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Volumn 66, Issue 3, 2003, Pages 383-406

Simulated dynamics and biological macromolecules

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL ANALYSIS; DYNAMICS;

EID: 0037344855     PISSN: 00344885     EISSN: None     Source Type: Journal    
DOI: 10.1088/0034-4885/66/3/203     Document Type: Article
Times cited : (34)

References (136)
  • 1
    • 34548717559 scopus 로고
    • Phase transition for a hard-sphere system
    • Alder B J and Wainwright T E 1957 Phase transition for a hard-sphere system J. Chem. Phys. 27 1208-9
    • (1957) J. Chem. Phys. , vol.27 , pp. 1208-1209
    • Alder, B.J.1    Wainwright, T.E.2
  • 3
    • 0034602807 scopus 로고    scopus 로고
    • Staphylococcal protein A: Unfolding pathways, unfolded states, and differences between the B and E domains
    • Alonso D O V and Daggett V 2000 Staphylococcal protein A: unfolding pathways, unfolded states, and differences between the B and E domains Proc. Natl Acad. Sci. USA 97 133-8
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 133-138
    • Alonso, D.O.V.1    Daggett, V.2
  • 4
    • 0031965674 scopus 로고    scopus 로고
    • Molecular dynamics simulations of hydrophobic collapse of ubiquitin
    • Alonso D O V and Daggett V 1998 Molecular dynamics simulations of hydrophobic collapse of ubiquitin Protein Sci. 7 860-74
    • (1998) Protein Sci. , vol.7 , pp. 860-874
    • Alonso, D.O.V.1    Daggett, V.2
  • 5
    • 0033117763 scopus 로고    scopus 로고
    • Matching theory and experiment in protein folding
    • Alm E and Baker D 1999 Matching theory and experiment in protein folding Curr. Opin. Struct. Biol. 9 189-96
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 189-196
    • Alm, E.1    Baker, D.2
  • 7
    • 0001529625 scopus 로고    scopus 로고
    • Dynamic lattice Monte Carlo simulation of a model protein at an oil/water interface
    • Anderson R E, Pande V S and Radke C J 2000 Dynamic lattice Monte Carlo simulation of a model protein at an oil/water interface J. Chem. Phys. 112 9167-85
    • (2000) J. Chem. Phys. , vol.112 , pp. 9167-9185
    • Anderson, R.E.1    Pande, V.S.2    Radke, C.J.3
  • 8
    • 0012581991 scopus 로고    scopus 로고
    • Long range electrostatics effects on peptide folding
    • Åqvist J 1998 Long range electrostatics effects on peptide folding Febs Lett. 457 414-18
    • (1998) Febs Lett. , vol.457 , pp. 414-418
    • Åqvist, J.1
  • 9
    • 0034604105 scopus 로고    scopus 로고
    • A surprising simplicity to protein folding
    • Baker D 2000 A surprising simplicity to protein folding Nature 405 39-42
    • (2000) Nature , vol.405 , pp. 39-42
    • Baker, D.1
  • 10
    • 0001295503 scopus 로고    scopus 로고
    • Principal component analysis and long time protein dynamics
    • Balsera M A, Wriggers W, Oono Y and Schulten K 1996 Principal component analysis and long time protein dynamics J. Phys. Chem. 100 2567-72
    • (1996) J. Phys. Chem. , vol.100 , pp. 2567-2572
    • Balsera, M.A.1    Wriggers, W.2    Oono, Y.3    Schulten, K.4
  • 11
    • 3042524904 scopus 로고
    • A well-behaved electrostatic potential based method for deriving atomic charges - The resp model
    • Bayly C I, Ciepak P, Cornell W D and Kollman P A 1993 A well-behaved electrostatic potential based method for deriving atomic charges-the resp model J. Phys. Chem. 97 10269-80
    • (1993) J. Phys. Chem. , vol.97 , pp. 10269-10280
    • Bayly, C.I.1    Ciepak, P.2    Cornell, W.D.3    Kollman, P.A.4
  • 14
    • 0034127361 scopus 로고    scopus 로고
    • Collective protein dynamics in relation to function
    • Berendsen H J C and Hayward S 2000 Collective protein dynamics in relation to function Curr. Opin. Struct. Biol. 10 165-9
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 165-169
    • Berendsen, H.J.C.1    Hayward, S.2
  • 15
    • 0033066284 scopus 로고    scopus 로고
    • Interactions of alpha-helices with lipid bilayers: A review of simulation studies
    • Biggin P C and Sansom M S P 1999 Interactions of alpha-helices with lipid bilayers: a review of simulation studies Biophys. Chem. 76 161-83
    • (1999) Biophys. Chem. , vol.76 , pp. 161-183
    • Biggin, P.C.1    Sansom, M.S.P.2
  • 16
    • 0034635340 scopus 로고    scopus 로고
    • Beta-hairpin stability and folding: Molecular dynamics studies of the first beta-hairpin of tendamistat
    • Bonvin A M J J and Van Gunsteren W F 2000 Beta-hairpin stability and folding: molecular dynamics studies of the first beta-hairpin of tendamistat J. Mol. Biol. 296 255-68
    • (2000) J. Mol. Biol. , vol.296 , pp. 255-268
    • Bonvin, A.M.J.J.1    Van Gunsteren, W.F.2
  • 17
    • 0031056829 scopus 로고    scopus 로고
    • Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
    • Booth D R et al 1997 Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis Nature 385 787-93
    • (1997) Nature , vol.385 , pp. 787-793
    • Booth, D.R.1
  • 18
    • 0032053619 scopus 로고    scopus 로고
    • Simulations of protein folding and unfolding
    • Brooks C L 1998 Simulations of protein folding and unfolding Curr. Opin. Struct. Biol. 8 222-6
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 222-226
    • Brooks, C.L.1
  • 19
    • 0022068152 scopus 로고
    • Active-site dynamics in protein molecules - A stochastic boundary molecular-dynamics approach
    • Brooks C L, Brunger A and Karplus M 1985 Active-site dynamics in protein molecules-a stochastic boundary molecular-dynamics approach Biopolymers 24 843-65
    • (1985) Biopolymers , vol.24 , pp. 843-865
    • Brooks, C.L.1    Brunger, A.2    Karplus, M.3
  • 23
    • 0032790341 scopus 로고    scopus 로고
    • Early events in the folding of an amphipathic peptide: A multinanosecond molecular dynamics study
    • Chipot C, Maigret B and Pohorille A 1999 Early events in the folding of an amphipathic peptide: a multinanosecond molecular dynamics study Proteins 36 383-99
    • (1999) Proteins , vol.36 , pp. 383-399
    • Chipot, C.1    Maigret, B.2    Pohorille, A.3
  • 24
    • 0032567163 scopus 로고    scopus 로고
    • Folding and translocation of the undecamer of poly-L-leucine cross the water-hexane interface. A molecular dynamics study
    • Chipot C and Pohorille A 1998 Folding and translocation of the undecamer of poly-L-leucine cross the water-hexane interface. A molecular dynamics study J. Am. Chem. Soc. 120 11912-24
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11912-11924
    • Chipot, C.1    Pohorille, A.2
  • 25
    • 84988098098 scopus 로고
    • Atomic charges derived from electrostatic potential: A detailed study
    • Chirlian L E and Francl M M 1987 Atomic charges derived from electrostatic potential: a detailed study J. Comp. Chem. 8 217-27
    • (1987) J. Comp. Chem. , vol.8 , pp. 217-227
    • Chirlian, L.E.1    Francl, M.M.2
  • 26
    • 0033612756 scopus 로고    scopus 로고
    • Stability and activity of mesophilic subtilisin E and its thermophilic homolog: Insights from molecular dynamics simulations
    • Colombo G and Merz K M 1999 Stability and activity of mesophilic subtilisin E and its thermophilic homolog: insights from molecular dynamics simulations J. Am. Chem. Soc. 121 6895-903
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 6895-6903
    • Colombo, G.1    Merz, K.M.2
  • 27
    • 84986513563 scopus 로고
    • Representation of the molecular electrostatic potential by a new atomic charge model
    • Cox S R and Williams D E 1981 Representation of the molecular electrostatic potential by a new atomic charge model J. Comp. Chem. 2 304-23
    • (1981) J. Comp. Chem. , vol.2 , pp. 223-304
    • Cox, S.R.1    Williams, D.E.2
  • 28
    • 0012571591 scopus 로고
    • Molecular-dynamics simulations of peptides
    • 90-comp
    • Daggett V 1995 Molecular-dynamics simulations of peptides Abstr. Pap. Am. Chem. Soc. 209 90-comp Part 1
    • (1995) Abstr. Pap. Am. Chem. Soc. , vol.209 , Issue.PART 1
    • Daggett, V.1
  • 29
  • 30
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N-log(N) method for Ewald sums in large systems
    • Darden T. York D and Pedersen L 1993 Particle mesh Ewald: an N-log(N) method for Ewald sums in large systems J. Chem. Phys. 98 10089-92
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 31
    • 0033557181 scopus 로고    scopus 로고
    • Folding-unfolding thermo-dynamics of a beta-heptapeptide from equilibrium simulations
    • Daura X, Van Gunsteren W F and Mark A E 1999 Folding-unfolding thermo-dynamics of a beta-heptapeptide from equilibrium simulations Proteins 34 269-80
    • (1999) Proteins , vol.34 , pp. 269-280
    • Daura, X.1    Van Gunsteren, W.F.2    Mark, A.E.3
  • 32
    • 0030627746 scopus 로고    scopus 로고
    • Dynamics of a type Vi reverse turn in a linear peptide in aqueous solution
    • Demchuk E, Bashford D and Case D A 1997 Dynamics of a type Vi reverse turn in a linear peptide in aqueous solution Folding Des. 2 35-46
    • (1997) Folding Des. , vol.2 , pp. 35-46
    • Demchuk, E.1    Bashford, D.2    Case, D.A.3
  • 33
    • 0344609869 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the hyperthermophilic protein Sac7d from Sulfolobus acidocaldarius: Contribution of salt bridges to thermostability
    • De Bakker P I W, Hunenberger P H and McCammon J A 1999 Molecular dynamics simulations of the hyperthermophilic protein Sac7d from Sulfolobus acidocaldarius: contribution of salt bridges to thermostability J. Mol. Biol. 285 1811-30
    • (1999) J. Mol. Biol. , vol.285 , pp. 1811-1830
    • De Bakker, P.I.W.1    Hunenberger, P.H.2    McCammon, J.A.3
  • 34
    • 0033578828 scopus 로고    scopus 로고
    • Is protein folding the reverse of protein unfolding: A lattice simulation analysis
    • Dinner A R and Karplus M 1999 Is protein folding the reverse of protein unfolding: a lattice simulation analysis J. Mol. Biol. 292 403-19
    • (1999) J. Mol. Biol. , vol.292 , pp. 403-419
    • Dinner, A.R.1    Karplus, M.2
  • 36
    • 0001120455 scopus 로고    scopus 로고
    • Molecular modelling of human Dt-diaphorase for enzyme-directed bioreductive drug design
    • Doughty S and Phillips R 2000 Molecular modelling of human Dt-diaphorase for enzyme-directed bioreductive drug design Mol. Simul. 24 209
    • (2000) Mol. Simul. , vol.24 , pp. 209
    • Doughty, S.1    Phillips, R.2
  • 37
    • 0032561237 scopus 로고    scopus 로고
    • Pathways to a protein folding intermediate observed in A 1-microsecond simulation in aqueous solution
    • Duan Y and Kollman P A 1998 Pathways to a protein folding intermediate observed in A 1-microsecond simulation in aqueous solution Science 282 740-4
    • (1998) Science , vol.282 , pp. 740-744
    • Duan, Y.1    Kollman, P.A.2
  • 38
    • 0032544002 scopus 로고    scopus 로고
    • The early stage of folding of villin headpiece subdomain observed in a 200-nanosecond solvated molecular dynamics simulation
    • Duan Y, Wang L and Kollman P A 1998 The early stage of folding of villin headpiece subdomain observed in a 200-nanosecond solvated molecular dynamics simulation Proc. Natl Acad. Sci. USA 95 9897-902
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 9897-9902
    • Duan, Y.1    Wang, L.2    Kollman, P.A.3
  • 42
    • 84977266737 scopus 로고
    • Due berechnung optischer und electrostatischer gitterpotentiale
    • Ewald P P 1921 Due berechnung optischer und electrostatischer gitterpotentiale Ann. Phys. 64 253-87
    • (1921) Ann. Phys. , vol.64 , pp. 253-287
    • Ewald, P.P.1
  • 43
    • 0033758069 scopus 로고    scopus 로고
    • Molecular dynamics simulations of lipid bilayers
    • Feller S E 2000 Molecular dynamics simulations of lipid bilayers Curr. Opin. Colloid Interface Sci. 5 217-23
    • (2000) Curr. Opin. Colloid Interface Sci. , vol.5 , pp. 217-223
    • Feller, S.E.1
  • 44
    • 0034718553 scopus 로고    scopus 로고
    • Folding simulations of a three-stranded antiparallel beta-sheet peptide
    • Ferrara P and Caflisch A 2000 Folding simulations of a three-stranded antiparallel beta-sheet peptide Proc. Natl Acad. Sci. USA 97 10780-5
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 10780-10785
    • Ferrara, P.1    Caflisch, A.2
  • 45
    • 0001767031 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of folding of two model peptides investigated by molecular dynamics simulations
    • Ferrara P, Apostolakis J and Caflisch A 2000a Thermodynamics and kinetics of folding of two model peptides investigated by molecular dynamics simulations J. Phys. Chem. 104 5000-10
    • (2000) J. Phys. Chem. , vol.104 , pp. 5000-50010
    • Ferrara, P.1    Apostolakis, J.2    Caflisch, A.3
  • 46
    • 0001744683 scopus 로고    scopus 로고
    • Targeted molecular dynamics simulations of protein unfolding
    • Ferrara P, Apostolakis J and Caflisch A 2000b Targeted molecular dynamics simulations of protein unfolding J. Phys. Chem. 104 4511-18
    • (2000) J. Phys. Chem. , vol.104 , pp. 4511-4518
    • Ferrara, P.1    Apostolakis, J.2    Caflisch, A.3
  • 48
    • 0033576252 scopus 로고    scopus 로고
    • Solution structure and dynamics of a complex between DNA and the antitumor bisnaphthalimide Lu-79553: Intercalated ring flipping on the millisecond time scale
    • Gallego J and Reid B 1999 Solution structure and dynamics of a complex between DNA and the antitumor bisnaphthalimide Lu-79553: intercalated ring flipping on the millisecond time scale Biochemistry 38 15104-15
    • (1999) Biochemistry , vol.38 , pp. 15104-15115
    • Gallego, J.1    Reid, B.2
  • 50
    • 0034308141 scopus 로고    scopus 로고
    • Unfolding of hen egg lysozyme by molecular dynamics simulations at 300 K: Insight into the role of the interdomain interface
    • Gilquin B, Guilbert C and Perahia D 2000 Unfolding of hen egg lysozyme by molecular dynamics simulations at 300 K: insight into the role of the interdomain interface Proteins: Struct. Function Genetics 41 58-74
    • (2000) Proteins: Struct. Function Genetics , vol.41 , pp. 58-74
    • Gilquin, B.1    Guilbert, C.2    Perahia, D.3
  • 51
    • 0034327255 scopus 로고    scopus 로고
    • Dynamic simulation of the mouse prion protein
    • Guilbert C, Ricard F and Smith J 2000 Dynamic simulation of the mouse prion protein Biopolymers 54 406-15
    • (2000) Biopolymers , vol.54 , pp. 406-415
    • Guilbert, C.1    Ricard, F.2    Smith, J.3
  • 52
    • 84946447903 scopus 로고
    • Investigation of the chemical-potential by molecular-dynamics simulation
    • Guillot B and Guissani Y 1985 Investigation of the chemical-potential by molecular-dynamics simulation Mol. Phys. 54 455-65
    • (1985) Mol. Phys. , vol.54 , pp. 455-465
    • Guillot, B.1    Guissani, Y.2
  • 53
    • 0029964867 scopus 로고    scopus 로고
    • Diffusion-limited contact formation in unfolded cytochrome C: Estimating the maximum rate of protein folding
    • Hagen S J, Hofrichter J, Szabo A and Eaton W A 1996 Diffusion-limited contact formation in unfolded cytochrome C: estimating the maximum rate of protein folding Proc. Natl Acad. Sci. USA 93 11615-17
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 11615-11617
    • Hagen, S.J.1    Hofrichter, J.2    Szabo, A.3    Eaton, W.A.4
  • 55
    • 0000081668 scopus 로고
    • Collective variable description of native protein dynamics
    • Hayward S and Go N 1995 Collective variable description of native protein dynamics Ann. Rev. Phys. Chem. 46 223-50
    • (1995) Ann. Rev. Phys. Chem. , vol.46 , pp. 223-250
    • Hayward, S.1    Go, N.2
  • 56
    • 0028877423 scopus 로고
    • Harmonicity and anharmonicity in protein dynamics: A normal mode analysis and principal components analysis
    • Hayward S, Kitao A and Go N 1995 Harmonicity and anharmonicity in protein dynamics: a normal mode analysis and principal components analysis Proteins: Struct. Function Genetics 23 177-86
    • (1995) Proteins: Struct. Function Genetics , vol.23 , pp. 177-186
    • Hayward, S.1    Kitao, A.2    Go, N.3
  • 57
    • 0001720011 scopus 로고    scopus 로고
    • Molecular dynamics of folding of secondary structures in Go-type models of proteins
    • Hoang T X and Cieplak M 2000 Molecular dynamics of folding of secondary structures in Go-type models of proteins J. Chem. Phys. 112 6851-62
    • (2000) J. Chem. Phys. , vol.112 , pp. 6851-6862
    • Hoang, T.X.1    Cieplak, M.2
  • 58
    • 0000432120 scopus 로고
    • The potential calculation and some applications
    • Hockney R W 1970 The potential calculation and some applications Methods Comput. Phys. 9 136-211
    • (1970) Methods Comput. Phys. , vol.9 , pp. 136-211
    • Hockney, R.W.1
  • 59
    • 0025753631 scopus 로고
    • Projection of Monte-Carlo and molecular-dynamics trajectories onto the normal mode axes - Human lysozyme
    • Horiuchi T and Go N 1991 Projection of Monte-Carlo and molecular-dynamics trajectories onto the normal mode axes-human lysozyme Proteins: Struct. Function Genetics 10 106-16
    • (1991) Proteins: Struct. Function Genetics , vol.10 , pp. 106-116
    • Horiuchi, T.1    Go, N.2
  • 60
    • 0028926875 scopus 로고
    • Computational approaches to study protein unfolding: Hen egg white lysozyme as a case study
    • Hunenberger P H, Mark A E and Van Gunsteren W F 1995 Computational approaches to study protein unfolding: hen egg white lysozyme as a case study Proteins 21 196-213
    • (1995) Proteins , vol.21 , pp. 196-213
    • Hunenberger, P.H.1    Mark, A.E.2    Van Gunsteren, W.F.3
  • 61
    • 0031815749 scopus 로고    scopus 로고
    • Review: How do small single-domain proteins fold?
    • Jackson S 1998 Review: how do small single-domain proteins fold? Folding Des. 3 R81-91
    • (1998) Folding Des. , vol.3
    • Jackson, S.1
  • 62
    • 84986473952 scopus 로고
    • Harmonic-analysis of large systems. 3. Comparison with molecular-dynamics
    • Janezic D, Venable R M and Brooks B R 1995 Harmonic-analysis of large systems. 3, Comparison with molecular-dynamics J. Comput. Chem. 16 1554-66
    • (1995) J. Comput. Chem. , vol.16 , pp. 1554-1566
    • Janezic, D.1    Venable, R.M.2    Brooks, B.R.3
  • 65
    • 0028327236 scopus 로고
    • Protein folding dynamics: The diffusion-collision model and experimental data
    • Karplus M and Weaver D L 1994 Protein folding dynamics: the diffusion-collision model and experimental data Protein Sci. 3 650-68
    • (1994) Protein Sci. , vol.3 , pp. 650-668
    • Karplus, M.1    Weaver, D.L.2
  • 66
    • 2342668583 scopus 로고    scopus 로고
    • Essential dynamics/factor analysis for the interpretation of molecular dynamics trajectories
    • Kazmierkiewicz R, Czaplewski C, Lammek B and Ciarkowski J 1999 Essential dynamics/factor analysis for the interpretation of molecular dynamics trajectories J. Comput. Aid. Mol. Des. 13 21-33
    • (1999) J. Comput. Aid. Mol. Des. , vol.13 , pp. 21-33
    • Kazmierkiewicz, R.1    Czaplewski, C.2    Lammek, B.3    Ciarkowski, J.4
  • 67
    • 0032484148 scopus 로고    scopus 로고
    • Non-native interactions in protein folding intermediates: Molecular dynamics simulations of hen lysozyme
    • Kazmirski S L and Daggett V 1998 Non-native interactions in protein folding intermediates: molecular dynamics simulations of hen lysozyme J. Mol. Biol. 284 793-806
    • (1998) J. Mol. Biol. , vol.284 , pp. 793-806
    • Kazmirski, S.L.1    Daggett, V.2
  • 68
    • 0033516512 scopus 로고    scopus 로고
    • Analysis methods for comparison of multiple molecular dynamics trajectories: Applications to protein unfolding pathways and denatured ensembles
    • Kazmirski S L, Li A and Daggett V 1999 Analysis methods for comparison of multiple molecular dynamics trajectories: applications to protein unfolding pathways and denatured ensembles J. Mol. Biol. 290 283-304
    • (1999) J. Mol. Biol. , vol.290 , pp. 283-304
    • Kazmirski, S.L.1    Li, A.2    Daggett, V.3
  • 69
    • 0033117937 scopus 로고    scopus 로고
    • Investigating protein dynamics in collective coordinate space
    • Kitao A and Go N 1999 Investigating protein dynamics in collective coordinate space Curr. Opin. Struct. Biol. 9 164-9
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 164-169
    • Kitao, A.1    Go, N.2
  • 70
    • 0032374086 scopus 로고    scopus 로고
    • Energy landscape of a native protein: Jumping-among-minima model Proteins: Struct
    • Kitao A, Hayward S and Go N 1998 Energy landscape of a native protein: jumping-among-minima model Proteins: Struct. Function Genetics 33 496-517
    • (1998) Function Genetics , vol.33 , pp. 496-517
    • Kitao, A.1    Hayward, S.2    Go, N.3
  • 71
    • 0028203492 scopus 로고
    • Monte Carlo simulation of protein folding. Lattice model and interaction scheme
    • Kolinski A and Skolnick J 1995 Monte Carlo simulation of protein folding. Lattice model and interaction scheme Proteins 18 338-52
    • (1995) Proteins , vol.18 , pp. 338-352
    • Kolinski, A.1    Skolnick, J.2
  • 72
    • 0032907372 scopus 로고    scopus 로고
    • Long-time dynamics of met-enkephalin: Comparison of theory with Brownian dynamics simulations
    • Freed
    • Kostov K and Freed 1999 Long-time dynamics of met-enkephalin: comparison of theory with Brownian dynamics simulations Biophys. J. 76 149-63
    • (1999) Biophys. J. , vol.76 , pp. 149-163
    • Kostov, K.1
  • 73
    • 0000011122 scopus 로고    scopus 로고
    • Mechanism of the unfolding of transmembrane alpha-helical segment (1-36)-bacteriorhodopsin studied by molecular dynamics simulations
    • Korzhnev D M, Orekhov V Y, Arseniev A S, Gratias R and Kessler H 1999 Mechanism of the unfolding of transmembrane alpha-helical segment (1-36)-bacteriorhodopsin studied by molecular dynamics simulations J. Phys. Chem. 103 7036-43
    • (1999) J. Phys. Chem. , vol.103 , pp. 7036-7043
    • Korzhnev, D.M.1    Orekhov, V.Y.2    Arseniev, A.S.3    Gratias, R.4    Kessler, H.5
  • 75
    • 0034716751 scopus 로고    scopus 로고
    • A ligand that is predicted to bind better to avidin than biotin: Insights from computational fluorine scanning
    • Kuhn B and Kollman P 2000 A ligand that is predicted to bind better to avidin than biotin: insights from computational fluorine scanning J. Am. Chem. Soc. 122 3909-16
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 3909-3916
    • Kuhn, B.1    Kollman, P.2
  • 76
    • 0033219497 scopus 로고    scopus 로고
    • Structure based prediction of binding affinity of human immunodeficiency virus-I protease inhibitors
    • Kulkarni S and Kulkarni V 1999 Structure based prediction of binding affinity of human immunodeficiency virus-I protease inhibitors J. Chem. Inform. Comput. Sci. 39 1128-40
    • (1999) J. Chem. Inform. Comput. Sci. , vol.39 , pp. 1128-1140
    • Kulkarni, S.1    Kulkarni, V.2
  • 77
    • 0033996292 scopus 로고    scopus 로고
    • Structure and dynamics of the pore-lining helix of the nicotinic receptor: Md simulations in water, lipid bilayers, and transbilayer bundles
    • Law R J, Forrest L R, Ranatunga K M, La Rocca P, Tieleman D and Sansom M S P 2000 Structure and dynamics of the pore-lining helix of the nicotinic receptor: Md simulations in water, lipid bilayers, and transbilayer bundles Proteins: Struct. Function Genetics 39 47-55
    • (2000) Proteins: Struct. Function Genetics , vol.39 , pp. 47-55
    • Law, R.J.1    Forrest, L.R.2    Ranatunga, K.M.3    La Rocca, P.4    Tieleman, D.5    Sansom, M.S.P.6
  • 79
    • 0034630957 scopus 로고    scopus 로고
    • Theoretical studies suggest a new antifolate as a more potent inhibitor of thymidylate synthase
    • Lee T and Kollman P 2000 Theoretical studies suggest a new antifolate as a more potent inhibitor of thymidylate synthase J. Am. Chem. Soc. 122 4385-93
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 4385-4393
    • Lee, T.1    Kollman, P.2
  • 80
    • 36549099780 scopus 로고
    • The structure of liquid water at an extended hydrophobic surface
    • Lee C Y, Mccammon J A and Rossky P J 1984 The structure of liquid water at an extended hydrophobic surface J. Chem. Phys. 80 4448-55
    • (1984) J. Chem. Phys. , vol.80 , pp. 4448-4455
    • Lee, C.Y.1    Mccammon, J.A.2    Rossky, P.J.3
  • 81
    • 0021104775 scopus 로고
    • Molecular-dynamics of native protein. 1. Computer-simulation of trajectories
    • Levitt M 1983 Molecular-dynamics of native protein. 1. Computer-simulation of trajectories J. Mol. Biol. 168 595-620
    • (1983) J. Mol. Biol. , vol.168 , pp. 595-620
    • Levitt, M.1
  • 82
    • 0024094768 scopus 로고
    • Accurate simulation of protein dynamics in solution
    • Levitt M and Sharon R 1988 Accurate simulation of protein dynamics in solution Proc. Natl Acad. Sci. USA 85 7557-61
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 7557-7561
    • Levitt, M.1    Sharon, R.2
  • 83
    • 0016610491 scopus 로고
    • Computer simulation of protein folding
    • Levitt M and Warshel A 1975 Computer simulation of protein folding Nature 253 694-8
    • (1975) Nature , vol.253 , pp. 694-698
    • Levitt, M.1    Warshel, A.2
  • 84
    • 0034607413 scopus 로고    scopus 로고
    • Similarities in the Hiv-1 and Asv integrase active sites upon metal cofactor binding
    • Lins R D, Straatsma T P and Briggs J M 2000 Similarities in the Hiv-1 and Asv integrase active sites upon metal cofactor binding Biopolymers 53 308-15
    • (2000) Biopolymers , vol.53 , pp. 308-315
    • Lins, R.D.1    Straatsma, T.P.2    Briggs, J.M.3
  • 85
    • 33646768692 scopus 로고
    • Zur theori und systematik der molekularkräfte
    • London F 1930 Zur theori und systematik der molekularkräfte Zeitschrift Für Physik 63 245-79
    • (1930) Zeitschrift Für Physik , vol.63 , pp. 245-279
    • London, F.1
  • 86
    • 0033917135 scopus 로고    scopus 로고
    • The key event in force-induced unfolding of titin's immunoglobulin domains
    • Lu H and Schulten K 2000 The key event in force-induced unfolding of titin's immunoglobulin domains Biophys. J. 79 51-65
    • (2000) Biophys. J. , vol.79 , pp. 51-65
    • Lu, H.1    Schulten, K.2
  • 87
    • 0000625873 scopus 로고
    • On tests and measures of groups divergence I
    • Mahalanobis P C 1930 On tests and measures of groups divergence I J. Asiatic Soc. Benagal 26 541
    • (1930) J. Asiatic Soc. Benagal , vol.26 , pp. 541
    • Mahalanobis, P.C.1
  • 88
    • 0000011119 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the charge-induced unfolding and refolding of unsolvated cytochrome C
    • Mao Y, Ratner M and Jarrold M 1999 Molecular dynamics simulations of the charge-induced unfolding and refolding of unsolvated cytochrome C J. Phys. Chem. 103 10017-21
    • (1999) J. Phys. Chem. , vol.103 , pp. 10017-100021
    • Mao, Y.1    Ratner, M.2    Jarrold, M.3
  • 89
    • 0032553333 scopus 로고    scopus 로고
    • Refolding of potato carboxypeptidase inhibitor by molecular dynamics simulations with disulfide bond constraints
    • Marti-Renom N, Stote R, Querol E, Aviles F and Karplus M 1998 Refolding of potato carboxypeptidase inhibitor by molecular dynamics simulations with disulfide bond constraints J. Mol. Biol. 284 145-72
    • (1998) J. Mol. Biol. , vol.284 , pp. 145-172
    • Marti-Renom, N.1    Stote, R.2    Querol, E.3    Aviles, F.4    Karplus, M.5
  • 90
    • 0012608253 scopus 로고
    • Molecular dynamics study of the bovine pancreatic trypsin inhibitor
    • ed H J C Berendsen (France: Orsay)
    • McCammon J A 1976 Molecular dynamics study of the bovine pancreatic trypsin inhibitor Models for Protein Dynamics ed H J C Berendsen (France: Orsay) p 137
    • (1976) Models for Protein Dynamics , pp. 137
    • McCammon, J.A.1
  • 92
    • 0000011126 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the cyclic decapeptide antibiotic, gramicidin S, in dimethyl sulfoxide solution
    • Mihailescu D and Smith J C 1999 Molecular dynamics simulation of the cyclic decapeptide antibiotic, gramicidin S, in dimethyl sulfoxide solution J. Phys. Chem. B 103 1586-94
    • (1999) J. Phys. Chem. B , vol.103 , pp. 1586-1594
    • Mihailescu, D.1    Smith, J.C.2
  • 93
    • 0032540881 scopus 로고    scopus 로고
    • Simulation of the Hiv-1 Vpu transmembrane domain as a pentameric bundle
    • Moore P B, Zhong Q F, Husslein T and Klein M 1998 Simulation of the Hiv-1 Vpu transmembrane domain as a pentameric bundle Febs Lett. 431 143-8
    • (1998) Febs Lett. , vol.431 , pp. 143-148
    • Moore, P.B.1    Zhong, Q.F.2    Husslein, T.3    Klein, M.4
  • 94
    • 0012524713 scopus 로고    scopus 로고
    • Simulations of human lysozyme: Conformations triggering amyloidosis in 156T mutant
    • at press
    • Moraitakis G and Goodfellow J M 2003 Simulations of human lysozyme: conformations triggering amyloidosis in 156T mutant Biophys. J. at press
    • (2003) Biophys. J.
    • Moraitakis, G.1    Goodfellow, J.M.2
  • 96
    • 0033716690 scopus 로고    scopus 로고
    • Molecular dynamics study of structure and gating of low molecular weight ion channels
    • Newns D, Zhong Q, Moore P, Husslein T, Pattnaik P and Klein M 2000 Molecular dynamics study of structure and gating of low molecular weight ion channels Parallel Comput. 26 965-76
    • (2000) Parallel Comput. , vol.26 , pp. 965-976
    • Newns, D.1    Zhong, Q.2    Moore, P.3    Husslein, T.4    Pattnaik, P.5    Klein, M.6
  • 98
    • 0034026757 scopus 로고    scopus 로고
    • Molecular dynamics simulations of protein-tyrosine phosphatase 1b. Ii. Substrate-enzyme interactions and dynamics
    • Peters G H, Frimurer T M, Andersen J N and Olsen O 2000 Molecular dynamics simulations of protein-tyrosine phosphatase 1b. Ii. Substrate-enzyme interactions and dynamics Biophys. J. 78 2191-200
    • (2000) Biophys. J. , vol.78 , pp. 2191-2200
    • Peters, G.H.1    Frimurer, T.M.2    Andersen, J.N.3    Olsen, O.4
  • 100
    • 0001155770 scopus 로고    scopus 로고
    • Simulation of the highly stable protein: Bovine gamma B-crystallin at room and high temperature
    • Purkiss A G, Slingsby C and Goodfellow J M 2000 Simulation of the highly stable protein: bovine gamma B-crystallin at room and high temperature Protein Pept. Lett. 7 211-17
    • (2000) Protein Pept. Lett. , vol.7 , pp. 211-217
    • Purkiss, A.G.1    Slingsby, C.2    Goodfellow, J.M.3
  • 102
    • 0032516049 scopus 로고    scopus 로고
    • Brownian dynamics simulations of protein folding: Access to milliseconds time scale and beyond
    • Rojnuckarin A, Kim S and Subramaniam S 1998 Brownian dynamics simulations of protein folding: access to milliseconds time scale and beyond Proc. Natl Acad. Sci. USA 95 4288-92
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 4288-4292
    • Rojnuckarin, A.1    Kim, S.2    Subramaniam, S.3
  • 103
    • 33646940952 scopus 로고
    • Numerical-integration of Cartesian equations of motion of a system with constraints-molecular-dynamics of N-alkanes
    • Ryckaert J P, Ciccotti G and Berendsen H J C 1977 Numerical-integration of Cartesian equations of motion of a system with constraints-molecular-dynamics of N-alkanes J. Comput. Phys. 23 327-41
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 104
    • 0034624666 scopus 로고    scopus 로고
    • Potassium channels: Watching a voltage-sensor tilt and twist
    • Sansom M S P 2000 Potassium channels: watching a voltage-sensor tilt and twist Curr. Biol. 10 R206-9
    • (2000) Curr. Biol. , vol.10
    • Sansom, M.S.P.1
  • 105
    • 0031059496 scopus 로고    scopus 로고
    • Theoretical studies of protein-folding thermodynamics and kinetics
    • Shakhnovich E I 1997 Theoretical studies of protein-folding thermodynamics and kinetics Curr. Opin. Struct. Biol. 7 29-40
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 29-40
    • Shakhnovich, E.I.1
  • 107
    • 0033786003 scopus 로고    scopus 로고
    • Differential modes of agonist binding to 5-hydroxytryptamine(2a) serotonin receptors revealed by mutation and molecular modeling of conserved residues in transmembrane region 5
    • Shapiro D, Kristiansen K, Kroeze W and Roth B 2000 Differential modes of agonist binding to 5-hydroxytryptamine(2a) serotonin receptors revealed by mutation and molecular modeling of conserved residues in transmembrane region 5 Mol. Pharmacol. 58 877-86
    • (2000) Mol. Pharmacol. , vol.58 , pp. 877-886
    • Shapiro, D.1    Kristiansen, K.2    Kroeze, W.3    Roth, B.4
  • 108
    • 0032539561 scopus 로고    scopus 로고
    • Molecular picture of folding of a small alpha/beta protein
    • Sheinerman F B and Brooks C L 1998 Molecular picture of folding of a small alpha/beta protein Proc. Natl Acad. Sci. USA 95 1562-7
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 1562-1567
    • Sheinerman, F.B.1    Brooks, C.L.2
  • 109
    • 0034036372 scopus 로고    scopus 로고
    • Simulations of ion permeation through a potassium channel: Molecular dynamics of Kesa in a phospholipid bilayers
    • Shrivastava I and Sansom M 2000 Simulations of ion permeation through a potassium channel: molecular dynamics of Kesa in a phospholipid bilayers Biophys. J. 78 557-70
    • (2000) Biophys. J. , vol.78 , pp. 557-570
    • Shrivastava, I.1    Sansom, M.2
  • 110
    • 84986468608 scopus 로고
    • An approach to computing electrostatic charges for molecules
    • Singh U C and Kollman P A 1984 An approach to computing electrostatic charges for molecules J. Comp. Chem. 5 129-45
    • (1984) J. Comp. Chem. , vol.5 , pp. 129-145
    • Singh, U.C.1    Kollman, P.A.2
  • 111
    • 0033951896 scopus 로고    scopus 로고
    • Simulation studies on bacteriorhodopsin alpha-helices
    • Son H and Sansom M 2000 Simulation studies on bacteriorhodopsin alpha-helices Eur. Biophys. J. Biophys. Lett. 28 674-82
    • (2000) Eur. Biophys. J. Biophys. Lett. , vol.28 , pp. 674-682
    • Son, H.1    Sansom, M.2
  • 112
    • 0033214379 scopus 로고    scopus 로고
    • Molecular dynamics simulations of human glutathione transferase P1-1: Conformational fluctuations of the apo-structure
    • Stella L, Di Iorio E, Nicotra M and Ricci G 1999 Molecular dynamics simulations of human glutathione transferase P1-1: conformational fluctuations of the apo-structure Proteins: Struct. Function Genetics 37 10-19
    • (1999) Proteins: Struct. Function Genetics , vol.37 , pp. 10-19
    • Stella, L.1    Di Iorio, E.2    Nicotra, M.3    Ricci, G.4
  • 113
    • 0031778441 scopus 로고    scopus 로고
    • Computational analysis of thermal stability: Effect of Ile → val mutations in human lysozyme
    • Sugita Y, Kitao A and Go N 1998 Computational analysis of thermal stability: effect of Ile → val mutations in human lysozyme Folding Des. 3 173-81
    • (1998) Folding Des. , vol.3 , pp. 173-181
    • Sugita, Y.1    Kitao, A.2    Go, N.3
  • 114
    • 0030006074 scopus 로고    scopus 로고
    • Molecular dynamics simulations of synthetic peptide folding
    • Sung S S and Wu X W 1996 Molecular dynamics simulations of synthetic peptide folding Proteins: Struct. Function Genetics 25 202-14
    • (1996) Proteins: Struct. Function Genetics , vol.25 , pp. 202-214
    • Sung, S.S.1    Wu, X.W.2
  • 115
    • 0343416136 scopus 로고    scopus 로고
    • Molecular dynamics simulation of metallothionein-drug complexes
    • Szilagyi Z and Fenselau C 2000 Molecular dynamics simulation of metallothionein-drug complexes Drug Metab. Disposition 28 174-9
    • (2000) Drug Metab. Disposition , vol.28 , pp. 174-179
    • Szilagyi, Z.1    Fenselau, C.2
  • 116
    • 0033518605 scopus 로고    scopus 로고
    • Molecular dynamics of A 15-residue poly(L-alanine) in water: Helix formation and energetics
    • Takano M, Yamato T, Higo J, Suyama A and Nagayama K 1999 Molecular dynamics of A 15-residue poly(L-alanine) in water: helix formation and energetics J. Am. Chem. Soc. 121 605-12
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 605-612
    • Takano, M.1    Yamato, T.2    Higo, J.3    Suyama, A.4    Nagayama, K.5
  • 117
    • 0016696599 scopus 로고
    • Studies on protein folding, unfolding and fluctuations Y computer simulation. I. The effect of specific amino acid sequence represented by specific inter-unit interactions
    • Taketomi J, Ueda Y and Go N 1975 Studies on protein folding, unfolding and fluctuations Y computer simulation. I. The effect of specific amino acid sequence represented by specific inter-unit interactions Int. J. Pept. Protein Res. 7 445-59
    • (1975) Int. J. Pept. Protein Res. , vol.7 , pp. 445-459
    • Taketomi, J.1    Ueda, Y.2    Go, N.3
  • 118
    • 0033117927 scopus 로고    scopus 로고
    • Deciphering the timescales and mechanisms of protein folding using minimal off-lattice models
    • Thirumalai D and Klimov D K 1999 Deciphering the timescales and mechanisms of protein folding using minimal off-lattice models Curr. Opin. Struct. Biol. 9 197-207
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 197-207
    • Thirumalai, D.1    Klimov, D.K.2
  • 119
    • 0031860932 scopus 로고    scopus 로고
    • A molecular dynamics study of the pores formed by Escherichia Coli Ompf porin in a fully hydrated palmitoyloleoylphosphatidylcholine bilayer
    • Tieleman D P and Berendsen H J C 1998 A molecular dynamics study of the pores formed by Escherichia Coli Ompf porin in a fully hydrated palmitoyloleoylphosphatidylcholine bilayer Biophys. J. 74 2786-801
    • (1998) Biophys J. , vol.74 , pp. 2786-2801
    • Tieleman, D.P.1    Berendsen, H.J.C.2
  • 120
    • 0031752966 scopus 로고    scopus 로고
    • Constant-pressure molecular dynamics investigation of cholesterol effects in a diapalmitoylphosphatidyl-choline bilayer
    • Tu K, Klein M L and Tobias D J 1996 Constant-pressure molecular dynamics investigation of cholesterol effects in a diapalmitoylphosphatidyl-choline bilayer Biophys. J. 75 2147-56
    • (1996) Biophys. J. , vol.75 , pp. 2147-2156
    • Tu, K.1    Klein, M.L.2    Tobias, D.J.3
  • 122
    • 0030972502 scopus 로고    scopus 로고
    • Molecular dynamics simulations of leu-enkephalin in water and DMSO
    • Van Der Spoel D and Berendsen H J C 1997 Molecular dynamics simulations of leu-enkephalin in water and DMSO Biophys. J. 72 2032-41
    • (1997) Biophys. J. , vol.72 , pp. 2032-2041
    • Van Der Spoel, D.1    Berendsen, H.J.C.2
  • 123
    • 84946450438 scopus 로고
    • Algorithms for macromolecular dynamics and constraint dynamics
    • van Gunsteren W F and Berendsen H J C 1977 Algorithms for macromolecular dynamics and constraint dynamics Mol. Phys. 34 1311-22
    • (1977) Mol. Phys. , vol.34 , pp. 1311-1322
    • van Gunsteren, W.F.1    Berendsen, H.J.C.2
  • 124
    • 36049060961 scopus 로고
    • Computer 'experiments' on classical fluids. Ii. Equilibrium correlation functions
    • Verlet L 1967 Computer 'experiments' on classical fluids. Ii. Equilibrium correlation functions Phys. Rev. 165 201-4
    • (1967) Phys. Rev. , vol.165 , pp. 201-204
    • Verlet, L.1
  • 126
    • 0030623698 scopus 로고    scopus 로고
    • Favourable native-like helical local interactions can accelerate protein folding
    • Viguera A R, Villegas V, Avilés F X and Serrano L 1996 Favourable native-like helical local interactions can accelerate protein folding Folding Des. 2 23-33
    • (1996) Folding Des. , vol.2 , pp. 23-33
    • Viguera, A.R.1    Villegas, V.2    Avilés, F.X.3    Serrano, L.4
  • 127
    • 0003085787 scopus 로고
    • Isothermal molecular dynamics calculations for liquid salts
    • Woodstock L V 1971 Isothermal molecular dynamics calculations for liquid salts Chem. Phys. Lett. 10 252-61
    • (1971) Chem. Phys. Lett. , vol.10 , pp. 252-261
    • Woodstock, L.V.1
  • 128
    • 0031804609 scopus 로고    scopus 로고
    • Inhibitors of Hiv-1 protease: A major success of structure-sssisted drug design
    • Wlodawer A and Vondrasek J 1998 Inhibitors of Hiv-1 protease: a major success of structure-sssisted drug design Ann. Rev. Biophys. Biomol. Struct. 27 249-84
    • (1998) Ann. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 249-284
    • Wlodawer, A.1    Vondrasek, J.2
  • 129
    • 0001369198 scopus 로고    scopus 로고
    • Bacteriorhodopsin alpha-helices in lipid settings: Insights for structure prediction
    • Woolf T B 1998a Bacteriorhodopsin alpha-helices in lipid settings: insights for structure prediction Int. J. Quantum Chem. 69 105-16
    • (1998) Int. J. Quantum Chem. , vol.69 , pp. 105-116
    • Woolf, T.B.1
  • 130
    • 0031961813 scopus 로고    scopus 로고
    • Molecular dynamics simulations of individual alpha-helices of bacteriorhodopsin in dimyristoylphosphatidylcholine. Ii. Interaction energy analysis
    • Woolf T B 1998b Molecular dynamics simulations of individual alpha-helices of bacteriorhodopsin in dimyristoylphosphatidylcholine. Ii. Interaction energy analysis Biophys. J. 74 115-31
    • (1998) Biophys. J. , vol.74 , pp. 115-131
    • Woolf, T.B.1
  • 131
    • 0034710426 scopus 로고    scopus 로고
    • Folding studies of a linear pentamer peptide adopting a reverse turn conformation in aqueous solution through molecular dynamics simulation
    • Wu X W and Wang S M 2000 Folding studies of a linear pentamer peptide adopting a reverse turn conformation in aqueous solution through molecular dynamics simulation J. Phys. Chem. 104 8023-34
    • (2000) J. Phys. Chem. , vol.104 , pp. 8023-8034
    • Wu, X.W.1    Wang, S.M.2
  • 132
    • 0000438267 scopus 로고    scopus 로고
    • Molecular dynamics simulation of a rhinovirus capsid under rotational symmetry boundary conditions
    • Yoneda S, Kitazawa M and Umeyama H 1996 Molecular dynamics simulation of a rhinovirus capsid under rotational symmetry boundary conditions J. Comput. Chem. 17 191-203
    • (1996) J. Comput. Chem. , vol.17 , pp. 191-203
    • Yoneda, S.1    Kitazawa, M.2    Umeyama, H.3
  • 133
    • 0033598375 scopus 로고    scopus 로고
    • Interpreting the folding kinetics of helical proteins
    • Zhou Y Q and Karplus M 1999 Interpreting the folding kinetics of helical proteins Nature 401 400-3
    • (1999) Nature , vol.401 , pp. 400-403
    • Zhou, Y.Q.1    Karplus, M.2
  • 135
    • 0033789318 scopus 로고    scopus 로고
    • Molecular dynamics simulation of human prion protein including both N-linked oligosaccharides and the Gpi anchor
    • Zuegg J and Gready J E 2000 Molecular dynamics simulation of human prion protein including both N-linked oligosaccharides and the Gpi anchor Glycobiology 10 959-74
    • (2000) Glycobiology , vol.10 , pp. 959-974
    • Zuegg, J.1    Gready, J.E.2
  • 136
    • 0345493918 scopus 로고    scopus 로고
    • Molecular dynamics simulations of human prion protein: Importance of correct treatment of electrostatic interactions
    • Zuegg J and Greedy J E 1999 Molecular dynamics simulations of human prion protein: importance of correct treatment of electrostatic interactions Biochemistry 38 13862-76
    • (1999) Biochemistry , vol.38 , pp. 13862-13876
    • Zuegg, J.1    Greedy, J.E.2


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