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Volumn 32, Issue 5, 2010, Pages 305-313

Peroxiredoxin: A central player in immune modulation

Author keywords

Helminth; Immunomodulation; Macrophage; Peroxiredoxin

Indexed keywords

GLUTATHIONE PEROXIDASE; HYDROGEN PEROXIDE; INTERLEUKIN 10; INTERLEUKIN 13; INTERLEUKIN 4; PEROXIREDOXIN; PEROXIREDOXIN 1; PEROXIREDOXIN 2; PEROXIREDOXIN 4; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE; THIOREDOXIN PEROXIDASE;

EID: 77950673750     PISSN: 01419838     EISSN: 13653024     Source Type: Journal    
DOI: 10.1111/j.1365-3024.2010.01201.x     Document Type: Review
Times cited : (95)

References (75)
  • 1
    • 0342939339 scopus 로고
    • Peroxide metabolism in the liver fluke
    • Barrett J. Peroxide metabolism in the liver fluke. J Parasitol 1980 66 : 697.
    • (1980) J Parasitol , vol.66 , pp. 697
    • Barrett, J.1
  • 2
    • 0023741521 scopus 로고
    • Helminth anti-oxidant enzymes - A protective mechanism against host oxidants
    • Callahan HL, Crouch RK James ER. Helminth anti-oxidant enzymes - a protective mechanism against host oxidants. Parasitol Today 1988 4 : 218 225.
    • (1988) Parasitol Today , vol.4 , pp. 218-225
    • Callahan, H.L.1    Crouch, R.K.2    James, E.R.3
  • 3
    • 0023718663 scopus 로고
    • Antioxidant systems in Schistosoma mansoni: Correlation between susceptibility to oxidant killing and the levels of scavengers of hydrogen peroxide and oxygen free radicals
    • Mkoji GM, Smith JM Prichard RK. Antioxidant systems in Schistosoma mansoni: correlation between susceptibility to oxidant killing and the levels of scavengers of hydrogen peroxide and oxygen free radicals. Int J Parasitol 1988 18 : 661 666.
    • (1988) Int J Parasitol , vol.18 , pp. 661-666
    • Mkoji, G.M.1    Smith, J.M.2    Prichard, R.K.3
  • 4
    • 0031148701 scopus 로고    scopus 로고
    • Schistosoma mansoni: The developmental regulation and immunolocalization of antioxidant enzymes
    • Mei H LoVerde PT. Schistosoma mansoni: the developmental regulation and immunolocalization of antioxidant enzymes. Exp Parasitol 1997 86 : 69 78.
    • (1997) Exp Parasitol , vol.86 , pp. 69-78
    • Mei, H.1    Loverde, P.T.2
  • 6
    • 0030742427 scopus 로고    scopus 로고
    • Cloning of peroxiredoxin, a novel antioxidant enzyme, from the helminth parasite Fasciola hepatica
    • McGonigle S, Curley GP Dalton JP. Cloning of peroxiredoxin, a novel antioxidant enzyme, from the helminth parasite Fasciola hepatica. Parasitology 1997 115 : 101 104.
    • (1997) Parasitology , vol.115 , pp. 101-104
    • McGonigle, S.1    Curley, G.P.2    Dalton, J.P.3
  • 7
    • 0029146377 scopus 로고
    • Isolation of Fasciola hepatica haemoglobin
    • McGonigle S Dalton JP. Isolation of Fasciola hepatica haemoglobin. Parasitology 1995 111 : 209 215.
    • (1995) Parasitology , vol.111 , pp. 209-215
    • McGonigle, S.1    Dalton, J.P.2
  • 9
    • 0032103063 scopus 로고    scopus 로고
    • Molecular cloning of an enzymatically active thioredoxin peroxidase from Onchocerca volvulus
    • Chandrashekar R, Curtis KC, Lu W Weil GJ. Molecular cloning of an enzymatically active thioredoxin peroxidase from Onchocerca volvulus. Mol Biochem Parasitol 1998 93 : 309 312.
    • (1998) Mol Biochem Parasitol , vol.93 , pp. 309-312
    • Chandrashekar, R.1    Curtis, K.C.2    Lu, W.3    Weil, G.J.4
  • 10
    • 0031435939 scopus 로고    scopus 로고
    • Molecular cloning, expression and enzymatic activity of a thioredoxin peroxidase from Dirofilaria immitis
    • Klimowski L, Chandrashekar R Tripp CA. Molecular cloning, expression and enzymatic activity of a thioredoxin peroxidase from Dirofilaria immitis. Mol Biochem Parasitol 1997 90 : 297 306.
    • (1997) Mol Biochem Parasitol , vol.90 , pp. 297-306
    • Klimowski, L.1    Chandrashekar, R.2    Tripp, C.A.3
  • 11
    • 39149108128 scopus 로고    scopus 로고
    • Thioredoxin peroxidase from Echinococcus granulosus: A candidate to extend the antigenic panel for the immunodiagnosis of human cystic echinococcosis
    • Margutti P, Ortona E, Delunardo F, et al. Thioredoxin peroxidase from Echinococcus granulosus: a candidate to extend the antigenic panel for the immunodiagnosis of human cystic echinococcosis. Diagn Microbiol Infect Dis 2008 60 : 279 285.
    • (2008) Diagn Microbiol Infect Dis , vol.60 , pp. 279-285
    • Margutti, P.1    Ortona, E.2    Delunardo, F.3
  • 12
    • 0029019144 scopus 로고
    • Brugia malayi: Differential susceptibility to and metabolism of hydrogen peroxide in adults and microfilariae
    • Ou X, Thomas GR, Chacón MR, Tang L Selkirk ME. Brugia malayi: differential susceptibility to and metabolism of hydrogen peroxide in adults and microfilariae. Exp Parasitol 1995 80 : 530 540.
    • (1995) Exp Parasitol , vol.80 , pp. 530-540
    • Ou, X.1    Thomas, G.R.2    Chacón, M.R.3    Tang, L.4    Selkirk, M.E.5
  • 14
    • 0029989092 scopus 로고    scopus 로고
    • Genes expressed in Brugia malayi infective third stage larvae
    • Blaxter ML, Raghavan N, Ghosh I, et al. Genes expressed in Brugia malayi infective third stage larvae. Mol Biochem Parasitol 1996 77 : 77 93.
    • (1996) Mol Biochem Parasitol , vol.77 , pp. 77-93
    • Blaxter, M.L.1    Raghavan, N.2    Ghosh, I.3
  • 15
    • 0032521486 scopus 로고    scopus 로고
    • Thioredoxin peroxidase from Onchocerca volvulus: A major hydrogen peroxide detoxifying enzyme in filarial parasites
    • Lu W, Egerton GL, Bianco AE Williams SA. Thioredoxin peroxidase from Onchocerca volvulus: a major hydrogen peroxide detoxifying enzyme in filarial parasites. Mol Biochem Parasitol 1998 91 : 221 235.
    • (1998) Mol Biochem Parasitol , vol.91 , pp. 221-235
    • Lu, W.1    Egerton, G.L.2    Bianco, A.E.3    Williams, S.A.4
  • 16
    • 68649087906 scopus 로고    scopus 로고
    • An integrated transcriptomics and proteomics analysis of the secretome of the helminth pathogen Fasciola hepatica: Proteins associated with invasion and infection of the mammalian host
    • Robinson MW, Menon R, Donnelly SM, Dalton JP Ranganathan S. An integrated transcriptomics and proteomics analysis of the secretome of the helminth pathogen Fasciola hepatica: proteins associated with invasion and infection of the mammalian host. Mol Cell Proteomics 2009 8 : 1891 1907.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 1891-1907
    • Robinson, M.W.1    Menon, R.2    Donnelly, S.M.3    Dalton, J.P.4    Ranganathan, S.5
  • 17
    • 33745195480 scopus 로고    scopus 로고
    • Redox balance mechanisms in Schistosoma mansoni rely on peroxiredoxins and albumin and implicate peroxiredoxins as novel drug targets
    • Sayed AA, Cook SK Williams DL. Redox balance mechanisms in Schistosoma mansoni rely on peroxiredoxins and albumin and implicate peroxiredoxins as novel drug targets. J Biol Chem 2006 281 : 17001 17010.
    • (2006) J Biol Chem , vol.281 , pp. 17001-17010
    • Sayed, A.A.1    Cook, S.K.2    Williams, D.L.3
  • 18
    • 58549104705 scopus 로고    scopus 로고
    • Peroxiredoxin-1 from Schistosoma japonicum functions as a scavenger against hydrogen peroxide but not nitric oxide
    • Kumagai T, Osada Y, Ohta N Kanazawa T. Peroxiredoxin-1 from Schistosoma japonicum functions as a scavenger against hydrogen peroxide but not nitric oxide. Mol Biochem Parasitol 2009 164 : 26 31.
    • (2009) Mol Biochem Parasitol , vol.164 , pp. 26-31
    • Kumagai, T.1    Osada, Y.2    Ohta, N.3    Kanazawa, T.4
  • 20
    • 15444362698 scopus 로고    scopus 로고
    • Crystal structure of the tryparedoxin peroxidase from the human parasite Trypanosoma cruzi
    • Piñeyro MD, Pizarro JC, Lema F, et al. Crystal structure of the tryparedoxin peroxidase from the human parasite Trypanosoma cruzi. J Struct Biol 2005 150 : 11 22.
    • (2005) J Struct Biol , vol.150 , pp. 11-22
    • Piñeyro, M.D.1    Pizarro, J.C.2    Lema, F.3
  • 22
    • 70349619224 scopus 로고    scopus 로고
    • Something old, something new, something borrowed; How the thermoacidophilic archaeon Sulfolobus solfataricus responds to oxidative stress
    • Maaty WS, Wiedenheft B, Tarlykov P, et al. Something old, something new, something borrowed; how the thermoacidophilic archaeon Sulfolobus solfataricus responds to oxidative stress. PLoS ONE 2009 4 (9 e6964.
    • (2009) PLoS ONE , vol.4 , Issue.9 , pp. 6964
    • Maaty, W.S.1    Wiedenheft, B.2    Tarlykov, P.3
  • 23
    • 68149100376 scopus 로고    scopus 로고
    • Insights into the catalytic mechanism of the Bcp family: Functional and structural analysis of Bcp1 from Sulfolobus solfataricus
    • D'Ambrosio K, Limauro D, Pedone E, et al. Insights into the catalytic mechanism of the Bcp family: functional and structural analysis of Bcp1 from Sulfolobus solfataricus. Proteins 2009 76 : 995 1006.
    • (2009) Proteins , vol.76 , pp. 995-1006
    • D'Ambrosio, K.1    Limauro, D.2    Pedone, E.3
  • 24
    • 33748787143 scopus 로고    scopus 로고
    • 2-Cys peroxiredoxins from Schistosoma japonicum: The expression profile and localization in the life cycle
    • Kumagai T, Osada Y Kanazawa T. 2-Cys peroxiredoxins from Schistosoma japonicum: the expression profile and localization in the life cycle. Mol Biochem Parasitol 2006 149 : 135 143.
    • (2006) Mol Biochem Parasitol , vol.149 , pp. 135-143
    • Kumagai, T.1    Osada, Y.2    Kanazawa, T.3
  • 25
    • 50049110849 scopus 로고    scopus 로고
    • Characterization of the antioxidant enzyme, thioredoxin peroxidase, from the carcinogenic human liver fluke, Opisthorchis viverrini
    • Suttiprapa S, Loukas A, Laha T, et al. Characterization of the antioxidant enzyme, thioredoxin peroxidase, from the carcinogenic human liver fluke, Opisthorchis viverrini. Mol Biochem Parasitol 2008 160 : 116 122.
    • (2008) Mol Biochem Parasitol , vol.160 , pp. 116-122
    • Suttiprapa, S.1    Loukas, A.2    Laha, T.3
  • 26
    • 34547775859 scopus 로고    scopus 로고
    • Proteomic analysis of Schistosoma mansoni egg secretions
    • Cass CL, Johnson JR, Califf LL, et al. Proteomic analysis of Schistosoma mansoni egg secretions. Mol Biochem Parasitol 2007 155 : 84 93.
    • (2007) Mol Biochem Parasitol , vol.155 , pp. 84-93
    • Cass, C.L.1    Johnson, J.R.2    Califf, L.L.3
  • 27
    • 48149106910 scopus 로고    scopus 로고
    • Excretory-secretory products of larval Fasciola hepatica investigated using a two-dimensional proteomic approach
    • Gourbal BE, Guillou F, Mitta G, et al. Excretory-secretory products of larval Fasciola hepatica investigated using a two-dimensional proteomic approach. Mol Biochem Parasitol 2008 161 : 63 66.
    • (2008) Mol Biochem Parasitol , vol.161 , pp. 63-66
    • Gourbal, B.E.1    Guillou, F.2    Mitta, G.3
  • 28
    • 58549116678 scopus 로고    scopus 로고
    • Proteomic analysis of Schistosoma mansoni proteins released during in vitro miracidium-to-sporocyst transformation
    • Wu XJ, Sabat G, Brown JF, et al. Proteomic analysis of Schistosoma mansoni proteins released during in vitro miracidium-to-sporocyst transformation. Mol Biochem Parasitol 2008 164 : 32 44.
    • (2008) Mol Biochem Parasitol , vol.164 , pp. 32-44
    • Wu, X.J.1    Sabat, G.2    Brown, J.F.3
  • 29
    • 67650517491 scopus 로고    scopus 로고
    • Excretory/secretory proteome of the adult developmental stage of human blood fluke, Schistosoma japonicum
    • Liu F, Cui SJ, Hu W, Feng Z, Wang ZQ Han ZG. Excretory/secretory proteome of the adult developmental stage of human blood fluke, Schistosoma japonicum. Mol Cell Proteomics 2009 8 : 1236 1251.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 1236-1251
    • Liu, F.1    Cui, S.J.2    Hu, W.3    Feng, Z.4    Wang, Z.Q.5    Han, Z.G.6
  • 30
    • 0033622036 scopus 로고    scopus 로고
    • Removal of hydrogen peroxide by a 1-cysteine peroxiredoxin enzyme of the filarial parasite Dirofilaria immitis
    • Chandrashekar R, Tsuji N, Morales TH, et al. Removal of hydrogen peroxide by a 1-cysteine peroxiredoxin enzyme of the filarial parasite Dirofilaria immitis. Parasitol Res 2000 86 : 200 206.
    • (2000) Parasitol Res , vol.86 , pp. 200-206
    • Chandrashekar, R.1    Tsuji, N.2    Morales, T.H.3
  • 31
    • 43749120513 scopus 로고    scopus 로고
    • The secretome of the filarial parasite, Brugia malayi: Proteomic profile of adult excretory-secretory products
    • Hewitson JP, Harcus YM, Curwen RS, et al. The secretome of the filarial parasite, Brugia malayi: proteomic profile of adult excretory-secretory products. Mol Biochem Parasitol 2008 160 : 8 21.
    • (2008) Mol Biochem Parasitol , vol.160 , pp. 8-21
    • Hewitson, J.P.1    Harcus, Y.M.2    Curwen, R.S.3
  • 32
    • 56249104176 scopus 로고    scopus 로고
    • Stage- and gender-specific proteomic analysis of Brugia malayi excretory-secretory products
    • Moreno Y Geary TG. Stage- and gender-specific proteomic analysis of Brugia malayi excretory-secretory products. PLoS Negl Trop Dis 2008 2 : e326.
    • (2008) PLoS Negl Trop Dis , vol.2 , pp. 326
    • Moreno, Y.1    Geary, T.G.2
  • 33
    • 65549088510 scopus 로고    scopus 로고
    • Brugia malayi excreted/secreted proteins at the host/parasite interface: Stage- and gender-specific proteomic profiling
    • Bennuru S, Semnani R, Meng Z, Ribeiro JM, Veenstra TD Nutman TB. Brugia malayi excreted/secreted proteins at the host/parasite interface: stage- and gender-specific proteomic profiling. PLoS Negl Trop Dis 2009 3 : e410.
    • (2009) PLoS Negl Trop Dis , vol.3 , pp. 410
    • Bennuru, S.1    Semnani, R.2    Meng, Z.3    Ribeiro, J.M.4    Veenstra, T.D.5    Nutman, T.B.6
  • 34
    • 0027530060 scopus 로고
    • Identification of a natural killer enhancing factor (NKEF) from human erythroid cells
    • Shau H, Gupta RK Golub SH. Identification of a natural killer enhancing factor (NKEF) from human erythroid cells. Cell Immunol 1993 147 : 1 11.
    • (1993) Cell Immunol , vol.147 , pp. 1-11
    • Shau, H.1    Gupta, R.K.2    Golub, S.H.3
  • 35
    • 0032999579 scopus 로고    scopus 로고
    • Cloning of the peroxiredoxin gene family in rats and characterization of the fourth member
    • Matsumoto A, Okado A, Fujii T, et al. Cloning of the peroxiredoxin gene family in rats and characterization of the fourth member. FEBS Lett 1999 443 : 246 250.
    • (1999) FEBS Lett , vol.443 , pp. 246-250
    • Matsumoto, A.1    Okado, A.2    Fujii, T.3
  • 36
    • 0032113082 scopus 로고    scopus 로고
    • TRANK, a novel cytokine that activates NF-kappa B and c-Jun N-terminal kinase
    • Haridas V, Ni J, Meager A, et al. TRANK, a novel cytokine that activates NF-kappa B and c-Jun N-terminal kinase. J Immunol 1998 161 : 1 6.
    • (1998) J Immunol , vol.161 , pp. 1-6
    • Haridas, V.1    Ni, J.2    Meager, A.3
  • 37
    • 0034073166 scopus 로고    scopus 로고
    • Peroxiredoxin IV is a secretable protein with heparin-binding properties under reduced conditions
    • Okado-Matsumoto A, Matsumoto A, Fujii J Taniguchi N. Peroxiredoxin IV is a secretable protein with heparin-binding properties under reduced conditions. J Biochem 2000 127 : 493 501.
    • (2000) J Biochem , vol.127 , pp. 493-501
    • Okado-Matsumoto, A.1    Matsumoto, A.2    Fujii, J.3    Taniguchi, N.4
  • 38
    • 56749174940 scopus 로고    scopus 로고
    • Exploring the full spectrum of macrophage activation
    • Mosser DM Edwards JP. Exploring the full spectrum of macrophage activation. Nat Rev Immunol 2008 8 : 958 969.
    • (2008) Nat Rev Immunol , vol.8 , pp. 958-969
    • Mosser, D.M.1    Edwards, J.P.2
  • 39
    • 33748087483 scopus 로고    scopus 로고
    • Innate immune responses to lung-stage helminth infection induce alternatively activated alveolar macrophages
    • Reece JJ, Siracusa MC Scott AL. Innate immune responses to lung-stage helminth infection induce alternatively activated alveolar macrophages. Infect Immun 2006 74 : 4970 4981.
    • (2006) Infect Immun , vol.74 , pp. 4970-4981
    • Reece, J.J.1    Siracusa, M.C.2    Scott, A.L.3
  • 40
    • 11144316758 scopus 로고    scopus 로고
    • Thioredoxin peroxidase secreted by Fasciola hepatica induces the alternative activation of macrophages
    • Donnelly S, O'Neill SM, Sekiya M, Mulcahy G Dalton JP. Thioredoxin peroxidase secreted by Fasciola hepatica induces the alternative activation of macrophages. Infect Immun 2005 73 : 166 173.
    • (2005) Infect Immun , vol.73 , pp. 166-173
    • Donnelly, S.1    O'Neill, S.M.2    Sekiya, M.3    Mulcahy, G.4    Dalton, J.P.5
  • 42
    • 11144286421 scopus 로고    scopus 로고
    • Chitinase and Fizz family members are a generalized feature of nematode infection with selective upregulation of Ym1 and Fizz1 by antigen-presenting cells
    • Nair MG, Gallagher IJ, Taylor MD, et al. Chitinase and Fizz family members are a generalized feature of nematode infection with selective upregulation of Ym1 and Fizz1 by antigen-presenting cells. Infect Immun 2005 73 : 385 394.
    • (2005) Infect Immun , vol.73 , pp. 385-394
    • Nair, M.G.1    Gallagher, I.J.2    Taylor, M.D.3
  • 43
    • 68149125252 scopus 로고    scopus 로고
    • Infection with a helminth parasite attenuates autoimmunity through TGF-beta-mediated suppression of Th17 and Th1 responses
    • Walsh KP, Brady MT, Finlay CM, Boon L Mills KH. Infection with a helminth parasite attenuates autoimmunity through TGF-beta-mediated suppression of Th17 and Th1 responses. J Immunol 2009 183 : 1577 1586.
    • (2009) J Immunol , vol.183 , pp. 1577-1586
    • Walsh, K.P.1    Brady, M.T.2    Finlay, C.M.3    Boon, L.4    Mills, K.H.5
  • 44
    • 0032741370 scopus 로고    scopus 로고
    • Kupffer cells from Schistosoma mansoni-infected mice participate in the prompt type 2 differentiation of hepatic T cells in response to worm antigens
    • Hayashi N, Matsui K, Tsutsui H, et al. Kupffer cells from Schistosoma mansoni-infected mice participate in the prompt type 2 differentiation of hepatic T cells in response to worm antigens. J Immunol 1999 163 : 6702 6711.
    • (1999) J Immunol , vol.163 , pp. 6702-6711
    • Hayashi, N.1    Matsui, K.2    Tsutsui, H.3
  • 45
    • 0033993917 scopus 로고    scopus 로고
    • Antigen-presenting cells recruited by Brugia malayi induce Th2 differentiation of naïve CD4(+) T cells
    • Loke P, MacDonald AS Allen JE. Antigen-presenting cells recruited by Brugia malayi induce Th2 differentiation of naïve CD4(+) T cells. Eur J Immunol 2000 30 : 1127 1135.
    • (2000) Eur J Immunol , vol.30 , pp. 1127-1135
    • Loke, P.1    MacDonald, A.S.2    Allen, J.E.3
  • 47
    • 0033825617 scopus 로고    scopus 로고
    • Alternatively activated macrophages induced by nematode infection inhibit proliferation via cell-to-cell contact
    • Loke P, MacDonald AS, Robb A, Maizels RM Allen JE. Alternatively activated macrophages induced by nematode infection inhibit proliferation via cell-to-cell contact. Eur J Immunol 2000 30 : 2669 2678.
    • (2000) Eur J Immunol , vol.30 , pp. 2669-2678
    • Loke, P.1    MacDonald, A.S.2    Robb, A.3    Maizels, R.M.4    Allen, J.E.5
  • 48
    • 40949097683 scopus 로고    scopus 로고
    • Regulatory conversation between antigen presenting cells and regulatory T cells enhance immune suppression
    • Mahnke K, Bedke T Enk AH. Regulatory conversation between antigen presenting cells and regulatory T cells enhance immune suppression. Cell Immunol 2007 250 : 1 13.
    • (2007) Cell Immunol , vol.250 , pp. 1-13
    • Mahnke, K.1    Bedke, T.2    Enk, A.H.3
  • 49
    • 55549093092 scopus 로고    scopus 로고
    • Helminth 2-Cys peroxiredoxin drives Th2 responses through a mechanism involving alternatively activated macrophages
    • Donnelly S, Stack CM, O'Neill SM, Sayed AA, Williams DL Dalton JP. Helminth 2-Cys peroxiredoxin drives Th2 responses through a mechanism involving alternatively activated macrophages. FASEB J 2008 22 : 4022 4032.
    • (2008) FASEB J , vol.22 , pp. 4022-4032
    • Donnelly, S.1    Stack, C.M.2    O'Neill, S.M.3    Sayed, A.A.4    Williams, D.L.5    Dalton, J.P.6
  • 50
    • 33646753396 scopus 로고    scopus 로고
    • Simvastatin promotes Th2-type responses through the induction of the chitinase family member Ym1 in dendritic cells
    • Arora M, Chen L, Paglia M, et al. Simvastatin promotes Th2-type responses through the induction of the chitinase family member Ym1 in dendritic cells. Proc Natl Acad Sci USA 2006 103 : 7777 7782.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7777-7782
    • Arora, M.1    Chen, L.2    Paglia, M.3
  • 51
    • 0037044804 scopus 로고    scopus 로고
    • Pag, a putative tumor suppressor, interacts with the Myc Box II domain of c-Myc and selectively alters its biological function and target gene expression
    • Mu ZM, Yin XY Prochownik EV. Pag, a putative tumor suppressor, interacts with the Myc Box II domain of c-Myc and selectively alters its biological function and target gene expression. J Biol Chem 2002 277 : 43175 43184.
    • (2002) J Biol Chem , vol.277 , pp. 43175-43184
    • Mu, Z.M.1    Yin, X.Y.2    Prochownik, E.V.3
  • 52
    • 0030803669 scopus 로고    scopus 로고
    • The PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity
    • Wen ST Van Etten RA. The PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity. Genes Dev 1997 11 : 2456 2467.
    • (1997) Genes Dev , vol.11 , pp. 2456-2467
    • Wen, S.T.1    Van Etten, R.A.2
  • 54
    • 35148890754 scopus 로고    scopus 로고
    • Peroxiredoxin 1 interacts with androgen receptor and enhances its transactivation
    • Park SY, Yu X, Ip C, Mohler JL, Bogner PN Park YM. Peroxiredoxin 1 interacts with androgen receptor and enhances its transactivation. Cancer Res 2007 6 : 9294 9303.
    • (2007) Cancer Res , vol.6 , pp. 9294-9303
    • Park, S.Y.1    Yu, X.2    Ip, C.3    Mohler, J.L.4    Bogner, P.N.5    Park, Y.M.6
  • 55
    • 47049097081 scopus 로고    scopus 로고
    • Mast cell-mediated immune responses through IgE antibody and Toll-like receptor 4 by malarial peroxiredoxin
    • Furuta T, Imajo-Ohmi S, Fukuda H, Kano S, Miyake K Watanabe N. Mast cell-mediated immune responses through IgE antibody and Toll-like receptor 4 by malarial peroxiredoxin. Eur J Immunol 2008 38 : 1341 1350.
    • (2008) Eur J Immunol , vol.38 , pp. 1341-1350
    • Furuta, T.1    Imajo-Ohmi, S.2    Fukuda, H.3    Kano, S.4    Miyake, K.5    Watanabe, N.6
  • 56
    • 4844229387 scopus 로고    scopus 로고
    • Helminth parasites-masters of regulation
    • Maizels RM. Helminth parasites-masters of regulation. Immunol Rev 2004 201 : 89 116.
    • (2004) Immunol Rev , vol.201 , pp. 89-116
    • Maizels, R.M.1
  • 57
    • 0026060650 scopus 로고
    • Downregulation of Th1 cytokine production accompanies induction of Th2 responses by a parasite helminth, Schistosoma mansoni
    • Pearce EJ, Caspar P, Grzych JM, Lewis FA Sher A. Downregulation of Th1 cytokine production accompanies induction of Th2 responses by a parasite helminth, Schistosoma mansoni. J Exp Med 1991 173 : 159 166.
    • (1991) J Exp Med , vol.173 , pp. 159-166
    • Pearce, E.J.1    Caspar, P.2    Grzych, J.M.3    Lewis, F.A.4    Sher, A.5
  • 58
    • 25144448562 scopus 로고    scopus 로고
    • Priming of the immune response by schistosome eggs
    • DOI 10.1111/j.1365-3024.2005.00765.x
    • Pearce EJ. Priming of the immune response by schistosome eggs. Parasite Immunol 2005 27 : 265 270. (Pubitemid 41344618)
    • (2005) Parasite Immunology , vol.27 , Issue.7-8 , pp. 265-270
    • Pearce, E.J.1
  • 59
    • 4043140752 scopus 로고    scopus 로고
    • Parasite-induced Th2 polarization is associated with down-regulated dendritic cell responsiveness to Th1 stimuli and a transient delay in T lymphocyte cycling
    • Jankovic D, Kullberg MC, Caspar P Sher A. Parasite induced Th2 polarization is associated with down-regulated dendritic cell responsiveness to Th1 stimuli and a transient delay in T lymphocyte cycling. J Immunol 2004 173 : 2419 2427. (Pubitemid 39063098)
    • (2004) Journal of Immunology , vol.173 , Issue.4 , pp. 2419-2427
    • Jankovic, D.1    Kullberg, M.C.2    Caspar, P.3    Sher, A.4
  • 60
    • 68149163162 scopus 로고    scopus 로고
    • The major component in schistosome eggs responsible for conditioning dendritic cells for Th2 polarization is a T2 ribonuclease (omega-1)
    • Steinfelder S, Andersen JF, Cannons JL, et al. The major component in schistosome eggs responsible for conditioning dendritic cells for Th2 polarization is a T2 ribonuclease (omega-1). J Exp Med 2009 206 : 1681 1690.
    • (2009) J Exp Med , vol.206 , pp. 1681-1690
    • Steinfelder, S.1    Andersen, J.F.2    Cannons, J.L.3
  • 61
    • 68149156007 scopus 로고    scopus 로고
    • Omega-1, a glycoprotein secreted by Schistosoma mansoni eggs, drives Th2 responses
    • Everts B, Perona-Wright G, Smits HH, et al. Omega-1, a glycoprotein secreted by Schistosoma mansoni eggs, drives Th2 responses. J Exp Med 2009 206 : 1673 1680.
    • (2009) J Exp Med , vol.206 , pp. 1673-1680
    • Everts, B.1    Perona-Wright, G.2    Smits, H.H.3
  • 62
    • 0035144556 scopus 로고    scopus 로고
    • + T helper cell and B-cell responses against a novel egg antigen, thioredoxin peroxidase
    • DOI 10.1128/IAI.69.2.1134-1141.2001
    • Williams DL, Asahi H, Botkin DJ Stadecker MJ. Schistosome infection stimulates host CD4(+) T helper cell and B-cell responses against a novel egg antigen, thioredoxin peroxidase. Infect Immun 2001 69 : 1134 1141. (Pubitemid 32109582)
    • (2001) Infection and Immunity , vol.69 , Issue.2 , pp. 1134-1141
    • Williams, D.L.1    Asahi, H.2    Botkin, D.J.3    Stadecker, M.J.4
  • 63
    • 0025996014 scopus 로고
    • Reconstitution of Ca (2+)-dependent K+ transport in erythrocyte membrane vesicles requires a cytoplasmic protein
    • Moore RB, Mankad MV, Shriver SK, Mankad VN Plishker GA. Reconstitution of Ca (2+)-dependent K+ transport in erythrocyte membrane vesicles requires a cytoplasmic protein. J Biol Chem 1991 266 : 18964 18968.
    • (1991) J Biol Chem , vol.266 , pp. 18964-18968
    • Moore, R.B.1    Mankad, M.V.2    Shriver, S.K.3    Mankad, V.N.4    Plishker, G.A.5
  • 64
    • 19244367952 scopus 로고    scopus 로고
    • The role of erythrocyte peroxiredoxin in detoxifying peroxides and in stimulating potassium efflux via the Gardos channels [4] (multiple letters)
    • DOI 10.1182/blood-2002-12-3682
    • Schröder E, Jönsson T Poole L. The role of erythrocyte peroxiredoxin in detoxifying peroxides and in stimulating potassium efflux via the Gardos channels. Blood 2003 101 : 2897 2898. (Pubitemid 36857662)
    • (2003) Blood , vol.101 , Issue.7 , pp. 2897-2898
    • Schroder, E.1    Jonsson, T.2    Poole, L.3    Johnson, R.M.4
  • 65
    • 34347209116 scopus 로고    scopus 로고
    • Autoantibody against peroxiredoxin I, an antioxidant enzyme, in patients with systemic sclerosis: Possible association with oxidative stress
    • DOI 10.1093/rheumatology/kem010
    • Iwata Y, Ogawa F, Komura K, et al. Autoantibody against peroxiredoxin I, an antioxidant enzyme, in patients with systemic sclerosis: possible association with oxidative stress. Rheumatology 2007 46 : 790 795. (Pubitemid 47061709)
    • (2007) Rheumatology , vol.46 , Issue.5 , pp. 790-795
    • Iwata, Y.1    Ogawa, F.2    Komura, K.3    Muroi, E.4    Hara, T.5    Shimizu, K.6    Hasegawa, M.7    Fujimoto, M.8    Tomita, Y.9    Sato, S.10
  • 66
    • 19444376126 scopus 로고    scopus 로고
    • Peroxiredoxin-I is an autoimmunogenic tumor antigen in non-small cell lung cancer
    • Chang JW, Lee SH, Jeong JY, et al. Peroxiredoxin-I is an autoimmunogenic tumor antigen in non-small cell lung cancer. FEBS Lett 2005 579 : 2873 2878.
    • (2005) FEBS Lett , vol.579 , pp. 2873-2878
    • Chang, J.W.1    Lee, S.H.2    Jeong, J.Y.3
  • 67
    • 42149099408 scopus 로고    scopus 로고
    • Plasticity of macrophage function during tumor progression: Regulation by distinct molecular mechanisms
    • Biswas SK, Sica A Lewis CE. Plasticity of macrophage function during tumor progression: regulation by distinct molecular mechanisms. J Immunol 2008 180 : 2011 2017.
    • (2008) J Immunol , vol.180 , pp. 2011-2017
    • Biswas, S.K.1    Sica, A.2    Lewis, C.E.3
  • 68
    • 1842290928 scopus 로고    scopus 로고
    • Differences in angiogenic potential of classically vs alternatively activated macrophages
    • Kodelja V, Müller C, Tenorio S, Schebesch C, Orfanos CE Goerdt S. Differences in angiogenic potential of classically vs alternatively activated macrophages. Immunobiology 1997 197 : 478 493. (Pubitemid 27489996)
    • (1997) Immunobiology , vol.197 , Issue.5 , pp. 478-493
    • Kodelja, V.1    Muller, C.2    Tenorio, S.3    Schebesch, C.4    Orfanos, C.E.5    Goerdt, S.6
  • 69
    • 57149108312 scopus 로고    scopus 로고
    • Identification and characterization of infiltrating macrophages in acetaminophen-induced liver injury
    • DOI 10.1189/jlb.0308173
    • Holt MP, Cheng L Ju C. Identification and characterization of infiltrating macrophages in acetaminophen-induced liver injury. J Leukoc Biol 2008 84 : 1410 1421. (Pubitemid 352774476)
    • (2008) Journal of Leukocyte Biology , vol.84 , Issue.6 , pp. 1410-1421
    • Holt, M.P.1    Cheng, L.2    Ju, C.3
  • 70
    • 2942627626 scopus 로고    scopus 로고
    • Hydrophobicity: An ancient damage-associated molecular pattern that initiates innate immune responses
    • Seong S Matzinger P. Hydrophobicity: an ancient damage-associated molecular pattern that initiates innate immune responses. Nat Rev Immunol 2004 4 : 469 478. (Pubitemid 38745558)
    • (2004) Nature Reviews Immunology , vol.4 , Issue.6 , pp. 469-478
    • Seong, S.-Y.1    Matzinger, P.2
  • 71
    • 33845951211 scopus 로고    scopus 로고
    • DAMPs, PAMPs and alarmins: All we need to know about danger
    • DOI 10.1189/jlb.0306164
    • Bianchi M. DAMPs, PAMPs and alarmins: all we need to know about danger. J Leukoc Biol 2007 81 : 1 5. (Pubitemid 46028489)
    • (2007) Journal of Leukocyte Biology , vol.81 , Issue.1 , pp. 1-5
    • Bianchi, M.E.1
  • 72
    • 34548857335 scopus 로고    scopus 로고
    • Inside, outside, upside down: Damage-associated molecular-pattern molecules (DAMPs) and redox
    • DOI 10.1016/j.it.2007.08.004, PII S1471490607002074
    • Rubartelli A Lotze M. Inside, outside, upside down: damage-associated molecular-pattern molecules (DAMPs) and redox. Trends Immunol 2007 28 : 429 436. (Pubitemid 47444554)
    • (2007) Trends in Immunology , vol.28 , Issue.10 , pp. 429-436
    • Rubartelli, A.1    Lotze, M.T.2
  • 73
    • 63449101111 scopus 로고    scopus 로고
    • Dangers in and out
    • Bianchi M Manfredi A. Dangers in and out. Science 2009 323 : 1683 1684.
    • (2009) Science , vol.323 , pp. 1683-1684
    • Bianchi, M.1    Manfredi, A.2
  • 75
    • 0028294049 scopus 로고
    • MEGA: Molecular evolutionary genetics analysis software for microcomputers
    • Kumar S, Tamura K Nei M. MEGA: Molecular Evolutionary Genetics Analysis software for microcomputers. Comput Appl Biosci 1994 10 : 189 191. (Pubitemid 24125441)
    • (1994) Computer Applications in the Biosciences , vol.10 , Issue.2 , pp. 189-191
    • Kumar, S.1    Tamura, K.2    Nei, M.3


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