메뉴 건너뛰기




Volumn 287, Issue 37, 2012, Pages 31574-31581

Revisiting the supramolecular organization of photosystem II in Chlamydomonas reinhardtii

Author keywords

[No Author keywords available]

Indexed keywords

CHLAMYDOMONAS REINHARDTII; ELECTRON MICROGRAPH; ELECTRON TRANSFER; GEL FILTRATION; HIGHER PLANTS; LIGHT-HARVESTING COMPLEX II; MULTI-PROTEIN COMPLEX; OXYGEN-EVOLVING ACTIVITIES; PHOTOSYSTEM II; SINGLE-PARTICLE IMAGE ANALYSIS; SUPERCOMPLEX; SUPRAMOLECULAR ORGANIZATIONS; THYLAKOID MEMBRANES;

EID: 84866095310     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.331991     Document Type: Article
Times cited : (88)

References (47)
  • 1
    • 11044234285 scopus 로고    scopus 로고
    • Supramolecular organization of thylakoid membrane proteins in green plants
    • Dekker, J. P., and Boekema, E. J. (2005) Supramolecular organization of thylakoid membrane proteins in green plants. Biochim. Biophys. Acta 1706, 12-39
    • (2005) Biochim. Biophys. Acta , vol.1706 , pp. 12-39
    • Dekker, J.P.1    Boekema, E.J.2
  • 2
    • 1642331709 scopus 로고    scopus 로고
    • Architecture of the photosynthetic oxygen-evolving center
    • Ferreira, K. N., Iverson, T. M., Maghlaoui, K., Barber, J., and Iwata, S. (2004) Architecture of the photosynthetic oxygen-evolving center. Science 303, 1831-1838
    • (2004) Science , vol.303 , pp. 1831-1838
    • Ferreira, K.N.1    Iverson, T.M.2    Maghlaoui, K.3    Barber, J.4    Iwata, S.5
  • 3
    • 62049085169 scopus 로고    scopus 로고
    • Cyanobacterial photosystem II at 2.9 Å resolution and the role of quinones, lipids, channels and chloride
    • Guskov, A., Kern, J., Gabdulkhakov, A., Broser, M., Zouni, A., and Saenger, W. (2009) Cyanobacterial photosystem II at 2.9 Å resolution and the role of quinones, lipids, channels and chloride. Nat. Struct. Mol. Biol. 16, 334-342
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 334-342
    • Guskov, A.1    Kern, J.2    Gabdulkhakov, A.3    Broser, M.4    Zouni, A.5    Saenger, W.6
  • 4
    • 85028099698 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 Å
    • Umena, Y., Kawakami, K., Shen, J. R., and Kamiya, N. (2011) Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 Å. Nature 473, 55-60
    • (2011) Nature , vol.473 , pp. 55-60
    • Umena, Y.1    Kawakami, K.2    Shen, J.R.3    Kamiya, N.4
  • 5
    • 1642602038 scopus 로고    scopus 로고
    • Crystal structure of spinach major light-harvesting complex at 2.72 Å resolution
    • Liu, Z., Yan, H., Wang, K., Kuang, T., Zhang, J., Gui, L., An, X., and Chang, W. (2004) Crystal structure of spinach major light-harvesting complex at 2.72 Å resolution. Nature 428, 287-292
    • (2004) Nature , vol.428 , pp. 287-292
    • Liu, Z.1    Yan, H.2    Wang, K.3    Kuang, T.4    Zhang, J.5    Gui, L.6    An, X.7    Chang, W.8
  • 6
    • 16344363252 scopus 로고    scopus 로고
    • Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 Å resolution
    • Standfuss, J., Terwisscha van Scheltinga, A. C., Lamborghini, M., and Kühlbrandt, W. (2005) Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 Å resolution. EMBO J. 24, 919-928
    • (2005) EMBO J. , vol.24 , pp. 919-928
    • Standfuss, J.1    Terwisscha Van Scheltinga, A.C.2    Lamborghini, M.3    Kühlbrandt, W.4
  • 7
    • 79952362580 scopus 로고    scopus 로고
    • Structural insights into energy regulation of light-harvesting complex CP29 from spinach
    • Pan, X., Li, M., Wan, T., Wang, L., Jia, C., Hou, Z., Zhao, X., Zhang, J., and Chang, W. (2011) Structural insights into energy regulation of light-harvesting complex CP29 from spinach. Nat. Struct. Mol. Biol. 18, 309-315
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 309-315
    • Pan, X.1    Li, M.2    Wan, T.3    Wang, L.4    Jia, C.5    Hou, Z.6    Zhao, X.7    Zhang, J.8    Chang, W.9
  • 8
    • 0034623285 scopus 로고    scopus 로고
    • Three-dimensional structure of Chlamydomonas reinhardtii and Synechococcus elongatus photosystem II complexes allows for comparison of their oxygen-evolving complex organization
    • Nield, J., Kruse, O., Ruprecht, J., da Fonseca, P., Büchel, C., and Barber, J. (2000) Three-dimensional structure of Chlamydomonas reinhardtii and Synechococcus elongatus photosystem II complexes allows for comparison of their oxygen-evolving complex organization. J. Biol. Chem. 275, 27940-27946
    • (2000) J. Biol. Chem. , vol.275 , pp. 27940-27946
    • Nield, J.1    Kruse, O.2    Ruprecht, J.3    Da Fonseca, P.4    Büchel, C.5    Barber, J.6
  • 9
    • 0033989509 scopus 로고    scopus 로고
    • 3D map of the plant photosystem II supercomplex obtained by cryoelectron microscopy and single particle analysis
    • Nield, J., Orlova, E. V., Morris, E. P., Gowen, B., van Heel, M., and Barber, J. (2000) 3D map of the plant photosystem II supercomplex obtained by cryoelectron microscopy and single particle analysis. Nat. Struct. Biol. 7, 44-47
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 44-47
    • Nield, J.1    Orlova, E.V.2    Morris, E.P.3    Gowen, B.4    Van Heel, M.5    Barber, J.6
  • 10
    • 80655135259 scopus 로고    scopus 로고
    • Supramolecular organization of photosystem II in green plants
    • Kouřil, R., Dekker, J. P., and Boekema, E. J. (2012) Supramolecular organization of photosystem II in green plants. Biochim. Biophys. Acta 1817, 2-12
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 2-12
    • Kouřil, R.1    Dekker, J.P.2    Boekema, E.J.3
  • 12
    • 0032032367 scopus 로고    scopus 로고
    • Localization of the 23-kDa subunit of the oxygen-evolving complex of photosystem II by electron microscopy
    • Boekema, E. J., Nield, J., Hankamer, B., and Barber, J. (1998) Localization of the 23-kDa subunit of the oxygen-evolving complex of photosystem II by electron microscopy. Eur. J. Biochem. 252, 268-276
    • (1998) Eur. J. Biochem. , vol.252 , pp. 268-276
    • Boekema, E.J.1    Nield, J.2    Hankamer, B.3    Barber, J.4
  • 13
    • 0031028204 scopus 로고    scopus 로고
    • Isolation and biochemical characterisation of monomeric and dimeric photosystem II complexes from spinach and their relevance to the organisation of photosystem II in vivo
    • Hankamer, B., Nield, J., Zheleva, D., Boekema, E., Jansson, S., and Barber, J. (1997) Isolation and biochemical characterisation of monomeric and dimeric photosystem II complexes from spinach and their relevance to the organisation of photosystem II in vivo. Eur. J. Biochem. 243, 422-429
    • (1997) Eur. J. Biochem. , vol.243 , pp. 422-429
    • Hankamer, B.1    Nield, J.2    Zheleva, D.3    Boekema, E.4    Jansson, S.5    Barber, J.6
  • 14
    • 0033486045 scopus 로고    scopus 로고
    • Supramolecular organization of photosystem II and its light-harvesting antenna in partially solubilized photosystem II membranes
    • Boekema, E. J., Van Roon, H., Van Breemen, J. F., and Dekker, J. P. (1999) Supramolecular organization of photosystem II and its light-harvesting antenna in partially solubilized photosystem II membranes. Eur. J. Biochem. 266, 444-452
    • (1999) Eur. J. Biochem. , vol.266 , pp. 444-452
    • Boekema, E.J.1    Van Roon, H.2    Van Breemen, J.F.3    Dekker, J.P.4
  • 16
    • 70350565366 scopus 로고    scopus 로고
    • Functional architecture of higher plant photosystem II supercomplexes
    • Caffarri, S., Kouril, R., Kereïche, S., Boekema, E. J., and Croce, R. (2009) Functional architecture of higher plant photosystem II supercomplexes. EMBO J. 28, 3052-3063
    • (2009) EMBO J. , vol.28 , pp. 3052-3063
    • Caffarri, S.1    Kouril, R.2    Kereïche, S.3    Boekema, E.J.4    Croce, R.5
  • 17
    • 79651473928 scopus 로고    scopus 로고
    • Fine structure of granal thylakoid membrane organization using cryo electron tomography
    • Kouřil, R., Oostergetel, G. T., and Boekema, E. J. (2011) Fine structure of granal thylakoid membrane organization using cryo electron tomography. Biochim. Biophys. Acta 1807, 368-374
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 368-374
    • Kouřil, R.1    Oostergetel, G.T.2    Boekema, E.J.3
  • 18
    • 77953209825 scopus 로고    scopus 로고
    • Arrangement of photosystem II and ATP synthase in chloroplast membranes of spinach and pea
    • Daum, B., Nicastro, D., Austin, J., 2nd, McIntosh, J. R., and Kühlbrandt, W. (2010) Arrangement of photosystem II and ATP synthase in chloroplast membranes of spinach and pea. Plant Cell 22, 1299-1312
    • (2010) Plant Cell , vol.22 , pp. 1299-1312
    • Daum, B.1    Nicastro, D.2    Austin II, J.3    McIntosh, J.R.4    Kühlbrandt, W.5
  • 19
    • 57749091785 scopus 로고    scopus 로고
    • Molecular remodeling of photosystem II during state transitions in Chlamydomonas reinhardtii
    • Iwai, M., Takahashi, Y., and Minagawa, J. (2008) Molecular remodeling of photosystem II during state transitions in Chlamydomonas reinhardtii. Plant Cell 20, 2177-2189
    • (2008) Plant Cell , vol.20 , pp. 2177-2189
    • Iwai, M.1    Takahashi, Y.2    Minagawa, J.3
  • 20
    • 31044441400 scopus 로고    scopus 로고
    • Structure, function and assembly of photosystem II and its light-harvesting proteins
    • Minagawa, J., and Takahashi, Y. (2004) Structure, function and assembly of photosystem II and its light-harvesting proteins. Photosynth. Res. 82, 241-263
    • (2004) Photosynth. Res. , vol.82 , pp. 241-263
    • Minagawa, J.1    Takahashi, Y.2
  • 21
    • 33845740676 scopus 로고    scopus 로고
    • Lack of the light-harvesting complex CP24 affects the structure and function of the grana membranes of higher plant chloroplasts
    • Kovács, L., Damkjaer, J., Kereïche, S., Ilioaia, C., Ruban, A. V., Boekema, E. J., Jansson, S., and Horton, P. (2006) Lack of the light-harvesting complex CP24 affects the structure and function of the grana membranes of higher plant chloroplasts. Plant Cell 18, 3106-3120
    • (2006) Plant Cell , vol.18 , pp. 3106-3120
    • Kovács, L.1    Damkjaer, J.2    Kereïche, S.3    Ilioaia, C.4    Ruban, A.V.5    Boekema, E.J.6    Jansson, S.7    Horton, P.8
  • 22
    • 48549086564 scopus 로고    scopus 로고
    • Minor antenna proteins CP24 and CP26 affect the interactions between photosystem II subunits and the electron transport rate in grana membranes of Arabidopsis
    • de Bianchi, S., Dall'Osto, L., Tognon, G., Morosinotto, T., and Bassi, R. (2008) Minor antenna proteins CP24 and CP26 affect the interactions between photosystem II subunits and the electron transport rate in grana membranes of Arabidopsis. Plant Cell 20, 1012-1028
    • (2008) Plant Cell , vol.20 , pp. 1012-1028
    • De Bianchi, S.1    Dall'Osto, L.2    Tognon, G.3    Morosinotto, T.4    Bassi, R.5
  • 23
    • 0013832925 scopus 로고
    • Cytochrome f and plastocyanin: Their sequence in the photosynthetic electron transport chain of Chlamydomonas reinhardi
    • Gorman, D. S., and Levine, R. P. (1965) Cytochrome f and plastocyanin: their sequence in the photosynthetic electron transport chain of Chlamydomonas reinhardi. Proc. Natl. Acad. Sci. U.S.A. 54, 1665-1669
    • (1965) Proc. Natl. Acad. Sci. U.S.A. , vol.54 , pp. 1665-1669
    • Gorman, D.S.1    Levine, R.P.2
  • 24
    • 31044439022 scopus 로고    scopus 로고
    • Identification of the mobile light-harvesting complex II polypeptides for state transitions in Chlamydomonas reinhardtii
    • Takahashi, H., Iwai, M., Takahashi, Y., and Minagawa, J. (2006) Identification of the mobile light-harvesting complex II polypeptides for state transitions in Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. U.S.A. 103, 477-482
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 477-482
    • Takahashi, H.1    Iwai, M.2    Takahashi, Y.3    Minagawa, J.4
  • 25
    • 65549147263 scopus 로고    scopus 로고
    • CP29, a monomeric light-harvesting complex II protein, is essential for state transitions in Chlamydomonas reinhardtii
    • Tokutsu, R., Iwai, M., and Minagawa, J. (2009) CP29, a monomeric light-harvesting complex II protein, is essential for state transitions in Chlamydomonas reinhardtii. J. Biol. Chem. 284, 7777-7782
    • (2009) J. Biol. Chem. , vol.284 , pp. 7777-7782
    • Tokutsu, R.1    Iwai, M.2    Minagawa, J.3
  • 26
    • 0014328849 scopus 로고
    • The lattice spacing of crystalline catalase as an internal standard of length in electron microscopy
    • Wrigley, N. G. (1968) The lattice spacing of crystalline catalase as an internal standard of length in electron microscopy. J. Ultrastruct. Res. 24, 454-464
    • (1968) J. Ultrastruct. Res. , vol.24 , pp. 454-464
    • Wrigley, N.G.1
  • 27
    • 0023090371 scopus 로고
    • Similarity measures between images
    • Van Heel, M. (1987) Similarity measures between images. Ultramicroscopy 21, 95-100
    • (1987) Ultramicroscopy , vol.21 , pp. 95-100
    • Van Heel, M.1
  • 28
    • 0027853061 scopus 로고
    • The effects of radiation damage on the structure of frozen hydrated HSV-1 capsids
    • Conway, J. F., Trus, B. L., Booy, F. P., Newcomb, W. W., Brown, J. C., and Steven, A. C. (1993) The effects of radiation damage on the structure of frozen hydrated HSV-1 capsids. J. Struct. Biol. 111, 222-233
    • (1993) J. Struct. Biol. , vol.111 , pp. 222-233
    • Conway, J.F.1    Trus, B.L.2    Booy, F.P.3    Newcomb, W.W.4    Brown, J.C.5    Steven, A.C.6
  • 29
    • 0035783171 scopus 로고    scopus 로고
    • Bsoft: Image and molecular processing in electron microscopy
    • Heymann, J. B. (2001) Bsoft: image and molecular processing in electron microscopy. J. Struct. Biol. 133, 156-169
    • (2001) J. Struct. Biol. , vol.133 , pp. 156-169
    • Heymann, J.B.1
  • 30
    • 33845336533 scopus 로고    scopus 로고
    • Bsoft: Image processing and molecular modeling for electron microscopy
    • Heymann, J. B., and Belnap, D. M. (2007) Bsoft: image processing and molecular modeling for electron microscopy. J. Struct. Biol. 157, 3-18
    • (2007) J. Struct. Biol. , vol.157 , pp. 3-18
    • Heymann, J.B.1    Belnap, D.M.2
  • 31
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank, J., Radermacher, M., Penczek, P., Zhu, J., Li, Y., Ladjadj, M., and Leith, A. (1996) SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116, 190-199
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 32
    • 58049204808 scopus 로고    scopus 로고
    • SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs
    • Shaikh, T. R., Gao, H., Baxter, W. T., Asturias, F. J., Boisset, N., Leith, A., and Frank, J. (2008) SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs. Nat. Protoc. 3, 1941-1974
    • (2008) Nat. Protoc. , vol.3 , pp. 1941-1974
    • Shaikh, T.R.1    Gao, H.2    Baxter, W.T.3    Asturias, F.J.4    Boisset, N.5    Leith, A.6    Frank, J.7
  • 33
    • 0030198739 scopus 로고    scopus 로고
    • Acommon-lines based method for determining orientations for N > 3 particle projections simultaneously
    • Penczek, P. A., Zhu, J., and Frank, J. (1996)Acommon-lines based method for determining orientations for N > 3 particle projections simultaneously. Ultramicroscopy 63, 205-218
    • (1996) Ultramicroscopy , vol.63 , pp. 205-218
    • Penczek, P.A.1    Zhu, J.2    Frank, J.3
  • 34
    • 0024213727 scopus 로고
    • Statistical image analysis of electron micrographs of ribosomal subunits
    • Harauz, G., Boekema, E., and van Heel, M. (1988) Statistical image analysis of electron micrographs of ribosomal subunits. Methods Enzymol. 164, 35-49
    • (1988) Methods Enzymol. , vol.164 , pp. 35-49
    • Harauz, G.1    Boekema, E.2    Van Heel, M.3
  • 35
    • 48749146415 scopus 로고
    • 2-evolving PS II particles by divalent salt-washing
    • 2-evolving PS II particles by divalent salt-washing. FEBS Lett. 164, 255-260
    • (1983) FEBS Lett. , vol.164 , pp. 255-260
    • Ono, T.A.1    Inoue, Y.2
  • 36
    • 0001617374 scopus 로고
    • 2-washed PS II particles depleted of 33-, 24-, and 16-kDa proteins
    • 2-washed PS II particles depleted of 33-, 24-, and 16-kDa proteins. FEBS Lett. 168, 281-286
    • (1984) FEBS Lett. , vol.168 , pp. 281-286
    • Ono, T.A.1    Inoue, Y.2
  • 38
    • 0035210531 scopus 로고    scopus 로고
    • Supermolecular organization of photosystem II and its associated light-harvesting antenna in Arabidopsis thaliana
    • Yakushevska, A. E., Jensen, P. E., Keegstra, W., van Roon, H., Scheller, H. V., Boekema, E. J., and Dekker, J. P. (2001) Supermolecular organization of photosystem II and its associated light-harvesting antenna in Arabidopsis thaliana. Eur. J. Biochem. 268, 6020-6028
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6020-6028
    • Yakushevska, A.E.1    Jensen, P.E.2    Keegstra, W.3    Van Roon, H.4    Scheller, H.V.5    Boekema, E.J.6    Dekker, J.P.7
  • 39
    • 0030006844 scopus 로고    scopus 로고
    • A current assessment of photosystem II structure
    • Nicholson, W. V., Ford, R. C., and Holzenburg, A. (1996) A current assessment of photosystem II structure. Biosci. Rep. 16, 159-187
    • (1996) Biosci. Rep. , vol.16 , pp. 159-187
    • Nicholson, W.V.1    Ford, R.C.2    Holzenburg, A.3
  • 40
    • 0029872540 scopus 로고    scopus 로고
    • Structure of photosystem II in spinach thylakoid membranes: Comparison of detergent-solubilized and native complexes by electron microscopy
    • Nicholson, W. V., Shepherd, F. H., Rosenberg, M. F., Ford, R. C., and Holzenburg, A. (1996) Structure of photosystem II in spinach thylakoid membranes: comparison of detergent-solubilized and native complexes by electron microscopy. Biochem. J. 315, 543-547
    • (1996) Biochem. J. , vol.315 , pp. 543-547
    • Nicholson, W.V.1    Shepherd, F.H.2    Rosenberg, M.F.3    Ford, R.C.4    Holzenburg, A.5
  • 42
    • 0034283146 scopus 로고    scopus 로고
    • Arrangement of photosystem II supercomplexes in crystalline macrodomains within the thylakoid membrane of green plant chloroplasts
    • Boekema, E. J., van Breemen, J. F., van Roon, H., and Dekker, J. P. (2000) Arrangement of photosystem II supercomplexes in crystalline macrodomains within the thylakoid membrane of green plant chloroplasts. J. Mol. Biol. 301, 1123-1133
    • (2000) J. Mol. Biol. , vol.301 , pp. 1123-1133
    • Boekema, E.J.1    Van Breemen, J.F.2    Van Roon, H.3    Dekker, J.P.4
  • 43
    • 0032408979 scopus 로고    scopus 로고
    • Evidence for a lack of photosystem segregation in Chlamydomonas reinhardtii (Chlorophyceae)
    • Bertos, N. R., and Gibbs, S. P. (1998) Evidence for a lack of photosystem segregation in Chlamydomonas reinhardtii (Chlorophyceae). J. Phycol. 34, 1009-1016
    • (1998) J. Phycol. , vol.34 , pp. 1009-1016
    • Bertos, N.R.1    Gibbs, S.P.2
  • 44
    • 0010229575 scopus 로고
    • Chloroplast ultrastructure in mutant strains of Chlamydomonas reinhardi lacking components of the photosynthetic apparatus
    • Goodenough, U. W., and Levine, R. P. (1969) Chloroplast ultrastructure in mutant strains of Chlamydomonas reinhardi lacking components of the photosynthetic apparatus. Plant Physiol. 44, 990-1000
    • (1969) Plant Physiol. , vol.44 , pp. 990-1000
    • Goodenough, U.W.1    Levine, R.P.2
  • 45
    • 79958161573 scopus 로고    scopus 로고
    • State transitions: The molecular remodeling of photosynthetic supercomplexes that controls energy flow in the chloroplast
    • Minagawa, J. (2011) State transitions: the molecular remodeling of photosynthetic supercomplexes that controls energy flow in the chloroplast. Biochim. Biophys. Acta 1807, 897-905
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 897-905
    • Minagawa, J.1
  • 46
    • 0030045873 scopus 로고    scopus 로고
    • Changes in light energy distribution upon state transitions: An in vivo photoacoustic study of the wild type and photosynthesis mutants from Chlamydomonas reinhardtii
    • Delosme, R., Olive, J., and Wollman, F. A. (1996) Changes in light energy distribution upon state transitions: an in vivo photoacoustic study of the wild type and photosynthesis mutants from Chlamydomonas reinhardtii. Biochim. Biophys. Acta 1273, 150-158
    • (1996) Biochim. Biophys. Acta , vol.1273 , pp. 150-158
    • Delosme, R.1    Olive, J.2    Wollman, F.A.3
  • 47
    • 77951622488 scopus 로고    scopus 로고
    • Isolation of the elusive supercomplex that drives cyclic electron flow in photosynthesis
    • Iwai, M., Takizawa, K., Tokutsu, R., Okamuro, A., Takahashi, Y., and Minagawa, J. (2010) Isolation of the elusive supercomplex that drives cyclic electron flow in photosynthesis. Nature 464, 1210-1213
    • (2010) Nature , vol.464 , pp. 1210-1213
    • Iwai, M.1    Takizawa, K.2    Tokutsu, R.3    Okamuro, A.4    Takahashi, Y.5    Minagawa, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.