메뉴 건너뛰기




Volumn 6, Issue 7, 1997, Pages 1449-1457

Absence of a stable intermediate on the folding pathway of protein A

Author keywords

Fast folding; Folding intermediate; Hydrogen exchange; Site directed mutagenesis

Indexed keywords

DEUTERIUM; HYDROGEN; ISOLEUCINE; PROTEIN A; TRYPTOPHAN;

EID: 0030755502     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060709     Document Type: Article
Times cited : (116)

References (63)
  • 1
    • 0029155772 scopus 로고
    • Impact of local and non-local interactions on thermodynamics and kinetics of protein folding
    • Abkevich VI, Gutin AM, Shakhnovich EI. 1995a. Impact of local and non-local interactions on thermodynamics and kinetics of protein folding. J Mol Biol 252:460-471.
    • (1995) J Mol Biol , vol.252 , pp. 460-471
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 3
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai Y, Milne JS, Mayne L, Englander SW. 1993. Primary structure effects on peptide group hydrogen exchange. Proteins 17:75-86.
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 4
    • 0028067152 scopus 로고
    • Protein stability parameters measured by hydrogen exchange
    • Bai Y, Milne JS, Mayne L, Englander SW. 1994. Protein stability parameters measured by hydrogen exchange. Proteins 20:4-14.
    • (1994) Proteins , vol.20 , pp. 4-14
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 5
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai Y, Sosnick TR, Mayne L, Englander SW. 1995. Protein folding intermediates: Native-state hydrogen exchange. Science 269:192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 6
    • 0029249945 scopus 로고
    • The nature of protein folding pathways: The classical versus the new view
    • Baldwin RL. 1995. The nature of protein folding pathways: The classical versus the new view. J Biomol NMR 5:103-109.
    • (1995) J Biomol NMR , vol.5 , pp. 103-109
    • Baldwin, R.L.1
  • 7
    • 0029973119 scopus 로고    scopus 로고
    • Direct observation of fast protein folding: The initial collapse of apomyoglobin
    • Ballew RM, Sabelko J, Gruebele M. 1996. Direct observation of fast protein folding: The initial collapse of apomyoglobin. Proc Natl Acad Sci USA 93:5159-5164.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5159-5164
    • Ballew, R.M.1    Sabelko, J.2    Gruebele, M.3
  • 8
    • 45149138663 scopus 로고
    • Comparison of different modes of two-dimensional reverse-correlation NMR for the study of proteins
    • Bax A, Ikura M, Kay LE, Torchia DA, Tschudin R. 1990. Comparison of different modes of two-dimensional reverse-correlation NMR for the study of proteins. J Magn Reson 86:304-318.
    • (1990) J Magn Reson , vol.86 , pp. 304-318
    • Bax, A.1    Ikura, M.2    Kay, L.E.3    Torchia, D.A.4    Tschudin, R.5
  • 9
    • 0029151245 scopus 로고
    • First-principles calculation of the folding free energy of a three-helix bundle protein
    • Boczko EM, Brooks CL. 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, C.L.2
  • 10
    • 0028608099 scopus 로고
    • The stability and unfolding of an IgG binding protein based upon the B domain of protein A from Staphylococcus aureus probed by tryptophan substitution and fluorescence spectroscopy
    • Bottomley SP, Popplewell AG, Scawen M, Wan T, Sutton BJ, Gore MG. 1994. The stability and unfolding of an IgG binding protein based upon the B domain of protein A from Staphylococcus aureus probed by tryptophan substitution and fluorescence spectroscopy. Protein Eng 7:1463-1470.
    • (1994) Protein Eng , vol.7 , pp. 1463-1470
    • Bottomley, S.P.1    Popplewell, A.G.2    Scawen, M.3    Wan, T.4    Sutton, B.J.5    Gore, M.G.6
  • 13
    • 0025804130 scopus 로고
    • Large differences in the helix propensities of alanine and glycine
    • Chakrabartty A, Schellman JA, Baldwin RL. 1991. Large differences in the helix propensities of alanine and glycine. Nature 351:586-588.
    • (1991) Nature , vol.351 , pp. 586-588
    • Chakrabartty, A.1    Schellman, J.A.2    Baldwin, R.L.3
  • 14
    • 0016169865 scopus 로고
    • Determination of the helix and β form of proteins in aqueous solution hy circular dichroism
    • Chen Y-H, Yang JT, Chau KH. 1974. Determination of the helix and β form of proteins in aqueous solution hy circular dichroism. Biochemistry 13:3350-3359.
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.-H.1    Yang, J.T.2    Chau, K.H.3
  • 15
    • 0026768829 scopus 로고
    • Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding I. Myohemerythrin
    • Dyson HJ, Merutka G, Waltho JP, Lerner RA, Wright PE. 1992a. Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding I. Myohemerythrin. J Mol Biol 226:795-817.
    • (1992) J Mol Biol , vol.226 , pp. 795-817
    • Dyson, H.J.1    Merutka, G.2    Waltho, J.P.3    Lerner, R.A.4    Wright, P.E.5
  • 16
    • 0026743136 scopus 로고
    • Folding of peptide fragments comprising the complete sequence of proteins: Models for the initiation of protein folding II Plastocyanin
    • Dyson HJ, Sayre JR, Merutka G, Shin H-C, Lerner RA, Wright PE. 1992b. Folding of peptide fragments comprising the complete sequence of proteins: Models for the initiation of protein folding II Plastocyanin. J Mol Biol 226:819-835.
    • (1992) J Mol Biol , vol.226 , pp. 819-835
    • Dyson, H.J.1    Sayre, J.R.2    Merutka, G.3    Shin, H.-C.4    Lerner, R.A.5    Wright, P.E.6
  • 17
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch H. 1967. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6:1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 19
    • 0028352044 scopus 로고
    • Kinetic mechanism of cytochrome c folding: Involvement of the heme and its ligands
    • Elöve GA, Bhuyan AK, Roder H. 1994. Kinetic mechanism of cytochrome c folding: Involvement of the heme and its ligands. Biochemistry 33:6925-6935.
    • (1994) Biochemistry , vol.33 , pp. 6925-6935
    • Elöve, G.A.1    Bhuyan, A.K.2    Roder, H.3
  • 20
    • 0028856785 scopus 로고
    • Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications
    • Fersht AR. 1995. Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications. Proc Natl Acad Sci USA 92:10869-10873.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10869-10873
    • Fersht, A.R.1
  • 21
    • 0026801084 scopus 로고
    • Three-dimensional solution structure of the B domain of staphylococcal protein A: Comparisons of the solution and crystal structures
    • Gouda H, Torigoe H, Saito A, Sato M, Arata Y, Shimada I. 1992. Three-dimensional solution structure of the B domain of staphylococcal protein A: Comparisons of the solution and crystal structures. Biochemistry 31:9665-9672.
    • (1992) Biochemistry , vol.31 , pp. 9665-9672
    • Gouda, H.1    Torigoe, H.2    Saito, A.3    Sato, M.4    Arata, Y.5    Shimada, I.6
  • 22
    • 0028944346 scopus 로고
    • Is hurst hydrophobic collapse necessary for protein folding?
    • Gutin AM, Abkevich VI, Shakhnovich EI. 1995. Is hurst hydrophobic collapse necessary for protein folding? Biochemistry 34:3066-3076.
    • (1995) Biochemistry , vol.34 , pp. 3066-3076
    • Gutin, A.M.1    Abkevich, V.I.2    Shakhnovich, E.I.3
  • 23
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higuchi R, Krummel B, Saiki RK. 1988. A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions. Nucleic Acids Res 16:7351-7367.
    • (1988) Nucleic Acids Res , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 24
    • 0028935887 scopus 로고
    • Structure and stability of monomeric lambda repressor: NMR evidence for two-state folding
    • Huang GS, Oas TG. 1995a. Structure and stability of monomeric lambda repressor: NMR evidence for two-state folding. Biochemistry 34:3884-3892.
    • (1995) Biochemistry , vol.34 , pp. 3884-3892
    • Huang, G.S.1    Oas, T.G.2
  • 25
    • 0029151158 scopus 로고
    • Submillisecond folding of monomeric lambda repressor
    • Huang GS, Oas TG. 1995b. Submillisecond folding of monomeric lambda repressor. Proc Natl Acad Sci USA 92:6878-6882.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6878-6882
    • Huang, G.S.1    Oas, T.G.2
  • 26
    • 0013994339 scopus 로고
    • Hydrogen exchange in proteins
    • Hvidt A, Nielsen SO. 1966. Hydrogen exchange in proteins. Adv Protein Chem 21:287-339.
    • (1966) Adv Protein Chem , vol.21 , pp. 287-339
    • Hvidt, A.1    Nielsen, S.O.2
  • 27
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
    • Jackson SE, Fersht AR. 1991. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. Biochemistry 30:10428-10435.
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 28
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings PA, Wright PE. 1993. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science 262:892-896.
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2
  • 30
    • 0030057477 scopus 로고    scopus 로고
    • Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues
    • Khorasanizadeh S, Peters ID, Roder H. 1996. Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues. Nat Struct Biol 3:193-205.
    • (1996) Nat Struct Biol , vol.3 , pp. 193-205
    • Khorasanizadeh, S.1    Peters, I.D.2    Roder, H.3
  • 31
    • 0029025915 scopus 로고
    • Kinetic traps in lysozyme folding
    • Kiefhaber T. 1995. Kinetic traps in lysozyme folding. Proc Natl Acad Sci USA 92:9029-9033.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9029-9033
    • Kiefhaber, T.1
  • 32
    • 0027375522 scopus 로고
    • Protein internal flexibility and global stability: Effect of urea on hydrogen exchange rates of bovine pancreatic trypsin inhibitor
    • Kim K-S, Woodward C. 1993. Protein internal flexibility and global stability: Effect of urea on hydrogen exchange rates of bovine pancreatic trypsin inhibitor. Biochemistry 32:9609-9613.
    • (1993) Biochemistry , vol.32 , pp. 9609-9613
    • Kim, K.-S.1    Woodward, C.2
  • 33
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim PS, Baldwin RL. 1982. Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu Rev Biochem 57:459-489.
    • (1982) Annu Rev Biochem , vol.57 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 34
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim PS, Baldwin RL. 1990. Intermediates in the folding reactions of small proteins. Annu Rev Biochem 59:631-660.
    • (1990) Annu Rev Biochem , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 35
    • 0028326042 scopus 로고
    • Monte Carlo simulations of protein folding. II. Application to protein A, ROP, and crambin
    • Kolinski A, Skolnick J. 1994. Monte Carlo simulations of protein folding. II. Application to protein A, ROP, and crambin. Proteins 75:353-366.
    • (1994) Proteins , vol.75 , pp. 353-366
    • Kolinski, A.1    Skolnick, J.2
  • 37
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 38
    • 0028578686 scopus 로고
    • Fast folding of a prototypic polypeptide: The immunoglobulin binding domain of streptococcal protein G
    • Kuszewski J, Clore GM, Gronenborn AM. 1994. Fast folding of a prototypic polypeptide: The immunoglobulin binding domain of streptococcal protein G. Protein Sci 3:1945-1952.
    • (1994) Protein Sci , vol.3 , pp. 1945-1952
    • Kuszewski, J.1    Clore, G.M.2    Gronenborn, A.M.3
  • 39
    • 0027730340 scopus 로고
    • Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A
    • Mayo SL, Baldwin RL. 1993. Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A. Science 262:873-876.
    • (1993) Science , vol.262 , pp. 873-876
    • Mayo, S.L.1    Baldwin, R.L.2
  • 40
    • 0029988634 scopus 로고    scopus 로고
    • Thermodynamics of transient conformations in the folding pathway of barnase: Reorganization of the folding intermediate at low pH
    • Oliveberg M, Fersht AR. 1996. Thermodynamics of transient conformations in the folding pathway of barnase: Reorganization of the folding intermediate at low pH. Biochemistry 35:2738-2749.
    • (1996) Biochemistry , vol.35 , pp. 2738-2749
    • Oliveberg, M.1    Fersht, A.R.2
  • 42
    • 0027948175 scopus 로고
    • Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding
    • Otzen DE, Itzhaki LS, ElMasry NF, Jackson SE, Fersht AR. 1994. Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding. Proc Natl Acad Sci USA 91:10422-10425.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10422-10425
    • Otzen, D.E.1    Itzhaki, L.S.2    ElMasry, N.F.3    Jackson, S.E.4    Fersht, A.R.5
  • 43
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace CN. 1986. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 137:266-280.
    • (1986) Methods Enzymol , vol.137 , pp. 266-280
    • Pace, C.N.1
  • 44
    • 0029153539 scopus 로고
    • Relationship between equilibrium amide proton exchange behavior and the folding pathway of barnase
    • Perrett S, Clarke J, Hounslow AM, Fersht AR. 1995. Relationship between equilibrium amide proton exchange behavior and the folding pathway of barnase. Biochemistry 34:9288-9298.
    • (1995) Biochemistry , vol.34 , pp. 9288-9298
    • Perrett, S.1    Clarke, J.2    Hounslow, A.M.3    Fersht, A.R.4
  • 45
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn OB. 1995. Molten globule and protein folding. Adv Protein Chem 47:83-229.
    • (1995) Adv Protein Chem , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 46
    • 0026751786 scopus 로고
    • The folding of hen lysozyme involves partially structured intermediates and multiple pathways
    • Radford SE, Dobson CM, Evans PA. 1992. The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature 355:302-307.
    • (1992) Nature , vol.355 , pp. 302-307
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 47
    • 0026705132 scopus 로고
    • Truncated, branched and/or cyclic analogues of neuropeptide Y: Importance of the pancreatic peptide fold in the design of specific YT receptor ligands
    • Reymond MT, Delmas L, Koerber SC, Brown MR, Rivier JE. 1992. Truncated, branched and/or cyclic analogues of neuropeptide Y: Importance of the pancreatic peptide fold in the design of specific YT receptor ligands. J Med Chem 35:3653-3659.
    • (1992) J Med Chem , vol.35 , pp. 3653-3659
    • Reymond, M.T.1    Delmas, L.2    Koerber, S.C.3    Brown, M.R.4    Rivier, J.E.5
  • 48
    • 0023705432 scopus 로고
    • Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR
    • Roder H, Elöve GA, Englander SW. 1988. Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR. Nature 335:700-704.
    • (1988) Nature , vol.335 , pp. 700-704
    • Roder, H.1    Elöve, G.A.2    Englander, S.W.3
  • 49
    • 0024331090 scopus 로고
    • Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchange
    • Roder H. 1989. Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchange. Methods Enzymol 176:446-473.
    • (1989) Methods Enzymol , vol.176 , pp. 446-473
    • Roder, H.1
  • 50
    • 0026754044 scopus 로고
    • A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range
    • Santoro MM, Bolen DW. 1992. A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range. Biochemistry 57:4901-4907.
    • (1992) Biochemistry , vol.57 , pp. 4901-4907
    • Santoro, M.M.1    Bolen, D.W.2
  • 51
    • 0027730097 scopus 로고
    • Rationally designing the accumulation of a folding intermediate of barnase by protein engineering
    • Sanz JM, Fersht AR. 1993. Rationally designing the accumulation of a folding intermediate of barnase by protein engineering. Biochemistry 52:13584-13592.
    • (1993) Biochemistry , vol.52 , pp. 13584-13592
    • Sanz, J.M.1    Fersht, A.R.2
  • 53
    • 0026486811 scopus 로고
    • In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences
    • Schnölzer M, Alewood P, Jones A, Alewood D, Kent SBH. 1992. In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences. Int J Pept Protein Res 40:180-193.
    • (1992) Int J Pept Protein Res , vol.40 , pp. 180-193
    • Schnölzer, M.1    Alewood, P.2    Jones, A.3    Alewood, D.4    Kent, S.B.H.5
  • 54
    • 0024742246 scopus 로고
    • Theory of cooperative transitions in protein molecules. I. Why denaturation of globular protein is a first-order phase transition
    • Shakhnovich EI, Finkelstein AV. 1989. Theory of cooperative transitions in protein molecules. I. Why denaturation of globular protein is a first-order phase transition. Biopolymers 28:1667-1680.
    • (1989) Biopolymers , vol.28 , pp. 1667-1680
    • Shakhnovich, E.I.1    Finkelstein, A.V.2
  • 57
    • 0030047378 scopus 로고    scopus 로고
    • Temperature and pH dependences of hydrogen exchange and global stability for ovomucoid third domain
    • Swint-Kruse L, Robertson AD. 1996. Temperature and pH dependences of hydrogen exchange and global stability for ovomucoid third domain. Biochemistry 55:171-180.
    • (1996) Biochemistry , vol.55 , pp. 171-180
    • Swint-Kruse, L.1    Robertson, A.D.2
  • 58
    • 0023758305 scopus 로고
    • NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A
    • Udgaonkar JB, Baldwin RL. 1988. NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A. Nature 555:694-699.
    • (1988) Nature , vol.555 , pp. 694-699
    • Udgaonkar, J.B.1    Baldwin, R.L.2
  • 59
    • 0028331876 scopus 로고
    • Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition
    • Viguera AR, Martinez JC, Filimonov VV, Mateo PL, Serrano L. 1994. Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition. Biochemistry 55:2142-2150.
    • (1994) Biochemistry , vol.55 , pp. 2142-2150
    • Viguera, A.R.1    Martinez, J.C.2    Filimonov, V.V.3    Mateo, P.L.4    Serrano, L.5
  • 60
    • 0028788480 scopus 로고
    • Evidence for a two-state transition in the folding process of the activation domain of human procarboxypeptidase A2
    • Villegas V, Azuaga A, Catasús L, Reverter D, Mateo PL, Avilés FX, Serrano L. 1995. Evidence for a two-state transition in the folding process of the activation domain of human procarboxypeptidase A2. Biochemistry 34:15105-15110.
    • (1995) Biochemistry , vol.34 , pp. 15105-15110
    • Villegas, V.1    Azuaga, A.2    Catasús, L.3    Reverter, D.4    Mateo, P.L.5    Avilés, F.X.6    Serrano, L.7
  • 61
    • 0029966342 scopus 로고    scopus 로고
    • Barriers to protein folding: Formation of buried polar interactions is a slow step in acquisition of structure
    • Waldburger CD, Jonsson T, Sauer RT. 1996. Barriers to protein folding: Formation of buried polar interactions is a slow step in acquisition of structure. Proc Natl Acad Sci USA 95:2629-2634.
    • (1996) Proc Natl Acad Sci USA , vol.95 , pp. 2629-2634
    • Waldburger, C.D.1    Jonsson, T.2    Sauer, R.T.3
  • 63
    • 0024293204 scopus 로고
    • Conformation of peptide fragments of proteins in aqueous solution: Implications for initiation of protein folding
    • Wright PE, Dyson HJ, Lerner RA. 1988. Conformation of peptide fragments of proteins in aqueous solution: Implications for initiation of protein folding. Biochemistry 27:7167-7175.
    • (1988) Biochemistry , vol.27 , pp. 7167-7175
    • Wright, P.E.1    Dyson, H.J.2    Lerner, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.