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Volumn 40, Issue 1, 2012, Pages 333-344

TRNA His-guanylyltransferase establishes tRNA His identity

Author keywords

[No Author keywords available]

Indexed keywords

HISTIDINE TRANSFER RNA; HISTIDINE TRANSFER RNA GUANYLYLTRANSFERASE; INORGANIC PYROPHOSPHATASE; TETRAMER; TRANSFER RNA; TRANSFERASE; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATE; NUCLEOTIDYLTRANSFERASE; TRNA GUANYLYLTRANSFERASE;

EID: 84855286097     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkr696     Document Type: Article
Times cited : (37)

References (47)
  • 1
    • 3643114575 scopus 로고    scopus 로고
    • Universal rules and idiosyncratic features in tRNA identity
    • Giegé R., Sissler, M. and Florentz, C. (1998) Universal rules and idiosyncratic features in tRNA identity. Nucleic Acids Res., 26, 5017-5035.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5017-5035
    • Giegé, R.1    Sissler, M.2    Florentz, C.3
  • 2
    • 0024472840 scopus 로고
    • Role of the extra C-G pair at the end of the acceptor stem of tRNA(His) in aminoacylation
    • Himeno, H., Hasegawa, T., Ueda, T., Watanabe, K., Miura, K. and Shimizu, M. (1989) Role of the extra G-C pair at the end of the acceptor stem of tRNAHis in aminoacylation. Nucleic Acids Res., 17, 7855-7863. (Pubitemid 19251952)
    • (1989) Nucleic Acids Research , vol.17 , Issue.19 , pp. 7855-7863
    • Himeno, H.1    Hasegawa, T.2    Ueda, T.3    Watanabe, K.4    Miura, K.5    Shimizu, M.6
  • 3
    • 0025114689 scopus 로고
    • Enzymatic aminoacylation of an eight-base-pair microhelix with histidine
    • Francklyn, C. and Schimmel, P. (1990) Enzymatic aminoacylation of an eight-base-pair microhelix with histidine. Proc. Natl Acad. Sci. USA, 87, 8655-8659.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 8655-8659
    • Francklyn, C.1    Schimmel, P.2
  • 4
    • 0028569503 scopus 로고
    • Histidylation by yeast HisRS of tRNA or tRNA-like structure relies on residues -1 and 73 but is dependent on the RNA context
    • Rudinger, J., Florentz, C. and Giegé R. (1994) Histidylation by yeast HisRS of tRNA or tRNA-like structure relies on residues -1 and 73 but is dependent on the RNA context. Nucleic Acids Res., 22, 5031-5037.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5031-5037
    • Rudinger, J.1    Florentz, C.2    Giegé, R.3
  • 6
    • 0034636138 scopus 로고    scopus 로고
    • Function of the extra 5'-phosphate carried by histidine tRNA
    • DOI 10.1021/bi9923297
    • Fromant, M., Plateau, P. and Blanquet, S. (2000) Function of the extra 50-phosphate carried by histidine tRNA. Biochemistry, 39, 4062-4067. (Pubitemid 30210383)
    • (2000) Biochemistry , vol.39 , Issue.14 , pp. 4062-4067
    • Fromant, M.1    Plateau, P.2    Blanquet, S.3
  • 7
    • 0942268921 scopus 로고    scopus 로고
    • G-1:C73 Recognition by an Arginine Cluster in the Active Site of Escherichia coli Histidyl-tRNA Synthetase
    • Connolly, S.A., Rosen, A.E., Musier-Forsyth, K. and Francklyn, C.S. (2004) G-1:C73 recognition by an arginine cluster in the active site of Escherichia coli histidyl-tRNA synthetase. Biochemistry, 43, 962-969. (Pubitemid 38141494)
    • (2004) Biochemistry , vol.43 , Issue.4 , pp. 962-969
    • Connolly, S.A.1    Rosen, A.E.2    Musier-Forsyth, K.3    Francklyn, C.S.4
  • 8
    • 33745615842 scopus 로고    scopus 로고
    • Evolutionary conservation of a functionally important backbone phosphate group critical for aminoacylation of histidine tRNAs
    • DOI 10.1261/rna.78606
    • Rosen, A.E., Brooks, B.S., Guth, E., Francklyn, C.S. and Musier-Forsyth, K. (2006) Evolutionary conservation of a functionally important backbone phosphate group critical for aminoacylation of histidine tRNAs. RNA, 12, 1315-1322. (Pubitemid 43990556)
    • (2006) RNA , vol.12 , Issue.7 , pp. 1315-1322
    • Rosen, A.E.1    Brooks, B.S.2    Guth, E.3    Francklyn, C.S.4    Musier-Forsyth, K.5
  • 9
    • 0347129810 scopus 로고    scopus 로고
    • Recognition of G-1:C73 Atomic Groups by Escherichia coli Histidyl-tRNA Synthetase
    • Rosen, A.E. and Musier-Forsyth, K. (2004) Recognition of G-1:C73 atomic groups by Escherichia coli histidyl-tRNA synthetase. J. Am. Chem. Soc., 126, 64-65. (Pubitemid 38090340)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.1 , pp. 64-65
    • Rosen, A.E.1    Musier-Forsyth, K.2
  • 10
    • 0022652241 scopus 로고
    • The additional guanylate at the 5' terminus of Escherichia coli tRNA(His) is the result of unusual processing by RNase P
    • Orellana, O., Cooley, L. and Söll, D. (1986) The additional guanylate at the 50 terminus of Escherichia coli tRNAHis is the result of unusual processing by RNase P. Mol. Cell. Biol., 6, 525-529. (Pubitemid 16158127)
    • (1986) Molecular and Cellular Biology , vol.6 , Issue.2 , pp. 525-529
    • Orellana, O.1    Cooley, L.2    Soll, D.3
  • 11
    • 0023871272 scopus 로고
    • Processing of histidine transfer RNA precursors. Abnormal cleavage site for RNase P
    • Burkard, U., Willis, I. and Söll, D. (1988) Processing of histidine transfer RNA precursors. Abnormal cleavage site for RNase P. J. Biol. Chem., 263, 2447-2451. (Pubitemid 18060310)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.5 , pp. 2447-2451
    • Burkard, U.1    Willis, I.2    Soll, D.3
  • 12
    • 0036702994 scopus 로고    scopus 로고
    • The residue immediately upstream of the RNase P cleavage site is a positive determinant
    • DOI 10.1016/S0300-9084(02)01462-1, PII S0300908402014621
    • Brannvall, M., Fredrik Pettersson, B.M. and Kirsebom, L.A. (2002) The residue immediately upstream of the RNase P cleavage site is a positive determinant. Biochimie., 84, 693-703. (Pubitemid 35363454)
    • (2002) Biochimie , vol.84 , Issue.8 , pp. 693-703
    • Brannvall, M.1    Fredrik Pettersson, B.M.2    Kirsebom, L.A.3
  • 13
    • 33644853072 scopus 로고    scopus 로고
    • TFAM detects co-evolution of tRNA identity rules with lateral transfer of histidyl-tRNA synthetase
    • DOI 10.1093/nar/gkj449
    • Ardell, D.H. and Andersson, S.G. (2006) TFAM detects co-evolution of tRNA identity rules with lateral transfer of histidyl-tRNA synthetase. Nucleic Acids Res., 34, 893-904. (Pubitemid 43380673)
    • (2006) Nucleic Acids Research , vol.34 , Issue.3 , pp. 893-904
    • Ardell, D.H.1    Andersson, S.G.E.2
  • 14
    • 33947398845 scopus 로고    scopus 로고
    • Loss of a universal tRNA feature
    • DOI 10.1128/JB.01203-06
    • Wang, C., Sobral, B.W. and Williams, K.P. (2007) Loss of a universal tRNA feature. J. Bacteriol., 189, 1954-1962. (Pubitemid 46446159)
    • (2007) Journal of Bacteriology , vol.189 , Issue.5 , pp. 1954-1962
    • Wang, C.1    Sobral, B.W.2    Williams, K.P.3
  • 15
    • 79953706300 scopus 로고    scopus 로고
    • Change of tRNA identity leads to a divergent orthogonal histidyl-tRNA synthetase/ tRNAHis pair
    • Yuan, J., Gogakos, T., Babina, A.M., Söll, D. and Randau, L. (2011) Change of tRNA identity leads to a divergent orthogonal histidyl-tRNA synthetase/ tRNAHis pair. Nucleic Acids Res., 39, 2286-2293.
    • (2011) Nucleic Acids Res , vol.39 , pp. 2286-2293
    • Yuan, J.1    Gogakos, T.2    Babina, A.M.3    Söll, D.4    Randau, L.5
  • 17
    • 0025335285 scopus 로고
    • Enzymatic addition of guanylate to histidine transfer RNA
    • DOI 10.1016/0076-6879(90)81143-I
    • Williams, J.B., Cooley, L. and Söll, D. (1990) Enzymatic addition of guanylate to histidine transfer RNA. Methods Enzymol., 181, 451-462. (Pubitemid 20219715)
    • (1990) Methods in Enzymology , vol.181 , pp. 451-462
    • Williams, J.B.1    Cooley, L.2    Soll, D.3
  • 18
    • 0026333172 scopus 로고
    • Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae: I. Purification and physical properties
    • Pande, S., Jahn, D. and Söll, D. (1991) Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. I. Purification and physical properties. J. Biol. Chem., 266, 22826-22831. (Pubitemid 21908725)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.34 , pp. 22826-22831
    • Pande, S.1    Jahn, D.2    Soll, D.3
  • 19
    • 0026317972 scopus 로고
    • Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae: II. Catalytic mechanism
    • Jahn, D. and Pande, S. (1991) Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. II. Catalytic mechanism. J. Biol. Chem., 266, 22832-22836. (Pubitemid 21908726)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.34 , pp. 22832-22836
    • Jahn, D.1    Pande, S.2
  • 20
    • 0348014687 scopus 로고    scopus 로고
    • His
    • DOI 10.1101/gad.1148603
    • Gu, W., Jackman, J.E., Lohan, A.J., Gray, M.W. and Phizicky, E.M. (2003) tRNAHis maturation: an essential yeast protein catalyzes addition of a guanine nucleotide to the 50 end of tRNAHis. Genes Dev., 17, 2889-2901. (Pubitemid 37523154)
    • (2003) Genes and Development , vol.17 , Issue.23 , pp. 2889-2901
    • Gu, W.1    Jackman, J.E.2    Lohan, A.J.3    Gray, M.W.4    Phizicky, E.M.5
  • 22
    • 0026769570 scopus 로고
    • Transfer RNA genes in the mitochondrial genome from a liverwort, Marchantia polymorpha: The absence of chloroplast-like tRNAs
    • Oda, K., Yamato, K., Ohta, E., Nakamura, Y., Takemura, M., Nozato, N., Akashi, K. and Ohyama, K. (1992) Transfer RNA genes in the mitochondrial genome from a liverwort, Marchantia polymorpha: the absence of chloroplast-like tRNAs. Nucleic Acids Res., 20, 3773-3777.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3773-3777
    • Oda, K.1    Yamato, K.2    Ohta, E.3    Nakamura, Y.4    Takemura, M.5    Nozato, N.6    Akashi, K.7    Ohyama, K.8
  • 23
    • 0141621017 scopus 로고    scopus 로고
    • RNA editing of larch mitochondrial tRNA(His) precursors is a prerequisite for processing
    • Maré hal-Drouard, L., Kumar, R., Remacle, C. and Small, I. (1996) RNA editing of larch mitochondrial tRNAHis precursors is a prerequisite for processing. Nucleic Acids Res., 24, 3229-3234. (Pubitemid 26278565)
    • (1996) Nucleic Acids Research , vol.24 , Issue.16 , pp. 3229-3234
    • Marechal-Drouard, L.1    Raman Kumar, R.K.2    Remacle, C.3    Small, L.4
  • 24
    • 0031021278 scopus 로고    scopus 로고
    • The mitochondrial genome of Arabidopsis thaliana contains 57 genes in 366, 924 nucleotides
    • Unseld, M., Marienfeld, J.R., Brandt, P. and Brennicke, A. (1997) The mitochondrial genome of Arabidopsis thaliana contains 57 genes in 366, 924 nucleotides. Nat. Genet., 15, 57-61.
    • (1997) Nat. Genet. , vol.15 , pp. 57-61
    • Unseld, M.1    Marienfeld, J.R.2    Brandt, P.3    Brennicke, A.4
  • 26
    • 24344499742 scopus 로고    scopus 로고
    • 5C
    • DOI 10.1128/MCB.25.18.8191-8201.2005
    • Gu, W., Hurto, R.L., Hopper, A.K., Grayhack, E.J. and Phizicky, E.M. (2005) Depletion of Saccharomyces cerevisiae tRNAHis guanylyltransferase Thg1p leads to uncharged tRNAHis with additional m5C. Mol. Cell. Biol., 25, 8191-8201. (Pubitemid 41263010)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.18 , pp. 8191-8201
    • Gu, W.1    Hurto, R.L.2    Hopper, A.K.3    Grayhack, E.J.4    Phizicky, E.M.5
  • 27
    • 77951171100 scopus 로고    scopus 로고
    • The requirement for the highly conserved G-1 residue of Saccharomyces cerevisiae tRNAHis can be circumvented by overexpression of tRNAHis and its synthetase
    • Preston, M.A. and Phizicky, E.M. (2010) The requirement for the highly conserved G-1 residue of Saccharomyces cerevisiae tRNAHis can be circumvented by overexpression of tRNAHis and its synthetase. RNA, 16, 1068-1077.
    • (2010) RNA , vol.16 , pp. 1068-1077
    • Preston, M.A.1    Phizicky, E.M.2
  • 28
    • 33646870599 scopus 로고    scopus 로고
    • His by recognition of the anticodon, one of several features unexpectedly shared with tRNA synthetases
    • DOI 10.1261/rna.54706
    • Jackman, J.E. and Phizicky, E.M. (2006) tRNAHis guanylyltransferase adds G-1 to the 50 end of tRNAHis by recognition of the anticodon, one of several features unexpectedly shared with tRNA synthetases. RNA, 12, 1007-1014. (Pubitemid 43788119)
    • (2006) RNA , vol.12 , Issue.6 , pp. 1007-1014
    • Jackman, J.E.1    Phizicky, E.M.2
  • 29
    • 77955662753 scopus 로고    scopus 로고
    • 30-50 tRNAHis guanylyltransferase in bacteria
    • Heinemann, I.U., Randau, L., Tomko, R.J. Jr and Söll, D. (2010) 30-50 tRNAHis guanylyltransferase in bacteria. FEBS Lett., 584, 3567-3572.
    • (2010) FEBS Lett , vol.584 , pp. 3567-3572
    • Heinemann, I.U.1    Randau, L.2    Tomko, Jr.R.J.3    Söll, D.4
  • 30
    • 79953016145 scopus 로고    scopus 로고
    • TRNA 50-end repair activities of tRNAHis guanylyltransferase (Thg1)-like proteins from bacteria and archaea
    • Rao, B.S., Maris, E.L. and Jackman, J.E. (2011) tRNA 50-end repair activities of tRNAHis guanylyltransferase (Thg1)-like proteins from bacteria and archaea. Nucleic Acids Res., 39, 1833-1842.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 1833-1842
    • Rao, B.S.1    Maris, E.L.2    Jackman, J.E.3
  • 31
    • 63049085489 scopus 로고    scopus 로고
    • TRNAs as regulators in gene expression
    • Li, Y. and Zhou, H. (2009) tRNAs as regulators in gene expression. Sci. China C Life Sci., 52, 245-252.
    • (2009) Sci. China C Life Sci. , vol.52 , pp. 245-252
    • Li, Y.1    Zhou, H.2
  • 32
    • 0033635215 scopus 로고    scopus 로고
    • Uncharged tRNA activates GCN2 by displacing the protein kinase moiety from a bipartite tRNA-binding domain
    • Dong, J., Qiu, H., Garcia-Barrio, M., Anderson, J. and Hinnebusch, A.G. (2000) Uncharged tRNA activates GCN2 by displacing the protein kinase moiety from a bipartite tRNA-binding domain. Mol. Cell, 6, 269-279.
    • (2000) Mol. Cell , vol.6 , pp. 269-279
    • Dong, J.1    Qiu, H.2    Garcia-Barrio, M.3    Anderson, J.4    Hinnebusch, A.G.5
  • 33
  • 34
    • 76249089296 scopus 로고    scopus 로고
    • Template-dependent 30-50 nucleotide addition is a shared feature of tRNAHis guanylyltransferase enzymes from multiple domains of life
    • Abad, M.G., Rao, B.S. and Jackman, J.E. (2010) Template-dependent 30-50 nucleotide addition is a shared feature of tRNAHis guanylyltransferase enzymes from multiple domains of life. Proc. Natl Acad. Sci. USA, 107, 674-679.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 674-679
    • Abad, M.G.1    Rao, B.S.2    Jackman, J.E.3
  • 35
    • 0026561924 scopus 로고
    • Overlapping nucleotide determinants for specific aminoacylation of RNA microhelices
    • Francklyn, C., Shi, J.P. and Schimmel, P. (1992) Overlapping nucleotide determinants for specific aminoacylation of RNA microhelices. Science, 255, 1121-1125.
    • (1992) Science , vol.255 , pp. 1121-1125
    • Francklyn, C.1    Shi, J.P.2    Schimmel, P.3
  • 36
  • 38
    • 78650524780 scopus 로고    scopus 로고
    • TRNAHis guanylyltransferase (THG1), a unique 30-50 nucleotidyl transferase, shares unexpected structural homology with canonical 50-30 DNA polymerases
    • Hyde, S.J., Eckenroth, B.E., Smith, B.A., Eberley, W.A., Heintz, N.H., Jackman, J.E. and Doublié , S. (2010) tRNAHis guanylyltransferase (THG1), a unique 30-50 nucleotidyl transferase, shares unexpected structural homology with canonical 50-30 DNA polymerases. Proc. Natl Acad. Sci. USA, 107, 20305-20310.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 20305-20310
    • Hyde, S.J.1    Eckenroth, B.E.2    Smith, B.A.3    Eberley, W.A.4    Heintz, N.H.5    Jackman, J.E.6    Doublié, S.7
  • 39
    • 34250875706 scopus 로고    scopus 로고
    • Initiation of RNA Decay in Escherichia coli by 5′ Pyrophosphate Removal
    • DOI 10.1016/j.molcel.2007.05.038, PII S1097276507003644
    • Celesnik, H., Deana, A. and Belasco, J.G. (2007) Initiation of RNA decay in Escherichia coli by 50 pyrophosphate removal. Mol. Cell, 27, 79-90. (Pubitemid 46991386)
    • (2007) Molecular Cell , vol.27 , Issue.1 , pp. 79-90
    • Celesnik, H.1    Deana, A.2    Belasco, J.G.3
  • 40
    • 38349117689 scopus 로고    scopus 로고
    • The bacterial enzyme RppH triggers messenger RNA degradation by 50 pyrophosphate removal
    • Deana, A., Celesnik, H. and Belasco, J.G. (2008) The bacterial enzyme RppH triggers messenger RNA degradation by 50 pyrophosphate removal. Nature, 451, 355-358.
    • (2008) Nature , vol.451 , pp. 355-358
    • Deana, A.1    Celesnik, H.2    Belasco, J.G.3
  • 41
    • 79952998913 scopus 로고    scopus 로고
    • A role for tRNAHis guanylyltransferase (Thg1)-like proteins from Dictyostelium discoideum in mitochondrial 50-tRNA editing
    • Abad, M.G., Long, Y., Willcox, A., Gott, J.M., Gray, M.W. and Jackman, J.E. (2011) A role for tRNAHis guanylyltransferase (Thg1)-like proteins from Dictyostelium discoideum in mitochondrial 50-tRNA editing. RNA, 17, 613-623.
    • (2011) RNA , vol.17 , pp. 613-623
    • Abad, M.G.1    Long, Y.2    Willcox, A.3    Gott, J.M.4    Gray, M.W.5    Jackman, J.E.6
  • 42
    • 0032992906 scopus 로고    scopus 로고
    • A novel nucleotide incorporation activity implicated in the editing of mitochondrial transfer RNAs in Acanthamoeba castellanii
    • DOI 10.1017/S1355838299981840
    • Price, D.H. and Gray, M.W. (1999) A novel nucleotide incorporation activity implicated in the editing of mitochondrial transfer RNAs in Acanthamoeba castellanii. RNA, 5, 302-317. (Pubitemid 29079289)
    • (1999) RNA , vol.5 , Issue.2 , pp. 302-317
    • Price, D.H.1    Gray, M.W.2
  • 43
    • 13244296941 scopus 로고    scopus 로고
    • In vitro characterization of a tRNA editing activity in the mitochondria of Spizellomyces punctatus, a chytridiomycete fungus
    • DOI 10.1074/jbc.M411273200
    • Bullerwell, C.E. and Gray, M.W. (2005) In vitro characterization of a tRNA editing activity in the mitochondria of Spizellomyces punctatus, a Chytridiomycete fungus. J. Biol. Chem., 280, 2463-2470. (Pubitemid 40189346)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.4 , pp. 2463-2470
    • Bullerwell, C.E.1    Gray, M.W.2
  • 44
    • 78650556009 scopus 로고    scopus 로고
    • Crystal structure of a reverse polymerase
    • Perona, J.J. and Oza, J.P. (2010) Crystal structure of a reverse polymerase. Proc. Natl Acad. Sci. USA, 107, 20149-20150.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 20149-20150
    • Perona, J.J.1    Oza, J.P.2
  • 45
    • 77954058183 scopus 로고    scopus 로고
    • Presence of a classical RRM-fold palm domain in Thg1-type 30-50nucleic acid polymerases and the origin of the GGDEF and CRISPR polymerase domains
    • Anantharaman, V., Iyer, L.M. and Aravind, L. (2010) Presence of a classical RRM-fold palm domain in Thg1-type 30-50nucleic acid polymerases and the origin of the GGDEF and CRISPR polymerase domains. Biol. Direct., 5, 43.
    • (2010) Biol. Direct , vol.5 , pp. 43
    • Anantharaman, V.1    Iyer, L.M.2    Aravind, L.3
  • 46
    • 42349104471 scopus 로고    scopus 로고
    • His guanylyltransferase
    • DOI 10.1021/bi702517q
    • Jackman, J.E. and Phizicky, E.M. (2008) Identification of critical residues for G-1 addition and substrate recognition by tRNAHis guanylyltransferase. Biochemistry, 47, 4817-4825. (Pubitemid 351555503)
    • (2008) Biochemistry , vol.47 , Issue.16 , pp. 4817-4825
    • Jackman, J.E.1    Phizicky, E.M.2
  • 47
    • 18044375584 scopus 로고    scopus 로고
    • 2/M phase transition in the yeast Saccharomyces cerevisiae
    • DOI 10.1128/EC.4.4.832-835.2005
    • Rice, T.S., Ding, M., Pederson, D.S. and Heintz, N.H. (2005) The highly conserved tRNAHis guanylyltransferase Thg1p interacts with the origin recognition complex and is required for the G2/M phase transition in the yeast Saccharomyces cerevisiae. Eukaryot. Cell., 4, 832-835. (Pubitemid 40600436)
    • (2005) Eukaryotic Cell , vol.4 , Issue.4 , pp. 832-835
    • Rice, T.S.1    Ding, M.2    Pederson, D.S.3    Heintz, N.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.