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 301–400 of 1,010
The Good, the Bad, and the Ugly of Rhizosphere Microbiome
Ali, M. A., Naveed, M., Mustafa, A., & Abbas, A. (2017) · Springer eBooks · doi:10.1007/978-981-10-3473-2_11 · Cited by 106
Stripping Away the Soil: Plant Growth Promoting Microbiology Opportunities in Aquaponics
Bartelme, R. P., Oyserman, B. O., Blom, J. E., Sepulveda‐Villet, O. J., & Newton, R. J. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.00008 · Cited by 115
Paganini, D., Uyoga, M. A., & Zimmermann, M. B. (2016) · Nutrients · doi:10.3390/nu8080494 · Cited by 107
Cyanobacteria Metal Interactions: Requirements, Toxicity, and Ecological Implications
Baptista, M. S., & Vasconcelos, T. (2006) · Critical Reviews in Microbiology · doi:10.1080/10408410600822934 · Cited by 105
Kouzuma, A., Kasai, T., Hirose, A., & Watanabe, K. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00609 · Cited by 106
Yao, H., Wang, Y., Lovell, S., Kumar, R. N., Ruvinsky, A. M., Battaile, K. P., Vakser, I. A., & Rivera, M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja305180n · Cited by 102
Zawadzka, A. M., Abergel, R. J., Nichiporuk, R. V., Andersen, U. N., & Raymond, K. N. (2009) · Biochemistry · doi:10.1021/bi8018674 · Cited by 104
Selective recognition of metal ions by metalloregulatory proteins
Chen, P. R., & He, C. (2008) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2007.12.010 · Cited by 102
Why microbes secrete molecules to modify their environment: the case of iron-chelating siderophores
Leventhal, G. E., Ackermann, M., & Schiessl, K. T. (2019) · Journal of The Royal Society Interface · doi:10.1098/rsif.2018.0674 · Cited by 100
Lewis, J. P. (2009) · Periodontology 2000 · doi:10.1111/j.1600-0757.2009.00329.x · Cited by 105
Ernst, F. D., Kuipers, E. J., Heijens, A., Sarwari, R., Stoof, J., Penn, C. W., Kusters, J. G., & van Vliet, A. H. M. (2005) · Infection and Immunity · doi:10.1128/iai.73.11.7252-7258.2005 · Cited by 101
Toward a mechanistic understanding of Feo-mediated ferrous iron uptake
Sestok, A. E., Linkous, R. O., & Smith, A. T. (2018) · Metallomics · doi:10.1039/c8mt00097b · Cited by 96
The Role of Ovotransferrin in Egg-White Antimicrobial Activity: A Review
Legros, J., Jan, S., Bonnassie, S., Gautier, M., Croguennec, T., Pezennec, S., Cochet, M.-F., Nau, F., Andrews, S. C., & Baron, F. (2021) · Foods · doi:10.3390/foods10040823 · Cited by 102
Self-citationIron Acquisition Mechanisms and Their Role in the Virulence of Burkholderia Species
Butt, A. T., & Thomas, M. S. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00460 · Cited by 103
Salvail, H., & Massé, É. (2011) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.102 · Cited by 108
NikR-mediated regulation of Helicobacter pylori acid adaptation
van Vliet, A. H. M., Ernst, F. D., & Kusters, J. G. (2004) · Trends in Microbiology · doi:10.1016/j.tim.2004.09.005 · Cited by 100
Plant Growth Promoting Rhizobacteria (PGPR) - Prospective and Mechanisms: A Review
Jeyanthi, V., & Kanimozhi, S. (2018) · Journal of Pure and Applied Microbiology · doi:10.22207/jpam.12.2.34 · Cited by 99
A molecular assessment of the iron stress response in the two phylogenetic clades of Trichodesmium
Chappell, P. D., & Webb, E. A. (2009) · Environmental Microbiology · doi:10.1111/j.1462-2920.2009.02026.x · Cited by 102
Characterization of a Bacillus subtilis transporter for petrobactin, an anthrax stealth siderophore
Zawadzka, A. M., Kim, Y., Maltseva, N., Nichiporuk, R. V., Fan, Y., Joachimiak, A., & Raymond, K. N. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904793106 · Cited by 99
Oral iron exacerbates colitis and influences the intestinal microbiome
Mahalhal, A., Williams, J. M., Johnson, S., Ellaby, N., Duckworth, C. A., Burkitt, M. D., Liu, X., Hold, G. L., Campbell, B. J., Pritchard, D. M., et al. (2018) · PLoS ONE · doi:10.1371/journal.pone.0202460 · Cited by 98
López-Gomollón, S., Hernández, J. A., Pellicer, S., Angarica, V. E., Peleato, M. L., & Fillat, M. F. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.09.010 · Cited by 98
Verma, P. P., Shelake, R. M., Das, S., Sharma, P., & Kim, J. (2019) · Springer eBooks · doi:10.1007/978-981-13-8391-5_11 · Cited by 100
Perspective on the biotechnological production of bacterial siderophores and their use
Soares, E. V. (2022) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-022-11995-y · Cited by 99
A small RNA promotes siderophore production through transcriptional and metabolic remodeling
Salvail, H., Lanthier-Bourbonnais, P., Sobota, J. M., Caza, M., Benjamin, J.-A. M., Mendieta, M. E. S., Lepine, F. L., Dozois, C. M., Imlay, J. A., & Massé, É. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1007805107 · Cited by 103
Beller, H. R., Letain, T. E., Chakicherla, A. Y., Kane, S. R., Legler, T. C., & Coleman, M. A. (2006) · Journal of Bacteriology · doi:10.1128/jb.00568-06 · Cited by 97
Origin and Evolution of the Sodium -Pumping NADH: Ubiquinone Oxidoreductase
Reyes‐Prieto, A., Barquera, B., & Juárez, O. X. (2014) · PLoS ONE · doi:10.1371/journal.pone.0096696 · Cited by 96
Siderophore-mediated iron acquisition in Bacillus anthracis and related strains
Hotta, K., Kim, C., Fox, D. T., & Koppisch, A. T. (2010) · Microbiology · doi:10.1099/mic.0.039404-0 · Cited by 100
Regulation of Iron Transport inStreptococcus pneumoniaeby RitR, an Orphan Response Regulator
Ulijasz, A. T., Andes, D. R., Glasner, J. D., & Weisblum, B. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.23.8123-8136.2004 · Cited by 97
Gioia, J., Qin, X., Jiang, H., Clinkenbeard, K. D., Lo, R. Y. C., Liu, Y., Fox, G. E., Yerrapragada, S., McLeod, M. P., McNeill, T. Z., et al. (2006) · Journal of Bacteriology · doi:10.1128/jb.00675-06 · Cited by 97
Mycobacterium tuberculosis Can Utilize Heme as an Iron Source
Jones, C. M., & Niederweis, M. (2011) · Journal of Bacteriology · doi:10.1128/jb.01312-10 · Cited by 94
Adler, C., Corbalán, N. S., Peralta, D. R., Pomares, M. F., de Cristóbal, R. E., & Vincent, P. A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0084734 · Cited by 97
Shcolnick, S., Shaked, Y., & Keren, N. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.11.015 · Cited by 96
Dellagi, A., Segond, D., Rigault, M., Fagard, M., Simon, C., Saindrenan, P., & Expert, D. (2009) · PLANT PHYSIOLOGY · doi:10.1104/pp.109.138636 · Cited by 96
Probing regulon of ArcA in Shewanella oneidensis MR-1 by integrated genomic analyses
Gao, H., Wang, X., Yang, Z. K., Palzkill, T. G., & Zhou, J. Z. (2008) · BMC Genomics · doi:10.1186/1471-2164-9-42 · Cited by 95
Shu, D., He, Y., Yue, H., & Yang, S. (2016) · RSC Advances · doi:10.1039/c6ra09209h · Cited by 94
Ferrous iron efflux systems in bacteria
Pi, H., & Helmann, J. D. (2017) · Metallomics · doi:10.1039/c7mt00112f · Cited by 93
Marchetti, M., Bei, O. D., Bettati, S., Campanini, B., Kovachka, S., Gianquinto, E., Spyrakis, F., & Ronda, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21062145 · Cited by 93
A survey of TonB‐dependent receptors in fluorescent pseudomonads
Cornélis, P., & Bodilis, J. (2009) · Environmental Microbiology Reports · doi:10.1111/j.1758-2229.2009.00041.x · Cited by 95
Ernst, F. D., Stoof, J., Horrevoets, W. M., Kuipers, E. J., Kusters, J. G., & van Vliet, A. H. M. (2006) · Infection and Immunity · doi:10.1128/iai.01196-06 · Cited by 94
García, C. A., Alcaraz, E. S., Franco, M. A., & de Rossi, B. P. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00926 · Cited by 94
Miethke, M., Monteferrante, C. G., Marahiel, M. A., & van Dijl, J. M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.05.027 · Cited by 98
Siderophores as molecular tools in medical and environmental applications
Kurth, C., Kage, H., & Nett, M. (2016) · Organic & Biomolecular Chemistry · doi:10.1039/c6ob01400c · Cited by 101
Gilbreath, J. J., Cody, W. L., Merrell, D. S., & Hendrixson, D. R. (2011) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00035-10 · Cited by 94
Identification of an Escherichia coli O157:H7 heme oxygenase with tandem functional repeats
Suits, M. D. L., Pal, G. P., Nakatsu, K., Matte, A., Cygler, M., & Jia, Z. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504289102 · Cited by 91
Iron in micronutrient Powder promotes an Unfavorable gut microbiota in Kenyan infants
Tang, M., Frank, D., Hendricks, A., Ir, D., Esamai, F., Liechty, E., Hambidge, K., & Krebs, N. (2017) · Nutrients · doi:10.3390/nu9070776 · Cited by 94
“Unabsorbed iron in the gut, usually caused by excessive iron intake (by fortification or supplementation), fosters growth of these pathogenic strains [6] and could potentially modify the balance of microbial species inhabiting the gut, and may thereby pose long-term health consequences.”
BackgroundThe FeoA protein is necessary for the FeoB transporter to import ferrous iron
Kim, H., Lee, H., & Shin, D. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.06.027 · Cited by 93
Ferric iron reductases and their contribution to unicellular ferrous iron uptake
Cain, T. J., & Smith, A. T. (2021) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2021.111407 · Cited by 92
Nandal, A., Huggins, C. C., Woodhall, M. R., McHugh, J. P., Rodríguez‐Quiñones, F., Quail, M. A., Guest, J. R., & Andrews, S. C. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06977.x · Cited by 93
Self-citationRea, R. B., Hill, C., & Gahan, C. G. M. (2005) · Applied and Environmental Microbiology · doi:10.1128/aem.71.12.8314-8322.2005 · Cited by 93
Bacterial Chat: Intestinal Metabolites and Signals in Host-Microbiota-Pathogen Interactions
Lustri, B. C., Sperandio, V., & Moreira, C. G. (2017) · Infection and Immunity · doi:10.1128/iai.00476-17 · Cited by 98
Monnet, C., Loux, V., Gibrat, J.-F., Spinnler, H.-É., Barbe, V., Vacherie, B., Gavory, F., Gourbeyre, E., Siguier, P., Chandler, M., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015489 · Cited by 92
Carpenter, C. D., & Payne, S. M. (2014) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2014.01.007 · Cited by 95
de Souza, R., Meyer, J., Schoenfeld, R., da Costa, P. B., & Passaglia, L. M. P. (2014) · Annals of Microbiology · doi:10.1007/s13213-014-0939-3 · Cited by 92
Neto, J. F. D. S., Braz, V. S., Italiani, V. C. S., & Marques, M. V. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp509 · Cited by 92
Yang, J., Sangwan, I., Lindemann, A., Hauser, F., Hennecke, H., Fischer, H., & O’Brian, M. R. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05101.x · Cited by 92
Abergel, R. J., Zawadzka, A. M., Hoette, T. M., & Raymond, K. N. (2009) · Journal of the American Chemical Society · doi:10.1021/ja903051q · Cited by 95
Lin, C.-T., Wu, C.-C., Chen, Y.-S., Lai, Y.-C., Chi, C., Lin, J.-C., Chen, Y., & Peng, H.-L. (2011) · Microbiology · doi:10.1099/mic.0.044065-0 · Cited by 86
Metal binding ability of microbial natural metal chelators and potential applications
Hofmann, M., Retamal-Morales, G., & Tischler, D. (2020) · Natural Product Reports · doi:10.1039/c9np00058e · Cited by 95
Schröder, J., & Tauch, A. (2010) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2010.00228.x · Cited by 91
Molecular evidence of iron limitation and availability in the global diazotroph Trichodesmium
Chappell, P. D., Moffett, J. W., Hynes, A., & Webb, E. A. (2012) · The ISME Journal · doi:10.1038/ismej.2012.13 · Cited by 91
Ghysels, B., Ochsner, U. A., Möllman, U., Heinisch, L., Vasil, M. L., Cornélis, P., & Matthijs, S. (2005) · FEMS Microbiology Letters · doi:10.1016/j.femsle.2005.04.010 · Cited by 91
Guo, X., Liu, N., Li, X., Ding, Y., Shang, F., Gao, Y., Ruan, J., & Huang, Y. (2015) · Applied and Environmental Microbiology · doi:10.1128/aem.03859-14 · Cited by 91
The Physiology and Metabolism of Enterococci
Ramsey, M. M., Hartke, A., & Huycke, M. M. (2014) · Cited by 90
Liu, J., Tang, L., Gao, H. J., Zhang, M., & Guo, C. (2018) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.9185 · Cited by 91
Association of ferritin autoantibodies with giant cell arteritis/polymyalgia rheumatica
Baerlecken, N. T., Linnemann, A., Gross, W. L., Moosig, F., Vázquez-Rodríguez, T. R., González-Gay, M. Á., Martin, J. J., Kötter, I., Henes, J. C., Melchers, I., et al. (2012) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2011-200413 · Cited by 90
Ferrosenescence: The iron age of neurodegeneration?
Sfera, A., Bullock, K., Price, A. I., Inderias, L., & Osorio, C. P. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2017.11.012 · Cited by 91
Mechanisms of group A Streptococcus resistance to reactive oxygen species
Henningham, A., Döhrmann, S., Nizet, V., & Cole, J. N. (2015) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuu009 · Cited by 92
Pysz, M. A., Conners, S. B., Montero, C. I., Shockley, K. R., Johnson, M. R., Ward, D. E., & Kelly, R. M. (2004) · Applied and Environmental Microbiology · doi:10.1128/aem.70.10.6098-6112.2004 · Cited by 90
Redox Sensing by Fe 2+ in Bacterial Fur Family Metalloregulators
Pinochet-Barros, A., & Helmann, J. D. (2018) · Antioxidants & Redox Signaling · doi:10.1089/ars.2017.7359 · Cited by 85
Iron Homeostasis in Bacillus subtilis Requires Siderophore Production and Biofilm Formation
Rizzi, A., Roy, S., Bellenger, J., & Beauregard, P. B. (2018) · Applied and Environmental Microbiology · doi:10.1128/aem.02439-18 · Cited by 89
Healy, C. M., Muñoz‐Wolf, N., Strydom, J., Faherty, L., Williams, N. C., Kenny, S., Donnelly, S. C., & Cloonan, S. M. (2021) · Respiratory Research · doi:10.1186/s12931-021-01722-y · Cited by 90
Fertilization of Microbial Composts: A Technology for Improving Stress Resilience in Plants
Ahmed, T., Noman, M., Qi, Y., Shahid, M., Hussain, S., Masood, H. A., Xu, L., Ali, H. M., Negm, S., El-kott, A. F., et al. (2023) · Plants · doi:10.3390/plants12203550 · Cited by 107
Discovery of Fur binding site clusters in Escherichia coli by information theory models
Chen, Z., Lewis, K. A., Shultzaberger, R. K., Lyakhov, I. G., Zheng, M., Doan, B., Storz, G., & Schneider, T. D. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm631 · Cited by 88
Virulence Plasmid Harbored by UropathogenicEscherichia coliFunctions in Acute Stages of Pathogenesis
Cusumano, C. K., Hung, C., Chen, S. L., & Hultgren, S. J. (2010) · Infection and Immunity · doi:10.1128/iai.01260-09 · Cited by 89
Lo, M., Murray, G. L., Khoo, C. A., Haake, D. A., Zuerner, R. L., & Adler, B. (2010) · Infection and Immunity · doi:10.1128/iai.00435-10 · Cited by 89
Budič, M., Rijavec, M., Petkovšek, Ž., & Žgur‐Bertok, D. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028769 · Cited by 88
Egg white versus Salmonella Enteritidis! A harsh medium meets a resilient pathogen
Baron, F., Nau, F., Guérin‐Dubiard, C., Bonnassié, S., Gautier, M., Andrews, S. C., & Jan, S. (2015) · Food Microbiology · doi:10.1016/j.fm.2015.09.009 · Cited by 93
Self-citationIroning out the problem: new mechanisms of iron homeostasis
Massé, É., & Arguin, M. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.06.005 · Cited by 93
Miethke, M., Hou, J., & Marahiel, M. A. (2011) · Biochemistry · doi:10.1021/bi201517h · Cited by 88
Youard, Z. A., Wenner, N., & Reimmann, C. (2010) · BioMetals · doi:10.1007/s10534-010-9399-9 · Cited by 88
Iron acquisition mechanisms of the Burkholderia cepacia complex
Thomas, M. S. (2007) · BioMetals · doi:10.1007/s10534-006-9065-4 · Cited by 88
Olakanmi, O., Schlesinger, L. S., & Britigan, B. E. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0606405 · Cited by 88
Heme Utilization in Campylobacter jejuni
Ridley, K. A., Rock, J. D., Li, Y., & Ketley, J. M. (2006) · Journal of Bacteriology · doi:10.1128/jb.00994-06 · Cited by 88
Beyond the Fur paradigm: iron-controlled gene expression in rhizobia
Rudolph, G., Hennecke, H., & Fischer, H. (2006) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2006.00030.x · Cited by 90
Weeratunga, S. K., Gee, C. E., Lovell, S., Zeng, Y., Woodin, C. L., & Rivera, M. (2009) · Biochemistry · doi:10.1021/bi900561a · Cited by 87
Characterization of Contaminants from a Sanitized Milk Processing Plant
Cleto, S., Matos, S., Kluskens, L., & Vieira, M. J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040189 · Cited by 86
Wang, J., Gerard Muyzer, C., Bodelier, P. L. E., & Laanbroek, H. J. (2009) · The ISME Journal · doi:10.1038/ismej.2009.7 · Cited by 86
Crystal Structure and Biochemical Features of EfeB/YcdB from Escherichia coli O157
Liu, X., Du, Q., Wang, Z., Zhu, D., Huang, Y., Li, N., Wei, T., Xu, S., & Gu, L. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.197780 · Cited by 85
The Effect of Iron Limitation on the Transcriptome and Proteome of Pseudomonas fluorescens Pf-5
Lim, C. K., Hassan, K. A., Tetu, S. G., Loper, J. E., & Paulsen, I. T. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039139 · Cited by 88
Rong, C., Huang, Y., Zhang, W., Jiang, W. Z., Li, Y., & Li, J. (2008) · Research in Microbiology · doi:10.1016/j.resmic.2008.06.005 · Cited by 85
Gallium-Protoporphyrin IX Inhibits Pseudomonas aeruginosa Growth by Targeting Cytochromes
Hijazi, S., Visca, P., & Frangipani, E. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00012 · Cited by 84
Molecular call and response: The physiology of bacterial small RNAs
Richards, G. R., & Vanderpool, C. K. (2011) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2011.07.013 · Cited by 84
Ferric Uptake Regulator Fur Is Conditionally Essential in Pseudomonas aeruginosa
Pasqua, M., Visaggio, D., Sciuto, A. L., Genah, S., Banin, E., Visca, P., & Imperi, F. (2017) · Journal of Bacteriology · doi:10.1128/jb.00472-17 · Cited by 88
Haynes, R. K., Chan, W., Wong, H. N., Li, K., Wu, W., Fan, K. M., Sung, H. H. Y., Williams, I. D., Prosperi, D., Melato, S., et al. (2010) · ChemMedChem · doi:10.1002/cmdc.201000225 · Cited by 86
The role of laterally transferred genes in adaptive evolution
Marri, P. R., Hao, W., & Golding, G. B. (2007) · BMC Evolutionary Biology · doi:10.1186/1471-2148-7-s1-s8 · Cited by 84
Niewerth, H., Schuldes, J., Parschat, K., Kiefer, P., Vorholt, J. A., Daniel, R., & Fetzner, S. (2012) · BMC Genomics · doi:10.1186/1471-2164-13-534 · Cited by 86
Ruales-Lonfat, C., Barona, J. F., Sienkiewicz, A., Vélez, J., Benítez, L. N., & Pulgarin, C. O. (2015) · Applied Catalysis B: Environmental · doi:10.1016/j.apcatb.2015.06.030 · Cited by 84
Grad, Y. H., Godfrey, P. A., Cerquiera, G., Mariani‐Kurkdjian, P., Gouali, M., Bingen, É., Shea, T. P., Haas, B. J., Griggs, A. D., Young, S., et al. (2013) · mBio · doi:10.1128/mbio.00452-12 · Cited by 81
Bru, J.-L., Rawson, B., Trinh, C., Whiteson, K., Høyland‐Kroghsbo, N. M., & Siryaporn, A. (2019) · Journal of Bacteriology · doi:10.1128/jb.00383-19 · Cited by 83
Overview of Proteus mirabilis pathogenicity and virulence. Insights into the role of metals
Chakkour, M., Hammoud, Z., Farhat, S., Roz, A. E., Ezzeddine, Z., & Ghssein, G. (2024) · Frontiers in Microbiology · doi:10.3389/fmicb.2024.1383618 · Cited by 105
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