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Volumn 137, Issue 2, 2004, Pages 321-328

Constitutive differences in Cu/Zn superoxide dismutase mRNA levels and activity in hemocytes of Biomphalaria glabrata (Mollusca) that are either susceptible or resistant to Schistosoma mansoni (Trematoda)

Author keywords

Biomphalaria glabrata; Hemocyte; Hydrogen peroxide; Respiratory burst; Schistosoma mansoni; Superoxide dismutase

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE;

EID: 4644297299     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2004.06.011     Document Type: Article
Times cited : (52)

References (49)
  • 1
    • 0015369017 scopus 로고
    • Genetic factors in the susceptibility of juvenile Biomphalaria glabrata to Schistosoma mansoni infection
    • C.S. Richards, and J.W. Merritt Jr. Genetic factors in the susceptibility of juvenile Biomphalaria glabrata to Schistosoma mansoni infection Am. J. Trop. Med. Hyg. 21 1972 425 434
    • (1972) Am. J. Trop. Med. Hyg. , vol.21 , pp. 425-434
    • Richards, C.S.1    Merritt Jr., J.W.2
  • 2
    • 0035218436 scopus 로고    scopus 로고
    • Coevolution and compatibility in the snail-schistosome system
    • J.P. Webster, and C.M. Davies Coevolution and compatibility in the snail-schistosome system Parasitology 123 2001 S41 S56
    • (2001) Parasitology , vol.123
    • Webster, J.P.1    Davies, C.M.2
  • 3
    • 0035071154 scopus 로고    scopus 로고
    • Compatibility and sex in a snail-schistosome system
    • J.P. Webster Compatibility and sex in a snail-schistosome system Parasitology 122 2001 423 432
    • (2001) Parasitology , vol.122 , pp. 423-432
    • Webster, J.P.1
  • 4
    • 0033574053 scopus 로고    scopus 로고
    • The identification of markers segregating with resistance to Schistosoma mansoni infection in the snail Biomphalaria glabrata
    • M. Knight, A.N. Miller, and C.N. Patterson The identification of markers segregating with resistance to Schistosoma mansoni infection in the snail Biomphalaria glabrata Proc. Natl. Acad. Sci. USA 96 1999 1510 1515
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1510-1515
    • Knight, M.1    Miller, A.N.2    Patterson, C.N.3
  • 5
    • 0035217036 scopus 로고    scopus 로고
    • Molecular approaches in the study of Biomphalaria glabrata-Schistosoma mansoni interactions: Linkage analysis and gene expression profiling
    • C.S. Jones, A.E. Lockyer, D. Rollinson, and L.R. Noble Molecular approaches in the study of Biomphalaria glabrata-Schistosoma mansoni interactions: linkage analysis and gene expression profiling Parasitology 123 2001 S181 S196
    • (2001) Parasitology , vol.123
    • Jones, C.S.1    Lockyer, A.E.2    Rollinson, D.3    Noble, L.R.4
  • 6
    • 0035218016 scopus 로고    scopus 로고
    • The relationship between Schistosoma mansoni and Biomphalaria glabrata: Genetic and molecular approaches
    • F.A. Lewis, C.N. Patterson, M. Knight, and C.S. Richards The relationship between Schistosoma mansoni and Biomphalaria glabrata: genetic and molecular approaches Parasitology 123 2001 S169 S179
    • (2001) Parasitology , vol.123
    • Lewis, F.A.1    Patterson, C.N.2    Knight, M.3    Richards, C.S.4
  • 7
    • 0035038423 scopus 로고    scopus 로고
    • Differential display analysis of hemocytes from schistosome-resistant and schistosome-susceptible intermediate hosts
    • O. Schneider, and U.E. Zelck Differential display analysis of hemocytes from schistosome-resistant and schistosome-susceptible intermediate hosts Parasitol. Res. 87 2001 489 491
    • (2001) Parasitol. Res. , vol.87 , pp. 489-491
    • Schneider, O.1    Zelck, U.E.2
  • 8
    • 0037330033 scopus 로고    scopus 로고
    • Comparative gene analysis of Biomphalaria glabrata hemocytes pre- and post-exposure to miracidia of Schistosoma mansoni
    • N. Raghavan, A.N. Miller, and M. Gardner Comparative gene analysis of Biomphalaria glabrata hemocytes pre- and post-exposure to miracidia of Schistosoma mansoni Mol. Biochem. Parasitol. 126 2003 181 191
    • (2003) Mol. Biochem. Parasitol. , vol.126 , pp. 181-191
    • Raghavan, N.1    Miller, A.N.2    Gardner, M.3
  • 9
    • 0030831258 scopus 로고    scopus 로고
    • A family of fibrinogen-related proteins that precipitates parasite-derived molecules is produced by an invertebrate after infection
    • C.M. Adema, L.A. Hertel, R.D. Miller, and E.S. Loker A family of fibrinogen-related proteins that precipitates parasite-derived molecules is produced by an invertebrate after infection Proc. Natl. Acad. Sci. USA 94 1997 8691 8696
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8691-8696
    • Adema, C.M.1    Hertel, L.A.2    Miller, R.D.3    Loker, E.S.4
  • 10
    • 0020638879 scopus 로고
    • Acquired resistance in snails. Induction of resistance to Schistosoma mansoni in Biomphalaria glabrata
    • K.J. Lie, K.H. Jeong, and D. Heyneman Acquired resistance in snails. Induction of resistance to Schistosoma mansoni in Biomphalaria glabrata Int. J. Parasitol. 13 1983 301 304
    • (1983) Int. J. Parasitol. , vol.13 , pp. 301-304
    • Lie, K.J.1    Jeong, K.H.2    Heyneman, D.3
  • 11
    • 0035060549 scopus 로고    scopus 로고
    • Molecular studies of the molluscan response to digenean infection
    • E.S. Loker, and C.J. Bayne Molecular studies of the molluscan response to digenean infection Adv. Exp. Med. Biol. 484 2001 209 222
    • (2001) Adv. Exp. Med. Biol. , vol.484 , pp. 209-222
    • Loker, E.S.1    Bayne, C.J.2
  • 12
    • 0018967079 scopus 로고
    • Macrophage-like hemocytes of resistant Biomphalaria glabrata are cytotoxic for sporocysts of Schistosoma mansoni in vitro
    • C.J. Bayne, P.M. Buckley, and P.C. DeWan Macrophage-like hemocytes of resistant Biomphalaria glabrata are cytotoxic for sporocysts of Schistosoma mansoni in vitro J. Parasitol. 66 1980 413 419
    • (1980) J. Parasitol. , vol.66 , pp. 413-419
    • Bayne, C.J.1    Buckley, P.M.2    Dewan, P.C.3
  • 13
    • 0029994689 scopus 로고    scopus 로고
    • Killing of Schistosoma mansoni sporocysts by Biomphalaria glabrata hemolymph in vitro: Alteration of hemocyte behavior after poly-l-lysine treatment of plastic, and the kinetics of killing by different host strains
    • A.M. Boehmler, S.E. Fryer, and C.J. Bayne Killing of Schistosoma mansoni sporocysts by Biomphalaria glabrata hemolymph in vitro: alteration of hemocyte behavior after poly-l-lysine treatment of plastic, and the kinetics of killing by different host strains J. Parasitol. 82 1996 332 335
    • (1996) J. Parasitol. , vol.82 , pp. 332-335
    • Boehmler, A.M.1    Fryer, S.E.2    Bayne, C.J.3
  • 14
    • 0035052928 scopus 로고    scopus 로고
    • Killing of Schistosoma mansoni sporocysts by hemocytes from resistant Biomphalaria glabrata: Role of reactive oxygen species
    • U.K. Hahn, R.C. Bender, and C.J. Bayne Killing of Schistosoma mansoni sporocysts by hemocytes from resistant Biomphalaria glabrata: role of reactive oxygen species J. Parasitol. 87 2001 292 299
    • (2001) J. Parasitol. , vol.87 , pp. 292-299
    • Hahn, U.K.1    Bender, R.C.2    Bayne, C.J.3
  • 15
    • 0035218399 scopus 로고    scopus 로고
    • Mechanisms of molluscan host resistance and of parasite strategies for survival
    • C.J. Bayne, U.K. Hahn, and R.C. Bender Mechanisms of molluscan host resistance and of parasite strategies for survival Parasitology 123 2001 S159 S167
    • (2001) Parasitology , vol.123
    • Bayne, C.J.1    Hahn, U.K.2    Bender, R.C.3
  • 16
    • 0027991050 scopus 로고
    • Free radicals and antioxidants: A personal view
    • B. Halliwell Free radicals and antioxidants: a personal view Nutr. Rev. 52 1994 253 265
    • (1994) Nutr. Rev. , vol.52 , pp. 253-265
    • Halliwell, B.1
  • 17
    • 0034850770 scopus 로고    scopus 로고
    • Involvement of nitric oxide in killing of Schistosoma mansoni sporocysts by hemocytes from resistant Biomphalaria glabrata
    • U.K. Hahn, R.C. Bender, and C.J. Bayne Involvement of nitric oxide in killing of Schistosoma mansoni sporocysts by hemocytes from resistant Biomphalaria glabrata J. Parasitol. 87 2001 778 785
    • (2001) J. Parasitol. , vol.87 , pp. 778-785
    • Hahn, U.K.1    Bender, R.C.2    Bayne, C.J.3
  • 18
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1
    • R. Schreck, P. Rieber, and P.A. Baeuerle Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1 EMBO J. 10 1991 2247 2258
    • (1991) EMBO J. , vol.10 , pp. 2247-2258
    • Schreck, R.1    Rieber, P.2    Baeuerle, P.A.3
  • 20
    • 0032411042 scopus 로고    scopus 로고
    • Roles of reactive oxygen species: Signaling and regulation of cellular functions
    • I.A. Gamaley, and I.V. Klyubin Roles of reactive oxygen species: signaling and regulation of cellular functions Int. Rev. Cytol. 188 1999 203 255
    • (1999) Int. Rev. Cytol. , vol.188 , pp. 203-255
    • Gamaley, I.A.1    Klyubin, I.V.2
  • 21
    • 0036911138 scopus 로고    scopus 로고
    • Hydrogen peroxide as second messenger in lymphocyte activation
    • M. Reth Hydrogen peroxide as second messenger in lymphocyte activation Nat. Immunol. 3 2002 1129 1134
    • (2002) Nat. Immunol. , vol.3 , pp. 1129-1134
    • Reth, M.1
  • 22
    • 0037157177 scopus 로고    scopus 로고
    • Hydrogen peroxide activates IκB kinases through phosphorylation of serine residues in the activation loops
    • H. Kamata, T. Manabe, S. Oka, K. Kamata, and H. Hirata Hydrogen peroxide activates IκB kinases through phosphorylation of serine residues in the activation loops FEBS Lett. 519 2002 231 237
    • (2002) FEBS Lett. , vol.519 , pp. 231-237
    • Kamata, H.1    Manabe, T.2    Oka, S.3    Kamata, K.4    Hirata, H.5
  • 23
    • 0037449777 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of IκBα activates NFκB through a redox-regulated and c-src-dependent mechanism following hypoxia/reoxygenation
    • C. Fan, Q. Li, D. Ross, and J.F. Engelhardt Tyrosine phosphorylation of IκBα activates NFκB through a redox-regulated and c-src-dependent mechanism following hypoxia/reoxygenation J. Biol. Chem. 278 2003 2072 2080
    • (2003) J. Biol. Chem. , vol.278 , pp. 2072-2080
    • Fan, C.1    Li, Q.2    Ross, D.3    Engelhardt, J.F.4
  • 24
    • 0037591401 scopus 로고    scopus 로고
    • Hydrogen peroxide activates NFκB through tyrosine phosphorylation of IκBα and serine phosphorylation of p65
    • Y. Takada, A. Mukhopadhyay, G.C. Kundu, H. Mahabeleshwar, S. Singh, and B.B. Aggarwal Hydrogen peroxide activates NFκB through tyrosine phosphorylation of IκBα and serine phosphorylation of p65 J. Biol. Chem. 278 2003 24233 24241
    • (2003) J. Biol. Chem. , vol.278 , pp. 24233-24241
    • Takada, Y.1    Mukhopadhyay, A.2    Kundu, G.C.3    Mahabeleshwar, H.4    Singh, S.5    Aggarwal, B.B.6
  • 26
    • 0033623993 scopus 로고    scopus 로고
    • Vanadium-induced κb-dependent transcription depends upon peroxide-induced activation of the p38 mitogen-activated protein kinase
    • I. Jaspers, J.M. Samet, S. Erzurum, and W. Reed Vanadium-induced κB-dependent transcription depends upon peroxide-induced activation of the p38 mitogen-activated protein kinase Am. J. Respir. Cell Mol. Biol. 23 2000 95 102
    • (2000) Am. J. Respir. Cell Mol. Biol. , vol.23 , pp. 95-102
    • Jaspers, I.1    Samet, J.M.2    Erzurum, S.3    Reed, W.4
  • 27
    • 0029730738 scopus 로고    scopus 로고
    • A conserved signaling pathway: The Drosophila Toll-dorsal pathway
    • M.P. Belvin, and K.V. Anderson A conserved signaling pathway: the Drosophila Toll-dorsal pathway Annu. Rev. Cell Dev. Biol. 12 1996 393 416
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 393-416
    • Belvin, M.P.1    Anderson, K.V.2
  • 28
    • 0029874138 scopus 로고    scopus 로고
    • The NF-κB and IκB proteins: New discoveries and insights
    • A.S. Baldwin The NF-κB and IκB proteins: new discoveries and insights Annu. Rev. Immunol. 14 1996 649 683
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 649-683
    • Baldwin, A.S.1
  • 29
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • I. Fridovich Superoxide radical and superoxide dismutases Ann. Rev. Biochem. 64 1995 97 112
    • (1995) Ann. Rev. Biochem. , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 30
  • 31
    • 75449122146 scopus 로고
    • Observations on hearts explanted in vitro from the snail Australorbis glabratus
    • E. Chernin Observations on hearts explanted in vitro from the snail Australorbis glabratus J. Parasitol. 49 1963 353 364
    • (1963) J. Parasitol. , vol.49 , pp. 353-364
    • Chernin, E.1
  • 32
    • 0018346567 scopus 로고
    • Schistosome sporocyst-killing amoebae isolated from Biomphalaria glabrata
    • H.H. Stibbs, A. Owczarzak, C.J. Bayne, and P. DeWan Schistosome sporocyst-killing amoebae isolated from Biomphalaria glabrata J. Invertebr. Pathol. 33 1979 159 170
    • (1979) J. Invertebr. Pathol. , vol.33 , pp. 159-170
    • Stibbs, H.H.1    Owczarzak, A.2    Bayne, C.J.3    Dewan, P.4
  • 33
    • 0002413383 scopus 로고
    • Laboratory maintenance of parasites
    • A.J. MacInnis M. Voge WH Freeman Co. San Francisco
    • M.J. Ulmer Laboratory maintenance of parasites A.J. MacInnis M. Voge Experiments and techniques in parasitology 1970 WH Freeman Co. San Francisco 143 144
    • (1970) Experiments and Techniques in Parasitology , pp. 143-144
    • Ulmer, M.J.1
  • 34
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • S.F. Altschul, T.L. Madden, and A.A. Schäffer Gapped BLAST and PSI-BLAST: a new generation of protein database search programs Nucleic Acids Res. 25 1997 3389 3402
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schäffer, A.A.3
  • 35
    • 0036199344 scopus 로고    scopus 로고
    • Schistosoma mansoni sporocysts in culture: Host plasma hemoglobin contributes to in vitro oxidative stress
    • R.C. Bender, L.M. Bixler, J.P. Lerner, and C.J. Bayne Schistosoma mansoni sporocysts in culture: host plasma hemoglobin contributes to in vitro oxidative stress J. Parasitol. 88 2002 14 18
    • (2002) J. Parasitol. , vol.88 , pp. 14-18
    • Bender, R.C.1    Bixler, L.M.2    Lerner, J.P.3    Bayne, C.J.4
  • 36
    • 0036509440 scopus 로고    scopus 로고
    • Molecular evolution and structure-function relationships of the superoxide dismutase gene families in angiosperms and their relationship to other eukaryotic and prokaryotic superoxide dismutases
    • R.C. Fink, and J.G. Scandalios Molecular evolution and structure-function relationships of the superoxide dismutase gene families in angiosperms and their relationship to other eukaryotic and prokaryotic superoxide dismutases Arch. Biochem. Biophys. 399 2002 19 36
    • (2002) Arch. Biochem. Biophys. , vol.399 , pp. 19-36
    • Fink, R.C.1    Scandalios, J.G.2
  • 37
    • 0032619552 scopus 로고    scopus 로고
    • Protein identification and analysis tools in the ExPASy server
    • M.R. Wilkins, E. Gasteiger, and A. Bairoch Protein identification and analysis tools in the ExPASy server Methods Mol. Biol. 112 1999 531 552
    • (1999) Methods Mol. Biol. , vol.112 , pp. 531-552
    • Wilkins, M.R.1    Gasteiger, E.2    Bairoch, A.3
  • 38
    • 0028934698 scopus 로고
    • Schistosoma mansoni: Cloning the gene encoding glutathione peroxidase
    • H. Mei, and P.T. LoVerde Schistosoma mansoni: cloning the gene encoding glutathione peroxidase Exp. Parasitol. 2 1995 319 322
    • (1995) Exp. Parasitol. , vol.2 , pp. 319-322
    • Mei, H.1    Loverde, P.T.2
  • 39
    • 0023718665 scopus 로고
    • Antioxidant systems in Schistosoma mansoni: Evidence for their role in protection of the adult worms against oxidant killing
    • G.M. Mkoji, J.M. Smith, and R.K. Prichard Antioxidant systems in Schistosoma mansoni: evidence for their role in protection of the adult worms against oxidant killing Int. J. Parasitol. 5 1988 667 673
    • (1988) Int. J. Parasitol. , vol.5 , pp. 667-673
    • Mkoji, G.M.1    Smith, J.M.2    Prichard, R.K.3
  • 40
    • 0029059884 scopus 로고
    • Cytochrome c peroxidase in Schistosoma mansoni: Enzyme kinetics and cellular localization
    • E.G. Campos, J.M. Smith, and R.K. Prichard Cytochrome c peroxidase in Schistosoma mansoni: enzyme kinetics and cellular localization Comp. Biochem. Physiol. 111B 1995 371 377
    • (1995) Comp. Biochem. Physiol. , vol.111 , pp. 371-377
    • Campos, E.G.1    Smith, J.M.2    Prichard, R.K.3
  • 41
    • 0033783654 scopus 로고    scopus 로고
    • Molecular and enzymatic characterization of Schistosoma mansoni thioredoxin peroxidase
    • M.A. Kwatia, D.J. Botkin, and D.L. Williams Molecular and enzymatic characterization of Schistosoma mansoni thioredoxin peroxidase J. Parasitol. 86 2000 908 915
    • (2000) J. Parasitol. , vol.86 , pp. 908-915
    • Kwatia, M.A.1    Botkin, D.J.2    Williams, D.L.3
  • 42
    • 84939677098 scopus 로고
    • Different regulation of the formation of intra- and extra-cellular oxygen radicals in macrophages
    • P. Dieter, U. Arlt, and E. Fitzke Different regulation of the formation of intra- and extra-cellular oxygen radicals in macrophages Biol. Signals 4 1995 331 337
    • (1995) Biol. Signals , vol.4 , pp. 331-337
    • Dieter, P.1    Arlt, U.2    Fitzke, E.3
  • 43
    • 0033822418 scopus 로고    scopus 로고
    • Phorbol myristate acetate induces neutrophil NADPH-oxidase activity by two separate signal transduction pathways: Dependent or independent of phosphatidylinositol 3-kinase
    • A. Karlsson, J.B. Nixon, and L.C. McPhail Phorbol myristate acetate induces neutrophil NADPH-oxidase activity by two separate signal transduction pathways: dependent or independent of phosphatidylinositol 3-kinase J. Leukocyte Biol. 67 2000 396 404
    • (2000) J. Leukocyte Biol. , vol.67 , pp. 396-404
    • Karlsson, A.1    Nixon, J.B.2    McPhail, L.C.3
  • 44
    • 0035057745 scopus 로고    scopus 로고
    • Evaluation of the process for superoxide production by NADPH oxidase in human neutrophils: Evidence for cytoplasmic origin of superoxide
    • T. Kobayashi, S. Tsunawaki, and H. Seguchi Evaluation of the process for superoxide production by NADPH oxidase in human neutrophils: evidence for cytoplasmic origin of superoxide Redox Rep. 6 2001 27 36
    • (2001) Redox Rep. , vol.6 , pp. 27-36
    • Kobayashi, T.1    Tsunawaki, S.2    Seguchi, H.3
  • 45
    • 0141853754 scopus 로고    scopus 로고
    • Production of hydrogen peroxide by peripheral blood monocytes and specific macrophages during experimental infection with Trypanosoma cruzi in vivo
    • Melo RCN, D.L. Fabrino, H. D'Avila, H.C. Teixeira, and A.P. Ferreira Production of hydrogen peroxide by peripheral blood monocytes and specific macrophages during experimental infection with Trypanosoma cruzi in vivo Cell Biol. Int. 27 2003 853 861
    • (2003) Cell Biol. Int. , vol.27 , pp. 853-861
    • Rcn, M.1    Fabrino, D.L.2    D'Avila, H.3    Teixeira, H.C.4    Ferreira, A.P.5
  • 46
    • 0029999693 scopus 로고    scopus 로고
    • Inhibition of IκB-α phosphorylation and degradation and subsequent NF-κB activation by glutathione peroxidase overexpression
    • C. Kretz-Remy, P. Mehlen, M.-E. Mirault, and A.-P. Arrigo Inhibition of IκB-α phosphorylation and degradation and subsequent NF-κB activation by glutathione peroxidase overexpression J. Cell Biol. 133 1996 1083 1093
    • (1996) J. Cell Biol. , vol.133 , pp. 1083-1093
    • Kretz-Remy, C.1    Mehlen, P.2    Mirault, M.-E.3    Arrigo, A.-P.4
  • 47
    • 0029170274 scopus 로고
    • The roles of hydrogen peroxide and superoxide as messengers in the activation of transcription factor NFκB
    • K.N. Schmidt, P. Amstad, P. Cerutti, and P.A. Baeuerle The roles of hydrogen peroxide and superoxide as messengers in the activation of transcription factor NFκB Chem. Biol. 2 1995 13 22
    • (1995) Chem. Biol. , vol.2 , pp. 13-22
    • Schmidt, K.N.1    Amstad, P.2    Cerutti, P.3    Baeuerle, P.A.4
  • 48
    • 0037114155 scopus 로고    scopus 로고
    • Hydrogen peroxide induces murine macrophage chemokine gene transcription via extracellular signal-regulated kinase- and cyclic adenosine 5′- monophosphate (cAMP)-dependent pathways: Involvement of NF-κB, activator protein 1, and cAMP response element binding protein
    • M. Jaramillo, and M. Olivier Hydrogen peroxide induces murine macrophage chemokine gene transcription via extracellular signal-regulated kinase- and cyclic adenosine 5′- monophosphate (cAMP)-dependent pathways: involvement of NF-κB, activator protein 1, and cAMP response element binding protein J. Immunol. 169 2002 7026 7038
    • (2002) J. Immunol. , vol.169 , pp. 7026-7038
    • Jaramillo, M.1    Olivier, M.2
  • 49
    • 0037443421 scopus 로고    scopus 로고
    • Cu/Zn superoxide dismutase plays important role in immune response
    • M. Marikovsky, V. Ziv, N. Nevo, C. Harris-Cerruti, and O. Mahler Cu/Zn superoxide dismutase plays important role in immune response J. Immunol. 170 2003 2993 3001
    • (2003) J. Immunol. , vol.170 , pp. 2993-3001
    • Marikovsky, M.1    Ziv, V.2    Nevo, N.3    Harris-Cerruti, C.4    Mahler, O.5


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