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Volumn 111, Issue 2, 2014, Pages

Apo-bacteriophytochromes modulate bacterialphotosynthesis in response to low light

Author keywords

Gene regulation; Photoregulation; Purple nonsulfur bacteria; Redox control

Indexed keywords

BACTERIAL PROTEIN; BACTERIOCHLOROPHYLL; BACTERIOPHYTOCHROME 2; BACTERIOPHYTOCHROME 3; BILIVERDIN; HEME OXYGENASE; OXYGEN; PHYTOCHROME; PROTEIN HISTIDINE KINASE; PROTEIN LH4; QUINONE DERIVATIVE; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 84892600069     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1322410111     Document Type: Article
Times cited : (25)

References (49)
  • 1
    • 78650885619 scopus 로고    scopus 로고
    • Engineered photoreceptors as novel optogenetic tools
    • Möglich A, Moffat K (2010) Engineered photoreceptors as novel optogenetic tools. Photochem Photobiol Sci 9(10):1286-1300.
    • (2010) Photochem Photobiol Sci , vol.9 , Issue.10 , pp. 1286-1300
    • Möglich A, M.1
  • 2
    • 65649113981 scopus 로고    scopus 로고
    • Mammalian expression of infrared fluorescent proteins engineered from a bacterial phytochrome
    • Shu X, et al. (2009) Mammalian expression of infrared fluorescent proteins engineered from a bacterial phytochrome. Science 324(5928):804-807.
    • (2009) Science , vol.324 , Issue.5928 , pp. 804-807
    • Shu, X.1
  • 3
    • 80053896548 scopus 로고    scopus 로고
    • Phytochrome structure and photochemistry: Recent advances toward a complete molecular picture
    • Ulijasz AT, Vierstra RD (2011) Phytochrome structure and photochemistry: Recent advances toward a complete molecular picture. Curr Opin Plant Biol 14(5):498-506.
    • (2011) Curr Opin Plant Biol , vol.14 , Issue.5 , pp. 498-506
    • Ulijasz, A.T.1    Vierstra, R.D.2
  • 4
    • 72049106410 scopus 로고    scopus 로고
    • Phytochrome functions in Arabidopsis development
    • Franklin KA, Quail PH (2010) Phytochrome functions in Arabidopsis development. J Exp Bot 61(1):11-24.
    • (2010) J Exp Bot , vol.61 , Issue.1 , pp. 11-24
    • Franklin, K.A.1    Quail, P.H.2
  • 5
    • 78951495450 scopus 로고    scopus 로고
    • Bacterial phytochromes: More than meets the light
    • Auldridge ME, Forest KT (2011) Bacterial phytochromes: More than meets the light. Crit Rev Biochem Mol Biol 46(1):67-88.
    • (2011) Crit Rev Biochem Mol Biol , vol.46 , Issue.1 , pp. 67-88
    • Auldridge, M.E.1    Forest, K.T.2
  • 6
    • 0242405551 scopus 로고    scopus 로고
    • The structural basis of light-harvesting in purple bacteria
    • Cogdell RJ, et al. (2003) The structural basis of light-harvesting in purple bacteria. FEBS Lett 555(1):35-39.
    • (2003) FEBS Lett , vol.555 , Issue.1 , pp. 35-39
    • Cogdell, R.J.1
  • 7
    • 25444438210 scopus 로고    scopus 로고
    • A new type of bacteriophytochrome acts in tandem with a classical bacteriophytochrome to control the antennae synthesis in Rhodopseudomonas palustris
    • Giraud E, et al. (2005) A new type of bacteriophytochrome acts in tandem with a classical bacteriophytochrome to control the antennae synthesis in Rhodopseudomonas palustris. J Biol Chem 280(37):32389-32397.
    • (2005) J Biol Chem , vol.280 , Issue.37 , pp. 32389-32397
    • Giraud, E.1
  • 8
    • 78149408524 scopus 로고    scopus 로고
    • Bacteriophytochrome-dependent regulation of lightharvesting complexes in Rhodopseudomonas palustris anaerobic cultures
    • Li M, Noll S, Beatty JT (2010) Bacteriophytochrome-dependent regulation of lightharvesting complexes in Rhodopseudomonas palustris anaerobic cultures. Curr Microbiol 61(5):429-434.
    • (2010) Curr Microbiol , vol.61 , Issue.5 , pp. 429-434
    • Li, M.1    Noll, S.2    Beatty, J.T.3
  • 9
    • 34547628072 scopus 로고    scopus 로고
    • Crystal structure of the chromophore binding domain of an unusual bacteriophytochrome, RpBphP3, reveals residues that modulate photoconversion
    • Yang X, Stojkovic EA, Kuk J, Moffat K (2007) Crystal structure of the chromophore binding domain of an unusual bacteriophytochrome, RpBphP3, reveals residues that modulate photoconversion. Proc Natl Acad Sci USA 104(30):12571-12576.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.30 , pp. 12571-12576
    • Yang, X.1    Stojkovic, E.A.2    Kuk, J.3    Moffat, K.4
  • 10
  • 11
    • 77952688009 scopus 로고    scopus 로고
    • Proton-transfer and hydrogen-bond interactions determine fluorescence quantum yield and photochemical efficiency of bacteriophytochrome
    • Toh KC, Stojkovic EA, van Stokkum IH, Moffat K, Kennis JT (2010) Proton-transfer and hydrogen-bond interactions determine fluorescence quantum yield and photochemical efficiency of bacteriophytochrome. Proc Natl Acad Sci USA 107(20): 9170-9175.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.20 , pp. 9170-9175
    • Toh, K.C.1    Stojkovic, E.A.2    Van Stokkum, I.H.3    Moffat, K.4    Kennis, J.T.5
  • 12
    • 79955392478 scopus 로고    scopus 로고
    • Primary reactions of bacteriophytochrome observed with ultrafast mid-infrared spectroscopy
    • Toh KC, et al. (2011) Primary reactions of bacteriophytochrome observed with ultrafast mid-infrared spectroscopy. J Phys Chem A 115(16):3778-3786.
    • (2011) J Phys Chem A , vol.115 , Issue.16 , pp. 3778-3786
    • Toh, K.C.1
  • 13
    • 0035856979 scopus 로고    scopus 로고
    • Bacteriophytochromes are photochromic histidine kinases using a biliverdin chromophore
    • Bhoo SH, Davis SJ, Walker J, Karniol B, Vierstra RD (2001) Bacteriophytochromes are photochromic histidine kinases using a biliverdin chromophore. Nature 414(6865):776-779.
    • (2001) Nature , vol.414 , Issue.6865 , pp. 776-779
    • Bhoo, S.H.1    Davis, S.J.2    Walker, J.3    Karniol, B.4    Vierstra, R.D.5
  • 14
    • 1642276701 scopus 로고    scopus 로고
    • The biliverdin chromophore binds covalently to a conserved cysteine residue in the N-terminus of Agrobacterium phytochrome Agp1
    • Lamparter T, et al. (2004) The biliverdin chromophore binds covalently to a conserved cysteine residue in the N-terminus of Agrobacterium phytochrome Agp1. Biochemistry 43(12):3659-3669.
    • (2004) Biochemistry , vol.43 , Issue.12 , pp. 3659-3669
    • Lamparter, T.1
  • 15
    • 53849142165 scopus 로고    scopus 로고
    • Function and distribution of bilin biosynthesis enzymes in photosynthetic organisms
    • Dammeyer T, Frankenberg-Dinkel N (2008) Function and distribution of bilin biosynthesis enzymes in photosynthetic organisms. Photochem Photobiol Sci 7(10):1121-1130.
    • (2008) Photochem Photobiol Sci , vol.7 , Issue.10 , pp. 1121-1130
    • Dammeyer, T.1    Frankenberg-Dinkel, N.2
  • 16
    • 23944495805 scopus 로고    scopus 로고
    • A bacteriophytochrome regulates the synthesis of LH4 complexes in Rhodopseudomonas palustris
    • Evans K, et al. (2005) A bacteriophytochrome regulates the synthesis of LH4 complexes in Rhodopseudomonas palustris. Photosynth Res 85(2):169-180.
    • (2005) Photosynth Res , vol.85 , Issue.2 , pp. 169-180
    • Evans, K.1
  • 17
    • 84870531300 scopus 로고    scopus 로고
    • Red/green cyanobacteriochromes: Sensors of color and power
    • Rockwell NC, Martin SS, Lagarias JC (2012) Red/green cyanobacteriochromes: Sensors of color and power. Biochemistry 51(48):9667-9677.
    • (2012) Biochemistry , vol.51 , Issue.48 , pp. 9667-9677
    • Rockwell, N.C.1    Martin, S.S.2    Lagarias, J.C.3
  • 18
  • 19
    • 0036007349 scopus 로고    scopus 로고
    • The 7.5-A electron density and spectroscopic properties of a novel low-light B800 LH2 from Rhodopseudomonas palustris
    • Hartigan N, Tharia HA, Sweeney F, Lawless AM, Papiz MZ (2002) The 7.5-A electron density and spectroscopic properties of a novel low-light B800 LH2 from Rhodopseudomonas palustris. Biophys J 82(2):963-977.
    • (2002) Biophys J , vol.82 , Issue.2 , pp. 963-977
    • Hartigan, N.1    Tharia, H.A.2    Sweeney, F.3    Lawless, A.M.4    Papiz, M.Z.5
  • 20
    • 48349141422 scopus 로고    scopus 로고
    • Bacteriophytochromes in anoxygenic photosynthetic bacteria
    • Giraud E, Verméglio A (2008) Bacteriophytochromes in anoxygenic photosynthetic bacteria. Photosynth Res 97(2):141-153.
    • (2008) Photosynth Res , vol.97 , Issue.2 , pp. 141-153
    • Giraud, E.1    Verméglio, A.2
  • 21
    • 45549107695 scopus 로고    scopus 로고
    • Mutational analysis of Deinococcus radiodurans bacteriophytochrome reveals key amino acids necessary for the photochromicity and proton exchange cycle of phytochromes
    • Wagner JR, et al. (2008) Mutational analysis of Deinococcus radiodurans bacteriophytochrome reveals key amino acids necessary for the photochromicity and proton exchange cycle of phytochromes. J Biol Chem 283(18):12212-12226.
    • (2008) J Biol Chem , vol.283 , Issue.18 , pp. 12212-12226
    • Wagner, J.R.1
  • 22
    • 0037015009 scopus 로고    scopus 로고
    • Phytochrome from Agrobacterium tumefaciens has unusual spectral properties and reveals an N-terminal chromophore attachment site
    • Lamparter T, Michael N, Mittmann F, Esteban B (2002) Phytochrome from Agrobacterium tumefaciens has unusual spectral properties and reveals an N-terminal chromophore attachment site. Proc Natl Acad Sci USA 99(18):11628-11633.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.18 , pp. 11628-11633
    • Lamparter, T.1    Michael, N.2    Mittmann, F.3    Esteban, B.4
  • 23
    • 0036583227 scopus 로고    scopus 로고
    • Phytochromes with noncovalently bound chromophores: The ability of apophytochromes to direct tetrapyrrole photoisomerization
    • Jorissen HJ, Quest B, Lindner I, Tandeau de Marsac N, GärtnerW (2002) Phytochromes with noncovalently bound chromophores: The ability of apophytochromes to direct tetrapyrrole photoisomerization. Photochem Photobiol 75(5):554-559.
    • (2002) Photochem Photobiol , vol.75 , Issue.5 , pp. 554-559
    • Jorissen Hj, Q.1
  • 24
    • 84864876501 scopus 로고    scopus 로고
    • Dimerization properties of the RpBphP2 chromophorebinding domain crystallized by homologue-directed mutagenesis
    • Bellini D, Papiz MZ (2012) Dimerization properties of the RpBphP2 chromophorebinding domain crystallized by homologue-directed mutagenesis. Acta Crystallogr D Biol Crystallogr 68(Pt 8):1058-1066.
    • (2012) Acta Crystallogr D Biol Crystallogr , vol.68 , Issue.PART 8 , pp. 1058-1066
    • Bellini, D.1    Papiz, M.Z.2
  • 25
    • 84864860526 scopus 로고    scopus 로고
    • Structure of a bacteriophytochrome and light-stimulated protomer swapping with a gene repressor
    • Bellini D, Papiz MZ (2012) Structure of a bacteriophytochrome and light-stimulated protomer swapping with a gene repressor. Structure 20(8):1436-1446.
    • (2012) Structure , vol.20 , Issue.8 , pp. 1436-1446
    • Bellini, D.1    Papiz, M.Z.2
  • 26
    • 33845239413 scopus 로고    scopus 로고
    • Rhodopseudomonas palustris CGA009 has two functional ppsR genes, each of which encodes a repressor of photosynthesis gene expression
    • Braatsch S, et al. (2006) Rhodopseudomonas palustris CGA009 has two functional ppsR genes, each of which encodes a repressor of photosynthesis gene expression. Biochemistry 45(48):14441-14451.
    • (2006) Biochemistry , vol.45 , Issue.48 , pp. 14441-14451
    • Braatsch, S.1
  • 27
    • 3242748298 scopus 로고    scopus 로고
    • Bacteriophytochrome and regulation of the synthesis of the photosynthetic apparatus in Rhodopseudomonas palustris: Pitfalls of using laboratory strains
    • Giraud E, et al. (2004) Bacteriophytochrome and regulation of the synthesis of the photosynthetic apparatus in Rhodopseudomonas palustris: Pitfalls of using laboratory strains. Photochem Photobiol Sci 3(6):587-591.
    • (2004) Photochem Photobiol Sci , vol.3 , Issue.6 , pp. 587-591
    • Giraud, E.1
  • 28
    • 34250630996 scopus 로고    scopus 로고
    • The O2-responsive repressor PpsR2 but not PpsR1 transduces a light signal sensed by the BphP1 phytochrome in Rhodopseudomonas palustris CGA009
    • Braatsch S, Johnson JA, Noll K, Beatty JT (2007) The O2-responsive repressor PpsR2 but not PpsR1 transduces a light signal sensed by the BphP1 phytochrome in Rhodopseudomonas palustris CGA009. FEMS Microbiol Lett 272(1):60-64.
    • (2007) FEMS Microbiol Lett , vol.272 , Issue.1 , pp. 60-64
    • Braatsch, S.1    Johnson, J.A.2    Noll, K.3    Beatty, J.T.4
  • 29
    • 76449108491 scopus 로고    scopus 로고
    • FixK, a global regulator of microaerobic growth, controls photosynthesis in Rhodopseudomonas palustris
    • Rey FE, Harwood CS (2010) FixK, a global regulator of microaerobic growth, controls photosynthesis in Rhodopseudomonas palustris. Mol Microbiol 75(4):1007-1020.
    • (2010) Mol Microbiol , vol.75 , Issue.4 , pp. 1007-1020
    • Rey, F.E.1    Harwood, C.S.2
  • 30
    • 5444249703 scopus 로고    scopus 로고
    • Characterization of a heme oxygenase of Clostridium tetani and its possible role in oxygen tolerance
    • Brüggemann H, Bauer R, Raffestin S, Gottschalk G (2004) Characterization of a heme oxygenase of Clostridium tetani and its possible role in oxygen tolerance. Arch Microbiol 182(2-3):259-263.
    • (2004) Arch Microbiol , vol.182 , Issue.2-3 , pp. 259-263
    • Brüggemann, H.1    Bauer, R.2    Raffestin, S.3    Gottschalk, G.4
  • 31
    • 77949297055 scopus 로고    scopus 로고
    • Transcriptional regulation of hemO encoding heme oxygenase in Clostridium perfringens
    • Hassan S, et al. (2010) Transcriptional regulation of hemO encoding heme oxygenase in Clostridium perfringens. J Microbiol 48(1):96-101.
    • (2010) J Microbiol , vol.48 , Issue.1 , pp. 96-101
    • Hassan, S.1
  • 32
    • 2442645409 scopus 로고    scopus 로고
    • Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: Implications for heme oxygenase function
    • Unno MM, et al. (2004) Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: Implications for heme oxygenase function. J Biol Chem 279(20):21055-21061.
    • (2004) J Biol Chem , vol.279 , Issue.20 , pp. 21055-21061
    • Unno, M.M.1
  • 33
    • 32344441400 scopus 로고    scopus 로고
    • Determination and comparison of the baseline proteomes of the versatile microbe Rhodopseudomonas palustris under its major metabolic states
    • VerBerkmoes NC, et al. (2006) Determination and comparison of the baseline proteomes of the versatile microbe Rhodopseudomonas palustris under its major metabolic states. J Proteome Res 5(2):287-298.
    • (2006) J Proteome Res , vol.5 , Issue.2 , pp. 287-298
    • Verberkmoes, N.C.1
  • 34
    • 0033993308 scopus 로고    scopus 로고
    • Phytochromes, cryptochromes, phototropin: Photoreceptor interactions in plants
    • Casal JJ (2000) Phytochromes, cryptochromes, phototropin: Photoreceptor interactions in plants. Photochem Photobiol 71(1):1-11.
    • (2000) Photochem Photobiol , vol.71 , Issue.1 , pp. 1-11
    • Casal, J.J.1
  • 35
    • 33646594462 scopus 로고    scopus 로고
    • Identification of a ubiquinone-binding site that affects autophosphorylation of the sensor kinase RegB
    • Swem LR, Gong X, Yu C-A, Bauer CE (2006) Identification of a ubiquinone-binding site that affects autophosphorylation of the sensor kinase RegB. J Biol Chem 281(10):6768-6775.
    • (2006) J Biol Chem , vol.281 , Issue.10 , pp. 6768-6775
    • Swem, L.R.1    Gong, X.2    Yu, C.-A.3    Bauer, C.E.4
  • 36
    • 79952180898 scopus 로고    scopus 로고
    • RegB kinase activity is controlled in part by monitoring the ratio of oxidized to reduced ubiquinones in the ubiquinone pool
    • Wu J, Bauer CE (2010) RegB kinase activity is controlled in part by monitoring the ratio of oxidized to reduced ubiquinones in the ubiquinone pool. MBio 1(5):e00272-10.
    • (2010) MBio , vol.1 , Issue.5
    • Wu, J.1    Bauer, C.E.2
  • 37
    • 77957187746 scopus 로고
    • Light-induced reactions of ubiquinone in photosynthetic bacterium, Chromatium D, II: Effects of inhibitors and other experimental conditions
    • Takamiya K, Takamiya A (1969) Light-induced reactions of ubiquinone in photosynthetic bacterium, Chromatium D, II: Effects of inhibitors and other experimental conditions. Plant Cell Physiol 10:113-127.
    • (1969) Plant Cell Physiol , vol.10 , pp. 113-127
    • Takamiya, K.1    Takamiya, A.2
  • 38
    • 0029200332 scopus 로고
    • Redox regulation of light-harvesting complex II and cab mRNA abundance in Dunaliella salina
    • Maxwell DP, Laudenbach DE, Huner N (1995) Redox regulation of light-harvesting complex II and cab mRNA abundance in Dunaliella salina. Plant Physiol 109(3):787-795.
    • (1995) Plant Physiol , vol.109 , Issue.3 , pp. 787-795
    • Maxwell, D.P.1    De, L.2    Huner, N.3
  • 39
    • 0028865421 scopus 로고
    • Light intensity regulation of cab gene transcription is signaled by the redox state of the plastoquinone pool
    • Escoubas JM, Lomas M, LaRoche J, Falkowski PG (1995) Light intensity regulation of cab gene transcription is signaled by the redox state of the plastoquinone pool. Proc Natl Acad Sci USA 92(22):10237-10241.
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.22 , pp. 10237-10241
    • Escoubas, J.M.1    Lomas, M.2    Laroche, J.3    Falkowski, P.G.4
  • 40
    • 33751214536 scopus 로고    scopus 로고
    • Quinone sensing by the circadian input kinase of the cyanobacterial circadian clock
    • Ivleva NB, Gao T, LiWang AC, Golden SS (2006) Quinone sensing by the circadian input kinase of the cyanobacterial circadian clock. Proc Natl Acad Sci USA 103(46):17468-17473.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.46 , pp. 17468-17473
    • Ivleva, N.B.1    Gao, T.2    Liwang, A.C.3    Golden, S.S.4
  • 41
    • 34547181229 scopus 로고    scopus 로고
    • Evolution of a bacteriophytochrome from light to redox sensor
    • Vuillet L, et al. (2007) Evolution of a bacteriophytochrome from light to redox sensor. EMBO J 26(14):3322-3331.
    • (2007) EMBO J , vol.26 , Issue.14 , pp. 3322-3331
    • Vuillet, L.1
  • 42
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential, and light
    • Taylor BL, Zhulin IB (1999) PAS domains: Internal sensors of oxygen, redox potential, and light. Microbiol Mol Biol Rev 63(2):479-506.
    • (1999) Microbiol Mol Biol Rev , vol.63 , Issue.2 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 43
    • 0025812763 scopus 로고    scopus 로고
    • Regulation of benzoate-CoA ligase in Rhodopseudomonas palustris
    • Kim M-K, Harwood CS (2006) Regulation of benzoate-CoA ligase in Rhodopseudomonas palustris. FEMS Microbiol Lett 83:199-203.
    • (2006) FEMS Microbiol Lett , vol.83 , pp. 199-203
    • Kim, M.-K.1    Harwood, C.S.2
  • 44
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram-negative bacteria
    • Simon R, Priefer U, Pühler A (1983) A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram-negative bacteria. Nat Biotechnol 1:784-791.
    • (1983) Nat Biotechnol , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 45
    • 0027158657 scopus 로고
    • Versatile suicide vectors which allow direct selection for gene replacement in gram-negative bacteria
    • Quandt J, Hynes MF (1993) Versatile suicide vectors which allow direct selection for gene replacement in gram-negative bacteria. Gene 127(1):15-21.
    • (1993) Gene , vol.127 , Issue.1 , pp. 15-21
    • Quandt, J.1    Hynes, M.F.2
  • 46
    • 33947219284 scopus 로고    scopus 로고
    • Redirection of metabolism for biological hydrogen production
    • Rey FE, Heiniger EK, Harwood CS (2007) Redirection of metabolism for biological hydrogen production. Appl Environ Microbiol 73(5):1665-1671.
    • (2007) Appl Environ Microbiol , vol.73 , Issue.5 , pp. 1665-1671
    • Rey, F.E.1    Heiniger, E.K.2    Harwood, C.S.3
  • 47
    • 77955388615 scopus 로고    scopus 로고
    • Carbon dioxide fixation as a central redox cofactor recycling mechanism in bacteria
    • McKinlay JB, Harwood CS 2010 Carbon dioxide fixation as a central redox cofactor recycling mechanism in bacteria Proc Natl Acad Sci USA 107 26 11669-11675
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.26 , pp. 11669-11675
    • McKinlay, J.B.1    Harwood, C.S.2
  • 48
    • 0022486877 scopus 로고
    • Visualization of bilin-linked peptides and proteins in polyacrylamide gels
    • Berkelman TR, Lagarias JC (1986) Visualization of bilin-linked peptides and proteins in polyacrylamide gels. Anal Biochem 156(1):194-201.
    • (1986) Anal Biochem , vol.156 , Issue.1 , pp. 194-201
    • Berkelman, T.R.1    Lagarias, J.C.2
  • 49
    • 57449104373 scopus 로고    scopus 로고
    • Multiple genome sequences reveal adaptations of a phototrophic bacterium to sediment microenvironments
    • Oda Y, et al. (2008) Multiple genome sequences reveal adaptations of a phototrophic bacterium to sediment microenvironments. Proc Natl Acad Sci USA 105(47): 18543-18548.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.47 , pp. 18543-18548
    • Oda, Y.1


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