Cited by 939Bacterial Genetics and BiotechnologyMicrobial Natural Products and BiosynthesisIron Metabolism and Disorders

The DOI matches its Crossref record; 80 of the 83 references it cites were found in a registry or an index.

Enterobactin: an archetype for microbial iron transport.

Open access

Raymond, Kenneth N., Dertz, Emily A., Kim, Sanggoo S.·2003·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.0630018100PMC PMC152965

Open this paper in CoChat — free account

Abstract

Bacteria have aggressive acquisition processes for iron, an essential nutrient. Siderophores are small iron chelators that facilitate cellular iron transport. The siderophore enterobactin is a triscatechol derivative of a cyclic triserine lactone. Studies of the chemistry, regulation, synthesis, recognition, and transport of enterobactin make it perhaps the best understood of the siderophore-mediated iron uptake systems, displaying a lot of function packed into this small molecule. However, recent surprises include the isolation of corynebactin, a closely related trithreonine triscatechol derivative lactone first found in Gram-positive bacteria, and the crystal structure of a ferric enterobactin complex of a protein identified as an antibacterial component of the human innate immune system.

Integrity signals

Registry

Crossref · 10.1073/pnas.0630018100

Cites

80 of 80 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Siderophores: Structure and Function of Microbial Iron Transport Compounds
Neilands, J. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.26723 · Cited by 1,652
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
The Neutrophil Lipocalin NGAL Is a Bacteriostatic Agent that Interferes with Siderophore-Mediated Iron Acquisition
Goetz, D. H., Holmes, M. A., Borregaard, N., Bluhm, M. E., Raymond, K. N., & Strong, R. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00708-6 · Cited by 1,355
Self-citation
Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase
Kjeldsen, L., Johnsen, A., Sengeløv, H., & Borregaard, N. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82217-7 · Cited by 1,286
Chemistry and biology of eukaryotic iron metabolism
Aisen, P. (2001) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(01)00063-2 · Cited by 804
Iron and metal regulation in bacteria
Hantke, K. (2001) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(00)00184-3 · Cited by 755
Iron transport in microbes, plants and animals
Danchin, A. (1988) · Biochimie · doi:10.1016/0300-9084(88)90122-8 · Cited by 607
Stoichiometric and site characteristics of the binding of iron to human transferrin
Aisen, P., Leibman, A., & Zweier, J. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)62337-9 · Cited by 601
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
Crystal structure of the outer membrane active transporter FepA from Escherichia coli.
Buchanan (1999) · Nature Structural Biology · doi:10.1038/4931 · Cited by 591

Show all 83 references

Research works printed but not linked: 5

J J Bullen, L C Leigh, H J Rogers Immunology 15, 581–588 (1968).
10.1016/0378-1097(90)90522-R · DOI
J J Bullen, H J Rogers, J E Lewin Immunology 20, 391–406 (1971).
A Trousseau Lect Clin Med 5, 95–117 (1872).
V Braun, K Hantke CRC Handbook of Microbial Iron Chelators, ed G Winkelmann (CRC, Boca Raton, FL), pp. 107–138 (1991).

Sorted by citations

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
Chemistry and biology of siderophores
Hider, R. C., & Kong, X. (2010) · Natural Product Reports · doi:10.1039/b906679a · Cited by 1,722
Bioinspired catecholic chemistry for surface modification
Ye, Q., Zhou, F., & Liu, W. (2011) · Chemical Society Reviews · doi:10.1039/c1cs15026j · Cited by 1,177
Bacterial Iron Sources: From Siderophores to Hemophores
Wandersman, C., & Delepelaire, P. (2004) · Annual Review of Microbiology · doi:10.1146/annurev.micro.58.030603.123811 · Cited by 1,095
Nonribosomal Peptide Synthesis—Principles and Prospects
Süßmuth, R. D., & Mainz, A. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201609079 · Cited by 986
Untitled work
(2011) · Cited by 918
Catechol‐Based Biomimetic Functional Materials
Sedó, J., Saiz‐Poseu, J., Busquè, F., & Ruiz‐Molina, D. (2012) · Advanced Materials · doi:10.1002/adma.201202343 · Cited by 766
Adaptive synergy between catechol and lysine promotes wet adhesion by surface salt displacement
Maier, G. P., Rapp, M. V., Waite, J. H., Israelachvili, J. N., & Butler, A. (2015) · Science · doi:10.1126/science.aab0556 · Cited by 722
Metals to combat antimicrobial resistance
Frei, A., Verderosa, A. D., Elliott, A. G., Zuegg, J., & Blaskovich, M. A. T. (2023) · Nature Reviews Chemistry · doi:10.1038/s41570-023-00463-4 · Cited by 670
Mechanisms of mammalian iron homeostasis
Pantopoulos, K., Porwal, S. K., Tartakoff, A., & Devireddy, L. (2012) · Biochemistry · doi:10.1021/bi300752r · Cited by 598
New roles for bacterial siderophores in metal transport and tolerance
Schalk, I. J., Hannauer, M., & Braud, A. (2011) · Environmental Microbiology · doi:10.1111/j.1462-2920.2011.02556.x · Cited by 602
Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases
Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554
Probiotic Bacteria Reduce Salmonella Typhimurium Intestinal Colonization by Competing for Iron
Deriu, E., Liu, J. Z., Pezeshki, M., Edwards, R. A., Ochoa, R. J., Contreras, H., Libby, S. J., Fang, F. C., & Raffatellu, M. (2013) · Cell Host & Microbe · doi:10.1016/j.chom.2013.06.007 · Cited by 550
The outer mucus layer hosts a distinct intestinal microbial niche
Li, H., Limenitakis, J. P., Fuhrer, T., Geuking, M. B., Lawson, M. A., Wyss, M., Brugiroux, S., Keller, I., Macpherson, J. A., Rupp, S., et al. (2015) · Nature Communications · doi:10.1038/ncomms9292 · Cited by 511
Antimicrobial Resistance of Hypervirulent Klebsiella pneumoniae: Epidemiology, Hypervirulence-Associated Determinants, and Resistance Mechanisms
Lee, C.-R., Lee, J. H., Park, K. S., Jeon, J. H., Kim, Y. B., Cha, C., Jeong, B. C., & Lee, S. H. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00483 · Cited by 496
Microbial Iron Acquisition: Marine and Terrestrial Siderophores
Sandy, M., & Butler, A. (2009) · Chemical Reviews · doi:10.1021/cr9002787 · Cited by 511
The siderophore-producing bacterium, Bacillus subtilis CAS15, has a biocontrol effect on Fusarium wilt and promotes the growth of pepper
Yu, X. M., Ai, C., Li, X., & Zhou, G. (2010) · European Journal of Soil Biology · doi:10.1016/j.ejsobi.2010.11.001 · Cited by 468
Microbial siderophores: a mini review
Saha, R., Saha, N., Donofrio, R. S., & Bestervelt, L. L. (2012) · Journal of Basic Microbiology · doi:10.1002/jobm.201100552 · Cited by 470
Characterization and Biological Function of the ISOCHORISMATE SYNTHASE2 Gene of Arabidopsis
Garcion, C., Lohmann, A., Lamodière, E., Catinot, J., Buchala, A. J., Dörmann, P., & Métraux, J. (2008) · PLANT PHYSIOLOGY · doi:10.1104/pp.108.119420 · Cited by 435
Neutrophil gelatinase-associated lipocalin as the real-time indicator of active kidney damage
Mori, K., & Nakao, K. (2007) · Kidney International · doi:10.1038/sj.ki.5002165 · Cited by 415
Synthesis, nature and utility of universal iron chelator – Siderophore: A review
Khan, A., Singh, P., & Srivastava, A. (2017) · Microbiological Research · doi:10.1016/j.micres.2017.10.012 · Cited by 430
Beyond iron: non-classical biological functions of bacterial siderophores
Johnstone, T. C., & Nolan, E. M. (2015) · Dalton Transactions · doi:10.1039/c4dt03559c · Cited by 429
Genome sequence of the enterobacterial phytopathogen Erwinia carotovora subsp. atroseptica and characterization of virulence factors
Bell, K. S., Sebaihia, M., Pritchard, L., Holden, M. T. G., Hyman, L. J., Holeva, M. C., Thomson, N. R., Bentley, S. D., Churcher, L. J. C., Mungall, K., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402424101 · Cited by 408
Nonproteinogenic Amino Acid Building Blocks for Nonribosomal Peptide and Hybrid Polyketide Scaffolds
Walsh, C. T., O’Brien, R. V., & Khosla, C. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201208344 · Cited by 408
Carbapenem-Resistant Klebsiella pneumoniae: Virulence Factors, Molecular Epidemiology and Latest Updates in Treatment Options
Karampatakis, T., Tsergouli, K., & Behzadi, P. (2023) · Antibiotics · doi:10.3390/antibiotics12020234 · Cited by 369
Dichotomy of gingipains action as virulence factors: from cleaving substrates with the precision of a surgeon’s knife to a meat chopper-like brutal degradation of proteins
Guo, Y., Nguyen, K.-A. T., & Potempa, J. (2010) · Periodontology 2000 · doi:10.1111/j.1600-0757.2010.00377.x · Cited by 367
Towards a unifying, systems biology understanding of large-scale cellular death and destruction caused by poorly liganded iron: Parkinson’s, Huntington’s, Alzheimer’s, prions, bactericides, chemical toxicology and others as examples
Kell, D. B. (2010) · Archives of Toxicology · doi:10.1007/s00204-010-0577-x · Cited by 361
New substrates for TonB-dependent transport: do we only see the ‘tip of the iceberg’?
Schauer, K., Rodionov, D. A., & de Reuse, H. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2008.04.012 · Cited by 360
Iron in infection and immunity
Nairz, M., & Weiss, G. (2020) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2020.100864 · Cited by 359
Siderophore uptake in bacteria and the battle for iron with the host; a bird’s eye view
Chu, B. C. H., Garcia-Herrero, A., Johanson, T. H., Krewulak, K. D., Lau, C. K. Y., Peacock, R. S., Slavinskaya, Z., & Vogel, H. J. (2010) · BioMetals · doi:10.1007/s10534-010-9361-x · Cited by 352
Plant Growth-Promoting Soil Bacteria: Nitrogen Fixation, Phosphate Solubilization, Siderophore Production, and Other Biological Activities
Timofeeva, A. M., Galyamova, M. R., & Sedykh, S. E. (2023) · Plants · doi:10.3390/plants12244074 · Cited by 367
The Chemistry of Lanthanides in Biology: Recent Discoveries, Emerging Principles, and Technological Applications
Cotruvo, J. A. (2019) · ACS Central Science · doi:10.1021/acscentsci.9b00642 · Cited by 338
Bacterial Siderophores: Classification, Biosynthesis, Perspectives of Use in Agriculture
Timofeeva, A. M., Galyamova, M. R., & Sedykh, S. E. (2022) · Plants · doi:10.3390/plants11223065 · Cited by 341
How pathogenic bacteria evade mammalian sabotage in the battle for iron
Fischbach, M. A., Lin, H., Liu, D. R., & Walsh, C. T. (2006) · Nature Chemical Biology · doi:10.1038/nchembio771 · Cited by 321
The pathogen-associated iroA gene cluster mediates bacterial evasion of lipocalin 2
Fischbach, M. A., Lin, H., Zhou, L., Yu, Y., Abergel, R. J., Liu, D. R., Raymond, K. N., Wanner, B. L., Strong, R. K., Walsh, C. T., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604636103 · Cited by 319
Self-citation
Gut Microbiota and Iron: The Crucial Actors in Health and Disease
Yilmaz, B., & Li, H. (2018) · Pharmaceuticals · doi:10.3390/ph11040098 · Cited by 317
Structure, activity, synthesis and biosynthesis of aryl-C-glycosides
Bililign, T., Griffith, B. R., & Thorson, J. S. (2005) · Natural Product Reports · doi:10.1039/b407364a · Cited by 306
Biocontrol potentiality of plant growth promoting bacteria (PGPR) - Pseudomonas fluorescens and Bacillus subtilis: A review
Sivasakthi, S., Usharani, G., & Saranraj, P. (2014) · African Journal of Agricultural Research · doi:10.5897/ajar2013.7914 · Cited by 303
A Mammalian Siderophore Synthesized by an Enzyme with a Bacterial Homolog Involved in Enterobactin Production
Devireddy, L. R., Hart, D. O., Goetz, D. H., & Green, M. R. (2010) · Cell · doi:10.1016/j.cell.2010.04.040 · Cited by 295
Coordination Chemistry of Microbial Iron Transport
Raymond, K. N., Allred, B. E., & Sia, A. K. (2015) · Accounts of Chemical Research · doi:10.1021/acs.accounts.5b00301 · Cited by 297
Self-citation
Nutritional iron turned inside out: intestinal stress from a gut microbial perspective
Kortman, G. A. M., Raffatellu, M., Swinkels, D. W., & Tjalsma, H. (2014) · FEMS Microbiology Reviews · doi:10.1111/1574-6976.12086 · Cited by 291
Bacterial survival strategies and responses under heavy metal stress: a comprehensive overview
Pal, A., Bhattacharjee, S., Saha, J., Sarkar, M. P., & Mandal, P. (2021) · Critical Reviews in Microbiology · doi:10.1080/1040841x.2021.1970512 · Cited by 291
Siderophores as drug delivery agents: application of the “Trojan Horse” strategy
Möllmann, U., Heinisch, L., Bauernfeind, A., Köhler, T., & Ankel‐Fuchs, D. (2009) · BioMetals · doi:10.1007/s10534-009-9219-2 · Cited by 275
Recent developments in understanding the iron acquisition strategies of gram positive pathogens
Sheldon, J. R., & Heinrichs, D. E. (2015) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuv009 · Cited by 272
Resistance and survival strategies of Salmonella enterica to environmental stresses
Spector, M. P., & Kenyon, W. J. (2011) · Food Research International · doi:10.1016/j.foodres.2011.06.056 · Cited by 284
Yersiniabactin Is a Virulence Factor for Klebsiella pneumoniae during Pulmonary Infection
Lawlor, M. S., O'Connor, C., & Miller, V. L. (2007) · Infection and Immunity · doi:10.1128/iai.00372-06 · Cited by 255
Pseudomonas syringae pv. actinidiae : a re‐emerging, multi‐faceted, pandemic pathogen
Scortichini, M., Marcelletti, S., Ferrante, P., Petriccione, M., & Firrao, G. (2012) · Molecular Plant Pathology · doi:10.1111/j.1364-3703.2012.00788.x · Cited by 254
Bacterial siderophores: diversity, uptake pathways and applications
Schalk, I. J. (2024) · Nature Reviews Microbiology · doi:10.1038/s41579-024-01090-6 · Cited by 254
New insights into the metal specificity of the Pseudomonas aeruginosa pyoverdine–iron uptake pathway
Braud, A., Hoegy, F., Jezequel, K., Lebeau, T., & Schalk, I. J. (2009) · Environmental Microbiology · doi:10.1111/j.1462-2920.2008.01838.x · Cited by 246
Siderocalin (Lcn 2) Also Binds Carboxymycobactins, Potentially Defending against Mycobacterial Infections through Iron Sequestration
Holmes, M. A., Paulsene, W., Jide, X., Ratledge, C., & Strong, R. K. (2005) · Structure · doi:10.1016/j.str.2004.10.009 · Cited by 246
Synthetic and natural iron chelators: Therapeutic potential and clinical use
Hatcher, H. C., Singh, R. N., Torti, F. M., & Torti, S. V. (2009) · Future Medicinal Chemistry · doi:10.4155/fmc.09.121 · Cited by 242
Polyphenol‐Induced Adhesive Liquid Metal Inks for Substrate‐Independent Direct Pen Writing
Rahim, M. A., Centurion, F., Han, J., Abbasi, R., Mayyas, M., Sun, J., Christoe, M. J., Esrafilzadeh, D., Allioux, F., Ghasemian, M. B., et al. (2020) · Advanced Functional Materials · doi:10.1002/adfm.202007336 · Cited by 243
Copper Stress Affects Iron Homeostasis by Destabilizing Iron-Sulfur Cluster Formation in Bacillus subtilis
Chillappagari, S., Seubert, A., Trip, H., Kuipers, O. P., Marahiel, M. A., & Miethke, M. (2010) · Journal of Bacteriology · doi:10.1128/jb.00058-10 · Cited by 249
Neutrophil gelatinase-associated lipocalin-mediated iron traffic in kidney epithelia
Schmidt-Ott, K. M., Mori, K., Kalandadze, A., Li, J.-Y., Paragas, N., Nicholas, T., Devarajan, P., & Barasch, J. (2006) · Current Opinion in Nephrology & Hypertension · doi:10.1097/01.mnh.0000232886.81142.58 · Cited by 237
Quantitative Metabolomics Reveals an Epigenetic Blueprint for Iron Acquisition in Uropathogenic Escherichia coli
Henderson, J. P., Crowley, J. R., Pinkner, J. S., Walker, J. N., Tsukayama, P., Stamm, W. E., Hooton, T. M., & Hultgren, S. J. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000305 · Cited by 231
Iron-binding properties of plant phenolics and cranberry's bio-effects
Guo, M., Perez, C., Wei, Y., Rapoza, E., Su, G. M., Bou‐Abdallah, F., & Chasteen, N. D. (2007) · Dalton Transactions · doi:10.1039/b705136k · Cited by 227
The shikimate pathway: gateway to metabolic diversity
Shende, V. V., Bauman, K. D., & Moore, B. S. (2024) · Natural Product Reports · doi:10.1039/d3np00037k · Cited by 224
Pyochelin, a siderophore of Pseudomonas aeruginosa: Physicochemical characterization of the iron(iii), copper(ii) and zinc(ii) complexes
Brandel, J., Humbert, N., Elhabiri, M., Schalk, I. J., Mislin, G. L. A., & Albrecht‐Gary, A. (2012) · Dalton Transactions · doi:10.1039/c1dt11804h · Cited by 214
Waging War against UropathogenicEscherichia coli: Winning Back the Urinary Tract
Sivick, K. E., & Mobley, H. L. T. (2009) · Infection and Immunity · doi:10.1128/iai.01000-09 · Cited by 216
The Pseudomonas aeruginosa Pyochelin-Iron Uptake Pathway and Its Metal Specificity
Braud, A., Hannauer, M., Mislin, G. L. A., & Schalk, I. J. (2009) · Journal of Bacteriology · doi:10.1128/jb.00010-09 · Cited by 224
General Overview of Klebsiella pneumonia: Epidemiology and the Role of Siderophores in Its Pathogenicity
Abbas, R., Chakkour, M., Dine, H. Z. E., Obaseki, E., Obeid, S. T., Jezzini, A., Ghssein, G., & Ezzeddine, Z. (2024) · Biology · doi:10.3390/biology13020078 · Cited by 227
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
Role of the Fur Regulon in Iron Transport in Bacillus subtilis
Ollinger, J., Song, K.-B., Antelmann, H., Hecker, M., & Helmann, J. D. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.10.3664-3673.2006 · Cited by 213
Bacterial characteristics of importance for recurrent urinary tract infections caused by Escherichia coli.
Ejrnæs, K. (2011) · PubMed · Cited by 207
Physiological Functions of Bacterial “Multidrug” Efflux Pumps
Henderson, P. J. F., Maher, C., Elbourne, L. D. H., Eijkelkamp, B. A., Paulsen, I. T., & Hassan, K. A. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01226 · Cited by 209
Anthrax pathogen evades the mammalian immune system through stealth siderophore production
Abergel, R. J., Wilson, M. K., Arceneaux, J. E. L., Hoette, T. M., Strong, R. K., Byers, B. R., & Raymond, K. N. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607055103 · Cited by 198
Self-citation
In Vitro Characterization of Salmochelin and Enterobactin Trilactone Hydrolases IroD, IroE, and Fes
Lin, H., Fischbach, M. A., Liu, D. R., & Walsh, C. T. (2005) · Journal of the American Chemical Society · doi:10.1021/ja0522027 · Cited by 197
Genome-Wide Screening of Genes Required for Swarming Motility inEscherichia coliK-12
Inoue, T., Shingaki, R., Hirose, S., Waki, K., Mori, H., & Fukui, K. (2006) · Journal of Bacteriology · doi:10.1128/jb.01294-06 · Cited by 197
Self-Assembly of Focal Point Oligo-catechol Ethylene Glycol Dendrons on Titanium Oxide Surfaces: Adsorption Kinetics, Surface Characterization, and Nonfouling Properties
Gillich, T., Benetti, E. M., Rakhmatullina, E., Konradi, R., Li, W., Zhang, A., Schlüter, A. D., & Textor, M. (2011) · Journal of the American Chemical Society · doi:10.1021/ja202760x · Cited by 196
The evolution of siderophore production as a competitive trait
Niehus, R., Picot, A., Oliveira, N. M., Mitri, S., & Foster, K. R. (2017) · Evolution · doi:10.1111/evo.13230 · Cited by 202
The structure of salmochelins: C-glucosylated enterobactins of Salmonella enterica §
Bister, B., Bischoff, D., NICHOLSON, G. J., Valdebenito, M., Schneider, K., Winkelmann, G., Hantke, K., & Süßmuth, R. D. (2004) · BioMetals · doi:10.1023/b:biom.0000029432.69418.6a · Cited by 188
Adaptive strategies by Southern Ocean phytoplankton to lessen iron limitation: Uptake of organically complexed iron and reduced cellular iron requirements
Strzepek, R. F., Maldonado, M. T., Hunter, K. A., Frew, R. D., & Boyd, P. W. (2011) · Limnology and Oceanography · doi:10.4319/lo.2011.56.6.1983 · Cited by 187
Enterococcal Metabolite Cues Facilitate Interspecies Niche Modulation and Polymicrobial Infection
Keogh, D., Tay, W. H., Ho, Y. Y., Dale, J. L., Chen, S., Umashankar, S., Williams, R. B. H., Chen, S. L., Dunny, G. M., & Kline, K. A. (2016) · Cell Host & Microbe · doi:10.1016/j.chom.2016.09.004 · Cited by 192
Bifunctional antimicrobial conjugates and hybrid antimicrobials
Klahn, P., & Brönstrup, M. (2017) · Natural Product Reports · doi:10.1039/c7np00006e · Cited by 183
TolC Is Involved in Enterobactin Efflux across the Outer Membrane of Escherichia coli
Bleuel, C., Große, C., Taudte, N., Scherer, J., Wesenberg, D., Krauss, G.-J., Nies, D. H., & Grass, G. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.19.6701-6707.2005 · Cited by 180
Bacterial heme-transport proteins and their heme-coordination modes
Tong, Y., & Guo, M. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.10.013 · Cited by 182
Gallium-based anti-infectives: targeting microbial iron-uptake mechanisms
Kelson, A. B., Carnevali, M., & Truong-Le, V. L. (2013) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2013.07.001 · Cited by 181
Untitled work
Krewulak (2011) · doi:10.1139/o10-141 · Cited by 170
Versatile tuning of supramolecular hydrogels through metal complexation of oxidation-resistant catechol-inspired ligands
Menyo, M. S., Hawker, C. J., & Waite, J. H. (2013) · Soft Matter · doi:10.1039/c3sm51824h · Cited by 172
In vitro characterization of IroB, a pathogen-associated C -glycosyltransferase
Fischbach, M. A., Lin, H., Liu, D. R., & Walsh, C. T. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408463102 · Cited by 169
Enterobactin-Mediated Delivery of β-Lactam Antibiotics Enhances Antibacterial Activity against Pathogenic Escherichia coli
Zheng, T., & Nolan, E. M. (2014) · Journal of the American Chemical Society · doi:10.1021/ja503911p · Cited by 167
Fate of ferrisiderophores after import across bacterial outer membranes: different iron release strategies are observed in the cytoplasm or periplasm depending on the siderophore pathways
Schalk, I. J., & Guillon, L. (2013) · Amino Acids · doi:10.1007/s00726-013-1468-2 · Cited by 167
Microbial siderophore – A boon to agricultural sciences
Ghosh, S. K., Bera, T., & Chakrabarty, A. M. (2020) · Biological Control · doi:10.1016/j.biocontrol.2020.104214 · Cited by 173
Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides
Ongpipattanakul, C., Desormeaux, E. K., DiCaprio, A. J., van der Donk, W. A., Mitchell, D. A., & Nair, S. K. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.2c00210 · Cited by 169
Biological inorganic chemistry at the beginning of the 21st century
Gray, H. B. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0730378100 · Cited by 161
The role of iron in host–microbiota crosstalk and its effects on systemic glucose metabolism
Mayneris‐Perxachs, J., Moreno‐Navarrete, J. M., & Fernández‐Real, J. M. (2022) · Nature Reviews Endocrinology · doi:10.1038/s41574-022-00721-3 · Cited by 161
Expression of Virulence Factors by Staphylococcus aureus Grown in Serum
Oogai, Y., Matsuo, M., Hashimoto, M., Kato, F., Sugai, M., & Komatsuzawa, H. (2011) · Applied and Environmental Microbiology · doi:10.1128/aem.05316-11 · Cited by 155
Enzyme Promiscuity: Engine of Evolutionary Innovation
Pandya, C., Farelli, J. D., Dunaway‐Mariano, D., & Allen, K. N. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.572990 · Cited by 158
Hypervirulent K. Pneumoniae Secretes More and More Active Iron-Acquisition Molecules than “Classical” K. Pneumoniae Thereby Enhancing its Virulence
Russo, T. A., Shon, A. S., Beanan, J. M., Olson, R., MacDonald, U., Pomakov, A. O., & Visitacion, M. P. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026734 · Cited by 153
Structure, Function and Binding Selectivity and Stereoselectivity of Siderophore–Iron Outer Membrane Transporters
Schalk, I. J., Mislin, G. L. A., & Brillet, K. (2012) · Current topics in membranes · doi:10.1016/b978-0-12-394390-3.00002-1 · Cited by 163
A Review of Pseudomonas aeruginosa Metallophores: Pyoverdine, Pyochelin and Pseudopaline
Ghssein, G., & Ezzeddine, Z. (2022) · Biology · doi:10.3390/biology11121711 · Cited by 164
Iron Acquisition Systems of Gram-negative Bacterial Pathogens Define TonB-Dependent Pathways to Novel Antibiotics
Klebba, P. E., Newton, S. M. C., Six, D. A., Kumar, A., Yang, T., Nairn, B. L., Munger, C., & Chakravorty, S. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01005 · Cited by 150
Iron Transport-Mediated Drug Delivery: Practical Syntheses and In Vitro Antibacterial Studies of Tris-Catecholate Siderophore–Aminopenicillin Conjugates Reveals Selectively Potent Antipseudomonal Activity
Ji, C. Y., Miller, P. A., & Miller, M. J. (2012) · Journal of the American Chemical Society · doi:10.1021/ja303446w · Cited by 152
Continuous‐cropping tobacco caused variance of chemical properties and structure of bacterial network in soils
Chen, S., Qi, G., Luo, T., Zhang, H., Jiang, Q., Wang, R., & Zhao, X. (2018) · Land Degradation and Development · doi:10.1002/ldr.3167 · Cited by 151
Metagenomic analysis with strain-level resolution reveals fine-scale variation in the human pregnancy microbiomePreprint
Goltsman, D. S. A., Sun, C. L., Proctor, D. M., DiGiulio, D. B., Robaczewska, A., Thomas, B. C., Shaw, G. M., Stevenson, D. K., Holmes, S., Banfield, J. F., et al. (2018) · Genome Research · doi:10.1101/gr.236000.118 · Cited by 149
Pseudomonas syringae pv. actinidiae Draft Genomes Comparison Reveal Strain-Specific Features Involved in Adaptation and Virulence to Actinidia Species
Marcelletti, S., Ferrante, P., Petriccione, M., Firrao, G., & Scortichini, M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027297 · Cited by 147
Structural and Functional Investigation of the Intermolecular Interaction between NRPS Adenylation and Carrier Protein Domains
Sundlov, J. A., Shi, C., Wilson, D. J., Aldrich, C. C., & Gulick, A. M. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.11.013 · Cited by 146
Roles of iron acquisition systems in virulence of extraintestinal pathogenic Escherichia coli: salmochelin and aerobactin contribute more to virulence than heme in a chicken infection model
Gao, Q., Wang, X., Xu, H., Xu, Y., Ling, J., Zhang, D., Gao, S., & Liu, X. (2012) · BMC Microbiology · doi:10.1186/1471-2180-12-143 · Cited by 146
Esterase-Catalyzed Siderophore Hydrolysis Activates an Enterobactin–Ciprofloxacin Conjugate and Confers Targeted Antibacterial Activity
Neumann, W., Sassone‐Corsi, M., Raffatellu, M., & Nolan, E. M. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b01042 · Cited by 146
The ins and outs of siderophore mediated iron uptake by extra-intestinal pathogenic Escherichia coli
Garénaux, A., Caza, M., & Dozois, C. M. (2011) · Veterinary Microbiology · doi:10.1016/j.vetmic.2011.05.023 · Cited by 141

Authors: Raymond, K. N., Dertz, E. A., & Kim, S. S.
Affiliations: University of California, Berkeley (US)
ORCID: Raymond, Kenneth N.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2003-03-24
Volume: 100
Issue: 7
Pages: 3584-3588
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.0630018100
PMC: PMC152965
OpenAlex: W1972422447
Cited by: 933
References: 83
Citations by year: 2026: 42 · 2025: 57 · 2024: 55 · 2023: 47 · 2022: 67 · 2021: 46 · 2020: 49 · 2019: 59 · 2018: 50 · 2017: 47 · 2016: 38 · 2015: 38 · 2014: 47 · 2013: 27 · 2012: 45
FWCI: 1.91
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute of Allergy and Infectious Diseases (R01AI011744, AI-11744)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Microbial Natural Products and Biosynthesis
Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Keywords: enterobactin, siderophores, bacterial iron acquisition, iron transport, siderophore biosynthesis, innate immunity, Gram-positive bacteria
MeSH terms: Bacteria, Binding Sites, Carrier Proteins, Enterobactin, Iron, Models, Molecular, Protein Conformation, Protein Structure, Secondary

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

Enterobactin: an archetype for microbial iron transport.

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks