Cited by 261Iron Metabolism and DisordersBacterial Genetics and BiotechnologyEscherichia coli research studies

The DOI matches its Crossref record; 178 of the 179 references it cites were found in a registry or an index.

Sequestration and Scavenging of Iron in Infection

Open access

Parrow, Nermi L., Fleming, Robert E., Minnick, Michael F.·2013·Infection and Immunity

Open this paper in CoChat — free account Open PDF

Abstract

The proliferative capability of many invasive pathogens is limited by the bioavailability of iron. Pathogens have thus developed strategies to obtain iron from their host organisms. In turn, host defense strategies have evolved to sequester iron from invasive pathogens. This review explores the mechanisms employed by bacterial pathogens to gain access to host iron sources, the role of iron in bacterial virulence, and iron-related genes required for the establishment or maintenance of infection. Host defenses to limit iron availability for bacterial growth during the acute-phase response and the consequences of iron overload conditions on susceptibility to bacterial infection are also examined. The evidence summarized herein demonstrates the importance of iron bioavailability in influencing the risk of infection and the ability of the host to clear the pathogen.

Integrity signals

Registry

Crossref · 10.1128/iai.00602-13

Cites

178 of 178 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?

Acute-Phase Proteins and Other Systemic Responses to Inflammation
Gabay, C., & Kushner, I. (1999) · New England Journal of Medicine · doi:10.1056/nejm199902113400607 · Cited by 6,734
Hepcidin Regulates Cellular Iron Efflux by Binding to Ferroportin and Inducing Its Internalization
Nemeth, E., Tuttle, M. S., Powelson, J., Vaughn, M. B., Donovan, A., Ward, D. M., Ganz, T., & Kaplan, J. (2004) · Science · doi:10.1126/science.1104742 · Cited by 4,803
Cloning and characterization of a mammalian proton-coupled metal-ion transporter
Gunshin, H., Mackenzie, B., Berger, U. V., Gunshin, Y., Romero, M. F., Boron, W. F., Nussberger, S., Gollan, J. L., & Hediger, M. A. (1997) · Nature · doi:10.1038/41343 · Cited by 3,166
Bacterial iron homeostasis
Andrews, S. C., Robinson, A. K., & Rodríguez-Quiñones, F. (2003) · FEMS Microbiology Reviews · doi:10.1016/s0168-6445(03)00055-x · Cited by 2,702
IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin
Nemeth, E., Rivera, S., Gabayan, V., Keller, C., Taudorf, S., Pedersen, B. K., & Ganz, T. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200420945 · Cited by 2,650 · cited 11×
“The APR markedly alters host iron metabolism in ways that serve to minimize iron bioavailability to pathogens (Fig.”
BackgroundInfluential
The catalytic decomposition of hydrogen peroxide by iron salts
Haber, F., & Weiss, J. (1934) · Proceedings of the Royal Society of London. Series A - Mathematical and Physical Sciences · doi:10.1098/rspa.1934.0221 · Cited by 2,571
Hepcidin, a urinary antimicrobial peptide synthesized in the liver
Park, C. H., Valore, E. V., Waring, A. J., & Ganz, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008922200 · Cited by 2,168
Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein
Nemeth, E., Valore, E. V., Territo, M., Schiller, G., Lichtenstein, A., & Ganz, T. (2003) · Blood · doi:10.1182/blood-2002-10-3235 · Cited by 1,417
LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity
Krause, A., Neitz, S., Mägert, H.-J., Schulz, A., Forssmann, W.-G., Schulz-Knappe, P., & Adermann, K. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01920-7 · Cited by 1,324
The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia, and inflammation
Nicolas, G., Chauvet, C., Viatte, L., Danan, J. L., Bigard, X., Devaux, I., Beaumont, C., Kahn, A., & Vaulont, S. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215686 · Cited by 1,214
An iron-regulated ferric reductase associated with the absorption of dietary iron
McKie, A. T., Barrow, D., Latunde-Dada, G. O., Rolfs, A., Sager, G., Mudaly, E., Mudaly, M., Richardson, C., Barlow, D., Bomford, A., et al. (2001) · Science · doi:10.1126/science.1057206 · Cited by 1,101
Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse
Vulpe, C. D., Kuo, Y.-M., Murphy, T. L., Cowley, L., Askwith, C., Libina, N., Gitschier, J., & Anderson, G. J. (1999) · Nature Genetics · doi:10.1038/5979 · Cited by 1,084
Hepcidin and iron regulation, 10 years later
Ganz, T. (2011) · Blood · doi:10.1182/blood-2011-01-258467 · Cited by 962
Iron-catalyzed hydroxyl radical formation. Stringent requirement for free iron coordination site.
Graf, E., Mahoney, J. R., Bryant, R. G., & Eaton, J. W. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43139-5 · Cited by 855
The hemochromatosis gene product complexes with the transferrin receptor and lowers its affinity for ligand binding
Feder, J. N., Penny, D. M., Irrinki, A., Lee, V. K., Lebrón, J. A., Watson, N., Tsuchihashi, Z., Sigal, E., Bjorkman, P. J., & Schatzman, R. C. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.4.1472 · Cited by 827
Iron metabolism in man
Bothwell, T. H., Charlton, R. W., Cook, J. D., & Finch, C. A. (1979) · Blackwell Scientific Publications eBooks · Cited by 730
IL-6-Induced Homodimerization of gp130 and Associated Activation of a Tyrosine Kinase
Murakami, M., Hibi, M., Nakagawa, N., Nakagawa, T., Yasukawa, K., Yamanishi, K., Taga, T., & Kishimoto, T. (1993) · Science · doi:10.1126/science.8511589 · Cited by 724
LACTOFERRIN, AN IRON-BINBING PROTEIN NI NEUTROPHILIC LEUKOCYTES
Masson, P. L., Heremans, J. F., & Schonne, E. (1969) · The Journal of Experimental Medicine · doi:10.1084/jem.130.3.643 · Cited by 700
A role of SMAD4 in iron metabolism through the positive regulation of hepcidin expression
Wang, R.-H., Li, C., Xu, X., Zheng, Y., Xiao, C., Zerfas, P., Cooperman, S., Eckhaus, M., Rouault, T., Mishra, L., et al. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.10.010 · Cited by 614
Iron Overload in Human Disease
Fleming, R. E., & Ponka, P. (2012) · New England Journal of Medicine · doi:10.1056/nejmra1004967 · Cited by 607
Passage of Heme-Iron Across the Envelope of Staphylococcus aureus
Mazmanian, S. K., Skaar, E. P., Gaspar, A. H., Humayun, M., Gornicki, P., Jelenska, J., Joachmiak, A., Missiakas, D. M., & Schneewind, O. (2003) · Science · doi:10.1126/science.1081147 · Cited by 593
Role of Iron in Bacterial Infection
Bullen, J. J., Rogers, H. J., & Griffiths, E. (1978) · Modern aspects of electrochemistry · doi:10.1007/978-3-642-66956-9_1 · Cited by 494
Identification of the receptor scavenging hemopexin-heme complexes
Hvidberg, V., Maniecki, M. B., Jacobsen, C., Højrup, P., Møller, H. J., & Moestrup, S. K. (2005) · Blood · doi:10.1182/blood-2005-03-1185 · Cited by 473
Characterization of the ferrous iron uptake system of Escherichia coli
Kammler, M., Schön, C., & Hantke, K. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.19.6212-6219.1993 · Cited by 460
The association between alcohol use, alcohol use disorders and tuberculosis (TB). A systematic review
Rehm, J., Samokhvalov, A. V., Neuman, M. G., Room, R., Parry, C., Lönnroth, K., Patra, J., Poznyak, V., & Popova, S. (2009) · BMC Public Health · doi:10.1186/1471-2458-9-450 · Cited by 458
Alcohol and cause-specific mortality in Russia: a retrospective case–control study of 48 557 adult deaths
Zaridze, D. G., Brennan, P., Boreham, J., Boroda, A. M., Karpov, R. S., Lazarev, A. F., Конобеевская, И. Н., Igitov, V., Terechova, T., Boffetta, P., et al. (2009) · The Lancet · doi:10.1016/s0140-6736(09)61034-5 · Cited by 449
Enterobactin, an iron transport compound from Salmonella typhimurium
Pollack, J. R., & Neilands, J. B. (1970) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(70)90819-3 · Cited by 433
IRON ABSORPTION AND LOADING IN β-THALASSÆMIA INTERMEDIA
Pippard, M. J., Warner, G. T., Callender, S. T., & Weatherall, D. J. (1979) · The Lancet · doi:10.1016/s0140-6736(79)92175-5 · Cited by 419
Iron and Hydrogen Peroxide Detoxification Properties of DNA-binding Protein from Starved Cells
Zhao, G., Ceci, P., Ilari, A., Giangiacomo, L., Laue, T. M., Chiancone, E., & Chasteen, N. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202094200 · Cited by 417
Non-transferrin-bound iron in plasma or serum from patients with idiopathic hemochromatosis
Grootveld, M. C., Bell, J. D., Halliwell, B. B., Aruoma, O. I., Bomford, A. B., & Sadler, P. J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83758-9 · Cited by 404
Hepatic acute phase proteins – Regulation by IL-6- and IL-1-type cytokines involving STAT3 and its crosstalk with NF-κB-dependent signaling
Bode, J. G., Albrecht, U., Häussinger, D., Heinrich, P. C., & Schaper, F. (2012) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2011.09.008 · Cited by 379
Structural basis of gating by the outer membrane transporter FecA
Ferguson, A. D., Chakraborty, R., Smith, B. S., Esser, L., van der Helm, D., & Deisenhofer, J. (2002) · Science · doi:10.1126/science.1067313 · Cited by 373
Hemojuvelin is essential for dietary iron sensing, and its mutation leads to severe iron overload
Niederkofler, V. (2005) · Journal of Clinical Investigation · doi:10.1172/jci25683 · Cited by 371
Ceruloplasmin. A scavenger of superoxide anion radicals.
Goldstein, I. M., Kaplan, H. B., Edelson, H. S., & Weissmann, G. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50692-x · Cited by 365
Lactoferrin is a lipid A-binding protein
Appelmelk, B. J., An, Y. Q., Geerts, M., Thijs, B. G., de Boer, H. A., MacLaren, D. M., Graaff, J., & Nuijens, J. H. (1994) · Infection and Immunity · doi:10.1128/iai.62.6.2628-2632.1994 · Cited by 362
Lactoferrin and transferrin: A comparative study
Aisen, P., & Leibman, A. (1972) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(72)90283-8 · Cited by 338
Human transferrin: cDNA characterization and chromosomal localization.
Yang, F., Lum, J. B., McGill, J. R., Moore, C. M., Naylor, S. L., van Bragt, P. H., Baldwin, W. D., & Bowman, B. H. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.9.2752 · Cited by 314
Staphylococcus aureus IsdB Is a Hemoglobin Receptor Required for Heme Iron Utilization
Torres, V. J., Pishchany, G., Humayun, M., Schneewind, O., & Skaar, E. P. (2006) · Journal of Bacteriology · doi:10.1128/jb.01335-06 · Cited by 302
Iron acquisition and virulence in Helicobacter pylori: a major role for FeoB, a high‐affinity ferrous iron transporter
Velayudhan, J., Hughes, N. J., McColm, A. A., Bagshaw, J. A., Clayton, C. L., Andrews, S. C., & Kelly, D. J. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01987.x · Cited by 298
Hepcidin regulation by innate immune and infectious stimuli
Armitage, A. E., Eddowes, L. A., Gileadi, U., Cole, S., Spottiswoode, N., Selvakumar, T. A., Ho, L.-P., Townsend, A. R. M., & Drakesmith, H. (2011) · Blood · doi:10.1182/blood-2011-04-351957 · Cited by 294
IsdG and IsdI, Heme-degrading Enzymes in the Cytoplasm of Staphylococcus aureus
Skaar, E. P., Gaspar, A. H., & Schneewind, O. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307952200 · Cited by 282
Comparative study of the iron-binding properties of human transferrinsI. Complete and sequential iron saturation and desaturation of the lactotransferrin
Mazurier, J., & Spik, G. (1980) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(80)90112-9 · Cited by 278
Hepcidin mRNA levels in mouse liver respond to inhibition of erythropoiesis
Vokurka, M., Krijt, J., Šulc, K., & Nečas, E. (2006) · Physiological Research · doi:10.33549/physiolres.930841 · Cited by 263
Structural basis for iron piracy by pathogenic Neisseria
Noinaj, N., Easley, N. C., Oke, M., Mizuno, N., Gumbart, J., Boura, E., Steere, A. N., Zak, O., Aisen, P., Tajkhorshid, E., et al. (2012) · Nature · doi:10.1038/nature10823 · Cited by 262
Orchestration of Iron Homeostasis
Fleming, R. E., & Bacon, B. R. (2005) · New England Journal of Medicine · doi:10.1056/nejmp048363 · Cited by 261
The Yfe system of Yersinia pestis transports iron and manganese and is required for full virulence of plague
Bearden, S. W., & Perry, R. D. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01360.x · Cited by 254
Haem iron‐transport system in enterohaemorrhagic Escherichia coli O157:H7
Torres, A. G., & Payne, S. M. (1997) · Molecular Microbiology · doi:10.1046/j.1365-2958.1997.2641628.x · Cited by 242
A Staphylococcus aureus Regulatory System that Responds to Host Heme and Modulates Virulence
Torres, V. J., Stauff, D. L., Pishchany, G., Bezbradica, J. S., Gordy, L. E., Iturregui, J., Anderson, K. L., Dunman, P. M., Joyce, S., & Skaar, E. P. (2007) · Cell Host & Microbe · doi:10.1016/j.chom.2007.03.001 · Cited by 241
Serum‐Induced Iron‐Acquisition Systems and TonB Contribute to Virulence inKlebsiella pneumoniaeCausing Primary Pyogenic Liver Abscess
Hsieh, P., Lin, T., Lee, C., Tsai, S., & Wang, J.-T. (2008) · The Journal of Infectious Diseases · doi:10.1086/588383 · Cited by 240
The Mobilization of Iron from the Perfused Mammalian Liver by a Serum Copper Enzyme, Ferroxidase I
Osaki, S., Johnson, D. A., & Frieden, E. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62284-7 · Cited by 236
Expression and localization of hepcidin in macrophages: a role in host defense against tuberculosis
Sow, F. B., Florence, W. C., Satoskar, A. R., Schlesinger, L. S., Zwilling, B. S., & Lafuse, W. P. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0407216 · Cited by 229
Hemin-induced lipid membrane disorder and increased permeability: a molecular model for the mechanism of cell lysis
Schmitt, T. H., Frezzatti, W. A., & Schreier, S. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1566 · Cited by 217
Expression and Characterization of a Heme Oxygenase (Hmu O) fromCorynebacterium diphtheriae
Wilks, A., & Schmitt, M. P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.2.837 · Cited by 205
Hepcidin mediates transcriptional changes that modulate acute cytokine-induced inflammatory responses in mice
De Domenico, I., Zhang, T. Y., Koening, C. L., Branch, R. W., London, N., Lo, E., Daynes, R. A., Kushner, J. P., Li, D., Ward, D. M., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci42011 · Cited by 197
Association of Pulmonary Tuberculosis with Increased Dietary Iron
Gangaidzo, I. T., Moyo, V. M., Mvundura, E., Aggrey, G., Murphree, N. L., Khumalo, H., Saungweme, T., Kasvosve, I., Gomo, Z. A. R., Rouault, T., et al. (2001) · The Journal of Infectious Diseases · doi:10.1086/323203 · Cited by 191
Hemochromatosis, Iron, and Septicemia Caused by Vibrio vulnificus
Bullen, J. J. (1991) · Archives of Internal Medicine · doi:10.1001/archinte.1991.00400080096018 · Cited by 190
Haptoglobin preserves the CD163 hemoglobin scavenger pathway by shielding hemoglobin from peroxidative modification
Buehler, P. W., Abraham, B., Vallelian, F., Linnemayr, C., Pereira, C. P., Cipollo, J. F., Jia, Y., Mikolajczyk, M. G., Boretti, F. S., Schoedon, G., et al. (2009) · Blood · doi:10.1182/blood-2008-08-174466 · Cited by 186
Crystal Structure of Hemoglobin Protease, a Heme Binding Autotransporter Protein from Pathogenic Escherichia coli
Otto, B. R., Sijbrandi, R., Luirink, J., Oudega, B., Heddle, J. G., Mizutani, K., Park, S., & Tame, J. R. H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412885200 · Cited by 180
Induction of activin B by inflammatory stimuli up-regulates expression of the iron-regulatory peptide hepcidin through Smad1/5/8 signaling
Besson-Fournier, C., Latour, C., Kautz, L., Bertrand, J., Ganz, T., Roth, M.-P., & Coppin, H. (2012) · Blood · doi:10.1182/blood-2012-02-411470 · Cited by 179
A new type of hemophore-dependent heme acquisition system of Serratia marcescens reconstituted in Escherichia coli
Ghigo, J., Létoffé, S., & Wandersman, C. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.11.3572-3579.1997 · Cited by 175
Contribution of TonB- and Feo-mediated iron uptake to growth of Salmonella typhimurium in the mouse
Tsolis, R. M., Bäumler, A. J., Heffron, F., & Stojiljkovic, I. (1996) · Infection and Immunity · doi:10.1128/iai.64.11.4549-4556.1996 · Cited by 174
Heme uptake across the outer membrane as revealed by crystal structures of the receptor–hemophore complex
Krieg, S., Huché, F., Diederichs, K., Izadi‐Pruneyre, N., Lecroisey, A., Wandersman, C., Delepelaire, P., & Welte, W. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809406106 · Cited by 170
Hemoglobin and Myoglobin Associated Oxidative Stress: from Molecular Mechanisms to Disease States
Reeder, B. J., & Wilson, M. T. (2005) · Current Medicinal Chemistry · doi:10.2174/092986705774463021 · Cited by 169
Staphylococcus aureus Fur Regulates the Expression of Virulence Factors That Contribute to the Pathogenesis of Pneumonia
Torres, V. J., Attia, A. S., Mason, W. J., Hood, M. I., Corbin, B. D., Beasley, F. C., Anderson, K. L., Stauff, D. L., McDonald, W. H., Zimmerman, L. J., et al. (2010) · Infection and Immunity · doi:10.1128/iai.01423-09 · Cited by 169
Selective modulation of TLR4-activated inflammatory responses by altered iron homeostasis in mice
Wang, L., Harrington, L., Trebicka, E., Shi, H. N., Kagan, J. C., Hong, C. C., Lin, H. Y., Babitt, J. L., & Cherayil, B. J. (2009) · Journal of Clinical Investigation · doi:10.1172/jci39939 · Cited by 162
Contribution of the Shigella flexneri Sit, Iuc, and Feo Iron Acquisition Systems to Iron Acquisition In Vitro and in Cultured Cells
Runyen-Janecky, L. J., Reeves, S. A., Gonzales, E. G., & Payne, S. M. (2003) · Infection and Immunity · doi:10.1128/iai.71.4.1919-1928.2003 · Cited by 155
Identification and Characterization of a Streptococcus pyogenes Operon Involved in Binding of Hemoproteins and Acquisition of Iron
Bates, C. S., Montañez, G. E., Woods, C. R., Vincent, R. M., & Eichenbaum, Z. (2003) · Infection and Immunity · doi:10.1128/iai.71.3.1042-1055.2003 · Cited by 154
Identification of a novel iron regulated staphylococcal surface protein with haptoglobin‐haemoglobin binding activity
Dryla, A., Gelbmann, D., Von Gabain, A., & Nagy, E. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03542.x · Cited by 153
Ferric citrate transport in Escherichia coli requires outer membrane receptor protein fecA
Wagegg, W., & Braun, V. (1981) · Journal of Bacteriology · doi:10.1128/jb.145.1.156-163.1981 · Cited by 152
Haptoglobin is synthesized during granulocyte differentiation, stored in specific granules, and released by neutrophils in response to activation
Theilgaard‐Mönch, K. (2006) · Blood · doi:10.1182/blood-2005-09-3890 · Cited by 151
RADIOACTIVE IRON AND ITS METABOLISM IN ANEMIA
Hahn, P. F., Bale, W. F., Lawrence, E. O., & Whipple, G. H. (1939) · The Journal of Experimental Medicine · doi:10.1084/jem.69.5.739 · Cited by 150
Absence of functional Hfe protects mice from invasive Salmonella enterica Serovar Typhimurium infection via induction of lipocalin-2
Nairz, M., Theurl, I., Schroll, A., Theurl, M., Fritsche, G., Lindner, E., Seifert, M., Crouch, M.-L. V., Hantke, K., Akira, S., et al. (2009) · Blood · doi:10.1182/blood-2009-05-223354 · Cited by 146
Molecular Mechanism of Hepcidin-Mediated Ferroportin Internalization Requires Ferroportin Lysines, Not Tyrosines or JAK-STAT
Ross, S. L., Tran, L., Winters, A., Lee, K.-J., Plewa, C., Foltz, I., King, C., Miranda, L. P., Allen, J., Beckman, H., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.03.017 · Cited by 145
A gene cluster involved in the utilization of both free heme and heme:hemopexin by Haemophilus influenzae type b
Cope, L. D., Yogev, R., Muller-Eberhard, U., & Hansen, E. J. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.10.2644-2653.1995 · Cited by 145
Bacillus anthracis secretes proteins that mediate heme acquisition from hemoglobin
Maresso, A. W., Garufi, G., & Schneewind, O. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000132 · Cited by 144
Staphylococcus aureus IsdG and IsdI, Heme-degrading Enzymes with Structural Similarity to Monooxygenases
Wu, R., Skaar, E. P., Zhang, R., Joachimiak, G., Gornicki, P., Schneewind, O., & Joachimiak, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m409526200 · Cited by 144
Interactions in the TonB-Dependent Energy Transduction Complex: ExbB and ExbD Form Homomultimers
Higgs, P. I., Myers, P. S., & Postle, K. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.22.6031-6038.1998 · Cited by 143
HO • radicals induce an unexpected high proportion of tandem base lesions refractory to repair by DNA glycosylases
Bergeron, F., Auvré, F., Radicella, J. P., & Ravanat, J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000193107 · Cited by 140
The IsdG‐family of haem oxygenases degrades haem to a novel chromophore
Reniere, M. L., Ukpabi, G. N., Harry, S. R., Stec, D. F., Krull, R., Wright, D. W., Bachmann, B. O., Murphy, M. E., & Skaar, E. P. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07076.x · Cited by 139
Characterization of a Hemoglobin Protease Secreted by the Pathogenic Escherichia coli Strain EB1
Otto, B. R., van Dooren, S. J. M., Nuijens, J. H., Luirink, J., & Oudega, B. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.188.6.1091 · Cited by 139
NEAT: a domain duplicated in genes near the components of a putative Fe3+siderophore transporter from Gram-positive pathogenic bacteria
Andrade, M. A., Ciccarelli, F. D., Perez-Iratxeta, C., & Bork, P. (2002) · Genome Biology · doi:10.1186/gb-2002-3-9-research0047 · Cited by 135
Use of Heme-Protein Complexes by the Yersinia enterocolitica HemR Receptor: Histidine Residues Are Essential for Receptor Function
Bracken, C. S., Baer, M. T., Abdur-Rashid, A., Helms, W. S., & Stojiljković, I. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.19.6063-6072.1999 · Cited by 133
Redox Cycling in Iron Uptake, Efflux, and Trafficking
Kosman, D. J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.113217 · Cited by 127
Heme Protein Radicals
Giulivi, C., & Cadenas, E. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00226-8 · Cited by 126
Characterization of the Vibrio cholerae outer membrane heme transport protein HutA: sequence of the gene, regulation of expression, and homology to the family of TonB-dependent proteins
Henderson, D. P., & Payne, S. M. (1994) · Journal of Bacteriology · doi:10.1128/jb.176.11.3269-3277.1994 · Cited by 125
Characterization of Ferric and Ferrous Iron Transport Systems inVibrio cholerae
Wyckoff, E. E., Mey, A. R., Leimbach, A., Fisher, C., & Payne, S. M. (2006) · Journal of Bacteriology · doi:10.1128/jb.00626-06 · Cited by 122
HmbR outer membrane receptors of pathogenic Neisseria spp.: iron-regulated, hemoglobin-binding proteins with a high level of primary structure conservation
Stojiljkovic, I., Larson, J., Hwa, V, Anic, S., & So, M. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.15.4670-4678.1996 · Cited by 121
The Secreted Pyomelanin Pigment of Legionella pneumophila Confers Ferric Reductase Activity
Chatfield, C. H., & Cianciotto, N. P. (2007) · Infection and Immunity · doi:10.1128/iai.00489-07 · Cited by 121
Bactericidal effect of bovine lactoferrin, LFcin, LFampin and LFchimera on antibiotic-resistant Staphylococcus aureus and Escherichia coli
Flores-Villaseñor, H. M., Canizalez‐Román, A., Reyes‐López, M., Nazmi, K., de la Garza, M., Zazueta-Beltrán, J., León-Sicairos, N. M., & Bolscher, J. G. M. (2010) · BioMetals · doi:10.1007/s10534-010-9306-4 · Cited by 121
Ferric Dicitrate Transport System (Fec) of Shigella flexneri 2a YSH6000 Is Encoded on a Novel Pathogenicity Island Carrying Multiple Antibiotic Resistance Genes
Luck, S. N., Turner, S. A., Rajakumar, K., Sakellaris, H., & Adler, B. (2001) · Infection and Immunity · doi:10.1128/iai.69.10.6012-6021.2001 · Cited by 120
Point mutations in a conserved region (TonB box) of Escherichia coli outer membrane protein BtuB affect vitamin B12 transport
Guðmundsdóttir, Á., Bell, P. E., Lundrigan, M. D., Bradbeer, C., & Kadner, R. J. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.12.6526-6533.1989 · Cited by 119
The Yersiniabactin Transport System Is Critical for the Pathogenesis of Bubonic and Pneumonic Plague
Fetherston, J. D., Kirillina, O. A., Bobrov, A. G., Paulley, J. T., & Perry, R. D. (2010) · Infection and Immunity · doi:10.1128/iai.01236-09 · Cited by 119
Aerobactin genes in Shigella spp
Lawlor, K. M., & Payne, S. M. (1984) · Journal of Bacteriology · doi:10.1128/jb.160.1.266-272.1984 · Cited by 117
Analyses of MbtB, MbtE, and MbtF Suggest Revisions to the Mycobactin Biosynthesis Pathway in Mycobacterium tuberculosis
McMahon, M. D., Rush, J. S., & Thomas, M. G. (2012) · Journal of Bacteriology · doi:10.1128/jb.00088-12 · Cited by 115
Intracellular survival of Burkholderia cenocepacia in macrophages is associated with a delay in the maturation of bacteria-containing vacuoles
Lamothe, J., Huynh, K. K., Grinstein, S., & Valvano, M. A. (2006) · Cellular Microbiology · doi:10.1111/j.1462-5822.2006.00766.x · Cited by 115
RADIOACTIVE IRON AND ITS EXCRETION IN URINE, BILE, AND FECES
Hahn, P. F., Bale, W. F., Hettig, R. A., Kamen, M. D., & Whipple, G. H. (1939) · The Journal of Experimental Medicine · doi:10.1084/jem.70.5.443 · Cited by 114
Escherichia coli K-12 ferrous iron uptake mutants are impaired in their ability to colonize the mouse intestine
Stojiljković, I., Cobeljić, M., & Hantke, K. (1993) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1993.tb06082.x · Cited by 111
Identification of an iron-regulated virulence determinant in Vibrio cholerae, using TnphoA mutagenesis
Goldberg, M. B., DiRita, V. J., & Calderwood, S. B. (1990) · Infection and Immunity · doi:10.1128/iai.58.1.55-60.1990 · Cited by 109
Characterization of lbpA, the structural gene for a lactoferrin receptor in Neisseria gonorrhoeae
Biswas, G. D., & Sparling, P. F. (1995) · Infection and Immunity · doi:10.1128/iai.63.8.2958-2967.1995 · Cited by 106
Transfer of heme from heme-albumin to hemopexin
Morgan, W. T., Liem, H. H., Sutor, R. P., & Müller‐Eberhard, U. (1976) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(76)90387-1 · Cited by 106
Ferritin L and H Subunits Are Differentially Regulated on a Post-transcriptional Level
Sammarco, M. C., Ditch, S., Banerjee, A., & Grabczyk, E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703456200 · Cited by 102
Nucleotide sequence of a cluster of Escherichia coli enterobactin biosynthesis genes: identification of entA and purification of its product 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
Liu, J., Duncan, K., & Walsh, C. T. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.2.791-798.1989 · Cited by 100
Fur Negatively Regulates hns and Is Required for the Expression of HilA and Virulence in Salmonella enterica Serovar Typhimurium
Troxell, B., Sikes, M. L., Fink, R. C., Vazquez-Torres, A., Jones-Carson, J., & Hassan, H. M. (2011) · Journal of Bacteriology · doi:10.1128/jb.00942-10 · Cited by 99
Organic Sequestering Agents, von St. Chaberek und A. E. Martell. John Wiley u. Sons, Inc. New York, Chapman u. Hall., Ltd., London 1959. 1. Aufl., 616 S., geb. $ 25.—
FISCHER, E. O. (1960) · Angewandte Chemie · doi:10.1002/ange.19600721524 · Cited by 97
Identification of an iron-regulated outer membrane protein of Neisseria meningitidis involved in the utilization of hemoglobin complexed to haptoglobin
Lewis, L. A., & Dyer, D. W. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.5.1299-1306.1995 · Cited by 97
Identification and Characterization of the Staphylococcus aureus Gene Cluster Coding for Staphyloferrin A
Cotton, J. L., Tao, J., & Balibar, C. J. (2009) · Biochemistry · doi:10.1021/bi801844c · Cited by 95
Nature of the FeO2 bonding in myoglobin and hemoglobin: A new molecular paradigm
Shikama, K. (2005) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2005.04.001 · Cited by 95
The Cytoplasmic Heme-binding Protein (PhuS) from the Heme Uptake System of Pseudomonas aeruginosa Is an Intracellular Heme-trafficking Protein to the δ-Regioselective Heme Oxygenase
Lansky, I. B., Lukat-Rodgers, G. S., Block, D., Rodgers, K. R., Ratliff, M., & Wilks, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600824200 · Cited by 92
Identification of an Escherichia coli O157:H7 heme oxygenase with tandem functional repeats
Suits, M. D. L., Pal, G. P., Nakatsu, K., Matte, A., Cygler, M., & Jia, Z. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504289102 · Cited by 91
IlsA, A Unique Surface Protein of Bacillus cereus Required for Iron Acquisition from Heme, Hemoglobin and Ferritin
Daou, N., Buisson, C., Gohar, M., Vidić, J., Bierne, H., Kallassy, M., Lereclus, D., & Nielsen‐LeRoux, C. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000675 · Cited by 90
Heme Degradation by Staphylococcus aureus IsdG and IsdI Liberates Formaldehyde Rather Than Carbon Monoxide
Matsui, T., Nambu, S., Ono, Y., Goulding, C. W., Tsumoto, K., & Ikeda‐Saito, M. (2013) · Biochemistry · doi:10.1021/bi400382p · Cited by 90
Overproduction, purification and characterization of the Escherichia coli ferritin
Hudson, A. J., Andrews, S. C., Hawkins, C., Williams, J. M., Izuhara, M., Meldrum, F. C., Mann, S., Harrison, P. M., & Guest, J. R. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb18457.x · Cited by 88
Hereditary hemochromatosis results in decreased iron acquisition and growth by Mycobacterium tuberculosis within human macrophages
Olakanmi, O., Schlesinger, L. S., & Britigan, B. E. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0606405 · Cited by 88
Neisseria meningitidis accelerates ferritin degradation in host epithelial cells to yield an essential iron source
Larson, J. A., Howie, H. L., & So, M. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04169.x · Cited by 85
Quantitative Measurement of Hematopoietic Cells of the Marrow1
Donohue, D. M., Gabrio, B. W., & Finch, C. A. (1958) · Journal of Clinical Investigation · doi:10.1172/jci103749 · Cited by 85
Hepatocyte-specific mutation of both NF-κB RelA and STAT3 abrogates the acute phase response in mice
Quinton, L. J., Blahna, M. T., Jones, M. R., Allen, E., Ferrari, J. D., Hilliard, K. L., Zhang, X., Sabharwal, V., Algül, H., Akira, S., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci59408 · Cited by 84
Cloning of a Vibrio cholerae vibriobactin gene cluster: identification of genes required for early steps in siderophore biosynthesis
Wyckoff, E. E., Stoebner, J. A., Reed, K. E., & Payne, S. M. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.22.7055-7062.1997 · Cited by 82
Identification of shuA, the gene encoding the heme receptor of Shigella dysenteriae, and analysis of invasion and intracellular multiplication of a shuA mutant
Mills, M., & Payne, S. M. (1997) · Infection and Immunity · doi:10.1128/iai.65.12.5358-5363.1997 · Cited by 78
High-Affinity Binding of the Staphylococcal HarA Protein to Haptoglobin and Hemoglobin Involves a Domain with an Antiparallel Eight-Stranded β-Barrel Fold
Dryla, A., Hoffmann, B., Gelbmann, D., Giefing, C., Hanner, M., Meinke, A., Anderson, A. S., Koppensteiner, W., Konrat, R., von Gabain, A., et al. (2007) · Journal of Bacteriology · doi:10.1128/jb.01366-06 · Cited by 73
A New Role for Heme, Facilitating Release of Iron from the Bacterioferritin Iron Biomineral
Yasmin, S., Andrews, S. C., Moore, G. R., & Brun, N. E. L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.175034 · Cited by 72
Characterization of the human transferrin and lactoferrin receptors in Haemophilus influenzae
Schryvers, A. B. (1988) · Molecular Microbiology · doi:10.1111/j.1365-2958.1988.tb00052.x · Cited by 71
Denatured H-ferritin subunit is a major constituent of haemosiderin in the liver of patients with iron overload
Miyazaki, E., Kato, J., Kobune, M., Okumura, K., Sasaki, K., Shintani, N., Arosio, P., & Niitsu, Y. (2002) · Gut · doi:10.1136/gut.50.3.413 · Cited by 71
Heme transfer to the bacterial cell envelope occurs via a secreted hemophore in the Gram-positive pathogen Bacillus anthracis
Fabian, M., Solomaha, E., Olson, J. S., & Maresso, A. W. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.040915 · Cited by 70
Shigella dysenteriae ShuS Promotes Utilization of Heme as an Iron Source and Protects against Heme Toxicity
Wyckoff, E. E., Lopreato, G. F., Tipton, K. A., & Payne, S. M. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.16.5658-5664.2005 · Cited by 69
Staphylococci express a receptor for human transferrin: identification of a 42-kilodalton cell wall transferrin-binding protein
Modun, B. J., Kendall, D. A., & Williams, P. M. (1994) · Infection and Immunity · doi:10.1128/iai.62.9.3850-3858.1994 · Cited by 68
Characterization of Heme Ligation Properties of Rv0203, a Secreted Heme Binding Protein Involved in Mycobacterium tuberculosis Heme Uptake
Owens, C. P., Du, J., Dawson, J. H., & Goulding, C. W. (2012) · Biochemistry · doi:10.1021/bi2018305 · Cited by 68
Solution Structure of Escherichia coli FeoA and Its Potential Role in Bacterial Ferrous Iron Transport
Lau, C. K. Y., Ishida, H., Liu, Z., & Vogel, H. J. (2012) · Journal of Bacteriology · doi:10.1128/jb.01121-12 · Cited by 68
Iron release from haemosiderin and production of iron-catalysed hydroxyl radicals in vitro
Ozaki, M., Kawabata, T., & Awai, M. (1988) · Biochemical Journal · doi:10.1042/bj2500589 · Cited by 66
Bacterioferritins and ferritins are distantly related in evolution Conservation of ferroxidase‐centre residues
Andrews, S. C., Smith, J. M., Yewdall, S. J., Guest, J. R., & Harrison, P. M. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)81177-a · Cited by 66
Overproduction, purification and characterization of the bacterioferritin of Escherichia coli and a C‐terminally extended variant
Andrews, S. C., Smith, J. M., Hawkins, C., Williams, J. M., Harrison, P. M., & Guest, J. R. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb17766.x · Cited by 65
The Siderophore Receptor IroN, but Not the High-Pathogenicity Island or the Hemin Receptor ChuA, Contributes to the Bacteremic Step of Escherichia coli Neonatal Meningitis
Nègre, V. L., Bonacorsi, S., Schubert, S., Bidet, P., Nassif, X., & Bingen, É. (2004) · Infection and Immunity · doi:10.1128/iai.72.2.1216-1220.2004 · Cited by 65
Specific Hemosiderin Deposition in Spleen Induced by a Low Dose of Cisplatin: Altered Iron Metabolism and Its Implication as an Acute Hemosiderin Formation Model
Wang, Y., Juan, L. V., Ma, X., Wang, D., Ma, H., Chang, Y., Nie, G., Jia, L., Duan, X., & Liang, X. (2010) · Current Drug Metabolism · doi:10.2174/138920010791636149 · Cited by 64
Effects of Chelators (Deferoxamine, Deferiprone and Deferasirox) on the Growth ofKlebsiella PneumoniaeandAeromonas HydrophilaIsolated from Transfusion-Dependent Thalassemia Patients
Chan, G., Chan, S., Ho, P., & Ha, S. (2009) · Hemoglobin · doi:10.3109/03630260903211888 · Cited by 64
Iron uptake and iron limited growth of Escherichia coli K-12
Hartmann, A., & Braun, V. (1981) · Archives of Microbiology · doi:10.1007/bf00414599 · Cited by 60
Duodenal Reductase Activity and Spleen Iron Stores Are Reduced and Erythropoiesis Is Abnormal in Dcytb Knockout Mice Exposed to Hypoxic Conditions3
Choi, J., Masaratana, P., Latunde-Dada, G. O., Arno, M. J., Simpson, R. J., & McKie, A. T. (2012) · Journal of Nutrition · doi:10.3945/jn.112.160358 · Cited by 60
The ABC Transporter HrtAB Confers Resistance to Hemin Toxicity and Is Regulated in a Hemin-Dependent Manner by the ChrAS Two-Component System in Corynebacterium diphtheriae
Bibb, L. A., & Schmitt, M. P. (2010) · Journal of Bacteriology · doi:10.1128/jb.00525-10 · Cited by 59
Extracellular Iron Reductases: Identification of a New Class of Enzymes by Siderophore-Producing Microorganisms
Vartivarian, S. E., & Cowart, R. E. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1109 · Cited by 58
Yersinia enterocolitica Infection with Multiple Liver Abscesses Uncovering a Primary Hemochromatosis
Höpfner, M., Nitsche, R., Rohr, A., Harms, D., Schubert, S., & Fölsch, U. R. (2001) · Scandinavian Journal of Gastroenterology · doi:10.1080/003655201750066004 · Cited by 56
Human endothelial cells regulate polymorphonuclear leukocyte degranulation
Topham, M. K., Carveth, H., McIntyre, T. M., Prescott, S. M., & Zimmerman, G. A. (1998) · The FASEB Journal · doi:10.1096/fasebj.12.9.733 · Cited by 56
The role of the cytoplasmic heme-binding protein (PhuS) of Pseudomonas aeruginosa in intracellular heme trafficking and iron homeostasis
Kaur, A. P., Lansky, I. B., & Wilks, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806068200 · Cited by 55
Brucella abortusRequires the Heme Transporter BhuA for Maintenance of Chronic Infection in BALB/c Mice
Paulley, J. T., Anderson, E. S., & Roop, R. M. (2007) · Infection and Immunity · doi:10.1128/iai.00460-07 · Cited by 54
The heme-binding protein (HbpA) of Haemophilus influenzae as a virulence determinant
Morton, D. J., Seale, T. W., Bakaletz, L. O., Jurcisek, J. A., Smith, A., VanWagoner, T. M., Whitby, P. W., & Stull, T. L. (2009) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2009.03.004 · Cited by 53
Burkholderia cenocepacia utilizes ferritin as an iron source
Whitby, P. W., VanWagoner, T. M., Springer, J. M., Morton, D. J., Seale, T. W., & Stull, T. L. (2006) · Journal of Medical Microbiology · doi:10.1099/jmm.0.46199-0 · Cited by 53
Anemia and impaired stress-induced erythropoiesis in aceruloplasminemic mice
Cherukuri, S., Tripoulas, N. A., Nurko, S., & Fox, P. L. (2004) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2004.07.003 · Cited by 52
Cloning and expression of the Haemophilus influenzae transferrin receptor genes
Loosmore, S. M., Yang, Y., Coleman, D. C., Shortreed, J. M., England, D. M., Harkness, R. E., Chong, P. C.-S., & Klein, M. H. (1996) · Molecular Microbiology · doi:10.1046/j.1365-2958.1996.406943.x · Cited by 51
Identification of an outer membrane protein involved in utilization of hemoglobin-haptoglobin complexes by nontypeable Haemophilus influenzae
Maciver, I., Latimer, J. L., Liem, H. H., Müller‐Eberhard, U., Hrkal, Z., & Hansen, E. J. (1996) · Infection and Immunity · doi:10.1128/iai.64.9.3703-3712.1996 · Cited by 51
Late stage erythroid precursor production is impaired in mice with chronic inflammation
Prince, O. D., Langdon, J., Layman, A. J., Prince, I. C., Sabogal, M. A., Mak, H. H., Berger, A. E., Cheadle, C., Chrest, F. J., Yu, Q., et al. (2012) · Haematologica · doi:10.3324/haematol.2011.053397 · Cited by 48
Ferritin upregulates hepatic expression of bone morphogenetic protein 6 and hepcidin in mice
Feng, Q., Migas, M. C., Waheed, A., Britton, R. S., & Fleming, R. E. (2012) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00020.2012 · Cited by 47
Bordetella pertussisTonB, a Bvg-Independent Virulence Determinant
Pradel, E., Guiso, N., Menozzi, F. D., & Locht, C. (2000) · Infection and Immunity · doi:10.1128/iai.68.4.1919-1927.2000 · Cited by 47
Normal Iron Absorption Determined by Means of Whole Body Counting and Red Cell Incorporation of 59Fe
Larsen, L., & Milman, N. T. (1975) · Acta Medica Scandinavica · doi:10.1111/j.0954-6820.1975.tb19539.x · Cited by 45
Extracellular iron reductase activity produced by Listeria monocytogenes
Barchini, E., & Cowart, R. E. (1996) · Archives of Microbiology · doi:10.1007/s002030050354 · Cited by 44
Increased ferritin synthesis and iron uptake in inflammatory mouse macrophages
Birgegård, G., & Caro, J. (1984) · Scandinavian Journal of Haematology · doi:10.1111/j.1600-0609.1984.tb02208.x · Cited by 44
Structural insight into the lactoferrin receptors from pathogenic Neisseria
Noinaj, N., Cornelissen, C. N., & Buchanan, S. K. (2013) · Journal of Structural Biology · doi:10.1016/j.jsb.2013.02.009 · Cited by 42
Comparison of siderophore production and utilization in pathogenic and environmental isolates of Yersinia enterocolitica
Chambers, C. E., & Sokol, P. A. (1994) · Journal of Clinical Microbiology · doi:10.1128/jcm.32.1.32-39.1994 · Cited by 41
Evidence for siderophore‐dependent iron acquisition in group B streptococcus
Clancy, A., Loar, J. W., Speziali, C. D., Oberg, M. D., Heinrichs, D. E., & Rubens, C. E. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04974.x · Cited by 39
Ceruloplasmin reduces the adhesion and scavenges superoxide during the interaction of activated polymorphonuclear leukocytes with endothelial cells.
Broadley, C., & Hoover, R. L. (1989) · PubMed · Cited by 38
Differential gene expression in Streptococcus pneumoniae in response to various iron sources
Gupta, R., Shah, P. H., & Swiatlo, E. (2009) · Microbial Pathogenesis · doi:10.1016/j.micpath.2009.05.003 · Cited by 37
Dietary iron regulates hepatic hepcidin 1 and 2 mRNAs in mice
Mazur, A., Feillet‐Coudray, C., Romier, B., Bayle, D., Gueux, E., Ruivard, M., Coudray, C., & Rayssiguier, Y. (2003) · Metabolism · doi:10.1016/s0026-0495(03)00277-4 · Cited by 36
Bacteremic cellulitis caused by Non-01, Non-0139 Vibrio cholerae: report of a case in a patient with hemochromatosis
Fernández, J. M., Serrano, M., Méndez, J. J. D. A., Sánchez, V., Escribano, E., & Ferreras, P. (2000) · Diagnostic Microbiology and Infectious Disease · doi:10.1016/s0732-8893(99)00153-4 · Cited by 36
Role of the Yersinia pestis Yersiniabactin Iron Acquisition System in the Incidence of Flea-Borne Plague
Sebbane, F., Jarrett, C. O., Gardner, D. J., Long, D., & Hinnebusch, B. J. (2010) · PLoS ONE · doi:10.1371/journal.pone.0014379 · Cited by 36
Function, Regulation, and Transcriptional Organization of the Hemin Utilization Locus of Bartonella quintana
Parrow, N. L., Abbott, J., Lockwood, A. R., Battisti, J. M., & Minnick, M. F. (2008) · Infection and Immunity · doi:10.1128/iai.01194-08 · Cited by 36
Self-citation
EspC, an autotransporter protein secreted by enteropathogenic Escherichia coli (EPEC), displays protease activity on human hemoglobin
Drago-Serrano, M. E., Parra, S. G., & Manjarrez-HernÃ¡ndez, H. A. (2006) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2006.00463.x · Cited by 35
Fatal Listeria Meningitis, Endocarditis and Pericarditis in a Patient with Haemochromatosis
Manso, C., Rivas, I., Peraire, J., Vidal, F., & Richart, C. (1997) · Scandinavian Journal of Infectious Diseases · doi:10.3109/00365549709019049 · Cited by 35
Lipoprotein MtsA of MtsABC in Streptococcus pyogenes primarily binds ferrous ion with bicarbonate as a synergistic anion
Sun, X., Ge, R., Chiu, J., Sun, H., & He, Q. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.03.020 · Cited by 35
Identification of functionally important regions of a haemoglobin receptor from Neisseria meningitidis
Perkins-Balding, D., Baer, M. T., & Stojiljković, I. (2003) · Microbiology · doi:10.1099/mic.0.26448-0 · Cited by 35
Ferritin L is the Sole Serum Ferritin Constituent and a Positive Hepatic Acute-Phase Protein
Naz, N., Moriconi, F., Ahmad, S., Amanzada, A., Khan, S., Mihm, S., Ramadori, G., & Malik, I. A. (2013) · Shock · doi:10.1097/shk.0b013e31829266b9 · Cited by 31
Escherichia coli Bacteremia, Meningitis, and Hemochromatosis
Christopher, G. W. (1985) · Archives of Internal Medicine · doi:10.1001/archinte.1985.00360100178031 · Cited by 26
Does the haemosiderin iron core determine its potential for chelation and the development of iron-induced tissue damage?
Ward, R. J., Legssyer, R., Henry, C., & Crichton, R. R. (2000) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(99)00237-8 · Cited by 25
Different isolates from Leishmania braziliensis complex induce distinct histopathological features in a murine model of infection
Pereira, C. G., Silva, A. L. N., de Castilhos, P., Mastrantônio, E. C., Souza, R. A., Ribeiro‐Romão, R. P., Rezende, R. J., Pena, J. D. O., Beletti, M. E., & de Souza, M. A. (2009) · Veterinary Parasitology · doi:10.1016/j.vetpar.2009.07.019 · Cited by 24
Ferroportin (SLC40A1) Q248H mutation is associated with lower circulating serum hepcidin levels in Rwandese HIV-positive women
Masaisa, F., Breman, C., Gahutu, J. B., Mukiibi, J. M., Delanghe, J., & Philippé, J. (2012) · Annals of Hematology · doi:10.1007/s00277-011-1400-3 · Cited by 22
Identification of a siderophore utilization locus in nontypeable Haemophilus influenzae
Morton, D. J., Turman, E. J., Hensley, P. D., VanWagoner, T. M., Seale, T. W., Whitby, P. W., & Stull, T. L. (2010) · BMC Microbiology · doi:10.1186/1471-2180-10-113 · Cited by 22
Utilization of myoglobin as a heme source by Haemophilus influenzae requires binding of myoglobin to haptoglobin
Morton, D. J., Van Wagoner, T. M., Seale, T. W., Whitby, P. W., & Stull, T. L. (2006) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2006.00230.x · Cited by 18
Passively Released Heme from Hemoglobin and Myoglobin Is a Potential Source of Nutrient Iron for Bordetella bronchiseptica
Mocny, J. C., Olson, J. S., & Connell, T. D. (2007) · Infection and Immunity · doi:10.1128/iai.00407-07 · Cited by 18
Polymorphisms in the Gene That Encodes the Iron Transport Protein Ferroportin 1 Influence Susceptibility to Tuberculosis
Baker, M. A., Wilson, D., Wallengren, K., Sandgren, A., Iartchouk, O., Broodie, N., Goonesekera, S. D., Sabeti, P. C., & Murray, M. B. (2012) · The Journal of Infectious Diseases · doi:10.1093/infdis/jis026 · Cited by 15
Disintegration of red cell membrane cytoskeleton by hemin.
Shaklai, N., Avissar, N. E., Rabizadeh, E., & Shaklai, M. (1986) · PubMed · Cited by 13
Changes of hepatic lactoferrin gene expression in two mouse models of the acute phase reaction
Ahmad, G., Sial, G. Z. K., Ramadori, P., Dudás, J., Batusic, D. S., & Ramadori, G. P. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.09.002 · Cited by 11
Yersinia Hepatic Abscesses and Iron Overload
Chiesa, C. (1987) · JAMA · doi:10.1001/jama.1987.03390230066023 · Cited by 10
Hypotransferrinemia and changes in plasma lipid and metabolic patterns in sepsis
Chiarla, C., Giovannini, I., & Siegel, J. H. (2008) · Amino Acids · doi:10.1007/s00726-008-0072-3 · Cited by 9

Research works printed but not linked: 1

ChaberekSMartellAE. 1959. Organic sequestering agents. John Wiley & Sons, Inc, New York, NY.

Sorted by citations

Staphylococcal Biofilm Development: Structure, Regulation, and Treatment Strategies
Schilcher, K., & Horswill, A. R. (2020) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00026-19 · Cited by 762
Sequential activation of microglia and astrocyte cytokine expression precedes increased iba‐1 or GFAP immunoreactivity following systemic immune challenge
Norden, D. M., Trojanowski, P. J., Villanueva, E., Navarro, E., & Godbout, J. P. (2015) · Glia · doi:10.1002/glia.22930 · Cited by 623
Anemia and iron metabolism in COVID-19: a systematic review and meta-analysis
Taneri, P. E., Gómez-Ochoa, S. A., Llanaj, E., Raguindin, P. F., Rojas, L. Z., Roa-Díaz, Z. M., Salvador, D., Groothof, D., Minder, B., Kopp-Heim, D., et al. (2020) · European Journal of Epidemiology · doi:10.1007/s10654-020-00678-5 · Cited by 369
Iron, copper, zinc, and manganese transport and regulation in pathogenic Enterobacteria: correlations between strains, site of infection and the relative importance of the different metal transport systems for virulence
Porcheron, G., Garénaux, A., Proulx, J., Sabri, M., & Dozois, C. M. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00090 · Cited by 385
Host-Associated Probiotics: A Key Factor in Sustainable Aquaculture
Doan, H. V., Hoseinifar, S. H., Ringø, E., Esteban, M. Á., Dadar, M., Dawood, M. A. O., & Faggio, C. (2019) · Reviews in Fisheries Science & Aquaculture · doi:10.1080/23308249.2019.1643288 · Cited by 365

See all 261

Authors: Parrow, N. L., Fleming, R. E., & Minnick, M. F.
Affiliations: National Institutes of Health (US)
Saint Louis University (US)
University of Montana (US)
ORCID: Parrow, Nermi L.
Fleming, Robert E.
Minnick, Michael F.
Venue: Infection and Immunity
Publisher: American Society for Microbiology
Published: 2013-10
Volume: 81
Issue: 10
Pages: 3503-3514
ISSN: 0019-9567 (ISSN-L)
1098-5522
DOI: 10.1128/iai.00602-13
PMC: PMC3811770
OpenAlex: W2126286427
Cited by: 261
References: 179
Citations by year: 2026: 14 · 2025: 26 · 2024: 25 · 2023: 24 · 2022: 25 · 2021: 26 · 2020: 31 · 2019: 26 · 2018: 16 · 2017: 16 · 2016: 11 · 2015: 11 · 2014: 8 · 2013: 1
FWCI: 7.42
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Infection and Immunity (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
The Mathematics Enthusiast (submittedVersion)
Funders: National Institutes of Health
Topics: Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Life Sciences › Immunology and Microbiology › Microbiology › Escherichia coli research studies
Keywords: iron sequestration, iron scavenging, iron bioavailability, bacterial virulence, host-pathogen interaction, acute phase response, iron overload, bacterial iron acquisition, host defense against infection
MeSH terms: Animals, Bacteria, Homeostasis, Humans, Iron

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

Sequestration and Scavenging of Iron in Infection

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