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Volumn 188, Issue 7, 2006, Pages 2383-2391

Nucleotide-dependent dimerization of the C-terminal domain of the ABC transporter CvaB in colicin V secretion

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ABC TRANSPORTER CVAA; ABC TRANSPORTER CVAB; CELL MEMBRANE PROTEIN; COLICIN; COLICIN V; DIMER; MONOMER; MUTANT PROTEIN; NUCLEOTIDE; OLIGOMER; TOLC PROTEIN; UNCLASSIFIED DRUG;

EID: 33645226642     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.188.7.2383-2391.2006     Document Type: Article
Times cited : (9)

References (49)
  • 1
    • 15944405722 scopus 로고    scopus 로고
    • Positive co-operative activity and dimerization of the isolated ABC ATPase domain of HlyB from Escherichia coli
    • Benabdelhak, H., L. Schmitt, C. Horn, K. Jumel, M. A. Blight, and I. B. Holland. 2005. Positive co-operative activity and dimerization of the isolated ABC ATPase domain of HlyB from Escherichia coli. Biochem. J. 386:489-495.
    • (2005) Biochem. J. , vol.386 , pp. 489-495
    • Benabdelhak, H.1    Schmitt, L.2    Horn, C.3    Jumel, K.4    Blight, M.A.5    Holland, I.B.6
  • 2
    • 0036258208 scopus 로고    scopus 로고
    • Cystic fibrosis: A worldwide analysis of CFTR mutations-correlation with incidence data and application to screening
    • Bobadilla, J. L., M. Macek, J. P. Fine, and P. M. Farrell. 2002. Cystic fibrosis: a worldwide analysis of CFTR mutations-correlation with incidence data and application to screening. Hum. Mutat. 19:575-606.
    • (2002) Hum. Mutat. , vol.19 , pp. 575-606
    • Bobadilla, J.L.1    Macek, M.2    Fine, J.P.3    Farrell, P.M.4
  • 3
    • 0038799725 scopus 로고    scopus 로고
    • Structure of Msba from Vibrio cholerae: A multidrug resistance ABC transporter homolog in a closed conformation
    • Chang, G. 2003. Structure of Msba from Vibrio cholerae: a multidrug resistance ABC transporter homolog in a closed conformation. J. Mol. Biol. 330:419-430.
    • (2003) J. Mol. Biol. , vol.330 , pp. 419-430
    • Chang, G.1
  • 4
    • 0035823075 scopus 로고    scopus 로고
    • Structure of Msba from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters
    • Chang, G., and C. B. Roth. 2001. Structure of Msba from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters. Science 293:1793-1800.
    • (2001) Science , vol.293 , pp. 1793-1800
    • Chang, G.1    Roth, C.B.2
  • 5
    • 0141527345 scopus 로고    scopus 로고
    • A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle
    • Chen, J., G. Lu, J. Lin, A. L. Davidson, and F. A. Quiocho. 2003. A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol. Cell 12:651-661.
    • (2003) Mol. Cell , vol.12 , pp. 651-661
    • Chen, J.1    Lu, G.2    Lin, J.3    Davidson, A.L.4    Quiocho, F.A.5
  • 7
    • 0034669176 scopus 로고    scopus 로고
    • Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis
    • Diederichs, K., J. Diez, G. Greller, C. Mueller, J. Breed, C. Schnell, C. Vonrhein, W. Boos, and W. Welte. 2000. Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis. EMBO J. 19:5951-5961.
    • (2000) EMBO J. , vol.19 , pp. 5951-5961
    • Diederichs, K.1    Diez, J.2    Greller, G.3    Mueller, C.4    Breed, J.5    Schnell, C.6    Vonrhein, C.7    Boos, W.8    Welte, W.9
  • 8
    • 18644362391 scopus 로고    scopus 로고
    • Structural basis of energy transduction in the transport cycle of MsbA
    • Dong, J., G. Yang, and H. S. Mchaourab. 2005. Structural basis of energy transduction in the transport cycle of MsbA. Science 308:1023-1028.
    • (2005) Science , vol.308 , pp. 1023-1028
    • Dong, J.1    Yang, G.2    Mchaourab, H.S.3
  • 9
    • 0035801375 scopus 로고    scopus 로고
    • Structure of the C-terminal ABC ATPase domain of human Tap1, the transporter associated with antigen processing
    • Gaudet, R., and D. C. Wiley. 2001. Structure of the C-terminal ABC ATPase domain of human Tap1, the transporter associated with antigen processing. EMBO J. 20:4964-4972.
    • (2001) EMBO J. , vol.20 , pp. 4964-4972
    • Gaudet, R.1    Wiley, D.C.2
  • 10
    • 0025134451 scopus 로고
    • Genetic analysis of an MDR-like export system: The secretion of colicin V
    • Gilson, L., H. K. Mahanty, and R. Kolter. 1990. Genetic analysis of an MDR-like export system: the secretion of colicin V. EMBO J. 9:3875-3894.
    • (1990) EMBO J. , vol.9 , pp. 3875-3894
    • Gilson, L.1    Mahanty, H.K.2    Kolter, R.3
  • 11
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 12
    • 0034350522 scopus 로고    scopus 로고
    • A self-assembling neural network for modeling polymer structure
    • Harrison, R. W. 1999. A self-assembling neural network for modeling polymer structure. J. Math. Chem. 26:125-137.
    • (1999) J. Math. Chem. , vol.26 , pp. 125-137
    • Harrison, R.W.1
  • 13
    • 0029587028 scopus 로고
    • Analysis of six protein structures predicted by comparative modeling techniques
    • Harrison, R. W., D. Chatterjee, and I. T. Weber. 1995. Analysis of six protein structures predicted by comparative modeling techniques. Proteins 23:463-471.
    • (1995) Proteins , vol.23 , pp. 463-471
    • Harrison, R.W.1    Chatterjee, D.2    Weber, I.T.3
  • 15
    • 4744358624 scopus 로고    scopus 로고
    • The ATP switch model for ABC transporters
    • Higgins, C. F., and K. J. Linton. 2004. The ATP switch model for ABC transporters. Nat. Struct. Mol. Biol. 11:918-926.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 918-926
    • Higgins, C.F.1    Linton, K.J.2
  • 16
    • 0032698874 scopus 로고    scopus 로고
    • ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules organisms from bacteria to humans
    • Holland, I. B., and M. A. Blight 1999. ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules organisms from bacteria to humans. J. Mol. Biol. 293:381-399.
    • (1999) J. Mol. Biol. , vol.293 , pp. 381-399
    • Holland, I.B.1    Blight, M.A.2
  • 17
    • 0344195661 scopus 로고    scopus 로고
    • Structure and function of HlyB, the ABC-transporter essential for haemolysin secretion from Escherichia coli
    • W. N. Konings, H. R. Kaback, and J. S. Lolkema (ed.). Elsevier Press, New York, N.Y.
    • Holland, I. B., and M. A. Blight. 1996. Structure and function of HlyB, the ABC-transporter essential for haemolysin secretion from Escherichia coli, p. 111-135. In W. N. Konings, H. R. Kaback, and J. S. Lolkema (ed.), The handbook of biological physics. Volume 2. Transport processes in eukaryotic and prokaryotic organisms. Elsevier Press, New York, N.Y.
    • (1996) The Handbook of Biological Physics Volume 2. Transport Processes in Eukaryotic and Prokaryotic Organisms , vol.2 , pp. 111-135
    • Holland, I.B.1    Blight, M.A.2
  • 19
    • 0034705293 scopus 로고    scopus 로고
    • Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily
    • Hopfner, K. P., A. Karcher, D. S. Shin, L. Craig, L. M. Arthur, J. P. Carney, and J. A. Tainer. 2000. Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily. Cell 101:789-800.
    • (2000) Cell , vol.101 , pp. 789-800
    • Hopfner, K.P.1    Karcher, A.2    Shin, D.S.3    Craig, L.4    Arthur, L.M.5    Carney, J.P.6    Tainer, J.A.7
  • 20
    • 0242494861 scopus 로고    scopus 로고
    • Nucleotide dependent monomer/dimer equilibrium of OpuAA, the nucleotide-binding protein of the osmotically regulated ABC transporter OpuA from Bacillus subtilis
    • Horn, C., E. Bremer, and L. Schmitt. 2003. Nucleotide dependent monomer/dimer equilibrium of OpuAA, the nucleotide-binding protein of the osmotically regulated ABC transporter OpuA from Bacillus subtilis. J. Mol. Biol. 334:403-419.
    • (2003) J. Mol. Biol. , vol.334 , pp. 403-419
    • Horn, C.1    Bremer, E.2    Schmitt, L.3
  • 21
    • 0000416248 scopus 로고
    • In vitro recombination and mutagenesis of DNA: SOEing together tailor-made genes
    • B. A. White (ed.). Humana Press, Totowa, NJ
    • Horton, R. M. 1993. In vitro recombination and mutagenesis of DNA: SOEing together tailor-made genes, p. 251-262. In B. A. White (ed.), Methods in molecular biology, vol. 15. Humana Press, Totowa, NJ.
    • (1993) Methods in Molecular Biology , vol.15 , pp. 251-262
    • Horton, R.M.1
  • 22
    • 0032542358 scopus 로고    scopus 로고
    • Crystal structure of the ATP-binding subunit of an ABC transporter
    • Hung, L. W., I. X. Wang, K. Nikaido, P. Q. Liu, G. F. L. Ames, and S. H. Kim. 1998. Crystal structure of the ATP-binding subunit of an ABC transporter. Nature 396:703-707.
    • (1998) Nature , vol.396 , pp. 703-707
    • Hung, L.W.1    Wang, I.X.2    Nikaido, K.3    Liu, P.Q.4    Ames, G.F.L.5    Kim, S.H.6
  • 23
    • 0030858697 scopus 로고    scopus 로고
    • Interactions of dedicated export membrane proteins of the colicin V secretion system: CvaA, a member of the membrane fusion protein family, interacts with CvaB and TolC
    • Hwang, J. W., X. T. Zhong, and P. C. Tai. 1997. Interactions of dedicated export membrane proteins of the colicin V secretion system: CvaA, a member of the membrane fusion protein family, interacts with CvaB and TolC. J. Bacteriol. 179:6264-6270.
    • (1997) J. Bacteriol. , vol.179 , pp. 6264-6270
    • Hwang, J.W.1    Zhong, X.T.2    Tai, P.C.3
  • 24
    • 0038711772 scopus 로고    scopus 로고
    • The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p
    • Janas, E., M. Hofacker, M. Chen, S. Gompf, C. van der Does, and R. Tampe. 2003. The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p. J. Biol. Chem. 278:26862-26869.
    • (2003) J. Biol. Chem. , vol.278 , pp. 26862-26869
    • Janas, E.1    Hofacker, M.2    Chen, M.3    Gompf, S.4    Van Der Does, C.5    Tampe, R.6
  • 25
    • 1842610700 scopus 로고    scopus 로고
    • The ABC transporter structure and mechanism: Perspectives on recent research
    • Jones, P. M., and A. M. George. 2004. The ABC transporter structure and mechanism: perspectives on recent research. Cell. Mol. Life Sci. 61:682-699.
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 682-699
    • Jones, P.M.1    George, A.M.2
  • 26
    • 0034941969 scopus 로고    scopus 로고
    • Crystal structures of the MJ1267 ATP-binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter
    • Karpowich, N., O. Martsinkevich, L. Linda Millen, Y.-R. Yuan, P. L. Dai, K. MacVey, P. J. Thomas, and J. F. Hunt. 2001. Crystal structures of the MJ1267 ATP-binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter. Structure 9:571-586.
    • (2001) Structure , vol.9 , pp. 571-586
    • Karpowich, N.1    Martsinkevich, O.2    Linda Millen, L.3    Yuan, Y.-R.4    Dai, P.L.5    MacVey, K.6    Thomas, P.J.7    Hunt, J.F.8
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 4143115811 scopus 로고    scopus 로고
    • Structure and mechanism of ABC transporters
    • Locher, K. P. 2004. Structure and mechanism of ABC transporters. Curr. Opin. Struct. Biol. 14:426-431.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 426-431
    • Locher, K.P.1
  • 30
    • 0037052565 scopus 로고    scopus 로고
    • The E. Coli Btucd structure: A framework for ABC transporter architecture and mechanism
    • Locher, K. P., A. T. Lee, and D. C. Rees. 2002. The E. Coli Btucd structure: a framework for ABC transporter architecture and mechanism. Science 296:1091-1098.
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 31
    • 0036829647 scopus 로고    scopus 로고
    • The "LSGGQ" motif in each nucleotide-binding domain of human P-glycoprotein is adjacent to the opposing Walker a sequence
    • Loo, T. W., M. C. Bartlett, and D. M. Clarke. 2002. The "LSGGQ" motif in each nucleotide-binding domain of human P-glycoprotein is adjacent to the opposing Walker A sequence. J. Biol. Chem. 277:41303-41306.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41303-41306
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 32
    • 7244240754 scopus 로고    scopus 로고
    • 12 ATP-binding cassette (ABC) transporter BtuCD
    • 12 ATP-binding cassette (ABC) transporter BtuCD. J. Biol. Chem. 279:45013-45019.
    • (2004) J. Biol. Chem. , vol.279 , pp. 45013-45019
    • Oloo, E.O.1    Tieleman, D.P.2
  • 33
    • 18644363550 scopus 로고    scopus 로고
    • Structure of the ABC transporter MsbAin complex with ADP. Vanadate and lipopolysaccharide
    • Reyes, C. L., and G. Chang. 2005. Structure of the ABC transporter MsbAin complex with ADP. Vanadate and lipopolysaccharide. Science 308:1028-1031.
    • (2005) Science , vol.308 , pp. 1028-1031
    • Reyes, C.L.1    Chang, G.2
  • 34
    • 0042818091 scopus 로고    scopus 로고
    • Disulfide cross-linking reveals a site of stable interaction between C-terminal regulatory domains of the two MalK subunits in the maltose transport complex
    • Samanta, S., T. Ayvaz, M. Reyes, H. A. Shuman, J. Chen, and A. L. Davidson. 2003. Disulfide cross-linking reveals a site of stable interaction between C-terminal regulatory domains of the two MalK subunits in the maltose transport complex. J. Biol. Chem. 278:35265-35271.
    • (2003) J. Biol. Chem. , vol.278 , pp. 35265-35271
    • Samanta, S.1    Ayvaz, T.2    Reyes, M.3    Shuman, H.A.4    Chen, J.5    Davidson, A.L.6
  • 36
    • 0038799733 scopus 로고    scopus 로고
    • Crystal Structure of the nucleotide binding domain of the ABC-transporter haemolysin B: Identification of a variable region within ABC helical domains
    • Schmitt, L., H. Benabdelhak, M. A. Blight, I. B. Holland, and M. T. Syubbs. 2003. Crystal Structure of the nucleotide binding domain of the ABC-transporter haemolysin B: identification of a variable region within ABC helical domains. J. Mol. Biol. 330:333-342.
    • (2003) J. Mol. Biol. , vol.330 , pp. 333-342
    • Schmitt, L.1    Benabdelhak, H.2    Blight, M.A.3    Holland, I.B.4    Syubbs, M.T.5
  • 37
    • 0036909285 scopus 로고    scopus 로고
    • Structure and mechanism of ABC transporters
    • Schmitt, L., and R. Tampé. 2002. Structure and mechanism of ABC transporters. Curr. Opin. Struct. Biol. 12:754-760.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 754-760
    • Schmitt, L.1    Tampé, R.2
  • 38
    • 0031810816 scopus 로고    scopus 로고
    • ATP-binding-cassette (ABC) transport systems: Functional and structural aspects of the ATP-hydrolyzing subunits/domains
    • Schneider, E., and S. Hunke. 1998. ATP-binding-cassette (ABC) transport systems: functional and structural aspects of the ATP-hydrolyzing subunits/domains. FEMS Microbiol. Rev. 22:1-20.
    • (1998) FEMS Microbiol. Rev. , vol.22 , pp. 1-20
    • Schneider, E.1    Hunke, S.2
  • 39
    • 0025954269 scopus 로고
    • Structure-function analysis of the histidine permease and comparison with cystic fibrosis mutations
    • Shyamala, V., V. Baichwal, E. Beall, and G. F. Ames. 1991. Structure-function analysis of the histidine permease and comparison with cystic fibrosis mutations. J. Biol. Chem. 266:18714-18719.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18714-18719
    • Shyamala, V.1    Baichwal, V.2    Beall, E.3    Ames, G.F.4
  • 40
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F. W., and B. A. Moffatt. 1986. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 41
    • 0030944568 scopus 로고    scopus 로고
    • Double-glycine-type leader peptides direct secretion of bacteriocins by ABC transporters: Colicin V secretion in Lactococcus lactis
    • van Belkum, M. J., R. W. Worobo, and M. E. Stiles. 1997. Double-glycine-type leader peptides direct secretion of bacteriocins by ABC transporters: colicin V secretion in Lactococcus lactis. Mol. Microbiol. 23:1293-1301.
    • (1997) Mol. Microbiol. , vol.23 , pp. 1293-1301
    • Van Belkum, M.J.1    Worobo, R.W.2    Stiles, M.E.3
  • 42
    • 0038374988 scopus 로고    scopus 로고
    • Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: Nucleotide-free and nucleotide-bound conformations
    • Verdon, G., S. V. Albers, B. W. Dijkstra, A. J. Driessen, and A. M. Thunnissen. 2003. Crystal structures of the ATPase subunit of the glucose ABC transporter from Sulfolobus solfataricus: nucleotide-free and nucleotide-bound conformations. J. Mol. Biol. 330:343-358.
    • (2003) J. Mol. Biol. , vol.330 , pp. 343-358
    • Verdon, G.1    Albers, S.V.2    Dijkstra, B.W.3    Driessen, A.J.4    Thunnissen, A.M.5
  • 44
    • 14544300522 scopus 로고    scopus 로고
    • CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains
    • Vergani, P., S. W. Lockless, A. C. Nairn, and D. C. Gadsby. 2005. CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains. Nature 433:876-880.
    • (2005) Nature , vol.433 , pp. 876-880
    • Vergani, P.1    Lockless, S.W.2    Nairn, A.C.3    Gadsby, D.C.4
  • 45
    • 0035943735 scopus 로고    scopus 로고
    • The crystal structure of the MJ0796 ATP-binding cassette: Implications for the structural consequences of ATP hydrolysis in the active site of an ABC-transporter
    • Yuan, Y., S. Blecker, O. Martsinkevich, L. Millen, P. J. Thomas, and J. F. Hunt. 2001. The crystal structure of the MJ0796 ATP-binding cassette: implications for the structural consequences of ATP hydrolysis in the active site of an ABC-transporter. J. Biol. Chem. 276:32313-32321.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32313-32321
    • Yuan, Y.1    Blecker, S.2    Martsinkevich, O.3    Millen, L.4    Thomas, P.J.5    Hunt, J.F.6
  • 46
    • 16644362409 scopus 로고    scopus 로고
    • The role of CAPS buffer in expanding the crystallization space of the nucleotide-binding domain of the ABC transporter haemolysin B from Escherichia coli
    • Zaitseva, J., I. B. Holland, and L. Schmitt. 2004. The role of CAPS buffer in expanding the crystallization space of the nucleotide-binding domain of the ABC transporter haemolysin B from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 60:1076-1084.
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 1076-1084
    • Zaitseva, J.1    Holland, I.B.2    Schmitt, L.3
  • 47
    • 21244454073 scopus 로고    scopus 로고
    • H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB
    • Zaitseva, J., S. Jenewein, T. Jumpertz, B. Holland, and L. Schmitt. 2005. H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB. EMBO J. 24:1901-1910.
    • (2005) EMBO J. , vol.24 , pp. 1901-1910
    • Zaitseva, J.1    Jenewein, S.2    Jumpertz, T.3    Holland, B.4    Schmitt, L.5
  • 48
    • 22244452024 scopus 로고    scopus 로고
    • Functional characterization and ATP-induced dimerization of the isolated ABC-domain of the haemolysin B transporter
    • Zaitseva, J., S. Jenewein, A. Wiedenmann, H. Benabdelhak, I. B. Holland, and L. Schmitt. 2005. Functional characterization and ATP-induced dimerization of the isolated ABC-domain of the haemolysin B transporter. Biochemistry 44:9680-9690.
    • (2005) Biochemistry , vol.44 , pp. 9680-9690
    • Zaitseva, J.1    Jenewein, S.2    Wiedenmann, A.3    Benabdelhak, H.4    Holland, I.B.5    Schmitt, L.6
  • 49
    • 0031894325 scopus 로고    scopus 로고
    • When an ATPase is not an ATPase: At low temperatures the CTD of the ABC transporter CvaB is a GTPase
    • Zhong, X., and P. C. Tai. 1998. When an ATPase is not an ATPase: at low temperatures the CTD of the ABC transporter CvaB is a GTPase. J. Bacteriol. 180:1347-1353.
    • (1998) J. Bacteriol. , vol.180 , pp. 1347-1353
    • Zhong, X.1    Tai, P.C.2


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