Meddling with metal sensors: Fur-Family proteins as signaling hubs

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Colman (2022) · doi:10.1073/pnas · Cited by 4,370 · see citing works

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Deutscher, J., Francke, C., & Postma, P. W. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00024-06 · Cited by 1,411 · see citing works

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 · see citing works

Metal homeostasis and resistance in bacteria

Chandrangsu, P., Rensing, C., & Helmann, J. D. (2017) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2017.15 · Cited by 812 · see citing works

A Comprehensive, CRISPR-based Functional Analysis of Essential Genes in Bacteria

Peters, J. M., Colavin, A., Shi, H., Czarny, T. L., Larson, M. H., Wong, S. S., Hawkins, J. S., Lu, C. H. S., Koo, B., Marta, E., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.003 · Cited by 716 · see citing works

Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operator of an iron transport operon in Escherichia coli

Bagg, A., & Neilands, J. B. (1987) · Biochemistry · doi:10.1021/bi00391a039 · Cited by 593 · see citing works

The PerR transcription factor senses H2O2 by metal-catalysed histidine oxidation

Lee, J.-W., & Helmann, J. D. (2006) · Nature · doi:10.1038/nature04537 · Cited by 547 · see citing works

ideR , an Essential Gene in Mycobacterium tuberculosis : Role of IdeR in Iron-Dependent Gene Expression, Iron Metabolism, and Oxidative Stress Response

Rodríguez, G. M., Voskuil, M. I., Gold, B., Schoolnik, G. K., & Smith, I. (2002) · Infection and Immunity · doi:10.1128/iai.70.7.3371-3381.2002 · Cited by 491 · see citing works

Functional specialization within the Fur family of metalloregulators

Lee, J.-W., & Helmann, J. D. (2007) · BioMetals · doi:10.1007/s10534-006-9070-7 · Cited by 432 · see citing works

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 403 · see citing works

ESX secretion systems: mycobacterial evolution to counter host immunity

Gröschel, M. I., Sayes, F., Simeone, R., Majlessi, L., & Brosch, R. (2016) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2016.131 · Cited by 382 · see citing works

The FUR (ferric uptake regulator) superfamily: Diversity and versatility of key transcriptional regulators

Fillat, M. F. (2014) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.01.029 · Cited by 329 · see citing works

Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition

Siegrist, M. S., Unnikrishnan, M., McConnell, M. J., Borowsky, M. L., Cheng, T., Siddiqi, N., Fortune, S. M., Moody, D. B., & Rubin, E. J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900589106 · Cited by 329 · see citing works

Iron homeostasis and management of oxidative stress response in bacteria

Cornélis, P., Wei, Q., Andrews, S. C., & Vinckx, T. (2011) · Metallomics · doi:10.1039/c1mt00022e · Cited by 321 · see citing works

Deciphering Fur transcriptional regulatory network highlights its complex role beyond iron metabolism in Escherichia coli

Seo, S. W., Kim, D., Latif, H., O’Brien, E. J., Szubin, R., & Palsson, B. Ø. (2014) · Nature Communications · doi:10.1038/ncomms5910 · Cited by 318 · see citing works

Advances in Microbial Physiology

(2019) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/s0065-2911(19)30013-x · Cited by 314 · see citing works

Type II Toxin-Antitoxin Systems: Evolution and Revolutions

Fraikin, N., Goormaghtigh, F., & Melderen, L. V. (2020) · Journal of Bacteriology · doi:10.1128/jb.00763-19 · Cited by 289 · see citing works

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 2× · see citing works

The Mismetallation of Enzymes during Oxidative Stress

Imlay, J. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.588814 · Cited by 270 · see citing works

Global Analysis of theMycobacterium tuberculosisZur (FurB) Regulon

Maciag, A. E., Dainese, E., Rodríguez, G. M., Milano, A., Provvedi, R., Pasca, M. R., Smith, I., Palù, G., Riccardi, G., & Manganelli, R. (2006) · Journal of Bacteriology · doi:10.1128/jb.01190-06 · Cited by 257 · see citing works

Global analysis of the <i>Bacillus subtilis</i> 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 · see citing works

Selection procedure for deregulated iron transport mutants (fur) in Escherichia coli K 12: fur not only affects iron metabolism

Hantke, K. (1987) · Molecular and General Genetics MGG · doi:10.1007/bf00337769 · Cited by 242 · see citing works

The <i>Bacillus subtilis</i> iron-sparing response is mediated by a Fur-regulated small RNA and three small, basic proteins

Gaballa, A., Antelmann, H., Aguilar, C., Khakh, S. K., Song, K.-B., Smaldone, G. T., & Helmann, J. D. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711752105 · Cited by 232 · see citing works

Characterization of a<i>Mycobacterium tuberculosis</i>ESX-3 Conditional Mutant: Essentiality and Rescue by Iron and Zinc

Serafini, A., Boldrin, F., Palù, G., & Manganelli, R. (2009) · Journal of Bacteriology · doi:10.1128/jb.00756-09 · Cited by 198 · see citing works

The Fur repressor controls transcription of iron‐activated and ‐repressed genes in Helicobacter pylori

Delany, I., Spohn, G., Rappuoli, R., & Scarlato, V. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02696.x · Cited by 192 · see citing works

The Opportunistic Human Pathogen Acinetobacter baumannii Senses and Responds to Light

Mussi, M. A., Gaddy, J. A., Cabruja, M., Arivett, B. A., Viale, A. M., Rasia, R. M., & Actis, L. A. (2010) · Journal of Bacteriology · doi:10.1128/jb.00917-10 · Cited by 184 · see citing works

Fur functions as an activator and as a repressor of putative virulence genes in Neisseria meningitidis

Delany, I., Rappuoli, R., & Scarlato, V. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04030.x · Cited by 181 · see citing works

Virulence Factors of Uropathogenic E. coli and Their Interaction with the Host

Lüthje, P., & Brauner, A. (2014) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2014.08.006 · Cited by 174 · see citing works

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 · see citing works

Direct inhibition by nitric oxide of the transcriptional ferric uptake regulation protein via nitrosylation of the iron

D’Autréaux, B., Touati, D., Bersch, B., Latour, J., & Michaud‐Soret, I. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252591299 · Cited by 171 · see citing works

Regulatory roles of the bacterial nitrogen-related phosphotransferase system

Pflüger‐Grau, K., & Görke, B. (2010) · Trends in Microbiology · doi:10.1016/j.tim.2010.02.003 · Cited by 158 · see citing works

Lateral Flagellar Gene System of Vibrio parahaemolyticus

Stewart, B. J., & McCarter, L. L. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.15.4508-4518.2003 · Cited by 155 · see citing works

Specificity of Metal Sensing: Iron and Manganese Homeostasis in Bacillus subtilis

Helmann, J. D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.587071 · Cited by 153 · see citing works

Peroxide Stress Elicits Adaptive Changes in Bacterial Metal Ion Homeostasis

Faulkner, M. J., & Helmann, J. D. (2011) · Antioxidants &amp; Redox Signaling · doi:10.1089/ars.2010.3682 · Cited by 151 · see citing works

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 · see citing works

Response ofBacillus subtilisto Nitric Oxide and the Nitrosating Agent Sodium Nitroprusside

Moore, C. M., NAKANO, M. M., Wang, T., Ye, R. W., & Helmann, J. D. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.14.4655-4664.2004 · Cited by 147 · see citing works

Bacterial sensors define intracellular free energies for correct enzyme metalation

Osman, D., Martini, M. A., Foster, A. W., Chen, J., Scott, A. J. P., Morton, R. J., Steed, J. W., Lurie-Luke, E., Huggins, T. G., Lawrence, A. D., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-018-0211-4 · Cited by 147 · see citing works

How Microbes Defend Themselves From Incoming Hydrogen Peroxide

Sen, A., & Imlay, J. A. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.667343 · Cited by 146 · see citing works

Bacterial iron detoxification at the molecular level

Bradley, J. M., Svistunenko, D. A., Wilson, M. T., Hemmings, A. M., Moore, G. R., & Le Brun, N. E. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.007746 · Cited by 140 · see citing works

Structure and regulon of <i>Campylobacter jejuni</i> ferric uptake regulator Fur define apo-Fur regulation

Butcher, J., Sarvan, S., Brunzelle, J. S., Couture, J.-F., & Stintzi, A. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1118321109 · Cited by 137 · see citing works

Bacterial lateral flagella: an inducible flagella system

Merino, S., Shaw, J. G., & Tomás, J. M. (2006) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2006.00403.x · Cited by 136 · see citing works

Biochemical Characterization of the Structural Zn2+ Site in the Bacillus subtilis Peroxide Sensor PerR

Lee, J., & Helmann, J. D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603968200 · Cited by 126 · see citing works

Bacterial Iron Homeostasis Regulation by sRNAs

Chareyre, S., & Mandin, P. (2018) · Microbiology Spectrum · doi:10.1128/microbiolspec.rwr-0010-2017 · Cited by 125 · see citing works

Structural and functional characterization of 2-oxo-histidine in oxidized PerR protein

Traoré, D. A. K., Ghazouani, A. E., Jacquamet, L., Borel, F., Ferrer, J.-L., Lascoux, D., Ravanat, J., Jaquinod, M., Blondin, G., Caux‐Thang, C., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.133 · Cited by 125 · see citing works

Recognition of DNA by Three Ferric Uptake Regulator (Fur) Homologs inBacillus subtilis

Fuangthong, M., & Helmann, J. D. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.21.6348-6357.2003 · Cited by 117 · see citing works

Mechanistic insights into metal ion activation and operator recognition by the ferric uptake regulator

Deng, Z., Wang, Q., Liu, Z., Zhang, M., Machado, A. C. D., Chiu, T.-P., Feng, C., Zhang, Q., Yu, L., Qi, L., et al. (2015) · Nature Communications · doi:10.1038/ncomms8642 · Cited by 117 · cited 2× · see citing works

Living without Fur: the subtlety and complexity of iron-responsive gene regulation in the symbiotic bacterium Rhizobium and other α-proteobacteria

Johnston, A. W. B., Todd, J. D., Curson, A. R. J., Lei, S., Nikolaidou-Katsaridou, N., Gelfand, M. S., & Rodionov, D. A. (2007) · BioMetals · doi:10.1007/s10534-007-9085-8 · Cited by 115 · see citing works

Structural and Mechanistic Basis of Zinc Regulation Across the E. coli Zur Regulon

Gilston, B. A., Wang, S., Marcus, M. D., Canalizo-Hernández, M. A., Swindell, E. P., Xue, Y., Mondragón, A., & O’Halloran, T. V. (2014) · PLoS Biology · doi:10.1371/journal.pbio.1001987 · Cited by 115 · see citing works

Interaction between the Bacterial Iron Response Regulator and Ferrochelatase Mediates Genetic Control of Heme Biosynthesis

Qi, Z., & O’Brian, M. R. (2002) · Molecular Cell · doi:10.1016/s1097-2765(01)00431-2 · Cited by 114 · see citing works

Bacterial zinc uptake regulator proteins and their regulons

Mikhaylina, A., Ksibe, A. Z., Scanlan, D. J., & Blindauer, C. A. (2018) · Biochemical Society Transactions · doi:10.1042/bst20170228 · Cited by 114 · see citing works

Iron-responsive bacterial small RNAs: variations on a theme

Oglesby-Sherrouse, A. G., & Murphy, E. R. (2013) · Metallomics · doi:10.1039/c3mt20224k · Cited by 112 · see citing works

The Fur-like protein Mur of Rhizobium leguminosarum is a Mn2+-responsive transcriptional regulator

Díaz-Mireles, E., Wexler, M., Sawers, R. G., Bellini, D., Todd, J. D., & Johnston, A. W. B. (2004) · Microbiology · doi:10.1099/mic.0.26961-0 · Cited by 111 · see citing works

Sequential induction of Fur-regulated genes in response to iron limitation in <i>Bacillus subtilis</i>

Pi, H., & Helmann, J. D. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1713008114 · Cited by 109 · see citing works

Essential genes in Bacillus subtilis : a re-evaluation after ten years

Commichau, F. M., Pietack, N., & Stülke, J. (2013) · Molecular BioSystems · doi:10.1039/c3mb25595f · Cited by 108 · see citing works

In Vitro Analysis of Protein-Operator Interactions of the NikR and Fur Metal-Responsive Regulators of Coregulated Genes inHelicobacter pylori

Delany, I., Ieva, R., Soragni, A., Hilleringmann, M., Rappuoli, R., & Scarlato, V. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.22.7703-7715.2005 · Cited by 98 · see citing works

O 2 availability impacts iron homeostasis in Escherichia coli

Beauchene, N. A., Mettert, E. L., Moore, L. J., Keleş, S., Willey, E. R., & Kiley, P. J. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707189114 · Cited by 94 · see citing works

Zinc-dependent regulation of zinc import and export genes by Zur

Choi, S.-H., Lee, K.-L., Shin, J.-H., Cho, Y.-B., Cha, S., & Roe, J. (2017) · Nature Communications · doi:10.1038/ncomms15812 · Cited by 89 · see citing works

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 · see citing works

Expression of Multidrug Resistance Efflux Pump Gene norA Is Iron Responsive in Staphylococcus aureus

Deng, X., Sun, F., Ji, Q., Liang, H., Missiakas, D. M., Lan, L., & He, C. (2012) · Journal of Bacteriology · doi:10.1128/jb.06582-11 · Cited by 86 · see citing works

Redox Sensing by Fe ²⁺ in Bacterial Fur Family Metalloregulators

Pinochet-Barros, A., & Helmann, J. D. (2018) · Antioxidants &amp; Redox Signaling · doi:10.1089/ars.2017.7359 · Cited by 85 · see citing works

Three New Regulators of Swarming in Vibrio parahaemolyticus

Jaques, S., & McCarter, L. L. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.7.2625-2635.2006 · Cited by 84 · see citing works

Observation of binding and polymerization of Fur repressor onto operator-containing DNA with electron and atomic force microscopes.

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 · see citing works

Derepression of the Bacillus subtilis PerR Peroxide Stress Response Leads to Iron Deficiency

Faulkner, M. J., Ma, Z., Fuangthong, M., & Helmann, J. D. (2012) · Journal of Bacteriology · doi:10.1128/jb.06566-11 · Cited by 76 · see citing works

Ferric uptake regulator (Fur) reversibly binds a [2Fe-2S] cluster to sense intracellular iron homeostasis in Escherichia coli

Fontenot, C. R., Tasnim, H., Valdes, K. A., Popescu, C. V., & Ding, H. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014814 · Cited by 74 · see citing works

Direct substitution and assisted dissociation pathways for turning off transcription by a MerR-family metalloregulator

Joshi, C. P., Panda, D., Martell, D. J., Andoy, N. M., Chen, T., Gaballa, A., Helmann, J. D., & Chen, P. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208508109 · Cited by 74 · see citing works

FurA is the master regulator of iron homeostasis and modulates the expression of tetrapyrrole biosynthesis genes in A nabaena sp. PCC 7120

González, A., Bes, M. T., Valladares, A., Peleato, M. L., & Fillat, M. F. (2012) · Environmental Microbiology · doi:10.1111/j.1462-2920.2012.02897.x · Cited by 69 · see citing works

Mapping the regulon of <i>Vibrio cholerae</i> ferric uptake regulator expands its known network of gene regulation

Davies, B. W., Bogard, R. W., & Mekalanos, J. J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107894108 · Cited by 69 · see citing works

Structural and Functional Characterization of Mycobacterium tuberculosis CmtR, a PbII/CdII-Sensing SmtB/ArsR Metalloregulatory Repressor

Wang, Y., Hemmingsen, L., & Giedroc, D. P. (2005) · Biochemistry · doi:10.1021/bi050094v · Cited by 67 · see citing works

Structural basis for the specialization of Nur, a nickel-specific Fur homolog, in metal sensing and DNA recognition

An, Y. J., Ahn, B., Han, A.-R., Kim, H.-M., Chung, K. M., Shin, J., Cho, Y., Roe, J., & Cha, S. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp198 · Cited by 66 · see citing works

The Zur of Xanthomonas campestris functions as a repressor and an activator of putative zinc homeostasis genes via recognizing two distinct sequences within its target promoters

Huang, D., Tang, D., Liao, Q., Li, H.-C., Chen, Q., He, Y.-Q., Feng, J., Jiang, B., Lu, G., Chen, B., et al. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn328 · Cited by 63 · see citing works

Origins of specificity and cross‐talk in metal ion sensing by <i><scp>B</scp>acillus subtilis</i><scp>Fur</scp>

Ma, Z., Faulkner, M. J., & Helmann, J. D. (2012) · Molecular Microbiology · doi:10.1111/mmi.12049 · Cited by 62 · see citing works

Regulatory circuits inHelicobacter pylori: network motifs and regulators involved in metal-dependent responses

Danielli, A., & Scarlato, V. (2010) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2010.00233.x · Cited by 62 · see citing works

Isolation and analysis of a fur mutant of Neisseria gonorrhoeae

Thomas, C. E., & Sparling, P. F. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.14.4224-4232.1996 · Cited by 60 · see citing works

Intracellular Zn(II) Intoxication Leads to Dysregulation of the PerR Regulon Resulting in Heme Toxicity in Bacillus subtilis

Chandrangsu, P., & Helmann, J. D. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1006515 · Cited by 60 · see citing works

Fur-like proteins: Beyond the ferric uptake regulator (Fur) paralog

Sevilla, E., Bes, M. T., Peleato, M. L., & Fillat, M. F. (2021) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2021.108770 · Cited by 57 · see citing works

Characterization of the Fur Regulon in Pseudomonas syringae pv. tomato DC3000

Butcher, B. G., Bronstein, P. A., Myers, C. R., Stodghill, P. V., Bolton, J. J., Markel, E. J., Filiatrault, M. J., Swingle, B. M., Gaballa, A., Helmann, J. D., et al. (2011) · Journal of Bacteriology · doi:10.1128/jb.00340-11 · Cited by 55 · see citing works

Gene Regulation and Transcriptomics

Samuels, D. S., Lybecker, M. C., Yang, X., Ouyang, Z., Bourret, T. J., Boyle, W. K., Stevenson, B., Drecktrah, D., & Caimano, M. J. (2020) · Current Issues in Molecular Biology · doi:10.21775/cimb.042.223 · Cited by 55 · see citing works

Perception and Homeostatic Control of Iron in the Rhizobia and Related Bacteria

O’Brian, M. R. (2015) · Annual Review of Microbiology · doi:10.1146/annurev-micro-091014-104432 · Cited by 50 · see citing works

ESX/Type VII Secretion Systems—An Important Way Out for Mycobacterial Proteins

Vaziri, F., & Brosch, R. (2019) · Microbiology Spectrum · doi:10.1128/microbiolspec.psib-0029-2019 · Cited by 50 · see citing works

YdiV regulates Escherichia coli ferric uptake by manipulating the DNA-binding ability of Fur in a SlyD-dependent manner

Zhang, F., Li, B., Dong, H., Chen, M., Yao, S., Li, J., Zhang, H., Liu, X., Wang, H., Song, N., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa696 · Cited by 49 · cited 1× · see citing works

Zur: Zinc-Sensing Transcriptional Regulator in a Diverse Set of Bacterial Species

Kandari, D., Joshi, H., & Bhatnagar, R. (2021) · Pathogens · doi:10.3390/pathogens10030344 · Cited by 46 · see citing works

Fur Represses Vibrio cholerae Biofilm Formation via Direct Regulation of vieSAB, cdgD, vpsU, and vpsA-K Transcription

Gao, H., Ma, L., Qin, Q., Qiu, Y., Zhang, J., Li, J., Lou, J., Diao, B., Zhao, H., Shi, Q., et al. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.587159 · Cited by 45 · see citing works

MntR ( R v2788): a transcriptional regulator that controls manganese homeostasis in M ycobacterium tuberculosis

Pandey, R., Russo, R., Ghanny, S., Huang, X., Helmann, J. D., & Rodríguez, G. M. (2015) · Molecular Microbiology · doi:10.1111/mmi.13207 · Cited by 44 · see citing works

Facilitated Unbinding via Multivalency-Enabled Ternary Complexes: New Paradigm for Protein–DNA Interactions

Chen, T., Cheng, Y., Huang, P.-S., & Chen, P. (2018) · Accounts of Chemical Research · doi:10.1021/acs.accounts.7b00541 · Cited by 44 · see citing works

Independent and cooperative regulation of staphylopine biosynthesis and trafficking by Fur and Zur

Fojcik, C., Arnoux, P., Ouerdane, L., Aigle, M., Alfonsi, L., & Borezée‐Durant, E. (2018) · Molecular Microbiology · doi:10.1111/mmi.13927 · Cited by 43 · see citing works

Oxidization without substrate unfolding triggers proteolysis of the peroxide-sensor, PerR

Ahn, B., & Baker, T. A. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1522687112 · Cited by 42 · see citing works

Tailoring a Global Iron Regulon to a Uropathogen

Banerjee, R., Weisenhorn, E., Schwartz, K. J., Myers, K. S., Glasner, J. D., Perna, N. T., Coon, J. J., Welch, R. A., & Kiley, P. J. (2020) · mBio · doi:10.1128/mbio.00351-20 · Cited by 38 · see citing works

Refined analysis of the Campylobacter jejuni iron-dependent/independent Fur- and PerR-transcriptomes

Butcher, J., Handley, R. A., van Vliet, A. H. M., & Stintzi, A. P. (2015) · BMC Genomics · doi:10.1186/s12864-015-1661-7 · Cited by 38 · see citing works

Stand-Alone EAL Domain Proteins Form a Distinct Subclass of EAL Proteins Involved in Regulation of Cell Motility and Biofilm Formation in Enterobacteria

Mouali, Y. E., Kim, H., Ahmad, I., Brauner, A., Liu, Y., Skurnik, M., Galperin, M. Y., & Römling, U. (2017) · Journal of Bacteriology · doi:10.1128/jb.00179-17 · Cited by 37 · see citing works

Heme binds to and inhibits the DNA‐binding activity of the global regulator FurA from Anabaena sp. PCC 7120

Hernández‐Rivas, J., Peleato, M. L., Fillat, M. F., & Bes, M. T. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.09.060 · Cited by 36 · see citing works

Fur Activates Expression of the 2-Oxoglutarate Oxidoreductase Genes ( oorDABC ) in Helicobacter pylori

Gilbreath, J. J., West, A. L., Pich, Ò. Q., Carpenter, B. M., Michel, S. L. J., & Merrell, D. S. (2012) · Journal of Bacteriology · doi:10.1128/jb.01226-12 · Cited by 36 · see citing works

Metal-responsive promoter DNA compaction by the ferric uptake regulator

Roncarati, D., Pelliciari, S., Doniselli, N., Maggi, S., Vannini, A., Valzania, L., Mazzei, L., Zambelli, B., Rivetti, C., & Danielli, A. (2016) · Nature Communications · doi:10.1038/ncomms12593 · Cited by 36 · see citing works

Vibrio cholerae fur mutations associated with loss of repressor activity: implications for the structural-functional relationships of fur

Lam, M. S., Litwin, C. M., Carroll, P., & Calderwood, S. B. (1994) · Journal of Bacteriology · doi:10.1128/jb.176.16.5108-5115.1994 · Cited by 35 · see citing works

Site‐directed mutagenesis and spectral studies suggest a putative role of FurA from Anabaena sp. PCC 7120 as a heme sensor protein

Pellicer, S., González, A., Peleato, M. L., Martínez, J. I., Fillat, M. F., & Bes, M. T. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08606.x · Cited by 33 · see citing works

Genome-Wide Characterization of the Fur Regulatory Network Reveals a Link between Catechol Degradation and Bacillibactin Metabolism in Bacillus subtilis

Pi, H., & Helmann, J. D. (2018) · mBio · doi:10.1128/mbio.01451-18 · Cited by 33 · see citing works

Quaternary Structure of Fur Proteins, a New Subfamily of Tetrameric Proteins

Pérard, J., Covès, J., Castellan, M., Solard, C., Savard, M., Miras, R., Galop, S., Signor, L., Crouzy, S., Michaud‐Soret, I., et al. (2016) · Biochemistry · doi:10.1021/acs.biochem.5b01061 · Cited by 32 · see citing works

Themes and Variations: Regulation of RpoN-Dependent Flagellar Genes across Diverse Bacterial Species

Tsang, J., & Hoover, T. R. (2014) · Scientifica · doi:10.1155/2014/681754 · Cited by 31 · see citing works

BlsA integrates light and temperature signals into iron metabolism through Fur in the human pathogen Acinetobacter baumannii

Tuttobene, M. R., Cribb, P., & Mussi, M. A. (2018) · Scientific Reports · doi:10.1038/s41598-018-26127-8 · Cited by 31 · see citing works

The novel type II toxin–antitoxin PacTA modulates Pseudomonas aeruginosa iron homeostasis by obstructing the DNA-binding activity of Fur

Song, Y., Zhang, S., Ye, Z.-R., Song, Y., Chen, L., Tong, A., He, Y., & Bao, R. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac867 · Cited by 31 · see citing works

Transcriptional Control of the Bradyrhizobium japonicum irr Gene Requires Repression by Fur and Antirepression by Irr

Hohle, T. H., & O’Brian, M. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.145979 · Cited by 30 · see citing works

Variation on a theme: investigating the structural repertoires used by ferric uptake regulators to control gene expression

Sarvan, S., Butcher, J., Stintzi, A., & Couture, J.-F. (2018) · BioMetals · doi:10.1007/s10534-018-0120-8 · Cited by 30 · see citing works

Regulation of Iron Uptake by Fine-Tuning the Iron Responsiveness of the Iron Sensor Fur

Choi, J., & Ryu, S. (2019) · Applied and Environmental Microbiology · doi:10.1128/aem.03026-18 · Cited by 30 · see citing works

The release of a distinct cell type from swarm colonies facilitates dissemination of Vibrio parahaemolyticus in the environment

Freitas, C., Glatter, T., & Ringgaard, S. (2019) · The ISME Journal · doi:10.1038/s41396-019-0521-x · Cited by 28 · see citing works

Bacillus subtilis Fur Is a Transcriptional Activator for the PerR-Repressed pfeT Gene, Encoding an Iron Efflux Pump

Pinochet‐Barros, A., & Helmann, J. D. (2020) · Journal of Bacteriology · doi:10.1128/jb.00697-19 · Cited by 24 · see citing works

A novel stress-inducible CmtR-ESX3-Zn2+ regulatory pathway essential for survival of Mycobacterium bovis under oxidative stress

Li, X., Chen, L., Liao, J., Hui, J., Li, W., & He, Z. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013017 · Cited by 24 · see citing works

Unraveling the Redox Properties of the Global Regulator FurA from Anabaena sp. PCC 7120: Disulfide Reductase Activity Based on Its CXXC Motifs

Botello‐Morte, L., Bes, M. T., Heras, B., Fernández‐Otal, Á., Peleato, M. L., & Fillat, M. F. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5376 · Cited by 23 · see citing works

Fur-Dam Regulatory Interplay at an Internal Promoter of the Enteroaggregative Escherichia coli Type VI Secretion sci1 Gene Cluster

Brunet, Y. R., Bernard, C., & Cascalès, E. (2020) · Journal of Bacteriology · doi:10.1128/jb.00075-20 · Cited by 23 · see citing works

Functional insights into the interplay between DNA interaction and metal coordination in ferric uptake regulators

Sarvan, S., Charih, F., Askoura, M., Butcher, J., Brunzelle, J. S., Stintzi, A. P., & Couture, J. (2018) · Scientific Reports · doi:10.1038/s41598-018-25157-6 · Cited by 21 · see citing works

Cysteine Mutational Studies Provide Insight into a Thiol-Based Redox Switch Mechanism of Metal and DNA Binding in FurA from Anabaena sp. PCC 7120

Botello‐Morte, L., Pellicer, S., Sein‐Echaluce, V. C., Contreras, L. M., Neira, J. L., Abián, O., Velázquez‐Campoy, A., Peleato, M. L., Fillat, M. F., & Bes, M. T. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6175 · Cited by 20 · see citing works

New insights into the tetrameric family of the Fur metalloregulators

Nader, S., Pérard, J., Carpentier, P., Arnaud, L., Crouzy, S., & Michaud‐Soret, I. (2019) · BioMetals · doi:10.1007/s10534-019-00201-8 · Cited by 20 · see citing works

Differential control of B radyrhizobium japonicum iron stimulon genes through variable affinity of the iron response regulator ( Irr ) for target gene promoters and selective loss of activator function

Jaggavarapu, S., & O’Brian, M. R. (2014) · Molecular Microbiology · doi:10.1111/mmi.12584 · Cited by 18 · see citing works

Genome-Wide Analysis of ResD, NsrR, and Fur Binding in Bacillus subtilis during Anaerobic Fermentative Growth by In Vivo Footprinting

Chumsakul, O., Anantsri, D. P., Quirke, T., Oshima, T., Nakamura, K., Ishikawa, S., & NAKANO, M. M. (2017) · Journal of Bacteriology · doi:10.1128/jb.00086-17 · Cited by 18 · see citing works

Biphasic unbinding of a metalloregulator from DNA for transcription (de)repression in Live Bacteria

Jung, W., Sengupta, K., Wendel, B. M., Helmann, J. D., & Chen, P. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa056 · Cited by 18 · see citing works

Ferric uptake regulators (Fur) from Vibrio cholerae and Helicobacter pylori bind a [2Fe-2S] cluster in response to elevation of intracellular free iron content

Fontenot, C. R., & Ding, H. (2022) · BioMetals · doi:10.1007/s10534-022-00390-9 · Cited by 17 · see citing works

Mechanistic insights into heme-mediated transcriptional regulation via a bacterial manganese-binding iron regulator, iron response regulator (Irr)

Nam, D., Matsumoto, Y., Uchida, T., O’Brian, M. R., & Ishimori, K. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011855 · Cited by 17 · see citing works

The protein–protein interaction network of the Escherichia coli EIIANtr regulatory protein reveals a role in cell motility and metabolic control

Gravina, F. S., Degaut, F. L. D., Gerhardt, E. C. M., Pedrosa, F. O., de Souza, E. M., de Souza, G. A., & Huergo, L. F. (2021) · Research in Microbiology · doi:10.1016/j.resmic.2021.103882 · Cited by 17 · see citing works

Genome-wide identification and characterization of Fur-binding sites in the cyanobacteria Synechocystis sp. PCC 6803 and PCC 6714

Riediger, M., Hernández‐Prieto, M. A., Song, K., Hess, W. R., & Futschik, M. E. (2021) · DNA Research · doi:10.1093/dnares/dsab023 · Cited by 16 · see citing works

Metal‐specific control of gene expression mediated by B radyrhizobium japonicum M ur and E scherichia coli F ur is determined by the cellular context

Hohle, T. H., & O’Brian, M. R. (2016) · Molecular Microbiology · doi:10.1111/mmi.13381 · Cited by 15 · see citing works

A composite filter for low FDR of protein-protein interactions detected by in vivo cross-linking

de Jong, L., Roseboom, W., & Kramer, G. (2020) · Journal of Proteomics · doi:10.1016/j.jprot.2020.103987 · Cited by 15 · see citing works

Crystal structure of S. aureus YlaN, an essential leucine rich protein involved in the control of cell shape

Xu, L., Sedelnikova, S. E., Baker, P. J., Hunt, A., Errington, J., & Rice, D. W. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21377 · Cited by 13 · see citing works

Proteome analysis of an Escherichia coli ptsN -null strain under different nitrogen regimes

Gravina, F. S., Sanchuki, H. B. S., Rodrigues, T. E., Gerhardt, E. C. M., Pedrosa, F. O., de Souza, E. M., Valdameri, G., de Souza, G. A., & Huergo, L. F. (2017) · Journal of Proteomics · doi:10.1016/j.jprot.2017.12.006 · Cited by 13 · see citing works

2‐oxoglutarate modulates the affinity of FurA for the ntcA promoter in Anabaena sp. PCC 7120

Guío, J., Sarasa‐Buisan, C., Velázquez‐Campoy, A., Bes, M. T., Fillat, M. F., Peleato, M. L., & Sevilla, E. (2019) · FEBS Letters · doi:10.1002/1873-3468.13610 · Cited by 11 · see citing works

Biochemical characterization of ferric uptake regulator (Fur) from Aliivibrio salmonicida. Mapping the DNA sequence specificity through binding studies and structural modelling

Berg, K., Pedersen, H. L., & Leiros, I. (2020) · BioMetals · doi:10.1007/s10534-020-00240-6 · Cited by 10 · see citing works

Regulation of the expression of the nickel uptake system in Vibrio cholerae by iron and heme via ferric uptake regulator (Fur)

Muranishi, K., Ishimori, K., & Uchida, T. (2022) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2022.111713 · Cited by 8 · see citing works

Metal binding and oligomerization properties of FurC (PerR) from Anabaena sp. PCC7120: an additional layer of regulation?

Sarasa‐Buisan, C., Emonot, E., Martínez‐Júlvez, M., Sevilla, E., Velázquez‐Campoy, A., Crouzy, S., Bes, M. T., Michaud‐Soret, I., & Fillat, M. F. (2022) · Metallomics · doi:10.1093/mtomcs/mfac077 · Cited by 7 · see citing works

Vibrio parahaemolyticus FcrX, a Fur‐controlled regulator that inhibits repression by Fur

Morabe, M. L., & McCarter, L. L. (2020) · Molecular Microbiology · doi:10.1111/mmi.14497 · Cited by 7 · see citing works

Thioredoxin Dependent Changes in the Redox States of FurA from Anabaena sp. PCC 7120

Guío, J., Bes, M. T., Balsera, M., Calvo-Beguería, L., Sevilla, E., Peleato, M. L., & Fillat, M. F. (2021) · Antioxidants · doi:10.3390/antiox10060913 · Cited by 7 · see citing works

The inability of Bacillus licheniformis perR mutant to grow is mainly due to the lack of PerR-mediated fur repression

Kim, J. H., Yang, Y.-M., Ji, C., Ryu, S.-H., Won, Y., Ju, S., Kwon, Y. M., Lee, Y.-E., Youn, H., & Lee, J. (2017) · The Journal of Microbiology · doi:10.1007/s12275-017-7051-x · Cited by 6 · see citing works

Evaluation of the regulatory model for Ni2+ sensing by Nur from Streptomyces coelicolor

Manley, O. M., Myers, P. D., Toney, D. J., Bolling, K. F., Rhodes, L. C., Gasparik, J. L., & Grossoehme, N. E. (2019) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2019.110859 · Cited by 6 · see citing works

Do FeS clusters rule bacterial iron regulation?

Lill, R. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.h120.016190 · Cited by 3 · see citing works

Untitled work

(2021) · doi:10.1021/acs

Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking

Capdevila, D. A., Rondón, J. J., Edmonds, K. A., Rocchio, J. S., Dujovne, M. V., & Giedroc, D. P. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00264 · Cited by 59 · see citing works

Microbial metal physiology: ions to ecosystems

Helmann, J. D. (2025) · Nature Reviews Microbiology · doi:10.1038/s41579-025-01213-7 · Cited by 46 · see citing works

Structural Perspectives on Metal Dependent Roles of Ferric Uptake Regulator (Fur)

Kang, S., Kang, H.-S., Chung, W., Kang, K., & Kim, D.-H. (2024) · Biomolecules · doi:10.3390/biom14080981 · Cited by 19 · see citing works

Structure, Function, and Biosynthesis of Siderophores Produced by Streptomyces Species

Wang, M., & Li, H. (2025) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.4c08231 · Cited by 17 · see citing works

Fpa (YlaN) is an iron(II) binding protein that functions to relieve Fur-mediated repression of gene expression in <i>Staphylococcus aureus</i>

Boyd, J. M., Ryan Kaler, K., Esquilín-Lebrón, K., Pall, A., Campbell, C. J., Foley, M. E., Rios-Delgado, G., Mustor, E. M., Stephens, T. G., Bovermann, H., et al. (2024) · mBio · doi:10.1128/mbio.02310-24 · Cited by 14 · see citing works

A Salmonella subset exploits erythrophagocytosis to subvert SLC11A1-imposed iron deprivation

Roche, B., Claudi, B., Cunrath, O., Bleck, C. K. E., Antelo-Varela, M., Li, J., & Bumann, D. (2025) · Cell Host & Microbe · doi:10.1016/j.chom.2025.04.013 · Cited by 15 · see citing works

The molecular mechanisms of the bacterial iron sensor IdeR

Marcos‐Torres, F. J., Juniar, L., & Griese, J. J. (2023) · Biochemical Society Transactions · doi:10.1042/bst20221539 · Cited by 13 · see citing works

Adaptive evolutionary strategies of microbes to manganese in nitrogen-culturing sludge

Liu, Y., Song, X., Wang, Y., Hou, X., Wang, Y., & Cao, X. (2023) · Journal of Cleaner Production · doi:10.1016/j.jclepro.2023.139666 · Cited by 12 · see citing works

Microbes vary strategically in their metalation of mononuclear enzymes

Rohaun, S. K., Sethu, R., & Imlay, J. A. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2401738121 · Cited by 11 · see citing works

Iron Homeostasis in Azotobacter vinelandii

Rosa‐Núñez, E., Echávarri‐Erasun, C., Armas, A. M., Escudero, V., Poza‐Carrión, C., Rubio, L. M., & González‐Guerrero, M. (2023) · Biology · doi:10.3390/biology12111423 · Cited by 8 · see citing works

Metabolic engineering of Bacillus subtilis for the production of active hemoglobins and myoglobins by improving heme supply

Wang, S., Jingwen, Z., Li, J., Chen, J., Du, G., Li, Z., Lee, S. Y., & Zhao, X. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2504795122 · Cited by 10 · see citing works

Iron-sulfur cluster biogenesis and regulation of intracellular iron homeostasis in Escherichia coli

Ding, H. (2025) · Metallomics · doi:10.1093/mtomcs/mfaf040 · Cited by 8 · see citing works

Characterization of the Zinc Uptake Repressor (Zur) from <i>Acinetobacter baumannii</i>

Kim, M., Le, M. T., Fan, L., Campbell, C., Sen, S., Capdevila, D. A., Stemmler, T. L., & Giedroc, D. P. (2024) · Biochemistry · doi:10.1021/acs.biochem.3c00679 · Cited by 8 · see citing works

Iron–sulfur cluster assembly scaffold protein IscU is required for activation of ferric uptake regulator (Fur) in Escherichia coli

Purcell, A. G., Fontenot, C. R., & Ding, H. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107142 · Cited by 6 · see citing works

The Role of Bacterial Siderophores in Infection Therapy: From Anti-Infective Mechanisms to Therapeutic Advances

Xiao, J., Bu, Y., Tao, Y., Zhou, Z., Zou, J., Cui, W., & Yang, Z. (2025) · International Journal of Nanomedicine · doi:10.2147/ijn.s576272 · Cited by 6 · see citing works

Multiple regulatory inputs including cell envelope stress orchestrate expression of the Escherichia coli rpoN operon

Sikora, F., Budja, L. V. P., Milojevic, O., Ziemniewicz, A., Dudys, P., & Görke, B. (2024) · Molecular Microbiology · doi:10.1111/mmi.15280 · Cited by 6 · see citing works

Detection of environmental pollutants using transcription factor-based whole-cell biosensors

Dou, Y., Zhang, J., Gong, X., Gan, Q., Yu, S., & Yan, Y. (2025) · Biotechnology for the Environment · doi:10.1186/s44314-025-00032-7 · Cited by 6 · see citing works

New Insights into Acinetobacter baumannii Pathogenesis and Therapeutic Implications

Morena, R., Morrone, H. L., Olivadese, V., Gullì, S. P., Serapide, F., & Russo, A. (2026) · Pathogens · doi:10.3390/pathogens15040391 · Cited by 5 · see citing works

(Re)-definition of the holo- and apo-Fur direct regulons of Helicobacter pylori

Vannini, A., Pinatel, E., Costantini, P. E., Pelliciari, S., Roncarati, D., Puccio, S., Bellis, G. D., Scarlato, V., Peano, C., & Danielli, A. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168573 · Cited by 5 · see citing works

YlaN is an iron(II) binding protein that functions to relieve Fur-mediated repression of gene expression in <i>Staphylococcus aureus</i>

Boyd, J. M., Esquilín-Lebrón, K., Campbell, C. J., Kaler, K. R., Norambuena, J., Foley, M. E., Stephens, T. G., Rios, G., Mereddy, G., Zheng, V., et al. (2023) · doi:10.1101/2023.10.03.560778 · Cited by 4 · see citing works

DNA Binding by BosR Controls RpoS ‐Dependent and ‐Independent Gene Expression in Borrelia burgdorferi

Grassmann, A. A., McLain, M. A., Freeman, M. R., Caimano, M. J., & Radolf, J. D. (2025) · Molecular Microbiology · doi:10.1111/mmi.70036 · Cited by 4 · see citing works

The transcriptional response to low temperature is weakly conserved across the Enterobacteriaceae

Hoang, J., & Stoebel, D. M. (2024) · mSystems · doi:10.1128/msystems.00785-24 · Cited by 4 · see citing works

Characterisation of Pseudomonas aeruginosa’s metal-responsive TonB-dependent transportersPreprint

Ferry, M., Ferriz, H., Sharp, C., Paschalidis, C., Boutant, E., Schalk, I. J., & Cunrath, O. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.14.618150 · Cited by 4 · see citing works

Binding of a [2Fe–2S] cluster drives dimerization of ferric uptake regulator (Fur) in Escherichia coli

Najafi, F., Purcell, A. G., Homes, F. H., & Ding, H. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110702 · Cited by 3 · see citing works

Mossbauer studies of the redox state of the ferric uptake regulator [2Fe-2S](2+) cluster in Escherichia coli

Fontenot, C. R., Hoepner, T., Xiong, J., Ding, H., & Popescu, C. V. (2025) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2025.112928 · Cited by 3 · see citing works

Moonlighting in metabolism: bifunctional enzymes control nitrogen metabolism in Bacillus subtilis

Gibhardt, J., Lieber, M. M., Götz, C. S., Völker, F., Blank, L. M., Forchhammer, K., Jayaraman, V., Noda‐García, L., & Commichau, F. M. (2026) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00430-25 · Cited by 3 · see citing works

Regulation of iron ion homeostasis in Staphylococcus aureus and its impact on physiology and virulence

Rios-Delgado, G., & Boyd, J. M. (2026) · mBio · doi:10.1128/mbio.01110-26 · Cited by 3 · see citing works

Resistance and removal mechanisms of deep-sea Bacillus sp. A260 in mitigating Mn2+ and microplastic pollution

Gu, Z., Zheng, R., Sun, C., & Wu, S. (2025) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2025.139429 · Cited by 3 · see citing works

Predicting metallophore structure and function through genome mining

Reitz, Z. L. (2024) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2024.06.007 · Cited by 3 · see citing works

Regulation of iron homeostasis by Fur and atypical response regulator SsoR via derepressor-inhibitor oscillation in Shewanella oneidensis

Jie, K., Liu, X., Hou, J., Xie, P., Tang, J., & Gao, H. (2025) · Applied and Environmental Microbiology · doi:10.1128/aem.01230-25 · Cited by 2 · see citing works

Distribution of hlyII and hlyIIR Genes among Bacillus cereus sensu lato

Nagel, A. S., Egorova, N. A., Kulbaev, I. S., Siunov, A. V., Andreeva‐Kovalevskaya, Z. I., & Solonin, A. S. (2025) · Mathematical Biology and Bioinformatics · doi:10.17537/2025.20.458 · Cited by 2 · see citing works

The BosR Is Back!

Samuels, D. S., & Lybecker, M. C. (2026) · Molecular Microbiology · doi:10.1111/mmi.70046 · Cited by 2 · see citing works

Combined transcriptome and metabolome analysis reveals the regulatory network of histidine kinase QseC in the two-component system of Glaesserella parasuis

Yan, X., Zhou, Y., Liu, S., Gu, C., Xiao, W., Zhao, M., Yu, Z., & He, L. (2025) · Frontiers in Microbiology · doi:10.3389/fmicb.2025.1637383 · Cited by 2 · see citing works

pH-driven metabolic reprogramming in Bacillus velezensis 83 regulates metabolite synthesis and sporulation: A transcriptional approach for bioprocess development

Balón-Rosas, L. Y., Luna‐Bulbarela, A., Serrano‐Carreón, L., & Galindo, E. (2025) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2025.05.016 · Cited by 1 · see citing works

In-depth transcriptomic and ChIP-seq analyses on IrrB regulation of iron homeostasis during initial life phase of Magnetospirillum gryphiswaldense

Wang, Q., Jc, H., Liu, M., Li, Q., & Li, X. (2026) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-026-04829-w · Cited by 1 · see citing works

Deletion of glpK in Salmonella Choleraesuis decreases virulence and confers immune protection in mice

Zhao, X., You, Y., Jie, J., Xie, Y., Hao, Z., Zhou, Y., & He, Q. (2026) · Gene · doi:10.1016/j.gene.2026.150056 · Cited by 1 · see citing works

The physiology and biochemistry of oxidative stress in bacteria

Rohaun, S. K., & Imlay, J. A. (2026) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2026.02.005 · Cited by 1 · see citing works

The oxidative stress regulator, PerR, is required for staphyloferrin B-mediated iron acquisition in <i>Staphylococcus aureus</i>

Sheikh, A. A., Flannagan, R. S., Nicholson, N. J., Jarycki, N., Fabelurin, R. O., Lewis, I. A., & Heinrichs, D. E. (2026) · Journal of Bacteriology · doi:10.1128/jb.00149-26

Control of iron homeostasis by a regulatory protein-protein interaction in Bacillus subtilis : The FurA (YlaN) acts as an antirepressor to the ferric uptake regulator FurPreprint

Demann, L., Bremenkamp, R., Stahl, K., Hormes, B., Warneke, R., Rappsilber, J., & Stülke, J. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.28.559918

Mechanism of geraniol against E. coli infection by regulating YDIVPreprint

Long, N., Dai, M., Wang, Y., Zhang, Y., Guo, W., & Pu, Z. (2024) · Research Square · doi:10.21203/rs.3.rs-3869163/v1

Cyanobacterial Zur: Zinc‐Sensing Transcriptional Regulators

Mikhaylina, A., Scanlan, D. J., & Blindauer, C. A. (2024) · Encyclopedia of Inorganic and Bioinorganic Chemistry · doi:10.1002/9781119951438.eibc2866

Review Article: Role of FeoA in the Interaction with the Fe2+-Fur Complex in E. coli

Alali, S. (2024) · Academia Open · doi:10.21070/acopen.9.2024.10425

The crystal structure of the small zinc-finger protein ZifS from Thermus thermophilus HB8

Kurinami, S., Fukui, K., Murakawa, T., Baba, S., Kumasaka, T., Okanishi, H., Kanai, Y., Yano, T., & Masui, R. (2025) · The Journal of Biochemistry · doi:10.1093/jb/mvaf028

Roles of biological heme-based sensors of O2 in controlling bacterial behavior

Fekete, F. J., & Weinert, E. E. (2025) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2025.113071

“Self-gapping” by a C-terminal domain arginine finger regulates GTP hydrolysis in bacterial zinc metallochaperonesPreprint

Rocchio, J. S., Osterberg, M. K., McRae, E. M., Jaiswal, N., Edmonds, K. A., Doyle, D. A., Skaar, E. P., & Giedroc, D. P. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.03.03.709369

The ESX-3 secretion system in mycobacteria: Evolution, structure, and multifunctional roles in pathogenesis

Wang, M., Cheng, J., Luo, D.-M., 李素清, Wang, D., Yang, D., & Wang, Q. (2026) · Microbial Pathogenesis · doi:10.1016/j.micpath.2026.108438

Control of the iron-sparing response in Staphylococcus aureus by a regulatory RNA

Barrault, M. (2023) · theses.fr (ABES) · doi:10.70675/6d13b6e4zd6f9z42bdz8c5bz5262c5da4c10

Organic Molecules are Involved in Ni-Struvite Biomineralization by Streptomyces mirabilis

Costa, F. S., Krüger, T., Ueberschaar, N., Kniemeyer, O., Brakhage, A. A., & Kothe, E. (2026) · Molecular Biotechnology · doi:10.1007/s12033-026-01580-3

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