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Volumn 33, Issue 1, 2012, Pages 121-129

Immunological role of thiol-dependent peroxiredoxin gene in Macrobrachium rosenbergii

Author keywords

DNA protection; Gene expression; Peroxiredoxin; Prawn; Virus

Indexed keywords

ESCHERICHIA COLI; INFECTIOUS HYPODERMAL AND HEMATOPOIETIC NECROSIS VIRUS; MACROBRACHIUM ROSENBERGII;

EID: 84861480701     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2012.04.010     Document Type: Article
Times cited : (41)

References (51)
  • 1
    • 19444375216 scopus 로고    scopus 로고
    • Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling
    • Rhee S.G., Chae H.Z., Kim K. Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radic Biol Med 2005, 38:1543-1552.
    • (2005) Free Radic Biol Med , vol.38 , pp. 1543-1552
    • Rhee, S.G.1    Chae, H.Z.2    Kim, K.3
  • 2
    • 36549021015 scopus 로고    scopus 로고
    • A peroxiredoxin from kuruma shrimp, Marsupenaeus japonicus, inhibited by peptidoglycan
    • Maningas M.B.B., Koyama T., Kondo H., Hirono I., Aoki T. A peroxiredoxin from kuruma shrimp, Marsupenaeus japonicus, inhibited by peptidoglycan. Dev Comp Immunol 2008, 32:198-203.
    • (2008) Dev Comp Immunol , vol.32 , pp. 198-203
    • Maningas, M.B.B.1    Koyama, T.2    Kondo, H.3    Hirono, I.4    Aoki, T.5
  • 3
    • 0028226006 scopus 로고
    • Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes
    • Chae H.Z., Robison K., Poole L.B., Church G., Storz G., Rhee S.G. Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Proc Natl Acad Sci U S A 1994, 91:7017-7021.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 7017-7021
    • Chae, H.Z.1    Robison, K.2    Poole, L.B.3    Church, G.4    Storz, G.5    Rhee, S.G.6
  • 4
    • 14644437730 scopus 로고    scopus 로고
    • Reactive oxygen species and development in microbial eukaryotes
    • Aguirre J., Momberg M.R., Hewitt D., Hansberg W. Reactive oxygen species and development in microbial eukaryotes. Trends Microbiol 2005, 13:111-118.
    • (2005) Trends Microbiol , vol.13 , pp. 111-118
    • Aguirre, J.1    Momberg, M.R.2    Hewitt, D.3    Hansberg, W.4
  • 5
    • 65649134322 scopus 로고    scopus 로고
    • Molecular cloning and characterization of peroxiredoxin 6 from Chinese mitten crab Eriocheir sinensis
    • Mu C., Zhao J., Wang L., Song L., Zhang H., Li C., et al. Molecular cloning and characterization of peroxiredoxin 6 from Chinese mitten crab Eriocheir sinensis. Fish Shellfish Immunol 2009, 26:821-827.
    • (2009) Fish Shellfish Immunol , vol.26 , pp. 821-827
    • Mu, C.1    Zhao, J.2    Wang, L.3    Song, L.4    Zhang, H.5    Li, C.6
  • 6
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy M.P. How mitochondria produce reactive oxygen species. Biochem J 2009, 417:1-13.
    • (2009) Biochem J , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 7
    • 0026636441 scopus 로고
    • Free radicals, antioxidants and human disease. Where are we now?
    • Halliwell B., Gutteridge J.M., Cross C.E. Free radicals, antioxidants and human disease. Where are we now?. J Lab Clin Med 1992, 119:598-620.
    • (1992) J Lab Clin Med , vol.119 , pp. 598-620
    • Halliwell, B.1    Gutteridge, J.M.2    Cross, C.E.3
  • 9
    • 0034648827 scopus 로고    scopus 로고
    • Peroxynitrite reductase activity of bacterial peroxiredoxins
    • Bryk R., Griffin P., Nathan C. Peroxynitrite reductase activity of bacterial peroxiredoxins. Nature 2000, 407:211-215.
    • (2000) Nature , vol.407 , pp. 211-215
    • Bryk, R.1    Griffin, P.2    Nathan, C.3
  • 11
    • 78650701797 scopus 로고    scopus 로고
    • Cloning, genomic structure, and expression analysis of peroxiredoxin V from bay scallop Argopecten irradians
    • Li J., Li L., Zhang S., Zhang G. Cloning, genomic structure, and expression analysis of peroxiredoxin V from bay scallop Argopecten irradians. Fish Shellfish Immunol 2011, 30:309-316.
    • (2011) Fish Shellfish Immunol , vol.30 , pp. 309-316
    • Li, J.1    Li, L.2    Zhang, S.3    Zhang, G.4
  • 13
    • 77952012285 scopus 로고    scopus 로고
    • Cloning and functional characterization of a typical 2-Cys peroxiredoxin from southern bluefin tuna (Thunnus maccoyii)
    • Sutton D.L., Loo G.H., Menz R.I., Schuller K.A. Cloning and functional characterization of a typical 2-Cys peroxiredoxin from southern bluefin tuna (Thunnus maccoyii). Comp Biochem Physiol B 2010, 156:97-106.
    • (2010) Comp Biochem Physiol B , vol.156 , pp. 97-106
    • Sutton, D.L.1    Loo, G.H.2    Menz, R.I.3    Schuller, K.A.4
  • 14
    • 0032741432 scopus 로고    scopus 로고
    • Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family
    • Knoops B., Clippe A., Bogard C., Arsalane K., Wattiez R., Hermans C., et al. Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family. J Biol Chem 1999, 274:30451-30458.
    • (1999) J Biol Chem , vol.274 , pp. 30451-30458
    • Knoops, B.1    Clippe, A.2    Bogard, C.3    Arsalane, K.4    Wattiez, R.5    Hermans, C.6
  • 15
    • 77950370157 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain involvement in peroxiredoxin 3 oxidation by phenethyl isothiocyanate and auranofin
    • Brown K.K., Cox A.G., Hampton M.B. Mitochondrial respiratory chain involvement in peroxiredoxin 3 oxidation by phenethyl isothiocyanate and auranofin. FEBS Lett 2010, 584:1257-1262.
    • (2010) FEBS Lett , vol.584 , pp. 1257-1262
    • Brown, K.K.1    Cox, A.G.2    Hampton, M.B.3
  • 16
    • 0023929362 scopus 로고
    • The isolation and purification of a specific " protector" protein which inhibits enzyme inactivation by thiol/Fe(III)/O2 mixed-function oxidation system
    • Kim K., Kim I., Lee K.Y., Rhee S.G., Stadtman E.R. The isolation and purification of a specific " protector" protein which inhibits enzyme inactivation by thiol/Fe(III)/O2 mixed-function oxidation system. J Biol Chem 1988, 263:4704-4711.
    • (1988) J Biol Chem , vol.263 , pp. 4704-4711
    • Kim, K.1    Kim, I.2    Lee, K.Y.3    Rhee, S.G.4    Stadtman, E.R.5
  • 17
    • 34248587901 scopus 로고    scopus 로고
    • Molecular cloning, expression of a peroxiredoxin gene in Chinese shrimp Fenneropenaeus chinensis and the antioxidant activity of its recombinant protein
    • Zhang Q., Li F., Zhang J., Wang B., Gao H., Huanga B., et al. Molecular cloning, expression of a peroxiredoxin gene in Chinese shrimp Fenneropenaeus chinensis and the antioxidant activity of its recombinant protein. Mol Immunol 2007, 44:3501-3509.
    • (2007) Mol Immunol , vol.44 , pp. 3501-3509
    • Zhang, Q.1    Li, F.2    Zhang, J.3    Wang, B.4    Gao, H.5    Huanga, B.6
  • 18
    • 0033963677 scopus 로고    scopus 로고
    • Entamoeba dispar: cloning and characterization of peroxiredoxin genes
    • Tachibana H., Xun-Jia C. Entamoeba dispar: cloning and characterization of peroxiredoxin genes. Exp Parasitol 2000, 94:51-55.
    • (2000) Exp Parasitol , vol.94 , pp. 51-55
    • Tachibana, H.1    Xun-Jia, C.2
  • 19
    • 34447546835 scopus 로고    scopus 로고
    • Human peroxiredoxin 5 gene organization, initial characterization of its promoter and identification of alternative forms of mRNA
    • Nguyên-nhu N.T., Berck J., Clippe A., Duconseille E., Cherif H., Boone C., et al. Human peroxiredoxin 5 gene organization, initial characterization of its promoter and identification of alternative forms of mRNA. Biochim Biophys Acta 2007, 1769:472-483.
    • (2007) Biochim Biophys Acta , vol.1769 , pp. 472-483
    • Nguyên-nhu, N.T.1    Berck, J.2    Clippe, A.3    Duconseille, E.4    Cherif, H.5    Boone, C.6
  • 20
    • 77951107582 scopus 로고    scopus 로고
    • Molecular cloning, expression and antioxidant activity of a peroxiredoxin 2 homologue from Lampetra japonica
    • Sun J., Liu X., Li Q. Molecular cloning, expression and antioxidant activity of a peroxiredoxin 2 homologue from Lampetra japonica. Fish Shellfish Immunol 2010, 28:795-801.
    • (2010) Fish Shellfish Immunol , vol.28 , pp. 795-801
    • Sun, J.1    Liu, X.2    Li, Q.3
  • 21
    • 77954958461 scopus 로고    scopus 로고
    • Analysis of the expression and antioxidative property of a peroxiredoxin 6 from Scophthalmus maximus
    • Zheng W.J., Hua Y.H., Zhang M., Sun L. Analysis of the expression and antioxidative property of a peroxiredoxin 6 from Scophthalmus maximus. Fish Shellfish Immunol 2010, 29:305-311.
    • (2010) Fish Shellfish Immunol , vol.29 , pp. 305-311
    • Zheng, W.J.1    Hua, Y.H.2    Zhang, M.3    Sun, L.4
  • 22
    • 67650621580 scopus 로고    scopus 로고
    • Molecular cloning, characterization and expression analysis of peroxiredoxin 6 from disk abalone Haliotis discus discus and the antioxidant activity of its recombinant protein
    • Nikapitiya C., De Zoysa M., Whang I., Kim C.G., Lee Y.H., Kim S.J., et al. Molecular cloning, characterization and expression analysis of peroxiredoxin 6 from disk abalone Haliotis discus discus and the antioxidant activity of its recombinant protein. Fish Shellfish Immunol 2009, 27:239-249.
    • (2009) Fish Shellfish Immunol , vol.27 , pp. 239-249
    • Nikapitiya, C.1    De Zoysa, M.2    Whang, I.3    Kim, C.G.4    Lee, Y.H.5    Kim, S.J.6
  • 23
    • 33750957055 scopus 로고    scopus 로고
    • Gene discovery in Carcinus maenas and Homarus americanus via expressed sequence tags
    • Towle D.W., Smith C.M. Gene discovery in Carcinus maenas and Homarus americanus via expressed sequence tags. Integr Comp Biol 2006, 46:912-918.
    • (2006) Integr Comp Biol , vol.46 , pp. 912-918
    • Towle, D.W.1    Smith, C.M.2
  • 24
    • 14844299758 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a peroxiredoxin gene from the mole cricket, Gryllotalpa orientalis
    • Kim I., Lee K.S., Hwang J.S., Ahn M.Y., Li J., Sohn H.D., et al. Molecular cloning and characterization of a peroxiredoxin gene from the mole cricket, Gryllotalpa orientalis. Comp Biochem Physiol B 2005, 140:579-587.
    • (2005) Comp Biochem Physiol B , vol.140 , pp. 579-587
    • Kim, I.1    Lee, K.S.2    Hwang, J.S.3    Ahn, M.Y.4    Li, J.5    Sohn, H.D.6
  • 25
    • 28844498034 scopus 로고    scopus 로고
    • White spot syndrome virus infection decreases the activity of antioxidant enzymes in Fenneropenaeus indicus
    • Mohankumar K., Ramasamy P. White spot syndrome virus infection decreases the activity of antioxidant enzymes in Fenneropenaeus indicus. Virus Res 2006, 115:69-75.
    • (2006) Virus Res , vol.115 , pp. 69-75
    • Mohankumar, K.1    Ramasamy, P.2
  • 26
    • 74649084011 scopus 로고    scopus 로고
    • Molecular cloning and expression of a 2-Cys peroxiredoxin gene in the crustacean Eurypanopeus depressus induced by acute hypo-osmotic stress
    • Horn J.V., Malhoe V., Delvina M., Thies M., Tolley S.G., Ueda T. Molecular cloning and expression of a 2-Cys peroxiredoxin gene in the crustacean Eurypanopeus depressus induced by acute hypo-osmotic stress. Comp Biochem Physiol B 2010, 155:309-315.
    • (2010) Comp Biochem Physiol B , vol.155 , pp. 309-315
    • Horn, J.V.1    Malhoe, V.2    Delvina, M.3    Thies, M.4    Tolley, S.G.5    Ueda, T.6
  • 27
    • 59649098901 scopus 로고    scopus 로고
    • Aquaculture in the Asia-Pacific region: applications of molecular population genetics
    • Mather P.B. Aquaculture in the Asia-Pacific region: applications of molecular population genetics. Pertanika J Trop Agric Sci 2008, 31:117-125.
    • (2008) Pertanika J Trop Agric Sci , vol.31 , pp. 117-125
    • Mather, P.B.1
  • 28
    • 0033505308 scopus 로고
    • The penaeid shrimp viruses TSV, IHHNV, WSSV, and YHV current status in the Americas, available diagnostic methods, and management strategies
    • Lightner V.D. The penaeid shrimp viruses TSV, IHHNV, WSSV, and YHV current status in the Americas, available diagnostic methods, and management strategies. J Appl Aquacult 1990, 9:27-52.
    • (1990) J Appl Aquacult , vol.9 , pp. 27-52
    • Lightner, V.D.1
  • 29
    • 79957854747 scopus 로고    scopus 로고
    • Gene profiling and characterization of arginine kinase-1 (MrAK-1) from freshwater giant prawn (Macrobrachium rosenbergii)
    • Arockiaraj J., Puganeshwaran V., Sarasvathi E., Singh A., Alinejaid T., Rofina Y.O., et al. Gene profiling and characterization of arginine kinase-1 (MrAK-1) from freshwater giant prawn (Macrobrachium rosenbergii). Fish Shellfish Immunol 2011, 31:81-89.
    • (2011) Fish Shellfish Immunol , vol.31 , pp. 81-89
    • Arockiaraj, J.1    Puganeshwaran, V.2    Sarasvathi, E.3    Singh, A.4    Alinejaid, T.5    Rofina, Y.O.6
  • 30
    • 84858332370 scopus 로고    scopus 로고
    • Effect of infectious hypodermal and haematopoietic necrosis virus (IHHNV) infection on caspase 3c expression and activity in freshwater prawn Macrobrachium rosenbergii
    • Arockiaraj J., Sarasvathi E., Puganeshwaran V., Singh A., Rofina Y.O., Bhassu S. Effect of infectious hypodermal and haematopoietic necrosis virus (IHHNV) infection on caspase 3c expression and activity in freshwater prawn Macrobrachium rosenbergii. Fish Shellfish Immunol 2012, 32:161-169.
    • (2012) Fish Shellfish Immunol , vol.32 , pp. 161-169
    • Arockiaraj, J.1    Sarasvathi, E.2    Puganeshwaran, V.3    Singh, A.4    Rofina, Y.O.5    Bhassu, S.6
  • 31
    • 33947380590 scopus 로고    scopus 로고
    • Roles of peroxiredoxin II in the regulation of proinflammatory responses to LPS and protection against endotoxin-induced lethal shock
    • Yang C.S., Lee D.S., Song C.H., An S.J., Li S., Kim J.M. Roles of peroxiredoxin II in the regulation of proinflammatory responses to LPS and protection against endotoxin-induced lethal shock. J Exp Med 2007, 204:583-594.
    • (2007) J Exp Med , vol.204 , pp. 583-594
    • Yang, C.S.1    Lee, D.S.2    Song, C.H.3    An, S.J.4    Li, S.5    Kim, J.M.6
  • 32
    • 81255171396 scopus 로고    scopus 로고
    • Bioinformatic characterization and gene expression pattern of apoptosis inhibitor from Macrobrachium rosenbergii challenged with infectious hypodermal and hematopoietic necrosis virus
    • Arockiaraj J., Puganeshwaran V., Sarasvathi E., Singh A., Rofina Y.O., Bhassu S. Bioinformatic characterization and gene expression pattern of apoptosis inhibitor from Macrobrachium rosenbergii challenged with infectious hypodermal and hematopoietic necrosis virus. Fish Shellfish Immunol 2011, 31:1259-1267.
    • (2011) Fish Shellfish Immunol , vol.31 , pp. 1259-1267
    • Arockiaraj, J.1    Puganeshwaran, V.2    Sarasvathi, E.3    Singh, A.4    Rofina, Y.O.5    Bhassu, S.6
  • 33
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method
    • Livak K.J., Schmittgenm T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 2001, 25:402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgenm, T.D.2
  • 35
    • 84858343100 scopus 로고    scopus 로고
    • Prophenoloxidase activating enzyme-III from giant freshwater prawn Macrobrachium rosenbergii: characterization, expression and specific enzyme activity
    • Arockiaraj J., Sarasvathi E., Puganeshwaran V., Singh A., Rofina Y.O., Bhassu S. Prophenoloxidase activating enzyme-III from giant freshwater prawn Macrobrachium rosenbergii: characterization, expression and specific enzyme activity. Mol Biol Rep 2012, 39:1377-1386.
    • (2012) Mol Biol Rep , vol.39 , pp. 1377-1386
    • Arockiaraj, J.1    Sarasvathi, E.2    Puganeshwaran, V.3    Singh, A.4    Rofina, Y.O.5    Bhassu, S.6
  • 36
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of proteinedye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of proteinedye binding. Anal Biochem 1976, 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 37
    • 0015298529 scopus 로고
    • Hepatic microsomal ethanol oxidation: hydrogen peroxide formation and the role of catalase
    • Thurman R.G., Ley H.G., Scholz R. Hepatic microsomal ethanol oxidation: hydrogen peroxide formation and the role of catalase. Eur J Biochem 1972, 25:420-430.
    • (1972) Eur J Biochem , vol.25 , pp. 420-430
    • Thurman, R.G.1    Ley, H.G.2    Scholz, R.3
  • 38
    • 2342632478 scopus 로고    scopus 로고
    • Immunological aspects of heat-shock proteins-the optimum stress of life
    • Prohaszka Z., Fust G. Immunological aspects of heat-shock proteins-the optimum stress of life. Mol Immunol 2004, 41:29-44.
    • (2004) Mol Immunol , vol.41 , pp. 29-44
    • Prohaszka, Z.1    Fust, G.2
  • 39
    • 33646478258 scopus 로고    scopus 로고
    • Differential expression of three Paralichthys olivaceus Hsp40 genes in responses to virus infection and heat shock
    • Dong C.W., Zhang Y.B., Zhang Q.Y., Gui J.F. Differential expression of three Paralichthys olivaceus Hsp40 genes in responses to virus infection and heat shock. Fish Shellfish Immunol 2006, 21:146-158.
    • (2006) Fish Shellfish Immunol , vol.21 , pp. 146-158
    • Dong, C.W.1    Zhang, Y.B.2    Zhang, Q.Y.3    Gui, J.F.4
  • 40
    • 50349096425 scopus 로고    scopus 로고
    • Identification of the small heat shock protein, HSP21, of shrimp Penaeus monodon and the gene expression of HSP21 is inactivated after white spot syndrome virus (WSSV) infection
    • Huang P.Y., Kang S.T., Chen W.Y., Hsu T.C., Lo C.F., Liu K.F., et al. Identification of the small heat shock protein, HSP21, of shrimp Penaeus monodon and the gene expression of HSP21 is inactivated after white spot syndrome virus (WSSV) infection. Fish Shellfish Immunol 2008, 25:250-257.
    • (2008) Fish Shellfish Immunol , vol.25 , pp. 250-257
    • Huang, P.Y.1    Kang, S.T.2    Chen, W.Y.3    Hsu, T.C.4    Lo, C.F.5    Liu, K.F.6
  • 41
    • 18844400905 scopus 로고    scopus 로고
    • Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism
    • Manevich Y., Fisher A.B. Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism. Free Radic Biol Med 2005, 38:1422-1432.
    • (2005) Free Radic Biol Med , vol.38 , pp. 1422-1432
    • Manevich, Y.1    Fisher, A.B.2
  • 42
    • 46249092601 scopus 로고    scopus 로고
    • Proliferating cells express mRNAs with shortened 3'-untranslated regions and fewer microRNA target sites
    • Sandberg R., Neilson J.R., Sarma A., Sharp P.A., Burge C.B. Proliferating cells express mRNAs with shortened 3'-untranslated regions and fewer microRNA target sites. Science 2008, 320:1643-1647.
    • (2008) Science , vol.320 , pp. 1643-1647
    • Sandberg, R.1    Neilson, J.R.2    Sarma, A.3    Sharp, P.A.4    Burge, C.B.5
  • 43
    • 38949111543 scopus 로고    scopus 로고
    • 3'-end mRNA processing: molecular mechanisms and implications for health and disease
    • Danckwardt S., Hentze M.W., Kulozik A.E. 3'-end mRNA processing: molecular mechanisms and implications for health and disease. EMBO J 2008, 27:482-498.
    • (2008) EMBO J , vol.27 , pp. 482-498
    • Danckwardt, S.1    Hentze, M.W.2    Kulozik, A.E.3
  • 44
    • 0001015125 scopus 로고    scopus 로고
    • Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate
    • Seo M.S., Kang S.W., Kim K., Baines I.C., Lee T.H., Rhee S.G. Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate. J Biol Chem 2000, 275:20346-20354.
    • (2000) J Biol Chem , vol.275 , pp. 20346-20354
    • Seo, M.S.1    Kang, S.W.2    Kim, K.3    Baines, I.C.4    Lee, T.H.5    Rhee, S.G.6
  • 45
    • 48749123953 scopus 로고    scopus 로고
    • The crystal structures of oxidized forms of human peroxiredoxin 5 with an intramolecular disulfide bond confirm the proposed enzymatic mechanism for atypical 2-Cys peroxiredoxins
    • Smeets A., Marchand C., Linard D., Knoops B., Declercq J.P. The crystal structures of oxidized forms of human peroxiredoxin 5 with an intramolecular disulfide bond confirm the proposed enzymatic mechanism for atypical 2-Cys peroxiredoxins. Arch Biochem Biophys 2008, 477:98-104.
    • (2008) Arch Biochem Biophys , vol.477 , pp. 98-104
    • Smeets, A.1    Marchand, C.2    Linard, D.3    Knoops, B.4    Declercq, J.P.5
  • 48
    • 39949084474 scopus 로고    scopus 로고
    • Physiological responses to salinity changes of the isopod Idotea chelipes from the Baltic brackish waters
    • Lapucki T., Normant M. Physiological responses to salinity changes of the isopod Idotea chelipes from the Baltic brackish waters. Comp Biochem Physiol A 2008, 149:299-305.
    • (2008) Comp Biochem Physiol A , vol.149 , pp. 299-305
    • Lapucki, T.1    Normant, M.2
  • 49
    • 0141456172 scopus 로고    scopus 로고
    • Salinity-mediated carbonic anhydrase induction in the gills of the euryhaline green crab, Carcinus maenas
    • Henry R.P., Gehnrich S., Weihrauch D., Towle D.W. Salinity-mediated carbonic anhydrase induction in the gills of the euryhaline green crab, Carcinus maenas. Comp Biochem Physiol A 2003, 136:243-258.
    • (2003) Comp Biochem Physiol A , vol.136 , pp. 243-258
    • Henry, R.P.1    Gehnrich, S.2    Weihrauch, D.3    Towle, D.W.4
  • 51
    • 2542464938 scopus 로고    scopus 로고
    • Two enzymes in one: two yeast peroxiredoxins display oxidative stress-dependant switching from a peroxidase to a molecular chaperone function
    • Jang H.H., Lee K.O., Chi Y.H., Jung B.G., Park S.K., Park J.H., et al. Two enzymes in one: two yeast peroxiredoxins display oxidative stress-dependant switching from a peroxidase to a molecular chaperone function. Cell 2004, 117:625-635.
    • (2004) Cell , vol.117 , pp. 625-635
    • Jang, H.H.1    Lee, K.O.2    Chi, Y.H.3    Jung, B.G.4    Park, S.K.5    Park, J.H.6


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