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Volumn 2, Issue 4, 1997, Pages

The Levinthal paradox: Yesterday and today

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL MODEL; PROTEIN FOLDING; REVIEW;

EID: 0030626588     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(97)00067-9     Document Type: Article
Times cited : (205)

References (75)
  • 1
    • 0002770218 scopus 로고
    • Protein folding: Theoretical studies of thermodynamics and dynamics
    • (Creighton, T., ed.), W.H. Freeman & Sons, New York
    • Karplus, M. & Shakhnovich, E. (1992). Protein folding: theoretical studies of thermodynamics and dynamics. In Protein Folding. (Creighton, T., ed.), pp. 127-195, W.H. Freeman & Sons, New York.
    • (1992) Protein Folding , pp. 127-195
    • Karplus, M.1    Shakhnovich, E.2
  • 3
    • 0028991962 scopus 로고
    • Modelling mutations and homologous proteins
    • Sali, A. (1995). Modelling mutations and homologous proteins. Biotechnology 6, 437-451.
    • (1995) Biotechnology , vol.6 , pp. 437-451
    • Sali, A.1
  • 4
    • 84995046262 scopus 로고
    • A large scale experiment to assess protein structure prediction methods
    • Moult, J., Judson, R., Fidelis, K. & Pedersen, J. (1995). A large scale experiment to assess protein structure prediction methods. Proteins 23, 454-460.
    • (1995) Proteins , vol.23 , pp. 454-460
    • Moult, J.1    Judson, R.2    Fidelis, K.3    Pedersen, J.4
  • 6
    • 84925403366 scopus 로고
    • Concluding remarks
    • (Sarma, R.H., ed.), Adenine Press, Guilderland, New York
    • Phillips, D.C. (1981). Concluding remarks. In Biomolecular Stereodynamics II. (Sarma, R.H., ed.), pp. 497-498, Adenine Press, Guilderland, New York.
    • (1981) Biomolecular Stereodynamics II , pp. 497-498
    • Phillips, D.C.1
  • 8
  • 9
    • 0025048105 scopus 로고
    • Molecular dynamics simulations in biology
    • Karplus, M. & Petsko, G.A. (1990). Molecular dynamics simulations in biology. Nature 347, 631-639.
    • (1990) Nature , vol.347 , pp. 631-639
    • Karplus, M.1    Petsko, G.A.2
  • 10
    • 0019119230 scopus 로고
    • Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 Å and 1.9 Å resolution
    • Marquart, M., Deisendorfer, J., Huber, R. & Palm, W. (1980). Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 Å and 1.9 Å resolution. J. Mol. Biol. 141, 369-381.
    • (1980) J. Mol. Biol. , vol.141 , pp. 369-381
    • Marquart, M.1    Deisendorfer, J.2    Huber, R.3    Palm, W.4
  • 12
    • 0024733407 scopus 로고
    • Intermediates and barrier crossing in a random energy model (with applications to protein folding)
    • Bryngelson, J.D. & Wolynes, P.G. (1989). Intermediates and barrier crossing in a random energy model (with applications to protein folding). J. Phys. Chem. 93, 6902-6915.
    • (1989) J. Phys. Chem. , vol.93 , pp. 6902-6915
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 13
    • 0001340839 scopus 로고
    • Kinetics of unfolding and refolding of single domain proteins
    • (Creighton, T., ed.), W.H. Freeman & Sons, New York
    • Schmid, F.X. (1992). Kinetics of unfolding and refolding of single domain proteins, In Protein Folding. (Creighton, T., ed.), pp. 197-241, W.H. Freeman & Sons, New York.
    • (1992) Protein Folding , pp. 197-241
    • Schmid, F.X.1
  • 14
    • 0026776874 scopus 로고
    • Computational complexity of a problem in molecular structure prediction
    • Ngo, J.T. & Marks, J. (1992). Computational complexity of a problem in molecular structure prediction. Protein Eng. 5, 313-321.
    • (1992) Protein Eng. , vol.5 , pp. 313-321
    • Ngo, J.T.1    Marks, J.2
  • 15
    • 0027690211 scopus 로고
    • Finding the lowest free energy conformation of a protein is an NP-hard problem: Proof and implications
    • Unger, R. & Moult, J. (1993). Finding the lowest free energy conformation of a protein is an NP-hard problem: proof and implications. Bull. Math. Biol. 55, 1183-1198.
    • (1993) Bull. Math. Biol. , vol.55 , pp. 1183-1198
    • Unger, R.1    Moult, J.2
  • 16
    • 0027692037 scopus 로고
    • Complexity of protein folding
    • Fraenkel, A.S. (1993). Complexity of protein folding. Bull. Math. Biol. 55, 1199-1210.
    • (1993) Bull. Math. Biol. , vol.55 , pp. 1199-1210
    • Fraenkel, A.S.1
  • 17
    • 0010034026 scopus 로고
    • Computational complexity, protein structure prediction, and the Levinthal paradox
    • (Merz, K. Jr. & Le Grand, S., eds.), Birkhäuser, Boston, MA
    • Ngo, J.T., Marks, J. & Karplus, M. (1994). Computational complexity, protein structure prediction, and the Levinthal paradox. In The Protein Folding Problem and Tertiary Structure Prediction. (Merz, K. Jr. & Le Grand, S., eds.), pp. 435-508, Birkhäuser, Boston, MA.
    • (1994) The Protein Folding Problem and Tertiary Structure Prediction , pp. 435-508
    • Ngo, J.T.1    Marks, J.2    Karplus, M.3
  • 18
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • Levinthal, C. (1968). Are there pathways for protein folding? J. Chim. Physique. 65, 44-45.
    • (1968) J. Chim. Physique. , vol.65 , pp. 44-45
    • Levinthal, C.1
  • 19
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K. & Chan, H.S. (1997). From Levinthal to pathways to funnels. Nat. Struct. Biol. 4, 10-19.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.1    Chan, H.S.2
  • 20
    • 0015597839 scopus 로고
    • Nucleation, rapid folding and globular intrachain regions in proteins
    • Wetlaufer, D.B. (1973). Nucleation, rapid folding and globular intrachain regions in proteins. Proc. Natl Acad. Sci. USA 70, 697-701.
    • (1973) Proc. Natl Acad. Sci. USA , vol.70 , pp. 697-701
    • Wetlaufer, D.B.1
  • 21
    • 0020972782 scopus 로고
    • Theoretical studies of protein folding
    • Go, N. (1983). Theoretical studies of protein folding. Annu. Rev. Biophys. Bioeng. 12, 183-210.
    • (1983) Annu. Rev. Biophys. Bioeng. , vol.12 , pp. 183-210
    • Go, N.1
  • 22
    • 0015505381 scopus 로고
    • A sequential model of nucleation-dependent protein-folding: Kinetic studies of ribonuclease A
    • Tsong, T.Y., Baldwin, R.L. & McPhie, P. (1972). A sequential model of nucleation-dependent protein-folding: kinetic studies of ribonuclease A. J. Mol. Biol. 63, 453-475.
    • (1972) J. Mol. Biol. , vol.63 , pp. 453-475
    • Tsong, T.Y.1    Baldwin, R.L.2    McPhie, P.3
  • 23
    • 0017251893 scopus 로고
    • Protein-folding dynamics
    • Karplus, M. & Weaver, D.L. (1976). Protein-folding dynamics. Nature 260, 404-406.
    • (1976) Nature , vol.260 , pp. 404-406
    • Karplus, M.1    Weaver, D.L.2
  • 24
    • 0028327236 scopus 로고
    • Folding dynamics: The diffusion-collision model and experimental data
    • Karplus, M. & Weaver, D.L. (1994). Folding dynamics: the diffusion-collision model and experimental data, Protein Sci. 3, 650-668.
    • (1994) Protein Sci. , vol.3 , pp. 650-668
    • Karplus, M.1    Weaver, D.L.2
  • 25
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of folding
    • Kim, P.S. & Baldwin, R.L. (1982). Specific intermediates in the folding reactions of small proteins and the mechanism of folding. Annu. Rev. Biochem. 51, 459-489.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 26
    • 0001756859 scopus 로고
    • Is there a single pathway for the folding of a polypeptide chain?
    • Harrison, S.C. & Durbin, R. (1985). Is there a single pathway for the folding of a polypeptide chain? Proc. Natl Acad. Sci. USA 82, 4028-4030.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 4028-4030
    • Harrison, S.C.1    Durbin, R.2
  • 27
    • 0021166064 scopus 로고
    • Diffusion-collision model for the folding kinetics of the γ-repressor operator-binding domain
    • Bashford, D., Weaver, D.L. & Karplus, M. (1984). Diffusion-collision model for the folding kinetics of the γ-repressor operator-binding domain, J. Biomol. Struct. Dyn. 1, 1243-1255.
    • (1984) J. Biomol. Struct. Dyn. , vol.1 , pp. 1243-1255
    • Bashford, D.1    Weaver, D.L.2    Karplus, M.3
  • 28
    • 0024264819 scopus 로고
    • Diffusion-collision model for the folding kinetics of myoglobin
    • Bashford, D., Cohen, F.E., Karplus, M., Kuntz, I.D. & Weaver, D.L. (1988). Diffusion-collision model for the folding kinetics of myoglobin. Proteins 4, 211-227.
    • (1988) Proteins , vol.4 , pp. 211-227
    • Bashford, D.1    Cohen, F.E.2    Karplus, M.3    Kuntz, I.D.4    Weaver, D.L.5
  • 30
    • 0022423920 scopus 로고
    • Theory for the folding and stability of globular proteins
    • Dill, K.A. (1985). Theory for the folding and stability of globular proteins. Biochemistry 24, 1501-1509.
    • (1985) Biochemistry , vol.24 , pp. 1501-1509
    • Dill, K.A.1
  • 31
    • 0023449962 scopus 로고
    • Spin glasses and the statistical mechanics of protein folding
    • Bryngelson, J.D. & Wolynes, P.G. (1987). Spin glasses and the statistical mechanics of protein folding. Proc. Natl. Acad. Sci. USA 84, 7524-7528.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 32
    • 0028947257 scopus 로고
    • Funnels, pathways and the energy landscape of protein folding: A synthesis
    • Bryngelson, J.D., Onuchic, J.N., Socci, N.D. & Wolynes, P.G. (1995). Funnels, pathways and the energy landscape of protein folding: a synthesis. Proteins 21,167-195.
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 33
    • 0028929556 scopus 로고
    • Principles of protein folding - A perspective from simple exact models
    • Dill, K.A., et al., & Chan, H.S. (1995). Principles of protein folding - a perspective from simple exact models. Protein Sci. 4, 561-602.
    • (1995) Protein Sci. , vol.4 , pp. 561-602
    • Dill, K.A.1    Chan, H.S.2
  • 34
    • 0028949547 scopus 로고
    • Theoretical studies of protein folding and unfolding
    • Karplus, M. & Šali, A. (1995). Theoretical studies of protein folding and unfolding. Curr. Opin. Struct. Biol. 5, 58-73.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 58-73
    • Karplus, M.1    Šali, A.2
  • 35
    • 0019569599 scopus 로고
    • Noninteracting local-structure model of folding and unfolding transition in globular proteins. I. Formulation
    • Go, N. & Abe, H. (1981). Noninteracting local-structure model of folding and unfolding transition in globular proteins. I. Formulation. Biopolymers 20, 991-1011.
    • (1981) Biopolymers , vol.20 , pp. 991-1011
    • Go, N.1    Abe, H.2
  • 37
  • 38
    • 0028958601 scopus 로고
    • Characterizing transition states in protein folding: An essential step in the puzzle
    • Fersht, A.R. (1994). Characterizing transition states in protein folding: an essential step in the puzzle. Curr. Opin. Struct. Biol. 5, 79-84.
    • (1994) Curr. Opin. Struct. Biol. , vol.5 , pp. 79-84
    • Fersht, A.R.1
  • 40
    • 0029973119 scopus 로고    scopus 로고
    • Direct observation of fast protein folding: The initial collapse of apomyoglobin
    • Ballew, R.M., Sabelko, J. & Gruebele, M. (1996). Direct observation of fast protein folding: the initial collapse of apomyoglobin. Proc. Natl Acad. Sci. USA 93, 5759-5764.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5759-5764
    • Ballew, R.M.1    Sabelko, J.2    Gruebele, M.3
  • 43
    • 0000710672 scopus 로고    scopus 로고
    • Diffusion dynamics of the reaction coordinate in protein folding
    • Socci, N.D., Onuchic, J.N. & Wolynes, P.G. (1996). Diffusion dynamics of the reaction coordinate in protein folding. J. Chem. Phys. 104, 5860-5868.
    • (1996) J. Chem. Phys. , vol.104 , pp. 5860-5868
    • Socci, N.D.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 44
    • 4243392673 scopus 로고
    • Proteins with selected sequences fold into unique native conformation
    • Shakhnovich, E.I. (1994). Proteins with selected sequences fold into unique native conformation. Phys. Rev. Lett. 72, 3907-3910.
    • (1994) Phys. Rev. Lett. , vol.72 , pp. 3907-3910
    • Shakhnovich, E.I.1
  • 46
    • 0029781355 scopus 로고    scopus 로고
    • The folding mechanism of larger model proteins: Role of native structure
    • Dinner, A.R., Šali, A. & Karplus, M. (1996). The folding mechanism of larger model proteins: role of native structure, Proc. Natl Acad. Sci. USA 93, 8356-8361.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 8356-8361
    • Dinner, A.R.1    Šali, A.2    Karplus, M.3
  • 47
    • 0028053187 scopus 로고
    • Understanding how proteins fold: The lysozyme story so far
    • Dobson, C.M., Evans, P.A. & Radford, S.E. (1994). Understanding how proteins fold: the lysozyme story so far. Trends Biochem. Sci. 19, 31-37.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 31-37
    • Dobson, C.M.1    Evans, P.A.2    Radford, S.E.3
  • 48
    • 0008113343 scopus 로고
    • Protein dynamics: From the native to the unfolded state and back again
    • (Pullman, A. et al., eds.), Kluwer Academic Publishers, Amsterdam
    • Karplus, M., Caflisch, A., Šali, A. & Shakhnovich, E. (1995). Protein dynamics: from the native to the unfolded state and back again. In Modelling of Biomolecular Structures and Mechanisms. (Pullman, A. et al., eds.), pp. 69-84, Kluwer Academic Publishers, Amsterdam.
    • (1995) Modelling of Biomolecular Structures and Mechanisms , pp. 69-84
    • Karplus, M.1    Caflisch, A.2    Šali, A.3    Shakhnovich, E.4
  • 49
    • 0028981210 scopus 로고
    • Negative activation enthalpies in the kinetics of protein folding
    • Oliveberg, M., Tan, Y.-J. & Fersht, A.R. (1995). Negative activation enthalpies in the kinetics of protein folding. Proc. Natl Acad. Sci. USA 92, 8926-8929.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 8926-8929
    • Oliveberg, M.1    Tan, Y.-J.2    Fersht, A.R.3
  • 50
    • 0028776642 scopus 로고
    • Matching speed and stability
    • Baldwin, R.L (1994). Matching speed and stability. Nature 369, 183-184.
    • (1994) Nature , vol.369 , pp. 183-184
    • Baldwin, R.L.1
  • 51
    • 0025127949 scopus 로고
    • Pieces of the folding puzzle
    • Baldwin, R.L. (1990). Pieces of the folding puzzle. Nature 346, 409-410.
    • (1990) Nature , vol.346 , pp. 409-410
    • Baldwin, R.L.1
  • 52
    • 0024995943 scopus 로고
    • Detection and characterization of a folding intermediate in barnase by NMR
    • Bycroft, M., Matouschek, A., Kellis, J.T. Jr., Serrano, L & Fersht, A.R. (1990). Detection and characterization of a folding intermediate in barnase by NMR. Nature 346, 488-490.
    • (1990) Nature , vol.346 , pp. 488-490
    • Bycroft, M.1    Matouschek, A.2    Kellis Jr., J.T.3    Serrano, L.4    Fersht, A.R.5
  • 53
    • 0025698613 scopus 로고
    • Transient folding intermediates characterized by protein engineering
    • Matouschek, A., Kellis, J.T. Jr., Serrano, L, Bycroft, M. & Fersht, A.R. (1990). Transient folding intermediates characterized by protein engineering. Nature 346, 440-445.
    • (1990) Nature , vol.346 , pp. 440-445
    • Matouschek, A.1    Kellis Jr., J.T.2    Serrano, L.3    Bycroft, M.4    Fersht, A.R.5
  • 54
    • 0028037217 scopus 로고
    • Single versus parallel pathways of protein folding and fractional formation of structure in the transition state
    • Fersht, A.R., Itzhaki, L.S., EIMasry, N.F., Matthews, J.M. & Otzen, D.E. (1994). Single versus parallel pathways of protein folding and fractional formation of structure in the transition state. Proc. Natl Acad. Sci. USA 91, 10426-10429.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10426-10429
    • Fersht, A.R.1    Itzhaki, L.S.2    Eimasry, N.F.3    Matthews, J.M.4    Otzen, D.E.5
  • 55
    • 0027318781 scopus 로고
    • Kinetics and thermodynamics in model proteins
    • Camacho, C.J. & Thirumalai, D. (1993). Kinetics and thermodynamics in model proteins. Proc. Natl Acad. Sci. USA 90, 6369-6372.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6369-6372
    • Camacho, C.J.1    Thirumalai, D.2
  • 56
    • 0028929204 scopus 로고
    • Kinetics of protein folding
    • Chan, H.S. (1995). Kinetics of protein folding. Nature 373, 664-665.
    • (1995) Nature , vol.373 , pp. 664-665
    • Chan, H.S.1
  • 57
    • 0028929204 scopus 로고
    • Comment: Kinetics of protein folding
    • Karplus, M., Šali, A. & Shakhnovich, E. (1995). Comment: kinetics of protein folding. Nature 373, 664-665.
    • (1995) Nature , vol.373 , pp. 664-665
    • Karplus, M.1    Šali, A.2    Shakhnovich, E.3
  • 58
    • 0002698766 scopus 로고    scopus 로고
    • Modelling protein folding: The beauty and power of simplicity
    • Shakhnovich, E. (1996). Modelling protein folding: the beauty and power of simplicity. Fold Des. 1, R50-R54.
    • (1996) Fold Des. , vol.1
    • Shakhnovich, E.1
  • 59
    • 0001222580 scopus 로고
    • Lattice representations of globular proteins: How good are they?
    • Kolinski, A. & Skolnick, J. (1993). Lattice representations of globular proteins: how good are they? J. Comp. Chem. 14, 1194-1202.
    • (1993) J. Comp. Chem. , vol.14 , pp. 1194-1202
    • Kolinski, A.1    Skolnick, J.2
  • 61
    • 0026723063 scopus 로고
    • Protein folding funnels: A kinetic approach to the sequence-structure relationship
    • Leopold, P.E., Montal, M. & Onuchic, J.N. (1992). Protein folding funnels: a kinetic approach to the sequence-structure relationship. Proc. Natl Acad. Sci. USA 89, 8721-8725.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 8721-8725
    • Leopold, P.E.1    Montal, M.2    Onuchic, J.N.3
  • 63
    • 0028882223 scopus 로고
    • Simple model of protein folding kinetics
    • Zwanzig, R. (1995). Simple model of protein folding kinetics. Proc. Natl Acad. Sci. USA 92, 9801-9804.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 9801-9804
    • Zwanzig, R.1
  • 64
    • 0030623529 scopus 로고    scopus 로고
    • Rate of protein folding near the point of thermodynamic equilibrium between the coil and the most stable chain fold
    • Finkelstein, A.V. & Badretdinov, A.Y. (1997). Rate of protein folding near the point of thermodynamic equilibrium between the coil and the most stable chain fold. Fold. Des. 2, 115-121.
    • (1997) Fold. Des. , vol.2 , pp. 115-121
    • Finkelstein, A.V.1    Badretdinov, A.Y.2
  • 65
    • 33645659844 scopus 로고    scopus 로고
    • On "Levinthal paradox" and the theory of folding
    • in press
    • Durup, J. (1997). On "Levinthal paradox" and the theory of folding. Theochem. in press.
    • (1997) Theochem
    • Durup, J.1
  • 66
    • 0030322669 scopus 로고    scopus 로고
    • Protein folding funnels: The nature of the transition state ensemble
    • Onuchic, J.N., Socci, N.D., Luthey-Schulten, Z. & Wolynes, P.C. (1996). Protein folding funnels: the nature of the transition state ensemble. Fold Des. 1, 441-450.
    • (1996) Fold Des. , vol.1 , pp. 441-450
    • Onuchic, J.N.1    Socci, N.D.2    Luthey-Schulten, Z.3    Wolynes, P.C.4
  • 69
    • 0029866436 scopus 로고    scopus 로고
    • Why is protein folding so fast?
    • Baldwin, R.L (1996). Why is protein folding so fast? Proc. Natl Acad. Sci. USA 93, 2627-2628.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 2627-2628
    • Baldwin, R.L.1
  • 71
  • 72
    • 0011804246 scopus 로고
    • Molecular dynamics studies of protein and peptide folding and unfolding
    • (Merz, K., Jr. & Le Grand, S., eds.), Birkhäuser, Boston, MA
    • Caflisch, A. & Karplus, M. (1994). Molecular dynamics studies of protein and peptide folding and unfolding. In The Protein Folding Problem and Tertiary Structure Prediction. (Merz, K., Jr. & Le Grand, S., eds.), pp. 195-232, Birkhäuser, Boston, MA.
    • (1994) The Protein Folding Problem and Tertiary Structure Prediction , pp. 195-232
    • Caflisch, A.1    Karplus, M.2
  • 73
    • 0028143603 scopus 로고
    • Characterization of the transition state of protein unfolding by use of molecular dynamics: Chymotrypsin inhibitor 2
    • Li, A. & Daggett, V. (1994). Characterization of the transition state of protein unfolding by use of molecular dynamics: chymotrypsin inhibitor 2. Proc. Natl. Acad. Sci. USA 91, 10430-10434.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10430-10434
    • Li, A.1    Daggett, V.2
  • 74
    • 0029151245 scopus 로고
    • First principles calculation of the folding free energy of a three-helix bundle protein
    • Boczko, E.M. & Brooks C.L, III (1995). First principles calculation of the folding free energy of a three-helix bundle protein. Science 269, 393-396.
    • (1995) Science , vol.269 , pp. 393-396
    • Boczko, E.M.1    Brooks III, C.L.2
  • 75
    • 33645689998 scopus 로고    scopus 로고
    • A quotation usually attributed to G Flaubert. It is interesting that in the United States, the expression "The Devil is in the details" is used instead
    • A quotation usually attributed to G Flaubert. It is interesting that in the United States, the expression "The Devil is in the details" is used instead.


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