Mammalian Siderophores, Siderophore-binding Lipocalins, and the Labile Iron Pool
Open accessAbstract
Bacteria use tight-binding, ferric-specific chelators called siderophores to acquire iron from the environment and from the host during infection; animals use proteins such as transferrin and ferritin to transport and store iron. Recently, candidate compounds that could serve endogenously as mammalian siderophore equivalents have been identified and characterized through associations with siderocalin, the only mammalian siderophore-binding protein currently known. Siderocalin, an antibacterial protein, acts by sequestering iron away from infecting bacteria as siderophore complexes. Candidate endogenous siderophores include compounds that only effectively transport iron as ternary complexes with siderocalin, explaining pleiotropic activities in normal cellular processes and specific disease states.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Siderophores are best characterized in bacteria, but eukaryotes including fungi and mammals produce siderophores too.
“These are best characterized in bacteria, but eukaryotes including fungi and mammals produce siderophores, too [16, 42, 67, 86, 106].”
From “Pumping iron”—how macrophages handle iron at the systemic, microenvironmental, and cellular levels (2017) · cites this paper as [42]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Two to tango: Regulation of Mammalian iron metabolism
Hentze, M. W., Muckenthaler, M. U., Galy, B., & Camaschella, C. (2010) · Cell · doi:10.1016/j.cell.2010.06.028 · Cited by 2,120 · see citing works
Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron
Flo, T. H., Smith, K. D., Sato, S., Rodriguez, D. J., Holmes, M. A., Strong, R. K., Akira, S., & Aderem, A. (2004) · Nature · doi:10.1038/nature03104 · Cited by 1,877 · see citing works
Self-citationMicroorganisms pumping iron: anaerobic microbial iron oxidation and reduction
Weber, K. A., Achenbach, L. A., & Coates, J. D. (2006) · Nature Reviews Microbiology · doi:10.1038/nrmicro1490 · Cited by 1,777 · 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
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 · see citing works
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 · see citing works
Self-citationNeilands, J. B. (1981) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.50.070181.003435 · Cited by 1,241 · see citing works
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 1,056 · 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
Iron withholding: a defense against infection and neoplasia
Weinberg, E. D. (1984) · Physiological Reviews · doi:10.1152/physrev.1984.64.1.65 · Cited by 881 · see citing works
Kakhlon, O., & Cabantchik, Z. I. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01006-7 · Cited by 839 · see citing works
Mineralization in ferritin: an efficient means of iron storage
Chasteen, N. D., & Harrison, P. M. (1999) · Journal of Structural Biology · doi:10.1006/jsbi.1999.4118 · Cited by 815 · see citing works
The roles of iron in health and disease
Lieu, P. T., Heiskala, M. K., Peterson, P. A., & Yang, Y. M. (2001) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(00)00006-6 · Cited by 813 · see citing works
Dual Action of Neutrophil Gelatinase–Associated Lipocalin
Schmidt-Ott, K. M., Mori, K., Li, J. Y., Kalandadze, A., Cohen, D. J., Devarajan, P., & Barasch, J. (2007) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006080882 · Cited by 772 · see citing works
Muckenthaler, M. U., Galy, B., & Hentze, M. W. (2008) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.28.061807.155521 · Cited by 701 · see citing works
A Cell-Surface Receptor for Lipocalin 24p3 Selectively Mediates Apoptosis and Iron Uptake
Devireddy, L. R., Gazin, C., Zhu, X., & Green, M. R. (2005) · Cell · doi:10.1016/j.cell.2005.10.027 · Cited by 672 · see citing works
An Iron Delivery Pathway Mediated by a Lipocalin
Yang, J., Goetz, D., Li, J.-Y., Wang, W., Mori, K., Setlik, D., Du, T., Erdjument-Bromage, H., Tempst, P., Strong, R., et al. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00710-4 · Cited by 651 · see citing works
Self-citationForging a field: the golden age of iron biology.
Andrews, N. C. (2008) · Blood · doi:10.1182/blood-2007-12-077388 · Cited by 623 · see citing works
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 · see citing works
Transferrin receptor is necessary for development of erythrocytes and the nervous system
Levy, J. E., Jin, O., Fujiwara, Y., Kuo, F., & Andrews, N. (1999) · Nature Genetics · doi:10.1038/7727 · Cited by 574 · see citing works
Structure of the human transferrin receptor-transferrin complex
Cheng, Y., Zak, O., Aisen, P., Harrison, S. C., & Walz, T. (2004) · Cell · doi:10.1016/s0092-8674(04)00130-8 · Cited by 571 · see citing works
Lack of a role for iron in the Lyme disease pathogen
Posey, J. E., & Gherardini, F. C. (2000) · Science · doi:10.1126/science.288.5471.1651 · Cited by 538 · see citing works
Labile iron pool: the main determinant of cellular response to oxidative stress
Kruszewski, M. K. (2003) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2003.08.004 · Cited by 529 · see citing works
Function and regulation of transferrin and ferritin.
Ponka, P., Beaumont, C., & Richardson, D. R. (1998) · PubMed · Cited by 524 · see citing works
Berger, T., Togawa, A., Duncan, G. S., Elia, A. J., You-Ten, A., Wakeham, A., Fong, H. E. H., Cheung, C. C., & Mak, T. W. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510847103 · Cited by 460 · see citing works
Transferrins and Heme-Compounds as Iron Sources for Pathogenic Bacteria
Otto, B. R., Vught, A. M. J. J. V.-V., & MacLaren, D. M. (1992) · Critical Reviews in Microbiology · doi:10.3109/10408419209114559 · Cited by 394 · see citing works
Low molecular weight intracellular iron transport compounds
Jacobs, A. J. (1977) · Blood · doi:10.1182/blood.v50.3.433.433 · Cited by 387 · see citing works
Devireddy, L. R., Teodoro, J. G., Richard, F. A., & Green, M. R. (2001) · Science · doi:10.1126/science.1061075 · Cited by 379 · see citing works
Iron, Infections, and Anemia of Inflammation
Jurado, R. L. (1997) · Clinical Infectious Diseases · doi:10.1086/515549 · Cited by 358 · see citing works
Lipocalin 2 promotes breast cancer progression
Yang, J., Bielenberg, D. R., Rodig, S. J., Doiron, R., Clifton, M. C., Kung, A. L., Strong, R. K., Zurakowski, D., & Moses, M. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810617106 · Cited by 356 · see citing works
Self-citationHvidberg, V., Jacobsen, C. B., Strong, R. K., Cowland, J. B., Moestrup, S. K., & Borregaard, N. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.12.031 · Cited by 351 · see citing works
Self-citationSolution 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
The pathogen-associated <i>iroA</i> 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 · see citing works
Anderson, G. J., & Vulpe, C. D. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0051-1 · Cited by 317 · see citing works
Iron traffics in circulation bound to a siderocalin (Ngal)–catechol complex
Bao, G., Clifton, M., Hoette, T. M., Mori, K., Deng, S.-X., Qiu, A., Viltard, M., Williams, D., Paragas, N., Leete, T., et al. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.402 · Cited by 307 · see citing works
Self-citationDevireddy, L. R., Hart, D. O., Goetz, D. H., & Green, M. R. (2010) · Cell · doi:10.1016/j.cell.2010.04.040 · Cited by 295 · see citing works
Coordination chemistry and microbial iron transport
Raymond, K. N., & Carrano, C. J. (1979) · Accounts of Chemical Research · doi:10.1021/ar50137a004 · Cited by 293 · see citing works
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 292 · see citing works
Living with Iron (and Oxygen): Questions and Answers about Iron Homeostasis
Theil, E. C., & Goss, D. J. (2009) · Chemical Reviews · doi:10.1021/cr900052g · Cited by 265 · see citing works
The high-pathogenicity island: an iron-uptake island
Carniel, E. (2001) · Microbes and Infection · doi:10.1016/s1286-4579(01)01412-5 · Cited by 253 · see citing works
Andrews, N. C. (1999) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(99)00065-5 · Cited by 246 · see citing works
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 · see citing works
Self-citationIron piracy: acquisition of transferrin‐bound iron by bacterial pathogens
Cornelissen, C. N., & Sparling, P. F. (1994) · Molecular Microbiology · doi:10.1111/j.1365-2958.1994.tb01320.x · Cited by 244 · see citing works
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 · see citing works
Self-citationHuman Tear Lipocalin Exhibits Antimicrobial Activity by Scavenging Microbial Siderophores
Fluckinger, M., Haas, H., Merschak, P., Glasgow, B. J., & Redl, B. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.9.3367-3372.2004 · Cited by 195 · see citing works
The Role of Iron in the Immune Response to Bacterial Infection
Cherayil, B. J. (2011) · Immunologic Research · doi:10.1007/s12026-010-8199-1 · Cited by 191 · see citing works
ColV plasmid-specific aerobactin synthesis by invasive strains of Escherichia coli
Warner, P. J., WILLIAMS, P. H., Bindereif, A., & Neilands, J. B. (1981) · Infection and Immunity · doi:10.1128/iai.33.2.540-545.1981 · Cited by 181 · see citing works
Breuer, W., Shvartsman, M., & Cabantchik, Z. I. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.03.010 · Cited by 175 · see citing works
Chemistry for an essential biological process: the reduction of ferric iron
Pierre, J. L., Fontecave, M., & Crichton, R. R. (2002) · Biometals · doi:10.1023/a:1020259021641 · Cited by 163 · see citing works
Vokes, S. A., Reeves, S. A., Torres, A. G., & Payne, S. M. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01448.x · Cited by 148 · see citing works
Structure of schizokinen, An iron-transport compound from Bacillus megaterium
Mullis, K. B., Pollack, J. R., & Neilands, J. B. (1971) · Biochemistry · doi:10.1021/bi00802a010 · Cited by 123 · see citing works
Iron Regulatory Proteins: From Molecular Mechanisms to Drug Development
Recalcati, S., Minotti, G., & Cairo, G. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2983 · Cited by 123 · see citing works
Redox Cycling in Iron Uptake, Efflux, and Trafficking
Kosman, D. J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.113217 · Cited by 123 · see citing works
Klee, S. R., Nassif, X., Kušećek, B., Merker, P., Béretti, J., Achtman, M., & Tinsley, C. R. (2000) · Infection and Immunity · doi:10.1128/iai.68.4.2082-2095.2000 · Cited by 105 · see citing works
Abergel, R. J., Clifton, M. C., Pizarro, J. C., Warner, J. A., Shuh, D. K., Strong, R. K., & Raymond, K. N. (2008) · Journal of the American Chemical Society · doi:10.1021/ja803524w · Cited by 101 · see citing works
Self-citationRatledge, C., & Ewing, M. (1996) · Microbiology · doi:10.1099/13500872-142-8-2207 · Cited by 96 · see citing works
Barghouthi, S. A., Young, R., Olson, M. O. J., Arceneaux, J. E. L., Clem, L. W., & Byers, B. R. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.4.1811-1816.1989 · Cited by 91 · see citing works
Formation of Iron-binding Compounds by Micro-organisms
Garibaldi, J. A., & Neilands, J. B. (1956) · Nature · doi:10.1038/177526a0 · Cited by 89 · see citing works
Mechanism of catalysis of Fe(II) oxidation by ferritin H chains
Treffry, A., Hirzmann, J., Yewdall, S. J., & Harrison, P. M. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80417-f · Cited by 88 · see citing works
Lipocalin 2 is required for BCR-ABL-induced tumorigenesis
Leng, X., Lin, H., Ding, T., Wang, Y., Wu, Y., Klumpp, S., Sun, T., Zhou, Y. K., Monaco, P., Belmont, J. W., et al. (2008) · Oncogene · doi:10.1038/onc.2008.209 · Cited by 87 · see citing works
Self-citationCharacterization of Human DHRS6, an Orphan Short Chain Dehydrogenase/Reductase Enzyme
Guo, K., Lukacik, P., Papagrigoriou, E., Meier, M., Lee, W. H., Adamski, J., & Oppermann, U. C. T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m511346200 · Cited by 86 · see citing works
Transferrin-iron uptake by gram-negative bacteria
Cornelissen, C. N. (2003) · Frontiers in bioscience · doi:10.2741/1076 · Cited by 79 · see citing works
Fernandez-Pol, J. A. (1978) · Cell · doi:10.1016/0092-8674(78)90235-0 · Cited by 72 · see citing works
Wessling‐Resnick, M. (1999) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409239991209318 · Cited by 72 · see citing works
Stack, T. D. P., Karpishin, T. B., & Raymond, K. N. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00030a075 · Cited by 71 · see citing works
Halaas, Ø., Steigedal, M., Haug, M., Awuh, J. A., Ryan, L., Brech, A., Sato, S., Husebye, H., Cangelosi, G. A., Akira, S., et al. (2010) · The Journal of Infectious Diseases · doi:10.1086/650493 · Cited by 68 · see citing works
Self-citationTransferrin receptor of the rabbit reticulocyte
Leibman, A., & Aisen, P. (1977) · Biochemistry · doi:10.1021/bi00626a004 · Cited by 67 · see citing works
Siderocalins: siderophore-binding proteins of the innate immune system
Clifton, M. C., Corrent, C., & Strong, R. K. (2009) · BioMetals · doi:10.1007/s10534-009-9207-6 · Cited by 67 · see citing works
Self-citationTrace Element Uptake and Distribution in Plants
Graham, R. D., & Stangoulis, J. (2003) · Journal of Nutrition · doi:10.1093/jn/133.5.1502s · Cited by 66 · see citing works
Abergel, R. J., Moore, E. G., Strong, R. K., & Raymond, K. N. (2006) · Journal of the American Chemical Society · doi:10.1021/ja062476+ · Cited by 65 · see citing works
Self-citationIron transport & homeostasis mechanisms: their role in health & disease.
Nadadur, S. S., Srirama, K., & Mudipalli, A. (2008) · PubMed · Cited by 64 · see citing works
Ironing Out the Wrinkles in Host Defense: Interactions between Iron Homeostasis and Innate Immunity
Wang, L., & Cherayil, B. J. (2009) · Journal of Innate Immunity · doi:10.1159/000210016 · Cited by 63 · see citing works
Lipocalin-2: pro- or anti-apoptotic?
Kehrer, J. P. (2009) · Cell Biology and Toxicology · doi:10.1007/s10565-009-9119-9 · Cited by 62 · see citing works
The Role of Electrostatics in Siderophore Recognition by the Immunoprotein Siderocalin1
Hoette, T. M., Abergel, R. J., Xu, J., Strong, R. K., & Raymond, K. N. (2008) · Journal of the American Chemical Society · doi:10.1021/ja8074665 · Cited by 59 · see citing works
Self-citationBcr-Abl-mediated suppression of normal hematopoiesis in leukemia
Lin, H. Z., Monaco, G., Sun, T., Ling, X., Stephens, C. L., Xie, S., Belmont, J. W., & Arlinghaus, R. B. (2005) · Oncogene · doi:10.1038/sj.onc.1208500 · Cited by 54 · see citing works
Catechol releases iron( iii ) from ferritin by direct chelation without iron( ii ) production
Sánchez, P., Gálvez, N., Colacio, E., Miñones-Moyano, E., & Dominguez-Vera, J. M. (2005) · Dalton Transactions · doi:10.1039/b416669h · Cited by 53 · see citing works
Hou, Z., Raymond, K. N., O'Sulliva, B., Esker, T. W., & Nishio, T. (1998) · Inorganic Chemistry · doi:10.1021/ic9810182 · Cited by 52 · see citing works
Klausen, P. H., Niemann, C. U., Cowland, J. B., Krabbe, K. S., & Borregaard, N. (2005) · European Journal Of Haematology · doi:10.1111/j.1600-0609.2005.00511.x · Cited by 46 · see citing works
Ford, S. P., Cooper, R. A., Evans, R. W., Hider, R. C., & WILLIAMS, P. H. (1988) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1988.tb14473.x · Cited by 39 · see citing works
Inhibition of cell proliferation and induction of apoptosis by ExFABP gene targeting
Marco, E. D., Sessarego, N., Zerega, B., Cancedda, R., & Cancedda, F. D. (2003) · Journal of Cellular Physiology · doi:10.1002/jcp.10310 · Cited by 39 · see citing works
Low molecular weight iron-binding factor from mammalian tissue that potentiates bacterial growth.
Jones, R. L., Peterson, C. M., Grady, R. W., & Cerami, A. (1980) · The Journal of experimental medicine · doi:10.1084/jem.151.2.418 · Cited by 38 · see citing works
Valerio, L. G. (2007) · Toxicology Mechanisms and Methods · doi:10.1080/15376510701556690 · Cited by 37 · see citing works
Acute phase lipocalin Ex‐FABP is involved in heart development and cell survival
Gentili, C., Tutolo, G., Zerega, B., Marco, E. D., Cancedda, R., & Cancedda, F. D. (2004) · Journal of Cellular Physiology · doi:10.1002/jcp.20165 · Cited by 36 · see citing works
Klumpp, C., Burger, A., Mislin, G. L. A., & Abdallah, M. A. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.01.034 · Cited by 32 · see citing works
The v-myc-induced Q83 Lipocalin Is a Siderocalin
Coudevylle, N., Geist, L., Hötzinger, M., Hartl, M., Kontaxis, G., Bister, K., & Konrat, R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.123331 · Cited by 26 · see citing works
Ironing Out Disease: Inherited Disorders of Iron Homeostasis
Anderson, G. J. (2001) · IUBMB Life · doi:10.1080/15216540120450 · Cited by 24 · see citing works
Multiple Apoptotic Defects in Hematopoietic Cells from Mice Lacking Lipocalin 24p3
Liu, Z., Yang, A., Wang, Z., Bunting, K. D., Davuluri, G., Green, M. R., & Devireddy, L. R. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.216549 · Cited by 21 · see citing works
Hartl, M., Dunzendorfer-Matt, T., Schüler, W., Siemeister, G., Kontaxis, G., Kloiber, K., Konrat, R., & Bister, K. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.08.018 · Cited by 17 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Nutritional immunity: the battle for nutrient metals at the host–pathogen interface
Murdoch, C. C., & Skaar, E. P. (2022) · Nature Reviews Microbiology · doi:10.1038/s41579-022-00745-6 · Cited by 701 · see citing works
Lipocalin 2: an emerging player in iron homeostasis and inflammation
Xiao, X., Yeoh, B. S., & Vijay-Kumar, M. (2017) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071816-064559 · Cited by 426 · see citing works
Iron transport and its regulation in plants
Kobayashi, T., Nozoye, T., & Nishizawa, N. K. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.439 · Cited by 403 · see citing works
Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humans
Caza, M., & Kronstad, J. W. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00080 · Cited by 306 · see citing works
Diverging roles of bacterial siderophores during infection
Holden, V. I., & Bachman, M. A. (2015) · Metallomics · doi:10.1039/c4mt00333k · Cited by 274 · see citing works
The Role of Iron and Siderophores in Infection, and the Development of Siderophore Antibiotics
Page, M. G. P. (2019) · Clinical Infectious Diseases · doi:10.1093/cid/ciz825 · Cited by 250 · see citing works
Metal limitation and toxicity at the interface between host and pathogen
Becker, K. W., & Skaar, E. P. (2014) · FEMS Microbiology Reviews · doi:10.1111/1574-6976.12087 · Cited by 223 · see citing works
The Yin and Yang of copper during infection
Besold, A. N., Culbertson, E. M., & Culotta, V. C. (2016) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-016-1335-1 · Cited by 215 · see citing works
Diverse functional roles of lipocalin-2 in the central nervous system
Jha, M. K., Lee, S., Park, D. H., Kook, H., Park, K.-G., Lee, I.-K., & Suk, K. (2015) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2014.12.006 · Cited by 195 · see citing works
Host resistance factor SLC11A1 restricts <i>Salmonella</i> growth through magnesium deprivation
Cunrath, O., & Bumann, D. (2019) · Science · doi:10.1126/science.aax7898 · Cited by 177 · see citing works
“Pumping iron”—how macrophages handle iron at the systemic, microenvironmental, and cellular levels
Nairz, M., Theurl, I., Swirski, F. K., & Weiss, G. (2017) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-017-1944-8 · Cited by 178 · see citing works
The Iron Tug-of-War between Bacterial Siderophores and Innate Immunity
Golonka, R. M., Yeoh, B. S., & Vijay–Kumar, M. (2019) · Journal of Innate Immunity · doi:10.1159/000494627 · Cited by 171 · see citing works
Iron speciation in the cytosol: an overview
Hider, R. C., & Kong, X. (2012) · Dalton Transactions · doi:10.1039/c2dt32149a · Cited by 168 · see citing works
Selective and Efficient Biomacromolecular Extraction of Rare-Earth Elements using Lanmodulin
Deblonde, G. J. ‐., Mattocks, J. A., Park, D. M., Reed, D. W., Cotruvo, J. A., & Jiao, Y. (2020) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.0c01303 · Cited by 168 · see citing works
Molecular basis of mycobacterial survival in macrophages
Awuh, J. A., & Flo, T. H. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2422-8 · Cited by 155 · see citing works
Grim, K. P., San Francisco, B., Radin, J. N., Brazel, E. B., Kelliher, J. L., Párraga Solórzano, P. K., Kim, P. C., McDevitt, C. A., & Kehl-Fie, T. E. (2017) · mBio · doi:10.1128/mbio.01281-17 · Cited by 152 · see citing works
Iron: the hard player in diabetes pathophysiology
Hansen, J. B., Moen, I. W., & Mandrup-Poulsen, T. R. (2014) · Acta Physiologica · doi:10.1111/apha.12256 · Cited by 141 · see citing works
Lipocalin 2 Deficiency Dysregulates Iron Homeostasis and Exacerbates Endotoxin-Induced Sepsis
Srinivasan, G., Aitken, J. D., Zhang, B., Carvalho, F. A., Chassaing, B., Shashidharamurthy, R., Borregaard, N., Jones, D. P., Gewirtz, A. T., & Vijay–Kumar, M. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1200892 · Cited by 137 · see citing works
Aron, A. T., Heffern, M. C., Lonergan, Z. R., Wal, M. N. V., Blank, B. R., Spangler, B., Zhang, Y., Park, H. M., Stahl, A., Renslo, A. R., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1708747114 · Cited by 132 · see citing works
Transition metal ions at the crossroads of mucosal immunity and microbial pathogenesis
Diaz-Ochoa, V. E., Jellbauer, S., Klaus, S., & Raffatellu, M. (2014) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2014.00002 · Cited by 129 · see citing works
The Iron Metallome in Eukaryotic Organisms
Dlouhy, A. C., & Outten, C. E. (2012) · Metal ions in life sciences · doi:10.1007/978-94-007-5561-1_8 · Cited by 121 · see citing works
Igarashi, K., & Watanabe‐Matsui, M. (2014) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.232.229 · Cited by 113 · see citing works
Leal, S. M., Roy, S., Vareechon, C., Carrion, S. D., Clark, H., Lopez-Berges, M. S., diPietro, A., Schrettl, M., Beckmann, N., Redl, B., et al. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003436 · Cited by 111 · see citing works
Bacterial siderophores promote plant growth: Screening of catechol and hydroxamate siderophores
Grobelak, A., & Hiller, J. (2017) · International Journal of Phytoremediation · doi:10.1080/15226514.2017.1290581 · Cited by 107 · see citing works
The Iron hand of Uropathogenic Escherichia Coli : The Role of Transition Metal Control in Virulence
Robinson, A. E., Heffernan, J. R., & Henderson, J. P. (2018) · Future Microbiology · doi:10.2217/fmb-2017-0295 · Cited by 95 · see citing works
Marchetti, M., Bei, O. D., Bettati, S., Campanini, B., Kovachka, S., Gianquinto, E., Spyrakis, F., & Ronda, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21062145 · Cited by 92 · see citing works
Choi, S., Britigan, B. E., & Narayanasamy, P. (2019) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.9b00100 · Cited by 93 · see citing works
Aguirre, J. D., Clark, H. M., McIlvin, M., Vazquez, C., Palmere, S. L., Grab, D. J., Seshu, J., Hart, P. J., Saito, M., & Culotta, V. C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.433540 · Cited by 82 · see citing works
Iron and zinc exploitation during bacterial pathogenesis
Ma, L. M., Terwilliger, A. L., & Maresso, A. W. (2015) · Metallomics · doi:10.1039/c5mt00170f · Cited by 83 · see citing works
Meszaros, E. C., & Malemud, C. (2012) · Therapeutic Advances in Chronic Disease · doi:10.1177/2040622312454157 · Cited by 90 · see citing works
Dinitrosyl iron complexes with glutathione as NO and NO+ donors
Borodulin, R. R., Kubrina, L. N., Mikoyan, V. D., Poltorakov, А. P., Shvydkiy, V. O., Burbaev, D. S., Сереженков, В. А., Yakhontova, E. R., & Vanin, A. F. (2012) · Nitric Oxide · doi:10.1016/j.niox.2012.11.001 · Cited by 73 · see citing works
Gebauer, M., Schiefner, A., Matschiner, G., & Skerra, A. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.12.004 · Cited by 71 · see citing works
Holden, V. I., Lenio, S., Kuick, R. D., Ramakrishnan, S. K., Shah, Y. M., & Bachman, M. A. (2014) · Infection and Immunity · doi:10.1128/iai.01849-14 · Cited by 63 · see citing works
Lim, D., Jeong, J., & Song, J. (2021) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13653 · Cited by 61 · see citing works
An overview of the biological metal uptake pathways in P seudomonas aeruginosa
Schalk, I. J., & Cunrath, O. (2016) · Environmental Microbiology · doi:10.1111/1462-2920.13525 · Cited by 61 · see citing works
Pseudomonas aeruginosa zinc homeostasis: Key issues for an opportunistic pathogen
Gonzalez, M. R., Ducret, V., Leoni, S., & Perron, K. (2018) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2018.01.018 · Cited by 57 · see citing works
Human Urinary Composition Controls Antibacterial Activity of Siderocalin*
Shields-Cutler, R. R., Crowley, J. R., Hung, C. S., Stapleton, A. E., Aldrich, C. C., Marschall, J., & Henderson, J. P. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.645812 · Cited by 56 · see citing works
Lipocalin 2 stimulates bone fibroblast growth factor 23 production in chronic kidney disease
Courbon, G., Francis, C. P., Gerber, C., Neuburg, S., Wang, X., Lynch, E. P., Isakova, T., Babitt, J. L., Wolf, M. S., Martin, A., et al. (2021) · Bone Research · doi:10.1038/s41413-021-00154-0 · Cited by 56 · see citing works
Choi, S., Switzer, B. L., Britigan, B. E., & Narayanasamy, P. (2020) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.0c00113 · Cited by 55 · see citing works
Iron in intracellular infection: to provide or to deprive?
Silva-Gomes, S., Vale-Costa, S., Appelberg, R., & Gomes, M. S. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00096 · Cited by 51 · see citing works
Lipocalin‐2—The myth of its expression and function
Li, D., Sun, W. Y., Fu, B., Xu, A., & Wang, Y. (2019) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.13332 · Cited by 54 · see citing works
Qu, Z., Li, P., Zhang, X., & Han, K. (2015) · Journal of Materials Chemistry B · doi:10.1039/c5tb02090e · Cited by 50 · see citing works
Siderophores as tools and treatments
Gräff, Á. T., & Barry, S. M. (2024) · npj Antimicrobials and Resistance · doi:10.1038/s44259-024-00053-4 · Cited by 49 · see citing works
Nakamura, I., Ohsumi, K., Takeda, S., Katsumata, K., Matsumoto, S., 赤松, 総., Mitori, H., & Nakai, T. (2019) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02689-18 · Cited by 44 · see citing works
New Perspectives on Circulating Ferritin: Its Role in Health and Disease
Fonseca, Ó., Ramos, H., Gomes, L. T. S., Gomes, M. S., & Moreira, A. C. (2023) · Molecules · doi:10.3390/molecules28237707 · Cited by 41 · see citing works
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 · see citing works
Biological Roles of Lipocalins in Chemical Communication, Reproduction, and Regulation of Microbiota
Stopková, R., Otcenásková, T., Matějková, T., Kuntová, B., & Stopka, P. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.740006 · Cited by 33 · see citing works
Harrington, J. M., Duckworth, O. W., & Haselwandter, K. (2015) · BioMetals · doi:10.1007/s10534-015-9821-4 · Cited by 33 · see citing works
The ligands of neutrophil gelatinase-associated lipocalin
Bao, G., Ho, C., & Barasch, J. M. (2015) · RSC Advances · doi:10.1039/c5ra18736b · Cited by 36 · see citing works
A systematic analysis of human lipocalin family and its expression in esophageal carcinoma
Du, Z., Wu, B., Wu, X., Lin, X., Qiu, X., Zhan, X.-F., Wang, S., Shen, J., Zheng, C.-P., Wu, Z., et al. (2015) · Scientific Reports · doi:10.1038/srep12010 · Cited by 34 · see citing works
Fluorescent sensors of siderophores produced by bacterial pathogens
Kumar, A., Yang, T., Chakravorty, S., Majumdar, A., Nairn, B. L., Six, D. A., Marcondes dos Santos, N., Price, S. L., Lawrenz, M. B., Actis, L. A., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101651 · Cited by 28 · see citing works
Sickinger, S., Maier, H. T., König, S., Vallant, N., Kofler, M., Schumpp, P., Schwelberger, H. G., Hermann, M., Obrist, P., Schneeberger, S., et al. (2013) · Transplant International · doi:10.1111/tri.12116 · Cited by 29 · see citing works
Balhara, M., Chaudhary, R., Ruhil, S., Singh, B., Dahiya, N. R., Parmar, V. S., Jaiwal, P. K., & Chhillar, A. K. (2016) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2016.1254196 · Cited by 28 · see citing works
Dewangan, S., Barik, T., Parida, R., Mawatwal, S., Dhiman, R., Giri, S., & Chatterjee, S. (2019) · Journal of Organometallic Chemistry · doi:10.1016/j.jorganchem.2019.120999 · Cited by 28 · see citing works
Singh, R. P., Kapoor, A., Sinha, A., Ma, Y., & Shankar, M. (2025) · The Microbe · doi:10.1016/j.microb.2025.100289 · Cited by 27 · see citing works
Understanding the Potential and Risk of Bacterial Siderophores in Cancer
Pita-Grisanti, V., Chasser, K. M., Sobol, T., & Cruz‐Monserrate, Z. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.867271 · Cited by 28 · see citing works
Siderophore-inspired nanoparticle-based biosensor for the selective detection of Fe 3+
Phillips, D. J., Davies, G., & Gibson, M. I. (2014) · Journal of Materials Chemistry B · doi:10.1039/c4tb01501k · Cited by 27 · see citing works
Leal, S. M., Roy, S., Vareechon, C., Carrion, S. D. J., Clark, H., López‐Berges, M. S., Pietro, A. D., Schrettl, M., Beckmann, N., Redl, B., et al. (2013) · PLoS Pathogens · doi:10.1371/annotation/4f388450-90fe-4c65-9b9b-71a2b7935ac0 · Cited by 26 · see citing works
Clifton, M. C., Rupert, P. B., Hoette, T. M., Raymond, K. N., Abergel, R. J., & Strong, R. K. (2019) · Journal of Structural Biology X · doi:10.1016/j.yjsbx.2019.100008 · Cited by 25 · see citing works
Self-citationChoi, S., Talmon, G. A., Britigan, B. E., & Narayanasamy, P. (2021) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.0c00896 · Cited by 24 · see citing works
Betten, R., Scharner, B., Probst, S., Edemir, B., Wolff, N. A., Langelueddecke, C., Lee, W., & Thévenod, F. (2018) · Cell Communication and Signaling · doi:10.1186/s12964-018-0285-3 · Cited by 22 · see citing works
Metal-antimicrobial peptides combo: promising weapons to combat bacteria invaders
Falcigno, L., Braccia, S., Bellavita, R., D’Auria, G., Falanga, A., & Galdiero, S. (2024) · Frontiers in Drug Discovery · doi:10.3389/fddsv.2024.1440378 · Cited by 23 · see citing works
Barkovskiy, M., Ilyukhina, E., Dauner, M., Eichinger, A., & Skerra, A. (2018) · Biological Chemistry · doi:10.1515/hsz-2018-0342 · Cited by 22 · see citing works
Bao, G., Barasch, J. M., Xu, J., Wang, W., Hu, F., & Deng, S. (2015) · RSC Advances · doi:10.1039/c5ra02509e · Cited by 21 · see citing works
Gao, J., Xing, F., Bai, Y., & Zhu, S. (2014) · Dalton Transactions · doi:10.1039/c4dt00118d · Cited by 21 · see citing works
Yersiniabactin is a quorum-sensing autoinducer and siderophore in uropathogenic Escherichia coli
Heffernan, J. R., Wildenthal, J. A., Tran, H. D., Katumba, G. L., McCoy, W. H., & Henderson, J. P. (2024) · mBio · doi:10.1128/mbio.00277-23 · Cited by 20 · see citing works
Ecker, F., Haas, H., Groll, M., & Huber, E. M. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201807093 · Cited by 19 · see citing works
The Tricky Ways Bacteria Cope with Iron Limitation
Braun, V., & Hantke, K. (2013) · Springer briefs in molecular science · doi:10.1007/978-94-007-6088-2_2 · Cited by 18 · see citing works
Ligand binding‐dependent functions of the lipocalin NLaz: an in vivo study in Drosophila
Ruiz, M., Ganfornina, M. D., Correnti, C., Strong, R. K., & Sánchez, D. (2013) · The FASEB Journal · doi:10.1096/fj.13-240556 · Cited by 18 · see citing works
Self-citationModulation of urinary siderophores by the diet, gut microbiota and inflammation in mice
Xiao, X., Yeoh, B. S., Saha, P., Tian, Y., Singh, V., Patterson, A. D., & Vijay-Kumar, M. (2017) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2016.11.014 · Cited by 16 · see citing works
Hottenrott, M. C., Wedel, J., Gaertner, S., Stamellou, E., Kraaij, T., Mandel, L., Lösel, R., Sticht, C., Hoeger, S., Ait-Hsiko, L., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073122 · Cited by 16 · see citing works
Dewangan, S., Barik, T., Mishra, S., Mawatwal, S., Kumari, S., Giri, S., Das, S., Dhiman, R., Wölper, C., & Chatterjee, S. (2018) · Applied Organometallic Chemistry · doi:10.1002/aoc.4612 · Cited by 16 · see citing works
The diversity of lipocalin receptors
Redl, B., & Habeler, M. (2021) · Biochimie · doi:10.1016/j.biochi.2021.09.008 · Cited by 15 · see citing works
Probst, S., Scharner, B., McErlean, R., Lee, W., & Thévenod, F. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20215398 · Cited by 15 · see citing works
Infection metallomics for critical care in the post‐COVID era
Patil, R. H., Luptáková, D., & Havlı́ček, V. (2021) · Mass Spectrometry Reviews · doi:10.1002/mas.21755 · Cited by 15 · see citing works
Boosting AMPs’ Power: From Structural Engineering to Nanotechnology-Based Delivery
Ajayi, O. E., Bellavita, R., Imbò, L. E., Palladino, S., Braccia, S., Falanga, A., & Galdiero, S. (2025) · Molecules · doi:10.3390/molecules30142979 · Cited by 14 · see citing works
Alhassen, S., Şenel, M., & Alachkar, A. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00693 · Cited by 14 · see citing works
Fungal NRPS-Dependent Siderophores: From Function to Prediction
Sørensen, J. L., Knudsen, M., Hansen, F. T., Olesen, C., Fuertes, P. R., Lee, T. V., Søndergaard, T. E., Pedersen, C. N. S., Brodersen, D. E., & Giese, H. (2014) · Fungal biology · doi:10.1007/978-1-4939-1191-2_15 · Cited by 13 · see citing works
Specificity and mechanism of TonB-dependent ferric catecholate uptake by Fiu
Yang, T., Zou, Y., Ng, H. L., Kumar, A., Newton, S. M., & Klebba, P. E. (2024) · Frontiers in Microbiology · doi:10.3389/fmicb.2024.1355253 · Cited by 11 · see citing works
“…bacterial iron acquisition in iron-deficient environments, including within human and animal organs, tissues, fluids, and secretions, where transferrin, siderocalin, and ferritin sequester iron as a defense mechanism (Cornelissen and Sparling, 1994; Abergel et al., 2008; Correnti and Strong, 2012).”
BackgroundStealthy microbes: How Neisseria gonorrhoeae hijacks bulwarked iron during infection
Stoudenmire, J. L., Greenawalt, A. N., & Cornelissen, C. N. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.1017348 · Cited by 12 · see citing works
Pachpatil, P. K., Kanojia, S. V., Ghosh, A., Majumdar, A. G., Wadawale, A., Mohapatra, M., Patro, B. S., Ghanty, T. K., & Goswami, D. (2022) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2022.132474 · Cited by 11 · see citing works
Siderophores and their Applications in Wood, Textile, and Paper Conservation
Rapti, S., Boyatzis, S. C., Rivers, S., & Πούρνου, Α. (2021) · Springer eBooks · doi:10.1007/978-3-030-69411-1_14 · Cited by 11 · see citing works
Fujiwara, Y., Tsuchiya, H., Sakai, N., Shibata, K., Fujimura, A., & Koshimizu, T. (2016) · Journal of Inflammation · doi:10.1186/s12950-016-0116-5 · Cited by 11 · see citing works
Hofmann, M., Heine, T., Schulz, V., Hofmann, S., & Tischler, D. (2019) · Biotechnology Reports · doi:10.1016/j.btre.2019.e00403 · Cited by 11 · see citing works
Dewangan, S., Mishra, A., Halder, B., Mishra, A., Dhiman, R., & Chatterjee, S. (2023) · Inorganica Chimica Acta · doi:10.1016/j.ica.2023.121511 · Cited by 10 · see citing works
Lokesh, K. N., Channarayappa, Venkataranganna, M. V., Raj, G. G., Patil, H., & Dave, H. (2017) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2017.10.001 · Cited by 10 · see citing works
Research Progress on Lipocalin-2 in Diabetic Encephalopathy
Zhang, W., Chen, S., & Zhuang, X. (2023) · Neuroscience · doi:10.1016/j.neuroscience.2023.02.011 · Cited by 11 · see citing works
Habeler, M., Lindner, H. H., & Redl, B. (2020) · Biological Chemistry · doi:10.1515/hsz-2020-0132 · Cited by 8 · see citing works
Manzoor, S., Ahmed, A., & Moin, S. T. (2021) · BioMetals · doi:10.1007/s10534-021-00332-x · Cited by 7 · see citing works
Barakat, H., Qureshi, K. A., Alsohim, A. S., & Rehan, M. (2022) · Molecules · doi:10.3390/molecules27134010 · Cited by 7 · see citing works
Kaur, A., Kaur, M., Bhalla, V., Singh, M., Bhanwer, A. J. S., & Kumar, M. (2021) · ChemistrySelect · doi:10.1002/slct.202004264 · Cited by 6 · see citing works
Fontana, A., Falasconi, I., Bellassi, P., Fanfoni, E., Puglisi, E., & Morelli, L. (2023) · Microorganisms · doi:10.3390/microorganisms11030587 · Cited by 7 · see citing works
Samsonov, S. A., Zsila, F., & Maszota‐Zieleniak, M. (2021) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2021.107861 · 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
Tang, H., Chang, P.-C., & Chen, C. Y. (2016) · Journal of Molecular Modeling · doi:10.1007/s00894-015-2897-5 · Cited by 4 · see citing works
Gibson, S., Fernando, R., Jacobs, H. K., & Gopalan, A. S. (2015) · Tetrahedron · doi:10.1016/j.tet.2015.10.031 · Cited by 4 · see citing works
Photo‐release of Metal Ions in Living Cells
Gwizdala, C., & Burdette, S. C. (2014) · doi:10.1002/9781118682975.ch9 · Cited by 4 · see citing works
Haddadin, R. N., Assaf, A. M., Homsi, A., Collier, P. J., & Shehabi, A. A. (2019) · Journal of Applied Microbiology · doi:10.1111/jam.14296 · Cited by 3 · see citing works
Bhagavan, N. V., & Ha, C. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-416687-5.00035-x · Cited by 3 · see citing works
Iron Sequestration in Immunity
Correnti, C., & Strong, R. K. (2004) · Wiley eBooks · doi:10.1002/9781119951438.eibc2142 · Cited by 3 · see citing works
Self-citation
- Authors
- Correnti, C., & Strong, R. K.
- Affiliations
- Fred Hutch Cancer Center (US)
- Corresponding author
- Strong, Roland K.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2012-04
- Volume
- 287
- Issue
- 17
- Pages
- 13524-13531
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3340207
- OpenAlex
- W1990262536
- Cited by
- 115
- References
- 88
- Citations by year
- 2025: 3 · 2024: 4 · 2023: 5 · 2022: 7 · 2021: 11 · 2020: 4 · 2019: 12 · 2018: 8 · 2017: 6 · 2016: 10 · 2015: 11 · 2014: 12 · 2013: 12 · 2012: 6
- FWCI
- 2.08
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (AI 059432, R01AI059432)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK073462, R21DK091729, DK091729, DK073462)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- siderocalin, labile iron pool, iron acquisition, iron transport, iron storage, transferrin, ferritin, antibacterial proteins
- MeSH terms
- Lipocalin-2, Animals, Anti-Bacterial Agents, Biological Transport, Carrier Proteins, Catechols, Chelating Agents, Humans, Hydrogen-Ion Concentration, Immunity, Innate, Iron, Kinetics, Models, Biological, Models, Chemical, Apoptosis, Siderophores, Lipocalins
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