메뉴 건너뛰기




Volumn 4, Issue 1, 2006, Pages 0025-0042

Stepwise translocation of Dpo4 polymerase during error-free bypass of an oxoG lesion

Author keywords

[No Author keywords available]

Indexed keywords

8 HYDROXYGUANINE; DEOXYCYTIDINE TRIPHOSPHATE; DNA POLYMERASE; DNA POLYMERASE 4; NUCLEIC ACID BASE; NUCLEOTIDE; PRIMER DNA; UNCLASSIFIED DRUG;

EID: 31144460784     PISSN: 15457885     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.0040011     Document Type: Article
Times cited : (130)

References (46)
  • 1
    • 21244506437 scopus 로고    scopus 로고
    • Eukaryotic translesion synthesis DNA polymerases: Specificity of structure and function
    • Prakash S, Johnson RE, Prakash L (2005) Eukaryotic translesion synthesis DNA polymerases: Specificity of structure and function. Annu Rev Biochem 74: 317-353.
    • (2005) Annu Rev Biochem , vol.74 , pp. 317-353
    • Prakash, S.1    Johnson, R.E.2    Prakash, L.3
  • 2
    • 10044241865 scopus 로고    scopus 로고
    • Functions of DNA polymerases
    • Bebenek K, Kunkel TA (2004) Functions of DNA polymerases. Adv Protein Chem 69: 137-165.
    • (2004) Adv Protein Chem , vol.69 , pp. 137-165
    • Bebenek, K.1    Kunkel, T.A.2
  • 3
    • 1942439667 scopus 로고    scopus 로고
    • Switching from high-fidelity replicases to low-fidelity lesion-bypass polymerases
    • Plosky BS, Woodgate R (2004) Switching from high-fidelity replicases to low-fidelity lesion-bypass polymerases. Curr Opin Genet Dev 14: 113-119.
    • (2004) Curr Opin Genet Dev , vol.14 , pp. 113-119
    • Plosky, B.S.1    Woodgate, R.2
  • 4
    • 19444383801 scopus 로고    scopus 로고
    • Trading places: How do DNA polymerases switch during translesion DNA synthesis?
    • Friedberg EC, Lehmann AR, Fuchs RP (2005) Trading places: How do DNA polymerases switch during translesion DNA synthesis? Mol Cell 18: 499-505.
    • (2005) Mol Cell , vol.18 , pp. 499-505
    • Friedberg, E.C.1    Lehmann, A.R.2    Fuchs, R.P.3
  • 5
    • 0035812849 scopus 로고    scopus 로고
    • Crystal structure of a Y-family DNA polymerase in action: A mechanism for error-prone and lesion-bypass replication
    • Ling H, Boudsocq F, Woodgate R, Yang W (2001) Crystal structure of a Yfamily DNA polymerase in action: A mechanism for error-prone and lesion-bypass replication. Cell 107: 91-102.
    • (2001) Cell , vol.107 , pp. 91-102
    • Ling, H.1    Boudsocq, F.2    Woodgate, R.3    Yang, W.4
  • 6
    • 0034762679 scopus 로고    scopus 로고
    • Crystal structure of a DinB family error-prone DNA polymerase from Sulfolobus solfataricus
    • Silvian LF, Toth EA, Pham P, Goodman MF, Ellenberger T (2001) Crystal structure of a DinB family error-prone DNA polymerase from Sulfolobus solfataricus. Nat Struct Biol 8: 984-989.
    • (2001) Nat Struct Biol , vol.8 , pp. 984-989
    • Silvian, L.F.1    Toth, E.A.2    Pham, P.3    Goodman, M.F.4    Ellenberger, T.5
  • 7
    • 0034847259 scopus 로고    scopus 로고
    • Structure of the catalytic core of S. cerevisiae DNA polymerase eta: Implications for translesion DNA synthesis
    • Trincao J, Johnson RE, Escalante CR, Prakash S, Prakash L, et al. (2001) Structure of the catalytic core of S. cerevisiae DNA polymerase eta: Implications for translesion DNA synthesis. Mol Cell 8: 417-426.
    • (2001) Mol Cell , vol.8 , pp. 417-426
    • Trincao, J.1    Johnson, R.E.2    Escalante, C.R.3    Prakash, S.4    Prakash, L.5
  • 8
    • 3142674288 scopus 로고    scopus 로고
    • Replication by human DNA polymerase-iota occurs by Hoogsteen base-pairing
    • Nair DT, Johnson RE, Prakash S, Prakash L, Aggarwal AK (2004) Replication by human DNA polymerase-iota occurs by Hoogsteen base-pairing. Nature 430: 377-380.
    • (2004) Nature , vol.430 , pp. 377-380
    • Nair, D.T.1    Johnson, R.E.2    Prakash, S.3    Prakash, L.4    Aggarwal, A.K.5
  • 9
    • 4143116647 scopus 로고    scopus 로고
    • Crystal structure of the catalytic core of human DNA polymerase kappa
    • Camb
    • Uljon SN, Johnson RE, Edwards TA, Prakash S, Prakash L, et al. (2004) Crystal structure of the catalytic core of human DNA polymerase kappa. Structure (Camb) 12: 1395-1404.
    • (2004) Structure , vol.12 , pp. 1395-1404
    • Uljon, S.N.1    Johnson, R.E.2    Edwards, T.A.3    Prakash, S.4    Prakash, L.5
  • 10
    • 0041864009 scopus 로고    scopus 로고
    • Replication of a cis-syn thymine dimer at atomic resolution
    • Ling H, Boudsocq F, Plosky BS, Woodgate R, Yang W (2003) Replication of a cis-syn thymine dimer at atomic resolution. Nature 424: 1083-1087.
    • (2003) Nature , vol.424 , pp. 1083-1087
    • Ling, H.1    Boudsocq, F.2    Plosky, B.S.3    Woodgate, R.4    Yang, W.5
  • 11
    • 1442355023 scopus 로고    scopus 로고
    • Crystal structure of a benzo[a]pyrene diol epoxide adduct in a ternary complex with a DNA polymerase
    • U S A
    • Ling H, Sayer JM, Plosky BS, Yagi H, Boudsocq F, et al. (2004) Crystal structure of a benzo[a]pyrene diol epoxide adduct in a ternary complex with a DNA polymerase. Proc Natl Acad Sci U S A 101: 2265-2269.
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 2265-2269
    • Ling, H.1    Sayer, J.M.2    Plosky, B.S.3    Yagi, H.4    Boudsocq, F.5
  • 12
    • 1642382214 scopus 로고    scopus 로고
    • Snapshots of replication through an abasic lesion; structural basis for base substitutions and frameshifts
    • Ling H, Boudsocq F, Woodgate R, Yang W (2004) Snapshots of replication through an abasic lesion; structural basis for base substitutions and frameshifts. Mol Cell 13: 751-762.
    • (2004) Mol Cell , vol.13 , pp. 751-762
    • Ling, H.1    Boudsocq, F.2    Woodgate, R.3    Yang, W.4
  • 14
    • 23844454020 scopus 로고    scopus 로고
    • DNA adduct bypass polymerization by Sulfolobus solfataricus DNA polymerase Dpo4. Analysis and crystal structures of multiple base-pair substitution and frameshift products with the adduct 1,N2-ethenoguanine
    • Zang H, Goodenough AK, Choi JY, Irimia A, Loukachevitch LV, et al. (2005) DNA adduct bypass polymerization by Sulfolobus solfataricus DNA polymerase Dpo4. Analysis and crystal structures of multiple base-pair substitution and frameshift products with the adduct 1,N2-ethenoguanine. J Biol Chem 280: 29750-29764.
    • (2005) J Biol Chem , vol.280 , pp. 29750-29764
    • Zang, H.1    Goodenough, A.K.2    Choi, J.Y.3    Irimia, A.4    Loukachevitch, L.V.5
  • 15
    • 27144542782 scopus 로고    scopus 로고
    • Fidelity of Dpo4: Effect of metal ions, nucleotide selection and pyrophosphorolysis
    • Vaisman A, Ling H, Woodgate R, Yang W (2005) Fidelity of Dpo4: Effect of metal ions, nucleotide selection and pyrophosphorolysis. EMBO J 24: 2957-2967.
    • (2005) EMBO J , vol.24 , pp. 2957-2967
    • Vaisman, A.1    Ling, H.2    Woodgate, R.3    Yang, W.4
  • 16
    • 1642524959 scopus 로고    scopus 로고
    • Accuracy, lesion bypass, strand displacement and translocation by DNA polymerases
    • Steitz TA, Yin YW (2004) Accuracy, lesion bypass, strand displacement and translocation by DNA polymerases. Philos Trans R Soc Lond B Biol Sci 359: 17-23.
    • (2004) Philos Trans R Soc Lond B Biol Sci , vol.359 , pp. 17-23
    • Steitz, T.A.1    Yin, Y.W.2
  • 17
    • 0027220197 scopus 로고
    • Conformational coupling in DNA polymerase fidelity
    • Johnson KA (1993) Conformational coupling in DNA polymerase fidelity. Annu Rev Biochem 62: 685-713.
    • (1993) Annu Rev Biochem , vol.62 , pp. 685-713
    • Johnson, K.A.1
  • 18
    • 2342484512 scopus 로고    scopus 로고
    • Lesion (in)tolerance reveals insights into DNA replication fidelity
    • Freisinger E, Grollman AP, Miller H, Kisker C (2004) Lesion (in)tolerance reveals insights into DNA replication fidelity. EMBO J 23: 1494-1505.
    • (2004) EMBO J , vol.23 , pp. 1494-1505
    • Freisinger, E.1    Grollman, A.P.2    Miller, H.3    Kisker, C.4
  • 19
    • 9244229513 scopus 로고    scopus 로고
    • Crystal structures of 2-acetylaminofluorene and 2-aminofluorene in complex with T7 DNA polymerase reveal mechanisms of mutagenesis
    • U S A
    • Dutta S, Li Y, Johnson D, Dzantiev L, Richardson CC, et al. (2004) Crystal structures of 2-acetylaminofluorene and 2-aminofluorene in complex with T7 DNA polymerase reveal mechanisms of mutagenesis. Proc Natl Acad Sci U S A 101: 16186-16191.
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 16186-16191
    • Dutta, S.1    Li, Y.2    Johnson, D.3    Dzantiev, L.4    Richardson, C.C.5
  • 20
    • 3543002207 scopus 로고    scopus 로고
    • Nucleotide insertion opposite a cis-syn thymine dimer by a replicative DNA polymerase from bacteriophage T7
    • Li Y, Dutta S, Doublie S, Bdour HM, Taylor JS, et al. (2004) Nucleotide insertion opposite a cis-syn thymine dimer by a replicative DNA polymerase from bacteriophage T7. Nat Struct Mol Biol 11: 784-790.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 784-790
    • Li, Y.1    Dutta, S.2    Doublie, S.3    Bdour, H.M.4    Taylor, J.S.5
  • 21
    • 1642588255 scopus 로고    scopus 로고
    • Structures of mismatch replication errors observed in a DNA polymerase
    • Johnson SJ, Beese LS (2004) Structures of mismatch replication errors observed in a DNA polymerase. Cell 116: 803-816.
    • (2004) Cell , vol.116 , pp. 803-816
    • Johnson, S.J.1    Beese, L.S.2
  • 22
    • 0037310493 scopus 로고    scopus 로고
    • Damage repair DNA polymerases Y
    • Yang W (2003) Damage repair DNA polymerases Y. Curr Opin Struct Biol 13: 23-30.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 23-30
    • Yang, W.1
  • 23
    • 0035966270 scopus 로고    scopus 로고
    • Yeast DNA polymerase eta utilizes an induced-fit mechanism of nucleotide incorporation
    • Washington MT, Prakash L, Prakash S (2001) Yeast DNA polymerase eta utilizes an induced-fit mechanism of nucleotide incorporation. Cell 107: 917-927.
    • (2001) Cell , vol.107 , pp. 917-927
    • Washington, M.T.1    Prakash, L.2    Prakash, S.3
  • 24
    • 1242307762 scopus 로고    scopus 로고
    • Mechanism of DNA polymerization catalyzed by Sulfolobus solfataricus P2 DNA polymerase IV
    • Fiala KA, Suo Z (2004) Mechanism of DNA polymerization catalyzed by Sulfolobus solfataricus P2 DNA polymerase IV. Biochemistry 43: 2116-2125.
    • (2004) Biochemistry , vol.43 , pp. 2116-2125
    • Fiala, K.A.1    Suo, Z.2
  • 25
    • 0034857266 scopus 로고    scopus 로고
    • Crystal structure of a DinB lesion bypass DNA polymerase catalytic fragment reveals a classic polymerase catalytic domain
    • Zhou BL, Pata JD, Steitz TA (2001) Crystal structure of a DinB lesion bypass DNA polymerase catalytic fragment reveals a classic polymerase catalytic domain. Mol Cell 8: 427-437.
    • (2001) Mol Cell , vol.8 , pp. 427-437
    • Zhou, B.L.1    Pata, J.D.2    Steitz, T.A.3
  • 27
    • 0344154463 scopus 로고    scopus 로고
    • Oxidative damage to DNA: Formation, measurement and biochemical features
    • Cadet J, Douki T, Gasparutto D, Ravanat JL (2003) Oxidative damage to DNA: Formation, measurement and biochemical features. Mutat Res 531: 5-23.
    • (2003) Mutat Res , vol.531 , pp. 5-23
    • Cadet, J.1    Douki, T.2    Gasparutto, D.3    Ravanat, J.L.4
  • 28
    • 0034031811 scopus 로고    scopus 로고
    • Review article: Chronic inflammation and reactive oxygen and nitrogen metabolism - Implications in DNA damage and mutagenesis
    • Grisham MB, Jourd'heuil D, Wink DA (2000) Review article: Chronic inflammation and reactive oxygen and nitrogen metabolism - Implications in DNA damage and mutagenesis. Aliment Pharmacol Ther 14: 3-9.
    • (2000) Aliment Pharmacol Ther , vol.14 , pp. 3-9
    • Grisham, M.B.1    Jourd'heuil, D.2    Wink, D.A.3
  • 29
    • 0025981359 scopus 로고
    • Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG
    • Shibutani S, Takeshita M, Grollman AP (1991) Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG. Nature 349: 431-434.
    • (1991) Nature , vol.349 , pp. 431-434
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 30
    • 0032558424 scopus 로고    scopus 로고
    • Steady-state and pre-steady-state kinetic analysis of 8-oxo-7,8-dihydroguanosine triphosphate incorporation and extension by replicative and repair DNA polymerases
    • Einolf HJ, Schnetz-Boutaud N, Guengerich FP (1998) Steady-state and pre-steady-state kinetic analysis of 8-oxo-7,8-dihydroguanosine triphosphate incorporation and extension by replicative and repair DNA polymerases. Biochemistry 37: 13300-13312.
    • (1998) Biochemistry , vol.37 , pp. 13300-13312
    • Einolf, H.J.1    Schnetz-Boutaud, N.2    Guengerich, F.P.3
  • 31
    • 0035830851 scopus 로고    scopus 로고
    • Fidelity of nucleotide insertion at 8-oxo-7,8-dihydroguanine by mammalian DNA polymerase delta. Steady-state and pre-steady-state kinetic analysis
    • Einolf HJ, Guengerich FP (2001) Fidelity of nucleotide insertion at 8-oxo-7,8-dihydroguanine by mammalian DNA polymerase delta. Steady-state and pre-steady-state kinetic analysis. J Biol Chem 276: 3764-3771.
    • (2001) J Biol Chem , vol.276 , pp. 3764-3771
    • Einolf, H.J.1    Guengerich, F.P.2
  • 32
    • 0034425754 scopus 로고    scopus 로고
    • Efficient and accurate replication in the presence of 7,8-dihydro-8-oxoguanine by DNA polymerase eta
    • Haracska L, Yu SL, Johnson RE, Prakash L, Prakash S (2000) Efficient and accurate replication in the presence of 7,8-dihydro-8-oxoguanine by DNA polymerase eta. Nat Genet 25: 458-461.
    • (2000) Nat Genet , vol.25 , pp. 458-461
    • Haracska, L.1    Yu, S.L.2    Johnson, R.E.3    Prakash, L.4    Prakash, S.5
  • 33
    • 0037227566 scopus 로고    scopus 로고
    • Structure of DNA polymerase beta with the mutagenic DNA lesion 8-oxodeoxyguanine reveals structural insights into its coding potential
    • Camb
    • Krahn JM, Beard WA, Miller H, Grollman AP, Wilson SH (2003) Structure of DNA polymerase beta with the mutagenic DNA lesion 8-oxodeoxyguanine reveals structural insights into its coding potential. Structure (Camb) 11: 121-127.
    • (2003) Structure , vol.11 , pp. 121-127
    • Krahn, J.M.1    Beard, W.A.2    Miller, H.3    Grollman, A.P.4    Wilson, S.H.5
  • 34
    • 4644259458 scopus 로고    scopus 로고
    • Structural basis for the dual coding potential of 8-oxoguanosine by a high-fidelity DNA polymerase
    • Brieba LG, Eichman BF, Kokoska RJ, Doublie S, Kunkel TA, et al. (2004) Structural basis for the dual coding potential of 8-oxoguanosine by a high-fidelity DNA polymerase. EMBO J 23: 3452-3461.
    • (2004) EMBO J , vol.23 , pp. 3452-3461
    • Brieba, L.G.1    Eichman, B.F.2    Kokoska, R.J.3    Doublie, S.4    Kunkel, T.A.5
  • 35
    • 4544273926 scopus 로고    scopus 로고
    • Error-prone replication of oxidatively damaged DNA by a high-fidelity DNA polymerase
    • Hsu GW, Ober M, Carell T, Beese LS (2004) Error-prone replication of oxidatively damaged DNA by a high-fidelity DNA polymerase. Nature 431: 217-221.
    • (2004) Nature , vol.431 , pp. 217-221
    • Hsu, G.W.1    Ober, M.2    Carell, T.3    Beese, L.S.4
  • 36
    • 0035890599 scopus 로고    scopus 로고
    • Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4): An archaeal DinB-like DNA polymerase with lesion-bypass properties akin to eukaryotic pol eta
    • Boudsocq F, Iwai S, Hanaoka F, Woodgate R (2001) Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4): An archaeal DinB-like DNA polymerase with lesion-bypass properties akin to eukaryotic pol eta. Nucleic Acids Res 29: 4607-4616.
    • (2001) Nucleic Acids Res , vol.29 , pp. 4607-4616
    • Boudsocq, F.1    Iwai, S.2    Hanaoka, F.3    Woodgate, R.4
  • 37
    • 0037388383 scopus 로고    scopus 로고
    • Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations
    • U S A
    • Johnson SJ, Taylor JS, Beese LS (2003) Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations. Proc Natl Acad Sci U S A 100: 3895-3900.
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 3895-3900
    • Johnson, S.J.1    Taylor, J.S.2    Beese, L.S.3
  • 38
    • 0030918969 scopus 로고    scopus 로고
    • Analysis of nucleotide insertion and extension at 8-oxo-7,8- dihydroguanine by replicative T7 polymerase exo-and human immunodeficiency virus-1 reverse transcriptase using steady-state and pre-steady-state kinetics
    • Furge LL, Guengerich FP (1997) Analysis of nucleotide insertion and extension at 8-oxo-7,8-dihydroguanine by replicative T7 polymerase exo-and human immunodeficiency virus-1 reverse transcriptase using steady-state and pre-steady-state kinetics. Biochemistry 36: 6475-6487.
    • (1997) Biochemistry , vol.36 , pp. 6475-6487
    • Furge, L.L.1    Guengerich, F.P.2
  • 39
    • 0033059505 scopus 로고    scopus 로고
    • "Action-at-a-distance" mutagenesis. 8-oxo-7, 8-dihydro-2′-deoxyguanosine causes base substitution errors at neighboring template sites when copied by DNA polymerase beta
    • Efrati E, Tocco G, Eritja R, Wilson SH, Goodman MF (1999) "Action-at-adistance" mutagenesis. 8-oxo-7, 8-dihydro-2′- deoxyguanosine causes base substitution errors at neighboring template sites when copied by DNA polymerase beta. J Biol Chem 274: 15920-15926.
    • (1999) J Biol Chem , vol.274 , pp. 15920-15926
    • Efrati, E.1    Tocco, G.2    Eritja, R.3    Wilson, S.H.4    Goodman, M.F.5
  • 40
    • 0030930760 scopus 로고    scopus 로고
    • Crystal structures of human DNA polymerase beta complexed with gapped and nicked DNA: Evidence for an induced fit mechanism
    • Sawaya MR, Prasad R, Wilson SH, Kraut J, Pelletier H (1997) Crystal structures of human DNA polymerase beta complexed with gapped and nicked DNA: Evidence for an induced fit mechanism. Biochemistry 36: 11205-11215.
    • (1997) Biochemistry , vol.36 , pp. 11205-11215
    • Sawaya, M.R.1    Prasad, R.2    Wilson, S.H.3    Kraut, J.4    Pelletier, H.5
  • 41
    • 0037168491 scopus 로고    scopus 로고
    • In vitro nucleotide misinsertion opposite the oxidized guanosine lesions spiroiminodihydantoin and guanidinohydantoin and DNA synthesis past the lesions using Escherichia coli DNA polymerase I (Klenow fragment)
    • Kornyushyna O, Berges AM, Muller JG, Burrows CJ (2002) In vitro nucleotide misinsertion opposite the oxidized guanosine lesions spiroiminodihydantoin and guanidinohydantoin and DNA synthesis past the lesions using Escherichia coli DNA polymerase I (Klenow fragment). Biochemistry 41: 15304-15314.
    • (2002) Biochemistry , vol.41 , pp. 15304-15314
    • Kornyushyna, O.1    Berges, A.M.2    Muller, J.G.3    Burrows, C.J.4
  • 42
    • 0028834955 scopus 로고
    • Gel fidelity assay measuring nucleotide misinsertion, exonucleolytic proofreading, and lesion bypass efficiencies
    • Creighton S, Bloom LB, Goodman MF (1995) Gel fidelity assay measuring nucleotide misinsertion, exonucleolytic proofreading, and lesion bypass efficiencies. Methods Enzymol 262: 232-256.
    • (1995) Methods Enzymol , vol.262 , pp. 232-256
    • Creighton, S.1    Bloom, L.B.2    Goodman, M.F.3
  • 43
    • 84920325457 scopus 로고
    • AMoRe: An Automated Package for Molecular Replacement
    • Navaza J (1994) AMoRe: An Automated Package for Molecular Replacement. Acta Crystallogr A 50: 157-163.
    • (1994) Acta Crystallogr A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 45
    • 7944237130 scopus 로고    scopus 로고
    • Combined pseudo-merohedral twinning, non-crystallographic symmetry and pseudo-translation in a monoclinic crystal form of the gammadelta T-cell ligand T10
    • Rudolph MG, Wingren C, Crowley MP, Chien YH, Wilson IA (2004) Combined pseudo-merohedral twinning, non-crystallographic symmetry and pseudo-translation in a monoclinic crystal form of the gammadelta T-cell ligand T10. Acta Crystallogr D Biol Crystallogr 60: 656-664.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 656-664
    • Rudolph, M.G.1    Wingren, C.2    Crowley, M.P.3    Chien, Y.H.4    Wilson, I.A.5
  • 46
    • 0032006209 scopus 로고    scopus 로고
    • Systematic analysis of domain motions in proteins from conformational change: New results on citrate synthase and T4 lysozyme
    • Hayward S, Berendsen HJ (1998) Systematic analysis of domain motions in proteins from conformational change: New results on citrate synthase and T4 lysozyme. Proteins 30: 144-154.
    • (1998) Proteins , vol.30 , pp. 144-154
    • Hayward, S.1    Berendsen, H.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.