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
Opening the Iron Box: Transcriptional Metalloregulation by the Fur Protein
Escolar, L., Pérez-Martín, J., & de Lorenzo, V. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.20.6223-6229.1999 · Cited by 815
Zheng, M., Wang, X., Templeton, L. J., Smulski, D. R., LaRossa, R. A., & Storz, G. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.15.4562-4570.2001 · Cited by 802
Siderophore-Mediated Iron Transport: Crystal Structure of FhuA with Bound Lipopolysaccharide
Ferguson, A. D., Hofmann, E., Coulton, J. W., Diederichs, K., & Welte, W. (1998) · Science · doi:10.1126/science.282.5397.2215 · Cited by 787
A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli.Preprint
Almirón, M. A., Link, A. J., Furlong, D., & Kolter, R. (1992) · Genes & Development · doi:10.1101/gad.6.12b.2646 · Cited by 768
Iron and metal regulation in bacteria
Hantke, K. (2001) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(00)00184-3 · Cited by 755
Guerinot, M. L. (1994) · Annual Review of Microbiology · doi:10.1146/annurev.mi.48.100194.003523 · Cited by 664
Role of iron in regulation of virulence genes
Litwin, C. M., & Calderwood, S. B. (1993) · Clinical Microbiology Reviews · doi:10.1128/cmr.6.2.137 · Cited by 651
Assembly of Iron-Sulfur Clusters
Zheng, L., Cash, V. L., Flint, D. H., & Dean, D. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.13264 · Cited by 650
Bagg, A., & Neilands, J. B. (1987) · Biochemistry · doi:10.1021/bi00391a039 · Cited by 593
Crystal structure of the outer membrane active transporter FepA from Escherichia coli.
Buchanan (1999) · Nature Structural Biology · doi:10.1038/4931 · Cited by 591
The crystal structure of Dps, a ferritin homolog that binds and protects DNA
Grant, R. A., Filman, D. J., Finkel, S. E., Kolter, R., & Hogle, J. M. (1998) · Nature Structural Biology · doi:10.1038/nsb0498-294 · Cited by 560
Lack of a role for iron in the Lyme disease pathogen
Posey, J. E., & Gherardini, F. C. (2000) · Science · doi:10.1126/science.288.5471.1651 · Cited by 538
Role of Iron in Bacterial Infection
Bullen, J. J., Rogers, H. J., & Griffiths, E. (1978) · Modern aspects of electrochemistry · doi:10.1007/978-3-642-66956-9_1 · Cited by 494
The ZnuABC high‐affinity zinc uptake system and its regulator Zur in Escherichia coli
Patzer, S. I., & Hantke, K. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00883.x · Cited by 490
Characterization of the ferrous iron uptake system of Escherichia coli
Kammler, M., Schön, C., & Hantke, K. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.19.6212-6219.1993 · Cited by 460
Schwartz, C. J., Giel, J. L., Patschkowski, T., Luther, C., Ruzicka, F. J., Beinert, H., & Kiley, P. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251550898 · Cited by 442
Touati, D., Jacques, M., Tardat, B., Bouchard, L., & Despied, S. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.9.2305-2314.1995 · Cited by 436
Iron and Hydrogen Peroxide Detoxification Properties of DNA-binding Protein from Starved Cells
Zhao, G., Ceci, P., Ilari, A., Giangiacomo, L., Laue, T. M., Chiancone, E., & Chasteen, N. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202094200 · Cited by 417
Ochsner, U. A., Wilderman, P. J., Vasil, A. I., & Vasil, M. L. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03084.x · Cited by 406
OxyR and SoxRS Regulation of fur
Zheng, M., Doan, B., Schneider, T. D., & Storz, G. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.15.4639-4643.1999 · Cited by 402
Bsat, N., Herbig, A. F., Casillas-Martínez, L., Setlow, P., & Helmann, J. D. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00921.x · Cited by 378
Structural basis of gating by the outer membrane transporter FecA
Ferguson, A. D., Chakraborty, R., Smith, B. S., Esser, L., van der Helm, D., & Deisenhofer, J. (2002) · Science · doi:10.1126/science.1067313 · Cited by 373
Fur Regulon in Gram-negative Bacteria
Stojiljković, I., Bäumler, A. J., & Hantke, K. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1163 · Cited by 371
Andrews, S. C. (1998) · Advances in Microbial Physiology · doi:10.1016/s0065-2911(08)60134-4 · Cited by 353
Self-citationIron regulation of Shiga-like toxin expression in Escherichia coli is mediated by the fur locus
Calderwood, S. B., & Mekalanos, J. J. (1987) · Journal of Bacteriology · doi:10.1128/jb.169.10.4759-4764.1987 · Cited by 334
Pohl, E., Haller, J. C., Mijovilovich, A., Meyer‐Klaucke, W., Garman, E., & Vasil, M. L. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03337.x · Cited by 326
Genetic Evidence that Ferric Reductase Is Required for Iron Uptake in Saccharomyces cerevisiae
Dancis, A., Klausner, R. D., Hinnebusch, A. G., & Barriocanal, J. G. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.5.2294-2301.1990 · Cited by 304
Microbial siderophore-mediated transport.
Winkelmann, G. (2002) · Biochemical Society Transactions · doi:10.1042/bst0300691 · Cited by 301 · cited 2×
“Siderophores usually form hexadentate octahedral complexes with ferric iron and typically employ hydroxamates, K-hydroxycarboxylates and catechols as extremely e¡ective Fe3þ ligands [13,14].”
BackgroundVelayudhan, J., Hughes, N. J., McColm, A. A., Bagshaw, J. A., Clayton, C. L., Andrews, S. C., & Kelly, D. J. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01987.x · Cited by 298
Self-citationBacterial iron transport: mechanisms, genetics, and regulation.
Braun, V., Hantke, K., & Köster, W. L. (1998) · PubMed · Cited by 297
Emerging themes in manganese transport, biochemistry and pathogenesis in bacteria
Kehres, D. G., & Maguire, M. E. (2003) · FEMS Microbiology Reviews · doi:10.1016/s0168-6445(03)00052-4 · Cited by 289
Recognition of DNA by Fur: a Reinterpretation of the Fur Box Consensus Sequence
Baichoo, N., & Helmann, J. D. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.21.5826-5832.2002 · Cited by 282 · cited 1×
“A similar reinterpretation of the Fur box was made by Baichoo and Helmann [114] for Bacillus subtilis, although they identi¢ed a binding site slightly larger (15 bp) than that of Lavrrar et al.”
MethodThe dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site.
Chiancone, E., Ilari, A., Stefanini, S., & Tsernoglou, D. (2000) · Nature Structural Biology · doi:10.1038/71236 · Cited by 280
Visca, P., Leoni, L., Wilson, M. J., & Lamont, I. L. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03088.x · Cited by 279
Repine, J. E., Fox, R. B., & Berger, E. M. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68927-1 · Cited by 279
SufC: an unorthodox cytoplasmic ABC/ATPase required for [Fe—S] biogenesis under oxidative stress
Nachin, L., Loiseau, L., Expert, D., & Barras, F. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg061 · Cited by 278
ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12
Köster, W. L. (2001) · Research in Microbiology · doi:10.1016/s0923-2508(01)01200-1 · Cited by 277
Kox, L. F. F., Wösten, M. M. S. M., & Groisman, E. A. (2000) · The EMBO Journal · doi:10.1093/emboj/19.8.1861 · Cited by 273
Niederhoffer, E. C., Naranjo, C. M., Bradley, K. L., & Fee, J. A. (1990) · Journal of Bacteriology · doi:10.1128/jb.172.4.1930-1938.1990 · Cited by 268
Identification and characterization of the transferrin receptor from Neisseria meningitidis
Schryvers, A. B., & Morris, L. J. (1988) · Molecular Microbiology · doi:10.1111/j.1365-2958.1988.tb00029.x · Cited by 258
Crosa, J. H. (1997) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.61.3.319-336.1997 · Cited by 256
Microbial iron transport via a siderophore shuttle: A membrane ion transport paradigm
Stintzi, A., Barnes, C., Xu, J., & Raymond, K. N. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.200318797 · Cited by 254
Bearden, S. W., & Perry, R. D. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01360.x · Cited by 254
Boyd, J., Oza, M. N., & Murphy, J. R. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.15.5968 · Cited by 253
Lactobacillus plantarum, an organism not requiring iron
Archibald, F. (1983) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1983.tb00504.x · Cited by 251
Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon
Baichoo, N., Wang, T., Ye, R., & Helmann, J. D. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03113.x · Cited by 250
Abdul-Tehrani, H., Hudson, A. J., Chang, Y.-S., Timms, A. R., Hawkins, C., Williams, J. M., Harrison, P. M., Guest, J. R., & Andrews, S. C. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.5.1415-1428.1999 · Cited by 246
Self-citationIron piracy: acquisition of transferrin‐bound iron by bacterial pathogens
Cornelissen, C. N., & Sparling, P. F. (1994) · Molecular Microbiology · doi:10.1111/j.1365-2958.1994.tb01320.x · Cited by 244
Emerging strategies in microbial haem capture
Genco, C. A., & Dixon, D. W. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02231.x · Cited by 242
Hantke, K. (1987) · Molecular and General Genetics MGG · doi:10.1007/bf00337769 · Cited by 241
Janakiraman, A., & Slauch, J. M. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01783.x · Cited by 233
TonB protein and energy transduction between membranes
Postle, K. (1993) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf00770246 · Cited by 217
Bozzi, M., Mignogna, G., Stefanini, S., Barra, D., Longhi, C., Valenti, P., & Chiancone, E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.6.3259 · Cited by 216
The reconstitution of clostridial ferredoxin
Malkin, R., & Rabinowitz, J. C. (1966) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(66)90561-4 · Cited by 213
Genes Essential to Iron Transport in the Cyanobacterium Synechocystis sp. Strain PCC 6803
Katoh, H., Hagino, N., Grossman, A. R., & Ogawa, T. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.9.2779-2784.2001 · Cited by 204
Protonmotive force, ExbB and ligand‐bound FepA drive conformational changes in TonB
Larsen, R. A., Thomas, M. G., & Postle, K. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01317.x · Cited by 197
Delany, I., Spohn, G., Rappuoli, R., & Scarlato, V. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02696.x · Cited by 192
Anderson, J. E., Sparling, P. F., & Cornelissen, C. N. (1994) · Journal of Bacteriology · doi:10.1128/jb.176.11.3162-3170.1994 · Cited by 188
de Lorenzo, V., Herrero, M., Giovannini, F., & Neilands, J. B. (1988) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1988.tb14032.x · Cited by 186
Zhou, D., Hardt, W.-D., & Galán, J. E. (1999) · Infection and Immunity · doi:10.1128/iai.67.4.1974-1981.1999 · Cited by 182
ColV plasmid-specific aerobactin synthesis by invasive strains of Escherichia coli
Warner, P. J., WILLIAMS, P. H., Bindereif, A., & Neilands, J. B. (1981) · Infection and Immunity · doi:10.1128/iai.33.2.540-545.1981 · Cited by 181
Furrer, J. L., Sanders, D. N., Hook-Barnard, I. G., & McIntosh, M. A. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02885.x · Cited by 180
Bruns, C. M., Nowalk, A. J., Arvai, A. S., McTigue, M. A., Vaughan, K. G., Mietzner, T. A., & McRee, D. E. (1997) · Nature Structural & Molecular Biology · doi:10.1038/nsb1197-919 · Cited by 177
SitABCD Is the Alkaline Mn2+Transporter of Salmonella enterica Serovar Typhimurium
Kehres, D. G., Janakiraman, A., Slauch, J. M., & Maguire, M. E. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.12.3159-3166.2002 · Cited by 177
The Lactobacillus Anomaly: Total Iron Abstinence
Weinberg, E. D. (1997) · Perspectives in Biology and Medicine · doi:10.1353/pbm.1997.0072 · Cited by 176
Contribution of TonB- and Feo-mediated iron uptake to growth of Salmonella typhimurium in the mouse
Tsolis, R. M., Bäumler, A. J., Heffron, F., & Stojiljkovic, I. (1996) · Infection and Immunity · doi:10.1128/iai.64.11.4549-4556.1996 · Cited by 174
Dubrac, S., & Touati, D. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.13.3802-3808.2000 · Cited by 174
Metal ion regulation of gene expression
de Lorenzo, V., Giovannini, F., Herrero, M., & Neilands, J. B. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90113-1 · Cited by 173
Escolar, L., Pérez-Martı́n, J., & de Lorenzo, V. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2119 · Cited by 173
Marlovits, T. C., Haase, W., Herrmann, C., Aller, S. G., & Unger, V. M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.242338299 · Cited by 171
A whole genome view of prokaryotic haem biosynthesis
Panek, H., & O’Brian, M. R. (2002) · Microbiology · doi:10.1099/00221287-148-8-2273 · Cited by 168
Higgs, P. I., Larsen, R. A., & Postle, K. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02880.x · Cited by 167
WILLIAMS, P. H., & Warner, P. J. (1980) · Infection and Immunity · doi:10.1128/iai.29.2.411-416.1980 · Cited by 167
Cadieux, N., & Kadner, R. J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.19.10673 · Cited by 162
Patzer, S. I., & Hantke, K. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.16.4806-4813.2001 · Cited by 160
Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA
Ferguson, A. D., Coulton, J. W., Diederichs, K., Welte, W., Braun, V., & Fiedler, H. (2000) · Protein Science · doi:10.1110/ps.9.5.956 · Cited by 160
Bacillus subtilis aconitase is an RNA-binding protein
Amaro, C. A., & Sonenshein, A. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10412 · Cited by 159
Qi, Z., Hamza, I., & O’Brian, M. R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.23.13056 · Cited by 158
Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases
Tang, Y., & Guest, J. R. (1999) · Microbiology · doi:10.1099/00221287-145-11-3069 · Cited by 158
Park, S. J., & Gunsalus, R. P. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.21.6255-6262.1995 · Cited by 157
Patzer, S. I., & Hantke, K. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.10.3307-3309.1999 · Cited by 155
Letain, T. E., & Postle, K. (1997) · Molecular Microbiology · doi:10.1046/j.1365-2958.1997.3331703.x · Cited by 155
Legrain, M., Mazarin, V., Irwin, S. W., Bouchon, B., Quentin-Millet, M. J., Jacobs, E. J., & Schryvers, A. B. (1993) · Gene · doi:10.1016/0378-1119(93)90348-7 · Cited by 155
Structural dynamics and functional domains of the Fur protein
Coy, M., & Neilands, J. B. (1991) · Biochemistry · doi:10.1021/bi00247a016 · Cited by 154
Clarke, T. E., Braun, V., Winkelmann, G., Tari, L. W., & Vogel, H. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109385200 · Cited by 154
Foster, J. W., & Hall, H. K. (1992) · Journal of Bacteriology · doi:10.1128/jb.174.13.4317-4323.1992 · Cited by 154
Woodmansee, A. N., & Imlay, J. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203977200 · Cited by 152
Two genetically-distinct and differentially-regulated aconitases (AcnA and AcnB) in Escherichia coli
Gruer, M. J., & Guest, J. R. (1994) · Microbiology · doi:10.1099/00221287-140-10-2531 · Cited by 149
The ferric uptake regulation (Fur) repressor is a zinc metalloprotein
Althaus, E. W., Outten, C. E., Olson, K. E., Cao, H., & O'Halloran, T. V. (1999) · Biochemistry · doi:10.1021/bi982788s · Cited by 147
Ma, J.-F., Ochsner, U. A., Klotz, M. G., Nanayakkara, V. K., Howell, M. L., Johnson, Z., Posey, J. E., Vasil, M. L., Monaco, J. J., & Hassett, D. J. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.12.3730-3742.1999 · Cited by 146
Angerer, A., Gaisser, S., & Braun, V. (1990) · Journal of Bacteriology · doi:10.1128/jb.172.2.572-578.1990 · Cited by 145
Interactions in the TonB-Dependent Energy Transduction Complex: ExbB and ExbD Form Homomultimers
Higgs, P. I., Myers, P. S., & Postle, K. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.22.6031-6038.1998 · Cited by 143
Reynolds, P. R., Mottur, G. P., & Bradbeer, C. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85667-3 · Cited by 141
Touati, D. (1988) · Journal of Bacteriology · doi:10.1128/jb.170.6.2511-2520.1988 · Cited by 138
The structure of the ferric siderophore binding protein FhuD complexed with gallichrome.
Vogel, H. J., Tari, L. W., Clarke, T. E., Ku, S.-Y., & Dougan, D. R. (2000) · Nature Structural Biology · doi:10.1038/74048 · Cited by 134
Park, S., Tseng, C., & Gunsalus, R. P. (1995) · Molecular Microbiology · doi:10.1111/j.1365-2958.1995.tb02261.x · Cited by 134
Crystal Structure of the Dimeric C-terminal Domain of TonB Reveals a Novel Fold
Chang, C., Mooser, A., Plückthun, A., & Wlodawer, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102778200 · Cited by 133
Surface signaling: novel transcription initiation mechanism starting from the cell surface
Braun, V. (1997) · Archives of Microbiology · doi:10.1007/s002030050451 · Cited by 127
Haem utilization in Vibrio cholerae involves multiple TonB‐dependent haem receptors
Mey, A. R., & Payne, S. M. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02683.x · Cited by 123
X-ray Absorption Spectroscopy of a New Zinc Site in the Fur Protein fromEscherichia coli
Jacquamet, L., Aberdam, D., Adrait, A., Hazemann, J., Latour, J., & Michaud‐Soret, I. (1998) · Biochemistry · doi:10.1021/bi9721344 · Cited by 119
Dussurget, O., Rodriguez, M., & Smith, I. (1996) · Molecular Microbiology · doi:10.1046/j.1365-2958.1996.1461511.x · Cited by 118
Ferric iron reduction by Cryptococcus neoformans
Nyhus, K. J., Wilborn, A. T., & Jacobson, E. S. (1997) · Infection and Immunity · doi:10.1128/iai.65.2.434-438.1997 · Cited by 117
Pohl, E., Holmes, R. K., & Hol, W. G. J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2339 · Cited by 117
Qi, Z., & O’Brian, M. R. (2002) · Molecular Cell · doi:10.1016/s1097-2765(01)00431-2 · Cited by 114
Specificity of the lactoferrin and transferrin receptors in Neisseria gonorrhoeae
Lee, B. C., & Schryvers, A. B. (1988) · Molecular Microbiology · doi:10.1111/j.1365-2958.1988.tb00095.x · Cited by 113
The fbpABC locus of Neisseria gonorrhoeae functions in the periplasm-to-cytosol transport of iron
Adhikari, P. A., Berish, S. A., Nowalk, A. J., Veraldi, K. L., Morse, S. A., & Mietzner, T. A. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.7.2145-2149.1996 · Cited by 112
Transport of Vitamin B12 in Escherichia coli
White, J. C., Girolamo, P. M. D., Fu, M. L., Preston, Y. A., & Bradbeer, C. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43828-3 · Cited by 112
Stojiljković, I., Cobeljić, M., & Hantke, K. (1993) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1993.tb06082.x · Cited by 111
Ferric reductases or flavin reductases?
Fontecave, M., Cov�s, J., & Pierre, J. (1994) · BioMetals · doi:10.1007/bf00205187 · Cited by 111
SirR, a Novel Iron-Dependent Repressor in Staphylococcus epidermidis
Hill, P. J., Cockayne, A., Landers, P., Morrissey, J. A., Sims, C. M., & Williams, P. M. (1998) · Infection and Immunity · doi:10.1128/iai.66.9.4123-4129.1998 · Cited by 110
Regulation of sod genes in Escherichia coli: relevance to superoxide dismutase function
Fee, J. A. (1991) · Molecular Microbiology · doi:10.1111/j.1365-2958.1991.tb01968.x · Cited by 109
Ghassemian, M., & Straus, N. A. (1996) · Microbiology · doi:10.1099/13500872-142-6-1469 · Cited by 105
Angerer, A., Enz, S., Ochs, M. M., & Braun, V. (1995) · Molecular Microbiology · doi:10.1111/j.1365-2958.1995.mmi_18010163.x · Cited by 105
Rohrbach, M. R., Braun, V., & Köster, W. L. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.24.7186-7193.1995 · Cited by 104
Blanton, K. J., Biswas, G. D., Tsai, J., Adams, J., Dyer, D. W., Davis, S. M., Koch, G. G., Sen, P. K., & Sparling, P. F. (1990) · Journal of Bacteriology · doi:10.1128/jb.172.9.5225-5235.1990 · Cited by 102
Microbial iron transport: iron acquisition by pathogenic microorganisms.
Byers, B. R., & Arceneaux, J. E. L. (1998) · PubMed · Cited by 101
Larsen, R. A., Thomas, M. G., Wood, G. E., & Postle, K. (1994) · Molecular Microbiology · doi:10.1111/j.1365-2958.1994.tb00457.x · Cited by 98
Functional domains of theEscherichia coli ferric uptake regulator protein (Fur)
Stojiljković, I., & Hantke, K. (1995) · Molecular and General Genetics MGG · doi:10.1007/bf00705650 · Cited by 98
Redox properties and Moessbauer spectroscopy of Azotobacter vinelandii bacterioferritin
Watt, G. D., Frankel, R. B., Papaefthymiou, G. C., Spartalian, K., & Stiefel, E. I. (1986) · Biochemistry · doi:10.1021/bi00363a023 · Cited by 97
Helicobacter pylori ribBA -Mediated Riboflavin Production Is Involved in Iron Acquisition
Worst, D. J., Gerrits, M. M., Vandenbroucke‐Grauls, C. M. J. E., & Kusters, J. G. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.6.1473-1479.1998 · Cited by 97
Vassinova, N., & Dp, K. (2000) · Microbiology · doi:10.1099/00221287-146-12-3171 · Cited by 95
Andrews, S. C., Brun, N. E. L., Barynin, V. V., THOMSON, A. J., Moore, G. R., Guest, J. R., & Harrison, P. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.40.23268 · Cited by 92
Self-citationWilson, T. J., Bertrand, N., Tang, J. ‐., Feng, J., Pan, M.-Y., Barber, C. E., Dow, J. M., & Daniels, M. J. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00852.x · Cited by 92
Braun, M., Killmann, H., & Braun, V. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01546.x · Cited by 90
Ding, X., Zeng, H., Schiering, N., Ringe, D., & Murphy, J. R. (1996) · Nature Structural & Molecular Biology · doi:10.1038/nsb0496-382 · Cited by 86
Tsai, J., Dyer, D. W., & Sparling, P. F. (1988) · Infection and Immunity · doi:10.1128/iai.56.12.3132-3138.1988 · Cited by 85
Wai, S. N., Nakayama, K., Umene, K., Moriya, T., & Amako, K. (1996) · Molecular Microbiology · doi:10.1111/j.1365-2958.1996.tb02633.x · Cited by 84
Cam, É. L., Frechon, D., Barray, M., Fourcade, A., & Delain, E. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.11816 · Cited by 82
An iron-dependent modification of several transfer RNA species in Escherichia coli
Rosenberg, A. H., & Gefter, M. L. (1969) · Journal of Molecular Biology · doi:10.1016/0022-2836(69)90197-1 · Cited by 76
Bereswill, S., Waidner, U., Odenbreit, S., Lichte, F., Fassbinder, F., Bode, G., & Kist, M. (1998) · Microbiology · doi:10.1099/00221287-144-9-2505 · Cited by 76
Winkelmann, G. (2001) · Wiley eBooks · doi:10.1002/3527600728 · Cited by 75
SPECTROCHEMICAL ANALYSIS OF INORGANIC ELEMENTS IN BACTERIA
Rouf, M. A. (1964) · Journal of Bacteriology · doi:10.1128/jb.88.6.1545-1549.1964 · Cited by 71
Garg, R. P., Vargo, C. J., Cui, X., & Kurtz, D. M. J. (1996) · Biochemistry · doi:10.1021/bi9600862 · Cited by 70
The Iron-Transport Systems of Escherichia coli
Braun, V. (1985) · Springer eBooks · doi:10.1007/978-1-4684-4601-2_18 · Cited by 68
Reduction of iron by extracellular iron reductases: implications for microbial iron acquisition
Cowart, R. E. (2002) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(02)00012-7 · Cited by 68
Usher, K. C., Özkan, E., Gardner, K. H., & Deisenhofer, J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.181353398 · Cited by 67
Pohl, E., Holmes, R. K., & Hol, W. G. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.35.22420 · Cited by 66
Dubrac, S., & Touati, D. (2002) · Microbiology · doi:10.1099/00221287-148-1-147 · Cited by 66
Hantke, K. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.19.6201-6204.1997 · Cited by 66
Fur-independent regulation of iron metabolism by Irr in Bradyrhizobium japonicum
Hamza, I., Qi, Z., King, N. D., & O’Brian, M. R. (2000) · Microbiology · doi:10.1099/00221287-146-3-669 · Cited by 65
Quail, M. A., Jordan, P., Jm, G., Butt, J. N., Lutz, M., THOMSON, A. J., Andrews, S. C., & Guest, J. R. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1856 · Cited by 64
Self-citationExchangeability of N Termini in the Ligand-gated Porins ofEscherichia coli
Scott, D. C., Cao, Z., Qi, Z., Bauler, M. N., Igo, J. D., Newton, S. M. C., & Klebba, P. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011282200 · Cited by 64
Structure of a Monoclinic Crystal Form of Cytochrome b1 (Bacterioferritin) from E. coli
Dautant, A., Meyer, J.-B., Yariv, J., PRECIGOUX, G., Sweet, R. M., Kalb, A. J., & Frolow, F. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444997006811 · Cited by 64
Iron supply to Escherichia coli by synthetic analogs of enterochelin
Heidinger, S., Braun, V., Pecoraro, V. L., & Raymond, K. N. (1983) · Journal of Bacteriology · doi:10.1128/jb.153.1.109-115.1983 · Cited by 59
BIOLOGICAL CYCLING OF IRON IN THE OCEAN
Price, N. M., & Morel, F. M. M. (1998) · Metal ions in biological systems · Cited by 59
Escolar, L., Pérez‐Martín, J., & de Lorenzo, V. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002839200 · Cited by 56
Stiefel, A., Mahren, S., Ochs, M. M., Schindler, P. T., Enz, S., & Braun, V. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.1.162-170.2001 · Cited by 56
Spiro, T. G. (1982) · Wiley eBooks · Cited by 55
Iron-regulated outer membrane protein of Bacteroides fragilis involved in heme uptake
Otto, B. R., Sparrius, M., Vught, A. M. J. J. V.-V., & MacLaren, D. M. (1990) · Infection and Immunity · doi:10.1128/iai.58.12.3954-3958.1990 · Cited by 54
Tseng, C. (2006) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1997.tb12754.x · Cited by 54
Fur–DNA Interactions at the Bidirectional fepDGC-entS Promoter Region in Escherichia coli
Lavrrar, J. L., Christoffersen, C. A., & McIntosh, M. A. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00849-5 · Cited by 53
Venuti, M. C., Rastetter, W. H., & Neilands, J. B. (1979) · Journal of Medicinal Chemistry · doi:10.1021/jm00188a002 · Cited by 53
Mademidis, A., Killmann, H., Kraas, W., Flechsler, I., Jung, G., & Braun, V. (1997) · Molecular Microbiology · doi:10.1046/j.1365-2958.1997.6592008.x · Cited by 51
Pettis, G. S., & Cohen, S. N. (1996) · Molecular Microbiology · doi:10.1046/j.1365-2958.1996.493986.x · Cited by 51
Schmitt, M. P., Talley, B. G., & Holmes, R. K. (1997) · Infection and Immunity · doi:10.1128/iai.65.12.5364-5367.1997 · Cited by 50
Maringanti, S., & Imlay, J. A. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.12.3792-3802.1999 · Cited by 49
Watnick, P. I., Eto, T., Takahashi, H., & Calderwood, S. B. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.1.243-247.1997 · Cited by 45
FhuA Barrel-Cork Hybrids Are Active Transporters and Receptors
Killmann, H., Braun, M., Herrmann, C., & Braun, V. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.11.3476-3487.2001 · Cited by 45
Lewin, A. C., Doughty, P., Flegg, L. M., Moore, G. R., & Spiro, S. (2002) · Microbiology · doi:10.1099/00221287-148-8-2449 · Cited by 43
Romão, C. V., Louro, R. O., Timkovich, R., Lübben, M., Liu, M., LeGall, J., Xavier, A. V., & Teixeira, M. S. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01939-6 · Cited by 43
Hantke, K. (2002) · PubMed · Cited by 38
Bovy, A. G., de Vrieze, G., Lugones, L. G., van Horssen, P., van den Berg, C., Borrias, M., & Weisbeek, P. J. (1993) · Molecular Microbiology · doi:10.1111/j.1365-2958.1993.tb01134.x · Cited by 37
Razquín, P., Schmitz, S., Fillat, M. F., Peleato, M. L., & Böhme, H. (1994) · Journal of Bacteriology · doi:10.1128/jb.176.23.7409-7411.1994 · Cited by 33
Is the fur gene of Rhizobium leguminosarum essential?
Luca, N. G. D., Wexler, M., Pereira, M. J., Yeoman, K. H., & Johnston, A. W. B. (1998) · FEMS Microbiology Letters · doi:10.1016/s0378-1097(98)00454-6 · Cited by 31
Structural and stereochemical aspects of iron transport in fungi
Winkelmann, G. (1990) · Biotechnology Advances · doi:10.1016/0734-9750(90)90013-2 · Cited by 30
Smith, A., Hooper, N. I., Shipulina, N., & Morgan, W. T. (1996) · Journal of Protein Chemistry · doi:10.1007/bf01908539 · Cited by 30
Feedback regulation of iron-sulfur cluster biosynthesis
Jeverson Frazzon, B., & Dean, D. R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.011579098 · Cited by 29
Wooldridge, K. G., Morrissey, J. A., & Williams, P. H. (1992) · Journal of General Microbiology · doi:10.1099/00221287-138-3-597 · Cited by 27
da Costa, P. N., Romão, C. V., LeGall, J., Xavier, A. V., Melo, E. C. C., Teixeira, M. S., & Saraiva, L. M. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02509.x · Cited by 24
Denoël, P., Crawford, R. M., Zygmunt, M. S., Tibor, A., Weynants, V. E., Godfroid, F., Hoover, D. L., & Letesson, J. (1997) · Infection and Immunity · doi:10.1128/iai.65.10.4337-4340.1997 · Cited by 24
Differential fiu–lacZ fusion regulation linked to Escherichia coli colony development
Newman, D. L., & Shapiro, J. A. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01423.x · Cited by 23
Iron-related modification of bacterial transfer RNA
McLennan, B. D., Buck, M., Humphreys, J., & Griffiths, E. (1981) · Nucleic Acids Research · doi:10.1093/nar/9.11.2629 · Cited by 22
Iron Chelation and Siderophores
Drechsel, H., & Winkelmann, G. (2022) · CRC Press eBooks · doi:10.1201/9781003211129-1 · Cited by 13
Human Nutrition and its Discontents: A Personal View
Schneider, H. A. (1996) · Perspectives in biology and medicine · doi:10.1353/pbm.1996.0050 · Cited by 5
SirR, a Novel Iron-Dependent Repressor inStaphylococcus epidermidis
Hill, P. J., Cockayne, A., Landers, P., Morrissey, J. A., Sims, C. M., & Williams, P. M. (1998) · Infection and Immunity · doi:10.1128/.66.9.4123-4129.1998 · Cited by 3
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
Mendes, R., Garbeva, P., & Raaijmakers, J. M. (2013) · FEMS Microbiology Reviews · doi:10.1111/1574-6976.12028 · Cited by 2,945
Mineral–Organic Associations: Formation, Properties, and Relevance in Soil Environments
Kleber, M., Eusterhues, K., Keiluweit, M., Mikutta, C., Mikutta, R., & Nico, P. (2014) · Advances in agronomy · doi:10.1016/bs.agron.2014.10.005 · Cited by 1,683
Plant growth-promoting rhizobacteria (PGPR): their potential as antagonists and biocontrol agents
Beneduzi, A., Ambrosini, A., & Passaglia, L. M. P. (2012) · Genetics and Molecular Biology · doi:10.1590/s1415-47572012000600020 · Cited by 1,532
Iron in infection and immunity
Cassat, J. E., & Skaar, E. P. (2013) · Cell Host & Microbe · doi:10.1016/j.chom.2013.04.010 · Cited by 1,214
Ganoderma lucidum reduces obesity in mice by modulating the composition of the gut microbiota
Chang, C., Lin, C.-S., Lu, C., Martel, J., Ko, Y., Ojcius, D. M., Tseng, S., Wu, T.-R., Chen, Y. M., Young, J. D., et al. (2015) · Nature Communications · doi:10.1038/ncomms8489 · Cited by 1,254
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