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Volumn 36, Issue 21, 2008, Pages 6848-6858

The divergent eukaryote Trichomonas vaginalis has an m7G cap methyltransferase capable of a single N2 methylation

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; METHYLTRANSFERASE; RNA;

EID: 57149085059     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkn706     Document Type: Article
Times cited : (10)

References (53)
  • 1
    • 0026730321 scopus 로고
    • Mass spectrometry of mRNA cap 4 from trypanosomatids reveals two novel nucleosides
    • Bangs,J.D., Crain,P.F., Hashizume,T., McCloskey,J.A. and Boothroyd,J.C. (1992) Mass spectrometry of mRNA cap 4 from trypanosomatids reveals two novel nucleosides. J. Biol. Chem., 267, 9805-9815.
    • (1992) J. Biol. Chem , vol.267 , pp. 9805-9815
    • Bangs, J.D.1    Crain, P.F.2    Hashizume, T.3    McCloskey, J.A.4    Boothroyd, J.C.5
  • 2
    • 47949123390 scopus 로고    scopus 로고
    • Spliceosomal snRNAs in the unicellular eukaryote Trichomonas vaginalis are structurally conserved but lack a 5′ cap structure
    • Simoes-Barbosa,A., Meloni,D., Wohlschlegel,J. A., Konarska,M.M. and Johnson,P.J. (2008) Spliceosomal snRNAs in the unicellular eukaryote Trichomonas vaginalis are structurally conserved but lack a 5′ cap structure. RNA, 14, 1617-1631.
    • (2008) RNA , vol.14 , pp. 1617-1631
    • Simoes-Barbosa, A.1    Meloni, D.2    Wohlschlegel, J.A.3    Konarska, M.M.4    Johnson, P.J.5
  • 3
    • 25444482810 scopus 로고    scopus 로고
    • Giardia lamblia RNA cap guanine-N2 methyltransferase (Tgs2)
    • Hausmann,S. and Shuman,S. (2005) Giardia lamblia RNA cap guanine-N2 methyltransferase (Tgs2). J. Biol. Chem., 280, 32101-32106.
    • (2005) J. Biol. Chem , vol.280 , pp. 32101-32106
    • Hausmann, S.1    Shuman, S.2
  • 4
    • 0034602344 scopus 로고    scopus 로고
    • A kingdom-level phylogeny of eukaryotes based on combined protein data
    • Baldauf,S.L., Roger,A.J., Wenk-Siefert,I. and Doolittle,W.F. (2000) A kingdom-level phylogeny of eukaryotes based on combined protein data. Science, 290, 972-977.
    • (2000) Science , vol.290 , pp. 972-977
    • Baldauf, S.L.1    Roger, A.J.2    Wenk-Siefert, I.3    Doolittle, W.F.4
  • 6
    • 0032716365 scopus 로고    scopus 로고
    • Upstream regulatory sequences required for expression of the Trichomonas vaginalis alpha-succinyl CoA synthetase gene
    • Liston,D.R., Carrero,J.C. and Johnson,P.J. (1999) Upstream regulatory sequences required for expression of the Trichomonas vaginalis alpha-succinyl CoA synthetase gene. Mol. Biochem. Parasitol., 104, 323-329.
    • (1999) Mol. Biochem. Parasitol , vol.104 , pp. 323-329
    • Liston, D.R.1    Carrero, J.C.2    Johnson, P.J.3
  • 7
    • 0034775449 scopus 로고    scopus 로고
    • Initiator recognition in a primitive eukaryote: IBP39, an initiator-binding protein from Trichomonas vaginalis
    • Liston,D.R., Lau,A.O., Ortiz,D., Smale,S.T. and Johnson,P.J. (2001) Initiator recognition in a primitive eukaryote: IBP39, an initiator-binding protein from Trichomonas vaginalis. Mol. Cell. Biol., 21, 7872-7882.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 7872-7882
    • Liston, D.R.1    Lau, A.O.2    Ortiz, D.3    Smale, S.T.4    Johnson, P.J.5
  • 8
    • 0345690206 scopus 로고    scopus 로고
    • Structural basis of core promoter recognition in a primitive eukaryote
    • Schumacher,M.A., Lau,A.O. and Johnson,P.J. (2003) Structural basis of core promoter recognition in a primitive eukaryote. Cell, 115 413-424.
    • (2003) Cell , vol.115 , pp. 413-424
    • Schumacher, M.A.1    Lau, A.O.2    Johnson, P.J.3
  • 10
    • 15444370758 scopus 로고    scopus 로고
    • Spliceosomal introns in the deep-branching eukaryote Trichomonas vaginalis
    • Vanacova,S., Yan,W., Carlton,J.M. and Johnson,P.J. (2005) Spliceosomal introns in the deep-branching eukaryote Trichomonas vaginalis. Proc. Natl Acad. Sci. USA, 102, 4430-4435.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 4430-4435
    • Vanacova, S.1    Yan, W.2    Carlton, J.M.3    Johnson, P.J.4
  • 11
    • 0023047717 scopus 로고
    • Cap trimethylation of U snRNA is cytoplasmic and dependent on U snRNP protein binding
    • Mattaj,I.W. (1986) Cap trimethylation of U snRNA is cytoplasmic and dependent on U snRNP protein binding. Cell, 46, 905-911.
    • (1986) Cell , vol.46 , pp. 905-911
    • Mattaj, I.W.1
  • 13
    • 0033539171 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae telomerase is an Sm small nuclear ribonucleoprotein particle
    • Seto,A.G., Zaug,A.J., Sobel,S.G., Wolin,S.L. and Cech,T.R. (1999) Saccharomyces cerevisiae telomerase is an Sm small nuclear ribonucleoprotein particle. Nature, 401, 177-180.
    • (1999) Nature , vol.401 , pp. 177-180
    • Seto, A.G.1    Zaug, A.J.2    Sobel, S.G.3    Wolin, S.L.4    Cech, T.R.5
  • 14
    • 0025237190 scopus 로고
    • trans-spliced Caenorhabditis elegans mRNAs retain trimethylguanosine caps
    • Liou,R.F. and Blumenthal,T. (1990) trans-spliced Caenorhabditis elegans mRNAs retain trimethylguanosine caps. Mol. Cell. Biol., 10, 1764-1768.
    • (1990) Mol. Cell. Biol , vol.10 , pp. 1764-1768
    • Liou, R.F.1    Blumenthal, T.2
  • 16
    • 14244264414 scopus 로고    scopus 로고
    • Specificity and mechanism of RNA cap guanine-N2 methyltransferase (Tgs1)
    • Hausmann,S. and Shuman,S. (2005) Specificity and mechanism of RNA cap guanine-N2 methyltransferase (Tgs1). J. Biol. Chem., 280, 4021-4024.
    • (2005) J. Biol. Chem , vol.280 , pp. 4021-4024
    • Hausmann, S.1    Shuman, S.2
  • 17
    • 0028176685 scopus 로고
    • m3G cap hypermethylation of U1 small nuclear ribonucleoprotein (snRNP) in vitro: Evidence that the U1 small nuclear RNA-(guanosine-N2)-methyltransferase is a non-snRNP cytoplasmic protein that requires a binding site on the Sm core domain
    • Plessel,G., Fischer,U. and Luhrmann,R. (1994) m3G cap hypermethylation of U1 small nuclear ribonucleoprotein (snRNP) in vitro: Evidence that the U1 small nuclear RNA-(guanosine-N2)-methyltransferase is a non-snRNP cytoplasmic protein that requires a binding site on the Sm core domain. Mol. Cell. Biol., 14, 4160-4172.
    • (1994) Mol. Cell. Biol , vol.14 , pp. 4160-4172
    • Plessel, G.1    Fischer, U.2    Luhrmann, R.3
  • 18
    • 0037017403 scopus 로고    scopus 로고
    • The importin-beta binding domain of snurportin1 is responsible for the Ran- and energy-independent nuclear import of spliceosomal U snRNPs in vitro
    • Huber,J., Dickmanns,A. and Luhrmann,R. (2002) The importin-beta binding domain of snurportin1 is responsible for the Ran- and energy-independent nuclear import of spliceosomal U snRNPs in vitro. J. Cell. Biol., 156, 467-479.
    • (2002) J. Cell. Biol , vol.156 , pp. 467-479
    • Huber, J.1    Dickmanns, A.2    Luhrmann, R.3
  • 20
    • 0029098641 scopus 로고
    • A common maturation pathway for small nucleolar RNAs
    • Terns,M.P., Grimm,C., Lund,E. and Dahlberg,J.E. (1995) A common maturation pathway for small nucleolar RNAs. EMBO J., 14, 4860-4871.
    • (1995) EMBO J , vol.14 , pp. 4860-4871
    • Terns, M.P.1    Grimm, C.2    Lund, E.3    Dahlberg, J.E.4
  • 21
    • 0034669349 scopus 로고    scopus 로고
    • The box C/D motif directs snoRNA 50-cap hypermethylation
    • Speckmann,W.A., Terns,R.M. and Terns,M.P. (2000) The box C/D motif directs snoRNA 50-cap hypermethylation. Nucleic Acids Res., 28 4467-4473.
    • (2000) Nucleic Acids Res , vol.28 , pp. 4467-4473
    • Speckmann, W.A.1    Terns, R.M.2    Terns, M.P.3
  • 22
    • 0042591787 scopus 로고    scopus 로고
    • Interaction between the small-nuclear-RNA cap hypermethylase and the spinal muscular atrophy protein, survival of motor neuron
    • Mouaikel,J., Narayanan,U., Verheggen,C., Matera,A.G., Bertrand,E., Tazi,J. and Bordonne,R. (2003) Interaction between the small-nuclear-RNA cap hypermethylase and the spinal muscular atrophy protein, survival of motor neuron. EMBO Rep., 4, 616-622.
    • (2003) EMBO Rep , vol.4 , pp. 616-622
    • Mouaikel, J.1    Narayanan, U.2    Verheggen, C.3    Matera, A.G.4    Bertrand, E.5    Tazi, J.6    Bordonne, R.7
  • 24
    • 0036238278 scopus 로고    scopus 로고
    • Hypermethylation of the cap structure of both yeast snRNAs and snoRNAs requires a conserved methyltransferase that is localized to the nucleolus
    • Mouaikel,J., Verheggen,C., Bertrand,E., Tazi,J. and Bordonne,R. (2002) Hypermethylation of the cap structure of both yeast snRNAs and snoRNAs requires a conserved methyltransferase that is localized to the nucleolus. Mol. Cell, 9, 891-901.
    • (2002) Mol. Cell , vol.9 , pp. 891-901
    • Mouaikel, J.1    Verheggen, C.2    Bertrand, E.3    Tazi, J.4    Bordonne, R.5
  • 25
    • 34447250502 scopus 로고    scopus 로고
    • Characterization of the Trypanosoma brucei cap hypermethylase Tgs1
    • Ruan,J.P., Ullu,E. and Tschudi,C. (2007) Characterization of the Trypanosoma brucei cap hypermethylase Tgs1. Mol. Biochem. Parasitol., 155, 66-69.
    • (2007) Mol. Biochem. Parasitol , vol.155 , pp. 66-69
    • Ruan, J.P.1    Ullu, E.2    Tschudi, C.3
  • 26
    • 0344012478 scopus 로고    scopus 로고
    • Sequence-structure-function relationships of Tgs1, the yeast snRNA/ snoRNA cap hypermethylase
    • Mouaikel,J., Bujnicki,J.M., Tazi,J. and Bordonne,R. (2003) Sequence-structure-function relationships of Tgs1, the yeast snRNA/ snoRNA cap hypermethylase. Nucleic Acids Res., 31, 4899-4909.
    • (2003) Nucleic Acids Res , vol.31 , pp. 4899-4909
    • Mouaikel, J.1    Bujnicki, J.M.2    Tazi, J.3    Bordonne, R.4
  • 28
    • 34247152861 scopus 로고    scopus 로고
    • Biochemical and genetic analysis of RNA cap guanine-N2 methyltransferases from Giardia lamblia and Schizosaccharomyces pombe
    • Hausmann,S., Ramirez,A., Schneider,S., Schwer,B. and Shuman,S. (2007) Biochemical and genetic analysis of RNA cap guanine-N2 methyltransferases from Giardia lamblia and Schizosaccharomyces pombe. Nucleic Acids Res., 35, 1411-1420.
    • (2007) Nucleic Acids Res , vol.35 , pp. 1411-1420
    • Hausmann, S.1    Ramirez, A.2    Schneider, S.3    Schwer, B.4    Shuman, S.5
  • 29
    • 34548801413 scopus 로고    scopus 로고
    • Detection of enzymatic activity of transfer RNA modification enzymes using radiolabeled tRNA substrates
    • Grosjean,H., Droogmans,L., Roovers,M. and Keith,G. (2007) Detection of enzymatic activity of transfer RNA modification enzymes using radiolabeled tRNA substrates. Methods Enzymol., 425, 55-101.
    • (2007) Methods Enzymol , vol.425 , pp. 55-101
    • Grosjean, H.1    Droogmans, L.2    Roovers, M.3    Keith, G.4
  • 30
    • 73049130725 scopus 로고
    • A method for determining the sedimentation behavior of enzymes: Application to protein mixtures
    • Martin,R.G. and Ames,B.N. (1961) A method for determining the sedimentation behavior of enzymes: Application to protein mixtures. J. Biol. Chem., 236, 1372-1379.
    • (1961) J. Biol. Chem , vol.236 , pp. 1372-1379
    • Martin, R.G.1    Ames, B.N.2
  • 31
    • 0038386050 scopus 로고    scopus 로고
    • 3D-Jury: A simple approach to improve protein structure predictions
    • Ginalski,K., Elofsson,A., Fischer,D. and Rychlewski,L. (2003) 3D-Jury: A simple approach to improve protein structure predictions. Bioinformatics, 19, 1015-1018.
    • (2003) Bioinformatics , vol.19 , pp. 1015-1018
    • Ginalski, K.1    Elofsson, A.2    Fischer, D.3    Rychlewski, L.4
  • 32
    • 3042513877 scopus 로고    scopus 로고
    • Structural characterization and comparative phylogenetic analysis of Escherichia coli HemK, a protein (N5)-glutamine methyltransferase
    • Yang,Z., Shipman,L., Zhang,M., Anton,B.P., Roberts,R.J. and Cheng,X. (2004) Structural characterization and comparative phylogenetic analysis of Escherichia coli HemK, a protein (N5)-glutamine methyltransferase. J. Mol. Biol., 340, 695-706.
    • (2004) J. Mol. Biol , vol.340 , pp. 695-706
    • Yang, Z.1    Shipman, L.2    Zhang, M.3    Anton, B.P.4    Roberts, R.J.5    Cheng, X.6
  • 33
    • 0029361476 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali,A. (1995) Comparative protein modeling by satisfaction of spatial restraints. Mol. Med. Today, 1, 270-277.
    • (1995) Mol. Med. Today , vol.1 , pp. 270-277
    • Sali, A.1
  • 34
    • 0031307019 scopus 로고    scopus 로고
    • Evaluation of comparative protein structure modeling by MODELLER-3
    • Sanchez,R. and Sali,A. (1997) Evaluation of comparative protein structure modeling by MODELLER-3. Proteins, 68 (Suppl 1), 50-58.
    • (1997) Proteins , vol.68 , Issue.SUPPL. 1 , pp. 50-58
    • Sanchez, R.1    Sali, A.2
  • 35
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • Sippl,M.J. (1993) Recognition of errors in three-dimensional structures of proteins. Proteins, 17, 355-362.
    • (1993) Proteins , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 36
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski,R.A., Moss,D.S. and Thornton,J.M. (1993) Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol., 231, 1049-1067.
    • (1993) J. Mol. Biol , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 38
    • 41249089761 scopus 로고    scopus 로고
    • The TbMTr1 spliced leader RNA cap 1 2′-O-ribose methyltransferase from Trypanosoma brucei acts with substrate specificity
    • Mittra,B., Zamudio,J.R., Bujnicki,J.M., Stepinski,J., Darzynkiewicz,E., Campbell,D.A. and Sturm,N.R. (2008) The TbMTr1 spliced leader RNA cap 1 2′-O-ribose methyltransferase from Trypanosoma brucei acts with substrate specificity. J. Biol. Chem., 283, 3161-3172.
    • (2008) J. Biol. Chem , vol.283 , pp. 3161-3172
    • Mittra, B.1    Zamudio, J.R.2    Bujnicki, J.M.3    Stepinski, J.4    Darzynkiewicz, E.5    Campbell, D.A.6    Sturm, N.R.7
  • 40
    • 0028029304 scopus 로고
    • Characterization of putative small nuclear RNAs from Giardia lamblia
    • Niu,X.H., Hartshorne,T., He,X.Y. and Agabian,N. (1994) Characterization of putative small nuclear RNAs from Giardia lamblia. Mol. Biochem. Parasitol., 66, 49-57.
    • (1994) Mol. Biochem. Parasitol , vol.66 , pp. 49-57
    • Niu, X.H.1    Hartshorne, T.2    He, X.Y.3    Agabian, N.4
  • 41
    • 0017190334 scopus 로고
    • Di-and trimethylated congeners of 7-methylguanine in Sindbis virus mRNA
    • HsuChen,C.C. and Dubin,D.T. (1976) Di-and trimethylated congeners of 7-methylguanine in Sindbis virus mRNA. Nature, 264, 190-191.
    • (1976) Nature , vol.264 , pp. 190-191
    • HsuChen, C.C.1    Dubin, D.T.2
  • 42
    • 0022515626 scopus 로고
    • Additional methylation at the N(2)-position of the cap of 26S Semliki Forest virus late mRNA and initiation of translation
    • van Duijn,L.P., Kasperaitis,M., Ameling,C. and Voorma,H.O. (1986) Additional methylation at the N(2)-position of the cap of 26S Semliki Forest virus late mRNA and initiation of translation. Virus Res., 5, 61-66.
    • (1986) Virus Res , vol.5 , pp. 61-66
    • van Duijn, L.P.1    Kasperaitis, M.2    Ameling, C.3    Voorma, H.O.4
  • 43
  • 45
    • 0033614843 scopus 로고    scopus 로고
    • Cai,A., Jankowska-Anyszka,M., Centers,A., Chlebicka,L., Stepinski,J., Stolarski,R., Darzynkiewicz,E. and Rhoads,R.E. (1999) Quantitative assessment of mRNA cap analogues as inhibitors of in vitro translation. Biochemistry, 38, 8538-8547.
    • Cai,A., Jankowska-Anyszka,M., Centers,A., Chlebicka,L., Stepinski,J., Stolarski,R., Darzynkiewicz,E. and Rhoads,R.E. (1999) Quantitative assessment of mRNA cap analogues as inhibitors of in vitro translation. Biochemistry, 38, 8538-8547.
  • 46
    • 18944375265 scopus 로고    scopus 로고
    • Identification in the ancient protist Giardia lamblia of two eukaryotic translation initiation factor 4E homologues with distinctive functions
    • Li,L. and Wang,C.C. (2005) Identification in the ancient protist Giardia lamblia of two eukaryotic translation initiation factor 4E homologues with distinctive functions. Eukaryot. Cell, 4, 948-959.
    • (2005) Eukaryot. Cell , vol.4 , pp. 948-959
    • Li, L.1    Wang, C.C.2
  • 47
    • 18944364447 scopus 로고    scopus 로고
    • Trm11p and Trm112p are both required for the formation of 2-methylguanosine at position 10 in yeast tRNA
    • Purushothaman,S.K., Bujnicki,J.M., Grosjean,H. and Lapeyre,B. (2005) Trm11p and Trm112p are both required for the formation of 2-methylguanosine at position 10 in yeast tRNA. Mol. Cell. Biol., 25, 4359-4370.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 4359-4370
    • Purushothaman, S.K.1    Bujnicki, J.M.2    Grosjean, H.3    Lapeyre, B.4
  • 48
    • 0022996130 scopus 로고
    • Isolation and characterization of the TRM1 locus, a gene essential for the N2,N2-dimethylguanosine modification of both mitochondrial and cytoplasmic tRNA in Saccharomyces cerevisiae
    • Ellis,S.R., Morales,M.J., Li,J.M., Hopper,A.K. and Martin,N.C. (1986) Isolation and characterization of the TRM1 locus, a gene essential for the N2,N2-dimethylguanosine modification of both mitochondrial and cytoplasmic tRNA in Saccharomyces cerevisiae. J. Biol. Chem., 261, 9703-9709.
    • (1986) J. Biol. Chem , vol.261 , pp. 9703-9709
    • Ellis, S.R.1    Morales, M.J.2    Li, J.M.3    Hopper, A.K.4    Martin, N.C.5
  • 49
    • 0032814863 scopus 로고    scopus 로고
    • Characterisation and enzymatic properties of tRNA(guanine 26, N (2), N (2))-dimethyltransferase (Trm1p) from Pyrococcus furiosus
    • Constantinesco,F., Motorin,Y. and Grosjean,H. (1999) Characterisation and enzymatic properties of tRNA(guanine 26, N (2), N (2))-dimethyltransferase (Trm1p) from Pyrococcus furiosus. J. Mol. Biol., 291, 375-392.
    • (1999) J. Mol. Biol , vol.291 , pp. 375-392
    • Constantinesco, F.1    Motorin, Y.2    Grosjean, H.3
  • 50
    • 0034666278 scopus 로고    scopus 로고
    • The human tRNA(m(2)(2)G(26)) dimethyltransferase: Functional expression and characterization of a cloned hTRM1 gene
    • Liu,J. and Straby,K.B. (2000) The human tRNA(m(2)(2)G(26)) dimethyltransferase: Functional expression and characterization of a cloned hTRM1 gene. Nucleic Acids Res., 28, 3445-3451.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3445-3451
    • Liu, J.1    Straby, K.B.2
  • 51
    • 4344606710 scopus 로고    scopus 로고
    • N2-methylation of guanosine at position 10 in tRNA is catalyzed by a THUMP domain-containing, S-adenosylmethionine-dependent methyltransferase, conserved in Archaea and Eukaryota
    • Armengaud,J., Urbonavicius,J., Fernandez,B., Chaussinand,G., Bujnicki,J.M. and Grosjean,H. (2004) N2-methylation of guanosine at position 10 in tRNA is catalyzed by a THUMP domain-containing, S-adenosylmethionine-dependent methyltransferase, conserved in Archaea and Eukaryota. J. Biol. Chem., 279, 37142-37152.
    • (2004) J. Biol. Chem , vol.279 , pp. 37142-37152
    • Armengaud, J.1    Urbonavicius, J.2    Fernandez, B.3    Chaussinand, G.4    Bujnicki, J.M.5    Grosjean, H.6
  • 52
    • 0033534617 scopus 로고    scopus 로고
    • Purification, cloning, and characterization of the 16 S RNA m2G1207 methyltransferase from Escherichia coli
    • Tscherne,J.S., Nurse,K., Popienick,P. and Ofengand,J. (1999) Purification, cloning, and characterization of the 16 S RNA m2G1207 methyltransferase from Escherichia coli. J. Biol. Chem., 274 924-929.
    • (1999) J. Biol. Chem , vol.274 , pp. 924-929
    • Tscherne, J.S.1    Nurse, K.2    Popienick, P.3    Ofengand, J.4
  • 53
    • 0012588361 scopus 로고    scopus 로고
    • RNA: (guanine-N2) methyltransferases RsmC/RsmD and their homologs revisited-bioinformatic analysis and prediction of the active site based on the uncharacterized Mj0882 protein structure
    • Bujnicki,J.M. and Rychlewski,L. (2002) RNA: (guanine-N2) methyltransferases RsmC/RsmD and their homologs revisited-bioinformatic analysis and prediction of the active site based on the uncharacterized Mj0882 protein structure. BMC Bioinformatics, 3, 10.
    • (2002) BMC Bioinformatics , vol.3 , pp. 10
    • Bujnicki, J.M.1    Rychlewski, L.2


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