메뉴 건너뛰기




Volumn 96, Issue 9, 2009, Pages 3519-3528

Peptide nanopores and lipid bilayers: Interactions by coarse-grained molecular-dynamics simulations

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDE; TRYPTOPHAN; CARRIER PROTEIN; PHOSPHATIDYLCHOLINE;

EID: 67650394202     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.01.046     Document Type: Article
Times cited : (28)

References (62)
  • 1
    • 26644444070 scopus 로고    scopus 로고
    • How lipids and proteins interact in a membrane: A molecular approach
    • Lee, A. G. 2005. How lipids and proteins interact in a membrane: a molecular approach. Mol. Biosyst. 1:203-212.
    • (2005) Mol. Biosyst , vol.1 , pp. 203-212
    • Lee, A.G.1
  • 2
    • 49549083949 scopus 로고    scopus 로고
    • Membrane proteins: Molecular dynamics simulations
    • Lindahl, E., and M. S. P. Sansom. 2008. Membrane proteins: molecular dynamics simulations. Curr. Opin. Struct. Biol. 18:425-431.
    • (2008) Curr. Opin. Struct. Biol , vol.18 , pp. 425-431
    • Lindahl, E.1    Sansom, M.S.P.2
  • 3
    • 33746647787 scopus 로고    scopus 로고
    • Peptides in lipid bilayers: The power of simple models
    • Killian, J. A., and T. K. M. Nyholm. 2006. Peptides in lipid bilayers: the power of simple models. Curr. Opin. Struct. Biol. 16:473-479.
    • (2006) Curr. Opin. Struct. Biol , vol.16 , pp. 473-479
    • Killian, J.A.1    Nyholm, T.K.M.2
  • 4
    • 33646198955 scopus 로고    scopus 로고
    • Molecular dynamics simulations of model trans-membrane peptides in lipid bilayers: A systematic investigation of hydrophobic mismatch
    • Kandasamy, S. K., and R. G. Larson. 2006. Molecular dynamics simulations of model trans-membrane peptides in lipid bilayers: a systematic investigation of hydrophobic mismatch. Biophys. J. 90:2326-2343.
    • (2006) Biophys. J , vol.90 , pp. 2326-2343
    • Kandasamy, S.K.1    Larson, R.G.2
  • 5
    • 33846963172 scopus 로고    scopus 로고
    • How protein transmembrane segments sense the lipid environment
    • Nyholm, T. K. M., S. Ozdirekcan, and J. A. Killian. 2007. How protein transmembrane segments sense the lipid environment. Biochemistry. 46:1457-1465.
    • (2007) Biochemistry , vol.46 , pp. 1457-1465
    • Nyholm, T.K.M.1    Ozdirekcan, S.2    Killian, J.A.3
  • 6
    • 37049023237 scopus 로고    scopus 로고
    • On the orientation of a designed transmembrane peptide: Toward the right tilt angle?
    • Ozdirekcan, S., C. Etchebest, J. A. Killian, and P. F. J. Fuchs. 2007. On the orientation of a designed transmembrane peptide: toward the right tilt angle? J. Am. Chem. Soc. 129:15174-15181.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 15174-15181
    • Ozdirekcan, S.1    Etchebest, C.2    Killian, J.A.3    Fuchs, P.F.J.4
  • 8
    • 17844379740 scopus 로고    scopus 로고
    • Structure and dynamics of model pore insertion into a membrane
    • Lopez, C. F., S. O. Nielsen, B. Ensing, P. B. Moore, and M. L. Klein. 2005. Structure and dynamics of model pore insertion into a membrane. Biophys. J. 88:3083-3094.
    • (2005) Biophys. J , vol.88 , pp. 3083-3094
    • Lopez, C.F.1    Nielsen, S.O.2    Ensing, B.3    Moore, P.B.4    Klein, M.L.5
  • 9
    • 21244431672 scopus 로고    scopus 로고
    • Simulation studies of protein-induced bilayer deformations, and lipid-induced protein tilting, on a mesoscopic model for lipid bilayers with embedded proteins
    • Venturoli, M., B. Smit, and M. M. Sperotto. 2005. Simulation studies of protein-induced bilayer deformations, and lipid-induced protein tilting, on a mesoscopic model for lipid bilayers with embedded proteins. Biophys. J. 88:1778-1798.
    • (2005) Biophys. J , vol.88 , pp. 1778-1798
    • Venturoli, M.1    Smit, B.2    Sperotto, M.M.3
  • 10
    • 52949117747 scopus 로고    scopus 로고
    • Cluster formation of transmembrane proteins due to hydrophobic matching
    • Schmidt, U., G. Guigas, and M. Weiss. 2008. Cluster formation of transmembrane proteins due to hydrophobic matching. Phys. Rev. Lett. 101:128104.
    • (2008) Phys. Rev. Lett , vol.101 , pp. 128104
    • Schmidt, U.1    Guigas, G.2    Weiss, M.3
  • 11
    • 0035855827 scopus 로고    scopus 로고
    • Stochastic sensors inspired by biology
    • Bayley, H., and P. S. Cremer. 2001. Stochastic sensors inspired by biology. Nature. 413:226-230.
    • (2001) Nature , vol.413 , pp. 226-230
    • Bayley, H.1    Cremer, P.S.2
  • 12
    • 1642485164 scopus 로고    scopus 로고
    • Coarse grained model for semiquantitative lipid simulations
    • Marrink, S. J., A. H. de Vries, and A. E. Mark. 2004. Coarse grained model for semiquantitative lipid simulations. J. Phys. Chem. B. 108:750-760.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 750-760
    • Marrink, S.J.1    de Vries, A.H.2    Mark, A.E.3
  • 16
    • 34548146523 scopus 로고    scopus 로고
    • G protein-coupled receptors self-assemble in dynamics simulations of model bilayers
    • Periole, X., T. Huber, S. J. Marrink, and T. P. Sakmar. 2007. G protein-coupled receptors self-assemble in dynamics simulations of model bilayers. J. Am. Chem. Soc. 129:10126-10132.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 10126-10132
    • Periole, X.1    Huber, T.2    Marrink, S.J.3    Sakmar, T.P.4
  • 17
    • 0029762032 scopus 로고    scopus 로고
    • Insertion and hairpin formation of membrane proteins: A Monte Carlo study
    • Baumgärtner, A. 1996. Insertion and hairpin formation of membrane proteins: a Monte Carlo study. Biophys. J. 71:1248-1255.
    • (1996) Biophys. J , vol.71 , pp. 1248-1255
    • Baumgärtner, A.1
  • 21
    • 11044233935 scopus 로고    scopus 로고
    • Coarse-grained simulations of lipid bilayers
    • Stevens, M. J. 2004. Coarse-grained simulations of lipid bilayers. J. Chem. Phys. 121:11942-11948.
    • (2004) J. Chem. Phys , vol.121 , pp. 11942-11948
    • Stevens, M.J.1
  • 22
    • 14544291957 scopus 로고    scopus 로고
    • A multiscale coarse-graining method for biomolecular systems
    • Izvekov, S., and G. A. Voth. 2005. A multiscale coarse-graining method for biomolecular systems. J. Phys. Chem. B. 109:2469-2473.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 2469-2473
    • Izvekov, S.1    Voth, G.A.2
  • 23
    • 33748266722 scopus 로고    scopus 로고
    • Mixed atomistic and coarse-grained molecular dynamics: Simulation of a membrane bound ion channel
    • Shi, Q., S. Izvekov, and G. A. Voth. 2006. Mixed atomistic and coarse-grained molecular dynamics: simulation of a membrane bound ion channel. J. Phys. Chem. B. 110:15045-15048.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 15045-15048
    • Shi, Q.1    Izvekov, S.2    Voth, G.A.3
  • 24
    • 33644893631 scopus 로고    scopus 로고
    • Coarse grained protein-lipid model with application to lipoprotein particles
    • Shih, A. Y., A. Arkhipov, P. L. Freddolino, and K. Schulten. 2006. Coarse grained protein-lipid model with application to lipoprotein particles. J. Phys. Chem. B. 110:3674-3684.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 3674-3684
    • Shih, A.Y.1    Arkhipov, A.2    Freddolino, P.L.3    Schulten, K.4
  • 25
    • 33746453289 scopus 로고    scopus 로고
    • Coarse-grained transmembrane proteins: Hydrophobic matching, aggregation, and their effect on fusion
    • Smeijers, A. F., K. Pieterse, A. J. Markvoort, and P. A. J. Hilbers. 2006. Coarse-grained transmembrane proteins: Hydrophobic matching, aggregation, and their effect on fusion. J. Phys. Chem. B. 110:13614-13623.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 13614-13623
    • Smeijers, A.F.1    Pieterse, K.2    Markvoort, A.J.3    Hilbers, P.A.J.4
  • 26
    • 33847242278 scopus 로고    scopus 로고
    • Coarse-grained molecular dynamics simulations of membrane proteins and peptides
    • Bond, P. J., J. Holyoake, A. Ivetac, S. Khalid, and M. S. P. Sansom. 2007. Coarse-grained molecular dynamics simulations of membrane proteins and peptides. J. Struct. Biol. 157:593-605.
    • (2007) J. Struct. Biol , vol.157 , pp. 593-605
    • Bond, P.J.1    Holyoake, J.2    Ivetac, A.3    Khalid, S.4    Sansom, M.S.P.5
  • 30
    • 38549168897 scopus 로고    scopus 로고
    • Coarse-grained molecular dynamics simulations of phase transitions in mixed lipid systems containing LPA, DOPA, and DOPE lipids
    • May, E. R., D. I. Kopelevich, and A. Narang. 2008. Coarse-grained molecular dynamics simulations of phase transitions in mixed lipid systems containing LPA, DOPA, and DOPE lipids. Biophys. J. 94:878-890.
    • (2008) Biophys. J , vol.94 , pp. 878-890
    • May, E.R.1    Kopelevich, D.I.2    Narang, A.3
  • 33
    • 0031740415 scopus 로고    scopus 로고
    • Hydrophobic mismatch between proteins and lipids in membranes
    • Killian, J. A. 1998. Hydrophobic mismatch between proteins and lipids in membranes. Biochim. Biophys. Acta. 1376:401-416.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 401-416
    • Killian, J.A.1
  • 34
    • 34347262391 scopus 로고    scopus 로고
    • Bilayer thickness and membrane protein function: An energetic perspective
    • Andersen, O. S., and R. E. Koeppe. 2007. Bilayer thickness and membrane protein function: an energetic perspective. Annu. Rev. Biophys. Biomol. Struct. 36:107-130.
    • (2007) Annu. Rev. Biophys. Biomol. Struct , vol.36 , pp. 107-130
    • Andersen, O.S.1    Koeppe, R.E.2
  • 35
    • 0035942298 scopus 로고    scopus 로고
    • Sensitivity of single membrane-spanning α-helical peptides to hydrophobic mismatch with a lipid bilayer: Effects on backbone structure, orientation, and extent of membrane incorporation
    • de Planque, M. R. R., E. Goormaghtigh, D. V. Greathouse, R. E. Koeppe, J. A. W. Kruijtzer, et al. 2001. Sensitivity of single membrane-spanning α-helical peptides to hydrophobic mismatch with a lipid bilayer: effects on backbone structure, orientation, and extent of membrane incorporation. Biochemistry. 40:5000-5010.
    • (2001) Biochemistry , vol.40 , pp. 5000-5010
    • de Planque, M.R.R.1    Goormaghtigh, E.2    Greathouse, D.V.3    Koeppe, R.E.4    Kruijtzer, J.A.W.5
  • 36
    • 0033790343 scopus 로고    scopus 로고
    • Helical membrane protein folding, stability, and evolution
    • Popot, J. L., and D. M. Engelman. 2000. Helical membrane protein folding, stability, and evolution. Annu. Rev. Biochem. 69:881-922.
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 881-922
    • Popot, J.L.1    Engelman, D.M.2
  • 37
    • 22244472946 scopus 로고    scopus 로고
    • Lipid bilayer perturbations around a transmembrane nanotube: A coarse grain molecular dynamics study
    • Nielsen, S. O., B. Ensing, V. Ortiz, P. B. Moore, and M. L. Klein. 2005. Lipid bilayer perturbations around a transmembrane nanotube: a coarse grain molecular dynamics study. Biophys. J. 88:3822-3828.
    • (2005) Biophys. J , vol.88 , pp. 3822-3828
    • Nielsen, S.O.1    Ensing, B.2    Ortiz, V.3    Moore, P.B.4    Klein, M.L.5
  • 38
    • 0032919444 scopus 로고    scopus 로고
    • Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy
    • Opella, S. J., F. M. Marassi, J. J. Gesell, A. P. Valente, Y. Kim, et al. 1999. Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy. Nat. Struct. Biol. 6:374-379.
    • (1999) Nat. Struct. Biol , vol.6 , pp. 374-379
    • Opella, S.J.1    Marassi, F.M.2    Gesell, J.J.3    Valente, A.P.4    Kim, Y.5
  • 39
    • 1542365497 scopus 로고    scopus 로고
    • Effect of the pore region of a transmembrane ion channel on the physical properties of a simple membrane
    • Saiz, L., S. Bandyopadhyay, and M. L. Klein. 2004. Effect of the pore region of a transmembrane ion channel on the physical properties of a simple membrane. J. Phys. Chem. B. 108:2608-2613.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 2608-2613
    • Saiz, L.1    Bandyopadhyay, S.2    Klein, M.L.3
  • 40
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore
    • Song, L., M. R. Hobaugh, C. Shustak, S. Cheley, H. Bayley, et al. 1996. Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore. Science. 274:1859-1866.
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5
  • 41
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • Yau, W. M., W. C. Wimley, K. Gawrisch, and S. H. White. 1998. The preference of tryptophan for membrane interfaces. Biochemistry. 37:14713-14718.
    • (1998) Biochemistry , vol.37 , pp. 14713-14718
    • Yau, W.M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4
  • 42
    • 0033597858 scopus 로고    scopus 로고
    • Different membrane anchoring positions of tryptophan and lysine in synthetic transmembrane α-helical peptides
    • de Planque, M. R. R., J. A. W. Kruijtzer, R. M. J. Liskamp, D. Marsh, D. V. Greathouse, et al. 1999. Different membrane anchoring positions of tryptophan and lysine in synthetic transmembrane α-helical peptides. J. Biol. Chem. 274:20839-20846.
    • (1999) J. Biol. Chem , vol.274 , pp. 20839-20846
    • de Planque, M.R.R.1    Kruijtzer, J.A.W.2    Liskamp, R.M.J.3    Marsh, D.4    Greathouse, D.V.5
  • 43
    • 0023907575 scopus 로고
    • Synthetic amphiphilic peptide models for protein ion channels
    • Lear, J. D., Z. R. Wasserman, and W. F. DeGrado. 1988. Synthetic amphiphilic peptide models for protein ion channels. Science. 240:1177-1181.
    • (1988) Science , vol.240 , pp. 1177-1181
    • Lear, J.D.1    Wasserman, Z.R.2    DeGrado, W.F.3
  • 44
    • 0035812426 scopus 로고    scopus 로고
    • Simulation of the spontaneous aggregation of phospholipids into bilayers
    • Marrink, S. J., E. Lindahl, O. Edholm, and A. E. Mark. 2001. Simulation of the spontaneous aggregation of phospholipids into bilayers. J. Am. Chem. Soc. 123:8638-8639.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 8638-8639
    • Marrink, S.J.1    Lindahl, E.2    Edholm, O.3    Mark, A.E.4
  • 45
    • 33644644163 scopus 로고    scopus 로고
    • Insertion and assembly of membrane proteins via simulation
    • Bond, P. J., and M. S. P. Sansom. 2006. Insertion and assembly of membrane proteins via simulation. J. Am. Chem. Soc. 128:2697-2704.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 2697-2704
    • Bond, P.J.1    Sansom, M.S.P.2
  • 47
    • 33847258823 scopus 로고    scopus 로고
    • Bilayer deformation by the Kv channel voltage sensor domain revealed by self-assembly simulations
    • Bond, P. J., and M. S. P. Sansom. 2007. Bilayer deformation by the Kv channel voltage sensor domain revealed by self-assembly simulations. Proc. Natl. Acad. Sci. USA. 104:2631-2636.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2631-2636
    • Bond, P.J.1    Sansom, M.S.P.2
  • 48
    • 53249150686 scopus 로고    scopus 로고
    • Coarse-grained molecular dynamics simulations of the energetics of helix insertion into a lipid bilayer
    • Bond, P. J., C. L. Wee, and M. S. P. Sansom. 2008. Coarse-grained molecular dynamics simulations of the energetics of helix insertion into a lipid bilayer. Biochemistry. 47:11321-11331.
    • (2008) Biochemistry , vol.47 , pp. 11321-11331
    • Bond, P.J.1    Wee, C.L.2    Sansom, M.S.P.3
  • 51
    • 0000112789 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fully hydrated dipalmitoylphosphatidycholine bilayer with different macroscopic boundary conditions and parameters
    • Tieleman, D. P., and H. J. C. Berendsen. 1996. Molecular dynamics simulations of a fully hydrated dipalmitoylphosphatidycholine bilayer with different macroscopic boundary conditions and parameters. J. Chem. Phys. 105:4871-4880.
    • (1996) J. Chem. Phys , vol.105 , pp. 4871-4880
    • Tieleman, D.P.1    Berendsen, H.J.C.2
  • 52
    • 7244251137 scopus 로고    scopus 로고
    • Photo-crosslinking analysis of preferential interactions between a transmembrane peptide and matching lipids
    • Ridder, A. N., R. E. Spelbrink, J. A. Demmers, D. T. Rijkers, R. M. Liskamp, et al. 2004. Photo-crosslinking analysis of preferential interactions between a transmembrane peptide and matching lipids. Biochemistry. 43:4482-4489.
    • (2004) Biochemistry , vol.43 , pp. 4482-4489
    • Ridder, A.N.1    Spelbrink, R.E.2    Demmers, J.A.3    Rijkers, D.T.4    Liskamp, R.M.5
  • 55
    • 13944255096 scopus 로고    scopus 로고
    • Understanding the energetics of helical peptide orientation in membranes
    • Sengupta, D., L. Meinhold, D. Langosch, G. M. Ullmann, and J. C. Smith. 2005. Understanding the energetics of helical peptide orientation in membranes. Proteins. 58:913-922.
    • (2005) Proteins , vol.58 , pp. 913-922
    • Sengupta, D.1    Meinhold, L.2    Langosch, D.3    Ullmann, G.M.4    Smith, J.C.5
  • 56
    • 33646138957 scopus 로고    scopus 로고
    • Evaluating tilt angles of membrane-associated helices: Comparison of computational and NMR techniques
    • Ulmschneider, M. B., M. S. P. Sansom, and A. Di Nola. 2006. Evaluating tilt angles of membrane-associated helices: comparison of computational and NMR techniques. Biophys. J. 90:1650-1660.
    • (2006) Biophys. J , vol.90 , pp. 1650-1660
    • Ulmschneider, M.B.1    Sansom, M.S.P.2    Di Nola, A.3
  • 57
    • 0037133485 scopus 로고    scopus 로고
    • Hydrophobic matching mechanism investigated by molecular dynamics simulations
    • Petrache, H. I., D. M. Zuckerman, J. N. Sachs, J. A. Killian, R. E. Koeppe, et al. 2002. Hydrophobic matching mechanism investigated by molecular dynamics simulations. Langmuir. 18:1340-1351.
    • (2002) Langmuir , vol.18 , pp. 1340-1351
    • Petrache, H.I.1    Zuckerman, D.M.2    Sachs, J.N.3    Killian, J.A.4    Koeppe, R.E.5
  • 58
    • 49449094868 scopus 로고    scopus 로고
    • Protein-lipid interactions with Fusobacterium nucleatum major outer membrane protein FomA: Spin-label EPR and polarized infrared spectroscopy
    • Anbazhagan, V., N. Vijay, J. H. Kleinschmidt, and D. Marsh. 2008. Protein-lipid interactions with Fusobacterium nucleatum major outer membrane protein FomA: spin-label EPR and polarized infrared spectroscopy. Biochemistry. 47:8414-8423.
    • (2008) Biochemistry , vol.47 , pp. 8414-8423
    • Anbazhagan, V.1    Vijay, N.2    Kleinschmidt, J.H.3    Marsh, D.4
  • 59
    • 44949145433 scopus 로고    scopus 로고
    • Incorporation of outer membrane protein OmpG in lipid membranes: Proteinlipid interactions and β-barrel orientation
    • Anbazhagan, V., J. Qu, J. H. Kleinschmidt, and D. Marsh. 2008. Incorporation of outer membrane protein OmpG in lipid membranes: proteinlipid interactions and β-barrel orientation. Biochemistry. 47:6189-6198.
    • (2008) Biochemistry , vol.47 , pp. 6189-6198
    • Anbazhagan, V.1    Qu, J.2    Kleinschmidt, J.H.3    Marsh, D.4
  • 60
    • 0030823233 scopus 로고    scopus 로고
    • Molecular sorting of lipids by bacteriorhodopsin in dilauroylphophatidylcholine/distearoylphosphatidylcholine lipid bilayers
    • Dumas, F., M. M. Sperotto, M. C. Lebrun, J. F. Tocanne, and O. G. Mouritsen. 1997. Molecular sorting of lipids by bacteriorhodopsin in dilauroylphophatidylcholine/distearoylphosphatidylcholine lipid bilayers. Biophys. J. 73:1940-1953.
    • (1997) Biophys. J , vol.73 , pp. 1940-1953
    • Dumas, F.1    Sperotto, M.M.2    Lebrun, M.C.3    Tocanne, J.F.4    Mouritsen, O.G.5
  • 61
    • 13444295344 scopus 로고    scopus 로고
    • Transmembrane peptide-induced lipid sorting and mechanism of L-α-to-inverted phase transition using coarse-grain molecular dynamics
    • Nielsen, S. O., C. F. Lopez, I. Ivanov, P. B. Moore, J. C. Shelley, et al. 2004. Transmembrane peptide-induced lipid sorting and mechanism of L-α-to-inverted phase transition using coarse-grain molecular dynamics. Biophys. J. 87:2107-2115.
    • (2004) Biophys. J , vol.87 , pp. 2107-2115
    • Nielsen, S.O.1    Lopez, C.F.2    Ivanov, I.3    Moore, P.B.4    Shelley, J.C.5
  • 62
    • 4444343863 scopus 로고    scopus 로고
    • Lipid bilayer topology of the transmembrane α-helix of M13 major coat protein and bilayer polarity profile by site-directed fluorescence spectroscopy
    • Koehorst, R. B. M., R. B. Spruijt, F. J. Vergeldt, and M. A. Hemminga. 2004. Lipid bilayer topology of the transmembrane α-helix of M13 major coat protein and bilayer polarity profile by site-directed fluorescence spectroscopy. Biophys. J. 87:1445-1455.
    • (2004) Biophys. J , vol.87 , pp. 1445-1455
    • Koehorst, R.B.M.1    Spruijt, R.B.2    Vergeldt, F.J.3    Hemminga, M.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.