메뉴 건너뛰기




Volumn 10, Issue 1, 2000, Pages 102-109

Recognition of distorted DNA structures by HMG domains

Author keywords

[No Author keywords available]

Indexed keywords

CURVED DNA; DNA; DNA BINDING PROTEIN; HIGH MOBILITY GROUP PROTEIN;

EID: 0033982040     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(99)00056-1     Document Type: Review
Times cited : (84)

References (49)
  • 4
    • 0029563931 scopus 로고
    • Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronuclear three and four dimensional NMR spectroscopy
    • Hardman C.H., Broadhurst R.H., Raine A.R.C., Grasser K.D., Thomas J.O., Laue E.D. Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronuclear three and four dimensional NMR spectroscopy. Biochemistry. 34:1995;16596-16607.
    • (1995) Biochemistry , vol.34 , pp. 16596-16607
    • Hardman, C.H.1    Broadhurst, R.H.2    Raine, A.R.C.3    Grasser, K.D.4    Thomas, J.O.5    Laue, E.D.6
  • 5
    • 0029131298 scopus 로고
    • Structural basis for DNA bending by the architectural transcription factor LEF-1
    • Love J.J., Xiang L., Case D.A., Giese K., Grosschedl R., Wright P.E. Structural basis for DNA bending by the architectural transcription factor LEF-1. Nature. 376:1995;791-795.
    • (1995) Nature , vol.376 , pp. 791-795
    • Love, J.J.1    Xiang, L.2    Case, D.A.3    Giese, K.4    Grosschedl, R.5    Wright, P.E.6
  • 6
  • 7
    • 0029075461 scopus 로고
    • Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex
    • Werner M.H., Huth J.R., Gronenborn A.M., Clore G.M. Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex. Cell. 81:1995;705-714.
    • (1995) Cell , vol.81 , pp. 705-714
    • Werner, M.H.1    Huth, J.R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 8
    • 0024584528 scopus 로고
    • Specific recognition of cruciform DNA by nuclear protein HMG1
    • Bianchi M.E., Beltrame M., Paonessa G. Specific recognition of cruciform DNA by nuclear protein HMG1. Science. 243:1989;1056-1059.
    • (1989) Science , vol.243 , pp. 1056-1059
    • Bianchi, M.E.1    Beltrame, M.2    Paonessa, G.3
  • 9
    • 0024401923 scopus 로고
    • High mobility group protein 1 preferentially conserves torsion in negatively supercoiled DNA
    • Sheflin L.G., Spaulding S.W. High mobility group protein 1 preferentially conserves torsion in negatively supercoiled DNA. Biochemistry. 28:1989;5658-5664.
    • (1989) Biochemistry , vol.28 , pp. 5658-5664
    • Sheflin, L.G.1    Spaulding, S.W.2
  • 10
    • 0026569275 scopus 로고
    • Specific binding of chromosomal protein HMG1 to DNA damaged by the anticancer drug cisplatin
    • Pil P.M., Lippard S.J. Specific binding of chromosomal protein HMG1 to DNA damaged by the anticancer drug cisplatin. Science. 256:1992;234-237.
    • (1992) Science , vol.256 , pp. 234-237
    • Pil, P.M.1    Lippard, S.J.2
  • 11
    • 0027156630 scopus 로고
    • The specific interactions of HMG1 and 2 with negatively supercoiled DNA are modulated by their acidic C-terminal domains and involve cysteine residues in their HMG1/2 boxes
    • Sheflin L.G., Fucile N.W., Spaulding S.W. The specific interactions of HMG1 and 2 with negatively supercoiled DNA are modulated by their acidic C-terminal domains and involve cysteine residues in their HMG1/2 boxes. Biochemistry. 32:1993;3238-3248.
    • (1993) Biochemistry , vol.32 , pp. 3238-3248
    • Sheflin, L.G.1    Fucile, N.W.2    Spaulding, S.W.3
  • 12
    • 0031566959 scopus 로고    scopus 로고
    • The acidic tail of the high mobility group protein HMG-D modulates the structural specificity of DNA binding
    • Payet D., Travers A. The acidic tail of the high mobility group protein HMG-D modulates the structural specificity of DNA binding. J Mol Biol. 266:1997;66-75.
    • (1997) J Mol Biol , vol.266 , pp. 66-75
    • Payet, D.1    Travers, A.2
  • 13
    • 0032548929 scopus 로고    scopus 로고
    • Determinants of DNA binding and bending by the Saccharomyces cerevisiae high mobility group protein NHP6A that are important for its biological activities. Role of the unique N terminus and putative intercalating methionine
    • Yen Y.M., Wong B., Johnson R.C. Determinants of DNA binding and bending by the Saccharomyces cerevisiae high mobility group protein NHP6A that are important for its biological activities. Role of the unique N terminus and putative intercalating methionine. J Biol Chem. 273:1998;4424-4435.
    • (1998) J Biol Chem , vol.273 , pp. 4424-4435
    • Yen, Y.M.1    Wong, B.2    Johnson, R.C.3
  • 14
    • 0033578010 scopus 로고    scopus 로고
    • Basis of cis-platin modified DNA by high-mobility-group proteins
    • The authors describe the crystal structure of the A domain of HMG1 complexed with cis-platinated DNA; this definitive structure resolves some controversial issues.
    • Ohndorf U-M., Rould M.A., He Q., Pabo C., Lippard S.J. Basis of cis-platin modified DNA by high-mobility-group proteins. Nature. 399:1999;708-712. The authors describe the crystal structure of the A domain of HMG1 complexed with cis-platinated DNA; this definitive structure resolves some controversial issues.
    • (1999) Nature , vol.399 , pp. 708-712
    • Ohndorf, U.-M.1    Rould, M.A.2    He, Q.3    Pabo, C.4    Lippard, S.J.5
  • 15
    • 13044260240 scopus 로고    scopus 로고
    • Co-crystallization and preliminary crystallographic analysis of the high mobility group domain of HMG-D bound to DNA
    • Murphy F.V. IV, Sehy J.V., Dow L.K., Gao Y.G., Churchill M.E.A. Co-crystallization and preliminary crystallographic analysis of the high mobility group domain of HMG-D bound to DNA. Acta Crystallogr. D55:1999;1594-1597.
    • (1999) Acta Crystallogr , vol.55 , pp. 1594-1597
    • Murphy F.V. IV1    Sehy, J.V.2    Dow, L.K.3    Gao, Y.G.4    Churchill, M.E.A.5
  • 16
    • 0032006926 scopus 로고    scopus 로고
    • Structure prediction of a complex between the chromosomal protein HMG-D and DNA
    • Balaeff A., Churchill M.E., Schulten K. Structure prediction of a complex between the chromosomal protein HMG-D and DNA. Proteins. 30:1998;113-135.
    • (1998) Proteins , vol.30 , pp. 113-135
    • Balaeff, A.1    Churchill, M.E.2    Schulten, K.3
  • 17
    • 0033522480 scopus 로고    scopus 로고
    • Solution structure of the HMG protein NHP6A and its interaction with DNA reveals the structural determinants for non-sequence-specific binding
    • This NMR study of the NHP6A-DNA complex identified specific intramolecular contacts as a basis for non-sequence-specific binding by the abundant chromosomal HMG domain proteins.
    • Allain F.H., Yen Y.M., Masse J.E., Schultze P., Dieckmann T., Johnson R.C., Feigon J. Solution structure of the HMG protein NHP6A and its interaction with DNA reveals the structural determinants for non-sequence-specific binding. EMBO J. 18:1999;2563-2579. This NMR study of the NHP6A-DNA complex identified specific intramolecular contacts as a basis for non-sequence-specific binding by the abundant chromosomal HMG domain proteins.
    • (1999) EMBO J , vol.18 , pp. 2563-2579
    • Allain, F.H.1    Yen, Y.M.2    Masse, J.E.3    Schultze, P.4    Dieckmann, T.5    Johnson, R.C.6    Feigon, J.7
  • 18
    • 0033584886 scopus 로고    scopus 로고
    • The recognition of distorted DNA structures by HMG-D - A footprinting and molecular modelling study
    • The authors demonstrated asymmetric binding of HMG-D to a DNA bulge and identified Val34 and Thr35 in the helix I-helix II loop as important determinants of DNA binding and bending.
    • Payet D., Hillisch A., Lowe N., Diekmann S., Travers A. The recognition of distorted DNA structures by HMG-D - a footprinting and molecular modelling study. J Mol Biol. 294:1999;79-91. The authors demonstrated asymmetric binding of HMG-D to a DNA bulge and identified Val34 and Thr35 in the helix I-helix II loop as important determinants of DNA binding and bending.
    • (1999) J Mol Biol , vol.294 , pp. 79-91
    • Payet, D.1    Hillisch, A.2    Lowe, N.3    Diekmann, S.4    Travers, A.5
  • 19
    • 0027142992 scopus 로고
    • The SRY high-mobility-group box recognises DNA by partial intercalation in the minor groove: A topological mechanism of sequence specificity
    • King C-Y., Weiss M.A. The SRY high-mobility-group box recognises DNA by partial intercalation in the minor groove: a topological mechanism of sequence specificity. Proc Natl Acad Sci USA. 90:1993;11990-11994.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11990-11994
    • King, C.-Y.1    Weiss, M.A.2
  • 20
    • 0029070956 scopus 로고
    • The HMG-1 box protein family: Classification and functional relationships
    • Baxevanis A.D., Landsman D. The HMG-1 box protein family: classification and functional relationships. Nucleic Acids Res. 23:1995;1604-1613.
    • (1995) Nucleic Acids Res , vol.23 , pp. 1604-1613
    • Baxevanis, A.D.1    Landsman, D.2
  • 21
    • 0029103236 scopus 로고
    • Reading the minor groove
    • Travers A.A. Reading the minor groove. Nat Struct Biol. 2:1995;615-618.
    • (1995) Nat Struct Biol , vol.2 , pp. 615-618
    • Travers, A.A.1
  • 22
    • 0028950413 scopus 로고
    • HMG-D is an architecture-specific protein that preferentially binds to DNA containing the dinucleotide TG
    • Churchill M.E.A., Jones D.N.M., Glaser T., Hefner H., Searles M.A., Travers A.A. HMG-D is an architecture-specific protein that preferentially binds to DNA containing the dinucleotide TG. EMBO J. 14:1995;1264-1275.
    • (1995) EMBO J , vol.14 , pp. 1264-1275
    • Churchill, M.E.A.1    Jones, D.N.M.2    Glaser, T.3    Hefner, H.4    Searles, M.A.5    Travers, A.A.6
  • 23
    • 0030000761 scopus 로고    scopus 로고
    • The DNA bend angle and binding affinity of an HMG box increased by the presence of short terminal arms
    • Lnenicek-Allen M., Read C.M., Crane-Robinson C. The DNA bend angle and binding affinity of an HMG box increased by the presence of short terminal arms. Nucleic Acids Res. 24:1996;1047-1051.
    • (1996) Nucleic Acids Res , vol.24 , pp. 1047-1051
    • Lnenicek-Allen, M.1    Read, C.M.2    Crane-Robinson, C.3
  • 24
    • 0028355759 scopus 로고
    • Mutational analysis of the DNA binding domain A of chromosomal protein HMG1
    • Falciola L., Murchie A.I., Lilley D.M.J., Bianchi M. Mutational analysis of the DNA binding domain A of chromosomal protein HMG1. Nucleic Acids Res. 22:1994;285-292.
    • (1994) Nucleic Acids Res , vol.22 , pp. 285-292
    • Falciola, L.1    Murchie, A.I.2    Lilley, D.M.J.3    Bianchi, M.4
  • 25
    • 0033554438 scopus 로고    scopus 로고
    • DNA bending induced by high mobility group proteins studied by fluorescence resonance energy transfer (FRET)
    • This study demonstrates that the DNA bending angle induced by a variety of HMG B-type domains upon binding bulged DNA is essentially the same. The reported values sharply disagree with the conclusions of Heyduk et al. [27].
    • Lorenz M., Hillisch A., Payet D., Buttinelli M., Travers A., Diekmann S. DNA bending induced by high mobility group proteins studied by fluorescence resonance energy transfer (FRET). Biochemistry. 38:1999;12150-12158. This study demonstrates that the DNA bending angle induced by a variety of HMG B-type domains upon binding bulged DNA is essentially the same. The reported values sharply disagree with the conclusions of Heyduk et al. [27].
    • (1999) Biochemistry , vol.38 , pp. 12150-12158
    • Lorenz, M.1    Hillisch, A.2    Payet, D.3    Buttinelli, M.4    Travers, A.5    Diekmann, S.6
  • 26
    • 0033617209 scopus 로고    scopus 로고
    • Structural and kinetic studies of a cisplatin-modified DNA icosamer binding to HMG1 domain B
    • The authors contrast the bending induced by the B domain of HMG1 upon binding to cis-platinated DNA with that revealed by the crystal structure of the HMG1 A domain bound to a similar ligand.
    • Jamieson E.R., Jacobson M.P., Barnes C.M., Chow C.S., Lippard S.J. Structural and kinetic studies of a cisplatin-modified DNA icosamer binding to HMG1 domain B. J Biol Chem. 274:1999;12346-12354. The authors contrast the bending induced by the B domain of HMG1 upon binding to cis-platinated DNA with that revealed by the crystal structure of the HMG1 A domain bound to a similar ligand.
    • (1999) J Biol Chem , vol.274 , pp. 12346-12354
    • Jamieson, E.R.1    Jacobson, M.P.2    Barnes, C.M.3    Chow, C.S.4    Lippard, S.J.5
  • 27
    • 0030877452 scopus 로고    scopus 로고
    • Conformational changes of DNA induced by binding of Chironomus high mobility group protein 1a (cHMG1a). Regions flanking an HMG1 box domain do not influence the bend angle of the DNA
    • Heyduk E., Heyduk T., Claus P., Wisniewski J.R. Conformational changes of DNA induced by binding of Chironomus high mobility group protein 1a (cHMG1a). Regions flanking an HMG1 box domain do not influence the bend angle of the DNA. J Biol Chem. 272:1997;19763-19770.
    • (1997) J Biol Chem , vol.272 , pp. 19763-19770
    • Heyduk, E.1    Heyduk, T.2    Claus, P.3    Wisniewski, J.R.4
  • 28
    • 0040602752 scopus 로고    scopus 로고
    • HMG1 proteins from evolutionary distant organisms distort B-DNA conformation in similar way
    • Wisniewski J.R., Krohn N.M., Heyduk E., Grasser K.D., Heyduk T. HMG1 proteins from evolutionary distant organisms distort B-DNA conformation in similar way. Biochim Biophys Acta. 1447:1999;25-34.
    • (1999) Biochim Biophys Acta , vol.1447 , pp. 25-34
    • Wisniewski, J.R.1    Krohn, N.M.2    Heyduk, E.3    Grasser, K.D.4    Heyduk, T.5
  • 29
    • 0033064093 scopus 로고    scopus 로고
    • Interactions of high mobility group proteins with DNA and chromatin
    • Churchill M.E.A., Changela A., Dow L.K., Krieg A.J. Interactions of high mobility group proteins with DNA and chromatin. Methods Enzymol. 304:1999;99-133.
    • (1999) Methods Enzymol , vol.304 , pp. 99-133
    • Churchill, M.E.A.1    Changela, A.2    Dow, L.K.3    Krieg, A.J.4
  • 30
    • 0028999513 scopus 로고
    • Differences in the DNA-binding properties of the HMG-box domains of HMG1 and the sex-determining factor SRY
    • Teo S-H., Grasser K.D., Thomas J.O. Differences in the DNA-binding properties of the HMG-box domains of HMG1 and the sex-determining factor SRY. Eur J Biochem. 230:1995;943-950.
    • (1995) Eur J Biochem , vol.230 , pp. 943-950
    • Teo, S.-H.1    Grasser, K.D.2    Thomas, J.O.3
  • 32
    • 0027504913 scopus 로고
    • Crystal structure of a yeast TBP/TATA-box complex
    • Kim Y., Geiger J.H., Hahn S., Sigler P.B. Crystal structure of a yeast TBP/TATA-box complex. Nature. 365:1993;512-520.
    • (1993) Nature , vol.365 , pp. 512-520
    • Kim, Y.1    Geiger, J.H.2    Hahn, S.3    Sigler, P.B.4
  • 33
    • 0027483012 scopus 로고
    • Co-crystal structure of TBP recognizing the minor groove of a TATA element
    • Kim J.L., Nikolov D.B., Burley S.K. Co-crystal structure of TBP recognizing the minor groove of a TATA element. Nature. 365:1993;520-527.
    • (1993) Nature , vol.365 , pp. 520-527
    • Kim, J.L.1    Nikolov, D.B.2    Burley, S.K.3
  • 36
    • 0028921099 scopus 로고
    • An SRY mutation causing human sex reversal resolves a general mechanism of structure-specific DNA recognition: Application to the four-way junction
    • Peters R., King C.Y., Ukiyama E., Falsafi S., Donahue P.K., Weiss M.A. An SRY mutation causing human sex reversal resolves a general mechanism of structure-specific DNA recognition: application to the four-way junction. Biochemistry. 34:1995;4569-4576.
    • (1995) Biochemistry , vol.34 , pp. 4569-4576
    • Peters, R.1    King, C.Y.2    Ukiyama, E.3    Falsafi, S.4    Donahue, P.K.5    Weiss, M.A.6
  • 37
    • 0029278806 scopus 로고
    • Modifying the helical structure of DNA by design: Recruitment of an architecture-specific protein to an enforced DNA bend
    • Wolfe S.A., Ferentz A.E., Grantchavora V., Churchill M.E.A., Verdine G.L. Modifying the helical structure of DNA by design: recruitment of an architecture-specific protein to an enforced DNA bend. Chem Biol. 2:1995;213-221.
    • (1995) Chem Biol , vol.2 , pp. 213-221
    • Wolfe, S.A.1    Ferentz, A.E.2    Grantchavora, V.3    Churchill, M.E.A.4    Verdine, G.L.5
  • 38
    • 0041092343 scopus 로고    scopus 로고
    • HMG box proteins bind to four-way DNA junctions in their open conformation
    • Pohler J.R.G., Norman D.G., Bramham J., Bianchi M.E., Lilley D.M.J. HMG box proteins bind to four-way DNA junctions in their open conformation. EMBO J. 17:1998;817-826.
    • (1998) EMBO J , vol.17 , pp. 817-826
    • Pohler, J.R.G.1    Norman, D.G.2    Bramham, J.3    Bianchi, M.E.4    Lilley, D.M.J.5
  • 39
    • 0033607614 scopus 로고    scopus 로고
    • Structure-specific binding of the two tandem HMG boxes of HMG1 to four-way junction DNA is mediated by the A domain
    • This footprinting study of the binding of intact HMG1 and its isolated A and B domains to four-way junction DNA provides novel insights into the preference of the A domain for this structure.
    • Webb M., Thomas J.O. Structure-specific binding of the two tandem HMG boxes of HMG1 to four-way junction DNA is mediated by the A domain. J Mol Biol. 294:1999;373-387. This footprinting study of the binding of intact HMG1 and its isolated A and B domains to four-way junction DNA provides novel insights into the preference of the A domain for this structure.
    • (1999) J Mol Biol , vol.294 , pp. 373-387
    • Webb, M.1    Thomas, J.O.2
  • 40
    • 0029117147 scopus 로고
    • Two mutations in the HMG-box with very different structural consequences provide insights into the nature of binding to 4-way junction DNA
    • Teo S.H., Grasser K.D., Hardman C.H., Broadhurst R.W., Laue E.D., Thomas J.O. Two mutations in the HMG-box with very different structural consequences provide insights into the nature of binding to 4-way junction DNA. EMBO J. 14:1995;3844-3853.
    • (1995) EMBO J , vol.14 , pp. 3844-3853
    • Teo, S.H.1    Grasser, K.D.2    Hardman, C.H.3    Broadhurst, R.W.4    Laue, E.D.5    Thomas, J.O.6
  • 41
    • 0033562334 scopus 로고    scopus 로고
    • Directional binding of HMG-I(Y) on four-way junction DNA and the molecular basis for competitive binding with HMG-1 and histone H1
    • Hill D.A., Pedulla M.L., Reeves R. Directional binding of HMG-I(Y) on four-way junction DNA and the molecular basis for competitive binding with HMG-1 and histone H1. Nucleic Acids Res. 27:1999;2135-2144.
    • (1999) Nucleic Acids Res , vol.27 , pp. 2135-2144
    • Hill, D.A.1    Pedulla, M.L.2    Reeves, R.3
  • 42
    • 0033214062 scopus 로고    scopus 로고
    • The binding motif recognized by HU on both nicked and cruciform DNA
    • Kamashev D., Balandina A., Rouviere-Yaniv J. The binding motif recognized by HU on both nicked and cruciform DNA. EMBO J. 18:1999;5434-5444.
    • (1999) EMBO J , vol.18 , pp. 5434-5444
    • Kamashev, D.1    Balandina, A.2    Rouviere-Yaniv, J.3
  • 43
    • 0033052037 scopus 로고    scopus 로고
    • The lack of chromosomal protein Hmg1 does not disrupt cell growth but causes lethal hypoglycaemia in newborn mice
    • The first report of the physiological effects of deleting HMG1 from the genome.
    • Calogero S., Grassi F., Aguzzi A., Voigtlander T., Ferrier P., Ferrari S., Bianchi M.E. The lack of chromosomal protein Hmg1 does not disrupt cell growth but causes lethal hypoglycaemia in newborn mice. Nat Genet. 22:1999;276-280. The first report of the physiological effects of deleting HMG1 from the genome.
    • (1999) Nat Genet , vol.22 , pp. 276-280
    • Calogero, S.1    Grassi, F.2    Aguzzi, A.3    Voigtlander, T.4    Ferrier, P.5    Ferrari, S.6    Bianchi, M.E.7
  • 44
    • 0028226799 scopus 로고
    • DNA chaperones: A solution to a persistence problem?
    • Travers A.A., Ner S.S., Churchill M.E. DNA chaperones: a solution to a persistence problem? Cell. 77:1994;167-169.
    • (1994) Cell , vol.77 , pp. 167-169
    • Travers, A.A.1    Ner, S.S.2    Churchill, M.E.3
  • 45
    • 0030994385 scopus 로고    scopus 로고
    • Stimulation of V(D)J cleavage by high mobility group proteins
    • van Gent D.C., Hiom K., Paull T.T., Gellert M. Stimulation of V(D)J cleavage by high mobility group proteins. EMBO J. 16:1997;2665-2670.
    • (1997) EMBO J , vol.16 , pp. 2665-2670
    • Van Gent, D.C.1    Hiom, K.2    Paull, T.T.3    Gellert, M.4
  • 46
    • 0031770944 scopus 로고    scopus 로고
    • The RAG-HMG1 complex enforces the 12/23 rule of V(D)J recombination specifically at the double-hairpin formation step
    • West R.B., Lieber M.R. The RAG-HMG1 complex enforces the 12/23 rule of V(D)J recombination specifically at the double-hairpin formation step. Mol Cell Biol. 18:1998;6408-6415.
    • (1998) Mol Cell Biol , vol.18 , pp. 6408-6415
    • West, R.B.1    Lieber, M.R.2
  • 47
    • 0032823310 scopus 로고    scopus 로고
    • The RAG1 homeodomain recruits HMG1 and HMG2 to facilitate recombination signal sequence binding and to enhance the intrinsic DNA-bending activity of RAG1-RAG2
    • Aidinis V., Bonaldi T., Beltrame M., Santagata S., Bianchi M.E., Spanopoulou E. The RAG1 homeodomain recruits HMG1 and HMG2 to facilitate recombination signal sequence binding and to enhance the intrinsic DNA-bending activity of RAG1-RAG2. Mol Cell Biol. 19:1999;6532-6542.
    • (1999) Mol Cell Biol , vol.19 , pp. 6532-6542
    • Aidinis, V.1    Bonaldi, T.2    Beltrame, M.3    Santagata, S.4    Bianchi, M.E.5    Spanopoulou, E.6
  • 49
    • 0033485515 scopus 로고    scopus 로고
    • The structure of a chromosomal high-mobility group protein-DNA complex reveals sequence-neutral mechanisms important for non-sequence-specific DNA recognition
    • note
    • •]).
    • (1999) EMBO J , vol.18 , pp. 6610-6618
    • Murphy F.V. IV1    Sweet, R.M.2    Churchill, M.E.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.