메뉴 건너뛰기




Volumn 45, Issue 6, 2008, Pages 994-1007

Mitochondrial mediation of environmental osmolytes discrimination during osmoadaptation in the extremely halotolerant black yeast Hortaea werneckii

Author keywords

14 3 3; ATPase; Dothideales; Ecology; Extremophiles; Metabolism; Mitochondria; Osmoadaptation; Proteome

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONE; LIPID; SODIUM CHLORIDE;

EID: 43049165906     PISSN: 10871845     EISSN: 10960937     Source Type: Journal    
DOI: 10.1016/j.fgb.2008.01.006     Document Type: Article
Times cited : (27)

References (52)
  • 1
    • 0034724182 scopus 로고    scopus 로고
    • Lipid rafts function in biosynthetic delivery of proteins to the cell surface in yeast
    • Bagnat M., et al. Lipid rafts function in biosynthetic delivery of proteins to the cell surface in yeast. Proc. Natl. Acad. Sci. USA 97 (2000) 3254-3259
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3254-3259
    • Bagnat, M.1
  • 2
    • 11144245522 scopus 로고    scopus 로고
    • Pseudouridylation at position 32 of mitochondrial and cytoplasmic tRNAs requires two distinct enzymes in Saccharomyces cerevisiae
    • Behm-Ansmant I., et al. Pseudouridylation at position 32 of mitochondrial and cytoplasmic tRNAs requires two distinct enzymes in Saccharomyces cerevisiae. J. Biol. Chem. 279 (2004) 52998-53006
    • (2004) J. Biol. Chem. , vol.279 , pp. 52998-53006
    • Behm-Ansmant, I.1
  • 3
    • 0024199702 scopus 로고
    • Purification of vacuolar membranes, mitochondria, and plasma membranes from Neurospora crassa and modes of discriminating among the different H+ATPases
    • Bowman E.J., and Bowman B.J. Purification of vacuolar membranes, mitochondria, and plasma membranes from Neurospora crassa and modes of discriminating among the different H+ATPases. Methods Enzymol. 157 (1988) 562-573
    • (1988) Methods Enzymol. , vol.157 , pp. 562-573
    • Bowman, E.J.1    Bowman, B.J.2
  • 4
    • 0035957331 scopus 로고    scopus 로고
    • 14-3-3 Protein is a regulator of the mitochondrial and chloroplast ATP synthase
    • Bunney T.D., et al. 14-3-3 Protein is a regulator of the mitochondrial and chloroplast ATP synthase. Proc. Natl. Acad. Sci. USA 98 (2001) 4249-4254
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4249-4254
    • Bunney, T.D.1
  • 5
    • 0030000860 scopus 로고    scopus 로고
    • A new pathway for protein export in Saccharomyces cerevisiae
    • Cleves A.E., et al. A new pathway for protein export in Saccharomyces cerevisiae. J. Cell Biol. 133 (1996) 1017-1026
    • (1996) J. Cell Biol. , vol.133 , pp. 1017-1026
    • Cleves, A.E.1
  • 6
    • 0036828866 scopus 로고    scopus 로고
    • A novel mitochondrial protein, Tar1p, is encoded on the antisense strand of the nuclear 25S rDNA
    • Coelho P.S., et al. A novel mitochondrial protein, Tar1p, is encoded on the antisense strand of the nuclear 25S rDNA. Genes Dev. 16 (2002) 2755-2760
    • (2002) Genes Dev. , vol.16 , pp. 2755-2760
    • Coelho, P.S.1
  • 7
    • 0036668632 scopus 로고    scopus 로고
    • Dealing with osmostress through MAP kinase activation
    • de Nadal E., et al. Dealing with osmostress through MAP kinase activation. EMBO Rep. 3 (2002) 735-740
    • (2002) EMBO Rep. , vol.3 , pp. 735-740
    • de Nadal, E.1
  • 8
    • 34548412860 scopus 로고    scopus 로고
    • Nonclassical export pathway: overexpression of NCE102 reduces protein and DNA damage and prolongs lifespan in an SGS1 deficient Saccharomyces cerevisiae
    • Desmyter L., et al. Nonclassical export pathway: overexpression of NCE102 reduces protein and DNA damage and prolongs lifespan in an SGS1 deficient Saccharomyces cerevisiae. Biogerontology 8 (2007) 527-535
    • (2007) Biogerontology , vol.8 , pp. 527-535
    • Desmyter, L.1
  • 9
    • 0034652301 scopus 로고    scopus 로고
    • Automated identification of amino acid sequence variations in proteins by HPLC/microspray tandem mass spectrometry
    • Gatlin C.L., et al. Automated identification of amino acid sequence variations in proteins by HPLC/microspray tandem mass spectrometry. Anal. Chem. 72 (2000) 757-763
    • (2000) Anal. Chem. , vol.72 , pp. 757-763
    • Gatlin, C.L.1
  • 10
    • 33750814308 scopus 로고    scopus 로고
    • Identification and characterization of ENA ATPases HwENA1 and HwENA2 from the halophilic black yeast Hortaea werneckii
    • Gorjan A., and Plemenitas A. Identification and characterization of ENA ATPases HwENA1 and HwENA2 from the halophilic black yeast Hortaea werneckii. FEMS Microbiol. Lett. 265 (2006) 41-50
    • (2006) FEMS Microbiol. Lett. , vol.265 , pp. 41-50
    • Gorjan, A.1    Plemenitas, A.2
  • 11
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green D.R., and Kroemer G. The pathophysiology of mitochondrial cell death. Science 305 (2004) 626-629
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 12
    • 0034034614 scopus 로고    scopus 로고
    • Hypersaline waters in salterns: natural ecological niches for halophilic black yeasts
    • Gunde-Cimerman N., Zalar P., de Hoog G.S., and Plemenitaš A. Hypersaline waters in salterns: natural ecological niches for halophilic black yeasts. FEMS Microbiol. Ecol. 32 (2000) 235-340
    • (2000) FEMS Microbiol. Ecol. , vol.32 , pp. 235-340
    • Gunde-Cimerman, N.1    Zalar, P.2    de Hoog, G.S.3    Plemenitaš, A.4
  • 13
    • 0036282743 scopus 로고    scopus 로고
    • Osmotic stress signaling and osmoadaptation in yeasts
    • Hohmann S. Osmotic stress signaling and osmoadaptation in yeasts. Microbiol. Mol. Biol. Rev. 66 (2002) 300-372
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 300-372
    • Hohmann, S.1
  • 14
    • 3242705680 scopus 로고    scopus 로고
    • The functional organization of mitochondrial genomes in human cells
    • Iborra F.J., et al. The functional organization of mitochondrial genomes in human cells. BMC Biol. 2 (2004) 9
    • (2004) BMC Biol. , vol.2 , pp. 9
    • Iborra, F.J.1
  • 15
    • 2442672938 scopus 로고    scopus 로고
    • Transcriptomic and proteomic analysis of a 14-3-3 gene-deficient yeast
    • Ichimura T., et al. Transcriptomic and proteomic analysis of a 14-3-3 gene-deficient yeast. Biochemistry 43 (2004) 6149-6158
    • (2004) Biochemistry , vol.43 , pp. 6149-6158
    • Ichimura, T.1
  • 16
    • 22044432618 scopus 로고    scopus 로고
    • Control of mitochondrial shape
    • Jensen R.E. Control of mitochondrial shape. Curr. Opin. Cell Biol. 17 (2005) 384-388
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 384-388
    • Jensen, R.E.1
  • 17
    • 0016893730 scopus 로고
    • [Succinate dehydrogenase activity of isolated myocardial mitochondria during chronic insufficiency]
    • Kleimenova N.N., et al. [Succinate dehydrogenase activity of isolated myocardial mitochondria during chronic insufficiency]. Bull. Exp. Biol. Med. 81 (1976) 37-40
    • (1976) Bull. Exp. Biol. Med. , vol.81 , pp. 37-40
    • Kleimenova, N.N.1
  • 18
    • 33746174612 scopus 로고    scopus 로고
    • Hypersaline conditions induce changes in cell-wall melanization and colony structure in a halophilic and a xerophilic black yeast species of the genus Trimmatostroma
    • Kogej T., et al. Hypersaline conditions induce changes in cell-wall melanization and colony structure in a halophilic and a xerophilic black yeast species of the genus Trimmatostroma. Mycol. Res. 110 (2006) 713-724
    • (2006) Mycol. Res. , vol.110 , pp. 713-724
    • Kogej, T.1
  • 19
    • 32044455999 scopus 로고    scopus 로고
    • The halophilic fungus Hortaea werneckii and the halotolerant fungus Aureobasidium pullulans maintain low intracellular cation concentrations in hypersaline environments
    • Kogej T., et al. The halophilic fungus Hortaea werneckii and the halotolerant fungus Aureobasidium pullulans maintain low intracellular cation concentrations in hypersaline environments. Appl. Environ. Microbiol. 71 (2005) 6600-6605
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 6600-6605
    • Kogej, T.1
  • 20
    • 34250875710 scopus 로고    scopus 로고
    • The MAP kinase HwHog1 from the halophilic black yeast Hortaea werneckii: coping with stresses in solar salterns
    • Lenassi M., et al. The MAP kinase HwHog1 from the halophilic black yeast Hortaea werneckii: coping with stresses in solar salterns. Saline Syst. 3 (2007) 3
    • (2007) Saline Syst. , vol.3 , pp. 3
    • Lenassi, M.1
  • 21
    • 1042284932 scopus 로고    scopus 로고
    • Protein profiling with cleavable isotope-coded affinity tag (cICAT) reagents: the yeast salinity stress response
    • Li J., et al. Protein profiling with cleavable isotope-coded affinity tag (cICAT) reagents: the yeast salinity stress response. Mol. Cell. Proteomics 2 (2003) 1198-1204
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1198-1204
    • Li, J.1
  • 22
    • 16544391103 scopus 로고    scopus 로고
    • Enhanced photosynthesis and redox energy production contribute to salinity tolerance in Dunaliella as revealed by homology-based proteomics
    • Liska A.J., et al. Enhanced photosynthesis and redox energy production contribute to salinity tolerance in Dunaliella as revealed by homology-based proteomics. Plant Physiol. 136 (2004) 2806-2817
    • (2004) Plant Physiol. , vol.136 , pp. 2806-2817
    • Liska, A.J.1
  • 23
    • 33845656956 scopus 로고    scopus 로고
    • Mitochondrial retrograde signaling
    • Liu Z., and Butow R.A. Mitochondrial retrograde signaling. Annu. Rev. Genet. 40 (2006) 159-185
    • (2006) Annu. Rev. Genet. , vol.40 , pp. 159-185
    • Liu, Z.1    Butow, R.A.2
  • 24
    • 0031009910 scopus 로고    scopus 로고
    • SHY1, the yeast homolog of the mammalian SURF-1 gene, encodes a mitochondrial protein required for respiration
    • Mashkevich G., et al. SHY1, the yeast homolog of the mammalian SURF-1 gene, encodes a mitochondrial protein required for respiration. J. Biol. Chem. 272 (1997) 14356-14364
    • (1997) J. Biol. Chem. , vol.272 , pp. 14356-14364
    • Mashkevich, G.1
  • 25
    • 0036081347 scopus 로고    scopus 로고
    • MIPS: a database for genomes and protein sequences
    • Mewes H.W., et al. MIPS: a database for genomes and protein sequences. Nucleic Acids Res. 30 (2002) 31-34
    • (2002) Nucleic Acids Res. , vol.30 , pp. 31-34
    • Mewes, H.W.1
  • 26
    • 33644875537 scopus 로고    scopus 로고
    • MIPS: analysis and annotation of proteins from whole genomes in 2005
    • Mewes H.W., et al. MIPS: analysis and annotation of proteins from whole genomes in 2005. Nucleic Acids Res. 34 (2006) D169-D172
    • (2006) Nucleic Acids Res. , vol.34
    • Mewes, H.W.1
  • 27
    • 0035781005 scopus 로고    scopus 로고
    • Plant mitochondria and oxidative stress: electron transport, NADPH turnover, and metabolism of reactive oxygen species
    • Moller I.M. Plant mitochondria and oxidative stress: electron transport, NADPH turnover, and metabolism of reactive oxygen species. Annu. Rev. Plant Physiol. Plant Mol. Biol. 52 (2001) 561-591
    • (2001) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.52 , pp. 561-591
    • Moller, I.M.1
  • 28
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert W. Protein import into mitochondria. Annu. Rev. Biochem. 66 (1997) 863-917
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 29
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: releasing power for life and unleashing the machineries of death
    • Newmeyer D.D., and Ferguson-Miller S. Mitochondria: releasing power for life and unleashing the machineries of death. Cell 112 (2003) 481-490
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 30
    • 0031041461 scopus 로고    scopus 로고
    • Metabolic and regulatory changes associated with growth of Saccharomyces cerevisiae in 14 M NaCl. Evidence for osmotic induction of glycerol dissimilation via the dihydroxyacetone pathway
    • Norbeck J., and Blomberg A. Metabolic and regulatory changes associated with growth of Saccharomyces cerevisiae in 14 M NaCl. Evidence for osmotic induction of glycerol dissimilation via the dihydroxyacetone pathway. J. Biol. Chem. 272 (1997) 5544-5554
    • (1997) J. Biol. Chem. , vol.272 , pp. 5544-5554
    • Norbeck, J.1    Blomberg, A.2
  • 31
    • 0018384650 scopus 로고
    • Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction
    • Ohkawa H., et al. Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal. Biochem. 95 (1979) 351-358
    • (1979) Anal. Biochem. , vol.95 , pp. 351-358
    • Ohkawa, H.1
  • 32
    • 1042266670 scopus 로고    scopus 로고
    • The yeast mitochondrial proteome, a study of fermentative and respiratory growth
    • Ohlmeier S., et al. The yeast mitochondrial proteome, a study of fermentative and respiratory growth. J. Biol. Chem. 279 (2004) 3956-3979
    • (2004) J. Biol. Chem. , vol.279 , pp. 3956-3979
    • Ohlmeier, S.1
  • 33
    • 33745898503 scopus 로고    scopus 로고
    • Role of oxidative stress in the extremely salt-tolerant yeast Hortaea werneckii
    • Petrovic U. Role of oxidative stress in the extremely salt-tolerant yeast Hortaea werneckii. FEMS Yeast Res. 6 (2006) 816-822
    • (2006) FEMS Yeast Res. , vol.6 , pp. 816-822
    • Petrovic, U.1
  • 34
    • 0032757006 scopus 로고    scopus 로고
    • Salt stress affects sterol biosynthesis in the halophilic black yeast Hortaea werneckii
    • Petrovic U., et al. Salt stress affects sterol biosynthesis in the halophilic black yeast Hortaea werneckii. FEMS Microbiol. Lett. 180 (1999) 325-330
    • (1999) FEMS Microbiol. Lett. , vol.180 , pp. 325-330
    • Petrovic, U.1
  • 35
    • 0036372944 scopus 로고    scopus 로고
    • Cellular responses to environmental salinity in the halophilic black yeast Hortaea werneckii
    • Petrovic U., et al. Cellular responses to environmental salinity in the halophilic black yeast Hortaea werneckii. Mol. Microbiol. 45 (2002) 665-672
    • (2002) Mol. Microbiol. , vol.45 , pp. 665-672
    • Petrovic, U.1
  • 36
    • 0034667203 scopus 로고    scopus 로고
    • Mirror orientation selection (MOS): a method for eliminating false positive clones from libraries generated by suppression subtractive hybridization
    • Rebrikov D.V., et al. Mirror orientation selection (MOS): a method for eliminating false positive clones from libraries generated by suppression subtractive hybridization. Nucleic Acids Res. 28 (2000) E90
    • (2000) Nucleic Acids Res. , vol.28
    • Rebrikov, D.V.1
  • 37
    • 0032491533 scopus 로고    scopus 로고
    • The yeast RAD7 and RAD16 genes are required for postincision events during nucleotide excision repair. In vitro and in vivo studies with rad7 and rad16 mutants and purification of a Rad7/Rad16-containing protein complex
    • Reed S.H., et al. The yeast RAD7 and RAD16 genes are required for postincision events during nucleotide excision repair. In vitro and in vivo studies with rad7 and rad16 mutants and purification of a Rad7/Rad16-containing protein complex. J. Biol. Chem. 273 (1998) 29481-29488
    • (1998) J. Biol. Chem. , vol.273 , pp. 29481-29488
    • Reed, S.H.1
  • 38
    • 36749053957 scopus 로고    scopus 로고
    • Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase
    • Reinders J., et al. Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase. Mol. Cell. Proteomics (2007)
    • (2007) Mol. Cell. Proteomics
    • Reinders, J.1
  • 39
    • 33745851905 scopus 로고    scopus 로고
    • Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics
    • Reinders J., et al. Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 5 (2006) 1543-1554
    • (2006) J. Proteome Res. , vol.5 , pp. 1543-1554
    • Reinders, J.1
  • 40
    • 0034708436 scopus 로고    scopus 로고
    • The transcriptional response of Saccharomyces cerevisiae to osmotic shock. Hot1p and Msn2p/Msn4p are required for the induction of subsets of high osmolarity glycerol pathway-dependent genes
    • Rep M., et al. The transcriptional response of Saccharomyces cerevisiae to osmotic shock. Hot1p and Msn2p/Msn4p are required for the induction of subsets of high osmolarity glycerol pathway-dependent genes. J. Biol. Chem. 275 (2000) 8290-8300
    • (2000) J. Biol. Chem. , vol.275 , pp. 8290-8300
    • Rep, M.1
  • 41
    • 9144257282 scopus 로고    scopus 로고
    • The FunCat, a functional annotation scheme for systematic classification of proteins from whole genomes
    • Ruepp A., et al. The FunCat, a functional annotation scheme for systematic classification of proteins from whole genomes. Nucleic Acids Res. 32 (2004) 5539-5545
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5539-5545
    • Ruepp, A.1
  • 42
    • 34250811284 scopus 로고    scopus 로고
    • Mitochondrial-nuclear communications
    • Ryan M.T., and Hoogenraad N.J. Mitochondrial-nuclear communications. Annu. Rev. Biochem. 76 (2007) 701-722
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 701-722
    • Ryan, M.T.1    Hoogenraad, N.J.2
  • 43
    • 0036536714 scopus 로고    scopus 로고
    • Mitochondrial dynamics and division in budding yeast
    • Shaw J.M., and Nunnari J. Mitochondrial dynamics and division in budding yeast. Trends Cell Biol. 12 (2002) 178-184
    • (2002) Trends Cell Biol. , vol.12 , pp. 178-184
    • Shaw, J.M.1    Nunnari, J.2
  • 44
    • 0345687191 scopus 로고    scopus 로고
    • The proteome of Saccharomyces cerevisiae mitochondria
    • Sickmann A., et al. The proteome of Saccharomyces cerevisiae mitochondria. Proc. Natl. Acad. Sci. USA 100 (2003) 13207-13212
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13207-13212
    • Sickmann, A.1
  • 45
    • 4644332290 scopus 로고    scopus 로고
    • Salt-induced changes in lipid composition and membrane fluidity of halophilic yeast-like melanized fungi
    • Turk M., et al. Salt-induced changes in lipid composition and membrane fluidity of halophilic yeast-like melanized fungi. Extremophiles 8 (2004) 53-61
    • (2004) Extremophiles , vol.8 , pp. 53-61
    • Turk, M.1
  • 46
    • 0033928677 scopus 로고    scopus 로고
    • Response of Saccharomyces cerevisiae to severe osmotic stress: evidence for a novel activation mechanism of the HOG MAP kinase pathway
    • Van Wuytswinkel O., et al. Response of Saccharomyces cerevisiae to severe osmotic stress: evidence for a novel activation mechanism of the HOG MAP kinase pathway. Mol. Microbiol. 37 (2000) 382-397
    • (2000) Mol. Microbiol. , vol.37 , pp. 382-397
    • Van Wuytswinkel, O.1
  • 47
    • 34948850255 scopus 로고    scopus 로고
    • Novel 3'-phosphoadenosine-5′-phosphatases from extremely halotolerant Hortaea werneckii reveal insight into molecular determinants of salt tolerance of black yeasts
    • Vaupotic T., et al. Novel 3'-phosphoadenosine-5′-phosphatases from extremely halotolerant Hortaea werneckii reveal insight into molecular determinants of salt tolerance of black yeasts. Fungal Genet. Biol. (2007)
    • (2007) Fungal Genet. Biol.
    • Vaupotic, T.1
  • 48
    • 35348986998 scopus 로고    scopus 로고
    • Differential gene expression and Hog1 interaction with osmoresponsive genes in the extremely halotolerant black yeast Hortaea werneckii
    • Vaupotic T., and Plemenitas A. Differential gene expression and Hog1 interaction with osmoresponsive genes in the extremely halotolerant black yeast Hortaea werneckii. BMC Genomics 8 (2007) 280
    • (2007) BMC Genomics , vol.8 , pp. 280
    • Vaupotic, T.1    Plemenitas, A.2
  • 49
    • 34447270809 scopus 로고    scopus 로고
    • Osmoadaptation-dependent activity of microsomal HMG-CoA reductase in the extremely halotolerant black yeast Hortaea werneckii is regulated by ubiquitination
    • Vaupotic T., and Plemenitas A. Osmoadaptation-dependent activity of microsomal HMG-CoA reductase in the extremely halotolerant black yeast Hortaea werneckii is regulated by ubiquitination. FEBS Lett. 581 (2007) 3391-3395
    • (2007) FEBS Lett. , vol.581 , pp. 3391-3395
    • Vaupotic, T.1    Plemenitas, A.2
  • 50
    • 0036308235 scopus 로고    scopus 로고
    • Merging mitochondria matters: cellular role and molecular machinery of mitochondrial fusion
    • Westermann B. Merging mitochondria matters: cellular role and molecular machinery of mitochondrial fusion. EMBO Rep. 3 (2002) 527-531
    • (2002) EMBO Rep. , vol.3 , pp. 527-531
    • Westermann, B.1
  • 51
    • 0035844224 scopus 로고    scopus 로고
    • Transcript expression in Saccharomyces cerevisiae at high salinity
    • Yale J., and Bohnert H.J. Transcript expression in Saccharomyces cerevisiae at high salinity. J. Biol. Chem. 276 (2001) 15996-16007
    • (2001) J. Biol. Chem. , vol.276 , pp. 15996-16007
    • Yale, J.1    Bohnert, H.J.2
  • 52
    • 0029000674 scopus 로고
    • An enzyme in yeast mitochondria that catalyzes a step in branched-chain amino acid biosynthesis also functions in mitochondrial DNA stability
    • Zelenaya-Troitskaya O., et al. An enzyme in yeast mitochondria that catalyzes a step in branched-chain amino acid biosynthesis also functions in mitochondrial DNA stability. EMBO J. 14 (1995) 3268-3276
    • (1995) EMBO J. , vol.14 , pp. 3268-3276
    • Zelenaya-Troitskaya, O.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.