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Volumn 34, Issue 23, 2015, Pages 2937-2952

Unexpected features and mechanism of heterodimer formation of a herpesvirus nuclear egress complex

Author keywords

Bergerat fold; crystal structure; interaction interface; nuclear egress complex; zinc finger

Indexed keywords

ANTIVIRUS AGENT; HETERODIMER; METALLOPROTEIN; MUTANT PROTEIN; NUCLEAR EGRESS COMPLEX; NUCLEOTIDE BINDING PROTEIN; UL50 PROTEIN; UL53 PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN; ZINC; UL53 PROTEIN, HUMAN HERPESVIRUS 1; VIRAL PROTEIN;

EID: 84950277486     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.15252/embj.201592651     Document Type: Article
Times cited : (61)

References (59)
  • 2
    • 0030987132 scopus 로고    scopus 로고
    • An atypical topoisomerase II from Archaea with implications for meiotic recombination
    • Bergerat A, de Massy B, Gadelle D, Varoutas PC, Nicolas A, Forterre P, (1997) An atypical topoisomerase II from Archaea with implications for meiotic recombination. Nature 386: 414-417
    • (1997) Nature , vol.386 , pp. 414-417
    • Bergerat, A.1    De Massy, B.2    Gadelle, D.3    Varoutas, P.C.4    Nicolas, A.5    Forterre, P.6
  • 3
    • 84902322686 scopus 로고    scopus 로고
    • Membrane deformation and scission by the HSV-1 nuclear egress complex
    • Bigalke JM, Heuser T, Nicastro D, Heldwein EE, (2014) Membrane deformation and scission by the HSV-1 nuclear egress complex. Nat Commun 5: 4131
    • (2014) Nat Commun , vol.5 , pp. 4131
    • Bigalke, J.M.1    Heuser, T.2    Nicastro, D.3    Heldwein, E.E.4
  • 4
    • 84950268155 scopus 로고    scopus 로고
    • Structural basis of membrane budding by the nuclear egress complex of herpesviruses
    • Bigalke JM, Heldwein EE, (2015) Structural basis of membrane budding by the nuclear egress complex of herpesviruses. EMBO J 34: 2921-2936
    • (2015) EMBO J , vol.34 , pp. 2921-2936
    • Bigalke, J.M.1    Heldwein, E.E.2
  • 5
    • 0038467608 scopus 로고    scopus 로고
    • Effects of charged cluster mutations on the function of herpes simplex virus type 1 UL34 protein
    • Bjerke SL, Cowan JM, Kerr JK, Reynolds AE, Baines JD, Roller RJ, (2003) Effects of charged cluster mutations on the function of herpes simplex virus type 1 UL34 protein. J Virol 77: 7601-7610
    • (2003) J Virol , vol.77 , pp. 7601-7610
    • Bjerke, S.L.1    Cowan, J.M.2    Kerr, J.K.3    Reynolds, A.E.4    Baines, J.D.5    Roller, R.J.6
  • 6
    • 3242715831 scopus 로고    scopus 로고
    • Comprehensive mutational analysis of a herpesvirus gene in the viral genome context reveals a region essential for virus replication
    • Bubeck A, Wagner M, Ruzsics Z, Lotzerich M, Iglesias M, Singh IR, Koszinowski UH, (2004) Comprehensive mutational analysis of a herpesvirus gene in the viral genome context reveals a region essential for virus replication. J Virol 78: 8026-8035
    • (2004) J Virol , vol.78 , pp. 8026-8035
    • Bubeck, A.1    Wagner, M.2    Ruzsics, Z.3    Lotzerich, M.4    Iglesias, M.5    Singh, I.R.6    Koszinowski, U.H.7
  • 7
    • 42449130222 scopus 로고    scopus 로고
    • Remodelling of the nuclear lamina during human cytomegalovirus infection: Role of the viral proteins pUL50 and pUL53
    • Camozzi D, Pignatelli S, Valvo C, Lattanzi G, Capanni C, Dal Monte P, Landini MP, (2008) Remodelling of the nuclear lamina during human cytomegalovirus infection: role of the viral proteins pUL50 and pUL53. J Gen Virol 89: 731-740
    • (2008) J Gen Virol , vol.89 , pp. 731-740
    • Camozzi, D.1    Pignatelli, S.2    Valvo, C.3    Lattanzi, G.4    Capanni, C.5    Dal Monte, P.6    Landini, M.P.7
  • 8
    • 0030863707 scopus 로고    scopus 로고
    • The null mutant of the U(L)31 gene of herpes simplex virus 1: Construction and phenotype in infected cells
    • Chang YE, Van Sant C, Krug PW, Sears AE, Roizman B, (1997) The null mutant of the U(L)31 gene of herpes simplex virus 1: construction and phenotype in infected cells. J Virol 71: 8307-8315
    • (1997) J Virol , vol.71 , pp. 8307-8315
    • Chang, Y.E.1    Van Sant, C.2    Krug, P.W.3    Sears, A.E.4    Roizman, B.5
  • 9
    • 84877122188 scopus 로고    scopus 로고
    • Activation of ATP binding for the autophosphorylation of DosS, a Mycobacterium tuberculosis histidine kinase lacking an ATP lid motif
    • Cho HY, Lee YH, Bae YS, Kim E, Kang BS, (2013) Activation of ATP binding for the autophosphorylation of DosS, a Mycobacterium tuberculosis histidine kinase lacking an ATP lid motif. J Biol Chem 288: 12437-12447
    • (2013) J Biol Chem , vol.288 , pp. 12437-12447
    • Cho, H.Y.1    Lee, Y.H.2    Bae, Y.S.3    Kim, E.4    Kang, B.S.5
  • 10
    • 84855961718 scopus 로고    scopus 로고
    • Reconstitution of the Kaposi's sarcoma-associated herpesvirus nuclear egress complex and formation of nuclear membrane vesicles by coexpression of ORF67 and ORF69 gene products
    • Desai PJ, Pryce EN, Henson BW, Luitweiler EM, Cothran J, (2012) Reconstitution of the Kaposi's sarcoma-associated herpesvirus nuclear egress complex and formation of nuclear membrane vesicles by coexpression of ORF67 and ORF69 gene products. J Virol 86: 594-598
    • (2012) J Virol , vol.86 , pp. 594-598
    • Desai, P.J.1    Pryce, E.N.2    Henson, B.W.3    Luitweiler, E.M.4    Cothran, J.5
  • 11
    • 0011274647 scopus 로고    scopus 로고
    • Cytomegalovirus: Nucleosides and foscarnet: Clinical applications
    • Richman D.D. (ed.), Chichester, UK: John Wiley & Sons
    • Drew WL, Buhles WC, (1996) Cytomegalovirus: nucleosides and foscarnet: clinical applications. In Antiviral Drug Resistance., Richman DD, (ed.), pp 594-598. Chichester, UK: John Wiley & Sons
    • (1996) Antiviral Drug Resistance , pp. 594-598
    • Drew, W.L.1    Buhles, W.C.2
  • 13
    • 0033985080 scopus 로고    scopus 로고
    • GHKL, an emergent ATPase/kinase superfamily
    • Dutta R, Inouye M, (2000) GHKL, an emergent ATPase/kinase superfamily. Trends Biochem Sci 25: 24-28
    • (2000) Trends Biochem Sci , vol.25 , pp. 24-28
    • Dutta, R.1    Inouye, M.2
  • 16
    • 84936774563 scopus 로고    scopus 로고
    • The herpes simplex virus protein pUL31 escorts nucleocapsids to sites of nuclear egress, a process coordinated by its N-terminal domain
    • Funk C, Ott M, Raschbichler V, Nagel CH, Binz A, Sodeik B, Bauerfeind R, Bailer SM, (2015) The herpes simplex virus protein pUL31 escorts nucleocapsids to sites of nuclear egress, a process coordinated by its N-terminal domain. PLoS Pathog 11: e1004957
    • (2015) PLoS Pathog , vol.11 , pp. e1004957
    • Funk, C.1    Ott, M.2    Raschbichler, V.3    Nagel, C.H.4    Binz, A.5    Sodeik, B.6    Bauerfeind, R.7    Bailer, S.M.8
  • 17
    • 70349541000 scopus 로고    scopus 로고
    • Biological insights from structures of two-component proteins
    • Gao R, Stock AM, (2009) Biological insights from structures of two-component proteins. Annu Rev Microbiol 63: 133-154
    • (2009) Annu Rev Microbiol , vol.63 , pp. 133-154
    • Gao, R.1    Stock, A.M.2
  • 18
    • 0036527281 scopus 로고    scopus 로고
    • Resistance of herpesviruses to antiviral drugs: Clinical impacts and molecular mechanisms
    • Gilbert C, Bestman-Smith J, Boivin G, (2002) Resistance of herpesviruses to antiviral drugs: clinical impacts and molecular mechanisms. Drug Resist Updat 5: 88-114
    • (2002) Drug Resist Updat , vol.5 , pp. 88-114
    • Gilbert, C.1    Bestman-Smith, J.2    Boivin, G.3
  • 19
    • 41949117422 scopus 로고    scopus 로고
    • Deletion of Epstein-Barr virus BFLF2 leads to impaired viral DNA packaging and primary egress as well as to the production of defective viral particles
    • Granato M, Feederle R, Farina A, Gonnella R, Santarelli R, Hub B, Faggioni A, Delecluse HJ, (2008) Deletion of Epstein-Barr virus BFLF2 leads to impaired viral DNA packaging and primary egress as well as to the production of defective viral particles. J Virol 82: 4042-4051
    • (2008) J Virol , vol.82 , pp. 4042-4051
    • Granato, M.1    Feederle, R.2    Farina, A.3    Gonnella, R.4    Santarelli, R.5    Hub, B.6    Faggioni, A.7    Delecluse, H.J.8
  • 20
    • 79954599465 scopus 로고    scopus 로고
    • Herpesviruses remodel host membranes for virus egress
    • Johnson DC, Baines JD, (2011) Herpesviruses remodel host membranes for virus egress. Nat Rev Microbiol 9: 382-394
    • (2011) Nat Rev Microbiol , vol.9 , pp. 382-394
    • Johnson, D.C.1    Baines, J.D.2
  • 23
    • 34249844954 scopus 로고    scopus 로고
    • Vesicle formation from the nuclear membrane is induced by coexpression of two conserved herpesvirus proteins
    • Klupp BG, Granzow H, Fuchs W, Keil GM, Finke S, Mettenleiter TC, (2007) Vesicle formation from the nuclear membrane is induced by coexpression of two conserved herpesvirus proteins. Proc Natl Acad Sci USA 104: 7241-7246
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 7241-7246
    • Klupp, B.G.1    Granzow, H.2    Fuchs, W.3    Keil, G.M.4    Finke, S.5    Mettenleiter, T.C.6
  • 24
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM, (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 26: 283-291
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 25
    • 84866920100 scopus 로고    scopus 로고
    • The ESCRT machinery is recruited by the viral BFRF1 protein to the nucleus-associated membrane for the maturation of Epstein-Barr Virus
    • Lee CP, Liu PT, Kung HN, Su MT, Chua HH, Chang YH, Chang CW, Tsai CH, Liu FT, Chen MR, (2012) The ESCRT machinery is recruited by the viral BFRF1 protein to the nucleus-associated membrane for the maturation of Epstein-Barr Virus. PLoS Pathog 8: e1002904
    • (2012) PLoS Pathog , vol.8 , pp. e1002904
    • Lee, C.P.1    Liu, P.T.2    Kung, H.N.3    Su, M.T.4    Chua, H.H.5    Chang, Y.H.6    Chang, C.W.7    Tsai, C.H.8    Liu, F.T.9    Chen, M.R.10
  • 27
    • 84881218748 scopus 로고    scopus 로고
    • Structure, function and regulation of the hsp90 machinery
    • Li J, Buchner J, (2013) Structure, function and regulation of the hsp90 machinery. Biomed J 36: 106-117
    • (2013) Biomed J , vol.36 , pp. 106-117
    • Li, J.1    Buchner, J.2
  • 28
    • 14744280502 scopus 로고    scopus 로고
    • Identification of an essential domain in the herpes simplex virus 1 UL34 protein that is necessary and sufficient to interact with UL31 protein
    • Liang L, Baines JD, (2005) Identification of an essential domain in the herpes simplex virus 1 UL34 protein that is necessary and sufficient to interact with UL31 protein. J Virol 79: 3797-3806
    • (2005) J Virol , vol.79 , pp. 3797-3806
    • Liang, L.1    Baines, J.D.2
  • 30
    • 33645980333 scopus 로고    scopus 로고
    • Functional domains of murine cytomegalovirus nuclear egress protein M53/p38
    • Lotzerich M, Ruzsics Z, Koszinowski UH, (2006) Functional domains of murine cytomegalovirus nuclear egress protein M53/p38. J Virol 80: 73-84
    • (2006) J Virol , vol.80 , pp. 73-84
    • Lotzerich, M.1    Ruzsics, Z.2    Koszinowski, U.H.3
  • 31
    • 84875489857 scopus 로고    scopus 로고
    • Interactions of the Kaposi's Sarcoma-associated herpesvirus nuclear egress complex: ORF69 is a potent factor for remodeling cellular membranes
    • Luitweiler EM, Henson BW, Pryce EN, Patel V, Coombs G, McCaffery JM, Desai PJ, (2013) Interactions of the Kaposi's Sarcoma-associated herpesvirus nuclear egress complex: ORF69 is a potent factor for remodeling cellular membranes. J Virol 87: 3915-3929
    • (2013) J Virol , vol.87 , pp. 3915-3929
    • Luitweiler, E.M.1    Henson, B.W.2    Pryce, E.N.3    Patel, V.4    Coombs, G.5    McCaffery, J.M.6    Desai, P.J.7
  • 32
    • 78049355534 scopus 로고    scopus 로고
    • Antiviral drug resistance of human cytomegalovirus
    • Lurain NS, Chou S, (2010) Antiviral drug resistance of human cytomegalovirus. Clin Microbiol Rev 23: 689-712
    • (2010) Clin Microbiol Rev , vol.23 , pp. 689-712
    • Lurain, N.S.1    Chou, S.2
  • 34
    • 9644268172 scopus 로고    scopus 로고
    • Budding events in herpesvirus morphogenesis
    • Mettenleiter TC, (2004) Budding events in herpesvirus morphogenesis. Virus Res 106: 167-180
    • (2004) Virus Res , vol.106 , pp. 167-180
    • Mettenleiter, T.C.1
  • 36
    • 31144448686 scopus 로고    scopus 로고
    • Egress of alphaherpesviruses
    • author reply 1611-1612
    • Mettenleiter TC, Minson T, (2006) Egress of alphaherpesviruses. J Virol 80: 1610-1611; author reply 1611-1612
    • (2006) J Virol , vol.80 , pp. 1610-1611
    • Mettenleiter, T.C.1    Minson, T.2
  • 37
    • 35048861785 scopus 로고    scopus 로고
    • Cytomegaloviral proteins pUL50 and pUL53 are associated with the nuclear lamina and interact with cellular protein kinase C
    • Milbradt J, Auerochs S, Marschall M, (2007) Cytomegaloviral proteins pUL50 and pUL53 are associated with the nuclear lamina and interact with cellular protein kinase C. J Gen Virol 88: 2642-2650
    • (2007) J Gen Virol , vol.88 , pp. 2642-2650
    • Milbradt, J.1    Auerochs, S.2    Marschall, M.3
  • 38
    • 84863614597 scopus 로고    scopus 로고
    • Specific residues of a conserved domain in the N terminus of the human cytomegalovirus pUL50 protein determine its intranuclear interaction with pUL53
    • Milbradt J, Auerochs S, Sevvana M, Muller YA, Sticht H, Marschall M, (2012) Specific residues of a conserved domain in the N terminus of the human cytomegalovirus pUL50 protein determine its intranuclear interaction with pUL53. J Biol Chem 287: 24004-24016
    • (2012) J Biol Chem , vol.287 , pp. 24004-24016
    • Milbradt, J.1    Auerochs, S.2    Sevvana, M.3    Muller, Y.A.4    Sticht, H.5    Marschall, M.6
  • 40
    • 0037008483 scopus 로고    scopus 로고
    • Cytomegalovirus recruitment of cellular kinases to dissolve the nuclear lamina
    • Muranyi W, Haas J, Wagner M, Krohne G, Koszinowski UH, (2002) Cytomegalovirus recruitment of cellular kinases to dissolve the nuclear lamina. Science 297: 854-857
    • (2002) Science , vol.297 , pp. 854-857
    • Muranyi, W.1    Haas, J.2    Wagner, M.3    Krohne, G.4    Koszinowski, U.H.5
  • 43
    • 33645961583 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 infection induces activation and recruitment of protein kinase C to the nuclear membrane and increased phosphorylation of lamin B
    • Park R, Baines JD, (2006) Herpes simplex virus type 1 infection induces activation and recruitment of protein kinase C to the nuclear membrane and increased phosphorylation of lamin B. J Virol 80: 494-504
    • (2006) J Virol , vol.80 , pp. 494-504
    • Park, R.1    Baines, J.D.2
  • 45
    • 77956019599 scopus 로고    scopus 로고
    • Dominant negative mutants of the murine cytomegalovirus M53 gene block nuclear egress and inhibit capsid maturation
    • Popa M, Ruzsics Z, Lotzerich M, Dolken L, Buser C, Walther P, Koszinowski UH, (2010) Dominant negative mutants of the murine cytomegalovirus M53 gene block nuclear egress and inhibit capsid maturation. J Virol 84: 9035-9046
    • (2010) J Virol , vol.84 , pp. 9035-9046
    • Popa, M.1    Ruzsics, Z.2    Lotzerich, M.3    Dolken, L.4    Buser, C.5    Walther, P.6    Koszinowski, U.H.7
  • 46
    • 77950466161 scopus 로고    scopus 로고
    • Analysis of a charge cluster mutation of herpes simplex virus type 1 UL34 and its extragenic suppressor suggests a novel interaction between pUL34 and pUL31 that is necessary for membrane curvature around capsids
    • Roller RJ, Bjerke SL, Haugo AC, Hanson S, (2010) Analysis of a charge cluster mutation of herpes simplex virus type 1 UL34 and its extragenic suppressor suggests a novel interaction between pUL34 and pUL31 that is necessary for membrane curvature around capsids. J Virol 84: 3921-3934
    • (2010) J Virol , vol.84 , pp. 3921-3934
    • Roller, R.J.1    Bjerke, S.L.2    Haugo, A.C.3    Hanson, S.4
  • 47
    • 10644239856 scopus 로고    scopus 로고
    • Conditional cytomegalovirus replication in vitro and in vivo
    • Rupp B, Ruzsics Z, Sacher T, Koszinowski UH, (2005) Conditional cytomegalovirus replication in vitro and in vivo. J Virol 79: 486-494
    • (2005) J Virol , vol.79 , pp. 486-494
    • Rupp, B.1    Ruzsics, Z.2    Sacher, T.3    Koszinowski, U.H.4
  • 48
    • 63149109165 scopus 로고    scopus 로고
    • Biochemical, biophysical, and mutational analyses of subunit interactions of the human cytomegalovirus nuclear egress complex
    • Sam MD, Evans BT, Coen DM, Hogle JM, (2009) Biochemical, biophysical, and mutational analyses of subunit interactions of the human cytomegalovirus nuclear egress complex. J Virol 83: 2996-3006
    • (2009) J Virol , vol.83 , pp. 2996-3006
    • Sam, M.D.1    Evans, B.T.2    Coen, D.M.3    Hogle, J.M.4
  • 49
    • 84906350501 scopus 로고    scopus 로고
    • Comparison of effects of inhibitors of viral and cellular protein kinases on human cytomegalovirus disruption of nuclear lamina and nuclear egress
    • Sharma M, Coen DM, (2014) Comparison of effects of inhibitors of viral and cellular protein kinases on human cytomegalovirus disruption of nuclear lamina and nuclear egress. J Virol 88: 10982-10985
    • (2014) J Virol , vol.88 , pp. 10982-10985
    • Sharma, M.1    Coen, D.M.2
  • 50
    • 84890880476 scopus 로고    scopus 로고
    • Human cytomegalovirus UL50 and UL53 recruit viral protein kinase UL97, not protein kinase C, for disruption of nuclear lamina and nuclear egress in infected cells
    • Sharma M, Kamil JP, Coughlin M, Reim NI, Coen DM, (2014) Human cytomegalovirus UL50 and UL53 recruit viral protein kinase UL97, not protein kinase C, for disruption of nuclear lamina and nuclear egress in infected cells. J Virol 88: 249-262
    • (2014) J Virol , vol.88 , pp. 249-262
    • Sharma, M.1    Kamil, J.P.2    Coughlin, M.3    Reim, N.I.4    Coen, D.M.5
  • 53
    • 84857100506 scopus 로고    scopus 로고
    • Human cytomegalovirus UL44 concentrates at the periphery of replication compartments, the site of viral DNA synthesis
    • Strang BL, Boulant S, Chang L, Knipe DM, Kirchhausen T, Coen DM, (2012) Human cytomegalovirus UL44 concentrates at the periphery of replication compartments, the site of viral DNA synthesis. J Virol 86: 2089-2095
    • (2012) J Virol , vol.86 , pp. 2089-2095
    • Strang, B.L.1    Boulant, S.2    Chang, L.3    Knipe, D.M.4    Kirchhausen, T.5    Coen, D.M.6
  • 54
    • 33645053126 scopus 로고    scopus 로고
    • Two-step red-mediated recombination for versatile high-efficiency markerless DNA manipulation in Escherichia coli
    • Tischer BK, von Einem J, Kaufer B, Osterrieder N, (2006) Two-step red-mediated recombination for versatile high-efficiency markerless DNA manipulation in Escherichia coli. Biotechniques 40: 191-197
    • (2006) Biotechniques , vol.40 , pp. 191-197
    • Tischer, B.K.1    Von Einem, J.2    Kaufer, B.3    Osterrieder, N.4
  • 55
    • 79955159135 scopus 로고    scopus 로고
    • En passant mutagenesis: A two step markerless red recombination system
    • Tischer BK, Smith GA, Osterrieder N, (2010) En passant mutagenesis: a two step markerless red recombination system. Methods Mol Biol 634: 421-430
    • (2010) Methods Mol Biol , vol.634 , pp. 421-430
    • Tischer, B.K.1    Smith, G.A.2    Osterrieder, N.3
  • 56
    • 77955296275 scopus 로고    scopus 로고
    • Structural and enzymatic insights into the ATP binding and autophosphorylation mechanism of a sensor histidine kinase
    • Trajtenberg F, Grana M, Ruetalo N, Botti H, Buschiazzo A, (2010) Structural and enzymatic insights into the ATP binding and autophosphorylation mechanism of a sensor histidine kinase. J Biol Chem 285: 24892-24903
    • (2010) J Biol Chem , vol.285 , pp. 24892-24903
    • Trajtenberg, F.1    Grana, M.2    Ruetalo, N.3    Botti, H.4    Buschiazzo, A.5
  • 57
    • 0038748230 scopus 로고    scopus 로고
    • Current and potential therapies for the treatment of herpes-virus infections
    • Villarreal EC, (2003) Current and potential therapies for the treatment of herpes-virus infections. Prog Drug Res 60: 263-307
    • (2003) Prog Drug Res , vol.60 , pp. 263-307
    • Villarreal, E.C.1
  • 58
    • 75649151032 scopus 로고    scopus 로고
    • Xia2: An expert system for macromolecular crystallography data reduction
    • Winter D, (2010) xia2: an expert system for macromolecular crystallography data reduction. J Appl Cryst 43: 186-190
    • (2010) J Appl Cryst , vol.43 , pp. 186-190
    • Winter, D.1
  • 59
    • 0142091343 scopus 로고    scopus 로고
    • Functional map of human cytomegalovirus AD169 defined by global mutational analysis
    • Yu D, Silva MC, Shenk T, (2003) Functional map of human cytomegalovirus AD169 defined by global mutational analysis. Proc Natl Acad Sci USA 100: 12396-12401
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12396-12401
    • Yu, D.1    Silva, M.C.2    Shenk, T.3


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