메뉴 건너뛰기




Volumn 44, Issue 49, 2005, Pages 16301-16309

In vitro functional characterization of BtuCD-F, the Escherichia coli ABC transporter for vitamin B12 uptake

Author keywords

[No Author keywords available]

Indexed keywords

CHARACTERIZATION; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ESCHERICHIA COLI; HYDROLYSIS; PROTEINS; VITAMINS;

EID: 28944442871     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0513103     Document Type: Article
Times cited : (128)

References (47)
  • 1
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins, C. F. (1992) ABC transporters: From microorganisms to man, Annu. Rev. Cell Biol. 8, 67-113.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 2
    • 0034917716 scopus 로고    scopus 로고
    • The human ATP-binding cassette (ABC) transporter superfamily
    • Dean, M., Rzhetsky, A., and Allikmets, R. (2001) The human ATP-binding cassette (ABC) transporter superfamily, Gen. Res. 11, 1156-1166.
    • (2001) Gen. Res. , vol.11 , pp. 1156-1166
    • Dean, M.1    Rzhetsky, A.2    Allikmets, R.3
  • 3
    • 0035019469 scopus 로고    scopus 로고
    • ABC transporters: Physiology, structure and mechanism - An overview
    • Higgins, C. F. (2001) ABC transporters: Physiology, structure and mechanism - an overview, Res. Microbiol. 152, 205-210.
    • (2001) Res. Microbiol. , vol.152 , pp. 205-210
    • Higgins, C.F.1
  • 4
    • 3943062954 scopus 로고    scopus 로고
    • ATP-binding cassette transporters in bacteria
    • Davidson, A. L., 61nd Chen, J. (2004) ATP-binding cassette transporters in bacteria, Annu. Rev. Biochem. 73, 241-268.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 241-268
    • Davidson, A.L.1    Chen, J.2
  • 5
    • 2942750350 scopus 로고    scopus 로고
    • ATP-binding cassette (ABC) transporters in human metabolism and diseases
    • Stefkova, J., Poledne, R., and Hubacek, J. A. (2004) ATP-binding cassette (ABC) transporters in human metabolism and diseases, Physiol. Res. 53, 235-243.
    • (2004) Physiol. Res. , vol.53 , pp. 235-243
    • Stefkova, J.1    Poledne, R.2    Hubacek, J.A.3
  • 6
    • 0032323640 scopus 로고    scopus 로고
    • Overview of bacterial ABC transporters
    • Nikaido, H., and Hall, J. A. (1998) Overview of bacterial ABC transporters, Methods Enzymol. 292, 3-20.
    • (1998) Methods Enzymol , vol.292 , pp. 3-20
    • Nikaido, H.1    Hall, J.A.2
  • 7
    • 0032698874 scopus 로고    scopus 로고
    • ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans
    • Holland, I. B., and Blight, M. A. (1999) ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in 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
  • 9
    • 0028215587 scopus 로고
    • Sequence relationships between integral inner membrane proteins of binding protein-dependent transport systems: Evolution by recurrent gene duplications
    • Saurin, W., and Dassa, E. (1994) Sequence relationships between integral inner membrane proteins of binding protein-dependent transport systems: Evolution by recurrent gene duplications, Protein Sci. 3, 325-344.
    • (1994) Protein Sci. , vol.3 , pp. 325-344
    • Saurin, W.1    Dassa, E.2
  • 10
    • 0031810816 scopus 로고    scopus 로고
    • ATP-binding-cassette (ABC) transport systems: Functional and structural aspects of the ATP-hydrolyzing subunits/domains
    • Schneider, E., and Hunke, S. (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
  • 11
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher, K. P., Lee, A. T., and Rees, D. C. (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
  • 12
    • 0019230249 scopus 로고
    • 12 in Escherichia coli: Some observations on the roles of the gene products of BtuC and TonB
    • 12 in Escherichia coli: Some observations on the roles of the gene products of BtuC and TonB, J. Biol. Chem. 255, 4313-4319.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4313-4319
    • Reynolds, P.R.1    Mottur, G.P.2    Bradbeer, C.3
  • 13
    • 0021893059 scopus 로고
    • 12 in Escherichia coli: Cloning of the btuCD region
    • 12 in Escherichia coli: Cloning of the btuCD region, J. Bacteriol. 162, 888-896.
    • (1985) J. Bacteriol. , vol.162 , pp. 888-896
    • Deveaux, L.C.1    Kadner, R.J.2
  • 14
    • 0032885183 scopus 로고    scopus 로고
    • A new class of cobalamin transport mutants (btuF) provides genetic evidence for a periplasmic binding protein in Salmonella typhimurium
    • Van Bibber, M., Bradbeer, C., Clark, N., and Roth, J. R. (1999) A new class of cobalamin transport mutants (btuF) provides genetic evidence for a periplasmic binding protein in Salmonella typhimurium, J. Bacteriol. 181, 5539-5541.
    • (1999) J. Bacteriol. , vol.181 , pp. 5539-5541
    • Van Bibber, M.1    Bradbeer, C.2    Clark, N.3    Roth, J.R.4
  • 16
    • 0037168666 scopus 로고    scopus 로고
    • The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter
    • Berths, E. L., Locher, K. P., Lee, A. T., and Rees, D. C. (2002) The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter, Proc. Natl. Acad. Sci. U.S.A. 99, 16642-16647.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 16642-16647
    • Berths, E.L.1    Locher, K.P.2    Lee, A.T.3    Rees, D.C.4
  • 17
    • 0037424465 scopus 로고    scopus 로고
    • 12 suggest a functionally important reduction in protein mobility upon ligand binding
    • 12 suggest a functionally important reduction in protein mobility upon ligand binding, J. Biol. Chem. 278, 8429-8434.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8429-8434
    • Karpowich, N.K.1    Huang, H.H.2    Smith, P.C.3    Hunt, J.F.4
  • 19
    • 0041529863 scopus 로고    scopus 로고
    • The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA
    • Patzlaff, J. S., van der Heide, T., and Poolman, B. (2003) The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA, J. Biol. Chem. 278, 29546-29551.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29546-29551
    • Patzlaff, J.S.1    Van Der Heide, T.2    Poolman, B.3
  • 20
    • 0023874147 scopus 로고
    • A method for the determination of inorganic phosphate in the presence of labile organic phosphate and high concentrations of protein: Application to lens ATPases
    • Chifflet, S., Torriglia, A., Chiesa, R., and Tolosa, S. (1988) A method for the determination of inorganic phosphate in the presence of labile organic phosphate and high concentrations of protein: Application to lens ATPases, Anal. Biochem. 168, 1-4.
    • (1988) Anal. Biochem. , vol.168 , pp. 1-4
    • Chifflet, S.1    Torriglia, A.2    Chiesa, R.3    Tolosa, S.4
  • 21
    • 0037126588 scopus 로고    scopus 로고
    • On the osmotic signal and osmosensing mechanism of an ABC transport system for glycine betaine
    • van der Heide, T., Stuart, M. C. A., and Poolman, B. (2001) On the osmotic signal and osmosensing mechanism of an ABC transport system for glycine betaine, EMBO J. 20, 7022-7032.
    • (2001) EMBO J. , vol.20 , pp. 7022-7032
    • Heide, T.1    Stuart, M.C.A.2    Poolman, B.3
  • 22
    • 0033973103 scopus 로고    scopus 로고
    • The detergent-soluble maltose transporter is activated by maltose binding protein and verapamil
    • Reich-Slotky, R., Panagiotidis, C., Reyes, M., and Shuman, H. A. (2000) The detergent-soluble maltose transporter is activated by maltose binding protein and verapamil, J. Bacteriol. 182, 993-1000.
    • (2000) J. Bacteriol. , vol.182 , pp. 993-1000
    • Reich-Slotky, R.1    Panagiotidis, C.2    Reyes, M.3    Shuman, H.A.4
  • 23
    • 0024291663 scopus 로고
    • Mechanisms of membrane protein insertion in liposomes during reconstitution procedures involving the use of detergents. 2. Incorporation of the light-driven proton pump bacteriorhodopsin
    • Rigaud, J.-L., Paternostre, M.-T., and Bluzat, A. (1988) Mechanisms of membrane protein insertion in liposomes during reconstitution procedures involving the use of detergents. 2. Incorporation of the light-driven proton pump bacteriorhodopsin, Biochemistry 27, 2677-2688.
    • (1988) Biochemistry , vol.27 , pp. 2677-2688
    • Rigaud, J.-L.1    Paternostre, M.-T.2    Bluzat, A.3
  • 24
    • 0029101114 scopus 로고
    • Reconstitution of membrane proteins into liposomes: Application to energy-transducing membrane proteins
    • Rigaud, J.-L., Pitard, B., and Levy, D. (1995) Reconstitution of membrane proteins into liposomes: Application to energy-transducing membrane proteins, Biochim. Biophys. Acta 1231, 223-246.
    • (1995) Biochim. Biophys. Acta , vol.1231 , pp. 223-246
    • Rigaud, J.-L.1    Pitard, B.2    Levy, D.3
  • 25
    • 0024282303 scopus 로고
    • Lipid requirement of the branched-chain amino acid transport system of Streptococcus cremoris
    • Driessen, A. J., Zheng, T., In't Veld, G., Op den Kamp, J. A., and Konings, W. N. (1988) Lipid requirement of the branched-chain amino acid transport system of Streptococcus cremoris, Biochemistry 27, 865-872.
    • (1988) Biochemistry , vol.27 , pp. 865-872
    • Driessen, A.J.1    Zheng, T.2    In't Veld, G.3    Op Den Kamp, J.A.4    Konings, W.N.5
  • 26
    • 0029897240 scopus 로고    scopus 로고
    • Unidirectional reconstitution into detergent-destabilized liposomes of the purified lactose transport system of Streptococcus thermophilus
    • Knol, J., Veenhoff, L., Liang, W.-J., Henderson, P. J. F., Leblanc, G., and Poolman, B. (1996) Unidirectional reconstitution into detergent-destabilized liposomes of the purified lactose transport system of Streptococcus thermophilus, J. Biol. Chem. 271, 15358-15366.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15358-15366
    • Knol, J.1    Veenhoff, L.2    Liang, W.-J.3    Henderson, P.J.F.4    Leblanc, G.5    Poolman, B.6
  • 27
    • 0035852667 scopus 로고    scopus 로고
    • Trapping the transition state of an ATP-binding cassette transporter: Evidence for a concerted mechanism of maltose transport
    • Chen, J., Sharma, S., Quiocho, F. A., and Davidson, A. L. (2001) Trapping the transition state of an ATP-binding cassette transporter: Evidence for a concerted mechanism of maltose transport, Proc. Natl. Acad. Sci. U.S.A. 98, 1525-1530.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 1525-1530
    • Chen, J.1    Sharma, S.2    Quiocho, F.A.3    Davidson, A.L.4
  • 28
    • 0030803791 scopus 로고    scopus 로고
    • Characterization of the adenosine triphosphatase activity of the periplasmic histidine permease, a traffic ATPase (ABC transporter)
    • Liu, C. E., Liu, P.-Q., and Ames, G. F.-L. (1997) Characterization of the adenosine triphosphatase activity of the periplasmic histidine permease, a traffic ATPase (ABC transporter), J. Biol. Chem. 272, 21883-21891.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21883-21891
    • Liu, C.E.1    Liu, P.-Q.2    Ames, G.F.-L.3
  • 29
    • 0026549522 scopus 로고
    • Mechanism of maltose transport in Escherichia coli: Transmembrane signaling by periplasmic binding proteins
    • Davidson, A. L., Shuman, H. A., and Nikaido, H. (1992) Mechanism of maltose transport in Escherichia coli: Transmembrane signaling by periplasmic binding proteins, Proc. Natl. Acad. Sci. U.S.A. 89, 2360-2364.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 2360-2364
    • Davidson, A.L.1    Shuman, H.A.2    Nikaido, H.3
  • 30
    • 0029557690 scopus 로고
    • The inhibition of maltose transport by the unliganded form of the maltose-binding protein of Escherichia coli: Experimental findings and mathematical treatment
    • Merino, G., Boos, W., Shuman, H. A., and Bohl, E. (1995) The inhibition of maltose transport by the unliganded form of the maltose-binding protein of Escherichia coli: Experimental findings and mathematical treatment, J. Theor. Biol. 177, 171-179.
    • (1995) J. Theor. Biol. , vol.177 , pp. 171-179
    • Merino, G.1    Boos, W.2    Shuman, H.A.3    Bohl, E.4
  • 31
    • 17544365410 scopus 로고    scopus 로고
    • Liganded and unliganded receptors interact with equal affinity with the membrane complex of periplasmic permeases, a subfamily of traffic ATPases
    • Ames, G. F.-L., Liu, C. E., Joshi, A. K., and Nikaido, H. (1996) Liganded and unliganded receptors interact with equal affinity with the membrane complex of periplasmic permeases, a subfamily of traffic ATPases, J. Biol. Chem. 271, 14264-14270.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14264-14270
    • Ames, G.F.-L.1    Liu, C.E.2    Joshi, A.K.3    Nikaido, H.4
  • 32
    • 0031571605 scopus 로고    scopus 로고
    • Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor
    • Quiocho, F. A., Spurlino, J. C., and Rodseth, L. E. (1997) Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor, Structure 5, 997-1015.
    • (1997) Structure , vol.5 , pp. 997-1015
    • Quiocho, F.A.1    Spurlino, J.C.2    Rodseth, L.E.3
  • 33
    • 0028971173 scopus 로고
    • Vanadate and bafilomycin Al are potent inhibitors of the ATPase activity of the reconstituted bacterial ATP-binding cassette transporter for maltose (MalFGK2)
    • Hunke, S., Drösse, S., and Schneider, E. (1995) Vanadate and bafilomycin Al are potent inhibitors of the ATPase activity of the reconstituted bacterial ATP-binding cassette transporter for maltose (MalFGK2). Biochem. Biophys. Res. Commun. 216, 589-594.
    • (1995) Biochem. Biophys. Res. Commun. , vol.216 , pp. 589-594
    • Hunke, S.1    Drösse, S.2    Schneider, E.3
  • 34
    • 0034828112 scopus 로고    scopus 로고
    • Purification and characterization of the heterologously expressed trehalose/maltose ABC transporter complex of the hyperthermophilic archaeon Thermococcus litoralis
    • Greller, G., Riek, R., and Boos, W. (2001) Purification and characterization of the heterologously expressed trehalose/maltose ABC transporter complex of the hyperthermophilic archaeon Thermococcus litoralis, Eur. J. Biochem. 268, 4011-4018.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4011-4018
    • Greller, G.1    Riek, R.2    Boos, W.3
  • 35
    • 0020320406 scopus 로고
    • Active transport of maltose in Escherichia coli K12: Role of the periplasmic maltose-binding protein and evidence for a substrate recognition site in the cytoplasmic membrane
    • Shuman, H. A. (1982) Active transport of maltose in Escherichia coli K12: Role of the periplasmic maltose-binding protein and evidence for a substrate recognition site in the cytoplasmic membrane, J. Biol. Chem. 257, 5455-5461.
    • (1982) J. Biol. Chem. , vol.257 , pp. 5455-5461
    • Shuman, H.A.1
  • 36
    • 0024726144 scopus 로고
    • Reconstitution of a bacterial periplasmic permease in proteoliposomes and demonstration of ATP hydrolysis concomitant with transport
    • Bishop, L., Agbayani, J., R., Ambudkar, S. V., Maloney, P. C., and Ames, G. F.-L. (1989) Reconstitution of a bacterial periplasmic permease in proteoliposomes and demonstration of ATP hydrolysis concomitant with transport, Proc. Natl. Acad. Sci. U.S.A. 86, 6953-6957.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 6953-6957
    • Bishop, L.1    Agbayani, J.R.2    Ambudkar, S.V.3    Maloney, P.C.4    Ames, G.F.-L.5
  • 37
    • 0025214263 scopus 로고
    • Overproduction, solubilization, and reconstitution of the maltose transport system from Escherichia coli
    • Davidson, A. L., and Nikaido, H. (1990) Overproduction, solubilization, and reconstitution of the maltose transport system from Escherichia coli, J. Biol. Chem. 265, 4254-4260.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4254-4260
    • Davidson, A.L.1    Nikaido, H.2
  • 38
    • 0031021530 scopus 로고    scopus 로고
    • Characterization of transport through the periplasmic histidine permease using proteoliposomes reconstituted by dialysis
    • Liu, C. E., and Ames, G. F.-L. (1997) Characterization of transport through the periplasmic histidine permease using proteoliposomes reconstituted by dialysis, J. Biol. Chem. 272, 859-866.
    • (1997) J. Biol. Chem. , vol.272 , pp. 859-866
    • Liu, C.E.1    Ames, G.F.-L.2
  • 39
    • 0344442852 scopus 로고    scopus 로고
    • On the role of the two extracytoplasmic substrate-binding domains in the ABC transporter OpuA
    • Biemans-Oldehinkel, E., and Poolman, B. (2003) On the role of the two extracytoplasmic substrate-binding domains in the ABC transporter OpuA, EMBO J. 22, 1-11.
    • (2003) EMBO J. , vol.22 , pp. 1-11
    • Biemans-Oldehinkel, E.1    Poolman, B.2
  • 40
    • 0026744442 scopus 로고
    • Interaction between maltose-binding protein and the membrane-associated maltose transporter complex in Escherichia coli
    • Dean, D. A., Hor, L. I., Shuman, H. A., and Nikaido, H. (1992) Interaction between maltose-binding protein and the membrane-associated maltose transporter complex in Escherichia coli, Mol. Microbiol. 6, 2033-2040.
    • (1992) Mol. Microbiol. , vol.6 , pp. 2033-2040
    • Dean, D.A.1    Hor, L.I.2    Shuman, H.A.3    Nikaido, H.4
  • 41
    • 0024604620 scopus 로고
    • Reconstitution of the histidine periplasmic transport system in membrane vesicles. Energy coupling and itneraction between the binding protein and the membrane complex
    • Prossnitz, E., Gee, A., and Ames, G. F.-L. (1989) Reconstitution of the histidine periplasmic transport system in membrane vesicles. Energy coupling and itneraction between the binding protein and the membrane complex, J. Biol. Chem. 264, 5006-5014.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5006-5014
    • Prossnitz, E.1    Gee, A.2    Ames, G.F.-L.3
  • 42
    • 3542996250 scopus 로고    scopus 로고
    • The binding specificity of OppA determines the selectivity of the oligopeptide ABC transporter
    • Doeven, M. K., Abele, R., Tampe, R., and Poolman, B. (2004) The binding specificity of OppA determines the selectivity of the oligopeptide ABC transporter, J. Biol. Chem. 279, 32301-32307.
    • (2004) J. Biol. Chem. , vol.279 , pp. 32301-32307
    • Doeven, M.K.1    Abele, R.2    Tampe, R.3    Poolman, B.4
  • 43
    • 0035004765 scopus 로고    scopus 로고
    • Purification and characterization of the membrane-bound complex of an ABC-transporter, the histidine permease
    • Ames, G. F.-L., Nikaido, K., Wang, I. X., Liu, P.-Q., Liu, C. E., and Hu, C. (2001) Purification and characterization of the membrane-bound complex of an ABC-transporter, the histidine permease, J. Bioenerg. Biomembr. 33, 79-92.
    • (2001) J. Bioenerg. Biomembr. , vol.33 , pp. 79-92
    • Ames, G.F.-L.1    Nikaido, K.2    Wang, I.X.3    Liu, P.-Q.4    Liu, C.E.5    Hu, C.6
  • 44
    • 1942532335 scopus 로고    scopus 로고
    • ABC transporter architecture and mechanism: Implications from the crystal structures of BtuCD and BtuF
    • Locher, K. P., and Borths, E. L. (2004) ABC transporter architecture and mechanism: implications from the crystal structures of BtuCD and BtuF, FEBS Lett. 564, 264-268.
    • (2004) FEBS Lett. , vol.564 , pp. 264-268
    • Locher, K.P.1    Borths, E.L.2
  • 45
    • 0032534754 scopus 로고    scopus 로고
    • The crystal structure of pneumococcal surface antigen PsaA reveals a metal-binding site and a novel structure for a putative ABC-type binding protein
    • Lawrence, M. C., Pilling, P. A., Epa, V. C., Berry, A. M., Ogunniyi, A. D., and Paton, J. C. (1998) The crystal structure of pneumococcal surface antigen PsaA reveals a metal-binding site and a novel structure for a putative ABC-type binding protein, Structure 6, 1553-1561.
    • (1998) Structure , vol.6 , pp. 1553-1561
    • Lawrence, M.C.1    Pilling, P.A.2    Epa, V.C.3    Berry, A.M.4    Ogunniyi, A.D.5    Paton, J.C.6
  • 46
    • 0032808951 scopus 로고    scopus 로고
    • Glucose transport in the extremely thermoacidophilic Sulfolobus solfataricus involves a high-affinity membrane-integrated binding protein
    • Albers, S. V., Elferink, M. G., Charlebois, R. L., Sensen, C. W., Driessen, A. J., and Konings, W. N. (1999) Glucose transport in the extremely thermoacidophilic Sulfolobus solfataricus involves a high-affinity membrane-integrated binding protein, J. Bacteriol. 181, 4285-4291.
    • (1999) J. Bacteriol. , vol.181 , pp. 4285-4291
    • Albers, S.V.1    Elferink, M.G.2    Charlebois, R.L.3    Sensen, C.W.4    Driessen, A.J.5    Konings, W.N.6
  • 47
    • 0036774002 scopus 로고    scopus 로고
    • ABC transporters: One, two or four extracytoplasmic substrate-binding sites?
    • van der Heide, T., and Poolman, B. (2002) ABC transporters: one, two or four extracytoplasmic substrate-binding sites?, EMBO Rep. 3, 938-943.
    • (2002) EMBO Rep. , vol.3 , pp. 938-943
    • Van Der Heide, T.1    Poolman, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.