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Volumn 118, Issue 3, 2015, Pages 119-129

Cytoplasmic sensing by the inner membrane histidine kinase EnvZ

Author keywords

Histidine kinase; Hydrogen:deuterium exchange mass spectrometry; Osmoregulation; Robustness; Super resolution microscopy; Two component regulatory system EnvZ OmpR

Indexed keywords

BACTERIAL PROTEIN; ENVZ PROTEIN, E COLI; ESCHERICHIA COLI PROTEIN; MULTIENZYME COMPLEX; OSMOLARITY RESPONSE REGULATOR PROTEINS; OUTER MEMBRANE PROTEIN; TRANSACTIVATOR PROTEIN;

EID: 84952630665     PISSN: 00796107     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pbiomolbio.2015.04.005     Document Type: Review
Times cited : (38)

References (58)
  • 3
    • 0037457896 scopus 로고    scopus 로고
    • Robustness and the cycle of phosphorylation and dephosphorylation in a two-component regulatory system
    • Batchelor E., Goulian M. Robustness and the cycle of phosphorylation and dephosphorylation in a two-component regulatory system. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:691-696.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 691-696
    • Batchelor, E.1    Goulian, M.2
  • 4
    • 0037025378 scopus 로고    scopus 로고
    • EnvZ-OmpR interaction and osmoregulation in E coli
    • Cai S.J., Inouye M. EnvZ-OmpR interaction and osmoregulation in E coli. J. Biol. Chem. 2002, 277:24155-24161.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24155-24161
    • Cai, S.J.1    Inouye, M.2
  • 5
    • 0034028431 scopus 로고    scopus 로고
    • Biophysical characterization of changes in amounts and activity of Escherichia coli cell and compartment water and turgor pressure in response to osmotic stress
    • Cayley D.S., Guttman H.J., Record M.T. Biophysical characterization of changes in amounts and activity of Escherichia coli cell and compartment water and turgor pressure in response to osmotic stress. Biophys. J. 2000, 78:1748-1764.
    • (2000) Biophys. J. , vol.78 , pp. 1748-1764
    • Cayley, D.S.1    Guttman, H.J.2    Record, M.T.3
  • 7
    • 84929500870 scopus 로고    scopus 로고
    • A FRET-based biosensor tracks OmpR acidification of Salmonella in the macrophage vacuole
    • Chakraborty S., Mizusaki H., Kenney L.J. A FRET-based biosensor tracks OmpR acidification of Salmonella in the macrophage vacuole. PLOS Biol. 2015, 10.1371/journal.pbio.1002116.
    • (2015) PLOS Biol.
    • Chakraborty, S.1    Mizusaki, H.2    Kenney, L.J.3
  • 8
    • 0026698151 scopus 로고
    • Functional roles assigned to the periplasmic, linker, and receiver domains of the Agrobacterium tumefaciens VirA protein
    • Chang C.H., Winans S.C. Functional roles assigned to the periplasmic, linker, and receiver domains of the Agrobacterium tumefaciens VirA protein. J. Bacteriol. 1992, 174:7033-7039.
    • (1992) J. Bacteriol. , vol.174 , pp. 7033-7039
    • Chang, C.H.1    Winans, S.C.2
  • 9
    • 0026006215 scopus 로고
    • Prokaryotic osmoregulation: genetics and physiology
    • Csonka L.N., Hanson A.D. Prokaryotic osmoregulation: genetics and physiology. Ann. Rev. Microbiol. 1991, 45:569-606.
    • (1991) Ann. Rev. Microbiol. , vol.45 , pp. 569-606
    • Csonka, L.N.1    Hanson, A.D.2
  • 10
    • 0031905590 scopus 로고    scopus 로고
    • CpxP, a stress-combative member of the Cpx regulon
    • Danese P.N., Silhavy T.J. CpxP, a stress-combative member of the Cpx regulon. J. Bacteriol. 1998, 180:831-839.
    • (1998) J. Bacteriol. , vol.180 , pp. 831-839
    • Danese, P.N.1    Silhavy, T.J.2
  • 11
    • 0033962665 scopus 로고    scopus 로고
    • Cpx two-component signal transduction in Escherichia coli: excessive CpxR-P levels underlie CpxA* phenotypes
    • De Wulf P., Lin E.C. Cpx two-component signal transduction in Escherichia coli: excessive CpxR-P levels underlie CpxA* phenotypes. J. Bacteriol. 2000, 182:1423-1426.
    • (2000) J. Bacteriol. , vol.182 , pp. 1423-1426
    • De Wulf, P.1    Lin, E.C.2
  • 12
    • 84899797358 scopus 로고    scopus 로고
    • Quantitative super-resolution microscopy: pitfalls and strategies for image analysis
    • Durisic N., Cuervo L.L., Lakadamyali M. Quantitative super-resolution microscopy: pitfalls and strategies for image analysis. Curr. Opin. Chem. Biol. 2014, 20:22-28.
    • (2014) Curr. Opin. Chem. Biol. , vol.20 , pp. 22-28
    • Durisic, N.1    Cuervo, L.L.2    Lakadamyali, M.3
  • 13
    • 84895068066 scopus 로고    scopus 로고
    • Single-molecule evaluation of fluorescent protein photoactivation efficiency using an in vivo nanotemplate
    • Durisic N., Laparra-Cuervo L., Sandoval-Alvarez A., Borbely J.S., Lakadamyali M. Single-molecule evaluation of fluorescent protein photoactivation efficiency using an in vivo nanotemplate. Nat. Methods 2014, 11:156-162.
    • (2014) Nat. Methods , vol.11 , pp. 156-162
    • Durisic, N.1    Laparra-Cuervo, L.2    Sandoval-Alvarez, A.3    Borbely, J.S.4    Lakadamyali, M.5
  • 16
    • 0038354822 scopus 로고    scopus 로고
    • Dual regulation by phospho-OmpR of ssrA/B gene expression in Salmonella pathogenicity island 2
    • Feng X., Oropeza R., Kenney L.J. Dual regulation by phospho-OmpR of ssrA/B gene expression in Salmonella pathogenicity island 2. Mol. Microbiol. 2003, 48:1131-1143.
    • (2003) Mol. Microbiol. , vol.48 , pp. 1131-1143
    • Feng, X.1    Oropeza, R.2    Kenney, L.J.3
  • 17
    • 84901612806 scopus 로고    scopus 로고
    • Crystallographic snapshot of the Escherichia coli EnvZ histidine kinase in an active conformation
    • Ferris H.U., Coles M., Lupas A.N., Hartmann M.D. Crystallographic snapshot of the Escherichia coli EnvZ histidine kinase in an active conformation. J. Struct. Biol. 2014, 186:376-379.
    • (2014) J. Struct. Biol. , vol.186 , pp. 376-379
    • Ferris, H.U.1    Coles, M.2    Lupas, A.N.3    Hartmann, M.D.4
  • 18
    • 84943393630 scopus 로고    scopus 로고
    • Single cell super-resolution imaging of E. coli OmpR during environmental stress
    • (In press)
    • Foo Y.H., Spahn C., Heilemann M., Kenney L.J. Single cell super-resolution imaging of E. coli OmpR during environmental stress. Integr. Biol. 2015, (In press).
    • (2015) Integr. Biol.
    • Foo, Y.H.1    Spahn, C.2    Heilemann, M.3    Kenney, L.J.4
  • 19
    • 0038290306 scopus 로고    scopus 로고
    • Identification of basic amino acid residues important for citrate binding by the periplasmic receptor domain of the sensor kinase CitA
    • Gerharz T., Reinelt S., Kaspar S., Scapozza L., Bott M. Identification of basic amino acid residues important for citrate binding by the periplasmic receptor domain of the sensor kinase CitA. Biochemistry 2003, 42:5917-5924.
    • (2003) Biochemistry , vol.42 , pp. 5917-5924
    • Gerharz, T.1    Reinelt, S.2    Kaspar, S.3    Scapozza, L.4    Bott, M.5
  • 20
    • 0037238108 scopus 로고    scopus 로고
    • The transmembrane domains of the sensor kinase KdpD of Escherichia coli are not essential for sensing K+ limitation
    • Heermann R., Fohrmann A., Altendorf K., Jung K. The transmembrane domains of the sensor kinase KdpD of Escherichia coli are not essential for sensing K+ limitation. Mol. Microbiol. 2003, 47:839-848.
    • (2003) Mol. Microbiol. , vol.47 , pp. 839-848
    • Heermann, R.1    Fohrmann, A.2    Altendorf, K.3    Jung, K.4
  • 21
    • 0031782823 scopus 로고    scopus 로고
    • Mutations that alter the kinase and phosphatase activities of the two-component sensor EnvZ
    • Hsing W., Russo F.D., Bernd K.K., Silhavy T.J. Mutations that alter the kinase and phosphatase activities of the two-component sensor EnvZ. J. Bacteriol. 1998, 180:4538-4546.
    • (1998) J. Bacteriol. , vol.180 , pp. 4538-4546
    • Hsing, W.1    Russo, F.D.2    Bernd, K.K.3    Silhavy, T.J.4
  • 22
    • 0027202361 scopus 로고
    • Ligand binding to the receptor domain regulates the ratio of kinase to phosphatase activities of the signaling domain of the hybrid Escherichia coli transmembrane receptor, Taz1
    • Jin T., Inouye M. Ligand binding to the receptor domain regulates the ratio of kinase to phosphatase activities of the signaling domain of the hybrid Escherichia coli transmembrane receptor, Taz1. J. Mol. Biol. 1993, 232:484-492.
    • (1993) J. Mol. Biol. , vol.232 , pp. 484-492
    • Jin, T.1    Inouye, M.2
  • 23
    • 0031572866 scopus 로고    scopus 로고
    • Kinase activity of EnvZ, an osmoregulatory signal transducing protein of Escherichia coli
    • Kenney L.J. Kinase activity of EnvZ, an osmoregulatory signal transducing protein of Escherichia coli. Arch. Biochem. Biophys. 1997, 346:303-311.
    • (1997) Arch. Biochem. Biophys. , vol.346 , pp. 303-311
    • Kenney, L.J.1
  • 24
    • 77949916191 scopus 로고    scopus 로고
    • How important is the phosphatase activity of sensor kinases?
    • Kenney L.J. How important is the phosphatase activity of sensor kinases?. Curr. Opin. Microbiol. 2010, 13:168-176.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 168-176
    • Kenney, L.J.1
  • 25
    • 34447102706 scopus 로고    scopus 로고
    • Application of fluorescence resonance energy transfer to examine EnvZ/OmpR interactions
    • King S.T., Kenney L.J. Application of fluorescence resonance energy transfer to examine EnvZ/OmpR interactions. Methods Enzymol. 2007, 422:352-360.
    • (2007) Methods Enzymol. , vol.422 , pp. 352-360
    • King, S.T.1    Kenney, L.J.2
  • 27
    • 0033954447 scopus 로고    scopus 로고
    • OmpR regulates the two-component system SsrA-SsrB in Salmonella pathogenicity island 2
    • Lee A.K., Detweiler C.S., Falkow S. OmpR regulates the two-component system SsrA-SsrB in Salmonella pathogenicity island 2. J. Bacteriol. 2000, 182:771-781.
    • (2000) J. Bacteriol. , vol.182 , pp. 771-781
    • Lee, A.K.1    Detweiler, C.S.2    Falkow, S.3
  • 28
    • 0024811077 scopus 로고
    • Signal transduction in the phosphate regulon of Escherichia coli involves phosphotransfer between PhoR and PhoB proteins
    • Makino K., Shinagawa H., Amemura M., Kawamoto T., Yamada M., Nakata A. Signal transduction in the phosphate regulon of Escherichia coli involves phosphotransfer between PhoR and PhoB proteins. J. Mol. Biol. 1989, 210:551-559.
    • (1989) J. Mol. Biol. , vol.210 , pp. 551-559
    • Makino, K.1    Shinagawa, H.2    Amemura, M.3    Kawamoto, T.4    Yamada, M.5    Nakata, A.6
  • 30
    • 0022896755 scopus 로고
    • Interaction between two regulatory proteins in osmoregulatory expression of ompF and ompC genes in Escherichia coli: a novel ompR mutation suppresses pleiotropic defects caused by an envZ mutation
    • Matsuyama S., Mizuno T., Mizushima S. Interaction between two regulatory proteins in osmoregulatory expression of ompF and ompC genes in Escherichia coli: a novel ompR mutation suppresses pleiotropic defects caused by an envZ mutation. J. Bacteriol. 1986, 168:1309-1314.
    • (1986) J. Bacteriol. , vol.168 , pp. 1309-1314
    • Matsuyama, S.1    Mizuno, T.2    Mizushima, S.3
  • 31
    • 0037192777 scopus 로고    scopus 로고
    • Phosphorylation alters the interaction of the response regulator OmpR with its sensor kinase EnvZ
    • Mattison K., Kenney L.J. Phosphorylation alters the interaction of the response regulator OmpR with its sensor kinase EnvZ. J. Biol. Chem. 2002, 277:11143-11148.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11143-11148
    • Mattison, K.1    Kenney, L.J.2
  • 32
    • 0036303447 scopus 로고    scopus 로고
    • A phosphorylation site mutant of OmpR reveals different binding conformations at ompF and ompC
    • Mattison K., Oropeza R., Byers N., Kenney L.J. A phosphorylation site mutant of OmpR reveals different binding conformations at ompF and ompC. J. Mol. Biol. 2002, 315:497-511.
    • (2002) J. Mol. Biol. , vol.315 , pp. 497-511
    • Mattison, K.1    Oropeza, R.2    Byers, N.3    Kenney, L.J.4
  • 33
    • 34948866886 scopus 로고    scopus 로고
    • Osmosensing properties of the histidine protein kinase MtrB from corynebacterium glutamicum
    • Moker N., Reihlen P., Kramer R., Morbach S. Osmosensing properties of the histidine protein kinase MtrB from corynebacterium glutamicum. J. Biol. Chem. 2007, 282:27666-27677.
    • (2007) J. Biol. Chem. , vol.282 , pp. 27666-27677
    • Moker, N.1    Reihlen, P.2    Kramer, R.3    Morbach, S.4
  • 34
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido H., Vaara M. Molecular basis of bacterial outer membrane permeability. Microbiol. Rev. 1985, 49:1-32.
    • (1985) Microbiol. Rev. , vol.49 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 35
    • 0032499693 scopus 로고    scopus 로고
    • Two-domain reconstitution of a functional protein histidine kinase
    • Park H., Saha S.K., Inouye M. Two-domain reconstitution of a functional protein histidine kinase. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:6728-6732.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 6728-6732
    • Park, H.1    Saha, S.K.2    Inouye, M.3
  • 36
    • 0041929590 scopus 로고    scopus 로고
    • Structure and mechanism in prokaryotic mechanosensitive channels
    • Perozo E., Rees D.C. Structure and mechanism in prokaryotic mechanosensitive channels. Curr. Opin. Struct. Biol. 2003, 13:432-442.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 432-442
    • Perozo, E.1    Rees, D.C.2
  • 38
    • 0141643091 scopus 로고    scopus 로고
    • The structure of the periplasmic ligand-binding domain of the sensor kinase CitA reveals the first extracellular PAS domain
    • Reinelt S., Hofmann E., Gerharz T., Bott M., Madden D.R. The structure of the periplasmic ligand-binding domain of the sensor kinase CitA reveals the first extracellular PAS domain. J. Biol. Chem. 2003, 278:39189-39196.
    • (2003) J. Biol. Chem. , vol.278 , pp. 39189-39196
    • Reinelt, S.1    Hofmann, E.2    Gerharz, T.3    Bott, M.4    Madden, D.R.5
  • 40
    • 0023644949 scopus 로고
    • Conserved domains in bacterial regulatory proteins that respond to environmental stimuli
    • Ronson C.W., Nixon B.T., Ausubel F.M. Conserved domains in bacterial regulatory proteins that respond to environmental stimuli. Cell 1987, 49:579-581.
    • (1987) Cell , vol.49 , pp. 579-581
    • Ronson, C.W.1    Nixon, B.T.2    Ausubel, F.M.3
  • 41
    • 33644755943 scopus 로고    scopus 로고
    • The cytoplasmic C-terminal domain of the Escherichia coli KdpD protein functions as a K+ sensor
    • Rothenbucher M.C., Facey S.J., Kiefer D., Kossmann M., Kuhn A. The cytoplasmic C-terminal domain of the Escherichia coli KdpD protein functions as a K+ sensor. J. Bacteriol. 2006, 188:1950-1958.
    • (2006) J. Bacteriol. , vol.188 , pp. 1950-1958
    • Rothenbucher, M.C.1    Facey, S.J.2    Kiefer, D.3    Kossmann, M.4    Kuhn, A.5
  • 42
    • 0026333013 scopus 로고
    • EnvZ controls the concentration of phosphorylated OmpR to mediate osmoregulation of the porin genes
    • Russo F.D., Silhavy T.J. EnvZ controls the concentration of phosphorylated OmpR to mediate osmoregulation of the porin genes. J. Mol. Biol. 1991, 222:567-580.
    • (1991) J. Mol. Biol. , vol.222 , pp. 567-580
    • Russo, F.D.1    Silhavy, T.J.2
  • 43
    • 0027276137 scopus 로고
    • Mutations that affect separate functions of OmpR the phosphorylated regulator of porin transcription in Escherichia coli
    • Russo F.D., Slauch J.M., Silhavy T.J. Mutations that affect separate functions of OmpR the phosphorylated regulator of porin transcription in Escherichia coli. J. Mol. Biol. 1993, 231:261-273.
    • (1993) J. Mol. Biol. , vol.231 , pp. 261-273
    • Russo, F.D.1    Slauch, J.M.2    Silhavy, T.J.3
  • 44
    • 0027193061 scopus 로고
    • Topology of the PhoR protein of Escherichia coli and functional analysis of internal deletion mutants
    • Scholten M., Tommassen J. Topology of the PhoR protein of Escherichia coli and functional analysis of internal deletion mutants. Mol. Microbiol. 1993, 8:269-275.
    • (1993) Mol. Microbiol. , vol.8 , pp. 269-275
    • Scholten, M.1    Tommassen, J.2
  • 45
    • 0032920056 scopus 로고    scopus 로고
    • The cytoplasmic kinase domain of PhoR is sufficient for the low phosphate-inducible expression of pho regulon genes in Bacillus subtilis
    • Shi L., Hulett F.M. The cytoplasmic kinase domain of PhoR is sufficient for the low phosphate-inducible expression of pho regulon genes in Bacillus subtilis. Mol. Microbiol. 1999, 31:211-222.
    • (1999) Mol. Microbiol. , vol.31 , pp. 211-222
    • Shi, L.1    Hulett, F.M.2
  • 48
    • 0023864296 scopus 로고
    • EnvZ functions through OmpR to control porin gene expression in Escherichia coli K-12
    • Slauch J.M., Garrett S., Jackson D.E., Silhavy T.J. EnvZ functions through OmpR to control porin gene expression in Escherichia coli K-12. J. Bacteriol. 1988, 170:439-441.
    • (1988) J. Bacteriol. , vol.170 , pp. 439-441
    • Slauch, J.M.1    Garrett, S.2    Jackson, D.E.3    Silhavy, T.J.4
  • 49
    • 84908584261 scopus 로고    scopus 로고
    • Physical properties of Escherichia coli spheroplast membranes
    • Sun Y., Sun T.L., Huang H.W. Physical properties of Escherichia coli spheroplast membranes. Biophys. J. 2014, 107:2082-2090.
    • (2014) Biophys. J. , vol.107 , pp. 2082-2090
    • Sun, Y.1    Sun, T.L.2    Huang, H.W.3
  • 50
    • 77949915674 scopus 로고    scopus 로고
    • Interaction fidelity in two-component signaling
    • Szurmant H., Hoch J.A. Interaction fidelity in two-component signaling. Curr. Opin. Microbiol. 2010, 13:190-197.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 190-197
    • Szurmant, H.1    Hoch, J.A.2
  • 51
    • 0028170316 scopus 로고
    • Transmembrane signal transduction by the Escherichia coli osmotic sensor, EnvZ: intermolecular complementation of transmembrane signalling
    • Tokishita S., Mizuno T. Transmembrane signal transduction by the Escherichia coli osmotic sensor, EnvZ: intermolecular complementation of transmembrane signalling. Mol. Microbiol. 1994, 13:435-444.
    • (1994) Mol. Microbiol. , vol.13 , pp. 435-444
    • Tokishita, S.1    Mizuno, T.2
  • 53
    • 0018650121 scopus 로고
    • Genetics and biochemistry of the peptidoglycan-associated proteins b and c of Escherichia coli K12
    • Verhoef C., Lugtenberg B., van Boxtel R., de Graaff P., Verheij H. Genetics and biochemistry of the peptidoglycan-associated proteins b and c of Escherichia coli K12. Mol. Gen. Genet. 1979, 169:137-146.
    • (1979) Mol. Gen. Genet. , vol.169 , pp. 137-146
    • Verhoef, C.1    Lugtenberg, B.2    van Boxtel, R.3    de Graaff, P.4    Verheij, H.5
  • 54
    • 0019220506 scopus 로고
    • Pleiotropic mutations rendering Escherichia coli K-12 resistant to bacteriophage TP1
    • Wandersman C., Moreno F., Schwartz M. Pleiotropic mutations rendering Escherichia coli K-12 resistant to bacteriophage TP1. J. Bacteriol. 1980, 143:1374-1383.
    • (1980) J. Bacteriol. , vol.143 , pp. 1374-1383
    • Wandersman, C.1    Moreno, F.2    Schwartz, M.3
  • 55
    • 84861849986 scopus 로고    scopus 로고
    • The inner membrane histidine kinase EnvZ senses osmolality via helix-coil transitions in the cytoplasm
    • Wang L.C., Morgan L.K., Godakumbura P., Kenney L.J., Anand G.S. The inner membrane histidine kinase EnvZ senses osmolality via helix-coil transitions in the cytoplasm. EMBO J. 2012, 31:2648-2659.
    • (2012) EMBO J. , vol.31 , pp. 2648-2659
    • Wang, L.C.1    Morgan, L.K.2    Godakumbura, P.3    Kenney, L.J.4    Anand, G.S.5
  • 56
    • 84902172298 scopus 로고    scopus 로고
    • Characterization and development of photoactivatable fluorescent proteins for single-molecule-based super resolution imaging
    • Wang S., Moffitt J.R., Dempsey G.T., Xie X.S., Zhuang X. Characterization and development of photoactivatable fluorescent proteins for single-molecule-based super resolution imaging. Proc. Natl. Acad. Sci. U. S. A. 2014, 111:8452-8457.
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. 8452-8457
    • Wang, S.1    Moffitt, J.R.2    Dempsey, G.T.3    Xie, X.S.4    Zhuang, X.5
  • 57
    • 0018668898 scopus 로고
    • Escherichia coli pleiotropic mutant that reduces amounts of several periplasmic and outer membrane proteins
    • Wanner B.L., Sarthy A., Beckwith J. Escherichia coli pleiotropic mutant that reduces amounts of several periplasmic and outer membrane proteins. J. Bacteriol. 1979, 140:229-239.
    • (1979) J. Bacteriol. , vol.140 , pp. 229-239
    • Wanner, B.L.1    Sarthy, A.2    Beckwith, J.3
  • 58
    • 0024453564 scopus 로고
    • Regulation of the phosphate regulon of Escherichia coli: analysis of mutant phoB and phoR genes causing different phenotypes
    • Yamada M., Makino K., Amemura M., Shinagawa H., Nakata A. Regulation of the phosphate regulon of Escherichia coli: analysis of mutant phoB and phoR genes causing different phenotypes. J. Bacteriol. 1989, 171:5601-5606.
    • (1989) J. Bacteriol. , vol.171 , pp. 5601-5606
    • Yamada, M.1    Makino, K.2    Amemura, M.3    Shinagawa, H.4    Nakata, A.5


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