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Volumn 16, Issue 11, 2015, Pages 1482-1500

The Iron age of host-microbe interactions

Author keywords

anemia of chronic disease; disease tolerance; heme; iron; macrophage; nutritional immunity; tissue damage control

Indexed keywords

IRON; HEME;

EID: 84946068281     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.15252/embr.201540558     Document Type: Review
Times cited : (176)

References (242)
  • 1
    • 84857538593 scopus 로고    scopus 로고
    • Disease tolerance as a defense strategy
    • Medzhitov R, Schneider DS, Soares MP, (2012) Disease tolerance as a defense strategy. Science 335: 936-941
    • (2012) Science , vol.335 , pp. 936-941
    • Medzhitov, R.1    Schneider, D.S.2    Soares, M.P.3
  • 2
    • 84922509025 scopus 로고    scopus 로고
    • Infection-avoidance behaviour in humans and other animals
    • Curtis VA, (2014) Infection-avoidance behaviour in humans and other animals. Trends Immunol 35: 457-464
    • (2014) Trends Immunol , vol.35 , pp. 457-464
    • Curtis, V.A.1
  • 4
    • 0016614384 scopus 로고
    • Nutritional immunity. Host's attempt to withold iron from microbial invaders
    • Weinberg ED, (1975) Nutritional immunity. Host's attempt to withold iron from microbial invaders. JAMA 231: 39-41
    • (1975) JAMA , vol.231 , pp. 39-41
    • Weinberg, E.D.1
  • 5
    • 67349234858 scopus 로고    scopus 로고
    • Iron availability and infection
    • Weinberg ED, (2009) Iron availability and infection. Biochim Biophys Acta 1790: 600-605
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 600-605
    • Weinberg, E.D.1
  • 7
    • 84877869322 scopus 로고    scopus 로고
    • Iron in infection and immunity
    • Cassat JE, Skaar EP, (2013) Iron in infection and immunity. Cell Host Microbe 13: 509-519
    • (2013) Cell Host Microbe , vol.13 , pp. 509-519
    • Cassat, J.E.1    Skaar, E.P.2
  • 10
    • 84923357083 scopus 로고    scopus 로고
    • Homeostasis, inflammation, and disease susceptibility
    • Kotas ME, Medzhitov R, (2015) Homeostasis, inflammation, and disease susceptibility. Cell 160: 816-827
    • (2015) Cell , vol.160 , pp. 816-827
    • Kotas, M.E.1    Medzhitov, R.2
  • 11
    • 84922527244 scopus 로고    scopus 로고
    • Tissue damage control in disease tolerance
    • Soares MP, Gozzelino R, Weis S, (2014) Tissue damage control in disease tolerance. Trends Immunol 35: 483-494
    • (2014) Trends Immunol , vol.35 , pp. 483-494
    • Soares, M.P.1    Gozzelino, R.2    Weis, S.3
  • 13
    • 84954358205 scopus 로고    scopus 로고
    • Two ways to survive infection: What resistance and tolerance can teach us about treating infectious diseases
    • Schneider DS, Ayres JS, (2008) Two ways to survive infection: what resistance and tolerance can teach us about treating infectious diseases. Nat Rev Immunol 8: 889-895
    • (2008) Nat Rev Immunol , vol.8 , pp. 889-895
    • Schneider, D.S.1    Ayres, J.S.2
  • 15
    • 0003264263 scopus 로고
    • Immunological tolerance
    • Medawar PB, (1961) Immunological tolerance. Nature 189: 14-17
    • (1961) Nature , vol.189 , pp. 14-17
    • Medawar, P.B.1
  • 16
    • 84924923567 scopus 로고    scopus 로고
    • Metal limitation and toxicity at the interface between host and pathogen
    • Becker KW, Skaar EP, (2014) Metal limitation and toxicity at the interface between host and pathogen. FEMS Microbiol Rev 38: 1235-1249
    • (2014) FEMS Microbiol Rev , vol.38 , pp. 1235-1249
    • Becker, K.W.1    Skaar, E.P.2
  • 17
    • 84868526205 scopus 로고    scopus 로고
    • Hepcidin and the iron-infection axis
    • Drakesmith H, Prentice AM, (2012) Hepcidin and the iron-infection axis. Science 338: 768-772
    • (2012) Science , vol.338 , pp. 768-772
    • Drakesmith, H.1    Prentice, A.M.2
  • 21
  • 22
    • 82555176482 scopus 로고    scopus 로고
    • Superinfection in malaria: Plasmodium shows its iron will
    • Portugal S, Drakesmith H, Mota MM, (2011) Superinfection in malaria: plasmodium shows its iron will. EMBO Rep 12: 1233-1242
    • (2011) EMBO Rep , vol.12 , pp. 1233-1242
    • Portugal, S.1    Drakesmith, H.2    Mota, M.M.3
  • 24
    • 84883390077 scopus 로고    scopus 로고
    • Iron fortification and malaria risk in children
    • Prentice AM, Verhoef H, Cerami C, (2013) Iron fortification and malaria risk in children. JAMA 310: 914-915
    • (2013) JAMA , vol.310 , pp. 914-915
    • Prentice, A.M.1    Verhoef, H.2    Cerami, C.3
  • 26
    • 30444459334 scopus 로고    scopus 로고
    • Effects of routine prophylactic supplementation with iron and folic acid on admission to hospital and mortality in preschool children in a high malaria transmission setting: Community-based, randomised, placebo-controlled trial
    • Sazawal S, Black RE, Ramsan M, Chwaya HM, Stoltzfus RJ, Dutta A, Dhingra U, Kabole I, Deb S, Othman MK, et al, (2006) Effects of routine prophylactic supplementation with iron and folic acid on admission to hospital and mortality in preschool children in a high malaria transmission setting: community-based, randomised, placebo-controlled trial. Lancet 367: 133-143
    • (2006) Lancet , vol.367 , pp. 133-143
    • Sazawal, S.1    Black, R.E.2    Ramsan, M.3    Chwaya, H.M.4    Stoltzfus, R.J.5    Dutta, A.6    Dhingra, U.7    Kabole, I.8    Deb, S.9    Othman, M.K.10    Al, E.11
  • 27
    • 84879888176 scopus 로고    scopus 로고
    • Effect of provision of daily zinc and iron with several micronutrients on growth and morbidity among young children in Pakistan: A cluster-randomised trial
    • Soofi S, Cousens S, Iqbal SP, Akhund T, Khan J, Ahmed I, Zaidi AK, Bhutta ZA, (2013) Effect of provision of daily zinc and iron with several micronutrients on growth and morbidity among young children in Pakistan: a cluster-randomised trial. Lancet 382: 29-40
    • (2013) Lancet , vol.382 , pp. 29-40
    • Soofi, S.1    Cousens, S.2    Iqbal, S.P.3    Akhund, T.4    Khan, J.5    Ahmed, I.6    Zaidi, A.K.7    Bhutta, Z.A.8
  • 31
    • 84889573712 scopus 로고    scopus 로고
    • Bacterial receptors for host transferrin and lactoferrin: Molecular mechanisms and role in host-microbe interactions
    • Morgenthau A, Pogoutse A, Adamiak P, Moraes TF, Schryvers AB, (2013) Bacterial receptors for host transferrin and lactoferrin: molecular mechanisms and role in host-microbe interactions. Future Microbiol 8: 1575-1585
    • (2013) Future Microbiol , vol.8 , pp. 1575-1585
    • Morgenthau, A.1    Pogoutse, A.2    Adamiak, P.3    Moraes, T.F.4    Schryvers, A.B.5
  • 33
    • 8644220677 scopus 로고    scopus 로고
    • Siderophore biosynthesis but not reductive iron assimilation is essential for Aspergillus fumigatus virulence
    • Schrettl M, Bignell E, Kragl C, Joechl C, Rogers T, Arst HN Jr, Haynes K, Haas H, (2004) Siderophore biosynthesis but not reductive iron assimilation is essential for Aspergillus fumigatus virulence. J Exp Med 200: 1213-1219
    • (2004) J Exp Med , vol.200 , pp. 1213-1219
    • Schrettl, M.1    Bignell, E.2    Kragl, C.3    Joechl, C.4    Rogers, T.5    Arst, H.N.6    Haynes, K.7    Haas, H.8
  • 34
    • 84916936154 scopus 로고    scopus 로고
    • Nutritional immunity. Escape from bacterial iron piracy through rapid evolution of transferrin
    • Barber MF, Elde NC, (2014) Nutritional immunity. Escape from bacterial iron piracy through rapid evolution of transferrin. Science 346: 1362-1366
    • (2014) Science , vol.346 , pp. 1362-1366
    • Barber, M.F.1    Elde, N.C.2
  • 36
    • 84874243821 scopus 로고    scopus 로고
    • Staphylococcus aureus FepA and FepB proteins drive heme iron utilization in Escherichia coli
    • Turlin E, Debarbouille M, Augustyniak K, Gilles AM, Wandersman C, (2013) Staphylococcus aureus FepA and FepB proteins drive heme iron utilization in Escherichia coli. PLoS ONE 8: e56529
    • (2013) PLoS ONE , vol.8 , pp. e56529
    • Turlin, E.1    Debarbouille, M.2    Augustyniak, K.3    Gilles, A.M.4    Wandersman, C.5
  • 37
    • 84883378968 scopus 로고    scopus 로고
    • Malaria parasite-synthesized heme is essential in the mosquito and liver stages and complements host heme in the blood stages of infection
    • Nagaraj VA, Sundaram B, Varadarajan NM, Subramani PA, Kalappa DM, Ghosh SK, Padmanaban G, (2013) Malaria parasite-synthesized heme is essential in the mosquito and liver stages and complements host heme in the blood stages of infection. PLoS Pathog 9: e1003522
    • (2013) PLoS Pathog , vol.9 , pp. e1003522
    • Nagaraj, V.A.1    Sundaram, B.2    Varadarajan, N.M.3    Subramani, P.A.4    Kalappa, D.M.5    Ghosh, S.K.6    Padmanaban, G.7
  • 40
    • 0014348401 scopus 로고
    • The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase
    • Tenhunen R, Marver HS, Schmid R, (1968) The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase. Proc Natl Acad Sci USA 61: 748
    • (1968) Proc Natl Acad Sci USA , vol.61 , pp. 748
    • Tenhunen, R.1    Marver, H.S.2    Schmid, R.3
  • 44
    • 84859885581 scopus 로고    scopus 로고
    • Variations in the heme oxygenase-1 microsatellite polymorphism are associated with plasma CD14 and viral load in HIV-infected African-Americans
    • Seu L, Burt TD, Witte JS, Martin JN, Deeks SG, McCune JM, (2012) Variations in the heme oxygenase-1 microsatellite polymorphism are associated with plasma CD14 and viral load in HIV-infected African-Americans. Genes Immun 13: 258-267
    • (2012) Genes Immun , vol.13 , pp. 258-267
    • Seu, L.1    Burt, T.D.2    Witte, J.S.3    Martin, J.N.4    Deeks, S.G.5    McCune, J.M.6
  • 48
    • 84922426001 scopus 로고    scopus 로고
    • 'Ride on the ferrous wheel'-the cycle of iron in macrophages in health and disease
    • Nairz M, Schroll A, Demetz E, Tancevski I, Theurl I, Weiss G, (2015) 'Ride on the ferrous wheel'-the cycle of iron in macrophages in health and disease. Immunobiology 220: 280-294
    • (2015) Immunobiology , vol.220 , pp. 280-294
    • Nairz, M.1    Schroll, A.2    Demetz, E.3    Tancevski, I.4    Theurl, I.5    Weiss, G.6
  • 49
    • 84929186045 scopus 로고    scopus 로고
    • Macrophages and iron trafficking at the birth and death of red cells
    • Korolnek T, Hamza I, (2015) Macrophages and iron trafficking at the birth and death of red cells. Blood 125: 2893-2897
    • (2015) Blood , vol.125 , pp. 2893-2897
    • Korolnek, T.1    Hamza, I.2
  • 52
    • 41649110613 scopus 로고    scopus 로고
    • Sequential regulation of ferroportin expression after erythrophagocytosis in murine macrophages: Early mRNA induction by haem, followed by iron-dependent protein expression
    • Delaby C, Pilard N, Puy H, Canonne-Hergaux F, (2008) Sequential regulation of ferroportin expression after erythrophagocytosis in murine macrophages: early mRNA induction by haem, followed by iron-dependent protein expression. Biochem J 411: 123-131
    • (2008) Biochem J , vol.411 , pp. 123-131
    • Delaby, C.1    Pilard, N.2    Puy, H.3    Canonne-Hergaux, F.4
  • 53
    • 13444252281 scopus 로고    scopus 로고
    • Iron release from macrophages after erythrophagocytosis is up-regulated by ferroportin 1 overexpression and down-regulated by hepcidin
    • Knutson MD, Oukka M, Koss LM, Aydemir F, Wessling-Resnick M, (2005) Iron release from macrophages after erythrophagocytosis is up-regulated by ferroportin 1 overexpression and down-regulated by hepcidin. Proc Natl Acad Sci USA 102: 1324-1328
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 1324-1328
    • Knutson, M.D.1    Oukka, M.2    Koss, L.M.3    Aydemir, F.4    Wessling-Resnick, M.5
  • 54
    • 84896353280 scopus 로고    scopus 로고
    • Coupling heme and iron metabolism via ferritin H chain
    • Gozzelino R, Soares MP, (2014) Coupling heme and iron metabolism via ferritin H chain. Antioxid Redox Signal 20: 1754-1769
    • (2014) Antioxid Redox Signal , vol.20 , pp. 1754-1769
    • Gozzelino, R.1    Soares, M.P.2
  • 55
    • 0030608152 scopus 로고    scopus 로고
    • Ferritins - Molecular properties, iron storage function and cellular regulation
    • Harrison PM, Arosio P, (1996) Ferritins-molecular properties, iron storage function and cellular regulation. Biochim Biophys Acta-Bioenergetics 1275: 161-203
    • (1996) Biochim Biophys Acta - Bioenergetics , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 56
    • 0025969686 scopus 로고
    • Regulation of ferritin and heme oxygenase synthesis in rat fibroblasts by different forms of iron
    • Eisenstein RS, Garcia MD, Pettingell W, Munro HN, (1991) Regulation of ferritin and heme oxygenase synthesis in rat fibroblasts by different forms of iron. Proc Natl Acad Sci USA 88: 688-692
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 688-692
    • Eisenstein, R.S.1    Garcia, M.D.2    Pettingell, W.3    Munro, H.N.4
  • 57
  • 61
    • 0038662619 scopus 로고    scopus 로고
    • Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein
    • Nemeth E, Valore EV, Territo M, Schiller G, Lichtenstein A, Ganz T, (2003) Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein. Blood 101: 2461-2463
    • (2003) Blood , vol.101 , pp. 2461-2463
    • Nemeth, E.1    Valore, E.V.2    Territo, M.3    Schiller, G.4    Lichtenstein, A.5    Ganz, T.6
  • 62
    • 84903578007 scopus 로고    scopus 로고
    • Identification of erythroferrone as an erythroid regulator of iron metabolism
    • Kautz L, Jung G, Valore EV, Rivella S, Nemeth E, Ganz T, (2014) Identification of erythroferrone as an erythroid regulator of iron metabolism. Nat Genet 46: 678-684
    • (2014) Nat Genet , vol.46 , pp. 678-684
    • Kautz, L.1    Jung, G.2    Valore, E.V.3    Rivella, S.4    Nemeth, E.5    Ganz, T.6
  • 63
    • 84893655780 scopus 로고    scopus 로고
    • Testosterone perturbs systemic iron balance through activation of epidermal growth factor receptor signaling in the liver and repression of hepcidin
    • Latour C, Kautz L, Besson-Fournier C, Island ML, Canonne-Hergaux F, Loreal O, Ganz T, Coppin H, Roth MP, (2014) Testosterone perturbs systemic iron balance through activation of epidermal growth factor receptor signaling in the liver and repression of hepcidin. Hepatology 59: 683-694
    • (2014) Hepatology , vol.59 , pp. 683-694
    • Latour, C.1    Kautz, L.2    Besson-Fournier, C.3    Island, M.L.4    Canonne-Hergaux, F.5    Loreal, O.6    Ganz, T.7    Coppin, H.8    Roth, M.P.9
  • 67
    • 84866531103 scopus 로고    scopus 로고
    • Iron levels in polarized macrophages: Regulation of immunity and autoimmunity
    • Recalcati S, Locati M, Gammella E, Invernizzi P, Cairo G, (2012) Iron levels in polarized macrophages: regulation of immunity and autoimmunity. Autoimmun Rev 11: 883-889
    • (2012) Autoimmun Rev , vol.11 , pp. 883-889
    • Recalcati, S.1    Locati, M.2    Gammella, E.3    Invernizzi, P.4    Cairo, G.5
  • 70
    • 0020502358 scopus 로고
    • Identification of interferon-gamma as the lymphokine that activates human macrophage oxidative metabolism and antimicrobial activity
    • Nathan CF, Murray HW, Wiebe ME, Rubin BY, (1983) Identification of interferon-gamma as the lymphokine that activates human macrophage oxidative metabolism and antimicrobial activity. J Exp Med 158: 670-689
    • (1983) J Exp Med , vol.158 , pp. 670-689
    • Nathan, C.F.1    Murray, H.W.2    Wiebe, M.E.3    Rubin, B.Y.4
  • 71
    • 0028576486 scopus 로고
    • The effects of iron deficiency and iron overload on cell-mediated immunity in the mouse
    • Omara FO, Blakley BR, (1994) The effects of iron deficiency and iron overload on cell-mediated immunity in the mouse. Br J Nutr 72: 899-909
    • (1994) Br J Nutr , vol.72 , pp. 899-909
    • Omara, F.O.1    Blakley, B.R.2
  • 72
    • 0025857732 scopus 로고
    • Role of iron in T cell activation: TH1 clones differ from TH2 clones in their sensitivity to inhibition of DNA synthesis caused by IgG Mabs against the transferrin receptor and the iron chelator deferoxamine
    • Thorson JA, Smith KM, Gomez F, Naumann PW, Kemp JD, (1991) Role of iron in T cell activation: TH1 clones differ from TH2 clones in their sensitivity to inhibition of DNA synthesis caused by IgG Mabs against the transferrin receptor and the iron chelator deferoxamine. Cell Immunol 134: 126-137
    • (1991) Cell Immunol , vol.134 , pp. 126-137
    • Thorson, J.A.1    Smith, K.M.2    Gomez, F.3    Naumann, P.W.4    Kemp, J.D.5
  • 74
    • 0034679577 scopus 로고    scopus 로고
    • Antimicrobial actions of the NADPH phagocyte oxidase and inducible nitric oxide synthase in experimental salmonellosis. I. Effects on microbial killing by activated peritoneal macrophages in vitro
    • Vazquez-Torres A, Jones-Carson J, Mastroeni P, Ischiropoulos H, Fang FC, (2000) Antimicrobial actions of the NADPH phagocyte oxidase and inducible nitric oxide synthase in experimental salmonellosis. I. Effects on microbial killing by activated peritoneal macrophages in vitro. J Exp Med 192: 227-236
    • (2000) J Exp Med , vol.192 , pp. 227-236
    • Vazquez-Torres, A.1    Jones-Carson, J.2    Mastroeni, P.3    Ischiropoulos, H.4    Fang, F.C.5
  • 75
    • 0034679699 scopus 로고    scopus 로고
    • Antimicrobial actions of the NADPH phagocyte oxidase and inducible nitric oxide synthase in experimental salmonellosis. II. Effects on microbial proliferation and host survival in vivo
    • Mastroeni P, Vazquez-Torres A, Fang FC, Xu Y, Khan S, Hormaeche CE, Dougan G, (2000) Antimicrobial actions of the NADPH phagocyte oxidase and inducible nitric oxide synthase in experimental salmonellosis. II. Effects on microbial proliferation and host survival in vivo. J Exp Med 192: 237-248
    • (2000) J Exp Med , vol.192 , pp. 237-248
    • Mastroeni, P.1    Vazquez-Torres, A.2    Fang, F.C.3    Xu, Y.4    Khan, S.5    Hormaeche, C.E.6    Dougan, G.7
  • 76
    • 0034255209 scopus 로고    scopus 로고
    • Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens
    • Nathan C, Shiloh MU, (2000) Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens. Proc Natl Acad Sci USA 97: 8841-8848
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8841-8848
    • Nathan, C.1    Shiloh, M.U.2
  • 77
    • 33646831500 scopus 로고    scopus 로고
    • NF-kappaB regulates phagocytic NADPH oxidase by inducing the expression of gp91phox
    • Anrather J, Racchumi G, Iadecola C, (2006) NF-kappaB regulates phagocytic NADPH oxidase by inducing the expression of gp91phox. J Biol Chem 281: 5657-5667
    • (2006) J Biol Chem , vol.281 , pp. 5657-5667
    • Anrather, J.1    Racchumi, G.2    Iadecola, C.3
  • 78
    • 0027939931 scopus 로고
    • Role of transcription factor NF-kappa B/Rel in induction of nitric oxide synthase
    • Xie QW, Kashiwabara Y, Nathan C, (1994) Role of transcription factor NF-kappa B/Rel in induction of nitric oxide synthase. J Biol Chem 269: 4705-4708
    • (1994) J Biol Chem , vol.269 , pp. 4705-4708
    • Xie, Q.W.1    Kashiwabara, Y.2    Nathan, C.3
  • 79
    • 0026034432 scopus 로고
    • Role of nitric oxide synthesis in macrophage antimicrobial activity
    • Nathan CF, Hibbs JB Jr, (1991) Role of nitric oxide synthesis in macrophage antimicrobial activity. Curr Opin Immunol 3: 65-70
    • (1991) Curr Opin Immunol , vol.3 , pp. 65-70
    • Nathan, C.F.1    Hibbs, J.B.2
  • 80
    • 0034769118 scopus 로고    scopus 로고
    • Nitric oxide and the immune response
    • Bogdan C, (2001) Nitric oxide and the immune response. Nat Immunol 2: 907-916
    • (2001) Nat Immunol , vol.2 , pp. 907-916
    • Bogdan, C.1
  • 82
    • 0027301897 scopus 로고
    • Biosynthesis of nitric oxide activates iron regulatory factor in macrophages
    • Drapier JC, Hirling H, Wietzerbin J, Kaldy P, Kuhn LC, (1993) Biosynthesis of nitric oxide activates iron regulatory factor in macrophages. EMBO J 12: 3643-3649
    • (1993) EMBO J , vol.12 , pp. 3643-3649
    • Drapier, J.C.1    Hirling, H.2    Wietzerbin, J.3    Kaldy, P.4    Kuhn, L.C.5
  • 83
    • 0029055581 scopus 로고
    • Rapid responses to oxidative stress mediated by iron regulatory protein
    • Pantopoulos K, Hentze MW, (1995) Rapid responses to oxidative stress mediated by iron regulatory protein. EMBO J 14: 2917-2924
    • (1995) EMBO J , vol.14 , pp. 2917-2924
    • Pantopoulos, K.1    Hentze, M.W.2
  • 84
    • 0029815291 scopus 로고    scopus 로고
    • Superoxide and hydrogen peroxide-dependent inhibition of iron regulatory protein activity: A protective stratagem against oxidative injury
    • Cairo G, Castrusini E, Minotti G, Bernelli-Zazzera A, (1996) Superoxide and hydrogen peroxide-dependent inhibition of iron regulatory protein activity: a protective stratagem against oxidative injury. Faseb J 10: 1326-1335
    • (1996) Faseb J , vol.10 , pp. 1326-1335
    • Cairo, G.1    Castrusini, E.2    Minotti, G.3    Bernelli-Zazzera, A.4
  • 85
    • 0029051815 scopus 로고
    • Linkage of cell-mediated immunity to iron metabolism
    • Weiss G, Wachter H, Fuchs D, (1995) Linkage of cell-mediated immunity to iron metabolism. Immunol Today 16: 495-500
    • (1995) Immunol Today , vol.16 , pp. 495-500
    • Weiss, G.1    Wachter, H.2    Fuchs, D.3
  • 86
    • 84923206848 scopus 로고    scopus 로고
    • Macrophage defense mechanisms against intracellular bacteria
    • Weiss G, Schaible UE, (2015) Macrophage defense mechanisms against intracellular bacteria. Immunol Rev 264: 182-203
    • (2015) Immunol Rev , vol.264 , pp. 182-203
    • Weiss, G.1    Schaible, U.E.2
  • 88
    • 0024431912 scopus 로고
    • Induction of hypoferremia and modulation of macrophage iron metabolism by tumor necrosis factor
    • Alvarez-Hernandez X, Liceaga J, McKay IC, Brock JH, (1989) Induction of hypoferremia and modulation of macrophage iron metabolism by tumor necrosis factor. Lab Invest 61: 319-322
    • (1989) Lab Invest , vol.61 , pp. 319-322
    • Alvarez-Hernandez, X.1    Liceaga, J.2    McKay, I.C.3    Brock, J.H.4
  • 89
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • Itoh K, Wakabayashi N, Katoh Y, Ishii T, Igarashi K, Engel JD, Yamamoto M, (1999) Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Dev 13: 76-86
    • (1999) Genes Dev , vol.13 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6    Yamamoto, M.7
  • 90
    • 84878572136 scopus 로고    scopus 로고
    • Toward clinical application of the Keap1-Nrf2 pathway
    • Suzuki T, Motohashi H, Yamamoto M, (2013) Toward clinical application of the Keap1-Nrf2 pathway. Trends Pharmacol Sci 34: 340-346
    • (2013) Trends Pharmacol Sci , vol.34 , pp. 340-346
    • Suzuki, T.1    Motohashi, H.2    Yamamoto, M.3
  • 91
    • 84897421970 scopus 로고    scopus 로고
    • The Nrf2 regulatory network provides an interface between redox and intermediary metabolism
    • Hayes JD, Dinkova-Kostova AT, (2014) The Nrf2 regulatory network provides an interface between redox and intermediary metabolism. Trends Biochem Sci 39: 199-218
    • (2014) Trends Biochem Sci , vol.39 , pp. 199-218
    • Hayes, J.D.1    Dinkova-Kostova, A.T.2
  • 93
    • 43049170080 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis senses host-derived carbon monoxide during macrophage infection
    • Shiloh MU, Manzanillo P, Cox JS, (2008) Mycobacterium tuberculosis senses host-derived carbon monoxide during macrophage infection. Cell Host Microbe 3: 323-330
    • (2008) Cell Host Microbe , vol.3 , pp. 323-330
    • Shiloh, M.U.1    Manzanillo, P.2    Cox, J.S.3
  • 94
    • 84901049327 scopus 로고    scopus 로고
    • Iron ERRs with Salmonella
    • Fang FC, Weiss G, (2014) Iron ERRs with Salmonella. Cell Host Microbe 15: 515-516
    • (2014) Cell Host Microbe , vol.15 , pp. 515-516
    • Fang, F.C.1    Weiss, G.2
  • 95
    • 64049100955 scopus 로고    scopus 로고
    • Iron in innate immunity: Starve the invaders
    • Ganz T, (2009) Iron in innate immunity: starve the invaders. Curr Opin Immunol 21: 63-67
    • (2009) Curr Opin Immunol , vol.21 , pp. 63-67
    • Ganz, T.1
  • 100
    • 34547863499 scopus 로고    scopus 로고
    • The co-ordinated regulation of iron homeostasis in murine macrophages limits the availability of iron for intracellular Salmonella typhimurium
    • Nairz M, Theurl I, Ludwiczek S, Theurl M, Mair SM, Fritsche G, Weiss G, (2007) The co-ordinated regulation of iron homeostasis in murine macrophages limits the availability of iron for intracellular Salmonella typhimurium. Cell Microbiol 9: 2126-2140
    • (2007) Cell Microbiol , vol.9 , pp. 2126-2140
    • Nairz, M.1    Theurl, I.2    Ludwiczek, S.3    Theurl, M.4    Mair, S.M.5    Fritsche, G.6    Weiss, G.7
  • 101
    • 50849096115 scopus 로고    scopus 로고
    • The iron export protein ferroportin 1 is differentially expressed in mouse macrophage populations and is present in the mycobacterial-containing phagosome
    • Van Zandt KE, Sow FB, Florence WC, Zwilling BS, Satoskar AR, Schlesinger LS, Lafuse WP, (2008) The iron export protein ferroportin 1 is differentially expressed in mouse macrophage populations and is present in the mycobacterial-containing phagosome. J Leukoc Biol 84: 689-700
    • (2008) J Leukoc Biol , vol.84 , pp. 689-700
    • Van Zandt, K.E.1    Sow, F.B.2    Florence, W.C.3    Zwilling, B.S.4    Satoskar, A.R.5    Schlesinger, L.S.6    Lafuse, W.P.7
  • 102
    • 77955413703 scopus 로고    scopus 로고
    • Divergent modulation of Chlamydia pneumoniae infection cycle in human monocytic and endothelial cells by iron, tryptophan availability and interferon gamma
    • Bellmann-Weiler R, Martinz V, Kurz K, Engl S, Feistritzer C, Fuchs D, Rupp J, Paldanius M, Weiss G, (2010) Divergent modulation of Chlamydia pneumoniae infection cycle in human monocytic and endothelial cells by iron, tryptophan availability and interferon gamma. Immunobiology 215: 842-848
    • (2010) Immunobiology , vol.215 , pp. 842-848
    • Bellmann-Weiler, R.1    Martinz, V.2    Kurz, K.3    Engl, S.4    Feistritzer, C.5    Fuchs, D.6    Rupp, J.7    Paldanius, M.8    Weiss, G.9
  • 104
    • 52549119182 scopus 로고    scopus 로고
    • A central role for free heme in the pathogenesis of severe malaria: The missing link?
    • Ferreira A, Balla J, Jeney V, Balla G, Soares MP, (2008) A central role for free heme in the pathogenesis of severe malaria: the missing link? J Mol Med 86: 1097-1111
    • (2008) J Mol Med , vol.86 , pp. 1097-1111
    • Ferreira, A.1    Balla, J.2    Jeney, V.3    Balla, G.4    Soares, M.P.5
  • 108
    • 84855550090 scopus 로고    scopus 로고
    • Malaria impairs resistance to Salmonella through heme- and heme oxygenase-dependent dysfunctional granulocyte mobilization
    • Cunnington AJ, de Souza JB, Walther M, Riley EM, (2012) Malaria impairs resistance to Salmonella through heme- and heme oxygenase-dependent dysfunctional granulocyte mobilization. Nat Med 18: 120-127
    • (2012) Nat Med , vol.18 , pp. 120-127
    • Cunnington, A.J.1    De Souza, J.B.2    Walther, M.3    Riley, E.M.4
  • 109
    • 33646427702 scopus 로고    scopus 로고
    • TLR4-dependent hepcidin expression by myeloid cells in response to bacterial pathogens
    • Peyssonnaux C, Zinkernagel AS, Datta V, Lauth X, Johnson RS, Nizet V, (2006) TLR4-dependent hepcidin expression by myeloid cells in response to bacterial pathogens. Blood 107: 3727-3732
    • (2006) Blood , vol.107 , pp. 3727-3732
    • Peyssonnaux, C.1    Zinkernagel, A.S.2    Datta, V.3    Lauth, X.4    Johnson, R.S.5    Nizet, V.6
  • 112
    • 0037926880 scopus 로고    scopus 로고
    • Cytokine-mediated regulation of iron transport in human monocytic cells
    • Ludwiczek S, Aigner E, Theurl I, Weiss G, (2003) Cytokine-mediated regulation of iron transport in human monocytic cells. Blood 101: 4148-4154
    • (2003) Blood , vol.101 , pp. 4148-4154
    • Ludwiczek, S.1    Aigner, E.2    Theurl, I.3    Weiss, G.4
  • 113
    • 84876409224 scopus 로고    scopus 로고
    • Anaemia in inflammatory rheumatic diseases
    • Weiss G, Schett G, (2013) Anaemia in inflammatory rheumatic diseases. Nat Rev Rheumatol 9: 205-215
    • (2013) Nat Rev Rheumatol , vol.9 , pp. 205-215
    • Weiss, G.1    Schett, G.2
  • 115
    • 30144435054 scopus 로고    scopus 로고
    • CD163 is the macrophage scavenger receptor for native and chemically modified hemoglobins in the absence of haptoglobin
    • Schaer DJ, Schaer CA, Buehler PW, Boykins RA, Schoedon G, Alayash AI, Schaffner A, (2006) CD163 is the macrophage scavenger receptor for native and chemically modified hemoglobins in the absence of haptoglobin. Blood 107: 373-380
    • (2006) Blood , vol.107 , pp. 373-380
    • Schaer, D.J.1    Schaer, C.A.2    Buehler, P.W.3    Boykins, R.A.4    Schoedon, G.5    Alayash, A.I.6    Schaffner, A.7
  • 116
    • 0036127426 scopus 로고    scopus 로고
    • Heme oxygenase-1 mediates the anti-inflammatory effect of interleukin-10 in mice
    • Lee TS, Chau LY, (2002) Heme oxygenase-1 mediates the anti-inflammatory effect of interleukin-10 in mice. Nat Med 8: 240-246
    • (2002) Nat Med , vol.8 , pp. 240-246
    • Lee, T.S.1    Chau, L.Y.2
  • 117
    • 0036191387 scopus 로고    scopus 로고
    • The physiology of lactoferrin
    • Brock JH, (2002) The physiology of lactoferrin. Biochem Cell Biol 80: 1-6
    • (2002) Biochem Cell Biol , vol.80 , pp. 1-6
    • Brock, J.H.1
  • 118
    • 0028963594 scopus 로고
    • Iron: Mammalian defense systems, mechanisms of disease, and chelation therapy approaches
    • Kontoghiorghes GJ, Weinberg ED, (1995) Iron: mammalian defense systems, mechanisms of disease, and chelation therapy approaches. Blood Rev 9: 33-45
    • (1995) Blood Rev , vol.9 , pp. 33-45
    • Kontoghiorghes, G.J.1    Weinberg, E.D.2
  • 119
    • 33748418332 scopus 로고    scopus 로고
    • Regulation of physiological and pathological Th1 and Th2 responses by lactoferrin
    • Fischer R, Debbabi H, Dubarry M, Boyaka P, Tome D, (2006) Regulation of physiological and pathological Th1 and Th2 responses by lactoferrin. Biochem Cell Biol 84: 303-311
    • (2006) Biochem Cell Biol , vol.84 , pp. 303-311
    • Fischer, R.1    Debbabi, H.2    Dubarry, M.3    Boyaka, P.4    Tome, D.5
  • 120
    • 84896324507 scopus 로고    scopus 로고
    • Immunomodulatory effects of recombinant lactoferrin during MRSA infection
    • Hwang SA, Kruzel ML, Actor JK, (2014) Immunomodulatory effects of recombinant lactoferrin during MRSA infection. Int Immunopharmacol 20: 157-163
    • (2014) Int Immunopharmacol , vol.20 , pp. 157-163
    • Hwang, S.A.1    Kruzel, M.L.2    Actor, J.K.3
  • 122
    • 0037198693 scopus 로고    scopus 로고
    • A component of innate immunity prevents bacterial biofilm development
    • Singh PK, Parsek MR, Greenberg EP, Welsh MJ, (2002) A component of innate immunity prevents bacterial biofilm development. Nature 417: 552-555
    • (2002) Nature , vol.417 , pp. 552-555
    • Singh, P.K.1    Parsek, M.R.2    Greenberg, E.P.3    Welsh, M.J.4
  • 123
    • 33645111877 scopus 로고    scopus 로고
    • Natural resistance, iron and infection: A challenge for clinical medicine
    • Bullen JJ, Rogers HJ, Spalding PB, Ward CG, (2006) Natural resistance, iron and infection: a challenge for clinical medicine. J Med Microbiol 55: 251-258
    • (2006) J Med Microbiol , vol.55 , pp. 251-258
    • Bullen, J.J.1    Rogers, H.J.2    Spalding, P.B.3    Ward, C.G.4
  • 124
    • 0026716209 scopus 로고
    • Regulation of cytokine release from mononuclear cells by the iron-binding protein lactoferrin
    • Crouch SP, Slater KJ, Fletcher J, (1992) Regulation of cytokine release from mononuclear cells by the iron-binding protein lactoferrin. Blood 80: 235-240
    • (1992) Blood , vol.80 , pp. 235-240
    • Crouch, S.P.1    Slater, K.J.2    Fletcher, J.3
  • 125
    • 84884946088 scopus 로고    scopus 로고
    • Iron acquisition by Mycobacterium tuberculosis residing within myeloid dendritic cells
    • Olakanmi O, Kesavalu B, Abdalla MY, Britigan BE, (2013) Iron acquisition by Mycobacterium tuberculosis residing within myeloid dendritic cells. Microb Pathog 65: 21-28
    • (2013) Microb Pathog , vol.65 , pp. 21-28
    • Olakanmi, O.1    Kesavalu, B.2    Abdalla, M.Y.3    Britigan, B.E.4
  • 126
    • 84899502867 scopus 로고    scopus 로고
    • Iron acquisition and regulation systems in Streptococcus species
    • Ge R, Sun X, (2014) Iron acquisition and regulation systems in Streptococcus species. Metallomics 6: 996-1003
    • (2014) Metallomics , vol.6 , pp. 996-1003
    • Ge, R.1    Sun, X.2
  • 127
    • 84925222674 scopus 로고    scopus 로고
    • The negatively charged regions of lactoferrin binding protein B, an adaptation against anti-microbial peptides
    • Morgenthau A, Beddek A, Schryvers AB, (2014) The negatively charged regions of lactoferrin binding protein B, an adaptation against anti-microbial peptides. PLoS ONE 9: e86243
    • (2014) PLoS ONE , vol.9 , pp. e86243
    • Morgenthau, A.1    Beddek, A.2    Schryvers, A.B.3
  • 128
    • 84884815303 scopus 로고    scopus 로고
    • Structural insight into the lactoferrin receptors from pathogenic Neisseria
    • Noinaj N, Cornelissen CN, Buchanan SK, (2013) Structural insight into the lactoferrin receptors from pathogenic Neisseria. J Struct Biol 184: 83-92
    • (2013) J Struct Biol , vol.184 , pp. 83-92
    • Noinaj, N.1    Cornelissen, C.N.2    Buchanan, S.K.3
  • 131
    • 77953690176 scopus 로고    scopus 로고
    • A mammalian siderophore synthesized by an enzyme with a bacterial homolog involved in enterobactin production
    • Devireddy LR, Hart DO, Goetz DH, Green MR, (2010) A mammalian siderophore synthesized by an enzyme with a bacterial homolog involved in enterobactin production. Cell 141: 1006-1017
    • (2010) Cell , vol.141 , pp. 1006-1017
    • Devireddy, L.R.1    Hart, D.O.2    Goetz, D.H.3    Green, M.R.4
  • 135
    • 84860222365 scopus 로고    scopus 로고
    • The multifaceted roles of neutrophil gelatinase associated lipocalin (NGAL) in inflammation and cancer
    • Chakraborty S, Kaur S, Guha S, Batra SK, (2012) The multifaceted roles of neutrophil gelatinase associated lipocalin (NGAL) in inflammation and cancer. Biochim Biophys Acta 1826: 129-169
    • (2012) Biochim Biophys Acta , vol.1826 , pp. 129-169
    • Chakraborty, S.1    Kaur, S.2    Guha, S.3    Batra, S.K.4
  • 136
    • 84876783277 scopus 로고    scopus 로고
    • Impaired neutrophil function in 24p3 null mice contributes to enhanced susceptibility to bacterial infections
    • Liu Z, Petersen R, Devireddy L, (2013) Impaired neutrophil function in 24p3 null mice contributes to enhanced susceptibility to bacterial infections. J Immunol 190: 4692-4706
    • (2013) J Immunol , vol.190 , pp. 4692-4706
    • Liu, Z.1    Petersen, R.2    Devireddy, L.3
  • 138
    • 34548785607 scopus 로고    scopus 로고
    • Respiratory protein-generated reactive oxygen species as an antimicrobial strategy
    • Jiang N, Tan NS, Ho B, Ding JL, (2007) Respiratory protein-generated reactive oxygen species as an antimicrobial strategy. Nat Immunol 8: 1114-1122
    • (2007) Nat Immunol , vol.8 , pp. 1114-1122
    • Jiang, N.1    Tan, N.S.2    Ho, B.3    Ding, J.L.4
  • 139
    • 76349096031 scopus 로고    scopus 로고
    • Rapid reprogramming of haemoglobin structure-function exposes multiple dual-antimicrobial potencies
    • Du R, Ho B, Ding JL, (2010) Rapid reprogramming of haemoglobin structure-function exposes multiple dual-antimicrobial potencies. EMBO J 29: 632-642
    • (2010) EMBO J , vol.29 , pp. 632-642
    • Du, R.1    Ho, B.2    Ding, J.L.3
  • 140
    • 84873022603 scopus 로고    scopus 로고
    • A perspective on the role of extracellular hemoglobin on the innate immune system
    • Lee SK, Ding JL, (2013) A perspective on the role of extracellular hemoglobin on the innate immune system. DNA Cell Biol 32: 36-40
    • (2013) DNA Cell Biol , vol.32 , pp. 36-40
    • Lee, S.K.1    Ding, J.L.2
  • 141
    • 0028131671 scopus 로고
    • Hemoglobin, a newly recognized lipopolysaccharide (LPS)-binding protein that enhances LPS biological activity
    • Kaca W, Roth RI, Levin J, (1994) Hemoglobin, a newly recognized lipopolysaccharide (LPS)-binding protein that enhances LPS biological activity. J Biol Chem 269: 25078-25084
    • (1994) J Biol Chem , vol.269 , pp. 25078-25084
    • Kaca, W.1    Roth, R.I.2    Levin, J.3
  • 142
    • 0035421993 scopus 로고    scopus 로고
    • Divalent-metal transport by NRAMP proteins at the interface of host-pathogen interactions
    • Forbes JR, Gros P, (2001) Divalent-metal transport by NRAMP proteins at the interface of host-pathogen interactions. Trends Microbiol 9: 397-403
    • (2001) Trends Microbiol , vol.9 , pp. 397-403
    • Forbes, J.R.1    Gros, P.2
  • 145
    • 80555133228 scopus 로고    scopus 로고
    • Nutritional immunity: Homology modeling of Nramp metal import
    • Cellier MF, (2012) Nutritional immunity: homology modeling of Nramp metal import. Adv Exp Med Biol 946: 335-351
    • (2012) Adv Exp Med Biol , vol.946 , pp. 335-351
    • Cellier, M.F.1
  • 146
    • 0031850526 scopus 로고    scopus 로고
    • Host resistance to intracellular infection: Mutation of natural resistance-associated macrophage protein 1 (Nramp1) impairs phagosomal acidification
    • Hackam DJ, Rotstein OD, Zhang W, Gruenheid S, Gros P, Grinstein S, (1998) Host resistance to intracellular infection: mutation of natural resistance-associated macrophage protein 1 (Nramp1) impairs phagosomal acidification. J Exp Med 188: 351-364
    • (1998) J Exp Med , vol.188 , pp. 351-364
    • Hackam, D.J.1    Rotstein, O.D.2    Zhang, W.3    Gruenheid, S.4    Gros, P.5    Grinstein, S.6
  • 147
    • 0034613681 scopus 로고    scopus 로고
    • Natural resistance to intracellular infections: Natural resistance-associated macrophage protein 1 (Nramp1) functions as a pH-dependent manganese transporter at the phagosomal membrane
    • Jabado N, Jankowski A, Dougaparsad S, Picard V, Grinstein S, Gros P, (2000) Natural resistance to intracellular infections: natural resistance-associated macrophage protein 1 (Nramp1) functions as a pH-dependent manganese transporter at the phagosomal membrane. J Exp Med 192: 1237-1248
    • (2000) J Exp Med , vol.192 , pp. 1237-1248
    • Jabado, N.1    Jankowski, A.2    Dougaparsad, S.3    Picard, V.4    Grinstein, S.5    Gros, P.6
  • 148
    • 0032590006 scopus 로고    scopus 로고
    • Nramp1: A link between intracellular iron transport and innate resistance to intracellular pathogens
    • Barton CH, Biggs TE, Baker ST, Bowen H, Atkinson PG, (1999) Nramp1: a link between intracellular iron transport and innate resistance to intracellular pathogens. J Leukoc Biol 66: 757-762
    • (1999) J Leukoc Biol , vol.66 , pp. 757-762
    • Barton, C.H.1    Biggs, T.E.2    Baker, S.T.3    Bowen, H.4    Atkinson, P.G.5
  • 150
    • 70349923239 scopus 로고    scopus 로고
    • Slc11a1 limits intracellular growth of Salmonella enterica sv. Typhimurium by promoting macrophage immune effector functions and impairing bacterial iron acquisition
    • Nairz M, Fritsche G, Crouch ML, Barton HC, Fang FC, Weiss G, (2009) Slc11a1 limits intracellular growth of Salmonella enterica sv. Typhimurium by promoting macrophage immune effector functions and impairing bacterial iron acquisition. Cell Microbiol 11: 1365-1381
    • (2009) Cell Microbiol , vol.11 , pp. 1365-1381
    • Nairz, M.1    Fritsche, G.2    Crouch, M.L.3    Barton, H.C.4    Fang, F.C.5    Weiss, G.6
  • 151
    • 77953618426 scopus 로고    scopus 로고
    • Iron metabolism in trypanosomatids, and its crucial role in infection
    • Taylor MC, Kelly JM, (2010) Iron metabolism in trypanosomatids, and its crucial role in infection. Parasitology 137: 899-917
    • (2010) Parasitology , vol.137 , pp. 899-917
    • Taylor, M.C.1    Kelly, J.M.2
  • 152
    • 0043136713 scopus 로고    scopus 로고
    • Nramp1 functionality increases inducible nitric oxide synthase transcription via stimulation of IFN regulatory factor 1 expression
    • Fritsche G, Dlaska M, Barton H, Theurl I, Garimorth K, Weiss G, (2003) Nramp1 functionality increases inducible nitric oxide synthase transcription via stimulation of IFN regulatory factor 1 expression. J Immunol 171: 1994-1998
    • (2003) J Immunol , vol.171 , pp. 1994-1998
    • Fritsche, G.1    Dlaska, M.2    Barton, H.3    Theurl, I.4    Garimorth, K.5    Weiss, G.6
  • 153
    • 58149345129 scopus 로고    scopus 로고
    • Nramp1-functionality increases iNOS expression via repression of IL-10 formation
    • Fritsche G, Nairz M, Werner ER, Barton HC, Weiss G, (2008) Nramp1-functionality increases iNOS expression via repression of IL-10 formation. Eur J Immunol 38: 3060-3067
    • (2008) Eur J Immunol , vol.38 , pp. 3060-3067
    • Fritsche, G.1    Nairz, M.2    Werner, E.R.3    Barton, H.C.4    Weiss, G.5
  • 154
    • 0029258822 scopus 로고
    • Nramp transfection transfers Ity/Lsh/Bcg-related pleiotropic effects on macrophage activation: Influence on oxidative burst and nitric oxide pathways
    • Barton CH, Whitehead SH, Blackwell JM, (1995) Nramp transfection transfers Ity/Lsh/Bcg-related pleiotropic effects on macrophage activation: influence on oxidative burst and nitric oxide pathways. Mol Med 1: 267-279
    • (1995) Mol Med , vol.1 , pp. 267-279
    • Barton, C.H.1    Whitehead, S.H.2    Blackwell, J.M.3
  • 155
    • 0036534742 scopus 로고    scopus 로고
    • Solute carrier 11a1 (Slc11a1; Formerly Nramp1) regulates metabolism and release of iron acquired by phagocytic, but not transferrin-receptor-mediated, iron uptake
    • Mulero V, Searle S, Blackwell JM, Brock JH, (2002) Solute carrier 11a1 (Slc11a1; formerly Nramp1) regulates metabolism and release of iron acquired by phagocytic, but not transferrin-receptor-mediated, iron uptake. Biochem J 363: 89-94
    • (2002) Biochem J , vol.363 , pp. 89-94
    • Mulero, V.1    Searle, S.2    Blackwell, J.M.3    Brock, J.H.4
  • 156
    • 84864768441 scopus 로고    scopus 로고
    • Slc11a1 (Nramp1) impairs growth of Salmonella enterica serovar typhimurium in macrophages via stimulation of lipocalin-2 expression
    • Fritsche G, Nairz M, Libby SJ, Fang FC, Weiss G, (2012) Slc11a1 (Nramp1) impairs growth of Salmonella enterica serovar typhimurium in macrophages via stimulation of lipocalin-2 expression. J Leukoc Biol 92: 353-359
    • (2012) J Leukoc Biol , vol.92 , pp. 353-359
    • Fritsche, G.1    Nairz, M.2    Libby, S.J.3    Fang, F.C.4    Weiss, G.5
  • 157
    • 84877150279 scopus 로고    scopus 로고
    • Neutrophil gelatinase-associated lipocalin and interleukin-10 regulate intramacrophage Chlamydia pneumoniae replication by modulating intracellular iron homeostasis
    • Bellmann-Weiler R, Schroll A, Engl S, Nairz M, Talasz H, Seifert M, Weiss G, (2013) Neutrophil gelatinase-associated lipocalin and interleukin-10 regulate intramacrophage Chlamydia pneumoniae replication by modulating intracellular iron homeostasis. Immunobiology 218: 969-978
    • (2013) Immunobiology , vol.218 , pp. 969-978
    • Bellmann-Weiler, R.1    Schroll, A.2    Engl, S.3    Nairz, M.4    Talasz, H.5    Seifert, M.6    Weiss, G.7
  • 158
    • 76449105595 scopus 로고    scopus 로고
    • Intracellular Mycobacterium avium intersect transferrin in the Rab11(+) recycling endocytic pathway and avoid lipocalin 2 trafficking to the lysosomal pathway
    • Halaas O, Steigedal M, Haug M, Awuh JA, Ryan L, Brech A, Sato S, Husebye H, Cangelosi GA, Akira S, et al, (2010) Intracellular Mycobacterium avium intersect transferrin in the Rab11(+) recycling endocytic pathway and avoid lipocalin 2 trafficking to the lysosomal pathway. J Infect Dis 201: 783-792
    • (2010) J Infect Dis , vol.201 , pp. 783-792
    • Halaas, O.1    Steigedal, M.2    Haug, M.3    Awuh, J.A.4    Ryan, L.5    Brech, A.6    Sato, S.7    Husebye, H.8    Cangelosi, G.A.9    Akira, S.10    Al, E.11
  • 160
    • 33845878232 scopus 로고    scopus 로고
    • Hereditary hemochromatosis results in decreased iron acquisition and growth by Mycobacterium tuberculosis within human macrophages
    • Olakanmi O, Schlesinger LS, Britigan BE, (2007) Hereditary hemochromatosis results in decreased iron acquisition and growth by Mycobacterium tuberculosis within human macrophages. J Leukoc Biol 81: 195-204
    • (2007) J Leukoc Biol , vol.81 , pp. 195-204
    • Olakanmi, O.1    Schlesinger, L.S.2    Britigan, B.E.3
  • 163
    • 84898042156 scopus 로고    scopus 로고
    • Inverse agonist of estrogen-related receptor gamma controls Salmonella typhimurium infection by modulating host iron homeostasis
    • Kim DK, Jeong JH, Lee JM, Kim KS, Park SH, Kim YD, Koh M, Shin M, Jung YS, Kim H, et al, (2014) Inverse agonist of estrogen-related receptor gamma controls Salmonella typhimurium infection by modulating host iron homeostasis. Nat Med 20: 419-424
    • (2014) Nat Med , vol.20 , pp. 419-424
    • Kim, D.K.1    Jeong, J.H.2    Lee, J.M.3    Kim, K.S.4    Park, S.H.5    Kim, Y.D.6    Koh, M.7    Shin, M.8    Jung, Y.S.9    Kim, H.10    Al, E.11
  • 165
    • 0030911247 scopus 로고    scopus 로고
    • Functional requirement of the hypoxia-responsive element in the activation of the inducible nitric oxide synthase promoter by the iron chelator desferrioxamine
    • Melillo G, Taylor LS, Brooks A, Musso T, Cox GW, Varesio L, (1997) Functional requirement of the hypoxia-responsive element in the activation of the inducible nitric oxide synthase promoter by the iron chelator desferrioxamine. J Biol Chem 272: 12236-12243
    • (1997) J Biol Chem , vol.272 , pp. 12236-12243
    • Melillo, G.1    Taylor, L.S.2    Brooks, A.3    Musso, T.4    Cox, G.W.5    Varesio, L.6
  • 166
    • 0033563095 scopus 로고    scopus 로고
    • Central role of transcription factor NF-IL6 for cytokine and iron-mediated regulation of murine inducible nitric oxide synthase expression
    • Dlaska M, Weiss G, (1999) Central role of transcription factor NF-IL6 for cytokine and iron-mediated regulation of murine inducible nitric oxide synthase expression. J Immunol 162: 6171-6177
    • (1999) J Immunol , vol.162 , pp. 6171-6177
    • Dlaska, M.1    Weiss, G.2
  • 169
    • 50549086197 scopus 로고    scopus 로고
    • Interferon-gamma limits the availability of iron for intramacrophage Salmonella typhimurium
    • Nairz M, Fritsche G, Brunner P, Talasz H, Hantke K, Weiss G, (2008) Interferon-gamma limits the availability of iron for intramacrophage Salmonella typhimurium. Eur J Immunol 38: 1923-1936
    • (2008) Eur J Immunol , vol.38 , pp. 1923-1936
    • Nairz, M.1    Fritsche, G.2    Brunner, P.3    Talasz, H.4    Hantke, K.5    Weiss, G.6
  • 170
    • 84879426573 scopus 로고    scopus 로고
    • Heme catabolism by heme oxygenase-1 confers host resistance to Mycobacterium infection
    • Silva-Gomes S, Appelberg R, Larsen R, Soares MP, Gomes MS, (2013) Heme catabolism by heme oxygenase-1 confers host resistance to Mycobacterium infection. Infect Immun 81: 2536-2545
    • (2013) Infect Immun , vol.81 , pp. 2536-2545
    • Silva-Gomes, S.1    Appelberg, R.2    Larsen, R.3    Soares, M.P.4    Gomes, M.S.5
  • 174
    • 84876906830 scopus 로고    scopus 로고
    • TNF dually mediates resistance and susceptibility to mycobacteria via mitochondrial reactive oxygen species
    • Roca FJ, Ramakrishnan L, (2013) TNF dually mediates resistance and susceptibility to mycobacteria via mitochondrial reactive oxygen species. Cell 153: 521-534
    • (2013) Cell , vol.153 , pp. 521-534
    • Roca, F.J.1    Ramakrishnan, L.2
  • 175
    • 67349115201 scopus 로고    scopus 로고
    • Iron metabolism in the anemia of chronic disease
    • Weiss G, (2009) Iron metabolism in the anemia of chronic disease. Biochim Biophys Acta 1790: 682-693
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 682-693
    • Weiss, G.1
  • 176
    • 15944383079 scopus 로고    scopus 로고
    • Anemia of chronic disease: Pathophysiology and laboratory diagnosis
    • Thomas C, Thomas L, (2005) Anemia of chronic disease: pathophysiology and laboratory diagnosis. Lab Hematol 11: 14-23
    • (2005) Lab Hematol , vol.11 , pp. 14-23
    • Thomas, C.1    Thomas, L.2
  • 177
    • 14744278436 scopus 로고    scopus 로고
    • Anemia of chronic disease
    • Weiss G, Goodnough LT, (2005) Anemia of chronic disease. N Engl J Med 352: 1011-1023
    • (2005) N Engl J Med , vol.352 , pp. 1011-1023
    • Weiss, G.1    Goodnough, L.T.2
  • 179
    • 84893048572 scopus 로고    scopus 로고
    • How i treat unexplained refractory iron deficiency anemia
    • Hershko C, Camaschella C, (2014) How I treat unexplained refractory iron deficiency anemia. Blood 123: 326-333
    • (2014) Blood , vol.123 , pp. 326-333
    • Hershko, C.1    Camaschella, C.2
  • 182
    • 0031018874 scopus 로고    scopus 로고
    • Regulation of cellular iron metabolism by erythropoietin: Activation of iron-regulatory protein and upregulation of transferrin receptor expression in erythroid cells
    • Weiss G, Houston T, Kastner S, Johrer K, Grunewald K, Brock JH, (1997) Regulation of cellular iron metabolism by erythropoietin: activation of iron-regulatory protein and upregulation of transferrin receptor expression in erythroid cells. Blood 89: 680-687
    • (1997) Blood , vol.89 , pp. 680-687
    • Weiss, G.1    Houston, T.2    Kastner, S.3    Johrer, K.4    Grunewald, K.5    Brock, J.H.6
  • 183
    • 84908144096 scopus 로고    scopus 로고
    • Erythroferrone contributes to recovery from anemia of inflammation
    • Kautz L, Jung G, Nemeth E, Ganz T, (2014) Erythroferrone contributes to recovery from anemia of inflammation. Blood 124: 2569-2574
    • (2014) Blood , vol.124 , pp. 2569-2574
    • Kautz, L.1    Jung, G.2    Nemeth, E.3    Ganz, T.4
  • 184
    • 0035092672 scopus 로고    scopus 로고
    • Nutritional deficiencies and blunted erythropoietin response as causes of the anemia of critical illness
    • Rodriguez RM, Corwin HL, Gettinger A, Corwin MJ, Gubler D, Pearl RG, (2001) Nutritional deficiencies and blunted erythropoietin response as causes of the anemia of critical illness. J Crit Care 16: 36-41
    • (2001) J Crit Care , vol.16 , pp. 36-41
    • Rodriguez, R.M.1    Corwin, H.L.2    Gettinger, A.3    Corwin, M.J.4    Gubler, D.5    Pearl, R.G.6
  • 185
    • 79952613173 scopus 로고    scopus 로고
    • Regulation of erythropoietin production
    • Jelkmann W, (2011) Regulation of erythropoietin production. J Physiol 589: 1251-1258
    • (2011) J Physiol , vol.589 , pp. 1251-1258
    • Jelkmann, W.1
  • 194
    • 84864800812 scopus 로고    scopus 로고
    • Free hemoglobin concentration in severe sepsis: Methods of measurement and prediction of outcome
    • Adamzik M, Hamburger T, Petrat F, Peters J, de Groot H, Hartmann M, (2012) Free hemoglobin concentration in severe sepsis: methods of measurement and prediction of outcome. Crit Care 16: R125
    • (2012) Crit Care , vol.16 , pp. R125
    • Adamzik, M.1    Hamburger, T.2    Petrat, F.3    Peters, J.4    De Groot, H.5    Hartmann, M.6
  • 195
    • 84860798758 scopus 로고    scopus 로고
    • Association between the haptoglobin and heme oxygenase 1 genetic profiles and soluble CD163 in susceptibility to and severity of human malaria
    • Mendonca VR, Luz NF, Santos NJ, Borges VM, Goncalves MS, Andrade BB, Barral-Netto M, (2012) Association between the haptoglobin and heme oxygenase 1 genetic profiles and soluble CD163 in susceptibility to and severity of human malaria. Infect Immun 80: 1445-1454
    • (2012) Infect Immun , vol.80 , pp. 1445-1454
    • Mendonca, V.R.1    Luz, N.F.2    Santos, N.J.3    Borges, V.M.4    Goncalves, M.S.5    Andrade, B.B.6    Barral-Netto, M.7
  • 196
    • 84874439878 scopus 로고    scopus 로고
    • Hemolysis and free hemoglobin revisited: Exploring hemoglobin and hemin scavengers as a novel class of therapeutic proteins
    • Schaer DJ, Buehler PW, Alayash AI, Belcher JD, Vercellotti GM, (2013) Hemolysis and free hemoglobin revisited: exploring hemoglobin and hemin scavengers as a novel class of therapeutic proteins. Blood 121: 1276-1284
    • (2013) Blood , vol.121 , pp. 1276-1284
    • Schaer, D.J.1    Buehler, P.W.2    Alayash, A.I.3    Belcher, J.D.4    Vercellotti, G.M.5
  • 197
    • 0028132836 scopus 로고
    • Redox signaling: Nitrosylation and related target interactions of nitric oxide
    • Stamler JS, (1994) Redox signaling: nitrosylation and related target interactions of nitric oxide. Cell 78: 931-936
    • (1994) Cell , vol.78 , pp. 931-936
    • Stamler, J.S.1
  • 198
    • 70350418736 scopus 로고    scopus 로고
    • Oxidized hemoglobin is an endogenous proinflammatory agonist that targets vascular endothelial cells
    • Silva G, Jeney V, Chora A, Larsen R, Balla J, Soares MP, (2009) Oxidized hemoglobin is an endogenous proinflammatory agonist that targets vascular endothelial cells. J Biol Chem 284: 29582-29595
    • (2009) J Biol Chem , vol.284 , pp. 29582-29595
    • Silva, G.1    Jeney, V.2    Chora, A.3    Larsen, R.4    Balla, J.5    Soares, M.P.6
  • 199
    • 0008239743 scopus 로고
    • Accelerated autoxidation and heme loss due to instability of sickle hemoglobin
    • Hebbel RP, Morgan WT, Eaton JW, Hedlund BE, (1988) Accelerated autoxidation and heme loss due to instability of sickle hemoglobin. Proc Natl Acad Sci USA 85: 237-241
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 237-241
    • Hebbel, R.P.1    Morgan, W.T.2    Eaton, J.W.3    Hedlund, B.E.4
  • 200
    • 0027358877 scopus 로고
    • Endothelial-cell heme uptake from heme proteins: Induction of sensitization and desensitization to oxidant damage
    • Balla J, Jacob HS, Balla G, Nath K, Eaton JW, Vercellotti GM, (1993) Endothelial-cell heme uptake from heme proteins: induction of sensitization and desensitization to oxidant damage. Proc Natl Acad Sci USA 90: 9285-9289
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9285-9289
    • Balla, J.1    Jacob, H.S.2    Balla, G.3    Nath, K.4    Eaton, J.W.5    Vercellotti, G.M.6
  • 201
    • 0014408353 scopus 로고
    • Exchange of heme among hemoglobins and between hemoglobin and albumin
    • Bunn HF, Jandl JH, (1968) Exchange of heme among hemoglobins and between hemoglobin and albumin. J Biol Chem 243: 465-475
    • (1968) J Biol Chem , vol.243 , pp. 465-475
    • Bunn, H.F.1    Jandl, J.H.2
  • 207
    • 34548226931 scopus 로고    scopus 로고
    • Heme induces neutrophil migration and reactive oxygen species generation through signaling pathways characteristic of chemotactic receptors
    • Porto BN, Alves LS, Fernandez PL, Dutra TP, Figueiredo RT, Graca-Souza AV, Bozza MT, (2007) Heme induces neutrophil migration and reactive oxygen species generation through signaling pathways characteristic of chemotactic receptors. J Biol Chem 282: 24430-24436
    • (2007) J Biol Chem , vol.282 , pp. 24430-24436
    • Porto, B.N.1    Alves, L.S.2    Fernandez, P.L.3    Dutra, T.P.4    Figueiredo, R.T.5    Graca-Souza, A.V.6    Bozza, M.T.7
  • 208
    • 84902585238 scopus 로고    scopus 로고
    • Heme-induced neutrophil extracellular traps contribute to the pathogenesis of sickle cell disease
    • Chen G, Zhang D, Fuchs TA, Manwani D, Wagner DD, Frenette PS, (2014) Heme-induced neutrophil extracellular traps contribute to the pathogenesis of sickle cell disease. Blood 123: 3818-3827
    • (2014) Blood , vol.123 , pp. 3818-3827
    • Chen, G.1    Zhang, D.2    Fuchs, T.A.3    Manwani, D.4    Wagner, D.D.5    Frenette, P.S.6
  • 209
    • 0029976817 scopus 로고    scopus 로고
    • An essential role for NF-kappaB in preventing TNF-alpha-induced cell death
    • Beg AA, Baltimore D, (1996) An essential role for NF-kappaB in preventing TNF-alpha-induced cell death. Science 274: 782-784
    • (1996) Science , vol.274 , pp. 782-784
    • Beg, A.A.1    Baltimore, D.2
  • 212
    • 18544384019 scopus 로고
    • Oxidation of tartaric acid in presence of iron
    • Fenton HJH, (1894) Oxidation of tartaric acid in presence of iron. J Chem Soc (Lond) 65: 899-910
    • (1894) J Chem Soc (Lond) , vol.65 , pp. 899-910
    • Fenton, H.J.H.1
  • 214
    • 14844327760 scopus 로고    scopus 로고
    • Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases
    • Kamata H, Honda S, Maeda S, Chang L, Hirata H, Karin M, (2005) Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases. Cell 120: 649-661
    • (2005) Cell , vol.120 , pp. 649-661
    • Kamata, H.1    Honda, S.2    Maeda, S.3    Chang, L.4    Hirata, H.5    Karin, M.6
  • 216
    • 0022497852 scopus 로고
    • Genetic control of programmed cell death in the nematode C. Elegans
    • Ellis HM, Horvitz HR, (1986) Genetic control of programmed cell death in the nematode C. elegans. Cell 44: 817-829
    • (1986) Cell , vol.44 , pp. 817-829
    • Ellis, H.M.1    Horvitz, H.R.2
  • 218
    • 10044265209 scopus 로고    scopus 로고
    • JNK potentiates TNF-stimulated necrosis by increasing the production of cytotoxic reactive oxygen species
    • Ventura JJ, Cogswell P, Flavell RA, Baldwin AS Jr, Davis RJ, (2004) JNK potentiates TNF-stimulated necrosis by increasing the production of cytotoxic reactive oxygen species. Genes Dev 18: 2905-2915
    • (2004) Genes Dev , vol.18 , pp. 2905-2915
    • Ventura, J.J.1    Cogswell, P.2    Flavell, R.A.3    Baldwin, A.S.4    Davis, R.J.5
  • 220
    • 60649095328 scopus 로고    scopus 로고
    • Heme oxygenase-1: From biology to therapeutic potential
    • Soares MP, Bach FH, (2009) Heme oxygenase-1: from biology to therapeutic potential. Trends Mol Med 15: 50-58
    • (2009) Trends Mol Med , vol.15 , pp. 50-58
    • Soares, M.P.1    Bach, F.H.2
  • 221
    • 0030886054 scopus 로고    scopus 로고
    • Reduced stress defense in heme oxygenase 1-deficient cells
    • Poss KD, Tonegawa S, (1997) Reduced stress defense in heme oxygenase 1-deficient cells. Proc Natl Acad Sci USA 94: 10925-10930
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10925-10930
    • Poss, K.D.1    Tonegawa, S.2
  • 222
    • 0030886381 scopus 로고    scopus 로고
    • Heme oxygenase 1 is required for mammalian iron reutilization
    • Poss KD, Tonegawa S, (1997) Heme oxygenase 1 is required for mammalian iron reutilization. Proc Natl Acad Sci USA 94: 10919-10924
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10919-10924
    • Poss, K.D.1    Tonegawa, S.2
  • 224
    • 78650676293 scopus 로고    scopus 로고
    • Dysfunction of the heme recycling system in heme oxygenase 1-deficient mice: Effects on macrophage viability and tissue iron distribution
    • Kovtunovych G, Eckhaus MA, Ghosh MC, Ollivierre-Wilson H, Rouault TA, (2010) Dysfunction of the heme recycling system in heme oxygenase 1-deficient mice: effects on macrophage viability and tissue iron distribution. Blood 116: 6054-6062
    • (2010) Blood , vol.116 , pp. 6054-6062
    • Kovtunovych, G.1    Eckhaus, M.A.2    Ghosh, M.C.3    Ollivierre-Wilson, H.4    Rouault, T.A.5
  • 226
    • 84861004720 scopus 로고    scopus 로고
    • Iron status predicts treatment failure and mortality in tuberculosis patients: A prospective cohort study from Dar es Salaam, Tanzania
    • Isanaka S, Aboud S, Mugusi F, Bosch RJ, Willett WC, Spiegelman D, Duggan C, Fawzi WW, (2012) Iron status predicts treatment failure and mortality in tuberculosis patients: a prospective cohort study from Dar es Salaam, Tanzania. PLoS ONE 7: e37350
    • (2012) PLoS ONE , vol.7 , pp. e37350
    • Isanaka, S.1    Aboud, S.2    Mugusi, F.3    Bosch, R.J.4    Willett, W.C.5    Spiegelman, D.6    Duggan, C.7    Fawzi, W.W.8
  • 228
    • 0037124078 scopus 로고    scopus 로고
    • Heme oxygenase-1-derived carbon monoxide requires the activation of transcription factor NF-kappa B to protect endothelial cells from tumor necrosis factor-alpha-mediated apoptosis
    • Brouard S, Berberat PO, Tobiasch E, Seldon MP, Bach FH, Soares MP, (2002) Heme oxygenase-1-derived carbon monoxide requires the activation of transcription factor NF-kappa B to protect endothelial cells from tumor necrosis factor-alpha-mediated apoptosis. J Biol Chem 277: 17950-17961
    • (2002) J Biol Chem , vol.277 , pp. 17950-17961
    • Brouard, S.1    Berberat, P.O.2    Tobiasch, E.3    Seldon, M.P.4    Bach, F.H.5    Soares, M.P.6
  • 231
    • 33947697792 scopus 로고    scopus 로고
    • X-linked G6PD deficiency protects hemizygous males but not heterozygous females against severe malaria
    • Guindo A, Fairhurst RM, Doumbo OK, Wellems TE, Diallo DA, (2007) X-linked G6PD deficiency protects hemizygous males but not heterozygous females against severe malaria. PLoS Med 4: e66
    • (2007) PLoS Med , vol.4 , pp. e66
    • Guindo, A.1    Fairhurst, R.M.2    Doumbo, O.K.3    Wellems, T.E.4    Diallo, D.A.5
  • 232
    • 33746317014 scopus 로고    scopus 로고
    • Human red blood cell polymorphisms and malaria
    • Williams TN, (2006) Human red blood cell polymorphisms and malaria. Curr Opin Microbiol 9: 388-394
    • (2006) Curr Opin Microbiol , vol.9 , pp. 388-394
    • Williams, T.N.1
  • 234
    • 0036562847 scopus 로고    scopus 로고
    • Effect of lactoferrin in combination with penicillin on the morphology and the physiology of Staphylococcus aureus isolated from bovine mastitis
    • Diarra MS, Petitclerc D, Lacasse P, (2002) Effect of lactoferrin in combination with penicillin on the morphology and the physiology of Staphylococcus aureus isolated from bovine mastitis. J Dairy Sci 85: 1141-1149
    • (2002) J Dairy Sci , vol.85 , pp. 1141-1149
    • Diarra, M.S.1    Petitclerc, D.2    Lacasse, P.3
  • 239
    • 84907567820 scopus 로고    scopus 로고
    • The peculiarities and paradoxes of Plasmodium heme metabolism
    • Sigala PA, Goldberg DE, (2014) The peculiarities and paradoxes of Plasmodium heme metabolism. Annu Rev Microbiol 68: 259-278
    • (2014) Annu Rev Microbiol , vol.68 , pp. 259-278
    • Sigala, P.A.1    Goldberg, D.E.2
  • 240
    • 77956323967 scopus 로고    scopus 로고
    • The therapeutic potential of carbon monoxide
    • Motterlini R, Otterbein LE, (2010) The therapeutic potential of carbon monoxide. Nat Rev Drug Discov 9: 728-743
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 728-743
    • Motterlini, R.1    Otterbein, L.E.2
  • 241
    • 84970582209 scopus 로고
    • Synthese des haematoporphyrins, protoporphyrins und haemins
    • Fischer H, Zeile K, (1929) Synthese des haematoporphyrins, protoporphyrins und haemins. Justus Liebigs Annalen der Chemie 468: 98-116
    • (1929) Justus Liebigs Annalen der Chemie , vol.468 , pp. 98-116
    • Fischer, H.1    Zeile, K.2
  • 242
    • 0033973712 scopus 로고    scopus 로고
    • The heme synthesis and degradation pathways: Role in oxidant sensitivity. Heme oxygenase has both pro- and antioxidant properties
    • Ryter SW, Tyrrell RM, (2000) The heme synthesis and degradation pathways: role in oxidant sensitivity. Heme oxygenase has both pro- and antioxidant properties. Free Radic Biol Med 28: 289-309
    • (2000) Free Radic Biol Med , vol.28 , pp. 289-309
    • Ryter, S.W.1    Tyrrell, R.M.2


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