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Volumn 26, Issue 5, 2009, Pages 716-723

A thioredoxin with antioxidant activity identified from Eriocheir sinensis

Author keywords

Antioxidant capacity; Eriocheir sinensis; Gene cloning; Innate immunity; mRNA expression; Thioredoxin

Indexed keywords

ANIMALIA; BACTERIA (MICROORGANISMS); DECAPODA (CRUSTACEA); ERIOCHEIR SINENSIS; ESCHERICHIA COLI; LISTONELLA ANGUILLARUM;

EID: 67349201053     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2009.02.024     Document Type: Article
Times cited : (44)

References (57)
  • 1
    • 0035951470 scopus 로고    scopus 로고
    • Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster
    • Kanzok S.M., Fechner A., Bauer H., Ulschmid J.K., Muller H.M., Botella-Munoz J., et al. Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster. Science 291 (2001) 643-646
    • (2001) Science , vol.291 , pp. 643-646
    • Kanzok, S.M.1    Fechner, A.2    Bauer, H.3    Ulschmid, J.K.4    Muller, H.M.5    Botella-Munoz, J.6
  • 3
    • 49349099323 scopus 로고    scopus 로고
    • Emerging potential of thioredoxin and thioredoxin interacting proteins in various disease conditions
    • Maulik N., and Das D.K. Emerging potential of thioredoxin and thioredoxin interacting proteins in various disease conditions. Biochim Biophys Acta 1780 (2008) 1368-1382
    • (2008) Biochim Biophys Acta , vol.1780 , pp. 1368-1382
    • Maulik, N.1    Das, D.K.2
  • 4
    • 23944446547 scopus 로고    scopus 로고
    • Redox regulation by intrinsic species and extrinsic nutrients in normal and cancer cells
    • McEligot A.J., Yang S., and Meyskens Jr. F.L. Redox regulation by intrinsic species and extrinsic nutrients in normal and cancer cells. Annu Rev Nutr 25 (2005) 261-295
    • (2005) Annu Rev Nutr , vol.25 , pp. 261-295
    • McEligot, A.J.1    Yang, S.2    Meyskens Jr., F.L.3
  • 6
    • 3142685079 scopus 로고    scopus 로고
    • Extracellular thiols and thiol/disulfide redox in metabolism
    • Moriarty-Craige S.E., and Jones D.P. Extracellular thiols and thiol/disulfide redox in metabolism. Annu Rev Nutr 24 (2004) 481-509
    • (2004) Annu Rev Nutr , vol.24 , pp. 481-509
    • Moriarty-Craige, S.E.1    Jones, D.P.2
  • 7
    • 11844280984 scopus 로고    scopus 로고
    • Comparative structural analysis of oxidized and reduced thioredoxin from Drosophila melanogaster
    • Wahl M.C., Irmler A., Hecker B., Schirmer R.H., and Becker K. Comparative structural analysis of oxidized and reduced thioredoxin from Drosophila melanogaster. J Mol Biol 345 (2005) 1119-1130
    • (2005) J Mol Biol , vol.345 , pp. 1119-1130
    • Wahl, M.C.1    Irmler, A.2    Hecker, B.3    Schirmer, R.H.4    Becker, K.5
  • 8
  • 9
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren A. Thioredoxin and glutaredoxin systems. J Biol Chem 264 (1989) 13963-13966
    • (1989) J Biol Chem , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 10
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • Arner E.S., and Holmgren A. Physiological functions of thioredoxin and thioredoxin reductase. Eur J Biochem 267 (2000) 6102-6109
    • (2000) Eur J Biochem , vol.267 , pp. 6102-6109
    • Arner, E.S.1    Holmgren, A.2
  • 11
    • 34548067718 scopus 로고    scopus 로고
    • Thioredoxin signaling as a target for cancer therapy
    • Powis G., and Kirkpatrick D.L. Thioredoxin signaling as a target for cancer therapy. Curr Opin Pharmacol 7 (2007) 392-397
    • (2007) Curr Opin Pharmacol , vol.7 , pp. 392-397
    • Powis, G.1    Kirkpatrick, D.L.2
  • 12
    • 0028139014 scopus 로고
    • The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase
    • Bjornstedt M., Xue J., Huang W., Akesson B., and Holmgren A. The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase. J Biol Chem 269 (1994) 29382-29384
    • (1994) J Biol Chem , vol.269 , pp. 29382-29384
    • Bjornstedt, M.1    Xue, J.2    Huang, W.3    Akesson, B.4    Holmgren, A.5
  • 16
    • 78651146370 scopus 로고
    • Enzymatic synthesis of deoxyribonucleotides. Iv. Isolation and characterization of thioredoxin, the hydrogen donor from Escherichia Coli
    • Laurent T.C., Moore E.C., and Reichard P. Enzymatic synthesis of deoxyribonucleotides. Iv. Isolation and characterization of thioredoxin, the hydrogen donor from Escherichia Coli. B J Biol Chem 239 (1964) 3436-3444
    • (1964) B J Biol Chem , vol.239 , pp. 3436-3444
    • Laurent, T.C.1    Moore, E.C.2    Reichard, P.3
  • 17
    • 0035029131 scopus 로고    scopus 로고
    • Properties and biological activities of thioredoxins
    • Powis G., and Montfort W.R. Properties and biological activities of thioredoxins. Annu Rev Pharmacol Toxicol 41 (2001) 261-295
    • (2001) Annu Rev Pharmacol Toxicol , vol.41 , pp. 261-295
    • Powis, G.1    Montfort, W.R.2
  • 21
    • 0035943725 scopus 로고    scopus 로고
    • Characterization of Sptrx, a novel member of the thioredoxin family specifically expressed in human spermatozoa
    • Miranda-Vizuete A., Ljung J., Damdimopoulos A.E., Gustafsson J.A., Oko R., Pelto-Huikko M., et al. Characterization of Sptrx, a novel member of the thioredoxin family specifically expressed in human spermatozoa. J Biol Chem 276 (2001) 31567-31574
    • (2001) J Biol Chem , vol.276 , pp. 31567-31574
    • Miranda-Vizuete, A.1    Ljung, J.2    Damdimopoulos, A.E.3    Gustafsson, J.A.4    Oko, R.5    Pelto-Huikko, M.6
  • 22
    • 0036834503 scopus 로고    scopus 로고
    • Study on the transmission of tremor disease (TD) in the Chinese mitten crab, Eriocheir sinensis (Crustacea: Decapoda)
    • Wang W., Zhu N., Gu Z., Du K., and Xu Z. Study on the transmission of tremor disease (TD) in the Chinese mitten crab, Eriocheir sinensis (Crustacea: Decapoda). J Invertebr Pathol 81 (2002) 202-204
    • (2002) J Invertebr Pathol , vol.81 , pp. 202-204
    • Wang, W.1    Zhu, N.2    Gu, Z.3    Du, K.4    Xu, Z.5
  • 23
    • 4544358441 scopus 로고    scopus 로고
    • Morphology of spiroplasmas in the Chinese mitten crab Eriocheir sinensis associated with tremor disease
    • Wang W., Chen J., Du K., and Xu Z. Morphology of spiroplasmas in the Chinese mitten crab Eriocheir sinensis associated with tremor disease. Res Microbiol 155 (2004) 630-635
    • (2004) Res Microbiol , vol.155 , pp. 630-635
    • Wang, W.1    Chen, J.2    Du, K.3    Xu, Z.4
  • 24
    • 0033591428 scopus 로고    scopus 로고
    • Phylogenetic perspectives in innate immunity
    • Hoffmann Ja K.F., Janeway C.A., and Ezekowitz R.A. Phylogenetic perspectives in innate immunity. Science 284 (1999) 1313-1318
    • (1999) Science , vol.284 , pp. 1313-1318
    • Hoffmann Ja, K.F.1    Janeway, C.A.2    Ezekowitz, R.A.3
  • 25
    • 0036012805 scopus 로고    scopus 로고
    • Generation of superoxide anion and SOD activity in haemocytes and muscle of American white shrimp (Litopenaeus vannamei) as a response to beta-glucan and sulphated polysaccharide
    • Campa-Cordova A.I., Hernandez-Saavedra N.Y., De Philippis R., and Ascencio F. Generation of superoxide anion and SOD activity in haemocytes and muscle of American white shrimp (Litopenaeus vannamei) as a response to beta-glucan and sulphated polysaccharide. Fish Shellfish Immunol 12 (2002) 353-366
    • (2002) Fish Shellfish Immunol , vol.12 , pp. 353-366
    • Campa-Cordova, A.I.1    Hernandez-Saavedra, N.Y.2    De Philippis, R.3    Ascencio, F.4
  • 26
    • 28844498034 scopus 로고    scopus 로고
    • White spot syndrome virus infection decreases the activity of antioxidant enzymes in Fenneropenaeus indicus
    • Mohankumar K., and Ramasamy P. White spot syndrome virus infection decreases the activity of antioxidant enzymes in Fenneropenaeus indicus. Virus Res 115 (2006) 69-75
    • (2006) Virus Res , vol.115 , pp. 69-75
    • Mohankumar, K.1    Ramasamy, P.2
  • 28
    • 35348964100 scopus 로고    scopus 로고
    • Proteomic analysis of differentially expressed proteins in Penaeus vannamei hemocytes upon Taura syndrome virus infection
    • Chongsatja P.O., Bourchookarn A., Lo C.F., Thongboonkerd V., and Krittanai C. Proteomic analysis of differentially expressed proteins in Penaeus vannamei hemocytes upon Taura syndrome virus infection. Proteomics 7 (2007) 3592-3601
    • (2007) Proteomics , vol.7 , pp. 3592-3601
    • Chongsatja, P.O.1    Bourchookarn, A.2    Lo, C.F.3    Thongboonkerd, V.4    Krittanai, C.5
  • 29
    • 65649134322 scopus 로고    scopus 로고
    • Molecular cloning and characterization of peroxiredoxin 6 from Chinese mitten crab Eriocheir sinensis
    • doi:10.1016/j.fsi.2008.10.006
    • 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, doi:10.1016/j.fsi.2008.10.006.
    • Fish Shellfish Immunol
    • Mu, C.1    Zhao, J.2    Wang, L.3    Song, L.4    Zhang, H.5    Li, C.6    et al7
  • 30
    • 0028986031 scopus 로고
    • Characterisation of shrimp haemocytes and plasma components by monoclonal antibodies
    • Rodriguez J., Boulo V., Mialhe E., and Bachere E. Characterisation of shrimp haemocytes and plasma components by monoclonal antibodies. J Cell Sci 108 Pt 3 (1995) 1043-1050
    • (1995) J Cell Sci , vol.108 , Issue.PART 3 , pp. 1043-1050
    • Rodriguez, J.1    Boulo, V.2    Mialhe, E.3    Bachere, E.4
  • 31
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25 (1997) 4876-4882
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 32
    • 45949109669 scopus 로고    scopus 로고
    • MEGA: a biologist-centric software for evolutionary analysis of DNA and protein sequences
    • Kumar S., Nei M., Dudley J., and Tamura K. MEGA: a biologist-centric software for evolutionary analysis of DNA and protein sequences. Brief Bioinformatics 9 (2008) 299-306
    • (2008) Brief Bioinformatics , vol.9 , pp. 299-306
    • Kumar, S.1    Nei, M.2    Dudley, J.3    Tamura, K.4
  • 33
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0
    • Tamura K., Dudley J., Nei M., and Kumar S. MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol Biol Evol 24 (2007) 1596-1599
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 34
    • 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., and Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 25 (2001) 402-408
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • Holmgren A. Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J Biol Chem 254 (1979) 9627-9632
    • (1979) J Biol Chem , vol.254 , pp. 9627-9632
    • Holmgren, A.1
  • 37
    • 0030671351 scopus 로고    scopus 로고
    • Human thioredoxin homodimers: regulation by pH, role of aspartate 60, and crystal structure of the aspartate 60→asparagine mutant
    • Andersen J.F., Sanders D.A., Gasdaska J.R., Weichsel A., Powis G., and Montfort W.R. Human thioredoxin homodimers: regulation by pH, role of aspartate 60, and crystal structure of the aspartate 60→asparagine mutant. Biochemistry 36 (1997) 13979-13988
    • (1997) Biochemistry , vol.36 , pp. 13979-13988
    • Andersen, J.F.1    Sanders, D.A.2    Gasdaska, J.R.3    Weichsel, A.4    Powis, G.5    Montfort, W.R.6
  • 38
    • 40649116241 scopus 로고    scopus 로고
    • Hexavalent chromium causes the oxidation of thioredoxin in human bronchial epithelial cells
    • Myers J.M., Antholine W.E., and Myers C.R. Hexavalent chromium causes the oxidation of thioredoxin in human bronchial epithelial cells. Toxicology 246 (2008) 222-233
    • (2008) Toxicology , vol.246 , pp. 222-233
    • Myers, J.M.1    Antholine, W.E.2    Myers, C.R.3
  • 40
    • 0030585429 scopus 로고    scopus 로고
    • Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer
    • Weichsel A., Gasdaska J.R., Powis G., and Montfort W.R. Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer. Structure 4 (1996) 735-751
    • (1996) Structure , vol.4 , pp. 735-751
    • Weichsel, A.1    Gasdaska, J.R.2    Powis, G.3    Montfort, W.R.4
  • 41
    • 34548269520 scopus 로고    scopus 로고
    • Molecular dynamics simulations of thioredoxin with S-glutathiolated cysteine-73
    • Han S. Molecular dynamics simulations of thioredoxin with S-glutathiolated cysteine-73. Biochem Biophys Res Commun 362 (2007) 532-537
    • (2007) Biochem Biophys Res Commun , vol.362 , pp. 532-537
    • Han, S.1
  • 42
    • 0028176651 scopus 로고
    • Oxidative stress as a mediator of apoptosis
    • Buttke T.M., and PA S. Oxidative stress as a mediator of apoptosis. Immunol Today 15 (1994) 7-10
    • (1994) Immunol Today , vol.15 , pp. 7-10
    • Buttke, T.M.1    PA, S.2
  • 43
    • 33845428642 scopus 로고    scopus 로고
    • Thioredoxin and related molecules - from biology to health and disease
    • Lillig C.H., and Holmgren A. Thioredoxin and related molecules - from biology to health and disease. Antioxid Redox Signal 9 (2007) 25-47
    • (2007) Antioxid Redox Signal , vol.9 , pp. 25-47
    • Lillig, C.H.1    Holmgren, A.2
  • 44
    • 0037060711 scopus 로고    scopus 로고
    • Clearing mechanisms of Vibrio vulnificus biotype I in the black tiger shrimp Penaeus monodon
    • Alday-Sanz V., Roque A., and Turnbull J.F. Clearing mechanisms of Vibrio vulnificus biotype I in the black tiger shrimp Penaeus monodon. Dis Aquat Org 48 (2002) 91-99
    • (2002) Dis Aquat Org , vol.48 , pp. 91-99
    • Alday-Sanz, V.1    Roque, A.2    Turnbull, J.F.3
  • 45
    • 34047189183 scopus 로고    scopus 로고
    • Effects of methyl parathion on Chasmagnathus granulatus hepatopancreas: protective role of sesamol
    • Bianchini A., and Monserrat J.M. Effects of methyl parathion on Chasmagnathus granulatus hepatopancreas: protective role of sesamol. Ecotoxicol Environ Saf 67 (2007) 100-108
    • (2007) Ecotoxicol Environ Saf , vol.67 , pp. 100-108
    • Bianchini, A.1    Monserrat, J.M.2
  • 46
    • 0034704081 scopus 로고    scopus 로고
    • The thioredoxin system of the malaria parasite Plasmodium falciparum. Glutathione reduction revisited
    • Kanzok S.M., Schirmer R.H., Turbachova I., Iozef R., and Becker K. The thioredoxin system of the malaria parasite Plasmodium falciparum. Glutathione reduction revisited. J Biol Chem 275 (2000) 40180-40186
    • (2000) J Biol Chem , vol.275 , pp. 40180-40186
    • Kanzok, S.M.1    Schirmer, R.H.2    Turbachova, I.3    Iozef, R.4    Becker, K.5
  • 47
    • 44749086615 scopus 로고    scopus 로고
    • Potential use of chitosan nanoparticles for oral delivery of DNA vaccine in Asian sea bass (Lates calcarifer) to protect from Vibrio (Listonella) anguillarum
    • Rajesh Kumar S., Ishaq Ahmed V.P., Parameswaran V., Sudhakaran R., Sarath Babu V., and Sahul Hameed A.S. Potential use of chitosan nanoparticles for oral delivery of DNA vaccine in Asian sea bass (Lates calcarifer) to protect from Vibrio (Listonella) anguillarum. Fish Shellfish Immunol 25 (2008) 47-56
    • (2008) Fish Shellfish Immunol , vol.25 , pp. 47-56
    • Rajesh Kumar, S.1    Ishaq Ahmed, V.P.2    Parameswaran, V.3    Sudhakaran, R.4    Sarath Babu, V.5    Sahul Hameed, A.S.6
  • 48
    • 33747755083 scopus 로고    scopus 로고
    • Pharmacokinetics and the active metabolite of enrofloxacin in Chinese mitten-handed crab (Eriocheir sinensis)
    • Tang J., Yang X.L., Zheng Z.L., Yu W.J., Hu K., and HJ Y. Pharmacokinetics and the active metabolite of enrofloxacin in Chinese mitten-handed crab (Eriocheir sinensis). Aquaculture 260 (2006) 69-76
    • (2006) Aquaculture , vol.260 , pp. 69-76
    • Tang, J.1    Yang, X.L.2    Zheng, Z.L.3    Yu, W.J.4    Hu, K.5    HJ, Y.6
  • 49
    • 0032802807 scopus 로고    scopus 로고
    • Expression of thioredoxin and thioredoxin reductase in placentae of pregnant mice exposed to lipopolysaccharide
    • Ejima K., Koji T., Nanri H., Kashimura M., and Ikeda M. Expression of thioredoxin and thioredoxin reductase in placentae of pregnant mice exposed to lipopolysaccharide. Placenta 20 (1999) 561-566
    • (1999) Placenta , vol.20 , pp. 561-566
    • Ejima, K.1    Koji, T.2    Nanri, H.3    Kashimura, M.4    Ikeda, M.5
  • 50
    • 17644377258 scopus 로고    scopus 로고
    • How neutrophils kill microbes
    • Segal A. How neutrophils kill microbes. Annu Rev Immunol 23 (2005) 197-223
    • (2005) Annu Rev Immunol , vol.23 , pp. 197-223
    • Segal, A.1
  • 51
    • 0242460542 scopus 로고    scopus 로고
    • Oxidative killing of microbes by neutrophils
    • Roos D., van Bruggen R., and Meischl C. Oxidative killing of microbes by neutrophils. Microbes Infect 5 (2003) 1307-1315
    • (2003) Microbes Infect , vol.5 , pp. 1307-1315
    • Roos, D.1    van Bruggen, R.2    Meischl, C.3
  • 52
    • 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., and 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 91 (1994) 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
  • 53
    • 0027209389 scopus 로고
    • Strategies of antioxidant defense
    • Sies H. Strategies of antioxidant defense. Eur J Biochem 215 (1993) 213-219
    • (1993) Eur J Biochem , vol.215 , pp. 213-219
    • Sies, H.1
  • 54
    • 0027323871 scopus 로고
    • Cloning, sequencing, and mutation of thiol-specific antioxidant gene of Saccharomyces cerevisiae
    • Chae H.Z., Kim I.H., Kim K., and Rhee S.G. Cloning, sequencing, and mutation of thiol-specific antioxidant gene of Saccharomyces cerevisiae. J Biol Chem 268 (1993) 16815-16821
    • (1993) J Biol Chem , vol.268 , pp. 16815-16821
    • Chae, H.Z.1    Kim, I.H.2    Kim, K.3    Rhee, S.G.4
  • 55
    • 0018263443 scopus 로고
    • The biology of oxygen radicals
    • Fridovich I. The biology of oxygen radicals. Science 201 (1978) 875-880
    • (1978) Science , vol.201 , pp. 875-880
    • Fridovich, I.1
  • 56
    • 0037297417 scopus 로고    scopus 로고
    • Non-reciprocal regulation of the redox state of the glutathione-glutaredoxin and thioredoxin systems
    • Trotter E.W., and Grant C.M. Non-reciprocal regulation of the redox state of the glutathione-glutaredoxin and thioredoxin systems. EMBO Rep 4 (2003) 184-188
    • (2003) EMBO Rep , vol.4 , pp. 184-188
    • Trotter, E.W.1    Grant, C.M.2
  • 57
    • 40049111243 scopus 로고    scopus 로고
    • Mitochondrial thioredoxin-2 from disk abalone (Haliotis discus discus): molecular characterization, tissue expression and DNA protection activity of its recombinant protein
    • De Zoysa M., Pushpamali W.A., Whang I., Kim S.J., and Lee J. Mitochondrial thioredoxin-2 from disk abalone (Haliotis discus discus): molecular characterization, tissue expression and DNA protection activity of its recombinant protein. Comp Biochem Physiol B, Biochem Mol Biol 149 (2008) 630-639
    • (2008) Comp Biochem Physiol B, Biochem Mol Biol , vol.149 , pp. 630-639
    • De Zoysa, M.1    Pushpamali, W.A.2    Whang, I.3    Kim, S.J.4    Lee, J.5


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