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 801–900 of 1,010
Martínez‐Bussenius, C., Navarro, C. A., Orellana, L. H., Paradela, A., & Jerez, C. A. (2016) · Journal of Proteomics · doi:10.1016/j.jprot.2016.03.039 · Cited by 41
Pant, R., Pandey, P., & Kotoky, R. (2016) · Ecological Engineering · doi:10.1016/j.ecoleng.2016.05.079 · Cited by 41
Bacterial cyclic β‐(1,2)‐glucans sequester iron to protect against iron‐induced toxicity
Javvadi, S. G., Pandey, S. S., Mishra, A., Pradhan, B. B., & Chatterjee, S. (2017) · EMBO Reports · doi:10.15252/embr.201744650 · Cited by 41
Lack of glyoxylate shunt dysregulates iron homeostasis in Pseudomonas aeruginosa
Ha, S., Shin, B., & Park, W. (2018) · Microbiology · doi:10.1099/mic.0.000623 · Cited by 45
Amor, M., Busigny, V., Louvat, P., Tharaud, M., Gélabert, A., Cartigny, P., Carlut, J., Isambert, A., Durand‐Dubief, M., Ona-Nguéma, G., et al. (2018) · Geochimica et Cosmochimica Acta · doi:10.1016/j.gca.2018.04.020 · Cited by 46
Nicolitch, O., Feucherolles, M., Churin, J.-L., Fauchery, L., Turpault, M., & Uroz, S. (2019) · Scientific Reports · doi:10.1038/s41598-019-50730-y · Cited by 41
A Salmochelin S4-Inspired Ciprofloxacin Trojan Horse Conjugate
Sanderson, T. J., Black, C. M., Southwell, J. W., Wilde, E. J., Pandey, A. K., Herman, R., Thomas, G. H., Boros, E., Duhme‐Klair, A., & Routledge, A. (2020) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.0c00568 · Cited by 41
Iron Reshapes the Gut Microbiome and Host Metabolism
Botta, A. M., Barra, N. G., Lam, N. H., Chow, S., Pantopoulos, K., Schertzer, J. D., & Sweeney, G. (2021) · Journal of Lipid and Atherosclerosis · doi:10.12997/jla.2021.10.2.160 · Cited by 44
Salgueiro, C. A., Morgado, L., Silva, M. A., Ferreira, M. R., Fernandes, T. M., & Portela, P. C. (2021) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2021.214284 · Cited by 41
Wang, Y., Zhang, G., Ya, H., Guo, M., Song, J., Zhang, T., Long, Y., Wang, B., & Liu, H. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.870413 · Cited by 43
Metal Content of Metallo-β-lactamase L1 Is Determined by the Bioavailability of Metal Ions
Hu, Z., Gunasekera, T. S., Spadafora, L. J., Bennett, B., & Crowder, M. W. (2008) · Biochemistry · doi:10.1021/bi8004768 · Cited by 41
Bott, M. H., & Brocker, M. (2012) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-012-4060-x · Cited by 42
Oxidative stress defense mechanisms to counter iron-promoted DNA damage inHelicobacter pylori
Wang, G., Conover, R. C., Olczak, A. A., Alamuri, P., Johnson, M. K., & Maier, R. J. (2005) · Free Radical Research · doi:10.1080/10715760500194018 · Cited by 41
Danese, I., Haine, V., Delrue, R.-M., Tibor, A., Lestrate, P., Nolan-Stevaux, O., Mertens, P., Paquet, J., Godfroid, J., Bolle, X. D., et al. (2004) · Infection and Immunity · doi:10.1128/iai.72.10.5783-5790.2004 · Cited by 41
Osman, D., & Cavet, J. S. (2011) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/b978-0-12-381043-4.00005-2 · Cited by 43
The ferric iron uptake regulator (Fur) from the extreme acidophile Acidithiobacillus ferrooxidans
Quatrini, R., Lefimil, C., Holmes, D. S., & Jedlicki, E. (2005) · Microbiology · doi:10.1099/mic.0.27581-0 · Cited by 40
Muselius, B., Sukumaran, A., Yeung, J., & Geddes‐McAlister, J. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.00546 · Cited by 45
Nickel stress-tolerance in plant-bacterial associations
Pishchik, V. N., Mirskaya, G. V., Chizhevskaya, E. P., Chebotar, V. K., & Chakrabarty, D. (2021) · PeerJ · doi:10.7717/peerj.12230 · Cited by 40
Gene Networks and Pathways Involved in Escherichia coli Response to Multiple Stressors
Abdelwahed, E. K., Hussein, N. A., Moustafa, A., Moneib, N. A., & Aziz, R. K. (2022) · Microorganisms · doi:10.3390/microorganisms10091793 · Cited by 40
Daoud, L., Al-Marzooq, F. I., Moubareck, C. A., Ghazawi, A., & Collyns, T. (2022) · PLoS ONE · doi:10.1371/journal.pone.0277946 · Cited by 39
Ahmad, R., Brandsdal, B. O., Michaud‐Soret, I., & Willassen, N. P. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22247 · Cited by 41
Understanding and engineering electrochemically active bacteria for sustainable biotechnology
Hirose, A., Kasai, T., Koga, R., Suzuki, Y., Kouzuma, A., & Watanabe, K. (2019) · Bioresources and Bioprocessing · doi:10.1186/s40643-019-0245-9 · Cited by 39
Microbial Competition in the Subpolar Southern Ocean: An Fe–C Co-limitation Experiment
Fourquez, M., Bressac, M., Deppeler, S., Ellwood, M. J., Obernosterer, I., Trull, T. W., & Boyd, P. W. (2020) · Frontiers in Marine Science · doi:10.3389/fmars.2019.00776 · Cited by 40
Sun, J., Wei, L., Yin, R., Jiang, F., & Shang, C. (2019) · Water Research · doi:10.1016/j.watres.2019.115453 · Cited by 40
Iron–Sulfur Cluster Biogenesis and Iron Homeostasis in Cyanobacteria
Gao, F. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.00165 · Cited by 43
Plaza, J. J. G. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.00101 · Cited by 42
Kontoghiorghes, G. J., Kolnagou, A., Demetriou, T., Neocleous, M., & Kontoghiorghe, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115546 · Cited by 41
Schneider, S., Sharp, K. H., Barker, P. D., & Paoli, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607516200 · Cited by 40
Chen, H., Wu, R., Xu, G., Fang, X., Qiu, X., Guo, H., Tian, B., & Hua, Y. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.04.106 · Cited by 40
Mechanisms of siderophore sorption to smectite and siderophore-enhanced release of structural Fe3+
Haack, E. A., Johnston, C. T., & Maurice, P. A. (2008) · Geochimica et Cosmochimica Acta · doi:10.1016/j.gca.2008.03.027 · Cited by 40
Siderophore-controlled Iron Assimilation in the Enterobacterium Erwinia chrysanthemi
Expert, D., Boughammoura, A., & Franza, T. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807749200 · Cited by 40
Galbis-Martínez, M., Padmanabhan, S., Murillo, F. J., & Arnanz, M. E. (2012) · Journal of Bacteriology · doi:10.1128/jb.06662-11 · Cited by 40
Involvement of AlgQ in Transcriptional Regulation of Pyoverdine Genes in Pseudomonas aeruginosa PAO1
Ambrosi, C., Tiburzi, F., Imperi, F., Putignani, L., & Visca, P. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.15.5097-5107.2005 · Cited by 40
Díaz-Mireles, E., Wexler, M., Todd, J. D., Bellini, D., Johnston, A. W. B., & Sawers, R. G. (2005) · Microbiology · doi:10.1099/mic.0.28342-0 · Cited by 40
Bitoun, J. P., Wu, G., & Ding, H. (2008) · BioMetals · doi:10.1007/s10534-008-9154-7 · Cited by 39
Hernández-Montiel, L. G., Rueda-Puente, E. O., Cordoba-Matson, M. V., Holguín-Peña, J. R., & Zulueta-Rodríguez, R. (2013) · Crop Protection · doi:10.1016/j.cropro.2013.01.008 · Cited by 39
Exploring the microbial metalloproteome using MIRAGE
Sevcenco, A., Pinkse, M. W. H., Wolterbeek, H. T., Verhaert, P. D. E. M., Hagen, W. R., & Hagedoorn, P. (2011) · Metallomics · doi:10.1039/c1mt00154j · Cited by 39
Metallomics: An integrated science for metals in biology and medicine
Sun, H., & Chai, Z. (2010) · Annual Reports Section A (Inorganic Chemistry) · doi:10.1039/b920672h · Cited by 39
Battisti, J. M., Sappington, K. N., Smitherman, L. S., Parrow, N. L., & Minnick, M. F. (2006) · Infection and Immunity · doi:10.1128/iai.00245-06 · Cited by 39
Siderophore-Mediated Iron Dissolution from Nontronites Is Controlled by Mineral Cristallochemistry
Parrello, D., Zegeye, A., Mustin, C., & Billard, P. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.00423 · Cited by 39
Wichard, T. (2016) · Frontiers in Marine Science · doi:10.3389/fmars.2016.00131 · Cited by 40
Zhou, J., Jiang, N., Wang, Z., Li, L., Zhang, J., Ma, R., Nie, H., & Li, Z. (2016) · Applied and Environmental Microbiology · doi:10.1128/aem.02412-16 · Cited by 39
Regulation of Iron Storage by CsrA Supports Exponential Growth of Escherichia coli
Pourciau, C., Pannuri, A., Potts, A. H., Yakhnin, H., Babitzke, P., & Romeo, T. (2019) · mBio · doi:10.1128/mbio.01034-19 · Cited by 39
Proteomic analysis of Flavobacterium psychrophilum cultured in vivo and in iron-limited media
LaFrentz, B. R., LaPatra, S., Call, D. R., Wiens, G. D., & Cain, K. D. (2009) · Diseases of Aquatic Organisms · doi:10.3354/dao02122 · Cited by 39
Iron trafficking system in Helicobacter pylori
Ge, R., & Sun, X. (2011) · BioMetals · doi:10.1007/s10534-011-9512-8 · Cited by 39
Vassiliadis, G., Péduzzi, J., Zirah, S., Thomas, X., Rebuffat, S., & Destoumieux‐Garzón, D. (2007) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00261-07 · Cited by 39
Kontoghiorghe, C., Kolnagou, A., & Kontoghiorghes, G. J. (2013) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2013.787408 · Cited by 40
Toukoki, C., Gold, K. M., McIver, K. S., & Eichenbaum, Z. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07157.x · Cited by 37
The Vibrio cholerae VexGH RND Efflux System Maintains Cellular Homeostasis by Effluxing Vibriobactin
Kunkle, D. E., Bina, X. R., & Bina, J. E. (2017) · mBio · doi:10.1128/mbio.00126-17 · Cited by 39
Zhang, Y., Pan, X., Wang, L., & Chen, L. (2020) · Journal of drug targeting · doi:10.1080/1061186x.2020.1824235 · Cited by 39
Ferric Uptake Regulator (FUR) protein: properties and implications in cyanobacteria
Kaushik, M. S., Singh, P. K., Tiwari, B., & Mishra, A. K. (2015) · Annals of Microbiology · doi:10.1007/s13213-015-1134-x · Cited by 38
Iron and pH ‐responsive FtrABCD ferrous iron utilization system of B ordetella species
Brickman, T. J., & Armstrong, S. K. (2012) · Molecular Microbiology · doi:10.1111/mmi.12003 · Cited by 39
Transfusion‐related biologic effects and free hemoglobin, heme, and iron
Ozment, C. P., Mamo, L. B., Campbell, M. L., Lokhnygina, Y. V., Ghio, A. J., & Turi, J. L. (2012) · Transfusion · doi:10.1111/j.1537-2995.2012.03837.x · Cited by 38
Diep, B. A., Phung, Q. T., Date, S. V., Arnott, D. P., Bakalarski, C. E., Xu, M. J., Nakamura, G. R., Swem, D. L., Alexander, M. K., Le, H. N., et al. (2013) · The Journal of Infectious Diseases · doi:10.1093/infdis/jit662 · Cited by 38
Acquisition of Iron by Alkaliphilic Bacillus Species
McMillan, D. G. G., Velasquez, I. B., Nunn, B. L., Goodlett, D. R., Hunter, K. A., Lamont, I. L., Sander, S. G., & Cook, G. M. (2010) · Applied and Environmental Microbiology · doi:10.1128/aem.01393-10 · Cited by 38
Cyanogenic Glycosides and the fate of cyanide in soil
Ubalua, A. O. (2010) · Australian Journal of Crop Science · Cited by 38
Antimicrobial Nanomaterials: Why Evolution Matters
Graves, J. L., Thomas, M. D., & Ewunkem, A. J. (2017) · Nanomaterials · doi:10.3390/nano7100283 · Cited by 38
Investigating the influence of iron on Campylobacter jejuni transcriptome in response to acid stress
Askoura, M., Youns, M., & Hegazy, W. A. H. (2019) · Microbial Pathogenesis · doi:10.1016/j.micpath.2019.103777 · Cited by 38
Shao, S., Li, C., Zhao, L., Zhang, Y., Yin, K., & Wang, Q. (2021) · Microbiological Research · doi:10.1016/j.micres.2021.126892 · Cited by 39
Novel Insights on Pyoverdine: From Biosynthesis to Biotechnological Application
Dell’Anno, F., Vitale, G. A., Buonocore, C., Vitale, L. A., Esposito, F. P., Coppola, D., Sala, G. D., Tedesco, P., & de Pascale, D. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911507 · Cited by 38
Protective role of bacillithiol in superoxide stress and Fe–S metabolism in Bacillus subtilis
Fang, Z., & Dos Santos, P. C. (2015) · MicrobiologyOpen · doi:10.1002/mbo3.267 · Cited by 38
Wu, C.-C., Wang, C., Chen, Y., Lin, T., Jinn, T., & Lin, C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0107812 · Cited by 38
Trace metal elements: a bridge between host and intestinal microorganisms
Ma, Y., Fei, Y., Ding, S., Jiang, H., Fang, J. Q., & Liu, G. (2023) · Science China Life Sciences · doi:10.1007/s11427-022-2359-4 · Cited by 39
The ins and outs of metal homeostasis by the root nodule actinobacterium Frankia
Furnholm, T., & Tisa, L. S. (2014) · BMC Genomics · doi:10.1186/1471-2164-15-1092 · Cited by 37
Valerio, L. G. (2007) · Toxicology Mechanisms and Methods · doi:10.1080/15376510701556690 · Cited by 38
Bailey, D. C., Drake, E. J., Grant, T. D., & Gulick, A. M. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00409 · Cited by 40
Reed, S., Neuman, H., Glahn, R. P., Koren, O., & Tako, E. (2017) · PLoS ONE · doi:10.1371/journal.pone.0182431 · Cited by 38
Roth, T. L., Switzer, A. D., Watanabe‐Chailland, M., Bik, E. M., Relman, D. A., Romick‐Rosendale, L. E., & Ollberding, N. J. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.02291 · Cited by 37
Effects of Fe(II) on anammox community activity and physiologic response
Ding, J., Seow, W., Zhou, J. Z., Zeng, R. J., Gu, J., & Zhou, Y. (2020) · Frontiers of Environmental Science & Engineering · doi:10.1007/s11783-020-1299-9 · Cited by 37
Improved production of heme using metabolically engineered Escherichia coli
Choi, K. R., Yu, H. E., Lee, H., & Lee, S. Y. (2022) · Biotechnology and Bioengineering · doi:10.1002/bit.28194 · Cited by 37
Griffiths, T. A. M., Mauk, A. G., & MacGillivray, R. T. A. (2005) · Biochemistry · doi:10.1021/bi051559k · Cited by 37
Differential gene expression in Streptococcus pneumoniae in response to various iron sources
Gupta, R., Shah, P. H., & Swiatlo, E. (2009) · Microbial Pathogenesis · doi:10.1016/j.micpath.2009.05.003 · Cited by 37
Regulation by Iron: RNA Rules the Rust
Kadner, R. J. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.20.6870-6873.2005 · Cited by 37
Benson, H. P., Boncompagni, É., & Guerinot, M. L. (2005) · Molecular Plant-Microbe Interactions · doi:10.1094/mpmi-18-0950 · Cited by 37
Takatsuka, M., Osada‐Oka, M., Satoh, E. F., Kitadokoro, K., Nishiuchi, Y., Niki, M., Inoue, M., Iwaï, K., Arakawa, T., Shimoji, Y., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020985 · Cited by 37
Stoof, J., Kuipers, E. J., Klaver, G. T., & van Vliet, A. H. M. (2010) · Infection and Immunity · doi:10.1128/iai.00365-10 · Cited by 37
Pleiotropic roles of iron-responsive transcriptional regulator Fur in Burkholderia multivorans
Yuhara, S., Komatsu, H., Goto, H., Ohtsubo, Y., Nagata, Y., & Tsuda, M. (2008) · Microbiology · doi:10.1099/mic.0.2007/015537-0 · Cited by 37
Staphylococcus aureus Pore-Forming Toxins
Robles, T. R., & Torres, V. J. (2016) · Current topics in microbiology and immunology · doi:10.1007/82_2016_16 · Cited by 39
Characterization of Enterobacteria Using MALDI-TOF Mass Spectrometry
Pribil, P. A., & Fenselau, C. (2005) · Analytical Chemistry · doi:10.1021/ac050737c · Cited by 37
Modulation of NB4 promyelocytic leukemic cell machinery by Anaplasma phagocytophilum
Pedra, J. H. F., Sukumaran, B., Carlyon, J. A., Berliner, N., & Fikrig, E. (2005) · Genomics · doi:10.1016/j.ygeno.2005.05.008 · Cited by 37
Junker, L. M., Peters, J. E., & Hay, A. G. (2006) · Microbiology · doi:10.1099/mic.0.28767-0 · Cited by 37
Integrating microbial siderophores into concepts of plant iron nutrition
Gu, S., Wang, N., Zheng, Y., Wang, T., Shen, Q., Zhang, F. S., Kümmerli, R., Wei, Z., & Zuo, Y. (2025) · Nature Plants · doi:10.1038/s41477-025-02171-x · Cited by 39
Hernández‐Rivas, J., Alonso, I., Pellicer, S., Peleato, M. L., Cases, R., Strasser, R. J., Barja, F., & Fillat, M. F. (2009) · Journal of Plant Physiology · doi:10.1016/j.jplph.2009.10.009 · Cited by 36
Parker, J. K., Chen, H., McCarty, S. E., Liu, L. Y., & Fuente, L. D. L. (2016) · Environmental Microbiology · doi:10.1111/1462-2920.13242 · Cited by 35
Expanding the Role of FurA as Essential Global Regulator in Cyanobacteria
González, A., Bes, M. T., Peleato, M. L., & Fillat, M. F. (2016) · PLoS ONE · doi:10.1371/journal.pone.0151384 · Cited by 35
Interplay between siderophores and colibactin genotoxin in Escherichia coli
Martín, P., Tronnet, S., Garcie, C., & Oswald, É. (2017) · IUBMB Life · doi:10.1002/iub.1612 · Cited by 38
Johnstone, T. C., & Nolan, E. M. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b09375 · Cited by 36
Activity of siderophores against drug-resistant Gram-positive and Gram-negative bacteria
Gokarn, K., & Pal, R. B. (2018) · Infection and Drug Resistance · doi:10.2147/idr.s148602 · Cited by 36
Zupok, A., Iobbi‐Nivol, C., Méjean, V., & Leimkühler, S. (2019) · Metallomics · doi:10.1039/c9mt00186g · Cited by 37
Wehrmann, M., Berthelot, C., Billard, P., & Klebensberger, J. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.02494 · Cited by 38
Leal, C., Fontaine, F., Aziz, A., Egas, C., Clément, C., & Trotel‐Aziz, P. (2021) · Environmental Microbiome · doi:10.1186/s40793-021-00372-3 · Cited by 36
Ammonia-Oxidizing Bacteria: Their Biochemistry and Molecular Biology
Sayavedra‐Soto, L. A., & Arp, D. J. (2014) · ASM Press eBooks · doi:10.1128/9781555817145.ch2 · Cited by 36
Lee, H., Kim, J., Lee, M., Park, S., & Lee, K. (2013) · Molecular Microbiology · doi:10.1111/mmi.12224 · Cited by 36
Keluskar, R. P., Nerurkar, A. S., & Desai, A. J. (2013) · Archives of Microbiology · doi:10.1007/s00203-013-0926-2 · Cited by 36
The Iron Stimulon and Fur Regulon of Geobacter sulfurreducens and Their Role in Energy Metabolism
Embree, M., Qiu, Y. L., Shieu, W., Nagarajan, H., O'Neil, R. A., Lovley, D. R., & Zengler, K. (2014) · Applied and Environmental Microbiology · doi:10.1128/aem.03916-13 · Cited by 35
Biophysical features of MagA expression in mammalian cells: implications for MRI contrast
Sengupta (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00029 · Cited by 36
Yu, X., Chen, M., Jiang, Z., Hu, Y. P., & Xie, Z. (2014) · Journal of Bacteriology · doi:10.1128/jb.01756-14 · Cited by 36
Hernández‐Rivas, J., Peleato, M. L., Fillat, M. F., & Bes, M. T. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.09.060 · Cited by 36
Weinbauer, M. G., Arrieta, J. M., Griebler, C., & Herndl, G. J. (2009) · Limnology and Oceanography · doi:10.4319/lo.2009.54.3.0774 · Cited by 36
Torres‐Romero, J. C., & Arroyo, R. (2009) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2009.06.003 · Cited by 36
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
