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Volumn 31, Issue 2, 1998, Pages 150-159

Interaction of transmembrane helices by a knobs-into-holes packing characteristic of soluble coiled coils

Author keywords

Bacteriorhodopsin; Cytochrome C oxidase; Packing; Photosynthetic reaction center; Zipper

Indexed keywords

BACTERIORHODOPSIN; CYTOCHROME C OXIDASE;

EID: 0032080907     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19980501)31:2<150::AID-PROT5>3.0.CO;2-Q     Document Type: Article
Times cited : (123)

References (55)
  • 1
    • 0022348605 scopus 로고
    • Structure of the photosynthetic reaction center from the purple bacterium Rhodopseudomonas virides
    • Deisenhofer, J., Epp, O., Miki, K., Huber, R., Michel, H. Structure of the photosynthetic reaction center from the purple bacterium Rhodopseudomonas virides. Nature 318: 618-623, 1985.
    • (1985) Nature , vol.318 , pp. 618-623
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 2
    • 0023408258 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26: The protein subunits
    • Allen, J.P., Feher, G., Yeates, T.O., Komiya, H., Rees, D.C. Structure of the reaction center from Rhodobacter sphaeroides R-26: The protein subunits. Proc. Natl. Acad. Sci. USA 84:6162-6166, 1987.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6162-6166
    • Allen, J.P.1    Feher, G.2    Yeates, T.O.3    Komiya, H.4    Rees, D.C.5
  • 3
    • 0028957690 scopus 로고
    • Crystallographic refinement at 2.3 A resolution and refined model of the photosynthetic reaction center from Rhodopseudomonas viridis
    • Deisenhofer, J., Epp, O., Sinning, I., Michel, H. Crystallographic refinement at 2.3 A resolution and refined model of the photosynthetic reaction center from Rhodopseudomonas viridis. J. Mol. Biol. 246:429-457, 1995.
    • (1995) J. Mol. Biol. , vol.246 , pp. 429-457
    • Deisenhofer, J.1    Epp, O.2    Sinning, I.3    Michel, H.4
  • 4
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high resolution electron cryomicroscopy
    • Henderson, R., Baldwin, J.M., Ceska, T.A., Zemlin, F., Beckmann, E., Downing, K.H. Model for the structure of bacteriorhodopsin based on high resolution electron cryomicroscopy. J. Mol. Biol. 213:899-911, 1990.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-911
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 6
    • 0028890031 scopus 로고
    • Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata, S., Ostermeier, C., Ludwig, B., Michel, H. Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376:660-669, 1995.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 7
    • 0029942862 scopus 로고    scopus 로고
    • The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A
    • Tsukihara, T., Aoyama, H., Yamashita, E., et al. The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A. Science 272:1136-1144, 1996.
    • (1996) Science , vol.272 , pp. 1136-1144
    • Tsukihara, T.1    Aoyama, H.2    Yamashita, E.3
  • 8
    • 0025869062 scopus 로고
    • High-resolution structures of photosynthetic reaction centers
    • Deisenhofer, J., Michel, H. High-resolution structures of photosynthetic reaction centers. Annu. Rev. Biophys. Biophys. Chem. 20:247-266, 1991.
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 247-266
    • Deisenhofer, J.1    Michel, H.2
  • 9
    • 0003136584 scopus 로고    scopus 로고
    • Membrane protein structure and stability: Implications of the first crystallographic analyses
    • White, S.H. (ed.). Oxford: Oxford University Press
    • Rees, D.C., Chirino, A.J., Kim, K-H., Komiya, H. Membrane protein structure and stability: Implications of the first crystallographic analyses. In: "Membrane Protein Structure." White, S.H. (ed.). Oxford: Oxford University Press, 1994:3-26.
    • Membrane Protein Structure , vol.1994 , pp. 3-26
    • Rees, D.C.1    Chirino, A.J.2    Kim, K.-H.3    Komiya, H.4
  • 10
    • 0023410587 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26: Membrane-protein interactions
    • Yeates, T.O., Komiya, H., Rees, D.C., Allen, J.P., Feher, G. Structure of the reaction center from Rhodobacter sphaeroides R-26: membrane-protein interactions. Proc. Natl. Acad. Sci. USA 84:6438-6442, 1987.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6438-6442
    • Yeates, T.O.1    Komiya, H.2    Rees, D.C.3    Allen, J.P.4    Feher, G.5
  • 11
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • Kühlbrand, W., Wang, D.N., Fujiyoshi, Y. Atomic model of plant light-harvesting complex by electron crystallography. Nature 367:614-621, 1994.
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrand, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 12
    • 0029637583 scopus 로고
    • Crystal structure of an integral membrane light-harvesting complex from photosynthetic bacteria
    • McDermott, G., Prince, S.M., Freer, A.A., et al. Crystal structure of an integral membrane light-harvesting complex from photosynthetic bacteria. Nature 374:517-521, 1995.
    • (1995) Nature , vol.374 , pp. 517-521
    • McDermott, G.1    Prince, S.M.2    Freer, A.A.3
  • 14
    • 0027507711 scopus 로고
    • Packing of secondary structural elements in proteins
    • Reddy, B.V.B., Blundell, R.L. Packing of secondary structural elements in proteins. J. Mol. Biol. 233:464-479, 1993.
    • (1993) J. Mol. Biol. , vol.233 , pp. 464-479
    • Reddy, B.V.B.1    Blundell, R.L.2
  • 15
    • 0029867179 scopus 로고    scopus 로고
    • Principles of helix-helix packing in proteins: The helical lattice superposition model
    • Walther, D., Eisenhaber, F., Argos, P. Principles of helix-helix packing in proteins: The helical lattice superposition model. J. Mol. Biol. 255:536-553, 1996.
    • (1996) J. Mol. Biol. , vol.255 , pp. 536-553
    • Walther, D.1    Eisenhaber, F.2    Argos, P.3
  • 16
    • 0025272940 scopus 로고
    • Alpha-helical coiled coils and bundles: How to design an alpha-helical protein
    • Cohen, C., Parry, D.A.D. alpha-helical coiled coils and bundles: How to design an alpha-helical protein. Proteins 7:1-15, 1990.
    • (1990) Proteins , vol.7 , pp. 1-15
    • Cohen, C.1    Parry, D.A.D.2
  • 17
    • 0026845838 scopus 로고
    • Structure of the leucine zipper
    • Alber, T. Structure of the leucine zipper. Curr. Opin. Genet. Dev. 2:205-210, 1992.
    • (1992) Curr. Opin. Genet. Dev. , vol.2 , pp. 205-210
    • Alber, T.1
  • 18
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas, A. Coiled coils: New structures and new functions. Trends Biochem. Sci. 21:375-382, 1996.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 375-382
    • Lupas, A.1
  • 19
    • 0000920828 scopus 로고
    • The packing of α-helices. Simple coiled-coils
    • Crick, F.H.C. The packing of α-helices. Simple coiled-coils. Acta Crystallog. 6:689-697, 1953.
    • (1953) Acta Crystallog. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 20
    • 0016774265 scopus 로고
    • Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure
    • McLachlan, A.D., Steward, M. Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure. J. Mol. Biol. 98:293-304, 1975.
    • (1975) J. Mol. Biol. , vol.98 , pp. 293-304
    • McLachlan, A.D.1    Steward, M.2
  • 21
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea, E.K., Klemm, J.D., Kim, P.S., Alber, T. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 243:539-544, 1991.
    • (1991) Science , vol.243 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 22
    • 0025938866 scopus 로고
    • Construction, purification, and characterization of a hybrid protein comprising the DNA binding domain of the LexA repressor and the Jun leucine zipper: A circular dichroism and mutangenesis study
    • Schmidt-Dörr, T., Oertel-Buchheit, P., Pernelle, C., Bracco, L., Schnarr, M., Granger-Schnarr, M. Construction, purification, and characterization of a hybrid protein comprising the DNA binding domain of the LexA repressor and the Jun leucine zipper: A circular dichroism and mutangenesis study. Biochemistry 30:9657-9664, 1991.
    • (1991) Biochemistry , vol.30 , pp. 9657-9664
    • Schmidt-Dörr, T.1    Oertel-Buchheit, P.2    Pernelle, C.3    Bracco, L.4    Schnarr, M.5    Granger-Schnarr, M.6
  • 23
    • 0027475082 scopus 로고
    • Packing and hydrophobic effects on protein folding and stability: Effects of beta-branched amino acids, valine and isoleucine, on the formation and stability of two-stranded alpha-helical coils/ leucine zippers
    • Zhu, B-Y., Zhou, N.B., Kay, C.M., Hodges, R.S. Packing and hydrophobic effects on protein folding and stability: Effects of beta-branched amino acids, valine and isoleucine, on the formation and stability of two-stranded alpha-helical coils/ leucine zippers. Protein Sci. 2:383-394, 1993.
    • (1993) Protein Sci. , vol.2 , pp. 383-394
    • Zhu, B.-Y.1    Zhou, N.B.2    Kay, C.M.3    Hodges, R.S.4
  • 24
    • 0029919676 scopus 로고    scopus 로고
    • Ion pairs significantly stabilize coiled-coils in the absence of electrolyte
    • Yu, Y., Monera, O.D., Hodges, R.S., Privalov, P.L. Ion pairs significantly stabilize coiled-coils in the absence of electrolyte. J. Mol. Biol. 255:367-372, 1996.
    • (1996) J. Mol. Biol. , vol.255 , pp. 367-372
    • Yu, Y.1    Monera, O.D.2    Hodges, R.S.3    Privalov, P.L.4
  • 25
    • 0028303384 scopus 로고
    • A thermodynamic scale for leucine zipper stability and dimerisation specificity: e and g interhelical interactions
    • Krylov, D., Mikhailenko, I., Vinson, C. A thermodynamic scale for leucine zipper stability and dimerisation specificity: e and g interhelical interactions. EMBO J. 13:2849-2861, 1994.
    • (1994) EMBO J. , vol.13 , pp. 2849-2861
    • Krylov, D.1    Mikhailenko, I.2    Vinson, C.3
  • 26
    • 0016842810 scopus 로고
    • Three dimensional model of purple membrane obtained by electron microscopy
    • Henderson, R., Unwin, N. Three dimensional model of purple membrane obtained by electron microscopy. Nature 257:28-32, 1975.
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, N.2
  • 27
    • 0028280706 scopus 로고
    • Four helix bundle diversity in globular proteins
    • Harris, N.L., Presnell, S.R., Cohen, F.E. Four helix bundle diversity in globular proteins. J. Mol. Biol. 236:1356-1368, 1994.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1356-1368
    • Harris, N.L.1    Presnell, S.R.2    Cohen, F.E.3
  • 28
    • 0028086531 scopus 로고
    • Specificity and promiscuity in membrane helix interactions
    • Lemmon, M.A., Engelman, D.M. Specificity and promiscuity in membrane helix interactions. Q. Rev. Biophys. 27:157-218, 1994.
    • (1994) Q. Rev. Biophys. , vol.27 , pp. 157-218
    • Lemmon, M.A.1    Engelman, D.M.2
  • 29
    • 0025789054 scopus 로고
    • Side-chain clusters in protein structures and their role in protein folding
    • Heringa, J., Argos, P. Side-chain clusters in protein structures and their role in protein folding. J. Mol. Biol. 220:151-171, 1991.
    • (1991) J. Mol. Biol. , vol.220 , pp. 151-171
    • Heringa, J.1    Argos, P.2
  • 30
    • 0028939948 scopus 로고
    • Increasing thermal stability of subtilisin from mutations suggested by strongly interacting side-chain clusters
    • Heringa, J., Argos, P., Egmond, M.R., de Vlieg, J. Increasing thermal stability of subtilisin from mutations suggested by strongly interacting side-chain clusters. Protein Eng. 8:21-30, 1995.
    • (1995) Protein Eng. , vol.8 , pp. 21-30
    • Heringa, J.1    Argos, P.2    Egmond, M.R.3    De Vlieg, J.4
  • 31
    • 0027491528 scopus 로고
    • Refined crystal structure ot the seryl-tRNA synthetase from Thermus thermophilus at 2.5 angströms resolution
    • Fujinaga, M., Berthet-Colominas, C., Yaremchuk, A.D. Refined crystal structure ot the seryl-tRNA synthetase from Thermus thermophilus at 2.5 angströms resolution. J. Mol. Biol. 234:222, 1993.
    • (1993) J. Mol. Biol. , vol.234 , pp. 222
    • Fujinaga, M.1    Berthet-Colominas, C.2    Yaremchuk, A.D.3
  • 33
    • 0026030641 scopus 로고
    • Database of homology-derived structures and the structural meaning of sequence alignment
    • Sander, C., Schneider, R. Database of homology-derived structures and the structural meaning of sequence alignment. Proteins 9:56-68, 1991.
    • (1991) Proteins , vol.9 , pp. 56-68
    • Sander, C.1    Schneider, R.2
  • 34
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., Van Dyke, M., Stock, J. Predicting coiled coils from protein sequences. Science 252:1162-1164, 1991.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 35
    • 0028279520 scopus 로고
    • Prediction of transmembrane segments in proteins utilising multiple sequence alignments
    • Persson, B., Argos, P. Prediction of transmembrane segments in proteins utilising multiple sequence alignments. J. Mol. Biol. 237:182-192, 1994.
    • (1994) J. Mol. Biol. , vol.237 , pp. 182-192
    • Persson, B.1    Argos, P.2
  • 36
    • 0029103215 scopus 로고
    • Characterization and modeling of membrane proteins using sequence analysis
    • Reithmeier, R.A.F. Characterization and modeling of membrane proteins using sequence analysis. Curr. Opin. Struct. Biol. 5:491-500, 1995.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 491-500
    • Reithmeier, R.A.F.1
  • 37
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens, D.L., Altenbach, C., Yang, K., Hubbell, W.L., Khorana, H.G. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 274:768-770, 1996.
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 38
    • 0029778268 scopus 로고    scopus 로고
    • Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F
    • Sheikh, S.P., Zvyaga, T.A., Lichtarge, O., Sakmar, T.P., Bourne, H.R. Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F. Nature 383:347-350, 1996.
    • (1996) Nature , vol.383 , pp. 347-350
    • Sheikh, S.P.1    Zvyaga, T.A.2    Lichtarge, O.3    Sakmar, T.P.4    Bourne, H.R.5
  • 39
    • 0028364239 scopus 로고
    • The role of interhelical ionic interactions in controlling protein folding and stability
    • Zhou, N.E., Kay, C.M., Hodges, R.S. The role of interhelical ionic interactions in controlling protein folding and stability. J. Mol. Biol. 237:500-512, 1994.
    • (1994) J. Mol. Biol. , vol.237 , pp. 500-512
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3
  • 40
    • 0000236570 scopus 로고
    • Peptide 'velcro': Design of a heterodimeric coiled coil
    • O'Shea, E.K., Lumb, K.J., Kim, P.S. Peptide 'velcro': Design of a heterodimeric coiled coil. Curr. Biol. 3:658-667, 1993.
    • (1993) Curr. Biol. , vol.3 , pp. 658-667
    • O'Shea, E.K.1    Lumb, K.J.2    Kim, P.S.3
  • 41
    • 0028330850 scopus 로고
    • Electrostatic interactions control the parallel and antiparallel orientation of alpha-helical chains in two-stranded alpha-helical coiled-coils
    • Monera, O.D., Kay, C.M., Hodges, R.S. Electrostatic interactions control the parallel and antiparallel orientation of alpha-helical chains in two-stranded alpha-helical coiled-coils. Biochemistry 33:3862-3871, 1994.
    • (1994) Biochemistry , vol.33 , pp. 3862-3871
    • Monera, O.D.1    Kay, C.M.2    Hodges, R.S.3
  • 42
    • 0001913674 scopus 로고    scopus 로고
    • Folding and assembly of integral membrane proteins
    • White, S.H. (ed.). Oxford: Oxford University Press
    • Popot, J-L., deVitry, C., Atteia, A. Folding and assembly of integral membrane proteins. In: "Membrane Protein Structure." White, S.H. (ed.). Oxford: Oxford University Press, 1994:41-97.
    • Membrane Protein Structure , vol.1994 , pp. 41-97
    • Popot, J.-L.1    DeVitry, C.2    Atteia, A.3
  • 45
    • 0030575833 scopus 로고    scopus 로고
    • Dimerisation of the glycophorin A transmembrane segment in membranes probed with the toxR transcription activator
    • Langosch, D.L., Brosig, B., Kolmar, H., Fritz, H-J. Dimerisation of the glycophorin A transmembrane segment in membranes probed with the toxR transcription activator. J. Mol. Biol. 263:525-530, 1996.
    • (1996) J. Mol. Biol. , vol.263 , pp. 525-530
    • Langosch, D.L.1    Brosig, B.2    Kolmar, H.3    Fritz, H.-J.4
  • 46
    • 0025314322 scopus 로고
    • Transmembrane helical interactions and the assembly of the T cell receptor complex
    • Manolius, N., Bonifacino, J.S., Klausner, R.D. Transmembrane helical interactions and the assembly of the T cell receptor complex. Science 249:274-277, 1990.
    • (1990) Science , vol.249 , pp. 274-277
    • Manolius, N.1    Bonifacino, J.S.2    Klausner, R.D.3
  • 47
    • 0026485306 scopus 로고
    • Role of transmembrane domain interactions in the assembly of class II MHC molecules
    • Cosson, P., Bonifacino, J.S. Role of transmembrane domain interactions in the assembly of class II MHC molecules. Science 258:659-662, 1992.
    • (1992) Science , vol.258 , pp. 659-662
    • Cosson, P.1    Bonifacino, J.S.2
  • 48
    • 0027143565 scopus 로고
    • Val-Ala mutations selectively alter helix-helix packing in the transmembrane segment of phage M13 coat protein
    • Deber, C.M., Khan, A.R., Zuomei, L., Joensson, C., Glibowicka, M., Wang, J. Val-Ala mutations selectively alter helix-helix packing in the transmembrane segment of phage M13 coat protein. Proc. Natl. Acad. Sci. USA 90: 11648-11652, 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11648-11652
    • Deber, C.M.1    Khan, A.R.2    Zuomei, L.3    Joensson, C.4    Glibowicka, M.5    Wang, J.6
  • 49
    • 0028063482 scopus 로고
    • Structural organization of the pentameric transmembrane alpha-helices of phospholamban, a cardiac ion channel
    • Arkin, I.T., Adams, P.D., MacKenzie, K.R., Lemmon, M.A., Brünger, A.T., Engelman, D.M. Structural organization of the pentameric transmembrane alpha-helices of phospholamban, a cardiac ion channel. EMBO J. 13:4757-4764, 1994.
    • (1994) EMBO J. , vol.13 , pp. 4757-4764
    • Arkin, I.T.1    Adams, P.D.2    MacKenzie, K.R.3    Lemmon, M.A.4    Brünger, A.T.5    Engelman, D.M.6
  • 50
    • 0029862745 scopus 로고    scopus 로고
    • A leucine zipper stabilizes the pentameric membrane domain of phospholamban and forms a coiled-coil pore structure
    • Simmerman, H.K.B., Kobayashi, Y.M., Autry, J.M., Jones, L.R. A leucine zipper stabilizes the pentameric membrane domain of phospholamban and forms a coiled-coil pore structure. J. Biol. Chem. 271:5941-5946, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5941-5946
    • Simmerman, H.K.B.1    Kobayashi, Y.M.2    Autry, J.M.3    Jones, L.R.4
  • 51
    • 0030661912 scopus 로고    scopus 로고
    • Dimerization of the synaptic vesicle protein synaptobrevin/VAMP II depends on specific residues within the transmembrane segment
    • Laage, R., Langosch, D. Dimerization of the synaptic vesicle protein synaptobrevin/VAMP II depends on specific residues within the transmembrane segment. Eur. J. Biochem. 249:540-546, 1997.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 540-546
    • Laage, R.1    Langosch, D.2
  • 52
    • 0029051933 scopus 로고
    • Structural model of the phospholamban ion channel complex in phospholipid membranes
    • Arkin, I.T., Rothman, M., Ludlam, C.F.C., et al. Structural model of the phospholamban ion channel complex in phospholipid membranes. J. Mol. Biol. 248:824-834, 1995.
    • (1995) J. Mol. Biol. , vol.248 , pp. 824-834
    • Arkin, I.T.1    Rothman, M.2    Ludlam, C.F.C.3
  • 53
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • MacKenzie, K.R., Prestegard, J.H., Engelman, D.M. A transmembrane helix dimer: Structure and implications. Science 276:131-133, 1997.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 54
  • 55
    • 0030926720 scopus 로고    scopus 로고
    • The three-dimensional structure of aquaporin-1
    • Walz, T., Hirai, T., Murata, K., et al. The three-dimensional structure of aquaporin-1. Nature 387:624-627, 1997.
    • (1997) Nature , vol.387 , pp. 624-627
    • Walz, T.1    Hirai, T.2    Murata, K.3


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