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 501–600 of 1,010
Xu, Y., Yang, S., You, G., & Hou, J. (2021) · Water Research · doi:10.1016/j.watres.2021.116979 · Cited by 68
Genetic regulation of fluxes: iron homeostasis of Escherichia coli
Semsey, S., Andersson, A. M. C., Krishna, S., Jensen, M. H., Massé, É., & Sneppen, K. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl627 · Cited by 70
Hibbing, M. E., & Fuqua, C. (2011) · Journal of Bacteriology · doi:10.1128/jb.00317-11 · Cited by 67
Smaldone, G. T., Antelmann, H., Gaballa, A., & Helmann, J. D. (2012) · Journal of Bacteriology · doi:10.1128/jb.05567-11 · Cited by 67
Allard, M., Moisan, H., Brouillette, É., Gervais, A. L., Jacques, M., Lacasse, P., Diarra, M. S., & Malouin, F. (2006) · Microbes and Infection · doi:10.1016/j.micinf.2006.01.022 · Cited by 67
Dissecting plant iron homeostasis under short and long-term iron fluctuations
Darbani, B., Briat, J., Holm, P. B., Husted, S., Noeparvar, S., & Borg, S. (2013) · Biotechnology Advances · doi:10.1016/j.biotechadv.2013.05.003 · Cited by 68
Rajasekaran, M. B., Nilapwar, S. M., Andrews, S. C., & Watson, K. A. (2009) · BioMetals · doi:10.1007/s10534-009-9262-z · Cited by 67
Self-citationHertlein, G., Müller, S., Garcia‐Gonzalez, E., Poppinga, L., Süßmuth, R. D., & Genersch, E. (2014) · PLoS ONE · doi:10.1371/journal.pone.0108272 · Cited by 67
Selected metal ions protect Bacillus subtilis biofilms from erosion
Grumbein, S., Opitz, M., & Lieleg, O. (2014) · Metallomics · doi:10.1039/c4mt00049h · Cited by 67
Lymberopoulos, M. H., Houle, S., Daigle, F., Léveillé, S., Brée, A., Moulin-Schouleur, M., Johnson, J. R., & Dozois, C. M. (2006) · Journal of Bacteriology · doi:10.1128/jb.00453-06 · Cited by 67
Léveillé, S., Caza, M., Johnson, J. R., Clabots, C., Sabri, M., & Dozois, C. M. (2006) · Infection and Immunity · doi:10.1128/iai.00107-06 · Cited by 67
Kortman, G. A. M., Mulder, M. L. M., Richters, T. J. W., Shanmugam, N. K. N., Trebicka, E., Boekhorst, J., Timmerman, H. M., Roelofs, R., Wiegerinck, E. T., Laarakkers, C. M., et al. (2015) · European Journal of Immunology · doi:10.1002/eji.201545642 · Cited by 65
Mancini, S., & Imlay, J. A. (2015) · Molecular Microbiology · doi:10.1111/mmi.12967 · Cited by 66
Clostridioides difficile LuxS mediates inter-bacterial interactions within biofilms
Slater, R. T., Frost, L. R., Jossi, S. E., Millard, A. D., & Unnikrishnan, M. (2019) · Scientific Reports · doi:10.1038/s41598-019-46143-6 · Cited by 71
Cancer Related Anemia: An Integrated Multitarget Approach and Lifestyle Interventions
Natalucci, V., Virgili, E., Calcagnoli, F., Valli, G., Agostini, D., Zeppa, S. D., Barbieri, E., & Emili, R. (2021) · Nutrients · doi:10.3390/nu13020482 · Cited by 72
Ghssein, G., & Ezzeddine, Z. (2022) · Biology · doi:10.3390/biology11101525 · Cited by 69
Iron acquisition strategies in pseudomonads: mechanisms, ecology, and evolution
Kümmerli, R. (2022) · BioMetals · doi:10.1007/s10534-022-00480-8 · Cited by 65
Gallium and gallium compounds: New insights into the “Trojan horse” strategy in medical applications
Sun, W., Qi, M., Cheng, S., Li, C., Dong, B., & Wang, L. (2023) · Materials & Design · doi:10.1016/j.matdes.2023.111704 · Cited by 70
Pyochelin Potentiates the Inhibitory Activity of Gallium on Pseudomonas aeruginosa
Frangipani, E., Bonchi, C., Minandri, F., Imperi, F., & Visca, P. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.03154-14 · Cited by 66
Control of bacterial iron homeostasis by manganese
Puri, S., Hohle, T. H., & O’Brian, M. R. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002342107 · Cited by 66
TroA of Streptococcus suis Is Required for Manganese Acquisition and Full Virulence
Schreur, P. J. W., Rebel, J. M. J., Smits, M. A., van Putten, J. P. M., & Smith, H. E. (2011) · Journal of Bacteriology · doi:10.1128/jb.05305-11 · Cited by 66
Effects of ferrous and manganese ions on anammox process in sequencing batch biofilm reactors
Huang, X., Gao, D., Peng, S., & Tao, Y. (2014) · Journal of Environmental Sciences · doi:10.1016/s1001-0742(13)60531-8 · Cited by 66
Polyphosphate Functions In Vivo as an Iron Chelator and Fenton Reaction Inhibitor
Beaufay, F., Quarles, E. K., Franz, A. A., Katamanin, O. M., Wholey, W.-Y., & Jakob, U. (2020) · mBio · doi:10.1128/mbio.01017-20 · Cited by 63
Characterization of the Shewanella oneidensis Fur gene: roles in iron and acid tolerance response
Yang, Y., Harris, D. P., Luo, F., Wu, L., Parsons, A. B., Palumbo, A. V., & Zhou, J. Z. (2008) · BMC Genomics · doi:10.1186/1471-2164-9-s1-s11 · Cited by 66
Fernandez, A., Lechardeur, D., Derré-Bobillot, A., Couvé, E., Gaudu, P., & Gruss, A. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000860 · Cited by 65
Sui, X., Wang, J., Zhao, Z., Liu, B., Liu, M., Liu, M., Shi, C., Feng, X., Fu, Y., Shi, D., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-05903-5 · Cited by 68
Bellapadrona, G., Ardini, M., Ceci, P., Stefanini, S., & Chiancone, E. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.10.053 · Cited by 65
Role of Porins in Iron Uptake byMycobacterium smegmatis
Jones, C. M., & Niederweis, M. (2010) · Journal of Bacteriology · doi:10.1128/jb.00986-10 · Cited by 65
Ferritin Nanocages: A Novel Platform for Biomedical Applications
Bhushan, B., Sukumar, U. K., Matai, I., Sachdev, A., Dubey, P., & Gopinath, P. (2014) · Journal of Biomedical Nanotechnology · doi:10.1166/jbn.2014.1980 · Cited by 65
Choi, E., Groisman, E. A., & Shin, D. (2009) · Journal of Bacteriology · doi:10.1128/jb.00958-09 · Cited by 65
Perturbation of Iron Homeostasis Promotes the Evolution of Antibiotic Resistance
Méhi, O., Bogos, B., Csörgő, B., Pál, F., Nyerges, Á., Papp, B., & Pál, C. (2014) · Molecular Biology and Evolution · doi:10.1093/molbev/msu223 · Cited by 65
The ‘liaisons dangereuses’ between iron and antibiotics
Ezraty, B., & Barras, F. (2016) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuw004 · Cited by 62
Lambais, M. R., Berdugo, S. E. B., dos Santos, E. D. C., Crowley, D. E., & Jumpponen, A. (2016) · Microbial Ecology · doi:10.1007/s00248-016-0878-6 · Cited by 66
Iron and Virulence in Stenotrophomonas Maltophilia: All We Know So Far
Kalidasan, V., Joseph, N. M. S., Kumar, S. S., Hamat, R. A., & Neela, V. K. (2018) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2018.00401 · Cited by 64
Opposite Sides of Pantoea agglomerans and Its Associated Commercial Outlook
Lorenzi, A. S., Bonatelli, M. L., Chia, M. A., Peressim, L., & Quecine, M. C. (2022) · Microorganisms · doi:10.3390/microorganisms10102072 · Cited by 65
Unsuspected control of siderophore production by N ‐acetylglucosamine in streptomycetes
Craig, M., Lambert, S., Jourdan, S., Tenconi, E., Colson, S., Maciejewska, M., Ongena, M., Martin, J. F., van Wezel, G. P., & Rigali, S. (2012) · Environmental Microbiology Reports · doi:10.1111/j.1758-2229.2012.00354.x · Cited by 64
Durant, L., Métais, A., Soulama-Mouze, C., Genevard, J.-M., Nassif, X., & Escaich, S. (2006) · Infection and Immunity · doi:10.1128/iai.01269-06 · Cited by 64
Valente, F. M. A., Almeida, C., Pacheco, I., Carita, J. N., Saraiva, L. M., & Pereira, I. A. C. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.9.3228-3235.2006 · Cited by 64
Crossley, R. A., Gaskin, D. J. H., Holmes, K., Mulholland, F., Wells, J. M., Kelly, D. J., van Vliet, A. H. M., & Walton, N. J. (2007) · Applied and Environmental Microbiology · doi:10.1128/aem.01919-07 · Cited by 64
Listeria monocytogenesferritin protects against multiple stresses and is required for virulence
Dussurget, O., Dumas, E., Archambaud, C., Chafsey, I., Chambon, C., Hébraud, M., & Cossart, P. (2005) · FEMS Microbiology Letters · doi:10.1016/j.femsle.2005.07.015 · Cited by 64
Khare, G., Nangpal, P., & Tyagi, A. K. (2017) · PLoS ONE · doi:10.1371/journal.pone.0169545 · Cited by 63
Koedooder, C., Guéneuguès, A., van Geersdaële, R., Vergé, V., Bouget, F., Labreuche, Y., Obernosterer, I., & Blain, S. (2018) · Frontiers in Marine Science · doi:10.3389/fmars.2018.00435 · Cited by 63
Transcriptional and Functional Analysis of the Neisseria gonorrhoeae Fur Regulon
Jackson, L. A., Ducey, T. F., Day, M. W., Zaitshik, J., Orvis, J., & Dyer, D. W. (2009) · Journal of Bacteriology · doi:10.1128/jb.00741-09 · Cited by 62
Liu, X., Olczak, T., Guo, H., Dixon, D. W., & Genco, C. A. (2006) · Infection and Immunity · doi:10.1128/iai.74.2.1222-1232.2006 · Cited by 64
Rondon, M. R., Ballering, K. S., & Thomas, M. G. (2004) · Microbiology · doi:10.1099/mic.0.27319-0 · Cited by 63
Pirated Siderophores Promote Sporulation in Bacillus subtilis
Grandchamp, G. M., Caro, L., & Shank, E. A. (2017) · Applied and Environmental Microbiology · doi:10.1128/aem.03293-16 · Cited by 62
Arai, H., Roh, J. H., & Kaplan, S. (2007) · Journal of Bacteriology · doi:10.1128/jb.01375-07 · Cited by 63
The battle for iron in enteric infections
Sousa Gerós, A., Simmons, A., Drakesmith, H., Aulicino, A., & Frost, J. N. (2020) · Immunology · doi:10.1111/imm.13236 · Cited by 58
Nanocolloidal Hydrogel with Sensing and Antibacterial Activities Governed by Iron Ion Sequestration
Chekini, M., Krivoshapkina, E. F., Shkodenko, L. A., Koshel, E. I., Shestovskaya, M. V., Dukhinova, M., Kheiri, S., Khuu, N., & Kumacheva, E. (2020) · Chemistry of Materials · doi:10.1021/acs.chemmater.0c03362 · Cited by 63
Nutrient-Limited Operational Strategies for the Microbial Production of Biochemicals
Rajpurohit, H., & Eiteman, M. A. (2022) · Microorganisms · doi:10.3390/microorganisms10112226 · Cited by 67
Origins of specificity and cross‐talk in metal ion sensing by Bacillus subtilisFur
Ma, Z., Faulkner, M. J., & Helmann, J. D. (2012) · Molecular Microbiology · doi:10.1111/mmi.12049 · Cited by 62
Osorio, H., Martínez, V., Nieto, P. A., Holmes, D. S., & Quatrini, R. (2008) · BMC Microbiology · doi:10.1186/1471-2180-8-203 · Cited by 62
Global transcriptional response of Caulobacter crescentus to iron availability
Neto, J. F. D. S., Lourenço, R. F., & Marques, M. V. (2013) · BMC Genomics · doi:10.1186/1471-2164-14-549 · Cited by 58
Pumping iron: mechanisms for iron uptake by Campylobacter
Miller, C. E., Williams, P. H., & Ketley, J. M. (2009) · Microbiology · doi:10.1099/mic.0.032425-0 · Cited by 61
Guillén, S., Nadal, L., Álvarez, I., Mañas, P., & Cebrián, G. (2021) · Foods · doi:10.3390/foods10030617 · Cited by 62
Clément, E., Mésini, P. J., Pattus, F., & Schalk, I. J. (2004) · Biochemistry · doi:10.1021/bi049768c · Cited by 61
Effect ofNeisseria meningitidisFur Mutations on Global Control of Gene Transcription
Delany, I., Grifantini, R., Bartolini, E., Rappuoli, R., & Scarlato, V. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.7.2483-2492.2006 · Cited by 61
Benítez, J. J., Keller, A. M., Ochieng, P., Yatsunyk, L. A., Huffman, D. L., Rosenzweig, A. C., & Chen, P. (2008) · Journal of the American Chemical Society · doi:10.1021/ja7107867 · Cited by 62
Roles of Agrobacterium tumefaciens RirA in Iron Regulation, Oxidative Stress Response, and Virulence
Ngok-ngam, P., Ruangkiattikul, N., Mahavihakanont, A., Virgem, S. S., Sukchawalit, R., & Mongkolsuk, S. (2009) · Journal of Bacteriology · doi:10.1128/jb.01380-08 · Cited by 61
Locatelli, F. M., Goo, K.-S., & Ulanová, D. (2016) · Metallomics · doi:10.1039/c5mt00324e · Cited by 61
Eshelman, K., Yao, H., Hewage, A. N. D. P., Deay, J. J., Chandler, J. R., & Rivera, M. (2017) · Metallomics · doi:10.1039/c7mt00042a · Cited by 61
Richter, K., Thomas, N., Zhang, G., Prestidge, C. A., Coenye, T., Wormald, P., & Vreugde, S. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00280 · Cited by 62
Crits‐Christoph, A., Robinson, C. K., Ma, B., Ravel, J., Wierzchoś, J., Ascaso, C., Artieda, O., Souza‐Egipsy, V., Casero, M. C., & DiRuggiero, J. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.00301 · Cited by 62
Siderophore natural products as pharmaceutical agents
Swayambhu, G., Bruno, M. J., Gulick, A. M., & Pfeifer, B. A. (2021) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2021.01.021 · Cited by 64
Xiong, J., Lü, J., Li, X. F., Qiu, Q., Chen, J., & Yan, C. (2021) · Soil Biology and Biochemistry · doi:10.1016/j.soilbio.2021.108395 · Cited by 60
Unraveling the Mechanism for the Viability Deficiency of Shewanella oneidensis oxyR Null Mutant
Shi, M., Wan, F., Mao, Y., & Gao, H. (2015) · Journal of Bacteriology · doi:10.1128/jb.00154-15 · Cited by 60
Robertson, J., Gizdavic‐Nikolaidis, M. R., Nieuwoudt, M. K., & Swift, S. (2018) · PeerJ · doi:10.7717/peerj.5135 · Cited by 62
Biological Functions of the Elements
Lindh, U. (2012) · Springer eBooks · doi:10.1007/978-94-007-4375-5_7 · Cited by 63
Paus, R., Schröder, J. ‐., Reich, K., Kabashima, K., Liu, F. T., Romani, N., Metz, M., Kerstan, A., Lee, P. H. A., Loser, K., et al. (2006) · Experimental Dermatology · doi:10.1111/j.1600-0625.2006.00506_1.x · Cited by 60
The hmuQ and hmuD Genes from Bradyrhizobium japonicum Encode Heme-Degrading Enzymes
Puri, S., & O'Brian, M. R. (2006) · Journal of Bacteriology · doi:10.1128/jb.00737-06 · Cited by 59
Eltarahony, M. M., Abu-Serie, M. M., Hamad, H. A. F., Zaki, S. A. E. F., & Abd-El-Haleem, D. A. M. (2021) · Scientific Reports · doi:10.1038/s41598-021-87363-z · Cited by 59
Chiang, S. M., & Schellhorn, H. E. (2010) · Journal of Molecular Evolution · doi:10.1007/s00239-010-9352-0 · Cited by 59
Functional identification of HugZ, a heme oxygenase from Helicobacter pylori
Guo, Y., Guo, G., Mao, X., Zhang, W., Xiao, J., Tong, W., Liu, T., Xiao, B., Liu, X., Feng, Y., et al. (2008) · BMC Microbiology · doi:10.1186/1471-2180-8-226 · Cited by 59
Sharma, A., Collins, G., & Pruden, A. J. (2009) · Journal of Applied Microbiology · doi:10.1111/j.1365-2672.2009.04323.x · Cited by 59
Growth of Aerobic Ripening Bacteria at the Cheese Surface Is Limited by the Availability of Iron
Monnet, C., Back, A., & Irlinger, F. (2012) · Applied and Environmental Microbiology · doi:10.1128/aem.00085-12 · Cited by 59
Kortman, G. A. M., Reijnders, D., & Swinkels, D. W. (2017) · Hemodialysis International · doi:10.1111/hdi.12553 · Cited by 60
Platero, R., Peixoto, L., O’Brian, M. R., & Fabiano, E. (2004) · Applied and Environmental Microbiology · doi:10.1128/aem.70.7.4349-4355.2004 · Cited by 59
Hydrogen peroxide‐induced oxidative stress responses in Desulfovibrio vulgaris Hildenborough
Zhou, A., He, Z., Redding‐Johanson, A. M., Mukhopadhyay, A., Hemme, C. L., Joachimiak, M. P., Luo, F., Deng, Y., Bender, K. S., He, Q., et al. (2010) · Environmental Microbiology · doi:10.1111/j.1462-2920.2010.02234.x · Cited by 59
Solute channels of the outer membrane: from bacteria to chloroplasts
Duy, D., Soll, J., & Philippar, K. (2007) · Biological Chemistry · doi:10.1515/bc.2007.120 · Cited by 59
Identification and Characterization of a New Ferric Enterobactin Receptor, CfrB, in Campylobacter
Xu, F., Zeng, X., Haigh, R. D., Ketley, J. M., & Lin, J. (2010) · Journal of Bacteriology · doi:10.1128/jb.00478-10 · Cited by 58
Kaur, A. P., Lansky, I. B., & Wilks, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806068200 · Cited by 55
Rhizosphere, Rhizosphere Biology, and Rhizospheric Engineering
Sharma, P., Sharma, M. M. M., Malik, A., Vashisth, M., Singh, D., Kumar, R., Singh, B. P., Patra, A., Mehta, S., & Pandey, V. (2021) · Springer eBooks · doi:10.1007/978-3-030-66587-6_21 · Cited by 59
Charron‐Lamoureux, V., Haroune, L., Pomerleau, M., Hall, L., Orban, F., Leroux, J., Rizzi, A., Bourassa, J.-S., Fontaine, N., d’Astous, É. V., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-38222-0 · Cited by 59
Vasques, N. C., Nogueira, M. A., & Hungría, M. (2024) · Agronomy · doi:10.3390/agronomy14081654 · Cited by 58
Kapoor, D., Sharma, P., Sharma, M. M. M., Yadav, S., & Husen, A. (2024) · Biocatalysis and Agricultural Biotechnology · doi:10.1016/j.bcab.2024.103358 · Cited by 58
Syntheses of Siderophore–Drug Conjugates Using a Convergent Thiol–Maleimide System
Juárez-Hernández, R. E., Miller, P. A., & Miller, M. J. (2012) · ACS Medicinal Chemistry Letters · doi:10.1021/ml300150y · Cited by 58
Romsang, A., Duang-nkern, J., Leesukon, P., Saninjuk, K., Vattanaviboon, P., & Mongkolsuk, S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0086763 · Cited by 59
The Fur Homologue inBorrelia burgdorferi
Katona, L. I., Tokarz, R., Kuhlow, C. J., Benach, J., & Benach, J. L. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.19.6443-6456.2004 · Cited by 58
Coordination of frontline defense mechanisms under severe oxidative stress
Kaur, A., Van, P. T., Busch, C. R., Robinson, C. K., Pan, M., Pang, W. L., Reiss, D. J., DiRuggiero, J., & Baliga, N. S. (2010) · Molecular Systems Biology · doi:10.1038/msb.2010.50 · Cited by 57
Regulation of a glutamyl-tRNA synthetase by the heme status
Levicán, G. J., Katz, A., de Armas-Ricard, M., Núñez, H., & Orellana, O. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611611104 · Cited by 58
Apigenin Impacts the Growth of the Gut Microbiota and Alters the Gene Expression of Enterococcus
Wang, M., Firrman, J., Zhang, L., Arango-Argoty, G., Tomasula, P. M., Liu, L., Xiao, W., & Yam, K. L. (2017) · Molecules · doi:10.3390/molecules22081292 · Cited by 59
Watson, R. J., Joyce, S. A., Spencer, G. V., & Clarke, D. J. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04574.x · Cited by 58
Kim, H., Lee, H., & Shin, D. (2013) · Journal of Bacteriology · doi:10.1128/jb.00343-13 · Cited by 57
Figueiredo, A. R. T., Özkaya, Ö., Kümmerli, R., & Kramer, J. (2021) · Ecology Letters · doi:10.1111/ele.13912 · Cited by 55
The impact of iron and heme availability on the healthy human gut microbiome in vivo and in vitro
Celis, A. I., Relman, D. A., & Huang, K. C. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2022.12.001 · Cited by 58
Lee, S., Kim, J.-A., Song, J.-S., Choe, S., Jang, G., & Kim, Y. (2024) · Frontiers in Microbiology · doi:10.3389/fmicb.2024.1430546 · Cited by 57
Barbier, M., Damron, F. H., Bielecki, P., Diez, M. S., Puchałka, J., Albertí, S., dos Santos, V. A. P. M., & Goldberg, J. B. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089941 · Cited by 57
Metallomics: An integrated biometal science
Ge, R., & Sun, H. (2009) · Science China Chemistry · doi:10.1007/s11426-009-0144-6 · Cited by 57
Cozen, A. E., Weirauch, M. T., Pollard, K. S., Bernick, D. L., Stuart, J. M., & Lowe, T. M. (2008) · Journal of Bacteriology · doi:10.1128/jb.00965-08 · Cited by 57
Structural Basis and Stereochemistry of Triscatecholate Siderophore Binding by FeuA
Peuckert, F., Miethke, M., Albrecht, A. G., Essen, L., & Marahiel, M. A. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200902495 · Cited by 57
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
