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Volumn 6, Issue 5, 1996, Pages 637-642

Time resolved fluorescence spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; TRYPTOPHAN DERIVATIVE;

EID: 0030272742     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(96)80030-3     Document Type: Article
Times cited : (102)

References (46)
  • 1
    • 0025732275 scopus 로고
    • Experimentally verifying molecular dynamics simulations through fluorescence anisotropy measurements
    • 1. Axelsen PH, Gratton E, Prendergast FG: Experimentally verifying molecular dynamics simulations through fluorescence anisotropy measurements. Biochemistry 1991, 30:1173-1179.
    • (1991) Biochemistry , vol.30 , pp. 1173-1179
    • Axelsen, P.H.1    Gratton, E.2    Prendergast, F.G.3
  • 3
    • 5644229302 scopus 로고    scopus 로고
    • Three-photon excitation of a tryptophan derivative using a fs-Ti-sapphire laser
    • 3. Gryczynski I, Malak H, Lakowicz JR: Three-photon excitation of a tryptophan derivative using a fs-Ti-sapphire laser. Biospectroscopy 1996, 2:9-15.
    • (1996) Biospectroscopy , vol.2 , pp. 9-15
    • Gryczynski, I.1    Malak, H.2    Lakowicz, J.R.3
  • 4
    • 0028029712 scopus 로고
    • Theory of light quenching: Effects on fluorescence polarization, intensity, and anisotropy decays
    • 4. Kusba J, Bogdanov V, Gryczynski I, Lakowicz JR: Theory of light quenching: effects on fluorescence polarization, intensity, and anisotropy decays. Biophys J 1994, 67:2024-2040.
    • (1994) Biophys J , vol.67 , pp. 2024-2040
    • Kusba, J.1    Bogdanov, V.2    Gryczynski, I.3    Lakowicz, J.R.4
  • 5
    • 0028950771 scopus 로고
    • Time-resolved fluorescence spectroscopy
    • 5. Holzwarth AR: Time-resolved fluorescence spectroscopy. Methods Enzymol 1995, 246:334-362. A recent review of time-resolved fluorescence spectroscopy as applied to studies of biochemical systems, with a particular emphasis on instrumentation and measurement techniques.
    • (1995) Methods Enzymol , vol.246 , pp. 334-362
    • Holzwarth, A.R.1
  • 6
    • 0002647421 scopus 로고
    • Laser sources and microchannel plate detectors for pulse fluorometry
    • Edited by Lakowicz JR. New York: Plenum
    • 6. Small EW: Laser sources and microchannel plate detectors for pulse fluorometry. In Topics in Fluorescence Spectroscopy, vol 1. Edited by Lakowicz JR. New York: Plenum; 1991:97-182.
    • (1991) Topics in Fluorescence Spectroscopy , vol.1 , pp. 97-182
    • Small, E.W.1
  • 7
    • 0000772394 scopus 로고
    • Frequency-domain fluorescence spectroscopy
    • Edited by Lakowicz JR. New York: Plenum
    • 7. Lakowicz JR, Gryczynski I: Frequency-domain fluorescence spectroscopy. In Topics in Fluorescence Spectroscopy, vol 1. Edited by Lakowicz JR. New York: Plenum; 1991:293-335.
    • (1991) Topics in Fluorescence Spectroscopy , vol.1 , pp. 293-335
    • Lakowicz, J.R.1    Gryczynski, I.2
  • 8
    • 0001363954 scopus 로고
    • Time-resolved fluorescence techniques: Methods and applications in biology
    • 8. Prendergast FG: Time-resolved fluorescence techniques: methods and applications in biology. Curr Opin Struct Biol 1991, 1:1054-1059.
    • (1991) Curr Opin Struct Biol , vol.1 , pp. 1054-1059
    • Prendergast, F.G.1
  • 9
    • 0001464493 scopus 로고
    • Analyzing the distribution of decay constants in pulse fluorometry using the maximum entropy method
    • 9. Livesy AK, Brochon, JC: Analyzing the distribution of decay constants in pulse fluorometry using the maximum entropy method. Biophys J 1987, 52:693-706.
    • (1987) Biophys J , vol.52 , pp. 693-706
    • Livesy, A.K.1    Brochon, J.C.2
  • 10
    • 0025192620 scopus 로고
    • Pade-Laplace method for the analysis of time-resolved fluorescence decay curves
    • 10. Bazjer Ž, Sharp JC, Sedarous SS, Prendergast FG: Pade-Laplace method for the analysis of time-resolved fluorescence decay curves. Eur J Biophys 1980, 18:101-115.
    • (1980) Eur J Biophys , vol.18 , pp. 101-115
    • Bazjer, Z.1    Sharp, J.C.2    Sedarous, S.S.3    Prendergast, F.G.4
  • 11
    • 0023317270 scopus 로고
    • Fluorescence lifetime distributions in proteins
    • 11. Alcala JR, Gratton E, Prendergast FG: Fluorescence lifetime distributions in proteins. Biophys J 1987, 51:597-604.
    • (1987) Biophys J , vol.51 , pp. 597-604
    • Alcala, J.R.1    Gratton, E.2    Prendergast, F.G.3
  • 12
    • 0028925439 scopus 로고
    • Protein fluorescence decay: Discrete components or distribution of lifetimes? really no way out of the dilemma?
    • 12. Vix A, Lami H: Protein fluorescence decay: discrete components or distribution of lifetimes? Really no way out of the dilemma? Biophys J 1995, 68:1145-1151. Specific criteria are given for distinguishing between discrete and distributed lifetime models in the analysis of fluorescence decay data.
    • (1995) Biophys J , vol.68 , pp. 1145-1151
    • Vix, A.1    Lami, H.2
  • 13
    • 0029111930 scopus 로고
    • Analytical approach to the recovery of short fluorescence lifetimes from fluorescence decay curves
    • 13. Bazjer Ž, Zelic A, Prendergast FG: Analytical approach to the recovery of short fluorescence lifetimes from fluorescence decay curves. Biophys J 1995, 69:1148-1161. New methods are presented for the numerical calculation of convolution integrals in TCSPC, leading to improved recovery of short fluorescence lifetimes.
    • (1995) Biophys J , vol.69 , pp. 1148-1161
    • Bazjer, Z.1    Zelic, A.2    Prendergast, F.G.3
  • 14
    • 33750927821 scopus 로고
    • Fluorescence decay of tryptophan conformers in aqueous solution
    • 14. Szabo AG, Rayner DM: Fluorescence decay of tryptophan conformers in aqueous solution. J Am Chem Soc 1980, 102:554-563.
    • (1980) J Am Chem Soc , vol.102 , pp. 554-563
    • Szabo, A.G.1    Rayner, D.M.2
  • 15
    • 0020763601 scopus 로고
    • On the origin of nonexponential fluorescence decay in tryptophan and its derivatives
    • 15. Petrich JW, Chang MC, McDonald DB, Fleming GR: On the origin of nonexponential fluorescence decay in tryptophan and its derivatives. J Am Chem Soc 1983, 105:3824-3832.
    • (1983) J Am Chem Soc , vol.105 , pp. 3824-3832
    • Petrich, J.W.1    Chang, M.C.2    McDonald, D.B.3    Fleming, G.R.4
  • 16
    • 0025830305 scopus 로고
    • Fluorescence of tryptophan dipeptides: Correlations with the rotamer model
    • 16. Chen RF, Knutson JR, Ziffer H, Porter D: Fluorescence of tryptophan dipeptides: correlations with the rotamer model. Biochemistry 1991, 30:5184-5195.
    • (1991) Biochemistry , vol.30 , pp. 5184-5195
    • Chen, R.F.1    Knutson, J.R.2    Ziffer, H.3    Porter, D.4
  • 18
    • 0029167814 scopus 로고
    • Conformational heterogeneity of tryptophan in a protein crystal
    • 18. Dahms TES, Willis KJ, Szabo AG: Conformational heterogeneity of tryptophan in a protein crystal. J Am Chem Soc 1995, 117:2321-2326. The existence of three ground-state tryptophan rotamers in crystalline erabutoxin b is established by time-resolved fluorescence measurements obtained as a function of crystal orientation.
    • (1995) J Am Chem Soc , vol.117 , pp. 2321-2326
    • Dahms, T.E.S.1    Willis, K.J.2    Szabo, A.G.3
  • 19
    • 0028175552 scopus 로고
    • Probing α-helical secondary structure at a specific site in model peptides via restriction of tryptophan side-chain rotamer conformation
    • 19. Willis KJ, Neugebauer W, Sikorska M, Szabo AG: Probing α-helical secondary structure at a specific site in model peptides via restriction of tryptophan side-chain rotamer conformation. Biophys J 1994, 66:1623-1630.
    • (1994) Biophys J , vol.66 , pp. 1623-1630
    • Willis, K.J.1    Neugebauer, W.2    Sikorska, M.3    Szabo, A.G.4
  • 20
    • 0029151752 scopus 로고
    • Probing local secondary structure by fluorescence: Time-resolved and circular dichroism studies of highly purified neurotoxins
    • 20. Dahms TES, Szabo AG: Probing local secondary structure by fluorescence: time-resolved and circular dichroism studies of highly purified neurotoxins. Biophys J 1995, 69:569-576. This paper demonstrates that the relative rotamer proportions, determined from the time-resolved fluorescence of an intrinsic tryptophan residue, is indicative of local β-sheet secondary structure.
    • (1995) Biophys J , vol.69 , pp. 569-576
    • Dahms, T.E.S.1    Szabo, A.G.2
  • 21
    • 0026670753 scopus 로고
    • A new intrinsic fluorescent probe for proteins. Biosynthetic incorporation of 5-hydroxytryptophan into oncomodulin
    • 21. Hogue CW, Rasquinha I, Szabo AG, MacManus JP: A new intrinsic fluorescent probe for proteins. Biosynthetic incorporation of 5-hydroxytryptophan into oncomodulin. FEBS Lett 1992, 310:269-272.
    • (1992) FEBS Lett , vol.310 , pp. 269-272
    • Hogue, C.W.1    Rasquinha, I.2    Szabo, A.G.3    MacManus, J.P.4
  • 22
    • 0027097564 scopus 로고
    • Spectral enhancement of proteins: Biological incorporation and fluorescence characterization of 5-hydroxytryptophan in bacteriophage λ cl repressor
    • 22. Ross JBA, Senear DF, Waxman E, Kombo BB, Rusinova E, Huang YT, Laws WR, Hasselbacher CA: Spectral enhancement of proteins: biological incorporation and fluorescence characterization of 5-hydroxytryptophan in bacteriophage λ cl repressor. Proc Natl Acad Sci USA 1992, 89:12023-12027.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 12023-12027
    • Ross, J.B.A.1    Senear, D.F.2    Waxman, E.3    Kombo, B.B.4    Rusinova, E.5    Huang, Y.T.6    Laws, W.R.7    Hasselbacher, C.A.8
  • 23
    • 0001072480 scopus 로고
    • Photophysics of a novel optical probe: 7-azaindole
    • 23. Negrerie MJ, Gai F, Petrich JW: Photophysics of a novel optical probe: 7-azaindole. J Phys Chem 1991, 95:8663-8670.
    • (1991) J Phys Chem , vol.95 , pp. 8663-8670
    • Negrerie, M.J.1    Gai, F.2    Petrich, J.W.3
  • 24
    • 0027721899 scopus 로고
    • Characterization of aminoacyladenylates in B. Subtilis tryptophanyl-tRNA synthetase, by the fluorescence of tryptophan analogs 5-hydroxytryptophan and 7-azatryptophan
    • 24. Hogue CWV, Szabo AG: Characterization of aminoacyladenylates in B. subtilis tryptophanyl-tRNA synthetase, by the fluorescence of tryptophan analogs 5-hydroxytryptophan and 7-azatryptophan. Biophys Chem 1993, 48:159-169.
    • (1993) Biophys Chem , vol.48 , pp. 159-169
    • Hogue, C.W.V.1    Szabo, A.G.2
  • 25
    • 0028849457 scopus 로고
    • Using 7-azatryptophan to probe small molecule-protein interactions on the picosecond time scale: The complex of avidin and biotinylated 7-azatryptophan
    • 25. Rich RL, Gai F, Lane JW, Petrich JW, Schwabacher AW: Using 7-azatryptophan to probe small molecule-protein interactions on the picosecond time scale: the complex of avidin and biotinylated 7-azatryptophan. J Am Chem Soc 1995, 117:733-739. Reports a time-resolved fluorescence study of biotinylated 7-aza-Trp bound to avidin which demonstrates the optical selectivity of 7-aza-Trp in the presence of several tryptophan residues.
    • (1995) J Am Chem Soc , vol.117 , pp. 733-739
    • Rich, R.L.1    Gai, F.2    Lane, J.W.3    Petrich, J.W.4    Schwabacher, A.W.5
  • 27
    • 0029030198 scopus 로고
    • 5-Hydroxytryptophan: An absorption and fluorescence probe which is a conservative replacement for [A14 tyrosine] in insulin
    • 27. Laws WR, Schwartz GP, Rusinova E, Burke GT, Chu Y-C, Katsoyannis PG, Ross JBA: 5-Hydroxytryptophan: an absorption and fluorescence probe which is a conservative replacement for [A14 tyrosine] in insulin. J Protein Chem 1995, 14:225-231.
    • (1995) J Protein Chem , vol.14 , pp. 225-231
    • Laws, W.R.1    Schwartz, G.P.2    Rusinova, E.3    Burke, G.T.4    Chu, Y.-C.5    Katsoyannis, P.G.6    Ross, J.B.A.7
  • 28
    • 0029865110 scopus 로고    scopus 로고
    • Transcriptional activation domain of the herpesvirus protein VP16 becomes conformationally constrained upon interaction with basal transcription factors
    • 28. Shen F, Triezenberg SJ, Hensley P, Porter D, Knutson JR: Transcriptional activation domain of the herpesvirus protein VP16 becomes conformationally constrained upon interaction with basal transcription factors. J Biol Chem 1996, 271:4827-4837. An elegant example of the use of tryptophan analogs in studies of protein-protein interactions. The results provide evidence for conformational changes in the transcriptional activator VP16 due to interactions with the basal transcription factors TBP and TFIIB.
    • (1996) J Biol Chem , vol.271 , pp. 4827-4837
    • Shen, F.1    Triezenberg, S.J.2    Hensley, P.3    Porter, D.4    Knutson, J.R.5
  • 29
    • 0029560442 scopus 로고
    • Flexibility of enzymes suspended in organic solvents probed by time-resolved fluorescence anisotropy. Evidence that enzyme activity and enantioselectivity are directly related to enzyme flexibility
    • 29. Broos J, Visser AJWG, Engbersen JEJ, Verboom W, Van Hoek A, Reinhoudt DN: Flexibility of enzymes suspended in organic solvents probed by time-resolved fluorescence anisotropy. Evidence that enzyme activity and enantioselectivity are directly related to enzyme flexibility. J Am Chem Soc 1995, 117:12657-12663. Provides direct evidence for restricted molecular flexibility of enzymes suspended in organic solvents and suggests a relationship between enantio-selectivity and enzyme flexibility.
    • (1995) J Am Chem Soc , vol.117 , pp. 12657-12663
    • Broos, J.1    Visser, A.J.W.G.2    Engbersen, J.E.J.3    Verboom, W.4    Van Hoek, A.5    Reinhoudt, D.N.6
  • 30
    • 0024653016 scopus 로고
    • Enzymatic catalysis in anhydrous organic solvents
    • 30. Klibanov AM: Enzymatic catalysis in anhydrous organic solvents. Trends Biochem Sci 1989, 14:141-144.
    • (1989) Trends Biochem Sci , vol.14 , pp. 141-144
    • Klibanov, A.M.1
  • 31
    • 0030052607 scopus 로고    scopus 로고
    • Tryptophan dynamics of the FK506 binding protein: Time-resolved fluorescence and simulations
    • 31. Silva ND, Prendergast FG: Tryptophan dynamics of the FK506 binding protein: time-resolved fluorescence and simulations. Biophys J 1996, 70:1122-1137. A very thorough study of the internal dynamics of the single tryptophan residue of FKBP12, both free and bound to immunosuppressants, which combines time-resolved anisotropy measurements with theoretical simulations.
    • (1996) Biophys J , vol.70 , pp. 1122-1137
    • Silva, N.D.1    Prendergast, F.G.2
  • 32
    • 0028925815 scopus 로고
    • Local and global dynamics during the folding of Escherichia coli dihydrofolate reductase by time-resolved fluorescence spectroscopy
    • 32. Jones BE, Beechem JM, Matthews CR: Local and global dynamics during the folding of Escherichia coli dihydrofolate reductase by time-resolved fluorescence spectroscopy. Biochemistry 1995, 34:1868-1877. An impressive study demonstrating that time-resolved fluorescence data can be collected during the course of a rapid protein-folding reaction.
    • (1995) Biochemistry , vol.34 , pp. 1868-1877
    • Jones, B.E.1    Beechem, J.M.2    Matthews, C.R.3
  • 33
    • 0028936789 scopus 로고
    • Nonlocal interactions stabilize long range loops in the initial folding intermediates of reduced bovine pancreatic trypsin inhibitor
    • 33. Ittah V, Haas E: Nonlocal interactions stabilize long range loops in the initial folding intermediates of reduced bovine pancreatic trypsin inhibitor. Biochemistry 1995, 34:4493-4506.
    • (1995) Biochemistry , vol.34 , pp. 4493-4506
    • Ittah, V.1    Haas, E.2
  • 34
    • 0028800425 scopus 로고
    • Analysis of the structure of ribonuclease A in native and partially denatured states by time-resolved nonradiative dynamic excitation energy transfer between site-specific extrinsic probes
    • 34. Buckler DR, Haas E, Scheraga HA: Analysis of the structure of ribonuclease A in native and partially denatured states by time-resolved nonradiative dynamic excitation energy transfer between site-specific extrinsic probes. Biochemistry 1995, 34:15965-15978. An impressive combination of protein chemistry, time-resolved fluorescence and sophisticated data analysis is used to characterize the conformation and dynamic flexibility of ribonuclease A under native and denaturing conditions.
    • (1995) Biochemistry , vol.34 , pp. 15965-15978
    • Buckler, D.R.1    Haas, E.2    Scheraga, H.A.3
  • 35
    • 0029918121 scopus 로고    scopus 로고
    • Time-resolved fluorescence studies of the molten globule state of apomyoglobin
    • 35. Rischel C, Thyberg P, Rigler R, Poulsen FM: Time-resolved fluorescence studies of the molten globule state of apomyoglobin. J Mol Biol 1996, 257:877-885.
    • (1996) J Mol Biol , vol.257 , pp. 877-885
    • Rischel, C.1    Thyberg, P.2    Rigler, R.3    Poulsen, F.M.4
  • 36
    • 0027931587 scopus 로고
    • Conformational flexibility in a staphylococcal nuclease mutant K45C from time-resolved resonance energy transfer measurements
    • 36. Wu P, Brand L: Conformational flexibility in a staphylococcal nuclease mutant K45C from time-resolved resonance energy transfer measurements. Biochemistry 1994, 33:10457-10462.
    • (1994) Biochemistry , vol.33 , pp. 10457-10462
    • Wu, P.1    Brand, L.2
  • 37
    • 0029992307 scopus 로고    scopus 로고
    • Fluorescence studies of DNA and RNA structure and dynamics
    • 37. Millar DP: Fluorescence studies of DNA and RNA structure and dynamics. Curr Opin Struct Biol 1996, 6:322-326. Applications of steady-state and time-resolved fluorescence techniques used to study DNA and RNA are reviewed, with an emphasis on studies that provide information on local and global aspects of nucleic acid structure.
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 322-326
    • Millar, D.P.1
  • 38
    • 0030067349 scopus 로고    scopus 로고
    • Torsional dynamics and orientation of DNA-DAPI complexes
    • 38. Barcellona ML, Gratton E: Torsional dynamics and orientation of DNA-DAPI complexes. Biochemistry 1996, 35:321-333. A combined analysis of DNA torsional dynamics and DAPI-DAPI energy transfer is used to delimit the torsion elastic constant recovered from the anisotropy decay of DAPI bound to DNA.
    • (1996) Biochemistry , vol.35 , pp. 321-333
    • Barcellona, M.L.1    Gratton, E.2
  • 40
    • 0029958871 scopus 로고    scopus 로고
    • Large-amplitude picosecond anisotropy decay of the intrinsic fluorescence of double-stranded DNA
    • 40. Georghiou S, Bradrick TD, Philippetis A, Beechem JM: Large-amplitude picosecond anisotropy decay of the intrinsic fluorescence of double-stranded DNA. Biophys J 1996, 70:1909-1922. Time-resolved anisotropy measurements of the intrinsic fluorescence of thymine residues in synthetic polynucleotides provide evidence for picosecond base motions in DNA.
    • (1996) Biophys J , vol.70 , pp. 1909-1922
    • Georghiou, S.1    Bradrick, T.D.2    Philippetis, A.3    Beechem, J.M.4
  • 41
    • 0024456523 scopus 로고
    • Structure and dynamics of a fluorescent DNA oligomer containing the EcoRI recognition sequence: Fluorescence, molecular dynamics, and NMR studies
    • 41. Nordlund TM, Andersson S, Nilsson L, Rigler R, Graslund A, McLaughlin LW: Structure and dynamics of a fluorescent DNA oligomer containing the EcoRI recognition sequence: fluorescence, molecular dynamics, and NMR studies. Biochemistry 1989, 28:9095-9103.
    • (1989) Biochemistry , vol.28 , pp. 9095-9103
    • Nordlund, T.M.1    Andersson, S.2    Nilsson, L.3    Rigler, R.4    Graslund, A.5    McLaughlin, L.W.6
  • 43
    • 0029896548 scopus 로고    scopus 로고
    • Conformational flexibility of three-way DNA junctions containing unpaired nucleotides
    • 43. Yang M, Millar DP: Conformational flexibility of three-way DNA junctions containing unpaired nucleotides. Biochemistry 1996, 35:7959-7967. Measurements of time-resolved FRET are combined with donor-acceptor distance distribution analysis to characterize the impact of bulged bases on the overall geometry and flexibility of three-way DNA junctions.
    • (1996) Biochemistry , vol.35 , pp. 7959-7967
    • Yang, M.1    Millar, D.P.2
  • 44
    • 0029008807 scopus 로고
    • Yeast TATA binding protein interaction with DNA: Fluorescence determination of oligomeric state, equilibrium binding, on-rate, and dissociation kinetics
    • 44. Perez-Howard GM, Weil PA, Beechem JM: Yeast TATA binding protein interaction with DNA: fluorescence determination of oligomeric state, equilibrium binding, on-rate, and dissociation kinetics. Biochemistry 1995, 34:8005-8017. A comprehensive study of TBP-DNA interactions based on measurements of fluorescence signals derived from both intrinsic tryptophan residues and extrinsic probes attached to DNA.
    • (1995) Biochemistry , vol.34 , pp. 8005-8017
    • Perez-Howard, G.M.1    Weil, P.A.2    Beechem, J.M.3
  • 45
    • 0028827717 scopus 로고
    • Interaction between the Escherichia coli regulatory protein TyrR and DNA: A fluorescence footprinting study
    • 45. Bailey M, Hagmar P, Millar DP, Davidson BE, Tong G, Haralambidis J, Sawyer WH: Interaction between the Escherichia coli regulatory protein TyrR and DNA: a fluorescence footprinting study. Biochemistry 1995, 34:15802-15812. This paper demonstrates that the time-resolved fluorescence properties of a fluorescein probe attached to DNA can be used to distinguish between the different DNA footprints associated with the dimeric and hexameric forms of the TyrR repressor protein.
    • (1995) Biochemistry , vol.34 , pp. 15802-15812
    • Bailey, M.1    Hagmar, P.2    Millar, D.P.3    Davidson, B.E.4    Tong, G.5    Haralambidis, J.6    Sawyer, W.H.7
  • 46
    • 0025790430 scopus 로고
    • Interaction of DNA with the klenow fragment of DNA polymerase I studied by time-resolved fluorescence spectroscopy
    • 46. Guest CR, Hochstrasser RA, Dupuy C, Allen DJ, Benkovic SJ, Millar DP: Interaction of DNA with the Klenow fragment of DNA polymerase I studied by time-resolved fluorescence spectroscopy. Biochemistry 1991, 30:8759-8770.
    • (1991) Biochemistry , vol.30 , pp. 8759-8770
    • Guest, C.R.1    Hochstrasser, R.A.2    Dupuy, C.3    Allen, D.J.4    Benkovic, S.J.5    Millar, D.P.6


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