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Volumn 2015, Issue 4, 2015, Pages

Native architecture of the chlamydomonas chloroplast revealed by in situ cryo-electron tomography

Author keywords

[No Author keywords available]

Indexed keywords

RIBULOSEBISPHOSPHATE CARBOXYLASE; STARCH;

EID: 85006320159     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.04889     Document Type: Article
Times cited : (249)

References (124)
  • 2
    • 15444366581 scopus 로고    scopus 로고
    • Cutting artefacts and cutting process in vitreous sections for cryo-electron microscopy
    • Al-Amoudi A, Studer D, Dubochet J. 2005. Cutting artefacts and cutting process in vitreous sections for cryo-electron microscopy. Journal of Structural Biology 150:109-121. doi: 10.1016/j.jsb.2005.01.003.
    • (2005) Journal of Structural Biology , vol.150 , pp. 109-121
    • Al-Amoudi, A.1    Studer, D.2    Dubochet, J.3
  • 4
    • 33745800028 scopus 로고    scopus 로고
    • Plastoglobules are lipoprotein subcompartments of the chloroplast that are permanently coupled to thylakoid membranes and contain biosynthetic enzymes
    • Austin JR II, Frost E, Vidi PA, Kessler F, Staehelin LA. 2006. Plastoglobules are lipoprotein subcompartments of the chloroplast that are permanently coupled to thylakoid membranes and contain biosynthetic enzymes. The Plant Cell 18:1693-1703. doi: 10.1105/tpc.105.039859.
    • (2006) The Plant Cell , vol.18 , pp. 1693-1703
    • Austin, J.1    Frost, E.2    Vidi, P.A.3    Kessler, F.4    Staehelin, L.A.5
  • 5
    • 79953722236 scopus 로고    scopus 로고
    • Three-dimensional architecture of grana and stroma thylakoids of higher plants as determined by electron tomography
    • Austin JR II, Staehelin LA. 2011. Three-dimensional architecture of grana and stroma thylakoids of higher plants as determined by electron tomography. Plant Physiology 155:1601-1611. doi: 10.1104/pp.110.170647
    • (2011) Plant Physiology , vol.155 , pp. 1601-1611
    • Austin, J.1    Staehelin, L.A.2
  • 6
    • 0002046705 scopus 로고
    • A mechanism for controlling the stacking and unstacking of chloroplast thylakoid membranes
    • Barber J, Chow WS. 1979. A mechanism for controlling the stacking and unstacking of chloroplast thylakoid membranes. FEBS Letters 105:5-10. doi: 10.1016/0014-5793(79)80875-3.
    • (1979) FEBS Letters , vol.105 , pp. 5-10
    • Barber, J.1    Chow, W.S.2
  • 7
    • 0033082710 scopus 로고    scopus 로고
    • Electron tomography of molecules and cells
    • Baumeister W, Grimm R, Walz J. 1999. Electron tomography of molecules and cells. Trends in Cell Biology 9:81-85. doi: 10.1016/S0962-8924(98)01423-8.
    • (1999) Trends in Cell Biology , vol.9 , pp. 81-85
    • Baumeister, W.1    Grimm, R.2    Walz, J.3
  • 9
    • 0016557674 scopus 로고
    • Multidimensional binary search trees used for associative searching
    • Bentley JL. 1975. Multidimensional binary search trees used for associative searching. Communications of the ACM 18:509-517. doi: 10.1145/361002.361007.
    • (1975) Communications of the ACM , vol.18 , pp. 509-517
    • Bentley, J.L.1
  • 11
    • 84875693344 scopus 로고    scopus 로고
    • Phosphorylation controls the localization and activation of the lumenal carbonic anhydrase in Chlamydomonas reinhardtii
    • Blanco-Rivero A, Shutova T, Roman MJ, Villarejo A, Martinez F. 2012. Phosphorylation controls the localization and activation of the lumenal carbonic anhydrase in Chlamydomonas reinhardtii. PLOS ONE 7:e49063. doi: 10.1371/journal.pone.0049063.
    • (2012) PLOS ONE , vol.7
    • Blanco-Rivero, A.1    Shutova, T.2    Roman, M.J.3    Villarejo, A.4    Martinez, F.5
  • 12
    • 0001018916 scopus 로고    scopus 로고
    • The intracellular localization of ribulose-1,5-bisphosphate Carboxylase/Oxygenase in Chlamydomonas reinhardtii
    • Borkhsenious ON, Mason CB, Moroney JV. 1998. The intracellular localization of ribulose-1,5-bisphosphate Carboxylase/Oxygenase in Chlamydomonas reinhardtii. Plant Physiology 116:1585-1591. doi: 10.1104/pp.116.4.1585.
    • (1998) Plant Physiology , vol.116 , pp. 1585-1591
    • Borkhsenious, O.N.1    Mason, C.B.2    Moroney, J.V.3
  • 13
    • 78649860473 scopus 로고    scopus 로고
    • Cryo-electron tomography on vitrified sections: A critical analysis of benefits and limitations for structural cell biology
    • Bouchet-Marquis C, Hoenger A. 2011. Cryo-electron tomography on vitrified sections: a critical analysis of benefits and limitations for structural cell biology. Micron 42:152-162. doi: 10.1016/j.micron.2010.07.003.
    • (2011) Micron , vol.42 , pp. 152-162
    • Bouchet-Marquis, C.1    Hoenger, A.2
  • 14
    • 77956006893 scopus 로고    scopus 로고
    • The three-dimensional organization of polyribosomes in intact human cells
    • Brandt F, Carlson LA, Hartl FU, Baumeister W, Grünewald K. 2010. The three-dimensional organization of polyribosomes in intact human cells. Molecular Cell 39:560-569. doi: 10.1016/j.molcel.2010.08.003.
    • (2010) Molecular Cell , vol.39 , pp. 560-569
    • Brandt, F.1    Carlson, L.A.2    Hartl, F.U.3    Baumeister, W.4    Grünewald, K.5
  • 17
    • 29144458149 scopus 로고    scopus 로고
    • Granal stacking of thylakoid membranes in higher plant chloroplasts: The physicochemical forces at work and the functional consequences that ensue
    • Chow WS, Kim EH, Horton P, Anderson JM. 2005. Granal stacking of thylakoid membranes in higher plant chloroplasts: the physicochemical forces at work and the functional consequences that ensue. Photochemical & Photobiological Sciences 4:1081-1090. doi: 10.1039/b507310n.
    • (2005) Photochemical & Photobiological Sciences , vol.4 , pp. 1081-1090
    • Chow, W.S.1    Kim, E.H.2    Horton, P.3    Erson, J.M.4
  • 18
    • 0014930077 scopus 로고
    • Three dimensional reconstructions of spherical viruses by fourier synthesis from electron micrographs
    • Crowther RA, Amos LA, Finch JT, De Rosier DJ, Klug A. 1970. Three dimensional reconstructions of spherical viruses by fourier synthesis from electron micrographs. Nature 226:421-425. doi: 10.1038/226421a0.
    • (1970) Nature , vol.226 , pp. 421-425
    • Crowther, R.A.1    Amos, L.A.2    Finch, J.T.3    De Rosier, D.J.4    Klug, A.5
  • 19
    • 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 II, McIntosh JR, Kühlbrandt W. 2010. Arrangement of photosystem II and ATP synthase in chloroplast membranes of spinach and pea. The Plant Cell 22:1299-1312. doi: 10.1105/tpc.109.071431.
    • (2010) The Plant Cell , vol.22 , pp. 1299-1312
    • Daum, B.1    Nicastro, D.2    Austin, J.3    McIntosh, J.R.4    Kühlbrandt, W.5
  • 20
    • 84879885524 scopus 로고    scopus 로고
    • In-situ integrity control of frozen-hydrated, vitreous lamellas prepared by the cryo-focused ion beam-scanning electron microscope
    • de Winter DA, Mesman RJ, Hayles MF, Schneijdenberg CT, Mathisen C, Post JA. 2013. In-situ integrity control of frozen-hydrated, vitreous lamellas prepared by the cryo-focused ion beam-scanning electron microscope. Journal of Structural Biology 183:11-18. doi: 10.1016/j.jsb.2013.05.016.
    • (2013) Journal of Structural Biology , vol.183 , pp. 11-18
    • De Winter, D.A.1    Mesman, R.J.2    Hayles, M.F.3    Schneijdenberg, C.T.4    Mathisen, C.5    Post, J.A.6
  • 21
    • 0035212719 scopus 로고    scopus 로고
    • Functional genomics of plant photosynthesis in the fast lane using Chlamydomonas reinhardtii
    • Dent RM, Han M, Niyogi KK. 2001. Functional genomics of plant photosynthesis in the fast lane using Chlamydomonas reinhardtii. Trends in Plant Science 6:364-371. doi: 10.1016/S1360-1385(01)02018-0.
    • (2001) Trends in Plant Science , vol.6 , pp. 364-371
    • Dent, R.M.1    Han, M.2    Niyogi, K.K.3
  • 23
    • 1642331709 scopus 로고    scopus 로고
    • Architecture of the photosynthetic oxygenevolving Center
    • Ferreira KN, Iverson TM, Maghlaoui K, Barber J, Iwata S. 2004. Architecture of the photosynthetic oxygenevolving Center. Science 303:1831-1838. doi: 10.1126/science.1093087.
    • (2004) Science , vol.303 , pp. 1831-1838
    • Ferreira, K.N.1    Iverson, T.M.2    Maghlaoui, K.3    Barber, J.4    Iwata, S.5
  • 24
    • 0032503986 scopus 로고    scopus 로고
    • Primary production of the biosphere: Integrating terrestrial and oceanic components
    • Field CB, Behrenfeld MJ, Randerson JT, Falkowski P. 1998. Primary production of the biosphere: integrating terrestrial and oceanic components. Science 281:237-240. doi: 10.1126/science.281.5374.237.
    • (1998) Science , vol.281 , pp. 237-240
    • Field, C.B.1    Behrenfeld, M.J.2    Randerson, J.T.3    Falkowski, P.4
  • 27
    • 84900851520 scopus 로고    scopus 로고
    • Coordinate transformation based cryo-correlative methods for electron tomography and focused ion beam milling
    • Fukuda Y, Schrod N, Schaffer M, Feng LR, Baumeister W, Lucic V. 2014. Coordinate transformation based cryo-correlative methods for electron tomography and focused ion beam milling. Ultramicroscopy 143:15-23. doi: 10.1016/j.ultramic.2013.11.008.
    • (2014) Ultramicroscopy , vol.143 , pp. 15-23
    • Fukuda, Y.1    Schrod, N.2    Schaffer, M.3    Feng, L.R.4    Baumeister, W.5    Lucic, V.6
  • 28
    • 0029137142 scopus 로고
    • Morphodynamical changes of the chloroplast of Chlamydomonas reinhardtii during the 1st round of division
    • Gaffal KP, Arnold CG, Friedrichs GJ, Gemple W. 1995. Morphodynamical changes of the chloroplast of Chlamydomonas reinhardtii during the 1st round of division. Archiv für Protistenkunde 145:10-23. doi: 10.1016/ S0003-9365(11)80297-6.
    • (1995) Archiv für Protistenkunde , vol.145 , pp. 10-23
    • Gaffal, K.P.1    Arnold, C.G.2    Friedrichs, G.J.3    Gemple, W.4
  • 29
    • 77954296052 scopus 로고    scopus 로고
    • The chloroplast protein CPSAR1, dually localized in the stroma and the inner envelope membrane, is involved in thylakoid biogenesis
    • Garcia C, Khan NZ, Nannmark U, Aronsson H. 2010. The chloroplast protein CPSAR1, dually localized in the stroma and the inner envelope membrane, is involved in thylakoid biogenesis. The Plant Journal 63:73-85. doi: 10.1111/j.1365-313X.2010.04225.x.
    • (2010) The Plant Journal , vol.63 , pp. 73-85
    • Garcia, C.1    Khan, N.Z.2    Nannmark, U.3    Aronsson, H.4
  • 30
    • 77953793713 scopus 로고    scopus 로고
    • Functional hybrid rubisco enzymes with plant small subunits and algal large subunits: Engineered rbcS cDNA for expression in Chlamydomonas
    • Genkov T, Meyer M, Griffiths H, Spreitzer RJ. 2010. Functional hybrid rubisco enzymes with plant small subunits and algal large subunits: engineered rbcS cDNA for expression in Chlamydomonas. The Journal of Biological Chemistry 285:19833-19841. doi: 10.1074/jbc.M110.124230.
    • (2010) The Journal of Biological Chemistry , vol.285 , pp. 19833-19841
    • Genkov, T.1    Meyer, M.2    Griffiths, H.3    Spreitzer, R.J.4
  • 31
    • 0344050940 scopus 로고
    • The ultrastructure of the chloroplasts of algae
    • Gibbs SP. 1962. The ultrastructure of the chloroplasts of algae. Journal of Ultrastructure Research 7:418-435. doi: 10.1016/S0022-5320(62)90038-2.
    • (1962) Journal of Ultrastructure Research , vol.7 , pp. 418-435
    • Gibbs, S.P.1
  • 32
    • 0015020492 scopus 로고
    • Structural differentiation of stacked and unstacked chloroplast membranes. Freeze-etch electron microscopy of wild-type and mutant strains of Chlamydomonas
    • Goodenough UW, Staehelin LA. 1971. Structural differentiation of stacked and unstacked chloroplast membranes. Freeze-etch electron microscopy of wild-type and mutant strains of Chlamydomonas. The Journal of Cell Biology 48:594-619. doi: 10.1083/jcb.48.3.594.
    • (1971) The Journal of Cell Biology , vol.48 , pp. 594-619
    • Goodenough, U.W.1    Staehelin, L.A.2
  • 33
    • 82555193810 scopus 로고    scopus 로고
    • Structural correlates of cytoplasmic and chloroplast lipid body synthesis in Chlamydomonas reinhardtii and stimulation of lipid body production with acetate boost
    • Goodson C, Roth R, Wang ZT, Goodenough U. 2011. Structural correlates of cytoplasmic and chloroplast lipid body synthesis in Chlamydomonas reinhardtii and stimulation of lipid body production with acetate boost. Eukaryot Cell 10:1592-1606. doi: 10.1128/ec.05242-11.
    • (2011) Eukaryot Cell , vol.10 , pp. 1592-1606
    • Goodson, C.1    Roth, R.2    Wang, Z.T.3    Goodenough, U.4
  • 34
    • 79953234083 scopus 로고    scopus 로고
    • Chloroplast genomes of photosynthetic eukaryotes
    • Green BR. 2011. Chloroplast genomes of photosynthetic eukaryotes. The Plant Journal 66:34-44. doi: 10.1111/j.1365-313X.2011.04541.x.
    • (2011) The Plant Journal , vol.66 , pp. 34-44
    • Green, B.R.1
  • 35
    • 0008129654 scopus 로고
    • The osmiophilic globules of chloroplasts: I. Osmiophilic globules as a normal component of chloroplasts and their isolation and composition in Vicia faba L
    • Greenwood AD, Leech RM, Williams JP. 1963. The osmiophilic globules of chloroplasts: I. Osmiophilic globules as a normal component of chloroplasts and their isolation and composition in Vicia faba L. Biochimica Et Biophysica Acta 78:148-162. doi: 10.1016/0006-3002(63)91620-2.
    • (1963) Biochimica Et Biophysica Acta , vol.78 , pp. 148-162
    • Greenwood, A.D.1    Leech, R.M.2    Williams, J.P.3
  • 37
    • 0034093493 scopus 로고    scopus 로고
    • Chlamydomonas reinhardtii and photosynthesis: Genetics to genomics
    • Grossman AR. 2000. Chlamydomonas reinhardtii and photosynthesis: genetics to genomics. Current Opinion in Plant Biology 3:132-137. doi: 10.1016/S1369-5266(99)00053-9.
    • (2000) Current Opinion in Plant Biology , vol.3 , pp. 132-137
    • Grossman, A.R.1
  • 38
    • 42649085386 scopus 로고    scopus 로고
    • Compression and crevasses in vitreous sections under different cutting conditions
    • Han HM, Zuber B, Dubochet J. 2008. Compression and crevasses in vitreous sections under different cutting conditions. Journal of Microscopy 230:167-171. doi: 10.1111/j.1365-2818.2008.01972.x.
    • (2008) Journal of Microscopy , vol.230 , pp. 167-171
    • Han, H.M.1    Zuber, B.2    Dubochet, J.3
  • 39
    • 0043011390 scopus 로고    scopus 로고
    • The Chlamydomonas reinhardtii cia3 mutant lacking a thylakoid lumen-localized carbonic anhydrase is limited by CO2 supply to rubisco and not photosystem II function in vivo
    • Hanson DT, Franklin LA, Samuelsson G, Badger MR. 2003. The Chlamydomonas reinhardtii cia3 mutant lacking a thylakoid lumen-localized carbonic anhydrase is limited by CO2 supply to rubisco and not photosystem II function in vivo. Plant Physiology 132:2267-2275. doi: 10.1104/pp.103.023481.
    • (2003) Plant Physiology , vol.132 , pp. 2267-2275
    • Hanson, D.T.1    Franklin, L.A.2    Samuelsson, G.3    Badger, M.R.4
  • 42
    • 34347396814 scopus 로고    scopus 로고
    • A technique for improved focused ion beam milling of cryoprepared life science specimens
    • Hayles MF, Stokes DJ, Phifer D, Findlay KC. 2007. A technique for improved focused ion beam milling of cryoprepared life science specimens. Journal of Microscopy 226:263-269. doi: 10.1111/j.1365-2818.2007.01775.x.
    • (2007) Journal of Microscopy , vol.226 , pp. 263-269
    • Hayles, M.F.1    Stokes, D.J.2    Phifer, D.3    Findlay, K.C.4
  • 43
    • 40349094722 scopus 로고    scopus 로고
    • 3-D ultrastructure of O. Tauri: Electron cryotomography of an entire eukaryotic cell
    • Henderson GP, Gan L, Jensen GJ. 2007. 3-D ultrastructure of O. tauri: electron cryotomography of an entire eukaryotic cell. PLOS ONE 2:749. doi: 10.1371/journal.pone.0000749.
    • (2007) PLOS ONE , vol.2 , pp. 749
    • Henderson, G.P.1    Gan, L.2    Jensen, G.J.3
  • 44
    • 0042345326 scopus 로고
    • Structure and Morphogenesis of lamellar systems in grana-containing chloroplasts
    • Heslop-Harrison J. 1963. Structure and Morphogenesis of lamellar systems in grana-containing chloroplasts. Planta 60:243-260. doi: 10.1007/BF01937960.
    • (1963) Planta , vol.60 , pp. 243-260
    • Heslop-Harrison, J.1
  • 46
    • 0014301575 scopus 로고
    • The presence of a crystalline matrix in pyrenoids of the diatom, Achnanthes brevipes
    • Holdsworth RH. 1968. The presence of a crystalline matrix in pyrenoids of the diatom, Achnanthes brevipes. The Journal of Cell Biology 37:831-837. doi: 10.1083/jcb.37.3.831.
    • (1968) The Journal of Cell Biology , vol.37 , pp. 831-837
    • Holdsworth, R.H.1
  • 47
    • 0015158987 scopus 로고
    • The isolation and partial characterization of the pyrenoid protein of Eremosphaera viridis
    • Holdsworth RH. 1971. The isolation and partial characterization of the pyrenoid protein of Eremosphaera viridis. The Journal of Cell Biology 51:499-513. doi: 10.1083/jcb.51.2.499.
    • (1971) The Journal of Cell Biology , vol.51 , pp. 499-513
    • Holdsworth, R.H.1
  • 48
    • 84860584901 scopus 로고    scopus 로고
    • PyTom: A python-based toolbox for localization of macromolecules in cryo-electron tomograms and subtomogram analysis
    • Hrabe T, Chen Y, Pfeffer S, Cuellar LK, Mangold AV, Förster F. 2012. PyTom: a python-based toolbox for localization of macromolecules in cryo-electron tomograms and subtomogram analysis. Journal of Structural Biology 178:177-188. doi: 10.1016/j.jsb.2011.12.003.
    • (2012) Journal of Structural Biology , vol.178 , pp. 177-188
    • Hrabe, T.1    Chen, Y.2    Pfeffer, S.3    Cuellar, L.K.4    Mangold, A.V.5    Förster, F.6
  • 49
    • 84890952715 scopus 로고    scopus 로고
    • Practical workflow for cryo focused-ionbeam milling of tissues and cells for cryo-TEM tomography
    • Hsieh C, Schmelzer T, Kishchenko G, Wagenknecht T, Marko M. 2014. Practical workflow for cryo focused-ionbeam milling of tissues and cells for cryo-TEM tomography. Journal of Structural Biology 185:32-41. doi: 10.1016/j.jsb.2013.10.019.
    • (2014) Journal of Structural Biology , vol.185 , pp. 32-41
    • Hsieh, C.1    Schmelzer, T.2    Kishchenko, G.3    Wagenknecht, T.4    Marko, M.5
  • 50
    • 0036410825 scopus 로고    scopus 로고
    • Electron tomographic analysis of frozen-hydrated tissue sections
    • Hsieh CE, Marko M, Frank J, Mannella CA. 2002. Electron tomographic analysis of frozen-hydrated tissue sections. Journal of Structural Biology 138:63-73. doi: 10.1016/S1047-8477(02)00034-5
    • (2002) Journal of Structural Biology , vol.138 , pp. 63-73
    • Hsieh, C.E.1    Marko, M.2    Frank, J.3    Mannella, C.A.4
  • 53
    • 74649083831 scopus 로고    scopus 로고
    • Organization, structure, and assembly of alpha-carboxysomes determined by electron cryotomography of intact cells
    • Iancu CV, Morris DM, Dou Z, Heinhorst S, Cannon GC, Jensen GJ. 2010. Organization, structure, and assembly of alpha-carboxysomes determined by electron cryotomography of intact cells. Journal of Molecular Biology 396:105-117. doi: 10.1016/j.jmb.2009.11.019.
    • (2010) Journal of Molecular Biology , vol.396 , pp. 105-117
    • Iancu, C.V.1    Morris, D.M.2    Dou, Z.3    Heinhorst, S.4    Cannon, G.C.5    Jensen, G.J.6
  • 54
    • 77956094365 scopus 로고    scopus 로고
    • Significant CO2 fixation by small prymnesiophytes in the subtropical and tropical northeast Atlantic Ocean
    • Jardillier L, Zubkov MV, Pearman J, Scanlan DJ. 2010. Significant CO2 fixation by small prymnesiophytes in the subtropical and tropical northeast Atlantic Ocean. The ISME Journal 4:1180-1192. doi: 10.1038/ismej.2010.36.
    • (2010) The ISME Journal , vol.4 , pp. 1180-1192
    • Jardillier, L.1    Zubkov, M.V.2    Pearman, J.3    Scanlan, D.J.4
  • 55
    • 0032473423 scopus 로고    scopus 로고
    • A novel alpha-type carbonic anhydrase associated with the thylakoid membrane in Chladomonas reinhardtii is required for growth at ambient CO2
    • Karlsson J, Clarke AK, Chen ZY, Hugghins SY, Park YI, Husic HD, Moroney JV, Samuelsson G. 1998. A novel alpha-type carbonic anhydrase associated with the thylakoid membrane in Chlamydomonas reinhardtii is required for growth at ambient CO2. The EMBO Journal 17:1208-1216. doi: 10.1093/ emboj/17.5.1208.
    • (1998) The EMBO Journal , vol.17 , pp. 1208-1216
    • Karlsson, J.1    Clarke, A.K.2    Chen, Z.Y.3    Hugghins, S.Y.4    Park, Y.I.5    Husic, H.D.6    Moroney, J.V.7    Samuelsson, G.8
  • 56
    • 2442455673 scopus 로고    scopus 로고
    • Green light for galactolipid trafficking
    • Kelly AA, Dormann P. 2004. Green light for galactolipid trafficking. Current Opinion in Plant Biology 7:262-269. doi: 10.1016/j.pbi.2004.03.009.
    • (2004) Current Opinion in Plant Biology , vol.7 , pp. 262-269
    • Kelly, A.A.1    Dormann, P.2
  • 57
    • 84875640465 scopus 로고    scopus 로고
    • New putative chloroplast vesicle transport components and cargo proteins revealed using a bioinformatics approach: An Arabidopsis model
    • Khan NZ, Lindquist E, Aronsson H. 2013. New putative chloroplast vesicle transport components and cargo proteins revealed using a bioinformatics approach: an Arabidopsis model. PLOS ONE 8:59898. doi: 10.1371/journal.pone.0059898.
    • (2013) PLOS ONE , vol.8 , pp. 59898
    • Khan, N.Z.1    Lindquist, E.2    Aronsson, H.3
  • 60
    • 40649085591 scopus 로고    scopus 로고
    • Structural analysis of photosynthetic membranes by cryo-electron tomography of intact Rhodopseudomonas viridis cells
    • Konorty M, Kahana N, Linaroudis A, Minsky A, Medalia O. 2008. Structural analysis of photosynthetic membranes by cryo-electron tomography of intact Rhodopseudomonas viridis cells. Journal of Structural Biology 161:393-400. doi: 10.1016/j.jsb.2007.09.014.
    • (2008) Journal of Structural Biology , vol.161 , pp. 393-400
    • Konorty, M.1    Kahana, N.2    Linaroudis, A.3    Minsky, A.4    Medalia, O.5
  • 61
    • 79960898027 scopus 로고    scopus 로고
    • Computer controlled cryo-electron microscopyTOM2 a software package for high-throughput applications
    • Korinek A, Beck F, Baumeister W, Nickell S, Plitzko JM. 2011. Computer controlled cryo-electron microscopyTOM2 a software package for high-throughput applications. Journal of Structural Biology 175:394-405. doi: 10.1016/j.jsb.2011.06.003.
    • (2011) Journal of Structural Biology , vol.175 , pp. 394-405
    • Korinek, A.1    Beck, F.2    Baumeister, W.3    Nickell, S.4    Plitzko, J.M.5
  • 62
    • 79651473928 scopus 로고    scopus 로고
    • Fine structure of granal thylakoid membrane organization using cryo electron tomography
    • Kouřil R, Oostergetel GT, Boekema EJ. 2011. Fine structure of granal thylakoid membrane organization using cryo electron tomography. Biochimica Et Biophysica Acta 1807:368-374. doi: 10.1016/j.bbabio.2010.11.007.
    • (2011) Biochimica Et Biophysica Acta , vol.1807 , pp. 368-374
    • Kouřil, R.1    Oostergetel, G.T.2    Boekema, E.J.3
  • 63
    • 0014535318 scopus 로고
    • The crystal lattice of the pyrenoid matrix of Prorocentrum micans
    • Kowallik K. 1969. The crystal lattice of the pyrenoid matrix of Prorocentrum micans. Journal of Cell Science 5:251-269.
    • (1969) Journal of Cell Science , vol.5 , pp. 251-269
    • Kowallik, K.1
  • 64
    • 59649107665 scopus 로고    scopus 로고
    • The green algal eyespot apparatus: A primordial visual system and more?
    • Kreimer G. 2009. The green algal eyespot apparatus: a primordial visual system and more? Current Genetics 55:19-43. doi: 10.1007/s00294-008-0224-8.
    • (2009) Current Genetics , vol.55 , pp. 19-43
    • Kreimer, G.1
  • 65
    • 0025153850 scopus 로고
    • Reflection confocal laser scanning microscopy of eyespots in flagellated green algae
    • Kreimer G, Melkonian M. 1990. Reflection confocal laser scanning microscopy of eyespots in flagellated green algae. European Journal of Cell Biology 53:101-111.
    • (1990) European Journal of Cell Biology , vol.53 , pp. 101-111
    • Kreimer, G.1    Melkonian, M.2
  • 67
    • 0020355744 scopus 로고
    • Thylakoid centers: Structures associated with the cyanobacterial photosynthetic membrane system
    • Kunkel DD. 1982. Thylakoid centers: structures associated with the cyanobacterial photosynthetic membrane system. Archives of Microbiology 133:97-99. doi: 10.1007/BF00413518.
    • (1982) Archives of Microbiology , vol.133 , pp. 97-99
    • Kunkel, D.D.1
  • 68
    • 0000104250 scopus 로고
    • Immunocytochemical localization of ribulose-1,5-bisphosphate carboxylase in the pyrenoid and thylakoid region of the chloroplast of Chlamydomonas reinhardtii
    • Lacoste-Royal G, Gibbs SP. 1987. Immunocytochemical localization of ribulose-1,5-bisphosphate carboxylase in the pyrenoid and thylakoid region of the chloroplast of Chlamydomonas reinhardtii. Plant Physiology 83: 602-606. doi: 10.1104/pp.83.3.602.
    • (1987) Plant Physiology , vol.83 , pp. 602-606
    • Lacoste-Royal, G.1    Gibbs, S.P.2
  • 69
    • 84861914247 scopus 로고    scopus 로고
    • Contribution of cryoelectron microscopy of vitreous sections to the understanding of biological membrane structure
    • Leforestier A, Lemercier N, Livolant F. 2012. Contribution of cryoelectron microscopy of vitreous sections to the understanding of biological membrane structure. Proceedings of the National Academy of Sciences of the USA 109:8959-8964. doi: 10.1073/pnas.1200881109.
    • (2012) Proceedings of the National Academy of Sciences of the USA , vol.109 , pp. 8959-8964
    • Leforestier, A.1    Lemercier, N.2    Livolant, F.3
  • 70
    • 79955602317 scopus 로고    scopus 로고
    • Insights into the complex 3-D architecture of thylakoid membranes in unicellular cyanobacterium Cyanothece sp. ATCC 51142
    • Liberton M, Austin JR II, Berg RH, Pakrasi HB. 2011a. Insights into the complex 3-D architecture of thylakoid membranes in unicellular cyanobacterium Cyanothece sp. ATCC 51142. Plant Signaling & Behavior 6:566-569. doi: 10.4161/psb.6.4.14946.
    • (2011) Plant Signaling & Behavior , vol.6 , pp. 566-569
    • Liberton, M.1    Austin, J.2    Berg, R.H.3    Pakrasi, H.B.4
  • 71
    • 79953707616 scopus 로고    scopus 로고
    • Unique thylakoid membrane architecture of a unicellular N2-fixing cyanobacterium revealed by electron tomography
    • Liberton M, Austin JR II, Berg RH, Pakrasi HB. 2011b. Unique thylakoid membrane architecture of a unicellular N2-fixing cyanobacterium revealed by electron tomography. Plant Physiology 155:1656-1666. doi: 10.1104/ pp.110.165332.
    • (2011) Plant Physiology , vol.155 , pp. 1656-1666
    • Liberton, M.1    Austin, J.2    Berg, R.H.3    Pakrasi, H.B.4
  • 72
    • 35748946615 scopus 로고    scopus 로고
    • Analysis of carboxysomes from Synechococcus PCC7942 reveals multiple Rubisco complexes with carboxysomal proteins CcmM and CcaA
    • Long BM, Badger MR, Whitney SM, Price GD. 2007. Analysis of carboxysomes from Synechococcus PCC7942 reveals multiple Rubisco complexes with carboxysomal proteins CcmM and CcaA. The Journal of Biological Chemistry 282:29323-29335. doi: 10.1074/jbc.M703896200.
    • (2007) The Journal of Biological Chemistry , vol.282 , pp. 29323-29335
    • Long, B.M.1    Badger, M.R.2    Whitney, S.M.3    Price, G.D.4
  • 73
    • 77951980276 scopus 로고    scopus 로고
    • Functional cyanobacterial beta-carboxysomes have an absolute requirement for both long and short forms of the CcmM protein
    • Long BM, Tucker L, Badger MR, Price GD. 2010. Functional cyanobacterial beta-carboxysomes have an absolute requirement for both long and short forms of the CcmM protein. Plant Physiology 153:285-293. doi: 10.1104/ pp.110.154948.
    • (2010) Plant Physiology , vol.153 , pp. 285-293
    • Long, B.M.1    Tucker, L.2    Badger, M.R.3    Price, G.D.4
  • 74
    • 79958037926 scopus 로고    scopus 로고
    • Identification of a novel gene, CIA6, required for normal pyrenoid formation in Chlamydomonas reinhardtii
    • Ma Y, Pollock SV, Xiao Y, Cunnusamy K, Moroney JV. 2011. Identification of a novel gene, CIA6, required for normal pyrenoid formation in Chlamydomonas reinhardtii. Plant Physiology 156:884-896. doi: 10.1104/pp.111.173922
    • (2011) Plant Physiology , vol.156 , pp. 884-896
    • Ma, Y.1    Pollock, S.V.2    Xiao, Y.3    Cunnusamy, K.4    Moroney, J.V.5
  • 75
    • 33847685630 scopus 로고    scopus 로고
    • Focused-ion-beam thinning of frozen-hydrated biological specimens for cryo-electron microscopy
    • Marko M, Hsieh C, Schalek R, Frank J, Mannella C. 2007. Focused-ion-beam thinning of frozen-hydrated biological specimens for cryo-electron microscopy. Nature Methods 4:215-217. doi: 10.1038/nmeth1014
    • (2007) Nature Methods , vol.4 , pp. 215-217
    • Marko, M.1    Hsieh, C.2    Schalek, R.3    Frank, J.4    Mannella, C.5
  • 76
    • 0031422417 scopus 로고    scopus 로고
    • Dual-axis tomography: An approach with alignment methods that preserve resolution
    • Mastronarde DN. 1997. Dual-axis tomography: an approach with alignment methods that preserve resolution. Journal of Structural Biology 120:343-352. doi: 10.1006/jsbi.1997.3919.
    • (1997) Journal of Structural Biology , vol.120 , pp. 343-352
    • Mastronarde, D.N.1
  • 77
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde DN. 2005. Automated electron microscope tomography using robust prediction of specimen movements. Journal of Structural Biology 152:36-51. doi: 10.1016/j.jsb.2005.07.007
    • (2005) Journal of Structural Biology , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 78
    • 0000287479 scopus 로고
    • Composition and function of pyrenoids: Cytochemical and immunocytochemical approaches
    • McKay RML, Gibbs SP. 1991. Composition and function of pyrenoids: cytochemical and immunocytochemical approaches. Canadian Journal of Botany 69:1040-1052. doi: 10.1139/b91-134.
    • (1991) Canadian Journal of Botany , vol.69 , pp. 1040-1052
    • McKay, R.1    Gibbs, S.P.2
  • 79
    • 84874669850 scopus 로고    scopus 로고
    • Origins and diversity of eukaryotic CO2-concentrating mechanisms: Lessons for the future
    • Meyer M, Griffiths H. 2013. Origins and diversity of eukaryotic CO2-concentrating mechanisms: lessons for the future. Journal of Experimental Botany 64:769-786. doi: 10.1093/jxb/ers390.
    • (2013) Journal of Experimental Botany , vol.64 , pp. 769-786
    • Meyer, M.1    Griffiths, H.2
  • 81
    • 75549087930 scopus 로고    scopus 로고
    • BioNumbers-the database of key numbers in molecular and cell biology
    • Milo R, Jorgensen P, Moran U, Weber G, Springer M. 2010. BioNumbers-the database of key numbers in molecular and cell biology. Nucleic Acids Research 38:D750-D753. doi: 10.1093/nar/gkp889.
    • (2010) Nucleic Acids Research , vol.38 , pp. D750-D753
    • Milo, R.1    Jorgensen, P.2    Moran, U.3    Weber, G.4    Springer, M.5
  • 82
    • 84907790384 scopus 로고    scopus 로고
    • Dynamics of carbon-concentrating mechanism induction and protein Relocalization during the dark-to-light transition in Synchronized Chlamydomonas reinhardtii
    • Mitchell MC, Meyer MT, Griffiths H. 2014. Dynamics of carbon-concentrating mechanism induction and protein Relocalization during the dark-to-light transition in Synchronized Chlamydomonas reinhardtii. Plant Physiology 166:1073-1082. doi: 10.1104/pp.114.246918.
    • (2014) Plant Physiology , vol.166 , pp. 1073-1082
    • Mitchell, M.C.1    Meyer, M.T.2    Griffiths, H.3
  • 83
    • 33748433657 scopus 로고    scopus 로고
    • Differences in chloroplast ultrastructure of Phaeocystis antarctica in low and high light
    • Moisan T, Ellisman M, Buitenhuys C, Sosinsky G. 2006. Differences in chloroplast ultrastructure of Phaeocystis antarctica in low and high light. Marine Biology 149:1281-1290. doi: 10.1007/s00227-006-0321-5.
    • (2006) Marine Biology , vol.149 , pp. 1281-1290
    • Moisan, T.1    Ellisman, M.2    Buitenhuys, C.3    Sosinsky, G.4
  • 85
    • 0037712992 scopus 로고    scopus 로고
    • Granum revisited. A three-dimensional model-where things fall into place
    • Mustárdy L, Garab G. 2003. Granum revisited. A three-dimensional model-where things fall into place. Trends in Plant Science 8:117-122. doi: 10.1016/S1360-1385(03)00015-3.
    • (2003) Trends in Plant Science , vol.8 , pp. 117-122
    • Mustárdy, L.1    Garab, G.2
  • 86
    • 33947105612 scopus 로고    scopus 로고
    • Thylakoid membrane perforations and connectivity enable intracellular traffic in cyanobacteria
    • Nevo R, Charuvi D, Shimoni E, Schwarz R, Kaplan A, Ohad I, Reich Z. 2007. Thylakoid membrane perforations and connectivity enable intracellular traffic in cyanobacteria. The EMBO Journal 26:1467-1473. doi: 10.1038/ sj.emboj.7601594.
    • (2007) The EMBO Journal , vol.26 , pp. 1467-1473
    • Nevo, R.1    Charuvi, D.2    Shimoni, E.3    Schwarz, R.4    Kaplan, A.5    Ohad, I.6    Reich, Z.7
  • 89
    • 0014176666 scopus 로고
    • Biogenesis of chloroplast membranes. I. Plastid dedifferentiation in a dark-grown algal mutant (Chlamydomonas reinhardii)
    • Ohad I, Siekevitz P, Palade GE. 1967a. Biogenesis of chloroplast membranes. I. Plastid dedifferentiation in a dark-grown algal mutant (Chlamydomonas reinhardii). The Journal of Cell Biology 35:521-552. doi: 10.1083/jcb.35.3.521.
    • (1967) The Journal of Cell Biology , vol.35 , pp. 521-552
    • Ohad, I.1    Siekevitz, P.2    Palade, G.E.3
  • 90
    • 0014177196 scopus 로고
    • Biogenesis of chloroplast membranes. II. Plastid differentiation during greening of a dark-grown algal mutant (Chlamydomonas reinhardii)
    • Ohad I, Siekevitz P, Palade GE. 1967b. Biogenesis of chloroplast membranes. II. Plastid differentiation during greening of a dark-grown algal mutant (Chlamydomonas reinhardii). The Journal of Cell Biology 35: 553-584.doi: 10.1083/jcb.35.3.553.
    • (1967) The Journal of Cell Biology , vol.35 , pp. 553-584
    • Ohad, I.1    Siekevitz, P.2    Palade, G.E.3
  • 91
    • 0014534940 scopus 로고
    • Ultrastructural observations on deep-etched thylakoids
    • Park RB, Pfeifhofer AO. 1969. Ultrastructural observations on deep-etched thylakoids. Journal of Cell Science 5:299-311.
    • (1969) Journal of Cell Science , vol.5 , pp. 299-311
    • Park, R.B.1    Pfeifhofer, A.O.2
  • 94
    • 84865781069 scopus 로고    scopus 로고
    • Structure and 3D arrangement of endoplasmic reticulum membrane-associated ribosomes
    • Pfeffer S, Brandt F, Hrabe T, Lang S, Eibauer M, Zimmermann R, Forster F. 2012. Structure and 3D arrangement of endoplasmic reticulum membrane-associated ribosomes. Structure 20:1508-1518. doi: 10.1016/j.str.2012.06.010.
    • (2012) Structure , vol.20 , pp. 1508-1518
    • Pfeffer, S.1    Brandt, F.2    Hrabe, T.3    Lang, S.4    Eibauer, M.5    Zimmermann, R.6    Forster, F.7
  • 95
    • 84898933675 scopus 로고    scopus 로고
    • Structure and dynamics of thylakoids in land plants
    • Pribil M, Labs M, Leister D. 2014. Structure and dynamics of thylakoids in land plants. Journal of Experimental Botany 65:1955-1972. doi: 10.1093/jxb/eru090.
    • (2014) Journal of Experimental Botany , vol.65 , pp. 1955-1972
    • Pribil, M.1    Labs, M.2    Leister, D.3
  • 97
    • 0031043931 scopus 로고    scopus 로고
    • CO2-concentrating mechanisms: A direct role for thylakoid lumen acidification?
    • Raven JA. 1997. CO2-concentrating mechanisms: a direct role for thylakoid lumen acidification? Plant Cell & Environment 20:147-154. doi: 10.1046/j.1365-3040.1997.d01-67.x.
    • (1997) Plant Cell & Environment , vol.20 , pp. 147-154
    • Raven, J.A.1
  • 98
    • 0030024554 scopus 로고    scopus 로고
    • Chlamydomonas reinhardtii mutants without ribulose-1,5bisphosphate carboxylase-oxygenase lack a detectable pyrenoid
    • Rawat M, Henk M, Lavigne L, Moroney J. 1996. Chlamydomonas reinhardtii mutants without ribulose-1,5bisphosphate carboxylase-oxygenase lack a detectable pyrenoid. Planta 198:263-270. doi: 10.1007/BF00206252.
    • (1996) Planta , vol.198 , pp. 263-270
    • Rawat, M.1    Henk, M.2    Lavigne, L.3    Moroney, J.4
  • 101
    • 84864386261 scopus 로고    scopus 로고
    • Integrative approaches for cellular cryo-electron tomography: Correlative imaging and focused ion beam micromachining
    • Rigort A, Villa E, Bauerlein FJ, Engel BD, Plitzko JM. 2012b. Integrative approaches for cellular cryo-electron tomography: correlative imaging and focused ion beam micromachining. Methods in Cell Biology 111:259-281. doi: 10.1016/b978-0-12-416026-2.00014-5.
    • (2012) Methods in Cell Biology , vol.111 , pp. 259-281
    • Rigort, A.1    Villa, E.2    Bauerlein, F.J.3    Engel, B.D.4    Plitzko, J.M.5
  • 102
    • 0000542459 scopus 로고
    • Structure and development of the chloroplast in Chlamydomonas. I. The normal green cell
    • Sager R, Palade GE. 1957. Structure and development of the chloroplast in Chlamydomonas. I. The normal green cell. The Journal of Biophysical and Biochemical Cytology 3:463-488. doi: 10.1083/jcb.3.3.463
    • (1957) The Journal of Biophysical and Biochemical Cytology , vol.3 , pp. 463-488
    • Sager, R.1    Palade, G.E.2
  • 105
    • 33644687594 scopus 로고    scopus 로고
    • Three-dimensional organization of higher-plant chloroplast thylakoid membranes revealed by electron tomography
    • Shimoni E, Rav-Hon O, Ohad I, Brumfeld V, Reich Z. 2005. Three-dimensional organization of higher-plant chloroplast thylakoid membranes revealed by electron tomography. The Plant Cell 17:2580-2586. doi: 10.1105/tpc.105.035030.
    • (2005) The Plant Cell , vol.17 , pp. 2580-2586
    • Shimoni, E.1    Rav-Hon, O.2    Ohad, I.3    Brumfeld, V.4    Reich, Z.5
  • 106
    • 84862180540 scopus 로고    scopus 로고
    • Identification and functional role of the carbonic anhydrase Cah3 in thylakoid membranes of pyrenoid of Chlamydomonas reinhardtii
    • Sinetova MA, Kupriyanova EV, Markelova AG, Allakhverdiev SI, Pronina NA. 2012. Identification and functional role of the carbonic anhydrase Cah3 in thylakoid membranes of pyrenoid of Chlamydomonas reinhardtii. Biochimica Et Biophysica Acta 1817:1248-1255. doi: 10.1016/j.bbabio.2012.02.014.
    • (2012) Biochimica Et Biophysica Acta , vol.1817 , pp. 1248-1255
    • Sinetova, M.A.1    Kupriyanova, E.V.2    Markelova, A.G.3    Allakhverdiev, S.I.4    Pronina, N.A.5
  • 107
    • 0041859209 scopus 로고    scopus 로고
    • Chloroplast structure: From chlorophyll granules to supra-molecular architecture of thylakoid membranes
    • Staehelin LA. 2003. Chloroplast structure: from chlorophyll granules to supra-molecular architecture of thylakoid membranes. Photosynthesis Research 76:185-196. doi: 10.1023/a:1024994525586.
    • (2003) Photosynthesis Research , vol.76 , pp. 185-196
    • Staehelin, L.A.1
  • 108
    • 0001363467 scopus 로고
    • Composition and function of plastoglobuli: I. Isolation and purification from chloroplasts and chromoplasts
    • Steinmüller D, Tevini M. 1985. Composition and function of plastoglobuli: I. Isolation and purification from chloroplasts and chromoplasts. Planta 163:201-207. doi: 10.1007/BF00393507.
    • (1985) Planta , vol.163 , pp. 201-207
    • Steinmüller, D.1    Tevini, M.2
  • 109
    • 84859080796 scopus 로고    scopus 로고
    • Initial steps of photosystem II de novo assembly and preloading with manganese take place in biogenesis centers in Synechocystis
    • Stengel A, Gugel IL, Hilger D, Rengstl B, Jung H, Nickelsen J. 2012. Initial steps of photosystem II de novo assembly and preloading with manganese take place in biogenesis centers in Synechocystis. The Plant Cell 24:660-675. doi: 10.1105/tpc.111.093914.
    • (2012) The Plant Cell , vol.24 , pp. 660-675
    • Stengel, A.1    Gugel, I.L.2    Hilger, D.3    Rengstl, B.4    Jung, H.5    Nickelsen, J.6
  • 110
    • 0001206497 scopus 로고
    • Rubisco activase mediates ATP-dependent activation of ribulose bisphosphate carboxylase
    • Streusand VJ, Portis AR. 1987. Rubisco activase mediates ATP-dependent activation of ribulose bisphosphate carboxylase. Plant Physiology 85:152-154. doi: 10.1104/pp.85.1.152.
    • (1987) Plant Physiology , vol.85 , pp. 152-154
    • Streusand, V.J.1    Portis, A.R.2
  • 111
    • 84865441692 scopus 로고    scopus 로고
    • Thinning of large mammalian cells for cryo-TEM characterization by cryo-FIB milling
    • Strunk KM, Wang K, Ke D, Gray JL, Zhang P. 2012. Thinning of large mammalian cells for cryo-TEM characterization by cryo-FIB milling. Journal of Microscopy 247:220-227. doi: 10.1111/j.1365-2818.2012.03635.x
    • (2012) Journal of Microscopy , vol.247 , pp. 220-227
    • Strunk, K.M.1    Wang, K.2    Ke, D.3    Gray, J.L.4    Zhang, P.5
  • 112
    • 0029110706 scopus 로고
    • In Situ association of Calvin cycle enzymes, ribulose-1,5-bisphosphate Carboxylase/Oxygenase activase, Ferredoxin-NADP+ Reductase, and Nitrite Reductase with thylakoid and pyrenoid membranes of Chlamydomonas reinhardtii chloroplasts as revealed by Immunoelectron microscopy
    • Suss KH, Prokhorenko I, Adler K. 1995. In Situ association of Calvin cycle enzymes, ribulose-1,5-bisphosphate Carboxylase/Oxygenase activase, Ferredoxin-NADP+ Reductase, and Nitrite Reductase with thylakoid and pyrenoid membranes of Chlamydomonas reinhardtii chloroplasts as revealed by Immunoelectron microscopy. Plant Physiology 107:1387-1397.
    • (1995) Plant Physiology , vol.107 , pp. 1387-1397
    • Suss, K.H.1    Prokhorenko, I.2    Adler, K.3
  • 114
    • 0038271917 scopus 로고    scopus 로고
    • Isolation and characterisation of Chlamydomonas reinhardtii mutants with an impaired CO2-concentrating mechanism
    • Thyssen C, Hermes M, Sultemeyer D. 2003. Isolation and characterisation of Chlamydomonas reinhardtii mutants with an impaired CO2-concentrating mechanism. Planta 217:102-112. doi: 10.1007/ s00425-002-0961-8.
    • (2003) Planta , vol.217 , pp. 102-112
    • Thyssen, C.1    Hermes, M.2    Sultemeyer, D.3
  • 115
    • 34250338914 scopus 로고    scopus 로고
    • Cryo-electron tomography reveals the comparative three-dimensional architecture of Prochlorococcus, a globally important marine cyanobacterium
    • Ting CS, Hsieh C, Sundararaman S, Mannella C, Marko M. 2007. Cryo-electron tomography reveals the comparative three-dimensional architecture of Prochlorococcus, a globally important marine cyanobacterium. Journal of Bacteriology 189:4485-4493. doi: 10.1128/jb.01948-06.
    • (2007) Journal of Bacteriology , vol.189 , pp. 4485-4493
    • Ting, C.S.1    Hsieh, C.2    Sundararaman, S.3    Mannella, C.4    Marko, M.5
  • 116
    • 37849013494 scopus 로고    scopus 로고
    • Photosystem II assembly and repair are differentially localized in Chlamydomonas
    • Uniacke J, Zerges W. 2007. Photosystem II assembly and repair are differentially localized in Chlamydomonas. The Plant Cell 19:3640-3654. doi: 10.1105/tpc.107.054882.
    • (2007) The Plant Cell , vol.19 , pp. 3640-3654
    • Uniacke, J.1    Zerges, W.2
  • 117
    • 60849108324 scopus 로고    scopus 로고
    • Chloroplast protein targeting involves localized translation in Chlamydomonas
    • Uniacke J, Zerges W. 2009. Chloroplast protein targeting involves localized translation in Chlamydomonas. Proceedings of the National Academy of Sciences of the USA 106:1439-1444. doi: 10.1073/pnas.0811268106.
    • (2009) Proceedings of the National Academy of Sciences of the USA , vol.106 , pp. 1439-1444
    • Uniacke, J.1    Zerges, W.2
  • 119
    • 84885847209 scopus 로고    scopus 로고
    • Opening windows into the cell: Focused-ion-beam milling for cryo-electron tomography
    • Villa E, Schaffer M, Plitzko JM, Baumeister W. 2013. Opening windows into the cell: focused-ion-beam milling for cryo-electron tomography. Current Opinion in Structural Biology 23:771-777. doi: 10.1016/j.sbi.2013.08.006.
    • (2013) Current Opinion in Structural Biology , vol.23 , pp. 771-777
    • Villa, E.1    Schaffer, M.2    Plitzko, J.M.3    Baumeister, W.4
  • 120
    • 0030437744 scopus 로고    scopus 로고
    • The induction of the CO2 concentrating mechanism in a starch-less mutant of Chlamydomonas reinhardtii
    • Villarejo A, Martinez F, del Pino Plumed M, Ramazanov Z. 1996. The induction of the CO2 concentrating mechanism in a starch-less mutant of Chlamydomonas reinhardtii. Physiologia Plantarum 98:798-802. doi: 10.1111/j.1399-3054.1996.tb06687.x.
    • (1996) Physiologia Plantarum , vol.98 , pp. 798-802
    • Villarejo, A.1    Martinez, F.2    Del Pino Plumed, M.3    Ramazanov, Z.4
  • 121
    • 84867910247 scopus 로고    scopus 로고
    • 3D structure determination of native mammalian cells using cryo-FIB and cryo-electron tomography
    • Wang K, Strunk K, Zhao G, Gray JL, Zhang P. 2012. 3D structure determination of native mammalian cells using cryo-FIB and cryo-electron tomography. Journal of Structural Biology 180:318-326. doi: 10.1016/j.jsb.2012.07.003.
    • (2012) Journal of Structural Biology , vol.180 , pp. 318-326
    • Wang, K.1    Strunk, K.2    Zhao, G.3    Gray, J.L.4    Zhang, P.5
  • 122
    • 77955511591 scopus 로고    scopus 로고
    • Towards native-state imaging in biological context in the electron microscope
    • Weston AE, Armer HE, Collinson LM. 2009. Towards native-state imaging in biological context in the electron microscope. Journal of Chemical Biology 3:101-112. doi: 10.1007/s12154-009-0033-7
    • (2009) Journal of Chemical Biology , vol.3 , pp. 101-112
    • Weston, A.E.1    Armer, H.E.2    Collinson, L.M.3
  • 123
    • 84862907893 scopus 로고    scopus 로고
    • Bubblegrams reveal the inner body of bacteriophage ϕKZ
    • Wu W, Thomas JA, Cheng N, Black LW, Steven AC. 2012. Bubblegrams reveal the inner body of bacteriophage ϕKZ. Science 335:182. doi: 10.1126/science.1214120.
    • (2012) Science , vol.335 , pp. 182
    • Wu, W.1    Thomas, J.A.2    Cheng, N.3    Black, L.W.4    Steven, A.C.5
  • 124
    • 33646902709 scopus 로고    scopus 로고
    • Protein profiling of plastoglobules in chloroplasts and Chromoplasts. A Surprising site for differential accumulation of metabolic enzymes
    • Ytterberg AJ, Peltier J-B, van Wijk KJ. 2006. Protein profiling of plastoglobules in chloroplasts and Chromoplasts. A Surprising site for differential accumulation of metabolic enzymes. Plant Physiology 140: 984-997. doi: 10.1104/pp.105.076083.
    • (2006) Plant Physiology , vol.140 , pp. 984-997
    • Ytterberg, A.J.1    Peltier, J.-B.2    Van Wijk, K.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.