The DOI matches its Crossref record; 185 of the 185 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
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
The cited source says what the claim attributes to it.
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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
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 401–500 of 1,010
Bhatt, G., & Denny, T. P. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.23.7896-7904.2004 · Cited by 86
Virulence factors ofEnterococcusstrains isolated from patients with inflammatory bowel disease
Golińska, E. (2013) · World Journal of Gastroenterology · doi:10.3748/wjg.v19.i23.3562 · Cited by 83
Oberholster, P. J., Myburgh, J. G., ASHTON, P. J., & Botha, A. (2009) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2009.08.011 · Cited by 83
Bacterial nucleoid dynamics: oxidative stress response in Staphylococcus aureus
Morikawa, K., Ohniwa, R. L., Kim, J., Maruyama, A., Ohta, T., & Takeyasu, K. (2006) · Genes to Cells · doi:10.1111/j.1365-2443.2006.00949.x · Cited by 82
Sebaihia, M., Preston, A., Maskell, D. J., Kuzmiak, H., Connell, T. D., King, N. D., Orndorff, P. E., Miyamoto, D. M., Thomson, N. R., Harris, D. J., et al. (2006) · Journal of Bacteriology · doi:10.1128/jb.01927-05 · Cited by 81
Physiological and Proteomic Analysis of Escherichia coli Iron-Limited Chemostat Growth
Folsom, J. P., Parker, A. E., & Carlson, R. P. (2014) · Journal of Bacteriology · doi:10.1128/jb.01606-14 · Cited by 80
Ferripyochelin uptake genes are involved in pyochelin-mediated signalling in Pseudomonas aeruginosa
Michel, L., Bachelard, A., & Reimmann, C. (2007) · Microbiology · doi:10.1099/mic.0.2006/002915-0 · Cited by 83
Zinc Homeostasis at the Bacteria/Host Interface—From Coordination Chemistry to Nutritional Immunity
Wątły, J., Potocki, S., & Rowińska‐Żyrek, M. (2016) · Chemistry - A European Journal · doi:10.1002/chem.201602376 · Cited by 84
Oxidative Stress Resistance in Porphyromonas Gingivalis
Henry, L. G., McKenzie, R. M. E., Robles, A. G., & Fletcher, H. M. (2012) · Future Microbiology · doi:10.2217/fmb.12.17 · Cited by 82
Efficient degradation and expression prioritization with small RNAs
Mitarai, N., Andersson, A. M. C., Krishna, S., Semsey, S., & Sneppen, K. (2007) · Physical Biology · doi:10.1088/1478-3975/4/3/003 · Cited by 81
Dps biomineralizing proteins: multifunctional architects of nature
Zeth, K. (2012) · Biochemical Journal · doi:10.1042/bj20120514 · Cited by 80
Fang, S., Zhuo, Z., Yu, X., Wang, H., & Feng, J. (2018) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2018.01.002 · Cited by 83
Gumpert, H., Kubicek-Sutherland, J. Z., Porse, A., Karami, N., Munck, C., Linkevičius, M., Adlerberth, I., Wold, A. E., Andersson, D. I., & Sommer, M. O. A. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.01852 · Cited by 81
Iron Acquisition Mechanisms and Their Role in the Virulence of Acinetobacter baumannii
Cook-Libin, S., Sykes, E. M. E., Kornelsen, V., & Kumar, A. (2022) · Infection and Immunity · doi:10.1128/iai.00223-22 · Cited by 86
Pseudomonas sp. M174 inhibits the fish pathogen Flavobacterium psychrophilum
Korkea‐aho, T., Heikkinen, J., Thompson, K. D., von Wright, A., & Austin, B. P. (2011) · Journal of Applied Microbiology · doi:10.1111/j.1365-2672.2011.05044.x · Cited by 80
Growth of Acinetobacter baumannii in Pellicle Enhanced the Expression of Potential Virulence Factors
Martí, S., Chabane, Y. N., Alexandre, S., Coquet, L., Vilà, J., Jouenne, T., & Dé, E. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026030 · Cited by 80
Lewis, J. P., Plata, K. B., Yu, F., Rosato, A. E., & Anaya-Bergman, C. (2006) · Microbiology · doi:10.1099/mic.0.29011-0 · Cited by 80
Mellata, M., Ameiss, K. A., Mo, H., & Curtiss, R. (2010) · Infection and Immunity · doi:10.1128/iai.00981-09 · Cited by 81
Chen, W., Kuo, T., Hsieh, F.-C., Chen, P.-Y., Wang, C.-S., Shih, Y., Lai, Y.-M., Liu, J., Yang, Y., & Shih, M. (2016) · Scientific Reports · doi:10.1038/srep32950 · Cited by 80
Principles of Enrichment, Isolation, Cultivation, and Preservation of Prokaryotes
Overmann, J. (2013) · Springer eBooks · doi:10.1007/978-3-642-30194-0_7 · Cited by 81
Global Gene Expression Analysis of Iron-Inducible Genes in Magnetospirillum magneticum AMB-1
Suzuki, T., Okamura, Y., Calugay, R. J., Takeyama, H., & Matsunaga, T. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.6.2275-2279.2006 · Cited by 79
Toulza, È., Tagliabue, A., Blain, S., & Piganeau, G. (2012) · PLoS ONE · doi:10.1371/journal.pone.0030931 · Cited by 83
Bypasses in intracellular glucose metabolism in iron‐limited Pseudomonas putida
Sasnow, S. S., Wei, H., & Aristilde, L. (2015) · MicrobiologyOpen · doi:10.1002/mbo3.287 · Cited by 77
Silva-Valenzuela, C. A., Blondel, C. J., Quezada, C. P., Porwollik, S., Andrews‐Polymenis, H. L., Toro, C. S., Zaldı́var, M., Contreras, I., McClelland, M., & Santiviago, C. A. (2011) · Infection and Immunity · doi:10.1128/iai.05497-11 · Cited by 79
Dopson, M., Baker‐Austin, C., & Bond, P. L. (2005) · Microbiology · doi:10.1099/mic.0.28362-0 · Cited by 79
Surveying Gut Microbiome Research in Africans: Toward Improved Diversity and Representation
Brewster, R., Tamburini, F. B., Asiimwe, E., Oduaran, O. H., Hazelhurst, S., & Bhatt, A. S. (2019) · Trends in Microbiology · doi:10.1016/j.tim.2019.05.006 · Cited by 85
Siderophore-Mediated Interactions Determine the Disease Suppressiveness of Microbial Consortia
Gu, S., Yang, T., Shao, Z., Wang, T., Cao, K., Jousset, A., Friman, V., Mallon, C. A., Mei, X., Wei, Z., et al. (2020) · mSystems · doi:10.1128/msystems.00811-19 · Cited by 87
Bearson, B. L., Bearson, S. M. D., Lee, I. S., & Brunelle, B. W. (2010) · Microbial Pathogenesis · doi:10.1016/j.micpath.2010.03.005 · Cited by 81
Fan, D., Wang, W., & Zhong, J. (2011) · Biochemical Engineering Journal · doi:10.1016/j.bej.2011.09.014 · Cited by 78
Proteobactin and a yersiniabactin‐related siderophore mediate iron acquisition in Proteus mirabilis
Himpsl, S. D., Pearson, M. M., Arewång, C.-J., Nusca, T. D., Sherman, D. H., & Mobley, H. L. T. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07317.x · Cited by 78
TonB-dependent transporters and their occurrence in cyanobacteria
Mirus, O., Strauß, S., Nicolaisen, K., von Haeseler, A., & Schleiff, E. (2009) · BMC Biology · doi:10.1186/1741-7007-7-68 · Cited by 83
Mellata, M., Touchman, J. W., & Curtiss, R. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004232 · Cited by 77
Metal site occupancy and allosteric switching in bacterial metal sensor proteins
Guerra, A. J., & Giedroc, D. P. (2012) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.11.021 · Cited by 77
Malviya, D., Sahu, P. K., Singh, U. B., Paul, S., Gupta, A., Gupta, A. R., Singh, S., Kumar, M., PAUL, D. Z., Rai, J. P., et al. (2020) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph17041434 · Cited by 76
Bearson, B. L., Bearson, S. M. D., Uthe, J. J., Dowd, S. E., Houghton, J. O., Lee, I., Toscano, M. J., & Lay, D. C., Jr. (2008) · Microbes and Infection · doi:10.1016/j.micinf.2008.04.011 · Cited by 75
Schröder, J., Maus, I., Trost, E., & Tauch, A. (2011) · BMC Genomics · doi:10.1186/1471-2164-12-545 · Cited by 76
Derepression of the Bacillus subtilis PerR Peroxide Stress Response Leads to Iron Deficiency
Faulkner, M. J., Ma, Z., Fuangthong, M., & Helmann, J. D. (2012) · Journal of Bacteriology · doi:10.1128/jb.06566-11 · Cited by 76
Estevez‐Canales, M., Kuzume, A., Borjas, Z., Füeg, M. P., Lovley, D. R., Wandlowski, T., & Esteve‐Núñez, A. (2014) · Environmental Microbiology Reports · doi:10.1111/1758-2229.12230 · Cited by 79
Bioavailability and Toxicity of Metal Nutrients during Anaerobic Digestion
de Aquino, S. F., & Stuckey, D. C. (2006) · Journal of Environmental Engineering · doi:10.1061/(asce)0733-9372(2007)133:1(28 · Cited by 76
Analysis of a Ferric Uptake Regulator (Fur) Mutant of Desulfovibrio vulgaris Hildenborough
Bender, K. S., Yen, H.-C., Hemme, C. L., Yang, Z. K., He, Z., He, Q., Zhou, J. Z., Huang, K. H., Alm, E. J., Hazen, T. C., et al. (2007) · Applied and Environmental Microbiology · doi:10.1128/aem.00276-07 · Cited by 76
How Listeria monocytogenes organizes its surface for virulence
Carvalho, F., Sousa, S., & Cabanes, D. (2014) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2014.00048 · Cited by 79
Porcheron, G., Habib, R., Houle, S., Caza, M., Lepine, F. L., Daigle, F., Massé, É., & Dozois, C. M. (2014) · Infection and Immunity · doi:10.1128/iai.02287-14 · Cited by 80
Pathogenic bacteria prefer heme.
Rouault, T. A. (2004) · Science · doi:10.1126/science.1102975 · Cited by 76
Álvarez, B., Álvarez, J., Menéndez, A., & Guijarro, J. A. (2008) · Microbiology · doi:10.1099/mic.0.2007/010900-0 · Cited by 75
Ruales-Lonfat, C., Benítez, N., Sienkiewicz, A., & Pulgarin, C. O. (2014) · Applied Catalysis B: Environmental · doi:10.1016/j.apcatb.2014.05.001 · Cited by 75
Ferritin Nanocages for Protein Delivery to Tumor Cells
Palombarini, F., Fabio, E. D., Boffi, A., Macone, A., & Bonamore, A. (2020) · Molecules · doi:10.3390/molecules25040825 · Cited by 74
The Gac regulon of P seudomonas fluorescens SBW 25
Cheng, X., de Bruijn, I., van der Voort, M., Loper, J. E., & Raaijmakers, J. M. (2013) · Environmental Microbiology Reports · doi:10.1111/1758-2229.12061 · Cited by 74
Joshi, C. P., Panda, D., Martell, D. J., Andoy, N. M., Chen, T., Gaballa, A., Helmann, J. D., & Chen, P. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208508109 · Cited by 73
Kortman, G. A. M., Dutilh, B. E., Maathuis, A. J. H., Engelke, U. F., Boekhorst, J., Keegan, K. P., Nielsen, F. G. G., Betley, J., Weir, J. C., Kingsbury, Z., et al. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.01481 · Cited by 73
Dryla, A., Hoffmann, B., Gelbmann, D., Giefing, C., Hanner, M., Meinke, A., Anderson, A. S., Koppensteiner, W., Konrat, R., von Gabain, A., et al. (2007) · Journal of Bacteriology · doi:10.1128/jb.01366-06 · Cited by 73
Roles of the EnvZ/OmpR Two-Component System and Porins in Iron Acquisition in Escherichia coli
Gerken, H. G., Vuong, P., Soparkar, K., & Misra, R. (2020) · mBio · doi:10.1128/mbio.01192-20 · Cited by 73
A critical review of exogenous additives for improving the anammox process
Zhang, Q., Lin, J., Kong, Z., & Zhang, Y. (2022) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2022.155074 · Cited by 73
Penwell, W. F., DeGrace, N., Tentarelli, S., Gauthier, L., Gilbert, C. M., Arivett, B. A., Miller, A. A., Durand-Réville, T. F., Joubran, C., & Actis, L. A. (2015) · ChemBioChem · doi:10.1002/cbic.201500147 · Cited by 73
Piggot, T. J., Holdbrook, D. A., & Khalid, S. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2012.08.021 · Cited by 71
Apoferritin Applications in Nanomedicine
Heger, Z., Skalíčková, S., Zítka, O., Adam, V., & Kizek, R. (2014) · Nanomedicine · doi:10.2217/nnm.14.119 · Cited by 73
Pfleger, B. F., Kim, Y., Nusca, T. D., Maltseva, N., Lee, J. Y., Rath, C. M. B., Scaglione, J. B., Janes, B. K., Anderson, E. C., Bergman, N. H., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808118105 · Cited by 76
Rudolph, G., Semini, G., Hauser, F., Lindemann, A., Friberg, M. T., Hennecke, H., & Fischer, H. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.2.733-744.2006 · Cited by 35
Lages, M. A., Balado, M., & Lemos, M. L. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.02335 · Cited by 72
Global analysis of iron assimilation and fur regulation in Yersinia pestis
Zhou, D., Qin, L., Han, Y., Qiu, J., Chen, Z., Li, B., Song, Y., Wang, J., Guo, Z., Zhai, J., et al. (2006) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2006.00208.x · Cited by 72
Regulation of Iron Homeostasis in Arabidopsis thaliana by the Clock Regulator Time for Coffee
Duc, C., Cellier, F., Lobréaux, S., Briat, J., & Gaymard, F. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.059873 · Cited by 77
Cotruvo, J. A., & Stubbe, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807348105 · Cited by 72
Sheng, M. M., Jia, H. K., Zhang, G. Y., Zeng, L. N., Zhang, T., Long, Y. H., Lan, J. Q., Hu, Z. Q., Zeng, Z., Wang, B., et al. (2020) · Journal of Microbiology and Biotechnology · doi:10.4014/jmb.1910.10066 · Cited by 73
Virulence factors of foodborne pathogen Campylobacter jejuni
Lopes, G. V., Ramires, T., Kleinübing, N. R., Scheik, L. K., Fiorentini, Â. M., & da Silva, W. P. (2021) · Microbial Pathogenesis · doi:10.1016/j.micpath.2021.105265 · Cited by 71
Iron Transport and Metabolism in Escherichia, Shigella, and Salmonella
Mey, A. R., Gómez-Garzón, C., & Payne, S. M. (2021) · EcoSal Plus · doi:10.1128/ecosalplus.esp-0034-2020 · Cited by 70
Microbial liberation of N-methylserotonin from orange fiber in gnotobiotic mice and humans
Han, N. D., Cheng, J., Delannoy-Bruno, O., Webber, D. M., Terrapon, N., Henrissat, B., Rodionov, D. A., Arzamasov, A. A., Osterman, A. L., Hayashi, D. K., et al. (2022) · Cell · doi:10.1016/j.cell.2022.06.004 · Cited by 71
The Impacts of Iron Overload and Ferroptosis on Intestinal Mucosal Homeostasis and Inflammation
Huo, C., Li, G., Hu, Y., & Sun, H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232214195 · Cited by 76
Lucana, D. O. D. O., Wedderhoff, I., & Groves, M. R. (2011) · Journal of Signal Transduction · doi:10.1155/2012/605905 · Cited by 71
Structural Basis for the Transcriptional Regulation of Heme Homeostasis in Lactococcus lactis
Sawai, H., Yamanaka, M., Sugimoto, H., Shiro, Y., & Aono, S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.370916 · Cited by 71
Uebe, R., Voigt, B., Schweder, T., Albrecht, D., Katzmann, E., Lang, C., Böttger, L. H., Matzanke, B. F., & Schüler, D. (2010) · Journal of Bacteriology · doi:10.1128/jb.00319-10 · Cited by 69
Vazquez-Gutierrez, P., de Wouters, T., Werder, J., Chassard, C., & Lacroix, C. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.01480 · Cited by 76
Esmaeel, Q., Pupin, M., Jacques, P., & Leclère, V. (2017) · Environmental Science and Pollution Research · doi:10.1007/s11356-017-9166-3 · Cited by 71
Chen, K., Gao, S.-H., Jin, M., Sun, S., Lu, J., Yang, P., Bond, P. L., Yuan, Z., & Guo, J. (2019) · Environment International · doi:10.1016/j.envint.2019.01.058 · Cited by 70
Amor, M., Tharaud, M., Gélabert, A., & Komeili, A. (2019) · Environmental Microbiology · doi:10.1111/1462-2920.14708 · Cited by 70
Gut microbiota bridges the iron homeostasis and host health
Xiao, L., Tang, R., Wang, J., Wan, D., Yin, Y., & Xie, L. (2023) · Science China Life Sciences · doi:10.1007/s11427-022-2302-5 · Cited by 70
Rosconi, F., Davyt, D., Martínez, V., Martínez, M., Abin‐Carriquiry, J. A., Zane, H. K., Butler, A., de Souza, E. M., & Fabiano, E. (2012) · Environmental Microbiology · doi:10.1111/1462-2920.12075 · Cited by 70
Gauss, G. H., Bénas, P., Wiedenheft, B., Young, M., Douglas, T., & Lawrence, C. M. (2006) · Biochemistry · doi:10.1021/bi060782u · Cited by 70
Nicolaisen, K., Hahn, A. S., Valdebenito, M., Moslavac, S., Samborski, A., Maldener, I., Wilken, C., Valladares, A., Flores, E., Hantke, K., et al. (2010) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2010.07.008 · Cited by 71
Leptospira interrogans requires a functional heme oxygenase to scavenge iron from hemoglobin
Murray, G. L., Ellis, K. M., Lo, M., & Adler, B. (2008) · Microbes and Infection · doi:10.1016/j.micinf.2008.04.010 · Cited by 70
Insights into the Molecular Basis of L-Form Formation and Survival in Escherichia coli
Glover, W. A., Yang, Y., & Zhang, Y. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007316 · Cited by 72
Przybyszewska, J., & Żekanowska, E. (2014) · Gastroenterology Review · doi:10.5114/pg.2014.45102 · Cited by 70
Motley, S. T., Morrow, B. J., Liu, X., Dodge, I. L., Vitiello, A., Ward, C. K., & Shaw, K. J. (2004) · Cellular Microbiology · doi:10.1111/j.1462-5822.2004.00407.x · Cited by 70
Impact of Anaerobiosis on Expression of the Iron-Responsive Fur and RyhB Regulons
Beauchene, N. A., Myers, K. S., Chung, D., Park, D. M., Weisnicht, A. M., Keleş, S., & Kiley, P. J. (2015) · mBio · doi:10.1128/mbio.01947-15 · Cited by 69
Kreutzer, M., Kage, H., & Nett, M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja300620z · Cited by 70
Gu, C., Wang, J., Liu, S., Liu, G., Lü, H., & Jin, R. (2016) · Environmental Science & Technology · doi:10.1021/acs.est.6b02116 · Cited by 70
The regulation of pathogenicity and mutualism in Photorhabdus
Joyce, S. A., Watson, R. J., & Clarke, D. J. (2006) · Current Opinion in Microbiology · doi:10.1016/j.mib.2006.01.004 · Cited by 70
Quatrini, R., Lefimil, C., Veloso, F. A., Pedroso, I., Holmes, D. S., & Jedlicki, E. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm068 · Cited by 69
Lau, C. K. Y., Ishida, H., Liu, Z., & Vogel, H. J. (2012) · Journal of Bacteriology · doi:10.1128/jb.01121-12 · Cited by 68
Bates, C. S., Toukoki, C., Neely, M. N., & Eichenbaum, Z. (2005) · Infection and Immunity · doi:10.1128/iai.73.9.5743-5753.2005 · Cited by 69
González, A., Bes, M. T., Valladares, A., Peleato, M. L., & Fillat, M. F. (2012) · Environmental Microbiology · doi:10.1111/j.1462-2920.2012.02897.x · Cited by 69
Senkovich, O., Ceaser, S., McGee, D. J., & Testerman, T. L. (2010) · Infection and Immunity · doi:10.1128/iai.01258-09 · Cited by 70
Bosello, M., Robbel, L., Linne, U., Xie, X., & Marahiel, M. A. (2011) · Journal of the American Chemical Society · doi:10.1021/ja1109453 · Cited by 69
Porse, A., Gumpert, H., Kubicek-Sutherland, J. Z., Karami, N., Adlerberth, I., Wold, A. E., Andersson, D. I., & Sommer, M. O. A. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00126 · Cited by 67
Caza, M., Lepine, F. L., & Dozois, C. M. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07570.x · Cited by 69
Turan, E., & Şimşek, A. (2021) · Meat Science · doi:10.1016/j.meatsci.2021.108522 · Cited by 68
Xia, Y., Wei, X., Gao, P., Wang, C., de Jong, A., Chen, J. H.-K., Rodríguez, M. J., Rodríguez‐Nogales, A., Diez‐Echave, P., Gálvez, J., et al. (2024) · Nature Microbiology · doi:10.1038/s41564-024-01807-6 · Cited by 70
Effect of Light on Iron Uptake by the Freshwater Cyanobacterium Microcystis aeruginosa
Fujii, M., Dang, T. C., Rose, A. L., Omura, T., & Waite, T. D. (2011) · Environmental Science & Technology · doi:10.1021/es103311h · Cited by 68
Molybdenum Trafficking for Nitrogen Fixation
Hernández, J. A., George, S. J., & Rubio, L. M. (2009) · Biochemistry · doi:10.1021/bi901217p · Cited by 73
The IsdC Protein from Staphylococcus aureus Uses a Flexible Binding Pocket to Capture Heme
Villareal, V. A., Pilpa, R. M., Robson, S. A., Fadeev, E. A., & Clubb, R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801126200 · Cited by 69
Transcriptomic Response of Listeria monocytogenes to Iron Limitation and fur Mutation
Ledala, N., Sengupta, M., Muthaiyan, A., Wilkinson, B. J., & Jayaswal, R. K. (2009) · Applied and Environmental Microbiology · doi:10.1128/aem.01389-09 · Cited by 72
Bifidobacteria strains isolated from stools of iron deficient infants can efficiently sequester iron
Vazquez-Gutierrez, P., Lacroix, C., Jaeggi, T., Zeder, C., Zimmermann, M. B., & Chassard, C. (2015) · BMC Microbiology · doi:10.1186/s12866-014-0334-z · Cited by 68
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
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
