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Volumn 279, Issue 6, 2012, Pages 910-918

Alternative folding pathways of the major porin OprF of Pseudomonas aeruginosa

Author keywords

barrel; Acinetobacter spp.; disulfide bonds; outer membrane; periplasmic chaperone; permeability

Indexed keywords

OPRF PROTEIN; OUTER MEMBRANE PROTEIN A; PORIN; S PHASE KINASE ASSOCIATED PROTEIN; UNCLASSIFIED DRUG;

EID: 84858441728     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2012.08481.x     Document Type: Review
Times cited : (36)

References (44)
  • 1
    • 0033985002 scopus 로고    scopus 로고
    • Trends in antimicrobial susceptibility of bacterial pathogens isolated from patients with bloodstream infections in the USA, Canada and Latin America
    • DOI 10.1016/S0924-8579(99)00131-4, PII S0924857999001314
    • Diekema DJ, Pfaller MA, Jones RN, Doern GV, Kugler KC, Beach ML, &, Sader HS, (2000) Trends in antimicrobial susceptibility of bacterial pathogens isolated from patients with bloodstream infections in the USA, Canada and Latin America. SENTRY Participants Group. Int J Antimicrob Agents 13, 257-271. (Pubitemid 30072742)
    • (2000) International Journal of Antimicrobial Agents , vol.13 , Issue.4 , pp. 257-271
    • Diekema, D.J.1    Pfaller, M.A.2    Jones, R.N.3    Doern, G.V.4    Kugler, K.C.5    Beach, M.L.6    Sader, H.S.7
  • 2
    • 0020441981 scopus 로고
    • Permeability of Pseudomonas aeruginosa outer membrane to hydrophilic solutes
    • Yoshimura F, &, Nikaido H, (1982) Permeability of Pseudomonas aeruginosa outer membrane to hydrophilic solutes. J Bacteriol 152, 636-642. (Pubitemid 13210595)
    • (1982) Journal of Bacteriology , vol.152 , Issue.2 , pp. 636-642
    • Yoshimura, F.1    Nikaido, H.2
  • 3
    • 24044514016 scopus 로고    scopus 로고
    • Efflux-mediated antimicrobial resistance
    • DOI 10.1093/jac/dki171
    • Poole K, (2005) Efflux-mediated antimicrobial resistance. J Antimicrob Chemother 56, 20-51. (Pubitemid 41418335)
    • (2005) Journal of Antimicrobial Chemotherapy , vol.56 , Issue.1 , pp. 20-51
    • Poole, K.1
  • 4
    • 0029129966 scopus 로고
    • Role of mexA-mexB-oprM in antibiotic efflux in Pseudomonas aeruginosa
    • Li XZ, Nikaido H, &, Poole K, (1995) Role of mexA-mexB-oprM in antibiotic efflux in Pseudomonas aeruginosa. Antimicrob Agents Chemother 39, 1948-1953.
    • (1995) Antimicrob Agents Chemother , vol.39 , pp. 1948-1953
    • Li, X.Z.1    Nikaido, H.2    Poole, K.3
  • 5
    • 22944473319 scopus 로고    scopus 로고
    • Pan-drug-resistant Pseudomonas aeruginosa causing nosocomial infection at a university hospital in Taiwan
    • DOI 10.1111/j.1469-0691.2005.01196.x
    • Hsueh PR, Tseng SP, Teng LJ, &, Ho SW, (2005) Pan-drug-resistant Pseudomonas aeruginosa causing nosocomial infection at a university hospital in Taiwan. Clin Microbiol Infect 11, 670-673. (Pubitemid 41051385)
    • (2005) Clinical Microbiology and Infection , vol.11 , Issue.8 , pp. 670-673
    • Hsueh, P.R.1    Tseng, S.P.2    Teng, L.J.3    Ho, S.W.4
  • 7
    • 0018357034 scopus 로고
    • Identification of the protein producing transmembrane diffusion pores in the outer membranes of Pseudomonas aeruginosa PA01
    • Hancock RE, Decad GM, &, Nikaido H, (1979) Identification of the protein producing transmembrane diffusion pores in the outer membrane of Pseudomonas aeruginosa PAO1. Biochim Biophys Acta 554, 323-331. (Pubitemid 9234253)
    • (1979) Biochimica et Biophysica Acta , vol.554 , Issue.2 , pp. 323-331
    • Hancock, R.E.W.1    Decad, G.M.2    Nikaido, H.3
  • 8
    • 0017109844 scopus 로고
    • Outer membrane of gram-negative bacteria. XII. Molecular-sieving function of cell wall
    • Decad GM, &, Nikaido H, (1976) Outer membrane of gram-negative bacteria. XII. Molecular-sieving function of cell wall. J Bacteriol 128, 325-336.
    • (1976) J Bacteriol , vol.128 , pp. 325-336
    • Decad, G.M.1    Nikaido, H.2
  • 9
    • 0026672679 scopus 로고
    • Reevaluation, using intact cells, of the exclusion limit and role of porin OprF in Pseudomonas aeruginosa outer membrane permeability
    • Bellido F, Martin NL, Siehnel RJ, &, Hancock RE, (1992) Reevaluation, using intact cells, of the exclusion limit and role of porin OprF in Pseudomonas aeruginosa outer membrane permeability. J Bacteriol 174, 5196-5203.
    • (1992) J Bacteriol , vol.174 , pp. 5196-5203
    • Bellido, F.1    Martin, N.L.2    Siehnel, R.J.3    Hancock, R.E.4
  • 10
    • 0025968741 scopus 로고
    • Identification and characterization of porins in Pseudomonas aeruginosa
    • Nikaido H, Nikaido K, &, Harayama S, (1991) Identification and characterization of porins in Pseudomonas aeruginosa. J Biol Chem 266, 770-779. (Pubitemid 21907182)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.2 , pp. 770-779
    • Nikaido, H.1    Nikaido, K.2    Harayama, S.3
  • 11
    • 0028230055 scopus 로고
    • Membrane topology and assembly of the outer membrane protein OmpA of Escherichia coli K12
    • Ried G, Koebnik R, Hindennach I, Mutschler B, &, Henning U, (1994) Membrane topology and assembly of the outer membrane protein OmpA of Escherichia coli K12. Mol Gen Genet 243, 127-135. (Pubitemid 24146409)
    • (1994) Molecular and General Genetics , vol.243 , Issue.2 , pp. 127-135
    • Ried, G.1    Koebnik, R.2    Hindennach, I.3    Mutschler, B.4    Henning, U.5
  • 12
    • 0031733336 scopus 로고    scopus 로고
    • Structure of the outer membrane protein A transmembrane domain
    • DOI 10.1038/2983
    • Pautsch A, &, Schulz GE, (1998) Structure of the outer membrane protein A transmembrane domain. Nat Struct Biol 5, 1013-1017. (Pubitemid 28506635)
    • (1998) Nature Structural Biology , vol.5 , Issue.11 , pp. 1013-1017
    • Pautsch, A.1    Schulz, G.E.2
  • 13
    • 1442325407 scopus 로고    scopus 로고
    • Structure of the OmpA-like domain of RmpM from Neisseria meningitidis
    • DOI 10.1111/j.1365-2958.2003.03903.x
    • Grizot S, &, Buchanan SK, (2004) Structure of the OmpA-like domain of RmpM from Neisseria meningitidis. Mol Microbiol 51, 1027-1037. (Pubitemid 38270797)
    • (2004) Molecular Microbiology , vol.51 , Issue.4 , pp. 1027-1037
    • Grizot, S.1    Buchanan, S.K.2
  • 14
    • 0029823940 scopus 로고    scopus 로고
    • Secondary structure of the outer membrane proteins OmpA of Escherichia coli and OprF of Pseudomonas aeruginosa
    • Sugawara E, Steiert M, Rouhani S, &, Nikaido H, (1996) Secondary structure of the outer membrane proteins OmpA of Escherichia coli and OprF of Pseudomonas aeruginosa. J Bacteriol 178, 6067-6069. (Pubitemid 26337797)
    • (1996) Journal of Bacteriology , vol.178 , Issue.20 , pp. 6067-6069
    • Sugawara, E.1    Steiert, M.2    Rouhani, S.3    Nikaido, H.4
  • 15
    • 0029053958 scopus 로고
    • Pseudomonas aeruginosa outer membrane protein OprF as an expression vector for foreign epitopes: The effects of positioning and length on the antigenicity of the epitope
    • Wong RS, Wirtz RA, &, Hancock RE, (1995) Pseudomonas aeruginosa outer membrane protein OprF as an expression vector for foreign epitopes: the effects of positioning and length on the antigenicity of the epitope. Gene 158, 55-60.
    • (1995) Gene , vol.158 , pp. 55-60
    • Wong, R.S.1    Wirtz, R.A.2    Hancock, R.E.3
  • 16
    • 0028321391 scopus 로고
    • OmpA protein of Escherichia coli outer membrane occurs in open and closed channel forms
    • Sugawara E, &, Nikaido H, (1994) OmpA protein of Escherichia coli outer membrane occurs in open and closed channel forms. J Biol Chem 269, 17981-17987. (Pubitemid 24206192)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.27 , pp. 17981-17987
    • Sugawara, E.1    Nikaido, H.2
  • 17
    • 33745218065 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa porin OprF exists in two different conformations
    • Sugawara E, Nestorovich EM, Bezrukov SM, &, Nikaido H, (2006) Pseudomonas aeruginosa porin OprF exists in two different conformations. J Biol Chem 281, 16220-16229.
    • (2006) J Biol Chem , vol.281 , pp. 16220-16229
    • Sugawara, E.1    Nestorovich, E.M.2    Bezrukov, S.M.3    Nikaido, H.4
  • 18
    • 33745216927 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa porin OprF: Properties of the channel
    • Nestorovich EM, Sugawara E, Nikaido H, &, Bezrukov SM, (2006) Pseudomonas aeruginosa porin OprF: properties of the channel. J Biol Chem 281, 16230-16237.
    • (2006) J Biol Chem , vol.281 , pp. 16230-16237
    • Nestorovich, E.M.1    Sugawara, E.2    Nikaido, H.3    Bezrukov, S.M.4
  • 19
    • 0028263998 scopus 로고
    • The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both Gram-positive and Gram- negative bacteria, possibly in the interaction of these domains with peptidoglycan
    • DOI 10.1111/j.1365-2958.1994.tb01021.x
    • De Mot R, &, Vanderleyden J, (1994) The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both gram-positive and gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan. Mol Microbiol 12, 333-334. (Pubitemid 24197488)
    • (1994) Molecular Microbiology , vol.12 , Issue.2 , pp. 333-334
    • De Mot, R.1    Vanderleyden, J.2
  • 20
    • 0029092472 scopus 로고
    • Proposal for a peptidoglycan-associating alpha-helical motif in the C-terminal regions of some bacterial cell-surface proteins
    • Koebnik R, (1995) Proposal for a peptidoglycan-associating alpha-helical motif in the C-terminal regions of some bacterial cell-surface proteins. Mol Microbiol 16, 1269-1270.
    • (1995) Mol Microbiol , vol.16 , pp. 1269-1270
    • Koebnik, R.1
  • 21
    • 79955523356 scopus 로고    scopus 로고
    • Characterization of an OmpA-like outer membrane protein of the acidophilic iron-oxidizing bacterium, Acidithiobacillus ferrooxidans
    • Manchur MA, Kikumoto M, Kanao T, Takada J, &, Kamimura K, (2011) Characterization of an OmpA-like outer membrane protein of the acidophilic iron-oxidizing bacterium, Acidithiobacillus ferrooxidans. Extremophiles 15, 403-410.
    • (2011) Extremophiles , vol.15 , pp. 403-410
    • Manchur, M.A.1    Kikumoto, M.2    Kanao, T.3    Takada, J.4    Kamimura, K.5
  • 22
    • 0024401938 scopus 로고
    • Pseudomonas aeruginosa outer membrane protein F: Structural role and relationship to the Escherichia coli omP protein
    • Woodruff WA, &, Hancock RE, (1989) Pseudomonas aeruginosa outer membrane protein F: structural role and relationship to the Escherichia coli OmpA protein. J Bacteriol 171, 3304-3309. (Pubitemid 19145686)
    • (1989) Journal of Bacteriology , vol.171 , Issue.6 , pp. 3304-3309
    • Woodruff, W.A.1    Hancock, R.E.W.2
  • 23
    • 0018150270 scopus 로고
    • Cell envelope and shape of Escherichia coli: Multiple mutants missing the outer membrane lipoprotein and other major outer membrane proteins
    • Sonntag I, Schwarz H, Hirota Y, &, Henning U, (1978) Cell envelope and shape of Escherichia coli: multiple mutants missing the outer membrane lipoprotein and other major outer membrane proteins. J Bacteriol 136, 280-285. (Pubitemid 9037978)
    • (1978) Journal of Bacteriology , vol.136 , Issue.1 , pp. 280-285
    • Sonntag, I.1    Schwarz, H.2    Hirota, Y.3    Henning, U.4
  • 24
    • 0028878069 scopus 로고
    • Epitope mapping of the Pseudomonas aeruginosa major outer membrane porin protein OprF
    • Rawling EG, Martin NL, &, Hancock RE, (1995) Epitope mapping of the Pseudomonas aeruginosa major outer membrane porin protein OprF. Infect Immun 63, 38-42.
    • (1995) Infect Immun , vol.63 , pp. 38-42
    • Rawling, E.G.1    Martin, N.L.2    Hancock, R.E.3
  • 25
    • 0036403720 scopus 로고    scopus 로고
    • Function of Pseudomonas porins in uptake and efflux
    • DOI 10.1146/annurev.micro.56.012302.160310
    • Hancock RE, &, Brinkman FS, (2002) Function of Pseudomonas porins in uptake and efflux. Annu Rev Microbiol 56, 17-38. (Pubitemid 35217446)
    • (2002) Annual Review of Microbiology , vol.56 , pp. 17-38
    • Hancock, R.E.W.1    Brinkman, F.S.L.2
  • 26
    • 33751579323 scopus 로고    scopus 로고
    • Analysis of Pseudomonas aeruginosa conditional psl variants reveals roles for the psl polysaccharide in adhesion and maintaining biofilm structure postattachment
    • DOI 10.1128/JB.01202-06
    • Ma L, Jackson KD, Landry RM, Parsek MR, &, Wozniak DJ, (2006) Analysis of Pseudomonas aeruginosa conditional psl variants reveals roles for the Psl polysaccharide in adhesion and maintaining biofilm structure postattachment. J Bacteriol 188, 8213-8221. (Pubitemid 44845693)
    • (2006) Journal of Bacteriology , vol.188 , Issue.23 , pp. 8213-8221
    • Ma, L.1    Jackson, K.D.2    Landry, R.M.3    Parsek, M.R.4    Wozniak, D.J.5
  • 27
    • 0033733267 scopus 로고    scopus 로고
    • Selecting and evolving functional proteins in vitro by ribosome display
    • Hanes J, Jermutus L, &, Pluckthun A, (2000) Selecting and evolving functional proteins in vitro by ribosome display. Methods Enzymol 328, 404-430.
    • (2000) Methods Enzymol , vol.328 , pp. 404-430
    • Hanes, J.1    Jermutus, L.2    Pluckthun, A.3
  • 28
    • 31344479308 scopus 로고    scopus 로고
    • Advances in understanding bacterial outer-membrane biogenesis
    • DOI 10.1038/nrmicro1322, PII N1322
    • Ruiz N, Kahne D, &, Silhavy TJ, (2006) Advances in understanding bacterial outer-membrane biogenesis. Nat Rev Microbiol 4, 57-66. (Pubitemid 43135287)
    • (2006) Nature Reviews Microbiology , vol.4 , Issue.1 , pp. 57-66
    • Silhavy, T.J.1    Ruiz, N.2    Kahne, D.3
  • 29
    • 79952129895 scopus 로고    scopus 로고
    • Factors affecting the folding of Pseudomonas aeruginosa OprF porin into the one-domain open conformer
    • Sugawara E, Nagano K, &, Nikaido H, (2010) Factors affecting the folding of Pseudomonas aeruginosa OprF porin into the one-domain open conformer. mBio 1, e00228-10.
    • (2010) MBio , vol.1
    • Sugawara, E.1    Nagano, K.2    Nikaido, H.3
  • 30
    • 0030797806 scopus 로고    scopus 로고
    • Protein folding coupled to disulphide bond formation
    • Creighton TE, (1997) Protein folding coupled to disulphide bond formation. Biol Chem 378, 731-744. (Pubitemid 27388932)
    • (1997) Biological Chemistry , vol.378 , Issue.8 , pp. 731-744
    • Creighton, T.E.1
  • 31
    • 0042768090 scopus 로고    scopus 로고
    • Protein disulfide bond formation in prokaryotes
    • DOI 10.1146/annurev.biochem.72.121801.161459
    • Kadokura H, Katzen F, &, Beckwith J, (2003) Protein disulfide bond formation in prokaryotes. Annu Rev Biochem 72, 111-135. (Pubitemid 36930443)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 111-135
    • Kadokura, H.1    Katzen, F.2    Beckwith, J.3
  • 32
    • 33751056360 scopus 로고    scopus 로고
    • Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif
    • Robert V, Volokhina EB, Senf F, Bos MP, Van Gelder P, &, Tommassen J, (2006) Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif. PLoS Biol 4, e377.
    • (2006) PLoS Biol , vol.4
    • Robert, V.1    Volokhina, E.B.2    Senf, F.3    Bos, M.P.4    Van Gelder, P.5    Tommassen, J.6
  • 33
    • 0025976068 scopus 로고
    • Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein
    • Struyve M, Moons M, &, Tommassen J, (1991) Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein. J Mol Biol 218, 141-148. (Pubitemid 121003335)
    • (1991) Journal of Molecular Biology , vol.218 , Issue.1 , pp. 141-148
    • Struyve, M.1    Moons, M.2    Tommassen, J.3
  • 34
    • 4744373535 scopus 로고    scopus 로고
    • Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture
    • DOI 10.1038/nsmb828
    • Korndorfer IP, Dommel MK, &, Skerra A, (2004) Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture. Nat Struct Mol Biol 11, 1015-1020. (Pubitemid 39315307)
    • (2004) Nature Structural and Molecular Biology , vol.11 , Issue.10 , pp. 1015-1020
    • Korndorfer, I.P.1    Dommel, M.K.2    Skerra, A.3
  • 35
    • 66649116274 scopus 로고    scopus 로고
    • Binding regions of outer membrane protein A in complexes with the periplasmic chaperone Skp. A site-directed fluorescence study
    • Qu J, Behrens-Kneip S, Holst O, &, Kleinschmidt JH, (2009) Binding regions of outer membrane protein A in complexes with the periplasmic chaperone Skp. A site-directed fluorescence study. Biochemistry (Mosc) 48, 4926-4936.
    • (2009) Biochemistry (Mosc) , vol.48 , pp. 4926-4936
    • Qu, J.1    Behrens-Kneip, S.2    Holst, O.3    Kleinschmidt, J.H.4
  • 36
    • 60549101514 scopus 로고    scopus 로고
    • The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains
    • Walton TA, Sandoval CM, Fowler CA, Pardi A, &, Sousa MC, (2009) The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains. Proc Natl Acad Sci USA 106, 1772-1777.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 1772-1777
    • Walton, T.A.1    Sandoval, C.M.2    Fowler, C.A.3    Pardi, A.4    Sousa, M.C.5
  • 37
    • 4143114616 scopus 로고    scopus 로고
    • Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation
    • DOI 10.1016/j.molcel.2004.07.023, PII S1097276504004435
    • Walton TA, &, Sousa MC, (2004) Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation. Mol Cell 15, 367-374. (Pubitemid 39092753)
    • (2004) Molecular Cell , vol.15 , Issue.3 , pp. 367-374
    • Walton, T.A.1    Sousa, M.C.2
  • 38
    • 17844405030 scopus 로고    scopus 로고
    • Kinetics of folding of Escherichia coli OmpA from narrow to large pore conformation in a planar bilayer
    • DOI 10.1021/bi047278e
    • Zakharian E, &, Reusch RN, (2005) Kinetics of folding of Escherichia coli OmpA from narrow to large pore conformation in a planar bilayer. Biochemistry (Mosc) 44, 6701-6707. (Pubitemid 40593821)
    • (2005) Biochemistry , vol.44 , Issue.17 , pp. 6701-6707
    • Zakharian, E.1    Reusch, R.N.2
  • 39
    • 0040606207 scopus 로고    scopus 로고
    • Growth temperature dependence of channel size of the major outer-membrane protein (OprF) in psychrotrophic Pseudomonas fluorescens strains
    • De E, Orange N, Saint N, Guerillon J, De Mot R, &, Molle G, (1997) Growth temperature dependence of channel size of the major outer-membrane protein (OprF) in psychrotrophic Pseudomonas fluorescens strains. Microbiology, 143 (Pt 3), 9-35.
    • (1997) Microbiology , vol.143 , Issue.PART 3 , pp. 9-35
    • De, E.1    Orange, N.2    Saint, N.3    Guerillon, J.4    De Mot, R.5    Molle, G.6
  • 41
    • 34447556772 scopus 로고    scopus 로고
    • Porins, efflux pumps and multidrug resistance in Acinetobacter baumannii
    • DOI 10.1093/jac/dkl509
    • Vila J, Marti S, &, Sanchez-Cespedes J, (2007) Porins, efflux pumps and multidrug resistance in Acinetobacter baumannii. J Antimicrob Chemother 59, 1210-1215. (Pubitemid 47073338)
    • (2007) Journal of Antimicrobial Chemotherapy , vol.59 , Issue.6 , pp. 1210-1215
    • Vila, J.1    Marti, S.2    Sanchez-Cespedes, J.3
  • 42
    • 0025856911 scopus 로고
    • Outer membrane permeability of Acinetobacter calcoaceticus and its implication in antibiotic resistance
    • Sato K, &, Nakae T, (1991) Outer membrane permeability of Acinetobacter calcoaceticus and its implication in antibiotic resistance. J Antimicrob Chemother 28, 35-45.
    • (1991) J Antimicrob Chemother , vol.28 , pp. 35-45
    • Sato, K.1    Nakae, T.2
  • 43
    • 79952329632 scopus 로고    scopus 로고
    • Efflux-mediated antibiotic resistance in Acinetobacter spp
    • Coyne S, Courvalin P, &, Perichon B, (2011) Efflux-mediated antibiotic resistance in Acinetobacter spp. Antimicrob Agents Chemother 55, 947-953.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 947-953
    • Coyne, S.1    Courvalin, P.2    Perichon, B.3
  • 44
    • 84956722160 scopus 로고    scopus 로고
    • OmpA/OprF: Slow porins or channels produced by alternative folding of outer membrane proteins
    • In (Benz R. ed.), Wiley-VCH, Weinheim
    • Sugawara E, &, Nikaido H, (2004) OmpA/OprF: slow porins or channels produced by alternative folding of outer membrane proteins. In Bacterial and Eukaryotic Porins (, Benz R, ed.), pp. 119-138. Wiley-VCH, Weinheim.
    • (2004) Bacterial and Eukaryotic Porins , pp. 119-138
    • Sugawara, E.1    Nikaido, H.2


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