Self-poisoning of Mycobacterium tuberculosis by interrupting siderophore recycling

Disorders of Iron Metabolism

Andrews, N. C. (1999) · New England Journal of Medicine · doi:10.1056/nejm199912233412607 · Cited by 2,130 · see citing works

Siderophore-Based Iron Acquisition and Pathogen Control

Miethke, M., & Marahiel, M. A. (2007) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00012-07 · Cited by 1,774 · see citing works

Chemistry and biology of siderophores

Hider, R. C., & Kong, X. (2010) · Natural Product Reports · doi:10.1039/b906679a · Cited by 1,722 · see citing works

Microplate alamar blue assay versus BACTEC 460 system for high-throughput screening of compounds against Mycobacterium tuberculosis and Mycobacterium avium

Collins, L., & Franzblau, S. G. (1997) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.41.5.1004 · Cited by 1,599 · see citing works

Iron and microbial infection

Schaible, U. E., & Kaufmann, S. H. E. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro1046 · Cited by 945 · see citing works

Enterobactin: an archetype for microbial iron transport.

Raymond, K. N., Dertz, E. A., & Kim, S. S. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0630018100 · Cited by 933 · see citing works

Genetics and Assembly Line Enzymology of Siderophore Biosynthesis in Bacteria

Crosa, J. H., & Walsh, C. T. (2002) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.66.2.223-249.2002 · Cited by 797 · see citing works

The architecture of respiratory complex I

Efremov, R. G., Baradaran, R., & Sazanov, L. A. (2010) · Nature · doi:10.1038/nature09066 · Cited by 616 · see citing works

Growth of Mycobacterium tuberculosis biofilms containing free mycolic acids and harbouring drug‐tolerant bacteria

Ojha, A. K., Baughn, A. D., Sambandan, D., Hsu, T., Trivelli, X., Guérardel, Y., Alahari, A., Kremer, L., Jacobs, W. R., & Hatfull, G. F. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06274.x · Cited by 541 · see citing works

The salicylate-derived mycobactin siderophores of <i>Mycobacterium tuberculosis</i> are essential for growth in macrophages

De Voss, J. J., Rutter, K., Schroeder, B. G., Su, H., Zhu, Y., & Barry, C. E. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.3.1252 · Cited by 532 · see citing works

Mycobactins: iron-chelating growth factors from mycobacteria

Snow, G. A. (1970) · Bacteriological Reviews · doi:10.1128/br.34.2.99-125.1970 · Cited by 378 · see citing works

Iron, mycobacteria and tuberculosis

Ratledge, C. (2003) · Tuberculosis · doi:10.1016/j.tube.2003.08.012 · Cited by 344 · 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

Solution equilibria of enterobactin and metal-enterobactin complexes

Loomis, L. D., & Raymond, K. N. (1991) · Inorganic Chemistry · doi:10.1021/ic00005a008 · Cited by 321 · see citing works

Small-molecule inhibition of siderophore biosynthesis in Mycobacterium tuberculosis and Yersinia pestis

Ferreras, J. A., Ryu, J., Lello, F. A. D., Tan, D. S., & Quadri, L. E. N. (2005) · Nature Chemical Biology · doi:10.1038/nchembio706 · Cited by 295 · see citing works

Mycobacterium tuberculosis and the intimate discourse of a chronic infection

Russell, D. G. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2010.00984.x · Cited by 291 · see citing works

Discovery of a Siderophore Export System Essential for Virulence of Mycobacterium tuberculosis

Wells, R. M., Jones, C. M., Xi, Z., Speer, A., Danilchanka, O., Doornbos, K. S., Sun, P., Wu, F., Tian, C., & Niederweis, M. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003120 · Cited by 267 · see citing works

Identification of an ABC Transporter Required for Iron Acquisition and Virulence inMycobacterium tuberculosis

Rodríguez, G. M., & Smith, I. (2005) · Journal of Bacteriology · doi:10.1128/jb.188.2.424-430.2006 · Cited by 257 · see citing works

Molecular basis of pyoverdine siderophore recycling in Pseudomonas aeruginosa

Imperi, F., Tiburzi, F., & Visca, P. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908760106 · Cited by 216 · see citing works

Present aspects of bacterial resistance in tuberculosis.

Canetti, G. (1965) · PubMed · doi:10.1164/arrd.1965.92.5.687 · Cited by 214 · see citing works

Mycobacterium tuberculosis ΔRD1 ΔpanCD: A safe and limited replicating mutant strain that protects immunocompetent and immunocompromised mice against experimental tuberculosis

Sambandamurthy, V. K., Derrick, S. C., Hsu, T., Chen, B., Larsen, M. H., Jalapathy, K. V., Chen, M., Kim, J., Porcelli, S. A., Chan, J., et al. (2006) · Vaccine · doi:10.1016/j.vaccine.2006.05.097 · Cited by 213 · see citing works

Exochelins of Mycobacterium tuberculosis remove iron from human iron-binding proteins and donate iron to mycobactins in the M. tuberculosis cell wall.

Gobin, J., & Horwitz, M. A. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.183.4.1527 · Cited by 208 · see citing works

A Comparative Lipidomics Platform for Chemotaxonomic Analysis of Mycobacterium tuberculosis

Layre, E., Sweet, L., Hong, S., Madigan, C. A., Desjardins, D., Young, D. C., Cheng, T., Annand, J. W., Kim, K., Shamputa, I. C., et al. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.10.013 · Cited by 201 · see citing works

Discovery and characterization of a unique mycobacterial heme acquisition system

Tullius, M. V., Harmston, C. A., Owens, C. P., Chim, N., Morse, R. P., McMath, L. M., Iniguez, A., Kimmey, J. M., Sawaya, M. R., Whitelegge, J. P., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009516108 · Cited by 199 · 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

Survival perspectives from the world's most successful pathogen, Mycobacterium tuberculosis

Hingley‐Wilson, S., Sambandamurthy, V. K., & Jacobs, W. R. (2003) · Nature Immunology · doi:10.1038/ni981 · Cited by 192 · see citing works

Iron acquisition by Mycobacterium tuberculosis: isolation and characterization of a family of iron-binding exochelins.

Gobin, J., Moore, C. H., Reeve, J. R., Wong, D. K., Gibson, B. W., & Horwitz, M. A. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.11.5189 · Cited by 181 · see citing works

Role of ferrichrome as a ferric ionophore in Ustilago sphaerogena

Emery, T. F. (1971) · Biochemistry · doi:10.1021/bi00784a033 · Cited by 180 · see citing works

Overexpression and purification of ferric enterobactin esterase from Escherichia coli. Demonstration of enzymatic hydrolysis of enterobactin and its iron complex.

Brickman, T. J., & McIntosh, M. A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49846-3 · Cited by 167 · see citing works

Siderophore electrochemistry: relation to intracellular iron release mechanism.

COOPER, S. R., MCARDLE, J. V., & Raymond, K. N. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.8.3551 · Cited by 135 · see citing works

Disruption of Mycobactin Biosynthesis Leads to Attenuation of Mycobacterium tuberculosis for Growth and Virulence

Reddy, P. V., Puri, R. V., Chauhan, P., Kar, R., Rohilla, A., Khera, A., & Tyagi, A. K. (2013) · The Journal of Infectious Diseases · doi:10.1093/infdis/jit250 · Cited by 127 · see citing works

The Ferrichrome Uptake Pathway inPseudomonas aeruginosaInvolves an Iron Release Mechanism with Acylation of the Siderophore and Recycling of the Modified Desferrichrome

Hannauer, M., Barda, Y., Mislin, G. L. A., Shanzer, A., & Schalk, I. J. (2010) · Journal of Bacteriology · doi:10.1128/jb.01539-09 · Cited by 114 · see citing works

The Mycobacterium tuberculosis High-Affinity Iron Importer, IrtA, Contains an FAD-Binding Domain

Ryndak, M. B., Wang, S., Smith, I., & Rodríguez, G. M. (2009) · Journal of Bacteriology · doi:10.1128/jb.00223-09 · Cited by 96 · see citing works

5‘-O-[(N-Acyl)sulfamoyl]adenosines as Antitubercular Agents that Inhibit MbtA: An Adenylation Enzyme Required for Siderophore Biosynthesis of the Mycobactins

Qiao, C., Gupte, A., Boshoff, H. I., Wilson, D. J., Bennett, E. M., Somu, R. V., Barry, C. E., & Aldrich, C. C. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm070905o · Cited by 94 · see citing works

Mycobacterium tuberculosis Can Utilize Heme as an Iron Source

Jones, C. M., & Niederweis, M. (2011) · Journal of Bacteriology · doi:10.1128/jb.01312-10 · Cited by 94 · see citing works

The Siderophore-Interacting Protein YqjH Acts as a Ferric Reductase in Different Iron Assimilation Pathways of Escherichia coli

Miethke, M., Hou, J., & Marahiel, M. A. (2011) · Biochemistry · doi:10.1021/bi201517h · Cited by 88 · see citing works

MmpS4 promotes glycopeptidolipids biosynthesis and export in Mycobacterium smegmatis

Deshayes, C., Bach, H., Euphrasie, D., Attarian, R., Coureuil, M., Sougakoff, W., Laval, F., Av‐Gay, Y., Daffé, M., Etienne, G., et al. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07385.x · Cited by 80 · see citing works

An efflux pump is involved in secretion of newly synthesized siderophore by Pseudomonas aeruginosa

Hannauer, M., Yeterian, E., Martin, L. W., Lamont, I. L., & Schalk, I. J. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.10.051 · Cited by 76 · see citing works

Iron Transport in Escherichia coli : Uptake and Modification of Ferrichrome

Hartmann, A., & Braun, V. (1980) · Journal of Bacteriology · doi:10.1128/jb.143.1.246-255.1980 · Cited by 69 · see citing works

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 · see citing works

Lipidomic discovery of deoxysiderophores reveals a revised mycobactin biosynthesis pathway in <i>Mycobacterium tuberculosis</i>

Madigan, C. A., Cheng, T.-Y., Layre, E., Young, D. C., McConnell, M. J., Debono, C. A., Murry, J. P., Wei, J.-R., Barry, C. E., Rodriguez, G. M., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1109958109 · Cited by 65 · see citing works

Iron transport in Mycobacterium smegmatis: Ferrimycobactin reductase (NAD(P)H:Ferrimycobactin oxidoreductase), the enzyme releasing iron from its carrier

Brown, K. A., & Ratledge, C. (1975) · FEBS Letters · doi:10.1016/0014-5793(75)80033-0 · Cited by 52 · see citing works

BordetellaAlcS Transporter Functions in Alcaligin Siderophore Export and Is Central to Inducer Sensing in Positive Regulation of Alcaligin System Gene Expression

Brickman, T. J., & Armstrong, S. K. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.11.3650-3661.2005 · Cited by 48 · see citing works

Mutational and Phylogenetic Analyses of the Mycobacterial mbt Gene Cluster

Chavadi, S. S., Stirrett, K. L., Edupuganti, U. R., Vergnolle, O., Sadhanandan, G., Marchiano, E. J., Martin, C., Qiu, W., Soll, C. E., & Quadri, L. E. N. (2011) · Journal of Bacteriology · doi:10.1128/jb.05811-11 · Cited by 46 · see citing works

Growth stimulation ofEscherichia coliin serum by iron(III) aerobactin. Recycling of aerobactin

Braun, V., Brazel-Faisst, C., & Schneider, R. (1984) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1984.tb00193.x · Cited by 35 · see citing works

Inability to detect mycobactin in Mycobacteria-infected tissues suggests an alternative iron acquisition mechanism by Mycobacteria in vivo

Lambrecht, R. S., & Collins, M. T. (1993) · Microbial Pathogenesis · doi:10.1006/mpat.1993.1022 · Cited by 34 · see citing works

Organ Pathology in the Absence of Bacteria?

Jones, C. M., & Niederweis, M. (2013) · The Journal of Infectious Diseases · doi:10.1093/infdis/jit606 · Cited by 3 · see citing works

Macrophage defense mechanisms against intracellular bacteria

Weiss, G., & Schaible, U. E. (2015) · Immunological Reviews · doi:10.1111/imr.12266 · Cited by 989 · see citing works

Bacterial siderophores in community and host interactions

Kramer, J., Özkaya, Ö., & Kümmerli, R. (2020) · Nature Reviews Microbiology · doi:10.1038/s41579-019-0284-4 · Cited by 998 · see citing works

Cross-Resistance between Clofazimine and Bedaquiline through Upregulation of MmpL5 in Mycobacterium tuberculosis

Hartkoorn, R. C., Uplekar, S. M., & Cole, S. T. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00037-14 · Cited by 493 · see citing works

Siderophores in Iron Metabolism: From Mechanism to Therapy Potential

Wilson, B., Bogdan, A. R., Miyazawa, M., Hashimoto, K., & Tsuji, Y. (2016) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.10.005 · Cited by 479 · see citing works

Transition Metals and Virulence in Bacteria

Palmer, L. D., & Skaar, E. P. (2016) · Annual Review of Genetics · doi:10.1146/annurev-genet-120215-035146 · Cited by 449 · see citing works

Infection with Mycobacterium tuberculosis induces the Warburg effect in mouse lungs

Shi, L., Salamon, H., Eugenín, E. A., Pine, R. I., Cooper, A. M., & Gennaro, M. L. (2015) · Scientific Reports · doi:10.1038/srep18176 · Cited by 237 · see citing works

Transposon-mediated site-specific recombination: A defined in vitro system

Reed, R. R. (1981) · Cell · doi:10.1016/0092-8674(81)90178-1 · Cited by 224 · see citing works

Separable roles for <i>Mycobacterium tuberculosis</i> ESX-3 effectors in iron acquisition and virulence

Tufariello, J. M., Chapman, J. R., Kerantzas, C. A., Wong, K.-W., Vilchèze, C., Jones, C. M., Cole, L. E., Tinaztepe, E., Thompson, V., Fenyö, D., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1523321113 · Cited by 215 · see citing works

Mycobacteria, metals, and the macrophage

Neyrolles, O., Wolschendorf, F., Mitra, A., & Niederweis, M. (2015) · Immunological Reviews · doi:10.1111/imr.12265 · Cited by 217 · see citing works

Siderophores: Importance in bacterial pathogenesis and applications in medicine and industry

Khasheii, B., Mahmoodi, P., & Mohammadzadeh, A. (2021) · Microbiological Research · doi:10.1016/j.micres.2021.126790 · Cited by 210 · see citing works

The Tuberculosis Drug Discovery and Development Pipeline and Emerging Drug TargetsPreprint

Mdluli, K. E., Kaneko, T., & Upton, A. M. (2015) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a021154 · Cited by 181 · see citing works

Genome-wide screen identifies host colonization determinants in a bacterial gut symbiont

Powell, J. E., Leonard, S. P., Kwong, W. K., Engel, P., & Moran, N. A. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1610856113 · Cited by 144 · see citing works

Iron Homeostasis in Mycobacterium tuberculosis: Mechanistic Insights into Siderophore-Mediated Iron Uptake

Sritharan, M. (2016) · Journal of Bacteriology · doi:10.1128/jb.00359-16 · Cited by 133 · see citing works

Copper import in Escherichia coli by the yersiniabactin metallophore system

Koh, E.-I., Robinson, A. E., Bandara, N., Rogers, B., & Henderson, J. P. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2441 · Cited by 124 · see citing works

Insights into the smooth‐to‐rough transitioning in Mycobacterium bolletii unravels a functional Tyr residue conserved in all mycobacterial MmpL family members

Bernut, A., Viljoen, A. J., Dupont, C., Sapriel, G., Blaise, M., Bouchier, C., Brosch, R., de Chastellier, C., Herrmann, J., & Kremer, L. (2015) · Molecular Microbiology · doi:10.1111/mmi.13283 · Cited by 129 · see citing works

Iron Acquisition in Mycobacterium tuberculosis

Chao, A., Sieminski, P. J., Owens, C. P., & Goulding, C. W. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00285 · Cited by 125 · see citing works

Breaking a pathogen's iron will: Inhibiting siderophore production as an antimicrobial strategy

Lamb, A. L. (2015) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2015.05.001 · Cited by 103 · see citing works

PPE Surface Proteins Are Required for Heme Utilization by Mycobacterium tuberculosis

Mitra, A., Speer, A., Lin, K., Ehrt, S., & Niederweis, M. (2017) · mBio · doi:10.1128/mbio.01720-16 · Cited by 95 · see citing works

Comprehensive analysis of iron utilization by Mycobacterium tuberculosis

Zhang, L., Hendrickson, R. C., Meikle, V., Lefkowitz, E. J., Ioerger, T. R., & Niederweis, M. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008337 · Cited by 92 · see citing works

Chalkophores

Kenney, G. E., & Rosenzweig, A. C. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062917-012300 · Cited by 91 · see citing works

Lipid transport in Mycobacterium tuberculosis and its implications in virulence and drug development

Bailo, R., Bhatt, A., & Aínsa, J. A. (2015) · Biochemical Pharmacology · doi:10.1016/j.bcp.2015.05.001 · Cited by 93 · see citing works

The Evolutionary Conservation of Escherichia coli Drug Efflux Pumps Supports Physiological Functions

Teelucksingh, T., Thompson, L. K., & Cox, G. (2020) · Journal of Bacteriology · doi:10.1128/jb.00367-20 · Cited by 91 · see citing works

MmpL transporter-mediated export of cell-wall associated lipids and siderophores in mycobacteria

Chalut, C. (2016) · Tuberculosis · doi:10.1016/j.tube.2016.06.004 · Cited by 85 · see citing works

The Expanding Diversity of Mycobacterium tuberculosis Drug Targets

Wellington, S., & Hung, D. T. (2018) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.7b00255 · Cited by 81 · see citing works

Resistance to Thiacetazone Derivatives Active against Mycobacterium abscessus Involves Mutations in the MmpL5 Transcriptional Repressor MAB_4384

Halloum, I., Viljoen, A. J., Khanna, V., Craig, D., Bouchier, C., Brosch, R., Coxon, G. D., & Kremer, L. (2017) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02509-16 · Cited by 79 · see citing works

Critical discussion on drug efflux in Mycobacterium tuberculosis

Remm, S., Earp, J. C., Dick, T., Dartois, V. A., & Seeger, M. A. (2021) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuab050 · Cited by 76 · see citing works

Methanobactins: Maintaining copper homeostasis in methanotrophs and beyond

Kenney, G. E., & Rosenzweig, A. C. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.tm117.000185 · Cited by 72 · see citing works

New antibiotics from Nature’s chemical inventory

Wencewicz, T. A. (2016) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2016.09.014 · Cited by 69 · see citing works

Transporters Involved in the Biogenesis and Functionalization of the Mycobacterial Cell Envelope

Jackson, M., Stevens, C. M., Zhang, L., Zgurskaya, H. I., & Niederweis, M. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00869 · Cited by 68 · see citing works

Iron acquisition strategies in mycobacteria

Fang, Z., Sampson, S. L., Warren, R. M., van Pittius, N. C. G., & Newton-Foot, M. (2015) · Tuberculosis · doi:10.1016/j.tube.2015.01.004 · Cited by 73 · see citing works

Sideromycins as Pathogen-Targeted Antibiotics

Wencewicz, T. A., & Miller, M. J. (2017) · Topics in medicinal chemistry · doi:10.1007/7355_2017_19 · Cited by 63 · see citing works

Fimsbactin and Acinetobactin Compete for the Periplasmic Siderophore Binding Protein BauB in Pathogenic Acinetobacter baumannii

Bohac, T. J., Fang, L., Giblin, D. E., & Wencewicz, T. A. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.8b01051 · Cited by 61 · see citing works

MmpS5/MmpL5 as an efflux pump in Mycobacterium species

Briffotaux, J., Huang, W., Wang, X., & Gicquel, B. (2017) · Tuberculosis · doi:10.1016/j.tube.2017.08.001 · Cited by 59 · see citing works

Methanobactins: from genome to function

Dassama, L. M. K., Kenney, G. E., & Rosenzweig, A. C. (2016) · Metallomics · doi:10.1039/c6mt00208k · Cited by 59 · see citing works

Cholesterol-dependent transcriptome remodeling reveals new insight into the contribution of cholesterol to Mycobacterium tuberculosis pathogenesis

Pawełczyk, J., Brzostek, A. M., Minias, A. E., Płociński, P., Rumijowska-Galewicz, A., Strapagiel, D., Zakrzewska‐Czerwińska, J., & Dziadek, J. (2021) · Scientific Reports · doi:10.1038/s41598-021-91812-0 · Cited by 55 · see citing works

Lipidomic Analysis Links Mycobactin Synthase K to Iron Uptake and Virulence in M. tuberculosis

Madigan, C. A., Martinot, A. J., Wei, J.-R., Madduri, A. V. R., Cheng, T., Young, D. C., Layre, E., Murry, J. P., Rubin, E. J., & Moody, D. B. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004792 · Cited by 52 · see citing works

PPE37 Is Essential for Mycobacterium tuberculosis Heme-Iron Acquisition (HIA), and a Defective PPE37 in Mycobacterium bovis BCG Prevents HIA

Tullius, M. V., Nava, S., & Horwitz, M. A. (2018) · Infection and Immunity · doi:10.1128/iai.00540-18 · Cited by 51 · see citing works

Regulation of Three Virulence Strategies of Mycobacterium tuberculosis: A Success Story

Zondervan, N. A., van Dam, J. C. J., Schaap, P. J., dos Santos, V. A. P. M., & Diez, M. S. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020347 · Cited by 48 · see citing works

Genome-wide Phenotypic Profiling Identifies and Categorizes Genes Required for Mycobacterial Low Iron Fitness

Dragset, M. S., Ioerger, T. R., Zhang, Y. J., Mærk, M., Ginbot, Z., Sacchettini, J. C., Flo, T. H., Rubin, E. J., & Steigedal, M. (2019) · Scientific Reports · doi:10.1038/s41598-019-47905-y · Cited by 49 · see citing works

Microbial siderophore-based iron assimilation and therapeutic applications

Li, K., Chen, W., & Bruner, S. D. (2016) · BioMetals · doi:10.1007/s10534-016-9935-3 · Cited by 51 · see citing works

Virtual Screening, pharmacophore development and structure based similarity search to identify inhibitors against IdeR, a transcription factor of Mycobacterium tuberculosis

Rohilla, A., Khare, G., & Tyagi, A. K. (2017) · Scientific Reports · doi:10.1038/s41598-017-04748-9 · Cited by 47 · 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

The Iron Response of Mycobacterium tuberculosis and Its Implications for Tuberculosis Pathogenesis and Novel Therapeutics

Rodríguez, G. M., Sharma, N., Biswas, A. K., & Sharma, N. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.876667 · Cited by 44 · see citing works

Iron Supplementation Therapy, A Friend and Foe of Mycobacterial Infections?

Agoro, R., & Mura, C. (2019) · Pharmaceuticals · doi:10.3390/ph12020075 · Cited by 41 · see citing works

Drivers and sites of diversity in the DNA adenine methylomes of 93 Mycobacterium tuberculosis complex clinical isolates

Modlin, S. J., Conkle-Gutierrez, D., Kim, C., Mitchell, S. N., Morrissey, C., Weinrick, B. C., Jacobs, W. R., Ramirez-Busby, S. M., Hoffner, S. E., & Valafar, F. (2020) · eLife · doi:10.7554/elife.58542 · Cited by 40 · see citing works

Trace metal elements: a bridge between host and intestinal microorganisms

Ma, Y., Fei, Y., Ding, S., Jiang, H., Fang, J. Q., & Liu, G. (2023) · Science China Life Sciences · doi:10.1007/s11427-022-2359-4 · Cited by 37 · see citing works

Mycobacterial siderophore: A review on chemistry and biology of siderophore and its potential as a target for tuberculosis

Patel, K. N., Butala, S., Khan, T. A., Suvarna, V., Sherje, A. P., & Dravyakar, B. R. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.08.030 · Cited by 36 · see citing works

A periplasmic cinched protein is required for siderophore secretion and virulence of Mycobacterium tuberculosis

Zhang, L., Kent, J. E., Whitaker, M., Young, D. C., Herrmann, D., Aleshin, A. E., Ko, Y., Cingolani, G., Saad, J. S., Moody, D. B., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-29873-6 · Cited by 35 · see citing works

Structure–function studies of acinetobactin analogs

Shapiro, J. A., & Wencewicz, T. A. (2017) · Metallomics · doi:10.1039/c7mt00064b · Cited by 34 · see citing works

Role of the Mycobacterium tuberculosis ESX-4 Secretion System in Heme Iron Utilization and Pore Formation by PPE Proteins

Sankey, N., Merrick, H., Singh, P., Rogers, J., Reddi, A. R., Hartson, S. D., & Mitra, A. (2023) · mSphere · doi:10.1128/msphere.00573-22 · Cited by 32 · see citing works

Synthesis and Pharmacokinetic Evaluation of Siderophore Biosynthesis Inhibitors forMycobacterium tuberculosis

Nelson, K. M., Viswanathan, K., Dawadi, S., Duckworth, B. P., Boshoff, H. I., Barry, C. E., & Aldrich, C. C. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00391 · Cited by 33 · see citing works

Iron homeostasis in Mycobacterium tuberculosis is essential for persistence

Pandey, M., Talwar, S., Bose, S., & Pandey, A. K. (2018) · Scientific Reports · doi:10.1038/s41598-018-35012-3 · Cited by 32 · see citing works

Iron Acquisition Mechanisms: Promising Target Against Mycobacterium tuberculosis

Hameed, S., Pal, R., & Fatima, Z. (2015) · The Open Microbiology Journal · doi:10.2174/1874285801509010091 · Cited by 29 · see citing works

Physicochemical properties and Mycobacterium tuberculosis transporters: keys to efficacious antitubercular drugs?

Fullam, E., & Young, R. J. (2020) · RSC Medicinal Chemistry · doi:10.1039/d0md00265h · Cited by 27 · see citing works

Phospholipid homeostasis, membrane tenacity and survival of Mtb in lipid rich conditions is determined by MmpL11 function

Bothra, A., Arumugam, P., Panchal, V., Menon, D., Srivastava, S., Shankaran, D., Nandy, A., Jaisinghani, N., Singh, A., Gokhale, R., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-26710-z · Cited by 22 · see citing works

Mycobacterium marinum produces distinct mycobactin and carboxymycobactin siderophores to promote growth in broth and phagocytes

Knobloch, P., Koliwer‐Brandl, H., Arnold, F. M., Hanna, N., Gonda, I., Adenau, S., Personnic, N., Barisch, C., Seeger, M. A., Soldati, T., et al. (2020) · Cellular Microbiology · doi:10.1111/cmi.13163 · Cited by 27 · see citing works

Iron Acquisition in Mycobacterium avium subsp. paratuberculosis

Wang, J., Moolji, J., Dufort, A., Staffa, A., Domenech, P., Reed, M. B., & Behr, M. A. (2015) · Journal of Bacteriology · doi:10.1128/jb.00922-15 · Cited by 25 · see citing works

A multi-targeting pre-clinical candidate against drug-resistant tuberculosis

Kaur, P., Potluri, V. K., Ahuja, V. K., Naveenkumar, C. N., Krishnamurthy, R. V., Gangadharaiah, S. T., Shivarudraiah, P., Eswaran, S., Nirmal, C. R., Balasubramanian, M., et al. (2021) · Tuberculosis · doi:10.1016/j.tube.2021.102104 · Cited by 25 · see citing works

Deciphering the Proteomic Landscape of Mycobacterium tuberculosis in Response to Acid and Oxidative Stresses

Choudhary, E., Sharma, R., Pal, P., & Agarwal, N. (2022) · ACS Omega · doi:10.1021/acsomega.2c03092 · Cited by 23 · see citing works

Dynamin‐like proteins mediate extracellular vesicle secretion in Mycobacterium tuberculosis

Gupta, S., Bhagavathula, M., Sharma, V., Sharma, N., Sharma, N., Biswas, A. K., Palacios, A., Salgueiro, V. C., Lavín, J. L., Dogra, N., et al. (2023) · EMBO Reports · doi:10.15252/embr.202255593 · Cited by 25 · see citing works

Siderophore transport by MmpL5-MmpS5 protein complex in Mycobacterium tuberculosis

Sandhu, P., & Akhter, Y. (2017) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2017.02.013 · Cited by 25 · see citing works

Mycobacterium tuberculosis Reporter Strains as Tools for Drug Discovery and Development

Abramovitch, R. B. (2018) · IUBMB Life · doi:10.1002/iub.1862 · Cited by 25 · see citing works

Structure and Mechanism of the Siderophore-Interacting Protein from the Fuscachelin Gene Cluster of Thermobifida fusca

Li, K., Chen, W., & Bruner, S. D. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00354 · Cited by 25 · see citing works

Mycobacterium tuberculosis Binds Human Serum Amyloid A, and the Interaction Modulates the Colonization of Human Macrophages and the Transcriptional Response of the Pathogen

Kawka, M., Brzostek, A. M., Dzitko, K., Kryczka, J. M., Bednarek, R., Płocińska, R., Płociński, P., Strapagiel, D., Gatkowska, J. M., Dziadek, J., et al. (2021) · Cells · doi:10.3390/cells10051264 · Cited by 24 · see citing works

Intricate link between siderophore secretion and drug efflux in Mycobacterium tuberculosis

Meikle, V., Zhang, L., & Niederweis, M. (2023) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01629-22 · Cited by 24 · see citing works

Transport mechanism of Mycobacterium tuberculosis MmpL/S family proteins and implications in pharmaceutical targeting

Ma, S., Huang, Y., Xie, F., Gong, Z., Zhang, Y., Stojkoska, A., & Xie, J. (2019) · Biological Chemistry · doi:10.1515/hsz-2019-0326 · Cited by 24 · see citing works

Expression Dysregulation as a Mediator of Fitness Costs in Antibiotic Resistance

Trauner, A., Banaei‐Esfahani, A., Gygli, S. M., Warmer, P., Feldmann, J., Zampieri, M., Borrell, S., Collins, B. C., Beisel, C., Aebersold, R. H., et al. (2021) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00504-21 · Cited by 24 · see citing works

Approaches for targeting the mycobactin biosynthesis pathway for novel anti-tubercular drug discovery: where we stand

Shyam, M., Shilkar, D., Rakshit, G., & Jayaprakash, V. (2022) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2022.2077328 · Cited by 23 · see citing works

A reevaluation of iron binding by Mycobactin J

McQueen, C. F., & Groves, J. T. (2018) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-018-1592-2 · Cited by 22 · see citing works

Intracellular accumulation of staphylopine impairs the fitness of Staphylococcus aureus cntE mutant

Chen, C., & Hooper, D. C. (2019) · FEBS Letters · doi:10.1002/1873-3468.13396 · Cited by 22 · see citing works

Intracellular Accumulation of Staphylopine Can Sensitize Staphylococcus aureus to Host-Imposed Zinc Starvation by Chelation-Independent Toxicity

Grim, K. P., Radin, J. N., Solórzano, P. K. P., Morey, J. R., Frye, K. A., Ganio, K., Neville, S. L., McDevitt, C. A., & Kehl‐Fie, T. E. (2020) · Journal of Bacteriology · doi:10.1128/jb.00014-20 · Cited by 22 · see citing works

Transcriptomic responses to antibiotic exposure in Mycobacterium tuberculosis

Poonawala, H., Zhang, Y., Kuchibhotla, S., Green, A. G., Cirillo, D. M., Marco, F. D., Spitlaeri, A., Miotto, P., & Farhat, M. R. (2024) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01185-23 · Cited by 20 · see citing works

Structural basis of siderophore export and drug efflux by Mycobacterium tuberculosis

Earp, J. C., Garaeva, A. A., Meikle, V., Niederweis, M., & Seeger, M. A. (2025) · Nature Communications · doi:10.1038/s41467-025-56888-6 · Cited by 20 · see citing works

Verapamil and its metabolite norverapamil inhibit the Mycobacterium tuberculosis MmpS5L5 efflux pump to increase bedaquiline activity

Fountain, A. J., Waller, N. J. E., Cheung, C., Jowsey, W. J., Chrisp, M. T., Troll, M. A., Edelstein, P. H., Cook, G. M., McNeil, M. B., & Ramakrishnan, L. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2426827122 · Cited by 20 · see citing works

Mycobactin Analogues with Excellent Pharmacokinetic Profile Demonstrate Potent Antitubercular Specific Activity and Exceptional Efflux Pump Inhibition

Shyam, M., Verma, H., Bhattacharje, G., Mukherjee, P., Singh, S., Kamilya, S., Jalani, P., Das, S., Dasgupta, A., Mondal, A., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01349 · Cited by 20 · see citing works

Microbial Siderophores: A New Insight on Healthcare Applications

Mayegowda, S. B., & Gadilingappa, M. N. (2025) · BME Frontiers · doi:10.34133/bmef.0112 · Cited by 18 · see citing works

Mycobacterium tuberculosis: Surviving and Indulging in an Unwelcoming Host

Mishra, A., & Surolia, A. (2018) · IUBMB Life · doi:10.1002/iub.1882 · Cited by 17 · see citing works

Targeting Mycobacterium tuberculosis iron-scavenging tools: a recent update on siderophores inhibitors

Kumar, G., & Adhikrao, P. A. (2023) · RSC Medicinal Chemistry · doi:10.1039/d3md00201b · Cited by 16 · see citing works

Intercellular communication and social behaviors in mycobacteria

Boopathi, S., Ramasamy, S., Haridevamuthu, B., Murugan, R., Veerabadhran, M., Jia, A., & Arockiaraj, J. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.943278 · Cited by 15 · see citing works

Stealing Survival: Iron Acquisition Strategies of Mycobacterium tuberculosis.

Shankar, G., & Akhter, Y. (2024) · Biochimie · doi:10.1016/j.biochi.2024.06.006 · Cited by 12 · see citing works

The mycobacterial ABC transporter IrtAB employs a membrane-facing crevice for siderophore-mediated iron uptake

Gonda, I., Sorrentino, S., Galazzo, L., Lichti, N. P., Arnold, F. M., Mehdipour, A. R., Bordignon, E., & Seeger, M. A. (2025) · Nature Communications · doi:10.1038/s41467-024-55136-7 · Cited by 16 · see citing works

Microbial Siderophores in Metal Detoxification and Therapeutics: Recent Prospective and Applications

Sharma, R., Bhardwaj, R., Gautam, V., Kohli, S. K., Kaur, P., Bali, R. S., Saini, P., Thukral, A. K., Arora, S., & Vig, A. P. (2018) · Microorganisms for sustainability · doi:10.1007/978-981-10-5514-0_15 · Cited by 14 · see citing works

Kinetic Analyses of the Siderophore Biosynthesis Inhibitor Salicyl-AMS and Analogues as MbtA Inhibitors and Antimycobacterial Agents

Bythrow, G. V., Mohandas, P., Güney, T., Standke, L. C., Germain, G. A., Lu, X., Ji, C. Y., Levendosky, K., Chavadi, S. S., Tan, D. S., et al. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b01153 · Cited by 13 · see citing works

A quorum-sensing regulatory cascade for siderophore-mediated iron homeostasis in Chromobacterium violaceum

Batista, B. B., de Lima, V. M., Picinato, B. A., Koide, T., & Neto, J. F. D. S. (2024) · mSystems · doi:10.1128/msystems.01397-23 · Cited by 14 · see citing works

A trans -Translation Inhibitor is Potentiated by Zinc and Kills Mycobacterium tuberculosis and Nontuberculous Mycobacteria

Varshney, A., Jia, Z., Howe, M. D., Keiler, K. C., & Baughn, A. D. (2025) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.4c00963 · Cited by 12 · see citing works

In Silico Drug Repurposing Studies for the Discovery of Novel Salicyl-AMP Ligase (MbtA)Inhibitors

Rakshit, G., Biswas, A., & Jayaprakash, V. (2023) · Pathogens · doi:10.3390/pathogens12121433 · Cited by 8 · see citing works

Dynamin-like proteins are essential for vesicle biogenesis in Mycobacterium tuberculosisPreprint

Gupta, S., Palacios, A., Khataokar, A., Weinrick, B. C., Lavín, J. L., Sampedro, L., Gil‐Carton, D., Anguíta, J., Menendez, M. C., García, M. J. G., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.01.14.906362 · Cited by 10 · see citing works

Toward Mycobacterium tuberculosis Virulence Inhibition: Beyond Cell Wall

Котлярова, М. С., Shumkov, M. S., & Гончаренко, А. В. (2024) · Microorganisms · doi:10.3390/microorganisms13010021 · Cited by 7 · see citing works

Petrobactin Is Exported from Bacillus anthracis by the RND-Type Exporter ApeX

Hagan, A. K., Tripathi, A., Berger, D., Sherman, D. H., & Hanna, P. C. (2017) · mBio · doi:10.1128/mbio.01238-17 · Cited by 8 · see citing works

The structure of Mycobacterium thermoresistibile MmpS5 reveals a conserved disulfide bond across mycobacteria

Cuthbert, B. J., Mendoza, J., de Miranda, R., Papavinasasundaram, K. G., Sassetti, C. M., & Goulding, C. W. (2024) · Metallomics · doi:10.1093/mtomcs/mfae011 · Cited by 6 · see citing works

Mycobacterium tuberculosis adaptation to host environment

Banerjee, A., Sengupta, S., Nandanwar, N., Pandey, M., Tripathi, D., Pandey, S., Kumar, A., & Peddireddy, V. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-91806-0.00005-9 · Cited by 4 · see citing works

Predictors of Change in the Anemia Status Among Pulmonary Tuberculosis Patients Following Anti-tuberculosis Treatment in Puducherry, India

Jovita, L., Sarkar, S., Basu, D., Nanda, N., & Joseph, N. M. (2023) · Cureus · doi:10.7759/cureus.44821 · Cited by 5 · see citing works

The RND efflux system ParXY affects siderophore secretion in Pseudomonas putida KT2440

Stein, N. V., Eder, M., Burr, F., Stoss, S., Holzner, L. J., Kunz, H., & Jung, H. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.02300-23 · Cited by 5 · see citing works

Ratio of Serum Superoxide Dismutase and Whole Blood Glutathione Peroxidase: A Noteworthy Parameter for Tuberculosis Diagnosis

Chattopadhyay, D. K. (2022) · Indian Journal of Medical Biochemistry · doi:10.5005/jp-journals-10054-0193 · Cited by 5 · see citing works

Rôles des sidérophores bactériens et de mammifères dans les interactions hôtes-pathogènes

Vaulont, S., & Schalk, I. J. (2015) · médecine/sciences · doi:10.1051/medsci/20153108014 · Cited by 5 · see citing works

Design of Novel Antimycobacterial Molecule Targeting Shikimate Pathway of Mycobacterium tuberculosis

Sivaranjani, P., Vankadoth, U. N., Nalamolu, R. M., Kumar, K. S., Chiranjeevi, P., Alexander, S. P., & Umamaheswari, A. (2019) · Indian Journal of Pharmaceutical Sciences · doi:10.36468/pharmaceutical-sciences.528 · Cited by 5 · see citing works

Enzymatic Pathway for Kupyaphore Degradation in Mycobacterium tuberculosis: Mechanism of Metal Homeostasis and Turnover

Bhosale, R. S., Chakraborty, A., Wong, T.-Y., Masal, D. P., Choudhury, R., Srivastava, S., Reddy, D. S., Aldrich, C. C., Kamat, S. S., Mohanty, D., et al. (2025) · ACS Chemical Biology · doi:10.1021/acschembio.5c00078 · Cited by 3 · see citing works

Contribution of Proteins to Membrane and Cell Wall Structures in Mycobacterium tuberculosis

Farnia, P., Velayati, A. A., Ghanavi, J., & Farnia, P. (2025) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-96883-9_4 · Cited by 3 · see citing works

Research progress on iron uptake pathways and mechanisms of foodborne microorganisms and their application in the food sector

Cui, F., Fan, R., Wang, D., Li, J., & Li, T. (2023) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2023.2204491 · Cited by 3 · see citing works

Structure and functional analysis of the siderophore periplasmic binding protein from the fuscachelin gene cluster of T hermobifida fusca

Li, K., & Bruner, S. D. (2015) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24959 · Cited by 3 · see citing works

Mycobacterial siderophore: A review on chemistry and biology of siderophore and its potential as a target for tuberculosis

Patel, K. N., Butala, S., Khan, T. A., Suvarna, V., Sherje, A. P., & Dravyakar, B. R. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.08.030 · Cited by 36 · see citing works

Discovery of a Siderophore Export System Essential for Virulence of Mycobacterium tuberculosis

Wells, R. M., Jones, C. M., Xi, Z., Speer, A., Danilchanka, O., Doornbos, K. S., Sun, P., Wu, F., Tian, C., & Niederweis, M. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003120 · Cited by 267 · see citing works

Johannes Geiss (1927-2020)

(2020) · Space Research Today · doi:10.1016/j.srt.2020.03.008

CHARACTERISTICS OF IRON EXCHANGE IN TUBERCULOSIS

qizi, Q. B. S., & Abdug‘afforova, D. (2024) · Zenodo (CERN European Organization for Nuclear Research) · doi:10.5281/zenodo.14270111

Iron Homeostasis in Mycobacterium tuberculosis: Mechanistic Insights into Siderophore-Mediated Iron Uptake

Sritharan, M. (2016) · Journal of Bacteriology · doi:10.1128/jb.00359-16 · Cited by 133 · see citing works