메뉴 건너뛰기




Volumn 8, Issue 12, 2013, Pages

Mycobacterium avium infection induces H-ferritin expression in mouse primary macrophages by activating Toll-like receptor 2

Author keywords

[No Author keywords available]

Indexed keywords

FERRITIN; FERRITIN HEAVY CHAIN; INDUCIBLE NITRIC OXIDE SYNTHASE; MESSENGER RNA; NITRIC OXIDE; TOLL LIKE RECEPTOR 2; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 84891960497     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0082874     Document Type: Article
Times cited : (22)

References (41)
  • 1
    • 0027402608 scopus 로고
    • The development of awareness of iron-withholding defense
    • Weinberg ED (1993) The development of awareness of ironwithholding defense. Perspect Biol Med 36: 215-221. PubMed: 8446492. (Pubitemid 23055082)
    • (1993) Perspectives in Biology and Medicine , vol.36 , Issue.2 , pp. 215-221
    • Weinberg, E.D.1
  • 2
    • 0035143276 scopus 로고    scopus 로고
    • Role of iron in experimental Mycobacterium avium infection
    • doi:10.1016/S1386-6532(00)00135-9. PubMed: 11166658
    • Gomes MS, Boelaert JR, Appelberg R (2001) Role of iron in experimental Mycobacterium avium infection. J Clin Virol 20: 117-122. doi:10.1016/S1386- 6532(00)00135-9. PubMed: 11166658.
    • (2001) J Clin Virol , vol.20 , pp. 117-122
    • Gomes, M.S.1    Boelaert, J.R.2    Appelberg, R.3
  • 3
  • 4
    • 0037011071 scopus 로고    scopus 로고
    • Correction of the iron overload defect in β-2-microglobulin knockout mice by lactoferrin abolishes their increased susceptibility to tuberculosis
    • DOI 10.1084/jem.20020897
    • Schaible UE, Collins HL, Priem F, Kaufmann SH (2002) Correction of the iron overload defect in beta-2-microglobulin knockout mice by lactoferrin abolishes their increased susceptibility to tuberculosis. J Exp Med 196: 1507-1513. doi:10.1084/jem.20020897. PubMed: 12461085. (Pubitemid 35424944)
    • (2002) Journal of Experimental Medicine , vol.196 , Issue.11 , pp. 1507-1513
    • Schaible, U.E.1    Collins, H.L.2    Priem, F.3    Kaufmann, S.H.E.4
  • 5
    • 53649106524 scopus 로고    scopus 로고
    • Increased susceptibility to Mycobacterium avium in hemochromatosis protein HFE-deficient mice
    • doi:10.1128/IAI.00612-08. PubMed: 18694968
    • Gomes-Pereira S, Rodrigues PN, Appelberg R, Gomes MS (2008) Increased susceptibility to Mycobacterium avium in hemochromatosis protein HFE-deficient mice. Infect Immun 76: 4713-4719. doi:10.1128/IAI.00612-08. PubMed: 18694968.
    • (2008) Infect Immun , vol.76 , pp. 4713-4719
    • Gomes-Pereira, S.1    Rodrigues, P.N.2    Appelberg, R.3    Gomes, M.S.4
  • 6
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • DOI 10.1016/0005-2728(96)00022-9
    • Harrison PM, Arosio P (1996) The ferritins: molecular properties, iron storage function and cellular regulation. Biochim Biophys Acta 1275: 161-203. doi:10.1016/0005-2728(96)00022-9. PubMed: 8695634. (Pubitemid 26248989)
    • (1996) Biochimica et Biophysica Acta - Bioenergetics , vol.1275 , Issue.3 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 7
    • 77953810574 scopus 로고    scopus 로고
    • Cytosolic and mitochondrial ferritins in the regulation of cellular iron homeostasis and oxidative damage
    • doi:10.1016/j.bbagen.2010.02.005. PubMed: 20176086
    • Arosio P, Levi S (2010) Cytosolic and mitochondrial ferritins in the regulation of cellular iron homeostasis and oxidative damage. Biochim Biophys Acta 1800: 783-792. doi:10.1016/j.bbagen.2010.02.005. PubMed: 20176086.
    • (2010) Biochim Biophys Acta , vol.1800 , pp. 783-792
    • Arosio, P.1    Levi, S.2
  • 9
    • 0037093202 scopus 로고    scopus 로고
    • Regulation of ferritin genes and protein
    • DOI 10.1182/blood.V99.10.3505
    • Torti FM, Torti SV (2002) Regulation of ferritin genes and protein. Blood 99: 3505-3516. doi:10.1182/blood.V99.10.3505. PubMed: 11986201. (Pubitemid 34534516)
    • (2002) Blood , vol.99 , Issue.10 , pp. 3505-3516
    • Torti, F.M.1    Torti, S.V.2
  • 10
    • 50949102412 scopus 로고    scopus 로고
    • Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network
    • doi:10.1146/annurev.nutr.28.061807.155521. PubMed: 18489257
    • Muckenthaler MU, Galy B, Hentze MW (2008) Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network. Annu Rev Nutr 28: 197-213. doi:10.1146/annurev.nutr.28.061807.155521. PubMed: 18489257.
    • (2008) Annu Rev Nutr , vol.28 , pp. 197-213
    • Muckenthaler, M.U.1    Galy, B.2    Hentze, M.W.3
  • 11
    • 0033213590 scopus 로고    scopus 로고
    • Differential roles of TLR2 and TLR4 in recognition of gram-negative and gram-positive bacterial cell wall components
    • DOI 10.1016/S1074-7613(00)80119-3
    • Takeuchi O, Hoshino K, Kawai T, Sanjo H, Takada H et al. (1999) Differential roles of TLR2 and TLR4 in recognition of gram-negative and gram-positive bacterial cell wall components. Immunity 11: 443-451. doi:10.1016/S1074-7613(00)80119-3. PubMed: 10549626. (Pubitemid 29504199)
    • (1999) Immunity , vol.11 , Issue.4 , pp. 443-451
    • Takeuchi, O.1    Hoshino, K.2    Kawai, T.3    Sanjo, H.4    Takada, H.5    Ogawa, T.6    Takeda, K.7    Akira, S.8
  • 12
    • 0028999596 scopus 로고
    • Altered responses to bacterial infection and endotoxic shock in mice lacking inducible nitric oxide synthase
    • doi: 10.1016/0092-8674(95)90085-3. PubMed: 7538909
    • MacMicking JD, Nathan C, Hom G, Chartrain N, Fletcher DS et al. (1995) Altered responses to bacterial infection and endotoxic shock in mice lacking inducible nitric oxide synthase. Cell 81: 641-650. doi: 10.1016/0092-8674(95) 90085-3. PubMed: 7538909.
    • (1995) Cell , vol.81 , pp. 641-650
    • Macmicking, J.D.1    Nathan, C.2    Hom, G.3    Chartrain, N.4    Fletcher, D.S.5
  • 13
    • 0034130261 scopus 로고    scopus 로고
    • Functional and immunological analysis of recombinant mouse H- and L-ferritins from Escherichia coli
    • DOI 10.1006/prep.2000.1212
    • Santambrogio P, Cozzi A, Levi S, Rovida E, Magni F et al. (2000) Functional and immunological analysis of recombinant mouse H- and L-ferritins from Escherichia coli. Protein Expr Purif 19: 212-218. doi: 10.1006/prep.2000. 1212. PubMed: 10833409. (Pubitemid 30387913)
    • (2000) Protein Expression and Purification , vol.19 , Issue.1 , pp. 212-218
    • Santambrogio, P.1    Cozzi, A.2    Levi, S.3    Rovida, E.4    Magni, F.5    Albertini, A.6    Arosio, P.7
  • 14
    • 0036581160 scopus 로고    scopus 로고
    • Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR
    • doi:10.1093/nar/30.9.e36. PubMed: 11972351
    • Pfaffl MW, Horgan GW, Dempfle L (2002) Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR. Nucleic Acids Res 30: e36. doi:10.1093/nar/30.9.e36. PubMed: 11972351.
    • (2002) Nucleic Acids Res , vol.30
    • Pfaffl, M.W.1    Horgan, G.W.2    Dempfle, L.3
  • 15
    • 0024121621 scopus 로고
    • Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5' untranslated region of ferritin heavy- and light-subunit mRNAs
    • DOI 10.1073/pnas.85.7.2171
    • Leibold EA, Munro HN (1988) Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5' untranslated region of ferritin heavy- and light-subunit mRNAs. Proc Natl Acad Sci U S A 85: 2171-2175. doi:10.1073/pnas.85.7.2171. PubMed: 3127826. (Pubitemid 24315851)
    • (1988) Proceedings of the National Academy of Sciences of the United States of America , vol.85 , Issue.7 , pp. 2171-2175
    • Leibold, E.A.1    Munro, H.N.2
  • 16
    • 0024365045 scopus 로고
    • A specific mRNA binding factor regulates the iron-dependent stability of cytoplasmic transferrin receptor mRNA
    • DOI 10.1016/0092-8674(89)90851-9
    • Müllner EW, Neupert B, Kühn LC (1989) A specific mRNA binding factor regulates the iron-dependent stability of cytoplasmic transferrin receptor mRNA. Cell 58: 373-382. doi:10.1016/0092-8674(89)90851-9. PubMed: 2752428. (Pubitemid 19191418)
    • (1989) Cell , vol.58 , Issue.2 , pp. 373-382
    • Mullner, E.W.1    Neupert, B.2    Kuhn, L.C.3
  • 17
    • 0029147036 scopus 로고
    • Relationship between virulence of Mycobacterium avium strains and induction of tumor necrosis factor alpha production in infected mice and in in vitro-cultured mouse macrophages
    • PubMed: 7558277
    • Sarmento AM, Appelberg R (1995) Relationship between virulence of Mycobacterium avium strains and induction of tumor necrosis factor alpha production in infected mice and in in vitro-cultured mouse macrophages. Infect Immun 63: 3759-3764. PubMed: 7558277.
    • (1995) Infect Immun , vol.63 , pp. 3759-3764
    • Sarmento, A.M.1    Appelberg, R.2
  • 18
    • 0028981059 scopus 로고
    • Role for NF-kappa B in the regulation of ferritin H by tumor necrosis factoralpha
    • doi:10.1074/jbc.270.25.15285. PubMed: 7797515
    • Kwak EL, Larochelle DA, Beaumont C, Torti SV, Torti FM (1995) Role for NF-kappa B in the regulation of ferritin H by tumor necrosis factoralpha. J Biol Chem 270: 15285-15293. doi:10.1074/jbc.270.25.15285. PubMed: 7797515.
    • (1995) J Biol Chem , vol.270 , pp. 15285-15293
    • Kwak, E.L.1    Larochelle, D.A.2    Beaumont, C.3    Torti, S.V.4    Torti, F.M.5
  • 19
    • 0036263080 scopus 로고    scopus 로고
    • Differential regulation of the mitogen-activated protein kinases by pathogenic and nonpathogenic mycobacteria
    • DOI 10.1128/IAI.70.6.3040-3052.2002
    • Roach SK, Schorey JS (2002) Differential regulation of the mitogenactivated protein kinases by pathogenic and nonpathogenic mycobacteria. Infect Immun 70: 3040-3052. doi:10.1128/IAI. 70.6.3040-3052.2002. PubMed: 12010996. (Pubitemid 34564165)
    • (2002) Infection and Immunity , vol.70 , Issue.6 , pp. 3040-3052
    • Roach, S.K.1    Schorey, J.S.2
  • 20
    • 79959539376 scopus 로고    scopus 로고
    • Iron regulatory protein 1 outcompetes iron regulatory protein 2 in regulating cellular iron homeostasis in response to nitric oxide
    • PubMed: 21566147
    • Styś A, Galy B, Starzyński RR, Smuda E, Drapier JC et al. (2011) Iron regulatory protein 1 outcompetes iron regulatory protein 2 in regulating cellular iron homeostasis in response to nitric oxide. J Biol Chem, 286: 22846-54. PubMed: 21566147.
    • (2011) J Biol Chem , vol.286 , pp. 22846-22854
    • Styś, A.1    Galy, B.2    Starzyński, R.R.3    Smuda, E.4    Drapier, J.C.5
  • 21
    • 0033215123 scopus 로고    scopus 로고
    • Human Toll-like receptors mediate cellular activation by Mycobacterium tuberculosis
    • Means TK, Wang S, Lien E, Yoshimura A, Golenbock DT et al. (1999) Human toll-like receptors mediate cellular activation by Mycobacterium tuberculosis. J Immunol 163: 3920-3927. PubMed: 10490993. (Pubitemid 29450920)
    • (1999) Journal of Immunology , vol.163 , Issue.7 , pp. 3920-3927
    • Means, T.K.1    Wang, S.2    Lien, E.3    Yoshimura, A.4    Golenbock, D.T.5    Fenton, M.J.6
  • 22
    • 33947199360 scopus 로고    scopus 로고
    • The diacylated lipopeptide FSL-1 enhances phagocytosis of bacteria by macrophages through a Toll-like receptor 2-mediated signalling pathway
    • DOI 10.1111/j.1574-695X.2007.00218.x
    • Mae M, Iyori M, Yasuda M, Shamsul HM, Kataoka H et al. (2007) The diacylated lipopeptide FSL-1 enhances phagocytosis of bacteria by macrophages through a Toll-like receptor 2-mediated signalling pathway. FEMS Immunol Med Microbiol 49: 398-409. doi:10.1111/j. 1574-695X.2007.00218.x. PubMed: 17316370. (Pubitemid 46435018)
    • (2007) FEMS Immunology and Medical Microbiology , vol.49 , Issue.3 , pp. 398-409
    • Mae, M.1    Iyori, M.2    Yasuda, M.3    Shamsul, H.M.4    Kataoka, H.5    Kiura, K.6    Hasebe, A.7    Totsuka, Y.8    Shibata, K.-I.9
  • 24
    • 2542564199 scopus 로고    scopus 로고
    • Differential gene expression in mononuclear phagocytes infected with pathogenic and non-pathogenic mycobacteria
    • DOI 10.1111/j.1365-2249.2004.02490.x
    • McGarvey JA, Wagner D, Bermudez LE (2004) Differential gene expression in mononuclear phagocytes infected with pathogenic and non-pathogenic mycobacteria. Clin Exp Immunol 136: 490-500. doi: 10.1111/j.1365-2249.2004. 02490.x. PubMed: 15147351. (Pubitemid 38703683)
    • (2004) Clinical and Experimental Immunology , vol.136 , Issue.3 , pp. 490-500
    • Mcgarvey, J.A.1    Wagner, D.2    Bermudez, L.E.3
  • 25
    • 27744476720 scopus 로고    scopus 로고
    • Effects of Anaplasma phagocytophilum on host cell ferritin mRNA and protein levels
    • DOI 10.1128/IAI.73.11.7629-7636.2005
    • Carlyon JA, Ryan D, Archer K, Fikrig E (2005) Effects of Anaplasma phagocytophilum on host cell ferritin mRNA and protein levels. Infect Immun 73: 7629-7636. doi:10.1128/IAI.73.11.7629-7636.2005. PubMed: 16239567. (Pubitemid 41587669)
    • (2005) Infection and Immunity , vol.73 , Issue.11 , pp. 7629-7636
    • Carlyon, J.A.1    Ryan, D.2    Archer, K.3    Fikrig, E.4
  • 26
    • 34547863499 scopus 로고    scopus 로고
    • The co-ordinated regulation of iron homeostasis in murine macrophages limits the availability of iron for intracellular Salmonella typhimurium
    • DOI 10.1111/j.1462-5822.2007.00942.x
    • Nairz M, Theurl I, Ludwiczek S, Theurl M, Mair SM et al. (2007) The coordinated regulation of iron homeostasis in murine macrophages limits the availability of iron for intracellular Salmonella typhimurium. Cell Microbiol 9: 2126-2140. doi:10.1111/j.1462-5822.2007.00942.x. PubMed: 17466014. (Pubitemid 47250286)
    • (2007) Cellular Microbiology , vol.9 , Issue.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
  • 27
    • 77949543589 scopus 로고    scopus 로고
    • Modulation of iron homeostasis in macrophages by bacterial intracellular pathogens
    • doi:10.1186/1471-2180-10-64. PubMed: 20184753
    • Pan X, Tamilselvam B, Hansen EJ, Daefler S (2010) Modulation of iron homeostasis in macrophages by bacterial intracellular pathogens. BMC Microbiol 10: 64. doi:10.1186/1471-2180-10-64. PubMed: 20184753.
    • (2010) BMC Microbiol , vol.10 , pp. 64
    • Pan, X.1    Tamilselvam, B.2    Hansen, E.J.3    Daefler, S.4
  • 29
    • 51149087071 scopus 로고    scopus 로고
    • Engagement of Toll-like receptor 2 in mouse macrophages infected with Mycobacterium avium induces non-oxidative and TNFindependent anti-mycobacterial activity
    • doi:10.1002/eji.200737954. PubMed: 18624355
    • Gomes MS, Sousa Fernandes S, Cordeiro JV, Silva Gomes S, Vieira A et al. (2008) Engagement of Toll-like receptor 2 in mouse macrophages infected with Mycobacterium avium induces non-oxidative and TNFindependent anti-mycobacterial activity. Eur J Immunol 38: 2180-2189. doi:10.1002/eji.200737954. PubMed: 18624355.
    • (2008) Eur J Immunol , vol.38 , pp. 2180-2189
    • Gomes, M.S.1    Sousa Fernandes, S.2    Cordeiro, J.V.3    Silva Gomes, S.4    Vieira, A.5
  • 30
    • 0032546922 scopus 로고    scopus 로고
    • Role of ferritin in the control of the labile iron pool in murine erythroleukemia cells
    • DOI 10.1074/jbc.273.25.15382
    • Picard V, Epsztejn S, Santambrogio P, Cabantchik ZI, Beaumont C (1998) Role of ferritin in the control of the labile iron pool in murine erythroleukemia cells. J Biol Chem 273: 15382-15386. doi:10.1074/jbc. 273.25.15382. PubMed: 9624120. (Pubitemid 28298142)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.25 , pp. 15382-15386
    • Picard, V.1    Epsztejn, S.2    Santambrogio, P.3    Cabantchik, Z.I.4    Beaumont, C.5
  • 31
    • 33746881453 scopus 로고    scopus 로고
    • Macrophage nutriprive antimicrobial mechanisms
    • DOI 10.1189/jlb.0206079
    • Appelberg R (2006) Macrophage nutriprive antimicrobial mechanisms. J Leukoc Biol 79: 1117-1128. doi:10.1189/jlb.0206079. PubMed: 16603587. (Pubitemid 44835544)
    • (2006) Journal of Leukocyte Biology , vol.79 , Issue.6 , pp. 1117-1128
    • Appelberg, R.1
  • 32
    • 1542373640 scopus 로고    scopus 로고
    • Analysis of the biologic functions of H- and L-ferritins in HeLa cells by transfection with siRNAs and cDNAs: Evidence for a proliferative role of L-ferritin
    • DOI 10.1182/blood-2003-06-1842
    • Cozzi A, Corsi B, Levi S, Santambrogio P, Biasiotto G et al. (2004) Analysis of the biologic functions of H- and L-ferritins in HeLa cells by transfection with siRNAs and cDNAs: evidence for a proliferative role of L-ferritin. Blood 103: 2377-2383. doi:10.1182/blood-2003-06-1842. PubMed: 14615379. (Pubitemid 38326261)
    • (2004) Blood , vol.103 , Issue.6 , pp. 2377-2383
    • Cozzi, A.1    Corsi, B.2    Levi, S.3    Santambrogio, P.4    Biasiotto, G.5    Arosio, P.6
  • 33
    • 0035353194 scopus 로고    scopus 로고
    • Repression of ferritin expression increases the labile iron pool, oxidative stress, and shortterm growth of human erythroleukemia cells
    • doi: 10.1182/blood.V97.9.2863. PubMed: 11313282
    • Kakhlon O, Gruenbaum Y, Cabantchik ZI (2001) Repression of ferritin expression increases the labile iron pool, oxidative stress, and shortterm growth of human erythroleukemia cells. Blood 97: 2863-2871. doi: 10.1182/blood.V97.9.2863. PubMed: 11313282.
    • (2001) Blood , vol.97 , pp. 2863-2871
    • Kakhlon, O.1    Gruenbaum, Y.2    Cabantchik, Z.I.3
  • 35
    • 67349115201 scopus 로고    scopus 로고
    • Iron metabolism in the anemia of chronic disease
    • doi:10.1016/j.bbagen. 2008.08.006. PubMed: 18786614
    • Weiss G (2009) Iron metabolism in the anemia of chronic disease. Biochim Biophys Acta 1790: 682-693. doi:10.1016/j.bbagen. 2008.08.006. PubMed: 18786614.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 682-693
    • Weiss, G.1
  • 36
    • 14544294358 scopus 로고    scopus 로고
    • Modification of iron regulation by the inflammatory response
    • DOI 10.1016/j.beha.2004.09.001, PII S1521692604000933
    • Weiss G (2005) Modification of iron regulation by the inflammatory response. Best Pract Res Clin Haematol 18: 183-201. PubMed: 15737884. (Pubitemid 40298364)
    • (2005) Best Practice and Research: Clinical Haematology , vol.18 , Issue.2 SPEC. ISS. , pp. 183-201
    • Weiss, G.1
  • 37
    • 85047693999 scopus 로고    scopus 로고
    • Anemia of inflammation: The cytokine-hepcidin link
    • DOI 10.1172/JCI200421441
    • Andrews NC (2004) Anemia of inflammation: the cytokine-hepcidin link. J Clin Invest 113: 1251-1253. doi:10.1172/JCI21441. PubMed: 15124013. (Pubitemid 39069921)
    • (2004) Journal of Clinical Investigation , vol.113 , Issue.9 , pp. 1251-1253
    • Andrews, N.C.1
  • 38
    • 0037125975 scopus 로고    scopus 로고
    • Nitrogen monoxide-mediated control of ferritin synthesis: Implications for macrophage iron homeostasis
    • doi:10.1073/pnas.192316099. PubMed: 12209009
    • Kim S, Ponka P (2002) Nitrogen monoxide-mediated control of ferritin synthesis: implications for macrophage iron homeostasis. Proc Natl Acad Sci U S A 99: 12214-12219. doi:10.1073/pnas.192316099. PubMed: 12209009.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 12214-12219
    • Kim, S.1    Ponka, P.2
  • 39
    • 0024431912 scopus 로고
    • Induction of hypoferremia and modulation of macrophage iron metabolism by tumor necrosis factor
    • Alvarez-Hernández X, Licéaga J, McKay IC, Brock JH (1989) Induction of hypoferremia and modulation of macrophage iron metabolism by tumor necrosis factor. Lab Invest 61: 319-322. PubMed: 2788773. (Pubitemid 19249645)
    • (1989) Laboratory Investigation , vol.61 , Issue.3 , pp. 319-322
    • Alvarez-Hernandez, X.1    Liceaga, J.2    McKay, I.C.3    Brock, J.H.4
  • 40
    • 33745526068 scopus 로고    scopus 로고
    • Tumour necrosis factor α causes hypoferraemia and reduced intestinal iron absorption in mice
    • DOI 10.1042/BJ20060215
    • Laftah AH, Sharma N, Brookes MJ, McKie AT, Simpson RJ et al. (2006) Tumour necrosis factor alpha causes hypoferraemia and reduced intestinal iron absorption in mice. Biochem J 397: 61-67. doi: 10.1042/BJ20060215. PubMed: 16566752. (Pubitemid 44032837)
    • (2006) Biochemical Journal , vol.397 , Issue.1 , pp. 61-67
    • Laftah, A.H.1    Sharma, N.2    Brookes, M.J.3    Mckie, A.T.4    Simpson, R.J.5    Iqbal, T.H.6    Tselepis, C.7
  • 41
    • 80052101945 scopus 로고    scopus 로고
    • Mycobacteria-induced anaemia revisited: A molecular approach reveals the involvement of NRAMP1 and lipocalin-2, but not of hepcidin
    • doi: 10.1016/j.imbio.2011.04.004. PubMed: 21601942
    • Rodrigues PN, Gomes SS, Neves JV, Gomes-Pereira S, Correia- Neves M et al. (2011) Mycobacteria-induced anaemia revisited: A molecular approach reveals the involvement of NRAMP1 and lipocalin-2, but not of hepcidin. Immunobiology 216: 1127-1134. doi: 10.1016/j.imbio.2011.04.004. PubMed: 21601942.
    • (2011) Immunobiology , vol.216 , pp. 1127-1134
    • Rodrigues, P.N.1    Gomes, S.S.2    Neves, J.V.3    Gomes-Pereira, S.4    Correia- Neves, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.