메뉴 건너뛰기




Volumn 518, Issue 7537, 2015, Pages 68-73

Transport domain unlocking sets the uptake rate of an aspartate transporter

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTATE TRANSPORTER; ASPARTIC ACID; EXCITATORY AMINO ACID TRANSPORTER; ION; PROTEOLIPOSOME; SOLVENT; UNCLASSIFIED DRUG; AMINO ACID TRANSPORTER; DETERGENT; LIGAND; MUTANT PROTEIN; PROTEOLIPID; PROTEOLIPOSOMES; SODIUM;

EID: 84923107452     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature14158     Document Type: Article
Times cited : (132)

References (55)
  • 1
    • 0029860263 scopus 로고    scopus 로고
    • Flux coupling in a neuronal glutamate transporter
    • Zerangue, N. & Kavanaugh, M. P. Flux coupling in a neuronal glutamate transporter. Nature 383, 634-637 (1996).
    • (1996) Nature , vol.383 , pp. 634-637
    • Zerangue, N.1    Kavanaugh, M.P.2
  • 2
    • 7244254186 scopus 로고    scopus 로고
    • Structure of a glutamate transporter homologue from Pyrococcus horikoshii
    • Yernool, D., Boudker, O., Jin, Y. & Gouaux, E. Structure of a glutamate transporter homologue from Pyrococcus horikoshii. Nature 431, 811-818 (2004).
    • (2004) Nature , vol.431 , pp. 811-818
    • Yernool, D.1    Boudker, O.2    Jin, Y.3    Gouaux, E.4
  • 3
    • 33846505059 scopus 로고    scopus 로고
    • Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter
    • Boudker, O., Ryan, R. M., Yernool, D., Shimamoto, K. & Gouaux, E. Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter. Nature 445, 387-393 (2007).
    • (2007) Nature , vol.445 , pp. 387-393
    • Boudker, O.1    Ryan, R.M.2    Yernool, D.3    Shimamoto, K.4    Gouaux, E.5
  • 4
    • 72449164409 scopus 로고    scopus 로고
    • Transportmechanismof a bacterial homologue of glutamate transporters
    • Reyes, N., Ginter, C. & Boudker, O. Transportmechanismof a bacterial homologue of glutamate transporters. Nature 462, 880-885 (2009).
    • (2009) Nature , vol.462 , pp. 880-885
    • Reyes, N.1    Ginter, C.2    Boudker, O.3
  • 5
    • 84857992685 scopus 로고    scopus 로고
    • Crystal structure of an asymmetric trimer of a bacterial glutamate transporter homolog
    • Verdon, G. & Boudker, O. Crystal structure of an asymmetric trimer of a bacterial glutamate transporter homolog. Nature Struct. Mol. Biol. 19, 355-357 (2012).
    • (2012) Nature Struct. Mol. Biol. , vol.19 , pp. 355-357
    • Verdon, G.1    Boudker, O.2
  • 6
    • 84901049540 scopus 로고    scopus 로고
    • Coupled ion binding and structural transitions along the transport cycle of glutamate transporters
    • Verdon, G., Oh, S., Serio, R. N. & Boudker, O. Coupled ion binding and structural transitions along the transport cycle of glutamate transporters. ELife 3, e02283 (2014).
    • (2014) ELife , vol.3
    • Verdon, G.1    Oh, S.2    Serio, R.N.3    Boudker, O.4
  • 7
    • 67650526059 scopus 로고    scopus 로고
    • Functional characterization of a Na1-dependent aspartate transporter from Pyrococcus horikoshii
    • Ryan, R. M., Compton, E. L. & Mindell, J. A. Functional characterization of a Na1-dependent aspartate transporter from Pyrococcus horikoshii. J. Biol. Chem. 284, 17540-17548 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 17540-17548
    • Ryan, R.M.1    Compton, E.L.2    Mindell, J.A.3
  • 8
    • 77951680965 scopus 로고    scopus 로고
    • Na1:aspartate coupling stoichiometry in the glutamate transporter homologue GltPh
    • Groeneveld, M. & Slotboom, D. J. Na1:aspartate coupling stoichiometry in the glutamate transporter homologue GltPh. Biochemistry 49, 3511-3513 (2010).
    • (2010) Biochemistry , vol.49 , pp. 3511-3513
    • Groeneveld, M.1    Slotboom, D.J.2
  • 9
    • 84885669136 scopus 로고    scopus 로고
    • Transport dynamics of a glutamate transporter homologue
    • Akyuz, N., Altman, R., Blanchard, S. C. & Boudker, O. Transport dynamics of a glutamate transporter homologue. Nature 502, 114-118 (2013).
    • (2013) Nature , vol.502 , pp. 114-118
    • Akyuz, N.1    Altman, R.2    Blanchard, S.C.3    Boudker, O.4
  • 10
    • 84885606528 scopus 로고    scopus 로고
    • Unsynchronised subunit motion in single trimeric sodium-coupled aspartate transporters
    • Erkens, G. B., Hanelt, I., Goudsmits, J. M., Slotboom, D. J. & van Oijen, A. M. Unsynchronised subunit motion in single trimeric sodium-coupled aspartate transporters. Nature 502, 119-123 (2013).
    • (2013) Nature , vol.502 , pp. 119-123
    • Erkens, G.B.1    Hanelt, I.2    Goudsmits, J.M.3    Slotboom, D.J.4    Van Oijen, A.M.5
  • 11
    • 84873571301 scopus 로고    scopus 로고
    • Conformational ensemble of the sodium-coupled aspartate transporter.Nature Struct.Mol
    • Georgieva, E. R., Borbat, P. P., Ginter, C., Freed, J. H. & Boudker, O. Conformational ensemble of the sodium-coupled aspartate transporter.Nature Struct.Mol. Biol. 20, 215-221 (2013).
    • (2013) Biol. , vol.20 , pp. 215-221
    • Georgieva, E.R.1    Borbat, P.P.2    Ginter, C.3    Freed, J.H.4    Boudker, O.5
  • 13
    • 77952402284 scopus 로고    scopus 로고
    • Single-molecule dynamics of gating in a neurotransmitter transporter homologue
    • Zhao, Y. et al. Single-molecule dynamics of gating in a neurotransmitter transporter homologue. Nature 465, 188-193 (2010).
    • (2010) Nature , vol.465 , pp. 188-193
    • Zhao, Y.1
  • 14
    • 84861090698 scopus 로고    scopus 로고
    • Structural intermediates in a model of the substrate translocation path of the bacterial glutamate transporter homologue GltPh
    • Stolzenberg, S., Khelashvili, G.& Weinstein, H. Structural intermediates in a model of the substrate translocation path of the bacterial glutamate transporter homologue GltPh. J. Phys. Chem. B 116, 5372-5383 (2012).
    • (2012) J. Phys. Chem. B , vol.116 , pp. 5372-5383
    • Stolzenberg, S.1    Khelashvili, G.2    Weinstein, H.3
  • 15
    • 77953857777 scopus 로고    scopus 로고
    • The position of an arginine residue influences substrate affinity and K1 coupling in the human glutamate transporter, EAAT1
    • Ryan, R. M., Kortt, N. C., Sirivanta, T. & Vandenberg, R. J. The position of an arginine residue influences substrate affinity and K1 coupling in the human glutamate transporter, EAAT1. J. Neurochem. 114, 565-575 (2010).
    • (2010) J. Neurochem. , vol.114 , pp. 565-575
    • Ryan, R.M.1    Kortt, N.C.2    Sirivanta, T.3    Vandenberg, R.J.4
  • 16
    • 0035798626 scopus 로고    scopus 로고
    • Coupled, but not uncoupled, fluxes in a neuronal glutamate transporter can be activated by lithium ions
    • Borre, L.&Kanner, B. I. Coupled, but not uncoupled, fluxes in a neuronal glutamate transporter can be activated by lithium ions. J. Biol. Chem. 276, 40396-40401 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 40396-40401
    • Borre, L.1    Kanner, B.I.2
  • 17
    • 84860383319 scopus 로고    scopus 로고
    • Enhanced photostability of cyanine fluorophores across the visible spectrum
    • Altman, R. B. et al. Enhanced photostability of cyanine fluorophores across the visible spectrum. Nature Methods 9, 428-429 (2012).
    • (2012) Nature Methods , vol.9 , pp. 428-429
    • Altman, R.B.1
  • 18
    • 84865066285 scopus 로고    scopus 로고
    • On the mechanisms of cyanine fluorophore photostabilization
    • Zheng, Q. et al. On the mechanisms of cyanine fluorophore photostabilization. J. Phys. Chem. Lett. 3, 2200-2203 (2012).
    • (2012) J. Phys. Chem. Lett. , vol.3 , pp. 2200-2203
    • Zheng, Q.1
  • 19
    • 84878890467 scopus 로고    scopus 로고
    • Small-molecule photostabilizing agents are modifiers of lipid bilayer properties
    • Alejo, J. L., Blanchard, S. C. & Andersen, O. S. Small-molecule photostabilizing agents are modifiers of lipid bilayer properties. Biophys. J. 104, 2410-2418 (2013).
    • (2013) Biophys. J. , vol.104 , pp. 2410-2418
    • Alejo, J.L.1    Blanchard, S.C.2    Andersen, O.S.3
  • 20
    • 77954814800 scopus 로고    scopus 로고
    • Conformational sampling of aminoacyl-tRNA during selection on the bacterial ribosome
    • Geggier, P. et al. Conformational sampling of aminoacyl-tRNA during selection on the bacterial ribosome. J. Mol. Biol. 399, 576-595 (2010).
    • (2010) J. Mol. Biol. , vol.399 , pp. 576-595
    • Geggier, P.1
  • 21
    • 24344507684 scopus 로고    scopus 로고
    • Individual subunits of the glutamate transporter EAAC1 homotrimer function independently of each other
    • Grewer, C. et al. Individual subunits of the glutamate transporter EAAC1 homotrimer function independently of each other. Biochemistry 44, 11913-11923 (2005).
    • (2005) Biochemistry , vol.44 , pp. 11913-11923
    • Grewer, C.1
  • 22
    • 34548148634 scopus 로고    scopus 로고
    • Rigidity of the subunit interfaces of the trimeric glutamate transporter GltT during translocation
    • Groeneveld, M. & Slotboom, D. J. Rigidity of the subunit interfaces of the trimeric glutamate transporter GltT during translocation. J. Mol. Biol. 372, 565-570 (2007).
    • (2007) J. Mol. Biol. , vol.372 , pp. 565-570
    • Groeneveld, M.1    Slotboom, D.J.2
  • 23
    • 85027948926 scopus 로고    scopus 로고
    • Binding thermodynamics of a glutamate transporter homolog
    • Reyes, N., Oh, S. & Boudker, O. Binding thermodynamics of a glutamate transporter homolog. Nature Struct. Mol. Biol. 20, 634-640 (2013).
    • (2013) Nature Struct. Mol. Biol. , vol.20 , pp. 634-640
    • Reyes, N.1    Oh, S.2    Boudker, O.3
  • 24
    • 0031909675 scopus 로고    scopus 로고
    • DL-threo-b-benzyloxyaspartate, a potent blocker of excitatory amino acid transporters
    • Shimamoto, K. et al. DL-threo-b-benzyloxyaspartate, a potent blocker of excitatory amino acid transporters. Mol. Pharmacol. 53, 195-201 (1998).
    • (1998) Mol. Pharmacol. , vol.53 , pp. 195-201
    • Shimamoto, K.1
  • 25
    • 84876416484 scopus 로고    scopus 로고
    • The cost of living in the membrane: A case study of hydrophobic mismatch for themulti-segment protein LeuT
    • Mondal, S., Khelashvili, G., Shi, L. & Weinstein, H. The cost of living in the membrane: a case study of hydrophobic mismatch for themulti-segment protein LeuT. Chem. Phys. Lipids 169, 27-38 (2013).
    • (2013) Chem. Phys. Lipids , vol.169 , pp. 27-38
    • Mondal, S.1    Khelashvili, G.2    Shi, L.3    Weinstein, H.4
  • 26
    • 84902007660 scopus 로고    scopus 로고
    • Not just an oil slick: Howthe energetics of protein-membrane interactions impacts the function and organization of transmembrane proteins
    • Mondal, S., Khelashvili, G.&Weinstein, H.Not just an oil slick: howthe energetics of protein-membrane interactions impacts the function and organization of transmembrane proteins. Biophys. J. 106, 2305-2316 (2014).
    • (2014) Biophys. J. , vol.106 , pp. 2305-2316
    • Mondal, S.1    Khelashvili, G.2    Weinstein, H.3
  • 27
    • 0014029736 scopus 로고
    • Simple allostericmodel formembranepumps
    • Jardetzky, O.Simple allostericmodel formembranepumps.Nature211,969-970 (1966).
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 28
    • 0014165282 scopus 로고
    • Translocations through natural membranes
    • Mitchell, P. Translocations through natural membranes. Adv. Enzymol. 29, 33-87 (1967).
    • (1967) Adv. Enzymol. , vol.29 , pp. 33-87
    • Mitchell, P.1
  • 29
    • 84885576596 scopus 로고    scopus 로고
    • A two-domain elevatormechanismfor sodium/proton antiport
    • Lee, C. et al. A two-domain elevatormechanismfor sodium/proton antiport. Nature 501, 573-577 (2013).
    • (2013) Nature , vol.501 , pp. 573-577
    • Lee, C.1
  • 30
    • 84878896166 scopus 로고    scopus 로고
    • Structural basis for substrate transport in the GLUT-homology family of monosaccharide transporters
    • Quistgaard, E. M., Low, C., Moberg, P., Tresaugues, L. & Nordlund, P. Structural basis for substrate transport in the GLUT-homology family of monosaccharide transporters. Nature Struct. Mol. Biol. 20, 766-768 (2013).
    • (2013) Nature Struct. Mol. Biol. , vol.20 , pp. 766-768
    • Quistgaard, E.M.1    Low, C.2    Moberg, P.3    Tresaugues, L.4    Nordlund, P.5
  • 31
    • 84892783318 scopus 로고    scopus 로고
    • Structural basis of the alternating-access mechanism in a bile acid transporter
    • Zhou, X. et al. Structural basis of the alternating-access mechanism in a bile acid transporter. Nature 505, 569-573 (2014).
    • (2014) Nature , vol.505 , pp. 569-573
    • Zhou, X.1
  • 32
    • 84893415732 scopus 로고    scopus 로고
    • Ultra-stable organic fluorophores for single-molecule research
    • Zheng, Q. et al. Ultra-stable organic fluorophores for single-molecule research. Chem. Soc. Rev. 43, 1044-1056 (2014).
    • (2014) Chem. Soc. Rev. , vol.43 , pp. 1044-1056
    • Zheng, Q.1
  • 33
    • 33847051154 scopus 로고    scopus 로고
    • Identification of two distinct hybrid state intermediates on the ribosome
    • Munro, J. B., Altman, R. B., O'Connor, N. & Blanchard, S. C. Identification of two distinct hybrid state intermediates on the ribosome. Mol. Cell25, 505-517(2007).
    • (2007) Mol. Cell , vol.25 , pp. 505-517
    • Munro, J.B.1    Altman, R.B.2    O'connor, N.3    Blanchard, S.C.4
  • 34
    • 66149152243 scopus 로고    scopus 로고
    • Mitigating unwanted photophysical processes for improved single-molecule fluorescence imaging
    • Dave, R., Terry, D. S., Munro, J. B. & Blanchard, S. C. Mitigating unwanted photophysical processes for improved single-molecule fluorescence imaging. Biophys. J. 96, 2371-2381 (2009).
    • (2009) Biophys. J. , vol.96 , pp. 2371-2381
    • Dave, R.1    Terry, D.S.2    Munro, J.B.3    Blanchard, S.C.4
  • 35
    • 1542285356 scopus 로고    scopus 로고
    • Restoration of single-channel currents using the segmental k-means method based on hidden Markov modeling
    • Qin, F. Restoration of single-channel currents using the segmental k-means method based on hidden Markov modeling. Biophys. J. 86, 1488-1501 (2004).
    • (2004) Biophys. J. , vol.86 , pp. 1488-1501
    • Qin, F.1
  • 36
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 37
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. , vol.D 50 , pp. 760-763
  • 38
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al.Phaser crystallographic software. J.Appl. Crystallogr.40, 658-674 (2007).
    • (2007) J.Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 39
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 40
    • 79953763877 scopus 로고    scopus 로고
    • REFMAC5 for the refinement of macromolecular crystal structures
    • Murshudov, G. N. et al. REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr. D 67, 355-367 (2011).
    • (2011) Acta Crystallogr. D , vol.67 , pp. 355-367
    • Murshudov, G.N.1
  • 42
    • 0031203438 scopus 로고    scopus 로고
    • Multifrequency two-dimensional Fourier transform ESR: An X/Ku-band spectrometer
    • Borbat, P. P., Crepeau, R. H. & Freed, J. H. Multifrequency two-dimensional Fourier transform ESR: an X/Ku-band spectrometer. J. Magn. Reson. 127, 155-167 (1997).
    • (1997) J. Magn. Reson. , vol.127 , pp. 155-167
    • Borbat, P.P.1    Crepeau, R.H.2    Freed, J.H.3
  • 43
    • 11344285129 scopus 로고    scopus 로고
    • The determination of pair distance distributions by pulsed ESR using Tikhonov regularization
    • Chiang, Y. W., Borbat, P. P. & Freed, J. H. The determination of pair distance distributions by pulsed ESR using Tikhonov regularization. J. Magn. Reson. 172, 279-295 (2005).
    • (2005) J. Magn. Reson. , vol.172 , pp. 279-295
    • Chiang, Y.W.1    Borbat, P.P.2    Freed, J.H.3
  • 44
    • 28044472953 scopus 로고    scopus 로고
    • Maximum entropy: A complement to Tikhonov regularization for determination of pair distance distributions by pulsed ESR
    • Chiang, Y. W., Borbat, P. P. & Freed, J. H. Maximum entropy: a complement to Tikhonov regularization for determination of pair distance distributions by pulsed ESR. J. Magn. Reson. 177, 184-196 (2005).
    • (2005) J. Magn. Reson. , vol.177 , pp. 184-196
    • Chiang, Y.W.1    Borbat, P.P.2    Freed, J.H.3
  • 45
    • 1642576012 scopus 로고    scopus 로고
    • Improved treatment of the protein backbone in empirical force fields
    • MacKerell, A. D. Jr, Feig, M. & Brooks, C. L. III. Improved treatment of the protein backbone in empirical force fields. J. Am. Chem. Soc. 126, 698-699 (2004).
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 698-699
    • Mackerell, A.D.1    Feig, M.2    Brooks, C.L.3
  • 46
    • 77953377650 scopus 로고    scopus 로고
    • Update of the CHARMM all-atom additive force field for lipids: Validation on six lipid types
    • Klauda, J. B. et al. Update of the CHARMM all-atom additive force field for lipids: validation on six lipid types. J. Phys. Chem. B 114, 7830-7843 (2010).
    • (2010) J. Phys. Chem. B , vol.114 , pp. 7830-7843
    • Klauda, J.B.1
  • 47
    • 27344436659 scopus 로고    scopus 로고
    • Scalable molecular dynamics with NAMD
    • Phillips, J. C. et al. Scalable molecular dynamics with NAMD. J. Comput. Chem. 26, 1781-1802 (2005).
    • (2005) J. Comput. Chem. , vol.26 , pp. 1781-1802
    • Phillips, J.C.1
  • 48
    • 79959713919 scopus 로고    scopus 로고
    • Definition and testing of the GROMOS force-field versions 54A7 and 54B7
    • Schmid, N. et al. Definition and testing of the GROMOS force-field versions 54A7 and 54B7. Eur. Biophys. J. 40, 843-856 (2011).
    • (2011) Eur. Biophys. J. , vol.40 , pp. 843-856
    • Schmid, N.1
  • 49
    • 84867820827 scopus 로고    scopus 로고
    • LAMBADA and InflateGRO2: Efficient membrane alignment and insertion of membrane proteins for molecular dynamics simulations
    • Schmidt, T. H. & Kandt, C. LAMBADA and InflateGRO2: Efficient membrane alignment and insertion of membrane proteins for molecular dynamics simulations. J. Chem. Inf. Model. 52, 2657-2669 (2012).
    • (2012) J. Chem. Inf. Model. , vol.52 , pp. 2657-2669
    • Schmidt, T.H.1    Kandt, C.2
  • 50
    • 84875592758 scopus 로고    scopus 로고
    • GROMACS 4.5: A high-throughput and highly parallel open source molecular simulation toolkit
    • Pronk, S. et al. GROMACS 4.5: a high-throughput and highly parallel open source molecular simulation toolkit. Bioinformatics 29, 845-854 (2013).
    • (2013) Bioinformatics , vol.29 , pp. 845-854
    • Pronk, S.1
  • 51
    • 47149096704 scopus 로고    scopus 로고
    • CHARMM-GUI: A web-based graphical user interface for CHARMM
    • Jo, S., Kim, T., Iyer, V. G. & Im, W. CHARMM-GUI: a web-based graphical user interface for CHARMM. J. Comput. Chem. 29, 1859-1865 (2008).
    • (2008) J. Comput. Chem. , vol.29 , pp. 1859-1865
    • Jo, S.1    Kim, T.2    Iyer, V.G.3    Im, W.4
  • 52
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott, O. & Olson, A. J. AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J. Comput. Chem. 31, 455-461 (2010).
    • (2010) J. Comput. Chem. , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 53
    • 4444221565 scopus 로고    scopus 로고
    • UCSFChimera - A visualization systemfor exploratory research and analysis
    • Pettersen, E. F. et al.UCSFChimera-a visualization systemfor exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 54
    • 84891782659 scopus 로고    scopus 로고
    • Pfam: The protein families database
    • Finn, R. D. et al. Pfam: the protein families database. Nucleic Acids Res. 42, D222-D230 (2014).
    • (2014) Nucleic Acids Res. , vol.42 , pp. D222-D230
    • Finn, R.D.1
  • 55
    • 80054078476 scopus 로고    scopus 로고
    • Fast, scalable generation of high-quality proteinmultiple sequence alignments using Clustal Omega
    • Sievers, F. et al. Fast, scalable generation of high-quality proteinmultiple sequence alignments using Clustal Omega. Mol. Syst. Biol. 7, 539 (2011).
    • (2011) Mol. Syst. Biol. , vol.7 , pp. 539
    • Sievers, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.