) · Applied and Environmental Microbiology · doi:10.1128/aem.01503-18 · Cited by 44
Shyntum, D. Y., Nkomo, N. P., Gricia, A. R., Shigange, N. L., Rabelo, D. B., & Moleleki, L. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.02379 · Cited by 44
Rangseekaew, P., Barros‐Rodríguez, A., ., W. P.-A., & Manzanera, M. (2022) · Biology · doi:10.3390/biology11020191 · Cited by 43
Kim, J. N., & Kwon, Y. M. (2013) · Microbiological Research · doi:10.1016/j.micres.2013.06.002 · Cited by 42
Kurabayashi, K., Agata, T., Asano, H., Tomita, H., & Hirakawa, H. (2016) · Infection and Immunity · doi:10.1128/iai.00369-16 · Cited by 42
Competition for iron shapes metabolic antagonism betweenBacillus subtilisandPseudomonas marginalis
Lyng, M., Jørgensen, J. P. B., Schostag, M. D., Jarmusch, S. A., Aguilar, D., Lozano-Andrade, C. N., & Kovács, Á. T. (2024) · The ISME Journal · doi:10.1093/ismejo/wrad001 · Cited by 41
Transcriptomic Responses of Bacterial Cells to Sublethal Metal Ion Stress
Hobman, J. L., Yamamoto, K., & Oshima, T. (2007) · Springer eBooks · doi:10.1007/7171_2006_074 · Cited by 42
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Orellana, R., Hixson, K. K., Murphy, S. J.-L., Mester, T., Sharma, M. L., Lipton, M. S. W., & Lovley, D. R. (2014) · Microbiology · doi:10.1099/mic.0.081398-0 · Cited by 44
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Metadata
- Authors
- Andrews, S. C., Robinson, A. K., & Rodríguez-Quiñones, F.
- Affiliations
- University of Reading (GB)
- Corresponding author
- Andrews, Simon C.
- ORCID
- Andrews, Simon C.
- Venue
- FEMS Microbiology Reviews
- Publisher
- Oxford University Press (OUP)
- Published
- 2003-06
- Volume
- 27
- Issue
- 2-3
- Pages
- 215-237
- ISSN
- 0168-6445 (ISSN-L)
- 1574-6976
- OpenAlex
- W2014723793
- Cited by
- 2,702
- References
- 185
- Citations by year
- 2026: 116 · 2025: 142 · 2024: 139 · 2023: 147 · 2022: 153 · 2021: 179 · 2020: 151 · 2019: 138 · 2018: 122 · 2017: 118 · 2016: 126 · 2015: 117 · 2014: 141 · 2013: 96 · 2012: 111
- FWCI
- 7.45
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEMS Microbiology Reviews (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Immunology and Microbiology › Microbiology › Escherichia coli research studies
- Keywords
- siderophores, iron acquisition, transferrin, lactoferrin, heme, ferritin, bacterioferritin, Dps protein, iron limitation, iron toxicity, iron storage
- MeSH terms
- Bacteria, Bacterial Proteins, DNA-Binding Proteins, Escherichia coli, Heme, Homeostasis, Iron, Models, Genetic, Gene Expression Regulation, Bacterial, Siderophores, Protein Structure, Tertiary
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