메뉴 건너뛰기




Volumn 46, Issue 12, 2009, Pages 1703-1707

Incorporation of 8-hydroxyguanosine (8-oxo-7,8-dihydroguanosine) 5′-triphosphate by bacterial and human RNA polymerases

Author keywords

8 Hydroxyguanosine 5 triphosphate; Free radicals; Oxidized ribonucleotide; RNA polymerase; Transcription

Indexed keywords

8 HYDROXYGUANOSINE (8 OXO 7,8 DIHYDROGUANOSINE) 5'' TRIPHOSPHATE; BACTERIAL DNA; DNA POLYMERASE; NUCLEIC ACID BASE; OLIGONUCLEOTIDE; PHOSPHATE; RIBONUCLEOTIDE; RIBONUCLEOTIDE, 2 HYDROXYADENOSINE 5'' TRIPHOSPHATE; RNA POLYMERASE; RNA POLYMERASE II; UNCLASSIFIED DRUG;

EID: 67349131535     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2009.04.005     Document Type: Article
Times cited : (16)

References (57)
  • 3
    • 0020508747 scopus 로고
    • Dietary carcinogens and anticarcinogens
    • Ames B.N. Dietary carcinogens and anticarcinogens. Science 221 (1983) 1256-1264
    • (1983) Science , vol.221 , pp. 1256-1264
    • Ames, B.N.1
  • 4
    • 0037440169 scopus 로고    scopus 로고
    • Mutagenic potentials of damaged nucleic acids produced by reactive oxygen/nitrogen species: approaches using synthetic oligonucleotides and nucleotides
    • Kamiya H. Mutagenic potentials of damaged nucleic acids produced by reactive oxygen/nitrogen species: approaches using synthetic oligonucleotides and nucleotides. Nucleic Acids Res. 31 (2003) 517-531
    • (2003) Nucleic Acids Res. , vol.31 , pp. 517-531
    • Kamiya, H.1
  • 5
    • 16544371202 scopus 로고    scopus 로고
    • Mutagenicities of 8-hydroxyguanine and 2-hydroxyadenine produced by reactive oxygen species
    • Kamiya H. Mutagenicities of 8-hydroxyguanine and 2-hydroxyadenine produced by reactive oxygen species. Biol. Pharm. Bull. 27 (2004) 475-479
    • (2004) Biol. Pharm. Bull. , vol.27 , pp. 475-479
    • Kamiya, H.1
  • 6
    • 51649086880 scopus 로고    scopus 로고
    • Oxidatively generated damage to the guanine moiety of DNA: mechanistic aspects and formation in cells
    • Cadet J., Douki T., and Ravanat J.L. Oxidatively generated damage to the guanine moiety of DNA: mechanistic aspects and formation in cells. Acc. Chem. Res. 41 (2008) 1075-1083
    • (2008) Acc. Chem. Res. , vol.41 , pp. 1075-1083
    • Cadet, J.1    Douki, T.2    Ravanat, J.L.3
  • 8
    • 0025891866 scopus 로고
    • NMR structural studies of the ionizing radiation adduct 7-hydro-8-oxodeoxyguanosine (8-oxo-7H-dG) opposite deoxyadenosine in a DNA duplex: 8-oxo-7H-dG(syn)·dA(anti) alignment at lesion site
    • Kouchakdjian M., Bodepudi V., Shibutani S., Eisenberg M., Johnson F., Grollman A.P., and Patel D.J. NMR structural studies of the ionizing radiation adduct 7-hydro-8-oxodeoxyguanosine (8-oxo-7H-dG) opposite deoxyadenosine in a DNA duplex: 8-oxo-7H-dG(syn)·dA(anti) alignment at lesion site. Biochemistry 30 (1991) 1403-1412
    • (1991) Biochemistry , vol.30 , pp. 1403-1412
    • Kouchakdjian, M.1    Bodepudi, V.2    Shibutani, S.3    Eisenberg, M.4    Johnson, F.5    Grollman, A.P.6    Patel, D.J.7
  • 9
    • 0028783875 scopus 로고
    • Influence of the oxidatively damaged adduct 8-oxodeoxyguanosine on the conformation, energetics, and thermodynamic stability of a DNA duplex
    • Plum G.E., Grollman A.P., Johnson F., and Breslauer K.J. Influence of the oxidatively damaged adduct 8-oxodeoxyguanosine on the conformation, energetics, and thermodynamic stability of a DNA duplex. Biochemistry 34 (1995) 16148-16160
    • (1995) Biochemistry , vol.34 , pp. 16148-16160
    • Plum, G.E.1    Grollman, A.P.2    Johnson, F.3    Breslauer, K.J.4
  • 10
    • 0028244511 scopus 로고
    • Synthesis and thermodynamic stabilities of damaged DNA involving 8-hydroxyguanine (7,8-dihydro-8-oxoguanine) in a ras gene fragment
    • Koizume S., Kamiya H., Inoue H., and Ohtsuka E. Synthesis and thermodynamic stabilities of damaged DNA involving 8-hydroxyguanine (7,8-dihydro-8-oxoguanine) in a ras gene fragment. Nucleosides Nucleotides 13 (1994) 1517-1534
    • (1994) Nucleosides Nucleotides , vol.13 , pp. 1517-1534
    • Koizume, S.1    Kamiya, H.2    Inoue, H.3    Ohtsuka, E.4
  • 11
    • 0025334691 scopus 로고
    • Mechanistic studies of ionizing radiation and oxidative mutagenesis: genetic effects of a single 8-hydroxyguanine (7-hydro-8-oxoguanine) residue inserted at a unique site in a viral genome
    • Wood M.L., Dizdaroglu M., Gajewski E., and Essigmann J.M. Mechanistic studies of ionizing radiation and oxidative mutagenesis: genetic effects of a single 8-hydroxyguanine (7-hydro-8-oxoguanine) residue inserted at a unique site in a viral genome. Biochemistry 29 (1990) 7024-7032
    • (1990) Biochemistry , vol.29 , pp. 7024-7032
    • Wood, M.L.1    Dizdaroglu, M.2    Gajewski, E.3    Essigmann, J.M.4
  • 12
    • 0026592966 scopus 로고
    • 8-Hydroxyguanine, an abundant form of oxidative DNA damage, causes G→T and A→C substitutions
    • Cheng K.C., Cahill D.S., Kasai H., Nishimura S., and Loeb L.A. 8-Hydroxyguanine, an abundant form of oxidative DNA damage, causes G→T and A→C substitutions. J. Biol. Chem. 267 (1992) 166-172
    • (1992) J. Biol. Chem. , vol.267 , pp. 166-172
    • Cheng, K.C.1    Cahill, D.S.2    Kasai, H.3    Nishimura, S.4    Loeb, L.A.5
  • 13
    • 0027215203 scopus 로고
    • Mutations in the mutY gene of Escherichia coli enhance the frequency of targeted G:C→T:A transversions induced by a single 8-oxoguanine residue in single-stranded DNA
    • Moriya M., and Grollman A.P. Mutations in the mutY gene of Escherichia coli enhance the frequency of targeted G:C→T:A transversions induced by a single 8-oxoguanine residue in single-stranded DNA. Mol. Gen. Genet. 239 (1993) 72-76
    • (1993) Mol. Gen. Genet. , vol.239 , pp. 72-76
    • Moriya, M.1    Grollman, A.P.2
  • 14
    • 0031056741 scopus 로고    scopus 로고
    • Leading versus lagging strand mutagenesis induced by 7,8-dihydro-8-oxo-2′-deoxyguanosine in E. coli
    • Wagner J., Kamiya H., and Fuchs R.P.P. Leading versus lagging strand mutagenesis induced by 7,8-dihydro-8-oxo-2′-deoxyguanosine in E. coli. J. Mol. Biol. 265 (1997) 302-309
    • (1997) J. Mol. Biol. , vol.265 , pp. 302-309
    • Wagner, J.1    Kamiya, H.2    Fuchs, R.P.P.3
  • 15
    • 0026650584 scopus 로고
    • c-Ha-ras containing 8-hydroxyguanine at codon 12 induces point mutations at the modified and adjacent positions
    • Kamiya H., Miura K., Ishikawa H., Inoue H., Nishimura S., and Ohtsuka E. c-Ha-ras containing 8-hydroxyguanine at codon 12 induces point mutations at the modified and adjacent positions. Cancer Res. 52 (1992) 3483-3485
    • (1992) Cancer Res. , vol.52 , pp. 3483-3485
    • Kamiya, H.1    Miura, K.2    Ishikawa, H.3    Inoue, H.4    Nishimura, S.5    Ohtsuka, E.6
  • 16
    • 0027399969 scopus 로고
    • Single-stranded shuttle phagemid for mutagenesis studies in mammalian cells: 8-oxoguanine in DNA induces targeted G·C→T·A transversions in simian kidney cells
    • Moriya M. Single-stranded shuttle phagemid for mutagenesis studies in mammalian cells: 8-oxoguanine in DNA induces targeted G·C→T·A transversions in simian kidney cells. Proc. Natl. Acad. Sci. USA 90 (1993) 1122-1126
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1122-1126
    • Moriya, M.1
  • 17
    • 0028944525 scopus 로고
    • 8-Hydroxyguanine (7,8-dihydro-8-oxoguanine) in hot spots of the c-Ha-ras gene: effects of sequence contexts on mutation spectra
    • Kamiya H., Murata-Kamiya N., Koizume S., Inoue H., Nishimura S., and Ohtsuka E. 8-Hydroxyguanine (7,8-dihydro-8-oxoguanine) in hot spots of the c-Ha-ras gene: effects of sequence contexts on mutation spectra. Carcinogenesis 16 (1995) 883-889
    • (1995) Carcinogenesis , vol.16 , pp. 883-889
    • Kamiya, H.1    Murata-Kamiya, N.2    Koizume, S.3    Inoue, H.4    Nishimura, S.5    Ohtsuka, E.6
  • 18
    • 0028848633 scopus 로고
    • Mutagenicity of a unique 8-oxoguanine in a human Ha-ras sequence in mammalian cells
    • Le Page F., Margot A., Grollman A.P., Sarasin A., and Gentil A. Mutagenicity of a unique 8-oxoguanine in a human Ha-ras sequence in mammalian cells. Carcinogenesis 16 (1995) 2779-2784
    • (1995) Carcinogenesis , vol.16 , pp. 2779-2784
    • Le Page, F.1    Margot, A.2    Grollman, A.P.3    Sarasin, A.4    Gentil, A.5
  • 19
    • 0033377611 scopus 로고    scopus 로고
    • Comparison of the mutagenic properties of 8-oxo-7,8-dihydro-2′-deoxyadenosine and 8-oxo-7,8-dihydro-2′-deoxyguanosine DNA lesions in mammalian cells
    • Tan X., Grollman A.P., and Shibutani S. Comparison of the mutagenic properties of 8-oxo-7,8-dihydro-2′-deoxyadenosine and 8-oxo-7,8-dihydro-2′-deoxyguanosine DNA lesions in mammalian cells. Carcinogenesis 20 (1999) 2287-2292
    • (1999) Carcinogenesis , vol.20 , pp. 2287-2292
    • Tan, X.1    Grollman, A.P.2    Shibutani, S.3
  • 20
    • 0032080121 scopus 로고    scopus 로고
    • Induction of chromosomal gene mutations in Escherichia coli by direct incorporation of oxidatively damaged nucleotides
    • Inoue M., Kamiya H., Fujikawa K., Ootsuyama Y., Murata-Kamiya N., Osaki T., Yasumoto K., and Kasai H. Induction of chromosomal gene mutations in Escherichia coli by direct incorporation of oxidatively damaged nucleotides. J. Biol. Chem. 273 (1998) 11069-11074
    • (1998) J. Biol. Chem. , vol.273 , pp. 11069-11074
    • Inoue, M.1    Kamiya, H.2    Fujikawa, K.3    Ootsuyama, Y.4    Murata-Kamiya, N.5    Osaki, T.6    Yasumoto, K.7    Kasai, H.8
  • 22
    • 30744470374 scopus 로고    scopus 로고
    • The Nudix hydrolase superfamily
    • McLennan A.G. The Nudix hydrolase superfamily. Cell. Mol. Life Sci. 63 (2006) 123-143
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 123-143
    • McLennan, A.G.1
  • 23
    • 85009806203 scopus 로고    scopus 로고
    • Mutations induced by oxidized DNA precursors and their prevention by nucleotide pool sanitization enzymes
    • Kamiya H. Mutations induced by oxidized DNA precursors and their prevention by nucleotide pool sanitization enzymes. Genes Environ. 29 (2007) 133-140
    • (2007) Genes Environ. , vol.29 , pp. 133-140
    • Kamiya, H.1
  • 24
    • 42449137498 scopus 로고    scopus 로고
    • Trace amounts of 8-oxo-dGTP in mitochondrial dNTP pools reduce DNA polymerase γ replication fidelity
    • Pursell Z.F., McDonald J.T., Mathews C.K., and Kunkel T.A. Trace amounts of 8-oxo-dGTP in mitochondrial dNTP pools reduce DNA polymerase γ replication fidelity. Nucleic Acids Res. 36 (2008) 2174-2181
    • (2008) Nucleic Acids Res. , vol.36 , pp. 2174-2181
    • Pursell, Z.F.1    McDonald, J.T.2    Mathews, C.K.3    Kunkel, T.A.4
  • 26
    • 0015524054 scopus 로고
    • Biochemistry of deoxyribonucleic acid-defective amber mutants of bacteriophage T4. 3. Nucleotide pools
    • Mathews C.K. Biochemistry of deoxyribonucleic acid-defective amber mutants of bacteriophage T4. 3. Nucleotide pools. J. Biol. Chem. 247 (1972) 7430-7438
    • (1972) J. Biol. Chem. , vol.247 , pp. 7430-7438
    • Mathews, C.K.1
  • 27
    • 0028143584 scopus 로고
    • Physiological concentrations of purines and pyrimidines
    • Traut T.W. Physiological concentrations of purines and pyrimidines. Mol. Cell. Biochem. 140 (1994) 1-22
    • (1994) Mol. Cell. Biochem. , vol.140 , pp. 1-22
    • Traut, T.W.1
  • 28
  • 31
    • 0142186288 scopus 로고    scopus 로고
    • Transcription elongation factor S-II maintains transcriptional fidelity and confers oxidative stress resistance
    • Koyama H., Ito T., Nakanishi T., Kawamura N., and Sekimizu K. Transcription elongation factor S-II maintains transcriptional fidelity and confers oxidative stress resistance. Genes Cells 8 (2003) 779-788
    • (2003) Genes Cells , vol.8 , pp. 779-788
    • Koyama, H.1    Ito, T.2    Nakanishi, T.3    Kawamura, N.4    Sekimizu, K.5
  • 32
    • 0037283774 scopus 로고    scopus 로고
    • A rapid purification method for human RNA polymerase II by two-step affinity chromatography
    • Hasegawa J., Endou M., Narita T., Yamada T., Yamaguchi Y., Wada T., and Handa H. A rapid purification method for human RNA polymerase II by two-step affinity chromatography. J. Biochem. 133 (2003) 133-138
    • (2003) J. Biochem. , vol.133 , pp. 133-138
    • Hasegawa, J.1    Endou, M.2    Narita, T.3    Yamada, T.4    Yamaguchi, Y.5    Wada, T.6    Handa, H.7
  • 33
    • 0032113494 scopus 로고    scopus 로고
    • Crucial role of the RNA:DNA hybrid in the processivity of transcription
    • Sidorenkov I., Komissarova N., and Kashlev M. Crucial role of the RNA:DNA hybrid in the processivity of transcription. Mol. Cell 2 (1998) 55-64
    • (1998) Mol. Cell , vol.2 , pp. 55-64
    • Sidorenkov, I.1    Komissarova, N.2    Kashlev, M.3
  • 34
    • 0034051171 scopus 로고    scopus 로고
    • The 8-nucleotide-long RNA:DNA hybrid is a primary stability determinant of the RNA polymerase II elongation complex
    • Kireeva M.L., Komissarova N., Waugh D.S., and Kashlev M. The 8-nucleotide-long RNA:DNA hybrid is a primary stability determinant of the RNA polymerase II elongation complex. J. Biol. Chem. 275 (2000) 6530-6536
    • (2000) J. Biol. Chem. , vol.275 , pp. 6530-6536
    • Kireeva, M.L.1    Komissarova, N.2    Waugh, D.S.3    Kashlev, M.4
  • 36
    • 33749681925 scopus 로고    scopus 로고
    • A mechanism of nucleotide misincorporation during transcription due to template-strand misalignment
    • Pomerantz R.T., Temiakov D., Anikin M., Vassylyev D.G., and McAllister W.T. A mechanism of nucleotide misincorporation during transcription due to template-strand misalignment. Mol. Cell 24 (2006) 245-255
    • (2006) Mol. Cell , vol.24 , pp. 245-255
    • Pomerantz, R.T.1    Temiakov, D.2    Anikin, M.3    Vassylyev, D.G.4    McAllister, W.T.5
  • 38
    • 34250698885 scopus 로고    scopus 로고
    • Hepatitis delta antigen binds to the clamp of RNA polymerase II and affects transcriptional fidelity
    • Yamaguchi Y., Mura T., Chanarat S., Okamoto S., and Handa H. Hepatitis delta antigen binds to the clamp of RNA polymerase II and affects transcriptional fidelity. Genes Cells 12 (2007) 863-875
    • (2007) Genes Cells , vol.12 , pp. 863-875
    • Yamaguchi, Y.1    Mura, T.2    Chanarat, S.3    Okamoto, S.4    Handa, H.5
  • 39
    • 0029133347 scopus 로고
    • Formation of 2-hydroxydeoxyadenosine triphosphate, an oxidatively damaged nucleotide, and its incorporation by DNA polymerases
    • Kamiya H., and Kasai H. Formation of 2-hydroxydeoxyadenosine triphosphate, an oxidatively damaged nucleotide, and its incorporation by DNA polymerases. J. Biol. Chem. 270 (1995) 19446-19450
    • (1995) J. Biol. Chem. , vol.270 , pp. 19446-19450
    • Kamiya, H.1    Kasai, H.2
  • 40
    • 0034622582 scopus 로고    scopus 로고
    • Two DNA polymerases of Escherichia coli display distinct misinsertion specificities for 2-hydroxy-dATP during DNA synthesis
    • Kamiya H., Maki H., and Kasai H. Two DNA polymerases of Escherichia coli display distinct misinsertion specificities for 2-hydroxy-dATP during DNA synthesis. Biochemistry 39 (2000) 9508-9513
    • (2000) Biochemistry , vol.39 , pp. 9508-9513
    • Kamiya, H.1    Maki, H.2    Kasai, H.3
  • 41
    • 0020445220 scopus 로고
    • Selective expansion of mitochondrial nucleoside triphosphate pools in antimetabolite-treated HeLa cells
    • Bestwick R.K., Moffett G.L., and Mathews C.K. Selective expansion of mitochondrial nucleoside triphosphate pools in antimetabolite-treated HeLa cells. J. Biol. Chem. 257 (1982) 9300-9304
    • (1982) J. Biol. Chem. , vol.257 , pp. 9300-9304
    • Bestwick, R.K.1    Moffett, G.L.2    Mathews, C.K.3
  • 42
    • 17844405031 scopus 로고    scopus 로고
    • Multiple enzyme activities of Escherichia coli MutT protein for sanitization of DNA and RNA precursor pools
    • Ito R., Hayakawa H., Sekiguchi M., and Ishibashi T. Multiple enzyme activities of Escherichia coli MutT protein for sanitization of DNA and RNA precursor pools. Biochemistry 44 (2005) 6670-6674
    • (2005) Biochemistry , vol.44 , pp. 6670-6674
    • Ito, R.1    Hayakawa, H.2    Sekiguchi, M.3    Ishibashi, T.4
  • 43
    • 0026513966 scopus 로고
    • MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis
    • Maki H., and Sekiguchi M. MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis. Nature 355 (1992) 273-275
    • (1992) Nature , vol.355 , pp. 273-275
    • Maki, H.1    Sekiguchi, M.2
  • 45
    • 0035830851 scopus 로고    scopus 로고
    • Fidelity of nucleotide insertion at 8-oxo-7,8-dihydroguanine by mammalian DNA polymerase δ: steady-state and pre-steady-state kinetic analysis
    • Einolf H.J., and Guengerich F.P. Fidelity of nucleotide insertion at 8-oxo-7,8-dihydroguanine by mammalian DNA polymerase δ: steady-state and pre-steady-state kinetic analysis. J. Biol. Chem. 276 (2001) 3764-3771
    • (2001) J. Biol. Chem. , vol.276 , pp. 3764-3771
    • Einolf, H.J.1    Guengerich, F.P.2
  • 46
    • 0027469856 scopus 로고
    • Effects of DNA lesions on transcription elongation by T7 RNA polymerase
    • Chen Y.H., and Bogenhagen D.F. Effects of DNA lesions on transcription elongation by T7 RNA polymerase. J. Biol. Chem. 268 (1993) 5849-5855
    • (1993) J. Biol. Chem. , vol.268 , pp. 5849-5855
    • Chen, Y.H.1    Bogenhagen, D.F.2
  • 47
    • 0032516880 scopus 로고    scopus 로고
    • Effects of nonbulky DNA base damages on Escherichia coli RNA polymerase-mediated elongation and promoter clearance
    • Viswanathan A., and Doetsch P.W. Effects of nonbulky DNA base damages on Escherichia coli RNA polymerase-mediated elongation and promoter clearance. J. Biol. Chem. 273 (1998) 21276-21281
    • (1998) J. Biol. Chem. , vol.273 , pp. 21276-21281
    • Viswanathan, A.1    Doetsch, P.W.2
  • 48
    • 0037470158 scopus 로고    scopus 로고
    • Effects of endogenous DNA base lesions on transcription elongation by mammalian RNA polymerase II: implications for transcription-coupled DNA repair and transcriptional mutagenesis
    • Kuraoka I., Endou M., Yamaguchi Y., Wada T., Handa H., and Tanaka K. Effects of endogenous DNA base lesions on transcription elongation by mammalian RNA polymerase II: implications for transcription-coupled DNA repair and transcriptional mutagenesis. J. Biol. Chem. 278 (2003) 7294-7299
    • (2003) J. Biol. Chem. , vol.278 , pp. 7294-7299
    • Kuraoka, I.1    Endou, M.2    Yamaguchi, Y.3    Wada, T.4    Handa, H.5    Tanaka, K.6
  • 49
    • 1842685197 scopus 로고    scopus 로고
    • Effect of 8-oxoguanine on transcription elongation by T7 RNA polymerase and mammalian RNA polymerase II
    • Tornaletti S., Maeda L.S., Kolodner R.D., and Hanawalt P.C. Effect of 8-oxoguanine on transcription elongation by T7 RNA polymerase and mammalian RNA polymerase II. DNA Repair (Amsterdam) 3 (2004) 483-494
    • (2004) DNA Repair (Amsterdam) , vol.3 , pp. 483-494
    • Tornaletti, S.1    Maeda, L.S.2    Kolodner, R.D.3    Hanawalt, P.C.4
  • 52
    • 0035928817 scopus 로고    scopus 로고
    • Specific binding of 8-oxoguanine-containing RNA to polynucleotide phosphorylase protein
    • Hayakawa H., Kuwano M., and Sekiguchi M. Specific binding of 8-oxoguanine-containing RNA to polynucleotide phosphorylase protein. Biochemistry 40 (2001) 9977-9982
    • (2001) Biochemistry , vol.40 , pp. 9977-9982
    • Hayakawa, H.1    Kuwano, M.2    Sekiguchi, M.3
  • 54
    • 33744752455 scopus 로고    scopus 로고
    • Human polynucleotide phosphorylase protein in response to oxidative stress
    • Hayakawa H., and Sekiguchi M. Human polynucleotide phosphorylase protein in response to oxidative stress. Biochemistry 45 (2006) 6749-6755
    • (2006) Biochemistry , vol.45 , pp. 6749-6755
    • Hayakawa, H.1    Sekiguchi, M.2
  • 55
    • 44649097525 scopus 로고    scopus 로고
    • Human polynucleotide phosphorylase reduces oxidative RNA damage and protects HeLa cell against oxidative stress
    • Wu J., and Li Z. Human polynucleotide phosphorylase reduces oxidative RNA damage and protects HeLa cell against oxidative stress. Biochem. Biophys. Res. Commun. 372 (2008) 288-292
    • (2008) Biochem. Biophys. Res. Commun. , vol.372 , pp. 288-292
    • Wu, J.1    Li, Z.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.