메뉴 건너뛰기




Volumn 239, Issue 2, 2009, Pages 130-136

Exposure to monomethylarsonous acid (MMAIII) leads to altered selenoprotein synthesis in a primary human lung cell model

Author keywords

Antioxidant response element; Arsenic; Carcinogenesis; Monomethylarsonous acid; Selenium; Thioredoxin reductase

Indexed keywords

ANTIOXIDANT; GLUTATHIONE PEROXIDASE; LUCIFERASE; MESSENGER RNA; METHANEARSONIC ACID; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); SELENIUM; SELENOPROTEIN; THIOREDOXIN REDUCTASE;

EID: 68949194237     PISSN: 0041008X     EISSN: 10960333     Source Type: Journal    
DOI: 10.1016/j.taap.2008.11.011     Document Type: Article
Times cited : (19)

References (57)
  • 2
    • 33751178410 scopus 로고    scopus 로고
    • The thioredoxin system in cancer
    • Arner E.S., and Holmgren A. The thioredoxin system in cancer. Semin. Cancer Biol. 16 (2006) 420-426
    • (2006) Semin. Cancer Biol. , vol.16 , pp. 420-426
    • Arner, E.S.1    Holmgren, A.2
  • 3
    • 0023886514 scopus 로고
    • Evidence for specific selenium target tissues and new biologically important selenoproteins
    • Behne D., Hilmert H., Scheid S., Gessner H., and Elger W. Evidence for specific selenium target tissues and new biologically important selenoproteins. Biochim. Biophys. Acta. 966 (1988) 12-21
    • (1988) Biochim. Biophys. Acta. , vol.966 , pp. 12-21
    • Behne, D.1    Hilmert, H.2    Scheid, S.3    Gessner, H.4    Elger, W.5
  • 4
    • 0030499036 scopus 로고    scopus 로고
    • Thioredoxin and thioredoxin reductase gene expression in human tumors and cell lines, and the effects of serum stimulation and hypoxia
    • Berggren M., Gallegos A., Gasdaska J.R., Gasdaska P.Y., Warneke J., and Powis G. Thioredoxin and thioredoxin reductase gene expression in human tumors and cell lines, and the effects of serum stimulation and hypoxia. Anticancer Res. 16 (1996) 3459-3466
    • (1996) Anticancer Res. , vol.16 , pp. 3459-3466
    • Berggren, M.1    Gallegos, A.2    Gasdaska, J.R.3    Gasdaska, P.Y.4    Warneke, J.5    Powis, G.6
  • 5
    • 27644506592 scopus 로고    scopus 로고
    • Insights into the hierarchy of selenium incorporation
    • Berry M.J. Insights into the hierarchy of selenium incorporation. Nat. Genet. 37 (2005) 1162-1163
    • (2005) Nat. Genet. , vol.37 , pp. 1162-1163
    • Berry, M.J.1
  • 6
    • 0027282772 scopus 로고
    • Functional characterization of the eukaryotic SECIS elements which direct selenocysteine insertion at UGA codons
    • Berry M.J., Banu L., Harney J.W., and Larsen P.R. Functional characterization of the eukaryotic SECIS elements which direct selenocysteine insertion at UGA codons. Embo. J. 12 (1993) 3315-3322
    • (1993) Embo. J. , vol.12 , pp. 3315-3322
    • Berry, M.J.1    Banu, L.2    Harney, J.W.3    Larsen, P.R.4
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 0034677213 scopus 로고    scopus 로고
    • A novel RNA binding protein, SBP2, is required for the translation of mammalian selenoprotein mRNAs
    • Copeland P.R., Fletcher J.E., Carlson B.A., Hatfield D.L., and Driscoll D.M. A novel RNA binding protein, SBP2, is required for the translation of mammalian selenoprotein mRNAs. EMBO J. 19 (2000) 306-314
    • (2000) EMBO J. , vol.19 , pp. 306-314
    • Copeland, P.R.1    Fletcher, J.E.2    Carlson, B.A.3    Hatfield, D.L.4    Driscoll, D.M.5
  • 12
    • 33846482728 scopus 로고    scopus 로고
    • Mitogenic signal transduction caused by monomethylarsonous acid in human bladder cells: role in arsenic-induced carcinogenesis
    • Eblin K.E., Bredfeldt T.G., Buffington S., and Gandolfi A.J. Mitogenic signal transduction caused by monomethylarsonous acid in human bladder cells: role in arsenic-induced carcinogenesis. Toxicol. Sci. 95 (2007) 321-330
    • (2007) Toxicol. Sci. , vol.95 , pp. 321-330
    • Eblin, K.E.1    Bredfeldt, T.G.2    Buffington, S.3    Gandolfi, A.J.4
  • 13
    • 44149106562 scopus 로고    scopus 로고
    • Immortalized human urothelial cells as a model of arsenic-induced bladder cancer
    • Eblin K.E., Bredfeldt T.G., and Gandolfi A.J. Immortalized human urothelial cells as a model of arsenic-induced bladder cancer. Toxicology 248 (2008) 67-76
    • (2008) Toxicology , vol.248 , pp. 67-76
    • Eblin, K.E.1    Bredfeldt, T.G.2    Gandolfi, A.J.3
  • 14
    • 0027395864 scopus 로고
    • Effects of acute sodium arsenite administration on the pulmonary chemical metabolizing enzymes, cytochrome P-450 monooxygenase, NAD(P)H:quinone acceptor oxidoreductase and glutathione S-transferase in guinea pig: comparison with effects in liver and kidney
    • Falkner K.C., McCallum G.P., Cherian M.G., and Bend J.R. Effects of acute sodium arsenite administration on the pulmonary chemical metabolizing enzymes, cytochrome P-450 monooxygenase, NAD(P)H:quinone acceptor oxidoreductase and glutathione S-transferase in guinea pig: comparison with effects in liver and kidney. Chem. Biol. Interact. 86 (1993) 51-68
    • (1993) Chem. Biol. Interact. , vol.86 , pp. 51-68
    • Falkner, K.C.1    McCallum, G.P.2    Cherian, M.G.3    Bend, J.R.4
  • 16
  • 18
    • 0032502777 scopus 로고    scopus 로고
    • A new human selenium-containing protein. Purification, characterization, and cDNA sequence
    • Gladyshev V.N., Jeang K.T., Wootton J.C., and Hatfield D.L. A new human selenium-containing protein. Purification, characterization, and cDNA sequence. J. Biol. Chem. 273 (1998) 8910-8915
    • (1998) J. Biol. Chem. , vol.273 , pp. 8910-8915
    • Gladyshev, V.N.1    Jeang, K.T.2    Wootton, J.C.3    Hatfield, D.L.4
  • 19
    • 0022222407 scopus 로고
    • The cell biology of aging
    • Hayflick L. The cell biology of aging. Clin. Geriatr. Med. 1 (1985) 15-27
    • (1985) Clin. Geriatr. Med. , vol.1 , pp. 15-27
    • Hayflick, L.1
  • 20
    • 0344622606 scopus 로고
    • The serial cultivation of human diploid cell strains
    • Hayflick L., and Moorhead P.S. The serial cultivation of human diploid cell strains. Exp. Cell Res. 25 (1961) 585-621
    • (1961) Exp. Cell Res. , vol.25 , pp. 585-621
    • Hayflick, L.1    Moorhead, P.S.2
  • 21
    • 33747643517 scopus 로고    scopus 로고
    • Arsenic induces NAD(P)H-quinone oxidoreductase I by disrupting the Nrf2 × Keap1 × Cul3 complex and recruiting Nrf2 × Maf to the antioxidant response element enhancer
    • He X., Chen M.G., Lin G.X., and Ma Q. Arsenic induces NAD(P)H-quinone oxidoreductase I by disrupting the Nrf2 × Keap1 × Cul3 complex and recruiting Nrf2 × Maf to the antioxidant response element enhancer. J. Biol. Chem. 281 (2006) 23620-23631
    • (2006) J. Biol. Chem. , vol.281 , pp. 23620-23631
    • He, X.1    Chen, M.G.2    Lin, G.X.3    Ma, Q.4
  • 22
    • 0037740965 scopus 로고    scopus 로고
    • Induction of hepatic thioredoxin reductase activity by sulforaphane, both in Hepa1c1c7 cells and in male Fisher 344 rats
    • Hintze K.J., Keck A.S., Finley J.W., and Jeffery E.H. Induction of hepatic thioredoxin reductase activity by sulforaphane, both in Hepa1c1c7 cells and in male Fisher 344 rats. J. Nutr. Biochem. 14 (2003) 173-179
    • (2003) J. Nutr. Biochem. , vol.14 , pp. 173-179
    • Hintze, K.J.1    Keck, A.S.2    Finley, J.W.3    Jeffery, E.H.4
  • 23
    • 0042920821 scopus 로고    scopus 로고
    • Thioredoxin reductase in human hepatoma cells is transcriptionally regulated by sulforaphane and other electrophiles via an antioxidant response element
    • Hintze K.J., Wald K.A., Zeng H., Jeffery E.H., and Finley J.W. Thioredoxin reductase in human hepatoma cells is transcriptionally regulated by sulforaphane and other electrophiles via an antioxidant response element. J. Nutr. 133 (2003) 2721-2727
    • (2003) J. Nutr. , vol.133 , pp. 2721-2727
    • Hintze, K.J.1    Wald, K.A.2    Zeng, H.3    Jeffery, E.H.4    Finley, J.W.5
  • 24
    • 0017653811 scopus 로고
    • Bovine thioredoxin system. Purification of thioredoxin reductase from calf liver and thymus and studies of its function in disulfide reduction
    • Holmgren A. Bovine thioredoxin system. Purification of thioredoxin reductase from calf liver and thymus and studies of its function in disulfide reduction. J. Biol. Chem. 252 (1977) 4600-4606
    • (1977) J. Biol. Chem. , vol.252 , pp. 4600-4606
    • Holmgren, A.1
  • 25
    • 10044222140 scopus 로고    scopus 로고
    • An integrated pharmacokinetic and pharmacodynamic study of arsenite action 2. Heme oxygenase induction in mice
    • Kenyon E.M., Del Razo L.M., Hughes M.F., and Kitchin K.T. An integrated pharmacokinetic and pharmacodynamic study of arsenite action 2. Heme oxygenase induction in mice. Toxicology 206 (2005) 389-401
    • (2005) Toxicology , vol.206 , pp. 389-401
    • Kenyon, E.M.1    Del Razo, L.M.2    Hughes, M.F.3    Kitchin, K.T.4
  • 26
    • 53649083711 scopus 로고    scopus 로고
    • Tissue distribution and urinary excretion of inorganic arsenic and its methylated metabolites in C57BL6 mice following subchronic exposure to arsenate in drinking water
    • Kenyon E.M., Hughes M.F., Adair B.M., Highfill J.H., Crecelius E.A., Clewell H.J., and Yager J.W. Tissue distribution and urinary excretion of inorganic arsenic and its methylated metabolites in C57BL6 mice following subchronic exposure to arsenate in drinking water. Toxicol. Appl. Pharmacol. 232 (2008) 448-455
    • (2008) Toxicol. Appl. Pharmacol. , vol.232 , pp. 448-455
    • Kenyon, E.M.1    Hughes, M.F.2    Adair, B.M.3    Highfill, J.H.4    Crecelius, E.A.5    Clewell, H.J.6    Yager, J.W.7
  • 27
    • 78651146370 scopus 로고
    • Enzymatic synthesis of deoxyribonucleotides. Iv. Isolation and characterization of thioredoxin, the hydrogen donor from Escherichia coli B
    • 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) J. Biol. Chem. , vol.239 , pp. 3436-3444
    • Laurent, T.C.1    Moore, E.C.2    Reichard, P.3
  • 28
    • 0017622366 scopus 로고
    • Metabolic interrelationships between arsenic and selenium
    • Levander Q.A. Metabolic interrelationships between arsenic and selenium. Environ. Health Perspect. 19 (1977) 159-164
    • (1977) Environ. Health Perspect. , vol.19 , pp. 159-164
    • Levander, Q.A.1
  • 29
    • 0014485135 scopus 로고
    • Effects of arsenic, mercury, thallium, and lead on selenium metabolism in rats
    • Levander Q.A., and Argrett L.C. Effects of arsenic, mercury, thallium, and lead on selenium metabolism in rats. Toxicol. Appl. Pharmacol. 14 (1969) 308-314
    • (1969) Toxicol. Appl. Pharmacol. , vol.14 , pp. 308-314
    • Levander, Q.A.1    Argrett, L.C.2
  • 30
    • 15944422921 scopus 로고    scopus 로고
    • Arsenic (+ 3 oxidation state) methyltransferase and the inorganic arsenic methylation phenotype
    • Li J., Waters S.B., Drobna Z., Devesa V., Styblo M., and Thomas D.J. Arsenic (+ 3 oxidation state) methyltransferase and the inorganic arsenic methylation phenotype. Toxicol. Appl. Pharmacol. 204 (2005) 164-169
    • (2005) Toxicol. Appl. Pharmacol. , vol.204 , pp. 164-169
    • Li, J.1    Waters, S.B.2    Drobna, Z.3    Devesa, V.4    Styblo, M.5    Thomas, D.J.6
  • 31
    • 0032705863 scopus 로고    scopus 로고
    • Methylarsenicals and arsinothiols are potent inhibitors of mouse liver thioredoxin reductase
    • Lin S., Cullen W.R., and Thomas D.J. Methylarsenicals and arsinothiols are potent inhibitors of mouse liver thioredoxin reductase. Chem. Res. Toxicol. 12 (1999) 924-930
    • (1999) Chem. Res. Toxicol. , vol.12 , pp. 924-930
    • Lin, S.1    Cullen, W.R.2    Thomas, D.J.3
  • 33
    • 0035852735 scopus 로고    scopus 로고
    • Induction of oxyradicals by arsenic: implication for mechanism of genotoxicity
    • Liu S.X., Athar M., Lippai I., Waldren C., and Hei T.K. Induction of oxyradicals by arsenic: implication for mechanism of genotoxicity. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 1643-1648
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 1643-1648
    • Liu, S.X.1    Athar, M.2    Lippai, I.3    Waldren, C.4    Hei, T.K.5
  • 34
    • 0034671770 scopus 로고    scopus 로고
    • SECIS-SBP2 interactions dictate selenocysteine incorporation efficiency and selenoprotein hierarchy
    • Low S.C., Grundner-Culemann E., Harney J.W., and Berry M.J. SECIS-SBP2 interactions dictate selenocysteine incorporation efficiency and selenoprotein hierarchy. Embo. J. 19 (2000) 6882-6890
    • (2000) Embo. J. , vol.19 , pp. 6882-6890
    • Low, S.C.1    Grundner-Culemann, E.2    Harney, J.W.3    Berry, M.J.4
  • 35
    • 34547644483 scopus 로고    scopus 로고
    • Targeting thioredoxin reductase is a basis for cancer therapy by arsenic trioxide
    • Lu J., Chew E.H., and Holmgren A. Targeting thioredoxin reductase is a basis for cancer therapy by arsenic trioxide. Proc. Natl. Acad. Sci. U.S.A. 104 (2007) 12288-12293
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 12288-12293
    • Lu, J.1    Chew, E.H.2    Holmgren, A.3
  • 36
    • 17844372715 scopus 로고    scopus 로고
    • Roles of methionine suldfoxide reductases in antioxidant defense, protein regulation and survival
    • Moskovitz J. Roles of methionine suldfoxide reductases in antioxidant defense, protein regulation and survival. Curr. Pharm. Des. 11 (2005) 1451-1457
    • (2005) Curr. Pharm. Des. , vol.11 , pp. 1451-1457
    • Moskovitz, J.1
  • 37
    • 0001939118 scopus 로고
    • The influence of arsenic on the toxicity of seleniforous grains
    • Moxon A. The influence of arsenic on the toxicity of seleniforous grains. Science (1938) 81
    • (1938) Science , pp. 81
    • Moxon, A.1
  • 39
    • 34250318625 scopus 로고    scopus 로고
    • From selenium to selenoproteins: synthesis, identity, and their role in human health
    • Papp L.V., Lu J., Holmgren A., and Khanna K.K. From selenium to selenoproteins: synthesis, identity, and their role in human health. Antioxid. Redox. Signal. 9 (2007) 775-806
    • (2007) Antioxid. Redox. Signal. , vol.9 , pp. 775-806
    • Papp, L.V.1    Lu, J.2    Holmgren, A.3    Khanna, K.K.4
  • 41
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl M.W. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic. Acids. Res. 29 (2001) e45
    • (2001) Nucleic. Acids. Res. , vol.29
    • Pfaffl, M.W.1
  • 42
    • 27744490852 scopus 로고    scopus 로고
    • HDACs and the senescent phenotype of WI-38 cells
    • Place R.F., Noonan E.J., and Giardina C. HDACs and the senescent phenotype of WI-38 cells. BMC Cell Biol. 6 (2005) 37
    • (2005) BMC Cell Biol. , vol.6 , pp. 37
    • Place, R.F.1    Noonan, E.J.2    Giardina, C.3
  • 43
    • 0142058235 scopus 로고    scopus 로고
    • Transcription factor Nrf2 activation by inorganic arsenic in cultured keratinocytes: involvement of hydrogen peroxide
    • Pi J., Qu W., Reece J.M., Kumagai Y., and Waalkes M.P. Transcription factor Nrf2 activation by inorganic arsenic in cultured keratinocytes: involvement of hydrogen peroxide. Exp. Cell. Res. 290 (2003) 234-245
    • (2003) Exp. Cell. Res. , vol.290 , pp. 234-245
    • Pi, J.1    Qu, W.2    Reece, J.M.3    Kumagai, Y.4    Waalkes, M.P.5
  • 44
    • 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., and Kim K. Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radic. Biol. Med. 38 (2005) 1543-1552
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 1543-1552
    • Rhee, S.G.1    Chae, H.Z.2    Kim, K.3
  • 45
    • 0035839624 scopus 로고    scopus 로고
    • The core promoter of human thioredoxin reductase 1: cloning, transcriptional activity, and Oct-1, Sp1, and Sp3 binding reveal a housekeeping-type promoter for the AU-rich element-regulated gene
    • Rundlof A.K., Carlsten M., and Arner E.S. The core promoter of human thioredoxin reductase 1: cloning, transcriptional activity, and Oct-1, Sp1, and Sp3 binding reveal a housekeeping-type promoter for the AU-rich element-regulated gene. J. Biol. Chem. 276 (2001) 30542-30551
    • (2001) J. Biol. Chem. , vol.276 , pp. 30542-30551
    • Rundlof, A.K.1    Carlsten, M.2    Arner, E.S.3
  • 47
    • 0036119737 scopus 로고    scopus 로고
    • High-throughput 96-well microplate assays for determining specific activities of glutathione peroxidase and thioredoxin reductase
    • Smith A.D., and Levander O.A. High-throughput 96-well microplate assays for determining specific activities of glutathione peroxidase and thioredoxin reductase. Methods Enzymol. 347 (2002) 113-121
    • (2002) Methods Enzymol. , vol.347 , pp. 113-121
    • Smith, A.D.1    Levander, O.A.2
  • 48
    • 0035312235 scopus 로고    scopus 로고
    • Selenium modifies the metabolism and toxicity of arsenic in primary rat hepatocytes
    • Styblo M., M., and Thomas D.J. Selenium modifies the metabolism and toxicity of arsenic in primary rat hepatocytes. Toxicol. Appl. Pharmacol. 172 (2001) 52-61
    • (2001) Toxicol. Appl. Pharmacol. , vol.172 , pp. 52-61
    • Styblo, M.1    M., Thomas, D.J.2
  • 50
    • 46249116457 scopus 로고    scopus 로고
    • Arsenic trioxide and auranofin inhibit selenoprotein synthesis: implications for chemotherapy for acute promyelocytic leukaemia
    • Talbot S., Nelson R., and Self W.T. Arsenic trioxide and auranofin inhibit selenoprotein synthesis: implications for chemotherapy for acute promyelocytic leukaemia. Br. J. Pharmacol. 154 (2008) 940-948
    • (2008) Br. J. Pharmacol. , vol.154 , pp. 940-948
    • Talbot, S.1    Nelson, R.2    Self, W.T.3
  • 53
    • 0021252067 scopus 로고
    • Arsenite-induced changes in methylation of the 70,000 dalton heat shock proteins in chicken embryo fibroblasts
    • Wang C., and Lazarides E. Arsenite-induced changes in methylation of the 70,000 dalton heat shock proteins in chicken embryo fibroblasts. Biochem. Biophys. Res. Commun. 119 (1984) 735-743
    • (1984) Biochem. Biophys. Res. Commun. , vol.119 , pp. 735-743
    • Wang, C.1    Lazarides, E.2
  • 54
    • 33846134723 scopus 로고    scopus 로고
    • Trivalent arsenicals induce lipid peroxidation, protein carbonylation, and oxidative DNA damage in human urothelial cells
    • Wang T.C., Jan K.Y., Wang A.S., and Gurr J.R. Trivalent arsenicals induce lipid peroxidation, protein carbonylation, and oxidative DNA damage in human urothelial cells. Mutat. Res. 615 (2007) 75-86
    • (2007) Mutat. Res. , vol.615 , pp. 75-86
    • Wang, T.C.1    Jan, K.Y.2    Wang, A.S.3    Gurr, J.R.4
  • 55
    • 36049010730 scopus 로고    scopus 로고
    • Nrf2 protects human bladder urothelial cells from arsenite and monomethylarsonous acid toxicity
    • Wang X.J., Sun Z., Chen W., Eblin K.E., Gandolfi J.A., and Zhang D.D. Nrf2 protects human bladder urothelial cells from arsenite and monomethylarsonous acid toxicity. Toxicol. Appl. Pharmacol. 225 (2007) 206-213
    • (2007) Toxicol. Appl. Pharmacol. , vol.225 , pp. 206-213
    • Wang, X.J.1    Sun, Z.2    Chen, W.3    Eblin, K.E.4    Gandolfi, J.A.5    Zhang, D.D.6
  • 56
    • 39749177838 scopus 로고    scopus 로고
    • Targeting thioredoxin reductase 1 reduction in cancer cells inhibits self-sufficient growth and DNA replication
    • Yoo M.H., Xu X.M., Carlson B.A., Patterson A.D., Gladyshev V.N., and Hatfield D.L. Targeting thioredoxin reductase 1 reduction in cancer cells inhibits self-sufficient growth and DNA replication. PLoS. ONE. 2 (2007) e1112
    • (2007) PLoS. ONE. , vol.2
    • Yoo, M.H.1    Xu, X.M.2    Carlson, B.A.3    Patterson, A.D.4    Gladyshev, V.N.5    Hatfield, D.L.6
  • 57
    • 0345700812 scopus 로고    scopus 로고
    • Synergy between sulforaphane and selenium in the induction of thioredoxin reductase 1 requires both transcriptional and translational modulation
    • Zhang J., Svehlikova V., Bao Y., Howie A.F., Beckett G.J., and Williamson G. Synergy between sulforaphane and selenium in the induction of thioredoxin reductase 1 requires both transcriptional and translational modulation. Carcinogenesis 24 (2003) 497-503
    • (2003) Carcinogenesis , vol.24 , pp. 497-503
    • Zhang, J.1    Svehlikova, V.2    Bao, Y.3    Howie, A.F.4    Beckett, G.J.5    Williamson, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.