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 accessAbstract
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“Given the low Fe bioavailability in an aqueous environment (free Fe3+ concentration below 10−9 M at pH 7) and the further strict active withholding of Fe within mammalian hosts (free serum Fe concentration of approximately 10−24 M) [9]”
From Host Iron Withholding Demands Siderophore Utilization for Candida glabrata to Survive Macrophage Killing (2011) · cites this paper as [9]
Citations
Cites
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
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-citationIsolation 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
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
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).
Cited by
Sorted by citations
Items 301–400 of 939
Clinical and laboratory insights into the threat of hypervirulent Klebsiella pneumoniae
Han, X., Yao, J., He, J., Liu, H., Jiang, Y., Zhao, D., Shi, Q., Zhou, J., Hu, H., Lan, P., et al. (2024) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2024.107275 · Cited by 43
Walsh, C. T., O’Brien, R. V., & Khosla, C. (2013) · Angewandte Chemie · doi:10.1002/ange.201208344 · Cited by 43
Collins, A. J., Fullmer, M. S., Gogarten, J. P., & Nyholm, S. V. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00123 · Cited by 44
Zajdowicz, S. L. W., Haller, J. C., Krafft, A. E., Hunsucker, S. W., Mant, C. T., Duncan, M. W., Hodges, R. S., Jones, D. N. M., & Holmes, R. K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034591 · Cited by 45
Song, Y., Sun, L., Lin, M., Chen, J., Qi, X., Hu, C., & Fang, J. (2019) · PLoS ONE · doi:10.1371/journal.pone.0211913 · Cited by 43
Zheng, T., & Nolan, E. M. (2015) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2015.02.034 · Cited by 43
Differential Function of Lip Residues in the Mechanism and Biology of an Anthrax Hemophore
Ekworomadu, M., Poor, C. B., Owens, C. P., Balderas, M. A., Fabián, M., Olson, J. S., Murphy, F. V., Balkabasi, E., Honsa, E. S., He, C., et al. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002559 · Cited by 42
Khalil, F., Franzmann, E., Ramcke, J., Dakischew, O., Lips, K. S., Reinhardt, A., Heisig, P., & Maison, W. (2014) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2014.02.022 · Cited by 42
Yokoo, S., Inoue, S., Suzuki, N., Amakawa, N., Matsui, H., Nakagami, H., Takahashi, A., Arai, R., & Katou, S. (2018) · Bioscience Reports · doi:10.1042/bsr20171457 · Cited by 42
Photoactive siderophores: Structure, function and biology
Butler, A., Harder, T., Ostrowski, A. D., & Carrano, C. J. (2021) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2021.111457 · Cited by 44
Speciation of Iron in the Aquatic Environment
Rabajczyk, A., & Namieśnik, J. (2014) · Water Environment Research · doi:10.2175/106143014x13975035525906 · Cited by 42
Fu, Y., Yin, M., Cao, L., Lu, Y., Li, Y., & Zhang, L. (2025) · Communications Biology · doi:10.1038/s42003-025-07687-8 · Cited by 44
Wei, Q., Krysiak, S., Achazi, K., Becherer, T., Noeske, P.-L. M., Paulus, F., Liebe, H., Grunwald, I., Dernedde, J., Hartwig, A., et al. (2014) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2014.08.001 · Cited by 41
Diastereoselective Assembly of Helicates Incorporating a Hexadentate Chiral Scaffold
Constable, E. C., Zhang, G., Housecroft, C. E., Neuburger, M. A., & Zampese, J. A. (2010) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.201000206 · Cited by 41
Tan, L., Tao, Y., Wang, T., Zou, F., Zhang, S., Kou, Q., Niu, A., Chen, Q., Chu, W., Chen, X., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01261 · Cited by 41
Maier, G. P., & Butler, A. (2017) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-017-1451-6 · Cited by 44
DIBI, a 3-hydroxypyridin-4-one chelator iron-binding polymer with enhanced antimicrobial activity
Ang, M. T. C., Gumbau‐Brisa, R., Allan, D. S., McDonald, R., Ferguson, M. J., Holbein, B. E., & Bierenstiel, M. (2018) · MedChemComm · doi:10.1039/c8md00192h · Cited by 41
A Salmochelin S4-Inspired Ciprofloxacin Trojan Horse Conjugate
Sanderson, T. J., Black, C. M., Southwell, J. W., Wilde, E. J., Pandey, A. K., Herman, R., Thomas, G. H., Boros, E., Duhme‐Klair, A., & Routledge, A. (2020) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.0c00568 · Cited by 41
Two Crystal Structures of the Isochorismate Pyruvate Lyase from Pseudomonas aeruginosa
Zaitseva, J., Lu, J.-P., Olechoski, K. L., & Lamb, A. L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605470200 · Cited by 41
Oxo-iron clusters in a bacterial iron-trafficking protein: new roles for a conserved motif
Zhu, H., Alexeev, D. G., Hunter, D. J. B., Campopiano, D. J., & Sadler, P. J. (2003) · Biochemical Journal · doi:10.1042/bj20031283 · Cited by 41
Li, N., Zhang, C., Li, B., Liu, X., Huang, Y., Xu, S., & Gu, L. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.316034 · Cited by 40
Reitz, Z. L., Sandy, M., & Butler, A. (2017) · Metallomics · doi:10.1039/c7mt00111h · Cited by 40
Rapid Identification of Pseudomonas spp. via Raman Spectroscopy Using Pyoverdine as Capture Probe
Pahlow, S., Stöckel, S., Pollok, S., Cialla‐May, D., Rösch, P., Weber, K., & Popp, J. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b02829 · Cited by 39
Bailey, D. C., Drake, E. J., Grant, T. D., & Gulick, A. M. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00409 · Cited by 40
Pini, E., Poli, G., Tuccinardi, T., Chiarelli, L. R., Mori, M., Gelain, A., Costantino, L., Villa, S., Meneghetti, F., & Barlocco, D. (2018) · Molecules · doi:10.3390/molecules23071506 · Cited by 39
Present and Future of Siderophore-Based Therapeutic and Diagnostic Approaches in Infectious Diseases
Tonziello, G., Caraffa, E., Pinchera, B., Granata, G., & Petrosillo, N. (2019) · Infectious Disease Reports · doi:10.4081/idr.2019.8208 · Cited by 40
Zhou, Z., Lai, J. R., & Walsh, C. T. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2006.06.011 · Cited by 39
Structural Characterization of Enterobactin Hydrolase IroE,
Larsen, N., Lin, H., Wei, R. R., Fischbach, M. A., & Walsh, C. T. (2006) · Biochemistry · doi:10.1021/bi060950i · Cited by 39
Microbial ligand coordination: Consideration of biological significance
Springer, S. D., & Butler, A. (2015) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2015.03.013 · Cited by 40
Shields‐Cutler, R. R., Crowley, J. R., Miller, C. D., Stapleton, A. E., Cui, W., & Henderson, J. P. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.759183 · Cited by 38
Kinetic and Inhibition Studies of Dihydroxybenzoate-AMP Ligase from Escherichia coli
Sikora, A. L., Wilson, D. J., Aldrich, C. C., & Blanchard, J. S. (2010) · Biochemistry · doi:10.1021/bi100350c · Cited by 38
He, R., Zhang, J., Shao, Y., Gu, S., Song, C., Qian, L., Yin, W., & Li, Z. (2023) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1011100 · Cited by 37
Engineering chemical interactions in microbial communities
Kenny, D. J., & Balskus, E. P. (2017) · Chemical Society Reviews · doi:10.1039/c7cs00664k · Cited by 40
Paczosa, M. K., Silver, R. J., McCabe, A. L., Tai, A., McLeish, C. H., Lazinski, D. W., & Mecsas, J. C. (2020) · Infection and Immunity · doi:10.1128/iai.00034-20 · Cited by 40
Ahire, J. J., Patil, K. P., Chaudhari, B. L., & Chincholkar, S. B. (2011) · Food Chemistry · doi:10.1016/j.foodchem.2010.12.126 · Cited by 37
Li, Y., Zhang, Y., Sun, X., Wu, Y., Yan, Z., Ju, X., Huang, Y., Zhou, H., Wang, Z., Wang, S., et al. (2024) · Genome Medicine · doi:10.1186/s13073-024-01310-x · Cited by 37
Virzì, G. M., Clementi, A., de Cal, M., Cruz, D. N., & Ronco, C. (2013) · Blood Purification · doi:10.1159/000346100 · Cited by 36
Post-translational Acetylation of MbtA Modulates Mycobacterial Siderophore Biosynthesis
Vergnolle, O., Xu, H., Tufariello, J. M., Favrot, L., Malek, A., Jacobs, W. R., & Blanchard, J. S. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.744532 · Cited by 36
Endophytic Actinobacteria: Nitrogen Fixation, Phytohormone Production, and Antibiosis
Swarnalakshmi, K., Senthilkumar, M., & Ramakrishnan, B. (2016) · Springer eBooks · doi:10.1007/978-981-10-0707-1_8 · Cited by 36
Johnstone, T. C., & Nolan, E. M. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b09375 · Cited by 36
Genes Involved in the Biosynthesis and Transport of Acinetobactin inAcinetobacter baumannii
Hasan, T., Choi, C. H., & Oh, M. H. (2015) · Genomics & Informatics · doi:10.5808/gi.2015.13.1.2 · Cited by 36
Bacillus cereus iron uptake protein fishes out an unstable ferric citrate trimer
Fukushima, T., Sia, A. K., Allred, B. E., Nichiporuk, R. V., Zhou, Z., Andersen, U. N., & Raymond, K. N. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1210131109 · Cited by 36
Self-citationAssembly of a Tetranuclear Host with a Tris(benzene‐ o ‐dithiolato) Ligand
Birkmann, B., Fröhlich, R., & Hahn, F. E. (2009) · Chemistry - A European Journal · doi:10.1002/chem.200901443 · Cited by 36
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
Novel Insights into Siderophore Formation in Myxobacteria
Gaitatzis, N., Kunze, B., & Müller, R. (2005) · ChemBioChem · doi:10.1002/cbic.200400206 · Cited by 36
Tong, Y., & Guo, M. (2007) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-007-0226-x · Cited by 36
Motz, R. N., Guo, C., Sargun, A., Walker, G. T., Sassone‐Corsi, M., Raffatellu, M., & Nolan, E. M. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.3c14490 · Cited by 35
War-Fe-re: iron at the core of fungal virulence and host immunity
Nevitt, T. (2011) · BioMetals · doi:10.1007/s10534-011-9431-8 · Cited by 35
Civciristov, S., Ellisdon, A. M., Suderman, R., Pon, C. K., Evans, B. A., Kleifeld, O., Charlton, S. J., Hlavacek, W. S., Canals, M., & Halls, M. L. (2018) · Science Signaling · doi:10.1126/scisignal.aan1188 · Cited by 38
Cho, H., Song, E., Heu, S., Baek, J., Lee, Y.-K., Lee, S., Lee, S., Park, D. S., Lee, T., Kim, J.-G., et al. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.00506 · Cited by 35
Structure, function, and regulation of thioesterases
Swarbrick, C. M. D., Nanson, J. D., Patterson, E. I., & Forwood, J. K. (2020) · Progress in Lipid Research · doi:10.1016/j.plipres.2020.101036 · Cited by 36
Naikare, H. K., Butcher, J., Flint, A., Xu, J., Raymond, K. N., & Stintzi, A. (2013) · Metallomics · doi:10.1039/c3mt20254b · Cited by 37
Self-citationRole of Siderophores in Crop Improvement
Desai, A. J., & Archana, G. (2011) · Springer eBooks · doi:10.1007/978-3-642-21061-7_6 · Cited by 36
Klebsiella pneumoniae liver abscesses: pathogenesis, treatment, and ongoing challenges
Angeles-Solano, M., Tabashsum, Z., Chen, L., & Rowe, S. E. (2025) · Infection and Immunity · doi:10.1128/iai.00508-24 · Cited by 36
Soe, C. Z., Telfer, T. J., Levina, A., Lay, P. A., & Codd, R. (2015) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2015.12.008 · Cited by 35
Dauner, M., & Skerra, A. (2019) · ChemBioChem · doi:10.1002/cbic.201900564 · Cited by 35
Weakland, D. R., Smith, S. N., Bell, B. A., Tripathi, A., & Mobley, H. L. T. (2020) · Infection and Immunity · doi:10.1128/iai.00117-20 · Cited by 34
Fortinez, C. M., Bloudoff, K., Harrigan, C., Sharon, I., Strauss, M., & Schmeing, T. M. (2022) · Nature Communications · doi:10.1038/s41467-022-28221-y · Cited by 34
Interleukin-8 Secretion in Response to Aferric Enterobactin Is Potentiated by Siderocalin
Nelson, A. L., Ratner, A. J., Barasch, J. M., & Weiser, J. N. (2007) · Infection and Immunity · doi:10.1128/iai.01719-06 · Cited by 34
Gerwien, F., Safyan, A., Wisgott, S., Brunke, S., Kasper, L., & Hube, B. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.01055 · Cited by 33
Lipocalin-2: A Nurturer of Tumor Progression and a Novel Candidate for Targeted Cancer Therapy
Živalj, M., Ginderachter, J. A. V., & Stijlemans, B. (2023) · Cancers · doi:10.3390/cancers15215159 · Cited by 35
Wise, D. J., Greenway, T., Li, M. H., Camus, A. C., & Robinson, E. H. (2008) · Journal of Aquatic Animal Health · doi:10.1577/h07-008.1 · Cited by 33
From Homodimer to Heterodimer and Back: Elucidating the TonB Energy Transduction Cycle
Gresock, M. G., Kastead, K. A., & Postle, K. (2015) · Journal of Bacteriology · doi:10.1128/jb.00484-15 · Cited by 33
Iron Regulates Expression of Bacillus cereus Hemolysin II via Global Regulator Fur
Sineva, E. V., Shadrin, A. M., Rodikova, E. A., Andreeva‐Kovalevskaya, Z. I., Protsenko, A. S., Mayorov, S. G., Galaktionova, D. Y., Magelky, E. M., & Solonin, A. S. (2012) · Journal of Bacteriology · doi:10.1128/jb.00199-12 · Cited by 33
Experimental Methods for Evaluating the Bacterial Uptake of Trojan Horse Antibacterials
Southwell, J. W., Black, C. M., & Duhme‐Klair, A. (2020) · ChemMedChem · doi:10.1002/cmdc.202000806 · Cited by 33
Sargun, A., Johnstone, T. C., Zhi, H., Raffatellu, M., & Nolan, E. M. (2021) · Chemical Science · doi:10.1039/d0sc04337k · Cited by 33
Siderophores: Chemical tools for precise antibiotic delivery
Rodríguez, D., & González‐Bello, C. (2023) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2023.129282 · Cited by 33
Pi, H., & Helmann, J. D. (2018) · mBio · doi:10.1128/mbio.01451-18 · Cited by 34
Upritchard, H. G., Yang, J., Bremer, P. J., Lamont, I. L., & McQuillan, A. J. (2011) · Langmuir · doi:10.1021/la202352j · Cited by 33
Gerner, R. R., Hossain, S., Sargun, A., Siada, K., Norton, G. J., Zheng, T., Neumann, W., Nuccio, S., Nolan, E. M., & Raffatellu, M. (2022) · mBio · doi:10.1128/mbio.02184-22 · Cited by 32
Chu, B. C. H., Otten, R., Krewulak, K. D., Mulder, F. A. A., & Vogel, H. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.564021 · Cited by 32
Caza, M., Garénaux, A., Lepine, F. L., & Dozois, C. M. (2015) · Molecular Microbiology · doi:10.1111/mmi.13059 · Cited by 32
Lee, A. A., Chen, Y. S., Ekalestari, E., Ho, S., Hsu, N., Kuo, T., & Wang, T. A. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201603921 · Cited by 32
Guo, J., Hu, X., Gao, Z., Li, G., Fu, F., Shang, X., Liang, Z., & Shan, Y. (2021) · Food Research International · doi:10.1016/j.foodres.2021.110274 · Cited by 32
Singh, V., Muthuramalingam, K., Kim, Y., Park, S., Kim, S. H., Lee, J., Hyun, C. L., Unno, T., & Cho, M. (2021) · Applied Biological Chemistry · doi:10.1186/s13765-020-00572-4 · Cited by 32
Self-citationThe impact of iron on Listeria monocytogenes; inside and outside the host
McLaughlin, H. P., Hill, C., & Gahan, C. G. M. (2010) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2010.10.005 · Cited by 33
Uhrynowski, W., Dębiec-Andrzejewska, K., Skłodowska, A., & Drewniak, Ł. (2017) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2017.04.137 · Cited by 32
Fighting Staphylococcus epidermidis Biofilm-Associated Infections: Can Iron Be the Key to Success?
Oliveira, F., Rohde, H., Vilanova, M., & Cerca, N. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.798563 · Cited by 31
Siderophore profiling of co-habitating soil bacteria by ultra-high resolution mass spectrometry
Boiteau, R. M., Fansler, S. J., Farris, Y., Shaw, J., Koppenaal, D., Paša‐Tolić, L., & Jansson, J. K. (2018) · Metallomics · doi:10.1039/c8mt00252e · Cited by 34
Klebsiella pneumoniae Infections and Antimicrobial Drug Resistance
Ashwath, P., Kotian, A., Deekshit, V. K., Prarthana, J., & Sannejal, A. D. (2020) · Springer eBooks · doi:10.1007/978-981-15-1695-5_12 · Cited by 31
Dutta, S., Biswas, P., Flörke, Ü., & Nag, K. (2010) · Inorganic Chemistry · doi:10.1021/ic100666t · Cited by 31
Harrington, J. M., Chittamuru, S., Dhungana, S., Jacobs, H. K., Gopalan, A. S., & Crumbliss, A. L. (2010) · Inorganic Chemistry · doi:10.1021/ic902595c · Cited by 30
Degradation of 2,3-Dihydroxybenzoate by a Novel meta -Cleavage Pathway
Marín, M., Plumeier, I., & Pieper, D. H. (2012) · Journal of Bacteriology · doi:10.1128/jb.00430-12 · Cited by 30
Song, W. Y., & Kim, H. J. (2019) · Natural Product Reports · doi:10.1039/c9np00046a · Cited by 31
de Araújo, T. O., Isaure, M., Alchoubassi, G., Bierła, K., Szpunar, J., Trcera, N., Chay, S., Alcon, C., da Silva, L. C., Curie, C., et al. (2020) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2020.03.014 · Cited by 30
Identification of genes involved in siderophore transport inStreptomyces coelicolorA3(2)
Bunet, R., Brock, A. K., Rexer, H.-U., & Eriko Takano, A. (2006) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2006.00362.x · Cited by 30
Neumann, W., Hadley, R. C., & Nolan, E. M. (2017) · Essays in Biochemistry · doi:10.1042/ebc20160084 · Cited by 30
Iron Acquisition by Bacterial Pathogens: Beyond Tris‐Catecholate Complexes
Zhang, Y., Sen, S., & Giedroc, D. P. (2020) · ChemBioChem · doi:10.1002/cbic.201900778 · Cited by 30
Molecular characterization of siderophore biosynthesis in Paracoccidioides brasiliensis
Silva, M. G., de Curcio, J. S., Bailão, M. G. S., Lima, R. M., Tomazett, M. V., de Souza, A. F., Cruz-Leite, V. R. M., Sbaraini, N., Bailão, A. M., Rodrigues, F. J. S., et al. (2020) · IMA Fungus · doi:10.1186/s43008-020-00035-x · Cited by 30
Phillips, D. J., Prokeš, I., Davies, G., & Gibson, M. I. (2014) · ACS Macro Letters · doi:10.1021/mz500686w · Cited by 29
Catechol-Based Functionalizable Ligands for Gallium-68 Positron Emission Tomography Imaging
Joaqui‐Joaqui, M. A., Pandey, M. K., Bansal, A., Raju, M. V. R., Armstrong-Pavlik, F., Dundar, A., Wong, H. L. S., DeGrado, T. R., & Pierre, V. C. (2020) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.0c00975 · Cited by 29
Saha, P., Yeoh, B. S., Xiao, X., Golonka, R. M., Abokor, A. A., Wenceslau, C. F., Shah, Y. M., Joe, B., & Vijay‐Kumar, M. (2020) · Gut Microbes · doi:10.1080/19490976.2020.1841548 · Cited by 29
Chen, D., Wu, R., Bryan, T. L., & Dunaway‐Mariano, D. (2009) · Biochemistry · doi:10.1021/bi802207t · Cited by 29
Comparison of Xenorhabdus bovienii bacterial strain genomes reveals diversity in symbiotic functions
Murfin, K. E., Whooley, A., Klassen, J. L., & Goodrich‐Blair, H. (2015) · BMC Genomics · doi:10.1186/s12864-015-2000-8 · Cited by 29
Chen, R., Konishi, Y., & Nomura, T. (2018) · Advanced Powder Technology · doi:10.1016/j.apt.2018.06.022 · Cited by 29
Role of siderophores in cystic fibrosis pathogenesis: Foes or friends?
Mossialos, D., & Amoutzias, G. D. (2008) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2008.06.008 · Cited by 30
Kiernan, D. P., O’Doherty, J. V., & Sweeney, T. (2023) · Animals · doi:10.3390/ani13192996 · Cited by 31
Gerstle, K., Klätschke, K., Hahn, U., & Piganeau, N. (2012) · RNA Biology · doi:10.4161/rna.19065 · Cited by 28
Bacillus spp.: A Prolific Siderophore Producer
Khan, A. U., Doshi, H., & Thakur, M. C. (2016) · Springer eBooks · doi:10.1007/978-3-319-44409-3_13 · Cited by 28
Dong, Y., Geng, J., Liu, J., Pang, M., Awan, F., Lu, C., & Liu, Y. (2019) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-019-09757-4 · Cited by 28
Metadata
- 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
- 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