메뉴 건너뛰기




Volumn 18, Issue 9, 1999, Pages 2631-2637

Structure and interactions of the translation initiation factor eIF1

Author keywords

eIF1; Structure; Translation initiation

Indexed keywords

INITIATION FACTOR; MUTANT PROTEIN;

EID: 0033522507     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.9.2631     Document Type: Article
Times cited : (111)

References (59)
  • 1
    • 0030755124 scopus 로고    scopus 로고
    • Structural basis of the RNA binding specificity of human U1A protein
    • Allain, F.H., Howe, P.W., Neuhaus, D. and Varani, G. (1997) Structural basis of the RNA binding specificity of human U1A protein. EMBO J., 16, 5764-5772.
    • (1997) EMBO J. , vol.16 , pp. 5764-5772
    • Allain, F.H.1    Howe, P.W.2    Neuhaus, D.3    Varani, G.4
  • 2
    • 0031033314 scopus 로고    scopus 로고
    • Conservation and diversity of eukaryotic translation initiation factor eIF3
    • Asano, K., Kinzy, T.G., Merrick, W.C. and Hershey, J.W.B. (1997) Conservation and diversity of eukaryotic translation initiation factor eIF3. J. Biol. Chem., 272, 1101-1109.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1101-1109
    • Asano, K.1    Kinzy, T.G.2    Merrick, W.C.3    Hershey, J.W.B.4
  • 3
    • 0032541138 scopus 로고    scopus 로고
    • Complex formation by all five homologues of mammalian translation initiation factor 3 subunits from yeast Saccharomyces cerevisiae
    • Asano, K., Phan, L., Anderson, J. and Hinnebusch, A.G. (1998) Complex formation by all five homologues of mammalian translation initiation factor 3 subunits from yeast Saccharomyces cerevisiae. J. Biol. Chem., 273, 18573-18585.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18573-18585
    • Asano, K.1    Phan, L.2    Anderson, J.3    Hinnebusch, A.G.4
  • 4
    • 0002934112 scopus 로고
    • Structure determination from NMR data I: Analysis of NMR data
    • Roberts, G.C.K. (ed.), IRL Press, Oxford, UK
    • Barsukov, I.L. and Lian, L.-Y. (1993) Structure determination from NMR data I: analysis of NMR data. In Roberts, G.C.K. (ed.), NMR of Macromolecules: A Practical Approach. IRL Press, Oxford, UK, pp. 315-357.
    • (1993) NMR of Macromolecules: A Practical Approach , pp. 315-357
    • Barsukov, I.L.1    Lian, L.-Y.2
  • 5
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological molecules
    • Bartels, C., Xia, T., Billeter, M., Güntert, P. and Wüthrich, K. (1995) The program XEASY for computer-supported NMR spectral analysis of biological molecules. J. Biomol. NMR, 6, 1-10.
    • (1995) J. Biomol. NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 8
    • 0020494571 scopus 로고
    • Protein synthesis initiation factors from human HeLa cells and rabbit reticulocytes are similar: Comparison of protein structure, activities and immunological properties
    • Brown-Luedi, M.L., Meyer, L.J., Milburn, S.C., Yau, P.M.P., Corbett, S. and Hershey, J.W.B. (1982) Protein synthesis initiation factors from human HeLa cells and rabbit reticulocytes are similar: comparison of protein structure, activities and immunological properties. Biochemistry, 21, 4202-4206.
    • (1982) Biochemistry , vol.21 , pp. 4202-4206
    • Brown-Luedi, M.L.1    Meyer, L.J.2    Milburn, S.C.3    Yau, P.M.P.4    Corbett, S.5    Hershey, J.W.B.6
  • 10
    • 0029041105 scopus 로고
    • NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5
    • Bycroft, M., Grünert, S., Murzin, A.G., Proctor, M. and St. Johnston, D. (1995) NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5. EMBO J., 14, 3563-3571.
    • (1995) EMBO J. , vol.14 , pp. 3563-3571
    • Bycroft, M.1    Grünert, S.2    Murzin, A.G.3    Proctor, M.4    St. Johnston, D.5
  • 12
    • 0025234838 scopus 로고
    • Genetic characterization of the Saccharomyces cerevisiae translation initiation suppressors sui1, sui2 and SUI3 and their effects on HIS4 expression
    • Castilho-Valavicius, B., Yoon, H. and Donahue, T.F. (1990) Genetic characterization of the Saccharomyces cerevisiae translation initiation suppressors sui1, sui2 and SUI3 and their effects on HIS4 expression. Genetics, 124, 483-495.
    • (1990) Genetics , vol.124 , pp. 483-495
    • Castilho-Valavicius, B.1    Yoon, H.2    Donahue, T.F.3
  • 13
    • 0031935826 scopus 로고    scopus 로고
    • The mof2/sui1 protein is a general monitor of translational accuracy
    • Cui, Y., Dinman, J.D., Kinzy, T.G. and Peltz, S.W. (1998) The mof2/sui1 protein is a general monitor of translational accuracy. Mol. Cell. Biol., 18, 1506-1516.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1506-1516
    • Cui, Y.1    Dinman, J.D.2    Kinzy, T.G.3    Peltz, S.W.4
  • 14
    • 0027053207 scopus 로고
    • On the multiple simultaneous superposition of molecular structures by rigid body transformation
    • Diamond, R. (1992) On the multiple simultaneous superposition of molecular structures by rigid body transformation. Protein Sci., 1, 1279-1287.
    • (1992) Protein Sci. , vol.1 , pp. 1279-1287
    • Diamond, R.1
  • 15
    • 0028282555 scopus 로고
    • 15N NMR relaxation
    • 15N NMR relaxation. Biochemistry, 33, 5984-6003.
    • (1994) Biochemistry , vol.33 , pp. 5984-6003
    • Farrow, N.A.1
  • 16
    • 0028773130 scopus 로고
    • Structure of a soluble, glycosylated form of the human complement regulatory protein CD59
    • Fletcher, C.M., Harrison, R.A., Lachmann, P.J. and Neuhaus, D. (1994) Structure of a soluble, glycosylated form of the human complement regulatory protein CD59. Structure, 2, 185-199.
    • (1994) Structure , vol.2 , pp. 185-199
    • Fletcher, C.M.1    Harrison, R.A.2    Lachmann, P.J.3    Neuhaus, D.4
  • 17
    • 0001083043 scopus 로고    scopus 로고
    • Treatment of NOE constraints involving equivalent or non-stereoassigned protons in calculations of biomacromolecular structures
    • Fletcher, C.M., Jones, D.M.N., Diamond, R. and Neuhaus, D. (1996) Treatment of NOE constraints involving equivalent or non-stereoassigned protons in calculations of biomacromolecular structures. J. Biomol. NMR, 8, 292-310.
    • (1996) J. Biomol. NMR , vol.8 , pp. 292-310
    • Fletcher, C.M.1    Jones, D.M.N.2    Diamond, R.3    Neuhaus, D.4
  • 18
    • 9444245493 scopus 로고
    • Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR
    • Grzesiek, S. and Bax, A. (1992) Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR. J. Am. Chem. Soc., 114, 6291-6293.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 21
    • 0025964204 scopus 로고
    • RNA binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins
    • Hoffman, D.W., Query, C.C., Golden, B.L., White, S.W. and Keene, J.D. (1991) RNA binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins. Proc. Natl Acad. Sci. USA, 88, 2495-2499.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 2495-2499
    • Hoffman, D.W.1    Query, C.C.2    Golden, B.L.3    White, S.W.4    Keene, J.D.5
  • 22
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. and Sander, C. (1993) Protein structure comparison by alignment of distance matrices. J. Mol. Biol., 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 23
    • 0026662288 scopus 로고
    • Human epidermal growth factor: High resolution solution structure and comparison with transforming growth factor α
    • Hommel, U., Harvey, T.S., Driscoll, P.C. and Campbell, I.D. (1992) Human epidermal growth factor: high resolution solution structure and comparison with transforming growth factor α. J. Mol. Biol., 227, 271-282.
    • (1992) J. Mol. Biol. , vol.227 , pp. 271-282
    • Hommel, U.1    Harvey, T.S.2    Driscoll, P.C.3    Campbell, I.D.4
  • 25
    • 0002568139 scopus 로고    scopus 로고
    • A comparative view of initiation site selection mechanisms
    • Hershey, J.W.B., Mathews, M.B. and Sonenberg, N. (eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Jackson, R.J. (1996) A comparative view of initiation site selection mechanisms. In Hershey, J.W.B., Mathews, M.B. and Sonenberg, N. (eds), Translational Control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 71-112.
    • (1996) Translational Control , pp. 71-112
    • Jackson, R.J.1
  • 27
    • 0029058994 scopus 로고
    • Structure of the dsRNA binding domain of E.coli RNase II
    • Kharrat, A., Macias, M.J., Gibson, T.J., Nilges, M. and Pastore, A. (1995) Structure of the dsRNA binding domain of E.coli RNase II. EMBO J., 14, 3572-3584.
    • (1995) EMBO J. , vol.14 , pp. 3572-3584
    • Kharrat, A.1    Macias, M.J.2    Gibson, T.J.3    Nilges, M.4    Pastore, A.5
  • 28
    • 0024546509 scopus 로고
    • The scanning model for translation: An update
    • Kozak, M. (1989) The scanning model for translation: an update. J. Cell Biol., 108, 229-241.
    • (1989) J. Cell Biol. , vol.108 , pp. 229-241
    • Kozak, M.1
  • 29
    • 0026244229 scopus 로고
    • Molscript - A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (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.J.1
  • 30
    • 58149365834 scopus 로고
    • Adiabatic pulses for wideband inversion and broadband decoupling
    • Kupce, E. and Freeman, R. (1995) Adiabatic pulses for wideband inversion and broadband decoupling. J. Magn. Reson., A115, 273-276.
    • (1995) J. Magn. Reson. , vol.A115 , pp. 273-276
    • Kupce, E.1    Freeman, R.2
  • 31
    • 0031915895 scopus 로고    scopus 로고
    • Universally conserved translation initiation factors
    • Kyrpides, N.C. and Woese, C.R. (1998) Universally conserved translation initiation factors. Proc. Natl Acad. Sci. USA, 95, 224-228.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 224-228
    • Kyrpides, N.C.1    Woese, C.R.2
  • 32
    • 10244251532 scopus 로고    scopus 로고
    • Identification of a human mitotic checkpoint gene: HsMAD2
    • Li, Y. and Benezra, R. (1996) Identification of a human mitotic checkpoint gene: HsMAD2. Science, 274, 246-248.
    • (1996) Science , vol.274 , pp. 246-248
    • Li, Y.1    Benezra, R.2
  • 33
    • 0028203301 scopus 로고
    • Crystal structure of the ribosomal protein S6 from Thermus thermophilus
    • Lindahl, M. et al. (1994) Crystal structure of the ribosomal protein S6 from Thermus thermophilus. EMBO J., 13, 1249-1254.
    • (1994) EMBO J. , vol.13 , pp. 1249-1254
    • Lindahl, M.1
  • 34
    • 0028838717 scopus 로고
    • Threading a database of protein cores
    • Madej, T., Gibrat, J.-F. and Bryant, S.H. (1995) Threading a database of protein cores. Proteins, 23, 356-369.
    • (1995) Proteins , vol.23 , pp. 356-369
    • Madej, T.1    Gibrat, J.-F.2    Bryant, S.H.3
  • 35
    • 0029688079 scopus 로고    scopus 로고
    • A sensitive HN(CA)CO experiment for deuterated proteins
    • Matsuo, H., Li, H. and Wagner, G. (1996) A sensitive HN(CA)CO experiment for deuterated proteins. J. Magn. Reson., B110, 112-115.
    • (1996) J. Magn. Reson. , vol.B110 , pp. 112-115
    • Matsuo, H.1    Li, H.2    Wagner, G.3
  • 36
    • 0002523042 scopus 로고    scopus 로고
    • The pathway and mechanism of eukaryotic protein synthesis
    • Hershey, J.W.B., Mathews, M.B. and Sonenberg, N. (eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Merrick, W.C. and Hershey, J.W.B. (1996) The pathway and mechanism of eukaryotic protein synthesis. In Hershey, J.W.B., Mathews, M.B. and Sonenberg, N. (eds), Translational Control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 31-69.
    • (1996) Translational Control , pp. 31-69
    • Merrick, W.C.1    Hershey, J.W.B.2
  • 37
    • 0029988528 scopus 로고    scopus 로고
    • Three dimensional structure and stability of the KH domain: Molecular insights into the fragile X syndrome
    • Musco, G., Stier, G., Joseph, C., Castiglione Morelli, M.A., Nilges, M., Gibson, T.J. and Pastore, A. (1996) Three dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome. Cell, 85, 237-245.
    • (1996) Cell , vol.85 , pp. 237-245
    • Musco, G.1    Stier, G.2    Joseph, C.3    Castiglione Morelli, M.A.4    Nilges, M.5    Gibson, T.J.6    Pastore, A.7
  • 38
    • 0032530310 scopus 로고    scopus 로고
    • Structure of the double stranded RNA binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA mediated activation
    • Nanduri, S., Carpick, B.W., Yang, Y., Williams, B.R. and Qin, J. (1998) Structure of the double stranded RNA binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA mediated activation. EMBO J., 17, 5458-5465.
    • (1998) EMBO J. , vol.17 , pp. 5458-5465
    • Nanduri, S.1    Carpick, B.W.2    Yang, Y.3    Williams, B.R.4    Qin, J.5
  • 39
    • 0028568642 scopus 로고
    • Purified yeast translational initiation factor eIF3 is an RNA binding protein complex that contains the PRT1 protein
    • Naranda, T., MacMillan, S.E. and Hershey, J.W.B. (1994) Purified yeast translational initiation factor eIF3 is an RNA binding protein complex that contains the PRT1 protein. J. Biol. Chem., 269, 32286-32292.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32286-32292
    • Naranda, T.1    MacMillan, S.E.2    Hershey, J.W.B.3
  • 40
    • 0030002818 scopus 로고    scopus 로고
    • SUI1/p16 is required for the activity of eukaryotic translation initiation factor 3 in Saccharomyces cerevisiae
    • Naranda, T., MacMillan, S.E., Donahue, T.F. and Hershey, J.W.B. (1996) SUI1/p16 is required for the activity of eukaryotic translation initiation factor 3 in Saccharomyces cerevisiae. Mol. Cell. Biol., 16, 2307-2313.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2307-2313
    • Naranda, T.1    MacMillan, S.E.2    Donahue, T.F.3    Hershey, J.W.B.4
  • 41
    • 0026672305 scopus 로고
    • NMR determination of residual structure in a urea denatured protein, the 434 repressor
    • Neri, D., Billeter, M., Wider, G. and Wüthrich, K. (1992) NMR determination of residual structure in a urea denatured protein, the 434 repressor. Science, 257, 1559-1563.
    • (1992) Science , vol.257 , pp. 1559-1563
    • Neri, D.1    Billeter, M.2    Wider, G.3    Wüthrich, K.4
  • 42
    • 0026746675 scopus 로고
    • 1H nuclear magnetic resonance spectroscopy: A zinc-finger with a third strand of β-sheet
    • 1H nuclear magnetic resonance spectroscopy: a zinc-finger with a third strand of β-sheet. J. Mol. Biol., 228, 637-651.
    • (1992) J. Mol. Biol. , vol.228 , pp. 637-651
    • Neuhaus, D.1    Nakaseko, Y.2    Schwabe, J.W.R.3    Klug, A.4
  • 43
    • 0028907436 scopus 로고
    • Calculation of protein structures with ambiguous distance restraints. Automated assignment of ambiguous NOE crosspeaks and disulphide connectivities
    • Nilges, M. (1995) Calculation of protein structures with ambiguous distance restraints. Automated assignment of ambiguous NOE crosspeaks and disulphide connectivities. J. Mol. Biol., 245, 645-660.
    • (1995) J. Mol. Biol. , vol.245 , pp. 645-660
    • Nilges, M.1
  • 44
    • 0028004607 scopus 로고
    • Crystal structure at 1.92 Å resolution of the RNA binding domain of the U1A spliceosomal protein complexed with an RNA hairpin
    • Oubridge,C., Ito, N., Evans, P.R., Teo, C.H. and Nagai, K. (1994) Crystal structure at 1.92 Å resolution of the RNA binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Nature, 372, 432-438.
    • (1994) Nature , vol.372 , pp. 432-438
    • Oubridge, C.1    Ito, N.2    Evans, P.R.3    Teo, C.H.4    Nagai, K.5
  • 45
    • 0032572776 scopus 로고    scopus 로고
    • Eukaryotic ribosomes require eIFs 1 and IA to locate initiation codons
    • Pestova, T.V., Borukhov, S.I. and Hellen, C.U.T. (1998) Eukaryotic ribosomes require eIFs 1 and IA to locate initiation codons. Nature, 394, 854-859.
    • (1998) Nature , vol.394 , pp. 854-859
    • Pestova, T.V.1    Borukhov, S.I.2    Hellen, C.U.T.3
  • 46
    • 0031876171 scopus 로고    scopus 로고
    • Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5
    • Phan, L., Zhang, X., Asano, K., Anderson, J., Vornlocher, H.-P., Greenberg, J.R., Qin, J. and Hinnebusch, A.G. (1998) Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5. Mol. Cell. Biol., 18, 4935-4946.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4935-4946
    • Phan, L.1    Zhang, X.2    Asano, K.3    Anderson, J.4    Vornlocher, H.-P.5    Greenberg, J.R.6    Qin, J.7    Hinnebusch, A.G.8
  • 47
    • 0026687213 scopus 로고
    • The structure of ribosomal protein S5 reveals sites of interaction with 16S rRNA
    • Ramakrishnan, V. and White, S.W. (1992) The structure of ribosomal protein S5 reveals sites of interaction with 16S rRNA. Nature, 358, 768-771.
    • (1992) Nature , vol.358 , pp. 768-771
    • Ramakrishnan, V.1    White, S.W.2
  • 48
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson, J.S. (1981) The anatomy and taxonomy of protein structure. Adv. Protein Chem., 34, 167-339.
    • (1981) Adv. Protein Chem. , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 49
    • 0032535613 scopus 로고    scopus 로고
    • Molecular basis of double stranded RNA-protein interactions: Structure of a dsRNA binding domain complexed with dsRNA
    • Ryter, J.M. and Schultz, S.C. (1998) Molecular basis of double stranded RNA-protein interactions: structure of a dsRNA binding domain complexed with dsRNA. EMBO J., 17, 7505-7513.
    • (1998) EMBO J. , vol.17 , pp. 7505-7513
    • Ryter, J.M.1    Schultz, S.C.2
  • 50
    • 0017701040 scopus 로고    scopus 로고
    • Initiation of mammalian protein synthesis. I. Purification and characterization of seven initiation factors
    • Schreier, M.H., Erni, B. and Staehelin, T. (1997) Initiation of mammalian protein synthesis. I. Purification and characterization of seven initiation factors. J. Mol. Biol., 116, 727-753.
    • (1997) J. Mol. Biol. , vol.116 , pp. 727-753
    • Schreier, M.H.1    Erni, B.2    Staehelin, T.3
  • 51
    • 0030207171 scopus 로고    scopus 로고
    • An optimized 3D NOESY-HSQC
    • Talluri, S. and Wagner, G. (1996) An optimized 3D NOESY-HSQC. J. Magn. Reson., A112, 200-205.
    • (1996) J. Magn. Reson. , vol.A112 , pp. 200-205
    • Talluri, S.1    Wagner, G.2
  • 52
    • 0017707116 scopus 로고
    • Initiation of mammalian protein synthesis. II. The assembly of the initiation complex with purified initiation factors
    • Trachsel, H., Erni, B., Schreier, M.H. and Staehelin, T. (1977) Initiation of mammalian protein synthesis. II. The assembly of the initiation complex with purified initiation factors. J. Mol. Biol., 116, 755-768.
    • (1977) J. Mol. Biol. , vol.116 , pp. 755-768
    • Trachsel, H.1    Erni, B.2    Schreier, M.H.3    Staehelin, T.4
  • 53
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest neighbour effects
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest neighbour effects. J. Biomol. NMR, 5, 67-81.
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 54
    • 0027934203 scopus 로고
    • An Escherichia coli protein consisting of a domain homologous to FK506-binding proteins (FKBP) and a new metal binding motif
    • Wülfing, C., Lombardero, J. and Plückthun, A. (1994) An Escherichia coli protein consisting of a domain homologous to FK506-binding proteins (FKBP) and a new metal binding motif. J. Biol. Chem., 269, 2895-2901.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2895-2901
    • Wülfing, C.1    Lombardero, J.2    Plückthun, A.3
  • 58
    • 0028541866 scopus 로고
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced sensitivity pulsed field gradient NMR techniques
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced sensitivity pulsed field gradient NMR techniques. J. Biomol. NMR, 4, 845-858.
    • (1994) J. Biomol. NMR , vol.4 , pp. 845-858
    • Zhang, O.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.