메뉴 건너뛰기




Volumn 11, Issue 11, 2012, Pages 5548-5555

Proteomics wants cRacker: Automated standardized data analysis of LC-MS derived proteomic data

Author keywords

automation; ion intensities; large scale data analysis; multivariate statistics; quantitative proteomics; software tool

Indexed keywords

ANALYSIS OF VARIANCE; ARTICLE; COMPUTER PROGRAM; DATA ANALYSIS; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; PRIORITY JOURNAL; PROFESSIONAL KNOWLEDGE; PROTEIN ANALYSIS; PROTEIN PROCESSING; PROTEOMICS; STATISTICAL ANALYSIS;

EID: 84868316169     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr300413v     Document Type: Article
Times cited : (29)

References (57)
  • 1
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R.; Mann, M. Mass spectrometry-based proteomics Nature 2003, 422 (6928) 198-207
    • (2003) Nature , vol.422 , Issue.6928 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 2
    • 77954925947 scopus 로고    scopus 로고
    • The multifunctional protein in peroxisomal beta-oxidation: Structure and substrate specificity of the Arabidopsis thaliana protein MFP2
    • Arent, S.; Christensen, C. E.; Pye, V. E.; Nørgaard, A.; Henriksen, A. The multifunctional protein in peroxisomal beta-oxidation: structure and substrate specificity of the Arabidopsis thaliana protein MFP2 J. Biol. Chem. 2010, 285 (31) 24066-24077
    • (2010) J. Biol. Chem. , vol.285 , Issue.31 , pp. 24066-24077
    • Arent, S.1    Christensen, C.E.2    Pye, V.E.3    Nørgaard, A.4    Henriksen, A.5
  • 3
    • 84856702955 scopus 로고    scopus 로고
    • The use of heavy nitrogen in quantitative proteomics experiments in plants
    • Arsova, B.; Kierszniowska, S.; Schulze, W. X. The use of heavy nitrogen in quantitative proteomics experiments in plants Trends Plant Sci. 2012, 17 (2) 102-112
    • (2012) Trends Plant Sci. , vol.17 , Issue.2 , pp. 102-112
    • Arsova, B.1    Kierszniowska, S.2    Schulze, W.X.3
  • 6
    • 0030003893 scopus 로고    scopus 로고
    • Ultrastructural and biochemical characterization of autophagy in higher plant cells subjected to carbon deprivation: Control by the supply of mitochondria with respiratory substrates
    • Aubert, S.; Gout, E.; Bligny, R.; Marty-Mazars, D.; Barrieu, F.; Alabouvette, J.; Marty, F.; Douce, R. Ultrastructural and biochemical characterization of autophagy in higher plant cells subjected to carbon deprivation: control by the supply of mitochondria with respiratory substrates J. Cell Biol. 1996, 133 (6) 1251-1263
    • (1996) J. Cell Biol. , vol.133 , Issue.6 , pp. 1251-1263
    • Aubert, S.1    Gout, E.2    Bligny, R.3    Marty-Mazars, D.4    Barrieu, F.5    Alabouvette, J.6    Marty, F.7    Douce, R.8
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 1976, 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 65649154049 scopus 로고    scopus 로고
    • StatQuant: A post-quantification analysis toolbox for improving quantitative mass spectrometry
    • van Breukelen, B.; van den Toorn, H. W. P.; Drugan, M. M.; Heck, A. J. R. StatQuant: a post-quantification analysis toolbox for improving quantitative mass spectrometry Bioinformatics (Oxford, England) 2009, 25 (11) 1472-1473
    • (2009) Bioinformatics (Oxford, England) , vol.25 , Issue.11 , pp. 1472-1473
    • Van Breukelen, B.1    Van Den Toorn, H.W.P.2    Drugan, M.M.3    Heck, A.J.R.4
  • 10
    • 0000724392 scopus 로고
    • Study of glucose starvation in excised maize root tips
    • Brouquisse, R.; James, F.; Raymond, P.; Pradet, A. Study of glucose starvation in excised maize root tips Plant Physiol. 1991, 96 (2) 619-626
    • (1991) Plant Physiol. , vol.96 , Issue.2 , pp. 619-626
    • Brouquisse, R.1    James, F.2    Raymond, P.3    Pradet, A.4
  • 12
    • 77952956167 scopus 로고    scopus 로고
    • Decoding signalling networks by mass spectrometry-based proteomics
    • Choudhary, C.; Mann, M. Decoding signalling networks by mass spectrometry-based proteomics Nat. Rev. Mol. Cell Biol. 2010, 11 (6) 427-439
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , Issue.6 , pp. 427-439
    • Choudhary, C.1    Mann, M.2
  • 13
    • 34547556725 scopus 로고    scopus 로고
    • Introduction to computational proteomics
    • Colinge, J.; Bennett, K. L. Introduction to computational proteomics PLoS Comput. Biol. 2007, 3 (7):e114
    • (2007) PLoS Comput. Biol. , vol.3 , Issue.7 , pp. 114
    • Colinge, J.1    Bennett, K.L.2
  • 14
    • 77949487184 scopus 로고    scopus 로고
    • Increase in catalase-3 activity as a response to use of alternative catabolic substrates during sucrose starvation
    • Contento, A. L; Bassham, D. C. Increase in catalase-3 activity as a response to use of alternative catabolic substrates during sucrose starvation Plant Physiol. Biochem. 2010, 48 (4) 232-238
    • (2010) Plant Physiol. Biochem. , vol.48 , Issue.4 , pp. 232-238
    • Contento, A.L.1    Bassham, D.C.2
  • 15
    • 4444288688 scopus 로고    scopus 로고
    • Transcriptome profiling of the response of Arabidopsis suspension culture cells to Suc starvation
    • Contento, A. L.; Kim, S.-J.; Bassham, D. C. Transcriptome profiling of the response of Arabidopsis suspension culture cells to Suc starvation Plant Physiol. 2004, 135 (4) 2330-2347
    • (2004) Plant Physiol. , vol.135 , Issue.4 , pp. 2330-2347
    • Contento, A.L.1    Kim, S.-J.2    Bassham, D.C.3
  • 16
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J.; Mann, M.. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification Nat. Biotechnol. 2008, 26 (12) 1367-1372
    • (2008) Nat. Biotechnol. , vol.26 , Issue.12 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 17
    • 11144320641 scopus 로고    scopus 로고
    • Open source system for analyzing, validating, and storing protein identification data
    • Craig, R.; Cortens, J. P.; Beavis, R. C. Open source system for analyzing, validating, and storing protein identification data J. Proteome Res. 2004, 3 (6) 1234-1242
    • (2004) J. Proteome Res. , vol.3 , Issue.6 , pp. 1234-1242
    • Craig, R.1    Cortens, J.P.2    Beavis, R.C.3
  • 18
    • 84868337141 scopus 로고    scopus 로고
    • Sugars, signalling, and plant development
    • not supplied
    • Eveland, A. L.; Jackson, D. P. Sugars, signalling, and plant development. J. Exp. Bot. 2011, not supplied.
    • (2011) J. Exp. Bot.
    • Eveland, A.L.1    Jackson, D.P.2
  • 20
    • 33745591083 scopus 로고    scopus 로고
    • Status of complete proteome analysis by mass spectrometry: SILAC labeled yeast as a model system
    • de Godoy, L. M. F.; Olsen, J. V.; de Souza, G. A.; Li, G.; Mortensen, P.; Mann, M. Status of complete proteome analysis by mass spectrometry: SILAC labeled yeast as a model system Genome Biol. 2006, 7 (6) R50
    • (2006) Genome Biol. , vol.7 , Issue.6 , pp. 50
    • De Godoy, L.M.F.1    Olsen, J.V.2    De Souza, G.A.3    Li, G.4    Mortensen, P.5    Mann, M.6
  • 21
    • 74049132731 scopus 로고    scopus 로고
    • Label-free, normalized quantification of complex mass spectrometry data for proteomic analysis
    • Griffin, N. M.; Yu, J.; Long, F.; Oh, P.; Shore, S.; Li, Y.; Koziol, J. A.; Schnitzer, J. E. Label-free, normalized quantification of complex mass spectrometry data for proteomic analysis Nat. Biotechnol. 2010, 28 (1) 83-89
    • (2010) Nat. Biotechnol. , vol.28 , Issue.1 , pp. 83-89
    • Griffin, N.M.1    Yu, J.2    Long, F.3    Oh, P.4    Shore, S.5    Li, Y.6    Koziol, J.A.7    Schnitzer, J.E.8
  • 22
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • Ishihama, Y.; Oda, Y.; Tabata, T.; Sato, T.; Nagasu, T.; Rappsilber, J.; Mann, M. Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein Mol. Cell. Proteomics 2005, 4 (9) 1265-1272
    • (2005) Mol. Cell. Proteomics , vol.4 , Issue.9 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3    Sato, T.4    Nagasu, T.5    Rappsilber, J.6    Mann, M.7
  • 23
    • 84980140250 scopus 로고
    • Growth and synthesis of proteins in cell suspensions of a kinetin dependent tobacco
    • Jouanneau, J. P.; Péaud-Lenoël, C. Growth and synthesis of proteins in cell suspensions of a kinetin dependent tobacco Plant Physiol. 1967, 20, 834-850
    • (1967) Plant Physiol. , vol.20 , pp. 834-850
    • Jouanneau, J.P.1    Péaud-Lenoël, C.2
  • 24
    • 0023002623 scopus 로고
    • Biochemical changes during sucrose deprivation in higher plant cells
    • Journet, E. P.; Bligny, R.; Douce, R. Biochemical changes during sucrose deprivation in higher plant cells J. Biol. Chem. 1986, 261 (7) 3193-3199
    • (1986) J. Biol. Chem. , vol.261 , Issue.7 , pp. 3193-3199
    • Journet, E.P.1    Bligny, R.2    Douce, R.3
  • 25
    • 65349168849 scopus 로고    scopus 로고
    • Ratio-dependent significance thresholds in reciprocal 15N-labeling experiments as a robust tool in detection of candidate proteins responding to biological treatment
    • Kierszniowska, S.; Walther, D.; Schulze, W. X. Ratio-dependent significance thresholds in reciprocal 15N-labeling experiments as a robust tool in detection of candidate proteins responding to biological treatment Proteomics 2009, 9 (7) 1916-1924
    • (2009) Proteomics , vol.9 , Issue.7 , pp. 1916-1924
    • Kierszniowska, S.1    Walther, D.2    Schulze, W.X.3
  • 26
    • 71049194213 scopus 로고    scopus 로고
    • Development and evaluation of normalization methods for label-free relative quantification of endogenous peptides
    • Kultima, K.; Nilsson, A.; Scholz, B.; Rossbach, U. L.; Falth, M.; Andren, P. E. Development and evaluation of normalization methods for label-free relative quantification of endogenous peptides Mol. Cell. Proteomics 2009, 8 (10) 2285-2295
    • (2009) Mol. Cell. Proteomics , vol.8 , Issue.10 , pp. 2285-2295
    • Kultima, K.1    Nilsson, A.2    Scholz, B.3    Rossbach, U.L.4    Falth, M.5    Andren, P.E.6
  • 27
    • 34249701830 scopus 로고    scopus 로고
    • Glycosyl hydrolases of cell wall are induced by sugar starvation in Arabidopsis
    • Lee, E.-J.; Matsumura, Y.; Soga, K.; Hoson, T.; Koizumi, N. Glycosyl hydrolases of cell wall are induced by sugar starvation in Arabidopsis Plant Cell Physiol. 2007, 48 (3) 405-413
    • (2007) Plant Cell Physiol. , vol.48 , Issue.3 , pp. 405-413
    • Lee, E.-J.1    Matsumura, Y.2    Soga, K.3    Hoson, T.4    Koizumi, N.5
  • 30
    • 33745663309 scopus 로고    scopus 로고
    • Large-scale analysis of mRNA translation states during sucrose starvation in arabidopsis cells identifies cell proliferation and chromatin structure as targets of translational control
    • Nicola, M.; Roncato, M. A.; Canoy, A. S.; Rouquié, D.; Sarda, X.; Freyssinet, G.; Robaglia, C. Large-scale analysis of mRNA translation states during sucrose starvation in arabidopsis cells identifies cell proliferation and chromatin structure as targets of translational control Plant Physiol. 2006, 141 (2) 663-673
    • (2006) Plant Physiol. , vol.141 , Issue.2 , pp. 663-673
    • Nicola, M.1    Roncato, M.A.2    Canoy, A.S.3    Rouquié, D.4    Sarda, X.5    Freyssinet, G.6    Robaglia, C.7
  • 32
    • 3042815334 scopus 로고    scopus 로고
    • Trypsin cleaves exclusively C-terminal to arginine and lysine residues
    • Olsen, J. V.; Ong, S.-E.; Mann, M. Trypsin cleaves exclusively C-terminal to arginine and lysine residues Mol. Cell. Proteomics 2004, 3 (6) 608-614
    • (2004) Mol. Cell. Proteomics , vol.3 , Issue.6 , pp. 608-614
    • Olsen, J.V.1    Ong, S.-E.2    Mann, M.3
  • 33
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong, S.-E.; Mann, M. Mass spectrometry-based proteomics turns quantitative Nature Chemical Biology 2005, 1 (5) 252-262
    • (2005) Nature Chemical Biology , vol.1 , Issue.5 , pp. 252-262
    • Ong, S.-E.1    Mann, M.2
  • 34
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S.-E.; Blagoev, B.; Kratchmarova, I.; Kristensen, D. B.; Steen, H.; Pandey, A.; Mann, M. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics Mol. Cell. Proteomics 2002, 1 (5) 376-386
    • (2002) Mol. Cell. Proteomics , vol.1 , Issue.5 , pp. 376-386
    • Ong, S.-E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 36
    • 12944269065 scopus 로고
    • Rapid identification of proteins by peptide-mass fingerprinting
    • Pappin, D J; Hojrup, P; Bleasby, A J. Rapid identification of proteins by peptide-mass fingerprinting Curr. Biol. 1993, 3 (6) 327-332
    • (1993) Curr. Biol. , vol.3 , Issue.6 , pp. 327-332
    • Pappin, D.J.1    Hojrup, P.2    Bleasby, A.J.3
  • 37
    • 77449122863 scopus 로고    scopus 로고
    • Trans-proteomic pipeline: A pipeline for proteomic analysis
    • Pedrioli, P. G. A. Trans-proteomic pipeline: a pipeline for proteomic analysis Methods Mol. Biol. (Clifton, NJ) 2010, 604, 213-238
    • (2010) Methods Mol. Biol. (Clifton, NJ) , vol.604 , pp. 213-238
    • Pedrioli, P.G.A.1
  • 38
    • 73149106617 scopus 로고    scopus 로고
    • Ribosome and transcript copy numbers, polysome occupancy and enzyme dynamics in Arabidopsis
    • Piques, M.; Schulze, W. X.; Höhne, M.; Usadel, B.; Gibon, Y.; Rohwer, J.; Stitt, M. Ribosome and transcript copy numbers, polysome occupancy and enzyme dynamics in Arabidopsis Mol. Syst. Biol. 2009, 5 (1) E1-E17
    • (2009) Mol. Syst. Biol. , vol.5 , Issue.1
    • Piques, M.1    Schulze, W.X.2    Höhne, M.3    Usadel, B.4    Gibon, Y.5    Rohwer, J.6    Stitt, M.7
  • 39
    • 0037317228 scopus 로고    scopus 로고
    • Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics
    • Rappsilber, J.; Ishihama, Y.; Mann, M. Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics Anal. Chem. 2003, 75 (3) 663-670
    • (2003) Anal. Chem. , vol.75 , Issue.3 , pp. 663-670
    • Rappsilber, J.1    Ishihama, Y.2    Mann, M.3
  • 40
    • 33745908987 scopus 로고    scopus 로고
    • Sugar Sensing and Signaling in Plants: Conserved and Novel Mechanisms
    • Rolland, F.; Baena-Gonzalez, E.; Sheen, J. Sugar Sensing and Signaling in Plants: Conserved and Novel Mechanisms Annu. Rev. Plant Biol. 2006, 57 (1) 675-709
    • (2006) Annu. Rev. Plant Biol. , vol.57 , Issue.1 , pp. 675-709
    • Rolland, F.1    Baena-Gonzalez, E.2    Sheen, J.3
  • 43
    • 72549094509 scopus 로고    scopus 로고
    • The problem of multiple testing
    • Sainani, K. L. The problem of multiple testing Phys. Med. Rehabil. 2009, 1 (12) 1098-1103
    • (2009) Phys. Med. Rehabil. , vol.1 , Issue.12 , pp. 1098-1103
    • Sainani, K.L.1
  • 44
    • 84857980282 scopus 로고    scopus 로고
    • Analysis of high accuracy, quantitative proteomics data in the MaxQB database
    • Schaab, C.; Geiger, T.; Stoehr, G.; Cox, J.; Mann, M. Analysis of high accuracy, quantitative proteomics data in the MaxQB database Mol. Cell. Proteomics 2012, 11 (3) M111.014068-M111.014068
    • (2012) Mol. Cell. Proteomics , vol.11 , Issue.3
    • Schaab, C.1    Geiger, T.2    Stoehr, G.3    Cox, J.4    Mann, M.5
  • 45
    • 77952538049 scopus 로고    scopus 로고
    • Quantitation in mass-spectrometry-based proteomics
    • Schulze, W. X.; Usadel, B. Quantitation in mass-spectrometry-based proteomics Annu. Rev. Plant Biol. 2010, 61, 491-516
    • (2010) Annu. Rev. Plant Biol. , vol.61 , pp. 491-516
    • Schulze, W.X.1    Usadel, B.2
  • 46
    • 0032535467 scopus 로고    scopus 로고
    • Modification of cysteine residues by alkylation. A tool in peptide mapping and protein identification
    • Sechi, S; Chait, B T. Modification of cysteine residues by alkylation. A tool in peptide mapping and protein identification Anal. Chem. 1998, 70 (24) 5150-5158
    • (1998) Anal. Chem. , vol.70 , Issue.24 , pp. 5150-5158
    • Sechi, S.1    Chait, B.T.2
  • 47
    • 79954562400 scopus 로고    scopus 로고
    • Proteomics to go: Proteomatic enables the user-friendly creation of versatile MS/MS data evaluation workflows
    • Specht, M.; Kuhlgert, S.; Fufezan, C.; Hippler, M. Proteomics to go: Proteomatic enables the user-friendly creation of versatile MS/MS data evaluation workflows Bioinformatics (Oxford, England) 2011, 27 (8) 1183-1184
    • (2011) Bioinformatics (Oxford, England) , vol.27 , Issue.8 , pp. 1183-1184
    • Specht, M.1    Kuhlgert, S.2    Fufezan, C.3    Hippler, M.4
  • 48
    • 4444335470 scopus 로고    scopus 로고
    • The ABC's (and XYZ's) of peptide sequencing
    • Steen, H.; Mann, M. The ABC's (and XYZ's) of peptide sequencing Nat. Rev. Mol. Cell Biol. 2004, 5 (9) 699-711
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , Issue.9 , pp. 699-711
    • Steen, H.1    Mann, M.2
  • 49
    • 36448956829 scopus 로고    scopus 로고
    • Pseudo internal standard approach for label-free quantitative proteomics
    • Tabata, T.; Sato, T.; Kuromitsu, J.; Oda, Y. Pseudo internal standard approach for label-free quantitative proteomics Anal. Chem. 2007, 79 (22) 8440-8445
    • (2007) Anal. Chem. , vol.79 , Issue.22 , pp. 8440-8445
    • Tabata, T.1    Sato, T.2    Kuromitsu, J.3    Oda, Y.4
  • 50
    • 84883359323 scopus 로고    scopus 로고
    • Collaborative software development using R-Forge
    • Theül, S.; Zeileis, A. Collaborative software development using R-Forge R J. 2009, 1, 9-14
    • (2009) R J. , vol.1 , pp. 9-14
    • Theül, S.1    Zeileis, A.2
  • 52
    • 71049189969 scopus 로고    scopus 로고
    • Normalization and statistical analysis of quantitative proteomics data generated by metabolic labeling
    • Ting, L.; Cowley, M. J.; Hoon, S. L.; Guilhaus, M.; Raftery, M. J.; Cavicchioli, R. Normalization and statistical analysis of quantitative proteomics data generated by metabolic labeling Mol. Cell. Proteomics 2009, 8 (10) 2227-2242
    • (2009) Mol. Cell. Proteomics , vol.8 , Issue.10 , pp. 2227-2242
    • Ting, L.1    Cowley, M.J.2    Hoon, S.L.3    Guilhaus, M.4    Raftery, M.J.5    Cavicchioli, R.6
  • 54
    • 77956338820 scopus 로고    scopus 로고
    • Sucrose: Metabolite and signaling molecule
    • Wind, J.; Smeekens, S.; Hanson, J. Sucrose: metabolite and signaling molecule Phytochemistry 2010, 71 (14-15) 1610-1614
    • (2010) Phytochemistry , vol.71 , Issue.14-15 , pp. 1610-1614
    • Wind, J.1    Smeekens, S.2    Hanson, J.3
  • 55
    • 77449148857 scopus 로고    scopus 로고
    • An overview of label-free quantitation methods in proteomics by mass spectrometry
    • Wong, J. W. H.; Cagney, G. An overview of label-free quantitation methods in proteomics by mass spectrometry Methods Mol. Biol. (Clifton, NJ) 2010, 604, 273-283
    • (2010) Methods Mol. Biol. (Clifton, NJ) , vol.604 , pp. 273-283
    • Wong, J.W.H.1    Cagney, G.2
  • 56
    • 42049094894 scopus 로고    scopus 로고
    • Computational methods for the comparative quantification of proteins in label-free LCn-MS experiments
    • Wong, J. W. H.; Sullivan, M. J.; Cagney, G. Computational methods for the comparative quantification of proteins in label-free LCn-MS experiments Brief. Bioinform. 2008, 9 (2) 156-165
    • (2008) Brief. Bioinform. , vol.9 , Issue.2 , pp. 156-165
    • Wong, J.W.H.1    Sullivan, M.J.2    Cagney, G.3
  • 57
    • 77955749536 scopus 로고    scopus 로고
    • Acknowledge and fix the multiple testing problem
    • Young, S S. Acknowledge and fix the multiple testing problem Int. J. Epidemiol. 2010, 39 (3) 934
    • (2010) Int. J. Epidemiol. , vol.39 , Issue.3 , pp. 934
    • Young, S.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.