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Volumn 289, Issue 31, 2014, Pages 21627-21639

Multiple interactions of the intrinsically disordered region between the helicase and nuclease domains of the archaeal Hef protein

Author keywords

[No Author keywords available]

Indexed keywords

ATOMIC FORCE MICROSCOPY; REPAIR;

EID: 84905389211     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.554998     Document Type: Article
Times cited : (33)

References (53)
  • 1
    • 0036698611 scopus 로고    scopus 로고
    • Novel endonuclease in Archaea cleaving DNA with various branched structure
    • Komori, K., Fujikane, R., Shinagawa, H., and Ishino, Y. (2002) Novel endonuclease in Archaea cleaving DNA with various branched structure. Genes Genet. Syst. 77, 227-241
    • (2002) Genes Genet. Syst. , vol.77 , pp. 227-241
    • Komori, K.1    Fujikane, R.2    Shinagawa, H.3    Ishino, Y.4
  • 2
    • 11144225798 scopus 로고    scopus 로고
    • Cooperation of the N-terminal helicase and C-terminal endonuclease activities of archaeal Hef protein in processing stalled replication forks
    • DOI 10.1074/jbc.M409243200
    • Komori, K., Hidaka, M., Horiuchi, T., Fujikane, R., Shinagawa, H., and Ishino, Y. (2004) Cooperation of the N-terminal helicase and C-terminal endonuclease activities of archaeal Hef protein in processing stalled replication forks. J. Biol. Chem. 279, 53175-53185 (Pubitemid 40051820)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.51 , pp. 53175-53185
    • Komori, K.1    Hidaka, M.2    Horiuchi, T.3    Fujikane, R.4    Shinagawa, H.5    Ishino, Y.6
  • 3
    • 32344447374 scopus 로고    scopus 로고
    • Structure-specific DNA nucleases: Structural basis for 3D-scissors
    • DOI 10.1016/j.sbi.2006.01.009, PII S0959440X06000066
    • Nishino, T., Ishino, Y., and Morikawa, K. (2006) Structure-specific DNA nucleases: structural basis for 3D-scissors. Curr. Opin. Struct. Biol. 16, 60-67 (Pubitemid 43221872)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.1 , pp. 60-67
    • Nishino, T.1    Ishino, Y.2    Morikawa, K.3
  • 4
    • 22144443201 scopus 로고    scopus 로고
    • Improved and versatile transformation system allowing multiple genetic manipulations of the hyperthermophilic archaeon Thermococcus kodakaraensis
    • DOI 10.1128/AEM.71.7.3889-3899.2005
    • Sato, T., Fukui, T., Atomi, H., and Imanaka, T. (2005) Improved and versatile transformation system allowing multiple genetic manipulations of the hyperthermophilic archaeon Thermococcus kodakaraensis. Appl. Environ. Microbiol. 71, 3889-3899 (Pubitemid 40980560)
    • (2005) Applied and Environmental Microbiology , vol.71 , Issue.7 , pp. 3889-3899
    • Sato, T.1    Fukui, T.2    Atomi, H.3    Imanaka, T.4
  • 5
    • 78650579621 scopus 로고    scopus 로고
    • Genetic analysis of DNA repair in the hyperthermophilic archaeon, Thermococcus kodakaraensis
    • Fujikane, R., Ishino, S., Ishino, Y., and Forterre, P. (2010) Genetic analysis of DNA repair in the hyperthermophilic archaeon, Thermococcus kodakaraensis. Genes Genet. Syst. 85, 243-257
    • (2010) Genes Genet. Syst. , vol.85 , pp. 243-257
    • Fujikane, R.1    Ishino, S.2    Ishino, Y.3    Forterre, P.4
  • 6
    • 77955981653 scopus 로고    scopus 로고
    • The archaeal Xpf/Mus81/ FANCM homolog Hef and the Holliday junction resolvase Hjc define alternative pathways that are essential for cell viability in Haloferax volcanii
    • Lestini, R., Duan, Z., and Allers, T. (2010) The archaeal Xpf/Mus81/ FANCM homolog Hef and the Holliday junction resolvase Hjc define alternative pathways that are essential for cell viability in Haloferax volcanii. DNA Repair 9, 994-1002
    • (2010) DNA Repair , vol.9 , pp. 994-1002
    • Lestini, R.1    Duan, Z.2    Allers, T.3
  • 8
    • 0037772376 scopus 로고    scopus 로고
    • An archaeal XPF repair endonuclease dependent on a heterotrimeric PCNA
    • DOI 10.1046/j.1365-2958.2003.03444.x
    • Roberts, J. A., Bell, S. D., and White, M. F. (2003) An archaeal XPF repair endonuclease dependent on a heterotrimeric PCNA. Mol. Microbiol. 48, 361-371 (Pubitemid 36819074)
    • (2003) Molecular Microbiology , vol.48 , Issue.2 , pp. 361-371
    • Roberts, J.A.1    Bell, S.D.2    White, M.F.3
  • 9
    • 16344394253 scopus 로고    scopus 로고
    • Structure of an XPF endonuclease with and without DNA suggests a model for substrate recognition
    • DOI 10.1038/sj.emboj.7600581
    • Newman, M., Murray-Rust, J., Lally, J., Rudolf, J., Fadden, A., Knowles, P. P., White, M. F., and McDonald, N. Q. (2005) Structure of an XPF endonuclease with and without DNA suggests a model for substrate recognition. EMBO J. 24, 895-905 (Pubitemid 40470139)
    • (2005) EMBO Journal , vol.24 , Issue.5 , pp. 895-905
    • Newman, M.1    Murray-Rust, J.2    Lally, J.3    Rudolf, J.4    Fadden, A.5    Knowles, P.P.6    White, M.F.7    McDonald, N.Q.8
  • 10
    • 84863347829 scopus 로고    scopus 로고
    • Replication fork dynamics and the DNA damage response
    • Jones, R. M., and Petermann, E. (2012) Replication fork dynamics and the DNA damage response. Biochem. J. 443, 13-26
    • (2012) Biochem. J. , vol.443 , pp. 13-26
    • Jones, R.M.1    Petermann, E.2
  • 11
    • 84860181097 scopus 로고    scopus 로고
    • Mechanisms of replication fork protection: A safeguard for genome stability
    • Errico, A., and Costanzo, V. (2012) Mechanisms of replication fork protection: a safeguard for genome stability. Crit. Rev. Biochem. Mol. Biol. 47, 222-235
    • (2012) Crit. Rev. Biochem. Mol. Biol. , vol.47 , pp. 222-235
    • Errico, A.1    Costanzo, V.2
  • 12
    • 82855169525 scopus 로고    scopus 로고
    • Orchestrating the nucleases involved in DNA interstrand cross-link (ICL) repair
    • Sengerová, B., Wang, A. T., and McHugh, P. J. (2011) Orchestrating the nucleases involved in DNA interstrand cross-link (ICL) repair. Cell Cycle 10, 3999-4008
    • (2011) Cell Cycle , vol.10 , pp. 3999-4008
    • Sengerová, B.1    Wang, A.T.2    McHugh, P.J.3
  • 13
    • 82855169522 scopus 로고    scopus 로고
    • Understanding the molecular basis of common fragile sites instability: Role of the proteins involved in the recovery of stalled replication forks
    • Franchitto, A., and Pichierri, P. (2011) Understanding the molecular basis of common fragile sites instability: role of the proteins involved in the recovery of stalled replication forks. Cell Cycle 10, 4039-4046
    • (2011) Cell Cycle , vol.10 , pp. 4039-4046
    • Franchitto, A.1    Pichierri, P.2
  • 14
    • 84872578210 scopus 로고    scopus 로고
    • Fanconi anaemia and the repair of Watson and Crick DNA crosslinks
    • Kottemann, M. C., and Smogorzewska, A. (2013) Fanconi anaemia and the repair of Watson and Crick DNA crosslinks. Nature 493, 356-363
    • (2013) Nature , vol.493 , pp. 356-363
    • Kottemann, M.C.1    Smogorzewska, A.2
  • 15
    • 84863670930 scopus 로고    scopus 로고
    • Regulation of DNA cross-link repair by the Fanconi anemia/BRCA pathway
    • Kim, H., and D'Andrea, A. D. (2012) Regulation of DNA cross-link repair by the Fanconi anemia/BRCA pathway. Genes Dev. 26, 1393-1408
    • (2012) Genes Dev. , vol.26 , pp. 1393-1408
    • Kim, H.1    D'Andrea, A.D.2
  • 16
    • 84859747536 scopus 로고    scopus 로고
    • Rescue of replication failure by Fanconi anaemia proteins
    • Constantinou, A. (2012) Rescue of replication failure by Fanconi anaemia proteins. Chromosoma 121, 21-36
    • (2012) Chromosoma , vol.121 , pp. 21-36
    • Constantinou, A.1
  • 17
    • 82755184119 scopus 로고    scopus 로고
    • The Fanconi anaemia pathway orchestrates incisions at sites of crosslinked DNA
    • Crossan, G. P., and Patel, K. J. (2012) The Fanconi anaemia pathway orchestrates incisions at sites of crosslinked DNA. J. Pathol. 226, 326-337
    • (2012) J. Pathol. , vol.226 , pp. 326-337
    • Crossan, G.P.1    Patel, K.J.2
  • 18
    • 79959635260 scopus 로고    scopus 로고
    • DNA interstrand crosslink repair and cancer
    • Deans, A. J., and West, S. C. (2011) DNA interstrand crosslink repair and cancer. Nat. Rev. Cancer 11, 467-480
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 467-480
    • Deans, A.J.1    West, S.C.2
  • 21
    • 84870057622 scopus 로고    scopus 로고
    • Intrinsically disordered proteins: A 10-year recap
    • Tompa, P. (2012) Intrinsically disordered proteins: a 10-year recap. Trends Biochem. Sci. 37, 509-516
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 509-516
    • Tompa, P.1
  • 24
    • 84860259978 scopus 로고    scopus 로고
    • Intrinsically disordered proteins: From sequence and conformational properties toward drug discovery
    • Rezaei-Ghaleh, N., Blackledge, M., and Zweckstetter, M. (2012) Intrinsically disordered proteins: from sequence and conformational properties toward drug discovery. Chembiochem 13, 930-950
    • (2012) Chembiochem , vol.13 , pp. 930-950
    • Rezaei-Ghaleh, N.1    Blackledge, M.2    Zweckstetter, M.3
  • 25
    • 58149250634 scopus 로고    scopus 로고
    • The GTOP database in 2009: Updated content and novel features to expand and deepen insights into protein structures and functions
    • Fukuchi, S., Homma, K., Sakamoto, S., Sugawara, H., Tateno, Y., Gojobori, T., and Nishikawa, K. (2009) The GTOP database in 2009: updated content and novel features to expand and deepen insights into protein structures and functions. Nucleic Acids Res. 37, D333-D337
    • (2009) Nucleic Acids Res. , vol.37
    • Fukuchi, S.1    Homma, K.2    Sakamoto, S.3    Sugawara, H.4    Tateno, Y.5    Gojobori, T.6    Nishikawa, K.7
  • 26
    • 66249093114 scopus 로고    scopus 로고
    • Development of an accurate classification system of proteins into structured and unstructured regions that uncovers novel structural domains: Its application to human transcription factors
    • Fukuchi, S., Homma, K., Minezaki, Y., Gojobori, T., and Nishikawa, K. (2009) Development of an accurate classification system of proteins into structured and unstructured regions that uncovers novel structural domains: its application to human transcription factors. BMC Struct. Biol. 9, 26
    • (2009) BMC Struct. Biol. , vol.9 , pp. 26
    • Fukuchi, S.1    Homma, K.2    Minezaki, Y.3    Gojobori, T.4    Nishikawa, K.5
  • 27
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C., and von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319 -326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 28
    • 0015937178 scopus 로고
    • Interaction of an apolipoprotein (apoLP-alanine) with phosphatidylcholine
    • Morrisett, J. D., David, J. S., Pownall, H. J., Gotto, A. M. Jr. (1973) Interaction of an apolipoprotein (apoLP-alanine) with phosphatidylcholine. Biochemistry 12, 1290-1299
    • (1973) Biochemistry , vol.12 , pp. 1290-1299
    • Morrisett, J.D.1    David, J.S.2    Pownall, H.J.3    Gotto Jr., A.M.4
  • 29
    • 0024435833 scopus 로고
    • 13C labeling
    • Neri, D., Szyperski, T., Otting, G., Senn, H., and Wüthrich, K. (1989) Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling. Biochemistry 28, 7510-7516 (Pubitemid 19238098)
    • (1989) Biochemistry , vol.28 , Issue.19 , pp. 7510-7516
    • Neri, D.1    Szyperski, T.2    Otting, G.3    Senn, H.4    Wuthrich, K.5
  • 30
    • 0026511733 scopus 로고
    • Relationship between electrostatics and redox function in human thioredoxin: Characterization of pH titration shifts using two-dimensional homo- and heteronuclear NMR
    • Forman-Kay, J. D., Clore, G. M., and Gronenborn, A. M. (1992) Relationship between electrostatics and redox function in human thioredoxin: characterization of pH titration shifts using two-dimensional homo- and heteronuclear NMR. Biochemistry 31, 3442-3452
    • (1992) Biochemistry , vol.31 , pp. 3442-3452
    • Forman-Kay, J.D.1    Clore, G.M.2    Gronenborn, A.M.3
  • 31
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 33
    • 54149113310 scopus 로고    scopus 로고
    • High-speed atomic force microscopy for nano-visualization of dynamic biomolecular processes
    • Ando, T., Uchihashi, T., and Fukuma, T. (2008) High-speed atomic force microscopy for nano-visualization of dynamic biomolecular processes. Prog. Surf. Sci. 83, 337-347
    • (2008) Prog. Surf. Sci. , vol.83 , pp. 337-347
    • Ando, T.1    Uchihashi, T.2    Fukuma, T.3
  • 34
    • 84878138537 scopus 로고    scopus 로고
    • Phosphorylation-coupled intramolecular dynamics of unstructured regions in chromatin remodeler FACT
    • Hashimoto, M., Kodera, N., Tsunaka, Y., Oda, M., Tanimoto, M., Ando, T., Morikawa, K., and Tate, S. (2013) Phosphorylation-coupled intramolecular dynamics of unstructured regions in chromatin remodeler FACT. Biophys. J. 104, 2222-2234
    • (2013) Biophys. J. , vol.104 , pp. 2222-2234
    • Hashimoto, M.1    Kodera, N.2    Tsunaka, Y.3    Oda, M.4    Tanimoto, M.5    Ando, T.6    Morikawa, K.7    Tate, S.8
  • 35
    • 84868097664 scopus 로고    scopus 로고
    • Comparative analyses of the two proliferating cell nuclear antigens from the hyperthermophilic archaeon, Thermococcus kodakarensis
    • Kuba, Y., Ishino, S., Yamagami, T., Tokuhara, M., Kanai, T., Fujikane, R., Daiyasu, H., Atomi, H., and Ishino, Y. (2012) Comparative analyses of the two proliferating cell nuclear antigens from the hyperthermophilic archaeon, Thermococcus kodakarensis. Genes Cells 17, 923-937
    • (2012) Genes Cells , vol.17 , pp. 923-937
    • Kuba, Y.1    Ishino, S.2    Yamagami, T.3    Tokuhara, M.4    Kanai, T.5    Fujikane, R.6    Daiyasu, H.7    Atomi, H.8    Ishino, Y.9
  • 36
    • 12444336898 scopus 로고    scopus 로고
    • X-ray and biochemical anatomy of an archaeal XPF/Rad1/Mus81 family nuclease: Similarity between its endonuclease domain and restriction enzymes
    • DOI 10.1016/S0969-2126(03)00046-7
    • Nishino, T., Komori, K., Ishino, Y., and Morikawa, K. (2003) X-ray and biochemical anatomy of an archaeal XPF/Rad1/Mus81 family nuclease: similarity between its endonuclease domain and restriction enzymes. Structure 11, 445-457 (Pubitemid 36419571)
    • (2003) Structure , vol.11 , Issue.4 , pp. 445-457
    • Nishino, T.1    Komori, K.2    Ishino, Y.3    Morikawa, K.4
  • 37
    • 11844252069 scopus 로고    scopus 로고
    • Crystal structure and functional implications of Pyrococcus furiosus Hef helicase domain involved in branched DNA processing
    • DOI 10.1016/j.str.2004.11.008, PII S0969212604003934
    • Nishino, T., Komori, K., Tsuchiya, D., Ishino, Y., and Morikawa, K. (2005) Crystal structure and functional implications of Pyrococcus furiosus Hef helicase domain involved in branched DNA processing. Structure 13, 143-153 (Pubitemid 40092482)
    • (2005) Structure , vol.13 , Issue.1 , pp. 143-153
    • Nishino, T.1    Komori, K.2    Tsuchiya, D.3    Ishino, Y.4    Morikawa, K.5
  • 38
    • 33748767654 scopus 로고    scopus 로고
    • Identification of a novel binding motif in Pyrococcus furiosus DNA ligase for the functional interaction with proliferating cell nuclear antigen
    • DOI 10.1074/jbc.M603403200
    • Kiyonari, S., Takayama, K., Nishida, H., and Ishino, Y. (2006) Identification of a novel binding motif in Pyrococcus furiosus DNA ligase for the functional interaction with proliferating cell nuclear antigen. J. Biol. Chem. 281, 28023-28032 (Pubitemid 44414515)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.38 , pp. 28023-28032
    • Kiyonari, S.1    Takayama, K.2    Nishida, H.3    Ishino, Y.4
  • 39
    • 34547615757 scopus 로고    scopus 로고
    • DNA polymerases BI and D from the hyperthermophilic archaeon Pyrococcus furiosus both bind to proliferating cell nuclear antigen with their C-terminal PIP-box motifs
    • DOI 10.1128/JB.00073-07
    • Tori, K., Kimizu, M., Ishino, S., and Ishino, Y. (2007) DNA polymerases BI and D from the hyperthermophilic archaeon Pyrococcus furiosus both bind to proliferating cell nuclear antigen with their C-terminal PIP-box motifs. J. Bacteriol. 189, 5652-5657 (Pubitemid 47206412)
    • (2007) Journal of Bacteriology , vol.189 , Issue.15 , pp. 5652-5657
    • Tori, K.1    Kimizu, M.2    Ishino, S.3    Ishino, Y.4
  • 40
    • 53049086145 scopus 로고    scopus 로고
    • Physical and functional interactions between uracil-DNA glycosylase and proliferating cell nuclear antigen from the euryarchaeon Pyrococcus furiosus
    • Kiyonari, S., Uchimura, M., Shirai, T., and Ishino, Y. (2008) Physical and functional interactions between uracil-DNA glycosylase and proliferating cell nuclear antigen from the euryarchaeon Pyrococcus furiosus. J. Biol. Chem. 283, 24185-24193
    • (2008) J. Biol. Chem. , vol.283 , pp. 24185-24193
    • Kiyonari, S.1    Uchimura, M.2    Shirai, T.3    Ishino, Y.4
  • 41
    • 0033777562 scopus 로고    scopus 로고
    • The puzzle of PCNA's many partners
    • Warbrick, E. (2000) The puzzle of PCNA's many partners. Bioessays 22, 997-1006
    • (2000) Bioessays , vol.22 , pp. 997-1006
    • Warbrick, E.1
  • 43
    • 6344277430 scopus 로고    scopus 로고
    • Reduced amino acid alphabet is sufficient to accurately recognize intrinsically disordered protein
    • DOI 10.1016/j.febslet.2004.09.036, PII S0014579304011512
    • Weathers, E. A., Paulaitis, M. E., Woolf, T. B., and Hoh, J. H. (2004) Reduced amino acid alphabet is sufficient to accurately recognize intrinsically disordered protein. FEBS Lett. 576, 348-352 (Pubitemid 39388626)
    • (2004) FEBS Letters , vol.576 , Issue.3 , pp. 348-352
    • Weathers, E.A.1    Paulaitis, M.E.2    Woolf, T.B.3    Hoh, J.H.4
  • 44
    • 0842268045 scopus 로고    scopus 로고
    • Supra-domains: Evolutionary Units Larger than Single Protein Domains
    • DOI 10.1016/j.jmb.2003.12.026
    • Vogel, C., Berzuini, C., Bashton, M., Gough, J., and Teichmann, S. A. (2004) Supra-domains: evolutionary units larger than single protein domains. J. Mol. Biol. 336, 809-823 (Pubitemid 38183030)
    • (2004) Journal of Molecular Biology , vol.336 , Issue.3 , pp. 809-823
    • Vogel, C.1    Berzuini, C.2    Bashton, M.3    Gough, J.4    Teichmann, S.A.5
  • 45
    • 22244450719 scopus 로고    scopus 로고
    • Protein families and their evolution - A structural perspective
    • DOI 10.1146/annurev.biochem.74.082803.133029
    • Orengo, C. A., and Thornton, J. M. (2005) Protein families and their evolution- a structural perspective. Annu. Rev. Biochem. 74, 867-900 (Pubitemid 40995526)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 867-900
    • Orengo, C.A.1    Thornton, J.M.2
  • 46
    • 72149090671 scopus 로고    scopus 로고
    • FANCM connects the genome instability disorders Bloom's syndrome and Fanconi anemia
    • Deans, A. J., and West, S. C. (2009) FANCM connects the genome instability disorders Bloom's syndrome and Fanconi anemia. Mol. Cell 36, 943-953
    • (2009) Mol. Cell , vol.36 , pp. 943-953
    • Deans, A.J.1    West, S.C.2
  • 49
    • 84860263013 scopus 로고    scopus 로고
    • The structure of the FANCM-MHF complex reveals physical features for functional assembly
    • Tao, Y., Jin, C., Li, X., Qi, S., Chu, L., Niu, L., Yao, X., and Teng, M. (2012) The structure of the FANCM-MHF complex reveals physical features for functional assembly. Nat. Commun. 3, 782
    • (2012) Nat. Commun. , vol.3 , pp. 782
    • Tao, Y.1    Jin, C.2    Li, X.3    Qi, S.4    Chu, L.5    Niu, L.6    Yao, X.7    Teng, M.8
  • 51
    • 84880768893 scopus 로고    scopus 로고
    • Readers of PCNA modifications
    • Ulrich, H. D., and Takahashi, T. (2013) Readers of PCNA modifications. Chromosoma 122, 259-274
    • (2013) Chromosoma , vol.122 , pp. 259-274
    • Ulrich, H.D.1    Takahashi, T.2
  • 53
    • 84878890561 scopus 로고    scopus 로고
    • RecJ-like protein from Pyrococcus furiosus has 3′-5′ exonuclease activity on RNA: Implications for proofreading of 3′-mismatched RNA primers in DNA replication
    • Yuan, H., Liu, X. P., Han, Z., Allers, T., Hou, J. L., and Liu, J. H. (2013) RecJ-like protein from Pyrococcus furiosus has 3′-5′ exonuclease activity on RNA: implications for proofreading of 3′-mismatched RNA primers in DNA replication. Nucleic Acids Res. 41, 5817-5826
    • (2013) Nucleic Acids Res. , vol.41 , pp. 5817-5826
    • Yuan, H.1    Liu, X.P.2    Han, Z.3    Allers, T.4    Hou, J.L.5    Liu, J.H.6


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