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Volumn 346, Issue 4, 2005, Pages 1147-1161

Three-dimensional structure of a macromolecular assembly that regulates type III secretion in Yersinia pestis

Author keywords

SycN; Tye A; Type III secretion; YopN; YscB

Indexed keywords

ARGININE; BACTERIAL PROTEIN; CHAPERONE; PROTEIN TYEA; PROTEIN YSCB; SPECIFIC YOP CHAPERONE N PROTEIN; UNCLASSIFIED DRUG; YERSINIA OUTER PROTEIN N;

EID: 13444303937     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.12.036     Document Type: Article
Times cited : (97)

References (55)
  • 1
    • 0036792393 scopus 로고    scopus 로고
    • The Yersinia Ysc-Yop "type III" weaponry
    • G.R. Cornelis The Yersinia Ysc-Yop "type III" weaponry Nature Rev. Mol. Cell. Biol. 3 2002 742 752
    • (2002) Nature Rev. Mol. Cell. Biol. , vol.3 , pp. 742-752
    • Cornelis, G.R.1
  • 2
    • 0035151519 scopus 로고    scopus 로고
    • Yersinia YopE is targeted for type III secretion by N-terminal, not mRNA, signals
    • S.A. Lloyd, M. Norman, R. Rosqvist, and H. Wolf-Watz Yersinia YopE is targeted for type III secretion by N-terminal, not mRNA, signals Mol. Microbiol. 39 2001 520 531
    • (2001) Mol. Microbiol. , vol.39 , pp. 520-531
    • Lloyd, S.A.1    Norman, M.2    Rosqvist, R.3    Wolf-Watz, H.4
  • 3
    • 0344826585 scopus 로고    scopus 로고
    • Yersinia yopQ mRNA encodes a bipartite type III secretion signal in the first 15 codons
    • K.S. Ramamurthi, and O. Schneewind Yersinia yopQ mRNA encodes a bipartite type III secretion signal in the first 15 codons Mol. Microbiol. 50 2003 1189 1198
    • (2003) Mol. Microbiol. , vol.50 , pp. 1189-1198
    • Ramamurthi, K.S.1    Schneewind, O.2
  • 4
    • 0036267324 scopus 로고    scopus 로고
    • Yersinia enterocolitica type III secretion: Mutational analysis of the yopQ secretion signal
    • K.S. Ramamurthi, and O. Schneewind Yersinia enterocolitica type III secretion: mutational analysis of the yopQ secretion signal J. Bacteriol. 184 2002 3321 3328
    • (2002) J. Bacteriol. , vol.184 , pp. 3321-3328
    • Ramamurthi, K.S.1    Schneewind, O.2
  • 5
    • 0033003131 scopus 로고    scopus 로고
    • Yersinia enterocolitica type III secretion: An mRNA signal that couples translation and secretion of YopQ
    • D.M. Anderson, and O. Schneewind Yersinia enterocolitica type III secretion: an mRNA signal that couples translation and secretion of YopQ Mol. Microbiol. 31 1999 1139 1148
    • (1999) Mol. Microbiol. , vol.31 , pp. 1139-1148
    • Anderson, D.M.1    Schneewind, O.2
  • 6
    • 1842413699 scopus 로고    scopus 로고
    • A mRNA signal for the type III secretion of Yop proteins by Yersinia enterocolitica
    • D.M. Anderson, and O. Schneewind A mRNA signal for the type III secretion of Yop proteins by Yersinia enterocolitica Science 278 1997 1140 1143
    • (1997) Science , vol.278 , pp. 1140-1143
    • Anderson, D.M.1    Schneewind, O.2
  • 7
    • 4444313212 scopus 로고    scopus 로고
    • The secretion signal of YopN, a regulatory protein of the Yersinia enterocolitica type III secretion pathway
    • J.W. Goss, J.A. Sorg, K.S. Ramamurthi, H. Ton-That, and O. Schneewind The secretion signal of YopN, a regulatory protein of the Yersinia enterocolitica type III secretion pathway J. Bacteriol. 186 2004 6320 6324
    • (2004) J. Bacteriol. , vol.186 , pp. 6320-6324
    • Goss, J.W.1    Sorg, J.A.2    Ramamurthi, K.S.3    Ton-That, H.4    Schneewind, O.5
  • 8
    • 0033872740 scopus 로고    scopus 로고
    • Competition between the Yops of Yersinia enterocolitica for delivery into eukaryotic cells: Role of the SycE chaperone binding domain of YopE
    • A.P. Boyd, I. Lambermont, and G.R. Cornelis Competition between the Yops of Yersinia enterocolitica for delivery into eukaryotic cells: role of the SycE chaperone binding domain of YopE J. Bacteriol. 182 2000 4811 4821
    • (2000) J. Bacteriol. , vol.182 , pp. 4811-4821
    • Boyd, A.P.1    Lambermont, I.2    Cornelis, G.R.3
  • 9
    • 0036283512 scopus 로고    scopus 로고
    • Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens
    • S.C. Birtalan, R.M. Phillips, and P. Ghosh Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens Mol. Cell 9 2002 971 980
    • (2002) Mol. Cell , vol.9 , pp. 971-980
    • Birtalan, S.C.1    Phillips, R.M.2    Ghosh, P.3
  • 10
    • 0037469577 scopus 로고    scopus 로고
    • The multitalented type III chaperones: All you can do with 15 kDa
    • M.F. Feldman, and G.R. Cornelis The multitalented type III chaperones: all you can do with 15 kDa FEMS Microbiol. Letters 219 2003 151 158
    • (2003) FEMS Microbiol. Letters , vol.219 , pp. 151-158
    • Feldman, M.F.1    Cornelis, G.R.2
  • 11
    • 0028113512 scopus 로고
    • Extracellular association and cytoplasmic partitioning of the IpaB and IpaC invasins of S. flexneri
    • R. Menard, P. Sansonetti, C. Parsot, and T. Vasselon Extracellular association and cytoplasmic partitioning of the IpaB and IpaC invasins of S. flexneri Cell 79 1994 515 525
    • (1994) Cell , vol.79 , pp. 515-525
    • Menard, R.1    Sansonetti, P.2    Parsot, C.3    Vasselon, T.4
  • 12
    • 0032947515 scopus 로고    scopus 로고
    • Role of SycD, the chaperone of the Yersinia Yop translocators YopB and YopD
    • C. Neyt, and G.R. Cornelis Role of SycD, the chaperone of the Yersinia Yop translocators YopB and YopD Mol. Microbiol. 31 1999 143 156
    • (1999) Mol. Microbiol. , vol.31 , pp. 143-156
    • Neyt, C.1    Cornelis, G.R.2
  • 14
    • 0029070827 scopus 로고
    • The chaperone-like protein YerA of Yersinia pseudotuberculosis stabilizes YopE in the cytoplasm but is dispensible for targeting to the secretion loci
    • E. Frithz-Lindsten, R. Rosqvist, L. Johansson, and A. Forsberg The chaperone-like protein YerA of Yersinia pseudotuberculosis stabilizes YopE in the cytoplasm but is dispensible for targeting to the secretion loci Mol. Microbiol. 16 1995 635 647
    • (1995) Mol. Microbiol. , vol.16 , pp. 635-647
    • Frithz-Lindsten, E.1    Rosqvist, R.2    Johansson, L.3    Forsberg, A.4
  • 15
    • 0035499438 scopus 로고    scopus 로고
    • Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion
    • C.E. Stebbins, and J.E. Galan Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion Nature 414 2001 77 81
    • (2001) Nature , vol.414 , pp. 77-81
    • Stebbins, C.E.1    Galan, J.E.2
  • 16
    • 0942279512 scopus 로고    scopus 로고
    • Salmonella type III secretion-associated chaperones confer secretion-pathway specificity
    • S.H. Lee, and J.E. Galan Salmonella type III secretion-associated chaperones confer secretion-pathway specificity Mol. Microbiol. 51 2004 483 495
    • (2004) Mol. Microbiol. , vol.51 , pp. 483-495
    • Lee, S.H.1    Galan, J.E.2
  • 17
    • 0345633461 scopus 로고    scopus 로고
    • The various and varying roles of specific chaperones in type III secretion systems
    • C. Parsot, C. Hamiaux, and A.L. Page The various and varying roles of specific chaperones in type III secretion systems Curr. Opin. Microbiol. 6 2003 7 14
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 7-14
    • Parsot, C.1    Hamiaux, C.2    Page, A.L.3
  • 18
    • 0031766236 scopus 로고    scopus 로고
    • A complex composed of SycN and YscB functions as a specific chaperone for YopN in Yersinia pestis
    • J.B. Day, and G.V. Plano A complex composed of SycN and YscB functions as a specific chaperone for YopN in Yersinia pestis Mol. Microbiol. 30 1998 777 788
    • (1998) Mol. Microbiol. , vol.30 , pp. 777-788
    • Day, J.B.1    Plano, G.V.2
  • 19
    • 0025762461 scopus 로고
    • The surface-located YopN protein is involved in calcium signal transduction in Yersinia pseudotuberculosis
    • A. Forsberg, A.M. Viitanen, M. Skurnik, and H. Wolf-Watz The surface-located YopN protein is involved in calcium signal transduction in Yersinia pseudotuberculosis Mol. Microbiol. 5 1991 977 986
    • (1991) Mol. Microbiol. , vol.5 , pp. 977-986
    • Forsberg, A.1    Viitanen, A.M.2    Skurnik, M.3    Wolf-Watz, H.4
  • 20
    • 0034085052 scopus 로고    scopus 로고
    • Yersinia enterocolitica TyeA, an intracellular regulator of the type III machinery, is required for specific targeting of YopE, YopH, YopM, and YopN into the cytosol of eukaryotic cells
    • L.W. Cheng, and O. Schneewind Yersinia enterocolitica TyeA, an intracellular regulator of the type III machinery, is required for specific targeting of YopE, YopH, YopM, and YopN into the cytosol of eukaryotic cells J. Bacteriol. 182 2000 3183 3190
    • (2000) J. Bacteriol. , vol.182 , pp. 3183-3190
    • Cheng, L.W.1    Schneewind, O.2
  • 21
    • 0032055051 scopus 로고    scopus 로고
    • TyeA, a protein involved in control of Yop release and in translocation of Yersinia Yop effectors
    • M. Iriarte, M.P. Sory, A. Boland, A.P. Boyd, S.D. Mills, I. Lambermont, and G.R. Cornelis TyeA, a protein involved in control of Yop release and in translocation of Yersinia Yop effectors EMBO J. 17 1998 1907 1918
    • (1998) EMBO J. , vol.17 , pp. 1907-1918
    • Iriarte, M.1    Sory, M.P.2    Boland, A.3    Boyd, A.P.4    Mills, S.D.5    Lambermont, I.6    Cornelis, G.R.7
  • 22
    • 0034864508 scopus 로고    scopus 로고
    • Regulated secretion of YopN by the type III machinery of Yersinia enterocolitica
    • L.W. Cheng, O. Kay, and O. Schneewind Regulated secretion of YopN by the type III machinery of Yersinia enterocolitica J. Bacteriol. 183 2001 5293 5301
    • (2001) J. Bacteriol. , vol.183 , pp. 5293-5301
    • Cheng, L.W.1    Kay, O.2    Schneewind, O.3
  • 23
    • 3242750578 scopus 로고    scopus 로고
    • Expression of a functional secreted YopN-TyeA hybrid protein in Yersinia pestis is the result of a +1 translational frameshift event
    • F. Ferracci, J.B. Day, H.J. Ezelle, and G.V. Plano Expression of a functional secreted YopN-TyeA hybrid protein in Yersinia pestis is the result of a +1 translational frameshift event J. Bacteriol. 186 2004 5160 5166
    • (2004) J. Bacteriol. , vol.186 , pp. 5160-5166
    • Ferracci, F.1    Day, J.B.2    Ezelle, H.J.3    Plano, G.V.4
  • 24
    • 0037241866 scopus 로고    scopus 로고
    • Translocation of YopE and YopN into eukaryotic cells by Yersinia pestis yopN, tyeA, sycN, yscB and lcrG deletion mutants measured using a phosphorylatable peptide tag and phosphospecific antibodies
    • J.B. Day, F. Ferracci, and G.V. Plano Translocation of YopE and YopN into eukaryotic cells by Yersinia pestis yopN, tyeA, sycN, yscB and lcrG deletion mutants measured using a phosphorylatable peptide tag and phosphospecific antibodies Mol. Microbiol. 47 2003 807 823
    • (2003) Mol. Microbiol. , vol.47 , pp. 807-823
    • Day, J.B.1    Ferracci, F.2    Plano, G.V.3
  • 25
    • 0036006256 scopus 로고    scopus 로고
    • Three-dimensional structure of the type III secretion chaperone SycE from Yersinia pestis
    • A.G. Evdokimov, J.E. Tropea, K.M. Routzahn, and D.S. Waugh Three-dimensional structure of the type III secretion chaperone SycE from Yersinia pestis Acta Crystallog. sect. D 58 2002 398 406
    • (2002) Acta Crystallog. Sect. D , vol.58 , pp. 398-406
    • Evdokimov, A.G.1    Tropea, J.E.2    Routzahn, K.M.3    Waugh, D.S.4
  • 26
    • 0035180725 scopus 로고    scopus 로고
    • Structural and biochemical characterization of the type III secretion chaperones CesT and SigE
    • Y. Luo, M.G. Bertero, E.A. Frey, R.A. Pfuetzner, M.R. Wenk, and L. Creagh Structural and biochemical characterization of the type III secretion chaperones CesT and SigE Nature Struct. Biol. 8 2001 1031 1036
    • (2001) Nature Struct. Biol. , vol.8 , pp. 1031-1036
    • Luo, Y.1    Bertero, M.G.2    Frey, E.A.3    Pfuetzner, R.A.4    Wenk, M.R.5    Creagh, L.6
  • 27
    • 2942543052 scopus 로고    scopus 로고
    • Structure of Spa15, a type III secretion chaperone from Shigella flexneri with broad specificity
    • A. van Eerde, C. Hamiaux, J. Perez, C. Parsot, and B.W. Dijkstra Structure of Spa15, a type III secretion chaperone from Shigella flexneri with broad specificity EMBO Rep. 5 2004 477 483
    • (2004) EMBO Rep. , vol.5 , pp. 477-483
    • Van Eerde, A.1    Hamiaux, C.2    Perez, J.3    Parsot, C.4    Dijkstra, B.W.5
  • 28
    • 13444295356 scopus 로고    scopus 로고
    • Structure of the Yersinia pestis type III secretion chaperone SycH in complex with a stable fragment of YscM2
    • J. Phan, J.E. Tropea, and D.S. Waugh Structure of the Yersinia pestis type III secretion chaperone SycH in complex with a stable fragment of YscM2 Acta Crystallog. sect. D 60 2004 1591 1599
    • (2004) Acta Crystallog. Sect. D , vol.60 , pp. 1591-1599
    • Phan, J.1    Tropea, J.E.2    Waugh, D.S.3
  • 29
    • 0344825097 scopus 로고    scopus 로고
    • Translocated intimin receptor and its chaperone interact with ATPase of the type III secretion apparatus of enteropathogenic Escherichia coli
    • A. Gauthier, and B.B. Finlay Translocated intimin receptor and its chaperone interact with ATPase of the type III secretion apparatus of enteropathogenic Escherichia coli J. Bacteriol. 185 2003 6747 6755
    • (2003) J. Bacteriol. , vol.185 , pp. 6747-6755
    • Gauthier, A.1    Finlay, B.B.2
  • 30
    • 1642305413 scopus 로고    scopus 로고
    • Docking of cytosolic chaperone-substrate complexes at the membrane ATPase during flagellar type III protein export
    • J. Thomas, G.P. Stafford, and C. Hughes Docking of cytosolic chaperone-substrate complexes at the membrane ATPase during flagellar type III protein export Proc. Natl Acad. Sci. USA 101 2004 3945 3950
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 3945-3950
    • Thomas, J.1    Stafford, G.P.2    Hughes, C.3
  • 32
    • 0028871926 scopus 로고
    • Dali: A network tool for protein structure comparison
    • L. Holm, and C. Sander Dali: a network tool for protein structure comparison Trends Biochem. Sci. 20 1995 478 480
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 33
    • 0030967331 scopus 로고    scopus 로고
    • Two independent type III secretion mechanisms for YopE in Yersinia enterocolitica
    • L.W. Cheng, D.M. Anderson, and O. Schneewind Two independent type III secretion mechanisms for YopE in Yersinia enterocolitica Mol. Microbiol. 24 1997 757 765
    • (1997) Mol. Microbiol. , vol.24 , pp. 757-765
    • Cheng, L.W.1    Anderson, D.M.2    Schneewind, O.3
  • 34
    • 13444294743 scopus 로고    scopus 로고
    • A pivotal role for reductive methylation in the de novo crystallization of a ternarycomplex composed of Yersinia pestis virulence factors YopN, SycN and YscB
    • F.D. Schubot, and D.S. Waugh A pivotal role for reductive methylation in the de novo crystallization of a ternarycomplex composed of Yersinia pestis virulence factors YopN, SycN and YscB Acta Crystallog. sect. D 60 2004 1981 1986
    • (2004) Acta Crystallog. Sect. D , vol.60 , pp. 1981-1986
    • Schubot, F.D.1    Waugh, D.S.2
  • 35
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • S. Doublie Preparation of selenomethionyl proteins for phase determination Methods Enzymol. 276 1997 523 530
    • (1997) Methods Enzymol. , vol.276 , pp. 523-530
    • Doublie, S.1
  • 36
    • 13444308764 scopus 로고    scopus 로고
    • A generic method for the production of recombinant proteins in Escherichia coli using a dual His6-MBP affinity tag
    • In the press.
    • Tropea, J. E., Cherry, S., Nallamsetty, S., Bignon, C. & Waugh, D. S. (2005). A generic method for the production of recombinant proteins in Escherichia coli using a dual His6-MBP affinity tag. Methods Mol. Biol. In the press.
    • (2005) Methods Mol. Biol.
    • Tropea, J.E.1    Cherry, S.2    Nallamsetty, S.3    Bignon, C.4    Waugh, D.S.5
  • 37
    • 0035711194 scopus 로고    scopus 로고
    • Tobacco etch virus protease: Mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency
    • Kapust, R. B., Tozser, J., Fox, J. D., Anderson, D. E., Cherry, S., Copeland, T. D. et al. (2001). Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency. Protein Eng. 14, 993-1000.
    • (2001) Protein Eng. , vol.14 , pp. 993-1000
    • Kapust, R.B.1    Tozser, J.2    Fox, J.D.3    Anderson, D.E.4    Cherry, S.5    Copeland, T.D.6
  • 39
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallog. sect. D 50 1994 760 763
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 41
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • T.C. Terwilliger Maximum-likelihood density modification Acta Crystallog. sect. D 56 2000 965 972
    • (2000) Acta Crystallog. Sect. D , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 42
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.-Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallog. sect. A 47 1991 110 119
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 43
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • G.N. Murshudov, A.A. Vagin, and E.J. Dodson Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallog. sect. D 53 1997 240 255
    • (1997) Acta Crystallog. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 44
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • A. Perrakis, R. Morris, and V.S. Lamzin Automated protein model building combined with iterative structure refinement Nature Struct. Biol. 6 1999 458 463
    • (1999) Nature Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 45
  • 46
    • 0021356554 scopus 로고
    • In vivo comparison of avirulent Vwa- and Pgm- or Pstr phenotypes of yersiniae
    • T. Une, and R.R. Brubaker In vivo comparison of avirulent Vwa- and Pgm- or Pstr phenotypes of yersiniae Infect. Immun. 43 1984 895 900
    • (1984) Infect. Immun. , vol.43 , pp. 895-900
    • Une, T.1    Brubaker, R.R.2
  • 47
    • 0025840282 scopus 로고
    • LcrD, a membrane-bound regulator of the Yersinia pestis low-calcium response
    • G.V. Plano, S.S. Barve, and S.C. Straley LcrD, a membrane-bound regulator of the Yersinia pestis low-calcium response J. Bacteriol. 173 1991 7293 7303
    • (1991) J. Bacteriol. , vol.173 , pp. 7293-7303
    • Plano, G.V.1    Barve, S.S.2    Straley, S.C.3
  • 48
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • L.M. Guzman, D. Belin, M.J. Carson, and J. Beckwith Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter J. Bacteriol. 177 1995 4121 4130
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 49
    • 0029170835 scopus 로고
    • PCR-ligation-PCR mutagenesis: A protocol for creating gene fusions and mutations
    • S.A. Ali, and A. Steinkasserer PCR-ligation-PCR mutagenesis: a protocol for creating gene fusions and mutations Biotechniques 18 1995 746 750
    • (1995) Biotechniques , vol.18 , pp. 746-750
    • Ali, S.A.1    Steinkasserer, A.2
  • 52
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • R.M. Esnouf An extensively modified version of MolScript that includes greatly enhanced coloring capabilities J. Mol. Graph. Model. 15 1997 132 134
    • (1997) J. Mol. Graph. Model. , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 54
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D photorealistic molecular graphics
    • E.A. Merritt, and D.J. Bacon Raster3D photorealistic molecular graphics Methods Enzymol. 277 1997 505 524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 55
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • P. Gouet, E. Courcelle, D.I. Stuart, and F. Metoz ESPript: analysis of multiple sequence alignments in PostScript Bioinformatics 15 1999 305 308
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4


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