메뉴 건너뛰기




Volumn 77, Issue 3, 2013, Pages 357-379

Functions, compositions, and evolution of the two types of carboxysomes: Polyhedral microcompartments that facilitate CO2 fixation in cyanobacteria and some proteobacteria

Author keywords

[No Author keywords available]

Indexed keywords

CARBONATE DEHYDRATASE; MICROCYSTIN; RIBULOSEBISPHOSPHATE CARBOXYLASE;

EID: 84884528591     PISSN: 10922172     EISSN: 10985557     Source Type: Journal    
DOI: 10.1128/MMBR.00061-12     Document Type: Review
Times cited : (314)

References (246)
  • 2
    • 0037318701 scopus 로고    scopus 로고
    • 2 concentrating mechanisms in cyanobacteria: Molecular components, their diversity and evolution
    • DOI 10.1093/jxb/erg076
    • 2 concentrating mechanisms in cyanobacteria: molecular components, their diversity and evolution. J. Exp. Bot. 54:609-622. (Pubitemid 36189206)
    • (2003) Journal of Experimental Botany , vol.54 , Issue.383 , pp. 609-622
    • Badger, M.R.1    Price, G.D.2
  • 3
    • 0142134258 scopus 로고    scopus 로고
    • Inorganic carbon concentrating mechanisms in relation to the biology of algae
    • DOI 10.1023/A:1025877902752
    • Raven JA. 2003. Inorganic carbon concentrating mechanisms in relation to the biology of algae. Photosynth. Res. 77:155-171. (Pubitemid 37293028)
    • (2003) Photosynthesis Research , vol.77 , Issue.2-3 , pp. 155-171
    • Raven, J.A.1
  • 6
    • 0037001967 scopus 로고    scopus 로고
    • Rubisco: Structure, regulatory interactions, and possibilities for a better enzyme
    • DOI 10.1146/annurev.arplant.53.100301.135233
    • Spreitzer RJ, Salvucci ME. 2002. Rubisco: structure, regulatory interactions, and possibilities for a better enzyme. Annu. Rev. Plant Biol. 53:449-475. (Pubitemid 36257503)
    • (2002) Annual Review of Plant Biology , vol.53 , pp. 449-475
    • Spreitzer, R.J.1    Salvucci, M.E.2
  • 10
    • 0030749057 scopus 로고    scopus 로고
    • The role of marine biota in the evolution of terrestrial biota: Gases and genes. Atmospheric composition and evolution of terrestrial biota
    • DOI 10.1023/A:1005855528289
    • Raven JA. 1997. The role of marine biota in the evolution of terrestrial biota: gases and genes. Atmospheric composition and evolution of terrestrial biota. Biogeochemistry 39:139-164. (Pubitemid 27433900)
    • (1997) Biogeochemistry , vol.39 , Issue.2 , pp. 139-164
    • Raven, J.A.1
  • 12
    • 1642547063 scopus 로고    scopus 로고
    • The evolution of C4 photosynthesis
    • Sage RF. 2004. The evolution of C4 photosynthesis. New Phytol. 161:341-370.
    • (2004) New Phytol , vol.161 , pp. 341-370
    • Sage, R.F.1
  • 14
    • 44649180011 scopus 로고    scopus 로고
    • 2- concentrating- mechanism (CCM): Functional components, Ci transporters, diversity, genetic regulation and prospects for engineering into plants
    • DOI 10.1093/jxb/erm112
    • 2-concentrating-mechanism (CCM): functional components, Ci transporters, diversity, genetic regulation and prospects for engineering into plants. J. Exp. Bot. 59:1441-1461. (Pubitemid 351786553)
    • (2008) Journal of Experimental Botany , vol.59 , Issue.7 , pp. 1441-1461
    • Price, G.D.1    Badger, M.R.2    Woodger, F.J.3    Long, B.M.4
  • 15
    • 84856965914 scopus 로고    scopus 로고
    • 2 concentrating mechanism
    • 2 concentrating mechanism. Photosynth. Res. 109:47-57.
    • (2011) Photosynth. Res , vol.109 , pp. 47-57
    • Price, G.D.1
  • 16
    • 0020589050 scopus 로고
    • Characterization of a homogenous preparation of carboxysomes from Thiobacillus neapolitanus
    • Cannon GC, Shively JM. 1983. Characterization of a homogenous preparation of carboxysomes from Thiobacillus neapolitanus. Arch. Microbiol. 134:52-59. (Pubitemid 13027358)
    • (1983) Archives of Microbiology , vol.134 , Issue.1 , pp. 52-59
    • Cannon, G.C.1    Shively, J.M.2
  • 17
    • 0023250899 scopus 로고
    • Activity of ribulose-1,5-bisphosphate carboxylase in intact and disrupted carboxysomes of Thiobacillus neapolitanus
    • Holthuijzen YA, Kuenen JG, Konings WN. 1987. Activity of ribulose- 1,5-bisphosphate carboxylase in intact and disrupted carboxysomes of Thiobacillus neapolitanus. FEMS Microbiol. Lett. 42:121-124. (Pubitemid 17094246)
    • (1987) FEMS Microbiology Letters , vol.42 , Issue.2-3 , pp. 121-124
    • Holthuijzen, Y.A.1    Kuenen, J.G.2    Konings, W.N.3
  • 18
    • 23644439946 scopus 로고    scopus 로고
    • The carbon-concentrating mechanism of the hydrothermal vent chemolithoautotroph Thiomicrospira crunogena
    • DOI 10.1128/JB.187.16.5761-5766.2005
    • Dobrinski KP, Longo DL, Scott KM. 2005. The carbon-concentrating mechanism of the hydrothermal vent chemolithoautotroph Thiomicrospira crunogena. J. Bacteriol. 187:5761-5766. (Pubitemid 41134313)
    • (2005) Journal of Bacteriology , vol.187 , Issue.16 , pp. 5761-5766
    • Dobrinski, K.P.1    Longo, D.L.2    Scott, K.M.3
  • 20
    • 0345548833 scopus 로고
    • Nature of the inorganic carbon species actively taken up by the cyanobacterium Anabaena variabilis
    • Volokita M, Zenvirth D, Kaplan A, Reinhold L. 1984. Nature of the inorganic carbon species actively taken up by the cyanobacterium Anabaena variabilis. Plant Physiol. 76:599-602.
    • (1984) Plant Physiol , vol.76 , pp. 599-602
    • Volokita, M.1    Zenvirth, D.2    Kaplan, A.3    Reinhold, L.4
  • 21
    • 0021906813 scopus 로고
    • Localization of carbonic anhydrase in the cyanobacterium Chlorogloeopsis fritschii
    • DOI 10.1016/0378-1097(85)90162-4
    • Lanaras T, Hawthornthwaite AM, Codd GA. 1985. Localization of carbonic anhydrase in the cyanobacterium Chlorogloeopsis fritschii. FEMS Microbiol. Lett. 26:285-288. (Pubitemid 15148762)
    • (1985) FEMS Microbiology Letters , vol.26 , Issue.3 , pp. 285-288
    • Lanaras, T.1    Hawthornthwaite, A.M.2    Codd, G.A.3
  • 22
    • 0038092371 scopus 로고
    • Carbonic anhydrase from the blue-green alga (cyanobacterium) Anabaena variabilis
    • Yagawa Y, Shiraiwa Y, Miyachi S. 1984. Carbonic anhydrase from the blue-green alga (cyanobacterium) Anabaena variabilis. Plant Cell Physiol. 25:775-783.
    • (1984) Plant Cell Physiol , vol.25 , pp. 775-783
    • Yagawa, Y.1    Shiraiwa, Y.2    Miyachi, S.3
  • 24
    • 44649143352 scopus 로고    scopus 로고
    • Microalgal carbon-dioxide-concentrating mechanisms: Chlamydomonas inorganic carbon transporters
    • DOI 10.1093/jxb/erm128
    • Spalding MH. 2008. Microalgal carbon-dioxide-concentrating mechanisms: Chlamydomonas inorganic carbon transporters. J. Exp. Bot. 59:1463-1473. (Pubitemid 351786555)
    • (2008) Journal of Experimental Botany , vol.59 , Issue.7 , pp. 1463-1473
    • Spalding, M.H.1
  • 25
    • 0003074396 scopus 로고    scopus 로고
    • 2 acquisition, concentration and fixation in cyanobacteria and algae
    • Leegood RC, Sharkey TD, Von Caemmerer S (ed), Kluwer, Dordrecht, The Netherlands
    • 2 acquisition, concentration and fixation in cyanobacteria and algae, p 369-397. In Leegood RC, Sharkey TD, Von Caemmerer S (ed), Photosynthesis: physiology and metabolism, vol 1. Kluwer, Dordrecht, The Netherlands.
    • (2004) Photosynthesis: Physiology and Metabolism , vol.1 , pp. 369-397
    • Badger, M.R.1    Spalding, M.H.2
  • 27
    • 55949125406 scopus 로고    scopus 로고
    • The photorespiratory glycolate metabolism is essential for cyanobacteria and might have been conveyed endosymbiontically to plants
    • Eisenhut M, Ruth W, Haimovich M, Bauwe H, Kaplan A, Hagemann M. 2008. The photorespiratory glycolate metabolism is essential for cyanobacteria and might have been conveyed endosymbiontically to plants. Proc. Natl. Acad. Sci. U. S. A. 105:17199-17204.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 17199-17204
    • Eisenhut, M.1    Ruth, W.2    Haimovich, M.3    Bauwe, H.4    Kaplan, A.5    Hagemann, M.6
  • 28
    • 0019325214 scopus 로고
    • Kinetic-properties of ribulose 1,5-bisphosphate carboxylase- oxygenase from Anabaena variabilis
    • Badger MR. 1980. Kinetic-properties of ribulose 1,5-bisphosphate carboxylase- oxygenase from Anabaena variabilis. Arch. Biochem. Biophys. 201:247-254.
    • (1980) Arch. Biochem. Biophys , vol.201 , pp. 247-254
    • Badger, M.R.1
  • 29
    • 0028888194 scopus 로고
    • Low activation state of ribulose- 1,5-bisphosphate carboxylase oxygenase in carboxysome-defective Synechococcus mutants
    • Schwarz R, Reinhold L, Kaplan A. 1995. Low activation state of ribulose- 1,5-bisphosphate carboxylase oxygenase in carboxysome-defective Synechococcus mutants. Plant Physiol. 108:183-190.
    • (1995) Plant Physiol , vol.108 , pp. 183-190
    • Schwarz, R.1    Reinhold, L.2    Kaplan, A.3
  • 30
    • 0001202064 scopus 로고
    • Association of carbonic anhydrase activity with carboxysomes isolated from the cyanobacterium Synechococcus PCC7942
    • Price GD, Coleman JR, Badger MR. 1992. Association of carbonic anhydrase activity with carboxysomes isolated from the cyanobacterium Synechococcus PCC7942. Plant Physiol. 100:784-793.
    • (1992) Plant Physiol , vol.100 , pp. 784-793
    • Price, G.D.1    Coleman, J.R.2    Badger, M.R.3
  • 31
    • 0024476132 scopus 로고
    • Photosynthesis and nitrogen relationships in leaves of C3 plants
    • Evans JR. 1989. Photosynthesis and nitrogen relationships in leaves of C3 plants. Oecologia 78:9-19.
    • (1989) Oecologia , vol.78 , pp. 9-19
    • Evans, J.R.1
  • 32
    • 0032503986 scopus 로고    scopus 로고
    • Primary production of the biosphere: Integrating terrestrial and oceanic components
    • DOI 10.1126/science.281.5374.237
    • Field CB, Behrenfeld MJ, Randerson JT, Falkowski P. 1998. Primary production of the biosphere-integrating terrestrial and oceanic components. Science 281:237-240. (Pubitemid 28334501)
    • (1998) Science , vol.281 , Issue.5374 , pp. 237-240
    • Field, C.B.1    Behrenfeld, M.J.2    Randerson, J.T.3    Falkowski, P.4
  • 33
    • 0002326959 scopus 로고    scopus 로고
    • Prochlorococcus growth rate and contribution to primary production in the equatorial and subtropical North Pacific Ocean
    • Liu HB, Nolla HA, Campbell L. 1997. Prochlorococcus growth rate and contribution to primary production in the equatorial and subtropical North Pacific Ocean. Aquat. Microb. Ecol. 12:39-47. (Pubitemid 127703861)
    • (1997) Aquatic Microbial Ecology , vol.12 , Issue.1 , pp. 39-47
    • Liu, H.1    Nolla, H.A.2    Campbell, L.3
  • 34
    • 0033558234 scopus 로고    scopus 로고
    • Prochlorococcus growth rates in the central equatorial Pacific: An application of the f(max) approach
    • Liu HB, Landry MR, Vaulot D, Campbell L. 1999. Prochlorococcus growth rates in the central equatorial Pacific: an application of the fmax approach. J. Geophys. Res. Oceans 104:3391-3399. (Pubitemid 29317140)
    • (1999) Journal of Geophysical Research C: Oceans , vol.104 , Issue.2 , pp. 3391-3399
    • Liu, H.1    Landry, M.R.2    Vaulot, D.3    Campbell, L.4
  • 36
    • 84856967222 scopus 로고    scopus 로고
    • 2-concentrating mechanism of Synechococcus WH5701 is composed of native and horizontally- acquired components
    • 2- concentrating mechanism of Synechococcus WH5701 is composed of native and horizontally- acquired components. Photosynth. Res. 109:59-72.
    • (2011) Photosynth. Res , vol.109 , pp. 59-72
    • Rae, B.D.1    Forster, B.2    Badger, M.R.3    Price, G.D.4
  • 37
  • 38
    • 18844436373 scopus 로고    scopus 로고
    • Expression and functional roles of the two distinct NDH-1 complexes and the carbon acquisition complex NdhD3/NdhF3/CupA/SII1735 in Synechocystis sp PCC 6803
    • DOI 10.1105/tpc.104.026526
    • Zhang P, Battchikova N, Jansen T, Appel J, Ogawa T, Aro EM. 2004. Expression and functional roles of the two distinct NDH-1 complexes and the carbon acquisition complex NdhD3/NdhF3/CupA/Sll1735 in Synechocystis sp PCC 6803. Plant Cell 16:3326-3340. (Pubitemid 41096009)
    • (2004) Plant Cell , vol.16 , Issue.12 , pp. 3326-3340
    • Zhang, P.1    Battchikova, N.2    Jansen, T.3    Appel, J.4    Ogawa, T.5    Aro, E.-M.6
  • 39
    • 79960626319 scopus 로고    scopus 로고
    • Membrane topology of the cyanobacterial bicarbonate transporter, SbtA, and identification of potential regulatory loops
    • Price GD, Shelden MC, Howitt SM. 2011. Membrane topology of the cyanobacterial bicarbonate transporter, SbtA, and identification of potential regulatory loops. Mol. Membr. Biol. 28:265-275.
    • (2011) Mol. Membr. Biol , vol.28 , pp. 265-275
    • Price, G.D.1    Shelden, M.C.2    Howitt, S.M.3
  • 41
    • 79953753172 scopus 로고    scopus 로고
    • The cyanobacterial bicarbonate transporter BicA: Its physiological role and the implications of structural similarities with human SLC26 transporters
    • Price GD, Howitt SM. 2011. The cyanobacterial bicarbonate transporter BicA: its physiological role and the implications of structural similarities with human SLC26 transporters. Biochem. Cell Biol. 89:178-188.
    • (2011) Biochem. Cell Biol , vol.89 , pp. 178-188
    • Price, G.D.1    Howitt, S.M.2
  • 42
    • 72049127525 scopus 로고    scopus 로고
    • Membrane topology of the cyanobacterial bicarbonate transporter, BicA, a member of the SulP (SLC26A) family
    • Shelden MC, Howitt SM, Price GD. 2010. Membrane topology of the cyanobacterial bicarbonate transporter, BicA, a member of the SulP (SLC26A) family. Mol. Membr. Biol. 27:12-23.
    • (2010) Mol. Membr. Biol , vol.27 , pp. 12-23
    • Shelden, M.C.1    Howitt, S.M.2    Price, G.D.3
  • 43
    • 0036322542 scopus 로고    scopus 로고
    • Structure, function and regulation of the cyanobacterial high-affinity bicarbonate transporter, BCT1
    • Omata T, Takahashi Y, Yamaguchi O, Nishimura T. 2002. Structure, function and regulation of the cyanobacterial high-affinity bicarbonate transporter, BCT1. Funct. Plant Biol. 29:151-159. (Pubitemid 34853352)
    • (2002) Functional Plant Biology , vol.29 , Issue.2-3 , pp. 151-159
    • Omata, T.1    Takahashi, Y.2    Yamaguchi, O.3    Nishimura, T.4
  • 44
    • 0033539480 scopus 로고    scopus 로고
    • Identification of an ATP-binding cassette transporter involved in bicarbonate uptake in the cyanobacterium Synechococcus sp strain PCC 7942
    • Omata T, Price GD, Badger MR, Okamura M, Gohta S, Ogawa T. 1999. Identification of an ATP-binding cassette transporter involved in bicarbonate uptake in the cyanobacterium Synechococcus sp strain PCC 7942. Proc. Natl. Acad. Sci. U. S. A. 96:13571-13576.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13571-13576
    • Omata, T.1    Price, G.D.2    Badger, M.R.3    Okamura, M.4    Gohta, S.5    Ogawa, T.6
  • 47
    • 0034644777 scopus 로고    scopus 로고
    • Two types of functionally distinct NAD(P)H dehydrogenases in Synechocystis sp strain PCC6803
    • Ohkawa H, Pakrasi HB, Ogawa T. 2000. Two types of functionally distinct NAD(P)H dehydrogenases in Synechocystis sp strain PCC6803. J. Biol. Chem. 275:31630-31634.
    • (2000) J. Biol. Chem , vol.275 , pp. 31630-31634
    • Ohkawa, H.1    Pakrasi, H.B.2    Ogawa, T.3
  • 49
    • 0036172404 scopus 로고    scopus 로고
    • 2 hydration in the cyanobacterium, Synechococcus sp. PCC7942
    • DOI 10.1046/j.1365-2958.2002.02753.x
    • 2 hydration in the cyanobacterium, Synechococcus sp. PCC7942. Mol. Microbiol. 43:425-435. (Pubitemid 34146732)
    • (2002) Molecular Microbiology , vol.43 , Issue.2 , pp. 425-435
    • Maeda, S.-I.1    Badger, M.R.2    Price, G.D.3
  • 50
    • 0036326617 scopus 로고    scopus 로고
    • Functionally distinct NAD(P)H dehydrogenases and their membrane localization in synechocystis sp. PCC6803
    • Ohkawa H, Sonoda M, Hagino N, Shibata M, Pakrasi HB, Ogawa T. 2002. Functionally distinct NAD(P)H dehydrogenases and their membrane localization in Synechocystis sp PCC6803. Funct. Plant Biol. 29:195-200. (Pubitemid 34853356)
    • (2002) Functional Plant Biology , vol.29 , Issue.2-3 , pp. 195-200
    • Ohkawa, H.1    Sonoda, M.2    Hagino, N.3    Shibata, M.4    Pakrasi, H.B.5    Ogawa, T.6
  • 51
    • 38048998618 scopus 로고    scopus 로고
    • Single particle analysis of thylakoid proteins from Thermosynechococcus elongatus and Synechocystis 6803: Localization of the CupA subunit of NDH-1
    • Folea IM, Zhang P, Nowaczyk MM, Ogawa T, Aro E-M, Boekema EJ. 2008. Single particle analysis of thylakoid proteins from Thermosynechococcus elongatus and Synechocystis 6803: localization of the CupA subunit of NDH-1. FEBS Lett. 582:249-254.
    • (2008) FEBS Lett , vol.582 , pp. 249-254
    • Folea, I.M.1    Zhang, P.2    Nowaczyk, M.M.3    Ogawa, T.4    Aro, E.-M.5    Boekema, E.J.6
  • 52
  • 53
    • 0036321693 scopus 로고    scopus 로고
    • Modes of active inorganic carbon uptake in the cyanobacterium, Synechococcus sp. PCC7942
    • Price GD, Maeda S, Omata T, Badger MR. 2002. Modes of active inorganic carbon uptake in the cyanobacterium, Synechococcus sp PCC7942. Funct. Plant Biol. 29:131-149. (Pubitemid 34853351)
    • (2002) Functional Plant Biology , vol.29 , Issue.2-3 , pp. 131-149
    • Price, G.D.1    Maeda, S.-I.2    Omata, T.3    Badger, M.R.4
  • 54
    • 29144469322 scopus 로고    scopus 로고
    • 2-concentrating mechanism in the cyanobacterium Synechococcus elongatus: Analysis by quantitative reverse transcription - Polymerase chain reaction
    • DOI 10.1139/b05-055
    • 2-concentrating mechanism in the cyanobacterium Synechococcus elongatus: analysis by quantitative reverse transcriptionpolymerase chain reaction. Can. J. Bot. 83:711-720. (Pubitemid 41806435)
    • (2005) Canadian Journal of Botany , vol.83 , Issue.7 , pp. 711-720
    • McGinn, P.J.1    Jones, M.J.2    Macdonald, A.B.3    Campbell, D.A.4
  • 55
    • 2342454971 scopus 로고    scopus 로고
    • 2-concentrating mechanism in Synechocystis sp. PCC6803
    • DOI 10.1111/j.1365-3040.2004.01175.x
    • 2- concentrating mechanism in Synechocystis sp PCC6803. Plant Cell Environ. 27:615-626. (Pubitemid 38600732)
    • (2004) Plant, Cell and Environment , vol.27 , Issue.5 , pp. 615-626
    • Mcginn, P.J.1    Price, G.D.2    Badger, M.R.3
  • 56
    • 0038324426 scopus 로고    scopus 로고
    • 2-concentrating mechanism in the cyanobacterium Synechocystis sp strain PCC6803
    • DOI 10.1104/pp.019349
    • 2-concentrating mechanism in the cyanobacterium Synechocystis sp strain PCC6803. Plant Physiol. 132:218-229. (Pubitemid 36590413)
    • (2003) Plant Physiology , vol.132 , Issue.1 , pp. 218-229
    • McGinn, P.J.1    Price, G.D.2    Maleszka, R.3    Badger, M.R.4
  • 58
    • 33644992198 scopus 로고    scopus 로고
    • Sensing of inorganic carbon limitation in Synechococcus PCC7942 is correlated with the size of the internal inorganic carbon pool and involves oxygen
    • DOI 10.1104/pp.105.069146
    • Woodger FJ, Badger MR, Price GD. 2005. Sensing of inorganic carbon limitation in Synechococcus PCC7942 is correlated with the size of the internal inorganic carbon pool and involves oxygen. Plant Physiol. 139:1959-1969. (Pubitemid 43899831)
    • (2005) Plant Physiology , vol.139 , Issue.4 , pp. 1959-1969
    • Woodger, F.J.1    Badger, M.R.2    Price, G.D.3
  • 59
    • 0000955215 scopus 로고
    • Photosynthesis and inorganic carbon usage by the marine cyanobacterium, Synechococcus sp
    • Badger MR, Andrews TJ. 1982. Photosynthesis and inorganic carbon usage by the marine cyanobacterium, Synechococcus sp. Plant Physiol. 70:517-523.
    • (1982) Plant Physiol , vol.70 , pp. 517-523
    • Badger, M.R.1    Andrews, T.J.2
  • 62
    • 0030067045 scopus 로고    scopus 로고
    • 2-concentrating mechanism
    • DOI 10.1016/0303-2647(95)01561-2
    • 2- concentrating mechanism. Biosystems 37:229-238. (Pubitemid 26024850)
    • (1996) BioSystems , vol.37 , Issue.3 , pp. 229-238
    • Fridlyand, L.1    Kaplan, A.2    Reinhold, L.3
  • 63
    • 0000240647 scopus 로고
    • Energization and activation of inorganic carbon uptake by light in cyanobacteria
    • Kaplan A, Zenvirth D, Marcus Y, Omata T, Ogawa T. 1987. Energization and activation of inorganic carbon uptake by light in cyanobacteria. Plant Physiol. 84:210-213.
    • (1987) Plant Physiol , vol.84 , pp. 210-213
    • Kaplan, A.1    Zenvirth, D.2    Marcus, Y.3    Omata, T.4    Ogawa, T.5
  • 68
    • 38249023837 scopus 로고
    • 2-concentrating mechanism in organisms grown under carbon-limitation in the chemostat
    • 2-concentrating mechanism in organisms grown under carbon-limitation in the chemostat. FEMS Microbiol. Lett. 58:179-182.
    • (1989) FEMS Microbiol. Lett , vol.58 , pp. 179-182
    • Karagouni, A.D.1    Kelly, D.P.2
  • 69
    • 32444441814 scopus 로고    scopus 로고
    • Thiobacillus Beijerinck 1904b, 597AL
    • Garrity GM, Brenner DJ, Krieg NR, Staley JT (ed), 2nd ed, part C. The proteobacteria: the alpha-, beta-, delta-, and epsilonproteobacteria. Springer-Verlag, New York, NY
    • Kelly D, Wood A, Stackebrandt E. 2005. Thiobacillus Beijerinck 1904b, 597AL, p 764-769. In Garrity GM, Brenner DJ, Krieg NR, Staley JT (ed), Bergey's manual of systematic bacteriology, 2nd ed, vol 2, part C. The proteobacteria: the alpha-, beta-, delta-, and epsilonproteobacteria. Springer-Verlag, New York, NY.
    • (2005) Bergey's Manual of Systematic Bacteriology , vol.2 , pp. 764-769
    • Kelly, D.1    Wood, A.2    Stackebrandt, E.3
  • 71
    • 0021227370 scopus 로고
    • The acidophilic thiobacilli and other acidophilic bacteria that share their habitat
    • Harrison AP, Jr. 1984. The acidophilic thiobacilli and other acidophilic bacteria that share their habitat. Annu. Rev. Microbiol. 38:265-292.
    • (1984) Annu. Rev. Microbiol , vol.38 , pp. 265-292
    • Harrison Jr., A.P.1
  • 72
    • 84861204499 scopus 로고    scopus 로고
    • Transcriptional response of the sulfur chemolithoautotroph Thiomicrospira crunogena to dissolved inorganic carbon limitation
    • Dobrinski KP, Enkemann SA, Yoder SJ, Haller E, Scott KM. 2012. Transcriptional response of the sulfur chemolithoautotroph Thiomicrospira crunogena to dissolved inorganic carbon limitation. J. Bacteriol. 194:2074-2081.
    • (2012) J. Bacteriol , vol.194 , pp. 2074-2081
    • Dobrinski, K.P.1    Enkemann, S.A.2    Yoder, S.J.3    Haller, E.4    Scott, K.M.5
  • 73
    • 0032442797 scopus 로고    scopus 로고
    • 2 by wild-type cells and ecaA, ecaB, and ccaA mutants of the cyanobacteria Synechococcus PCC7942 and Synechocystis PCC6803
    • 2 by wild-type cells and ecaA, ecaB, and ccaA mutants of the cyanobacteria Synechococcus PCC7942 and Synechocystis PCC6803. Can. J. Bot 76:1153-1160. (Pubitemid 29042849)
    • (1998) Canadian Journal of Botany , vol.76 , Issue.6 , pp. 1153-1160
    • So, A.K.C.1    Van Spall, H.G.C.2    Coleman, J.R.3    Espie, G.S.4
  • 74
    • 3943066746 scopus 로고
    • The ultrastructure of the vegetative cell of blue-green algae
    • Wildon DC, Mercer FV. 1963. The ultrastructure of the vegetative cell of blue-green algae. Aust. J. Biol. Sci. 16:585-596.
    • (1963) Aust. J. Biol. Sci , vol.16 , pp. 585-596
    • Wildon, D.C.1    Mercer, F.V.2
  • 75
    • 34250576175 scopus 로고
    • Electron microscope studies on ultrathin sections of Oscillatoria chalybea Mertens
    • Hall WT, Claus G. 1961. Electron microscope studies on ultrathin sections of Oscillatoria chalybea Mertens. Protoplasma 54:355-368.
    • (1961) Protoplasma , vol.54 , pp. 355-368
    • Hall, W.T.1    Claus, G.2
  • 76
    • 0014484341 scopus 로고
    • Ultrastructure of blue-green algae
    • Gantt E, Conti SF. 1969. Ultrastructure of blue-green algae. J. Bacteriol. 97:1486-1493.
    • (1969) J. Bacteriol , vol.97 , pp. 1486-1493
    • Gantt, E.1    Conti, S.F.2
  • 78
    • 0042993889 scopus 로고
    • Organization of the centroplasm in Nostoc pruniforme
    • Jensen TE, Bowen CC. 1961. Organization of the centroplasm in Nostoc pruniforme. Proc. Iowa Acad. Sci. 68:89-96.
    • (1961) Proc. Iowa Acad. Sci , vol.68 , pp. 89-96
    • Jensen, T.E.1    Bowen, C.C.2
  • 79
    • 0015816557 scopus 로고
    • Functional organelles in prokaryotes: Polyhedral inclusions (carboxysomes) of Thiobacillus neapolitanus
    • Shively JM, Ball F, Brown DH, Saunders RE. 1973. Functional organelles in prokaryotes: polyhedral inclusions (carboxysomes) of Thiobacillus neapolitanus. Science 182:584-586.
    • (1973) Science , vol.182 , pp. 584-586
    • Shively, J.M.1    Ball, F.2    Brown, D.H.3    Saunders, R.E.4
  • 80
    • 0015826540 scopus 로고
    • Electron microscopy of the carboxysomes (polyhedral bodies) of Thiobacillus neapolitanus
    • Shively JM, Ball FL, Kline BW. 1973. Electron microscopy of the carboxysomes (polyhedral bodies) of Thiobacillus neapolitanus. J. Bacteriol. 116:1405-1411.
    • (1973) J. Bacteriol , vol.116 , pp. 1405-1411
    • Shively, J.M.1    Ball, F.L.2    Kline, B.W.3
  • 81
    • 0042993885 scopus 로고
    • Polyhedral bodies and ribulose 1,5- diphosphate carboxylase of blue-green alga Anabaena cylindrica
    • Codd GA, Stewart WDP. 1976. Polyhedral bodies and ribulose 1,5- diphosphate carboxylase of blue-green alga Anabaena cylindrica. Planta 130:323-326.
    • (1976) Planta , vol.130 , pp. 323-326
    • Codd, G.A.1    Stewart, W.D.P.2
  • 82
    • 0018930056 scopus 로고
    • 2 fixing capacity in the obligate chemolithotroph Thiobacillus neapolitanus grown under different limitations in the chemostat
    • DOI 10.1007/BF00427725
    • 2 fixing capacity in the obligate chemolithotroph Thiobacillus neapolitanus grown under different limitations in the chemostat. Arch. Microbiol. 124:185-189. (Pubitemid 10019884)
    • (1980) Archives of Microbiology , vol.124 , Issue.2-3 , pp. 185-189
    • Beudeker, R.F.1    Cannon, G.C.2    Kuenen, J.G.3    Shively, J.M.4
  • 83
    • 84953970349 scopus 로고
    • Polyhedral bodies (carboxysomes) of nitrogen-fixing blue-green algae
    • Stewart WDP, Codd GA. 1975. Polyhedral bodies (carboxysomes) of nitrogen-fixing blue-green algae. Br. Phycol. J. 10:273-278.
    • (1975) Br. Phycol. J , vol.10 , pp. 273-278
    • Stewart, W.D.P.1    Codd, G.A.2
  • 84
    • 0021809204 scopus 로고
    • 2-fixing cyanobacterium Anabaena cylindrica
    • DOI 10.1016/0378-1097(85)90218-6
    • Cossar JD, Rowell P, Darling AJ, Murray S, Codd GA, Stewart WDP. 1985. Localization of ribulose 1,5-bisphosphate carboxylase/oxygenase in the N2-fixing cyanobacterium Anabaena cylindrica. FEMS Microbiol. Lett. 28:65-68. (Pubitemid 15013549)
    • (1985) FEMS Microbiology Letters , vol.28 , Issue.1 , pp. 65-68
    • Cossar, J.D.1    Rowell, P.2    Darling, A.J.3
  • 85
    • 0042993879 scopus 로고
    • Ribulose 1,5-bisphosphate carboxylase and polyhedral bodies of Chlorogloeopsis fritschii
    • Lanaras T, Codd GA. 1981. Ribulose 1,5-bisphosphate carboxylase and polyhedral bodies of Chlorogloeopsis fritschii. Planta 153:279-285.
    • (1981) Planta , vol.153 , pp. 279-285
    • Lanaras, T.1    Codd, G.A.2
  • 86
    • 0019810767 scopus 로고
    • Structural and immunoelectrophoretic comparison of soluble and particulate ribulose bisphosphate carboxylases from the cyanobacterium Chlorogloeopsis fritschii
    • Lanaras T, Codd GA. 1981. Structural and immunoelectrophoretic comparison of soluble and particulate ribulose bisphosphate carboxylases from the cyanobacterium Chlorogloeopsis fritschii. Arch. Microbiol. 130:213-217. (Pubitemid 12169229)
    • (1981) Archives of Microbiology , vol.130 , Issue.3 , pp. 213-217
    • Lanaras, T.1    Codd, G.A.2
  • 87
    • 84897583634 scopus 로고
    • 2 uptake in the cyanobacterium Synechococcus PCC7942 without apparent inhibition of internal carbonic anhydrase activity
    • 2 uptake in the cyanobacterium Synechococcus PCC7942 without apparent inhibition of internal carbonic anhydrase activity. Plant Physiol. 89:37-43.
    • (1989) Plant Physiol , vol.89 , pp. 37-43
    • Price, G.D.1    Badger, M.R.2
  • 88
    • 0026287021 scopus 로고
    • A model for inorganic carbon fluxes and photosynthesis in cyanobacterial carboxysomes
    • Reinhold L, Kosloff R, Kaplan A. 1991. A model for inorganic carbon fluxes and photosynthesis in cyanobacterial carboxysomes. Can. J. Bot. 69:984-988.
    • (1991) Can. J. Bot , vol.69 , pp. 984-988
    • Reinhold, L.1    Kosloff, R.2    Kaplan, A.3
  • 89
    • 0002571441 scopus 로고
    • Inorganic carbon fluxes and photosynthesis in cyanobacteria - A quantitative model
    • Biggins J (ed), Providence, Rhode Island, USA, August 10-15, 1986, M. Nijhoff Publishers, Dordrecht, The Netherlands
    • Reinhold L, Zviman M, Kaplan A. 1987. Inorganic carbon fluxes and photosynthesis in cyanobacteria-a quantitative model, p 289-296. In Biggins J (ed), Proceedings of the VIIth International Congress on Photosynthesis, Providence, Rhode Island, USA, August 10-15, 1986, vol 4. M. Nijhoff Publishers, Dordrecht, The Netherlands.
    • (1987) Proceedings of the VIIth International Congress on Photosynthesis , vol.4 , pp. 289-296
    • Reinhold, L.1    Zviman, M.2    Kaplan, A.3
  • 90
    • 0024894768 scopus 로고
    • A quantitative model for inorganic carbon fluxes and photosynthesis in cyanobacteria
    • Reinhold L, Zviman M, Kaplan A. 1989. A quantitative model for inorganic carbon fluxes and photosynthesis in cyanobacteria. Plant Physiol. Biochem. 27:945-954.
    • (1989) Plant Physiol. Biochem , vol.27 , pp. 945-954
    • Reinhold, L.1    Zviman, M.2    Kaplan, A.3
  • 95
    • 0034038419 scopus 로고    scopus 로고
    • Identification and localization of the carboxysome peptide Csos3 and its corresponding gene in Thiobacillus neapolitanus
    • DOI 10.1007/s002030000141
    • Baker SH, Williams DS, Aldrich HC, Gambrell AC, Shively JM. 2000. Identification and localization of the carboxysome peptide Csos3 and its corresponding gene in Thiobacillus neapolitanus. Arch. Microbiol. 173:278-283. (Pubitemid 30202223)
    • (2000) Archives of Microbiology , vol.173 , Issue.4 , pp. 278-283
    • Baker, S.H.1    Williams, D.S.2    Aldrich, H.C.3    Gambrell, A.C.4    Shively, J.M.5
  • 96
    • 84856947618 scopus 로고    scopus 로고
    • Over-expression of the -carboxysomal CcmM protein in Synechococcus PCC7942 reveals a tight co-regulation of carboxysomal carbonic anhydrase (CcaA) and M58 content
    • Long BM, Rae BD, Badger MR, Price GD. 2011. Over-expression of the -carboxysomal CcmM protein in Synechococcus PCC7942 reveals a tight co-regulation of carboxysomal carbonic anhydrase (CcaA) and M58 content. Photosynth. Res. 109:33-45.
    • (2011) Photosynth. Res , vol.109 , pp. 33-45
    • Long, B.M.1    Rae, B.D.2    Badger, M.R.3    Price, G.D.4
  • 97
    • 77951980276 scopus 로고    scopus 로고
    • Functional cyanobacterial β-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 β-carboxysomes have an absolute requirement for both long and short forms of the CcmM protein. Plant Physiol. 153:285-293.
    • (2010) Plant Physiol , vol.153 , pp. 285-293
    • Long, B.M.1    Tucker, L.2    Badger, M.R.3    Price, G.D.4
  • 98
    • 35748946615 scopus 로고    scopus 로고
    • Analysis of carboxysomes from Synechococcus PCC7942 reveals multiple rubisco complexes with carboxysomal proteins CcmM and CcaA
    • DOI 10.1074/jbc.M703896200
    • 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. J. Biol. Chem. 282:29323-29335. (Pubitemid 350043344)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.40 , pp. 29323-29335
    • Long, B.M.1    Badger, M.R.2    Whitney, S.M.3    Price, G.D.4
  • 99
    • 38649141503 scopus 로고    scopus 로고
    • A multiprotein bicarbonate dehydration complex essential to carboxysome function in cyanobacteria
    • DOI 10.1128/JB.01283-07
    • Cot SSW, So AKC, Espie GS. 2008. A multiprotein bicarbonate dehydration complex essential to carboxysome function in cyanobacteria. J. Bacteriol. 190:936-945. (Pubitemid 351170937)
    • (2008) Journal of Bacteriology , vol.190 , Issue.3 , pp. 936-945
    • Cot, S.S.-W.1    So, A.K.-C.2    Espie, G.S.3
  • 100
    • 0032840522 scopus 로고    scopus 로고
    • Microbial ribulose 1,5-bisphosphate carboxylase/oxygenase: A different perspective
    • DOI 10.1023/A:1006211417981
    • Tabita FR. 1999. Microbial ribulose 1,5-bisphosphate carboxylase/ oxygenase: a different perspective. Photosynth. Res. 60:1-28. (Pubitemid 29384472)
    • (1999) Photosynthesis Research , vol.60 , Issue.1 , pp. 1-28
    • Tabita, F.R.1
  • 101
    • 0018409915 scopus 로고
    • Generic assignments, strain histories and properties of pure cultures of cyanobacteria
    • Rippka R, Deruelles J, Waterbury J, Herdman M, Stanier R. 1979. Generic assignments, strain histories and properties of pure cultures of cyanobacteria. Microbiology 111:1-61. (Pubitemid 9142236)
    • (1979) Journal of General Microbiology , vol.111 , Issue.1 , pp. 1-61
    • Rippka, R.1    Deruelles, J.2    Waterbury, J.B.3
  • 104
    • 79959659081 scopus 로고    scopus 로고
    • Genome fluctuations in cyanobacteria reflect evolutionary, developmental and adaptive traits
    • Larsson J, Nylander JA, Bergman B. 2011. Genome fluctuations in cyanobacteria reflect evolutionary, developmental and adaptive traits. BMC Evol. Biol. 11:187.
    • (2011) BMC Evol. Biol , vol.11 , pp. 187
    • Larsson, J.1    Nylander, J.A.2    Bergman, B.3
  • 105
    • 80155142141 scopus 로고    scopus 로고
    • Large-scale phylogenomic analyses indicate a deep origin of primary plastids within cyanobacteria
    • Criscuolo A, Gribaldo S. 2011. Large-scale phylogenomic analyses indicate a deep origin of primary plastids within cyanobacteria. Mol. Biol. Evol. 28:13019-13032.
    • (2011) Mol. Biol. Evol , vol.28 , pp. 13019-13032
    • Criscuolo, A.1    Gribaldo, S.2
  • 106
    • 73349098709 scopus 로고    scopus 로고
    • Timing of morphological and ecological innovations in the cyanobacteria - A key to understanding the rise in atmospheric oxygen
    • Blank CE, Sanchez-Baracaldo P. 2010. Timing of morphological and ecological innovations in the cyanobacteria-a key to understanding the rise in atmospheric oxygen. Geobiology 8:1-23.
    • (2010) Geobiology , vol.8 , pp. 1-23
    • Blank, C.E.1    Sanchez-Baracaldo, P.2
  • 107
    • 34347387547 scopus 로고    scopus 로고
    • The ancestor of the Paulinella chromatophore obtained a carboxysomal operon by horizontal gene transfer from a Nitrococcus-like γ- proteobacterium
    • DOI 10.1186/1471-2148-7-85
    • Marin B, Nowack ECM, Glockner G, Melkonian M. 2007. The ancestor of the Paulinella chromatophore obtained a carboxysomal operon by horizontal gene transfer from a Nitrococcus-like gamma-proteobacterium. BMC Evol. Biol. 7:85. doi:10.1186/1471-2148-7-85. (Pubitemid 47024467)
    • (2007) BMC Evolutionary Biology , vol.7 , pp. 85
    • Marin, B.1    Nowack, E.C.M.2    Glockner, G.3    Melkonian, M.4
  • 108
    • 84856972928 scopus 로고    scopus 로고
    • Carboxysomes: Cyanobacterial RubisCO comes in small packages
    • Espie GS, Kimber MS. 2011. Carboxysomes: cyanobacterial RubisCO comes in small packages. Photosynth. Res. 109:7-20.
    • (2011) Photosynth. Res , vol.109 , pp. 7-20
    • Espie, G.S.1    Kimber, M.S.2
  • 109
    • 84866732609 scopus 로고    scopus 로고
    • Ultrastructure, molecular phylogenetics, and chlorophyll a content of novel cyanobacterial symbionts in temperate sponges
    • Erwin PM, Lopez-Legentil S, Turon X. 2012. Ultrastructure, molecular phylogenetics, and chlorophyll a content of novel cyanobacterial symbionts in temperate sponges. Microb. Ecol. 64:771-783.
    • (2012) Microb. Ecol , vol.64 , pp. 771-783
    • Erwin, P.M.1    Lopez-Legentil, S.2    Turon, X.3
  • 110
    • 0000650063 scopus 로고
    • Genus thiobacillus
    • Staley JT, Bryant MP (ed), Williams & Wilkins, Baltimore, MD
    • Kelly D, Harrison A. 1989. Genus Thiobacillus, p 1842-1858. In Staley JT, Bryant MP (ed), Bergey's manual of systematic bacteriology, vol 3. Williams & Wilkins, Baltimore, MD.
    • (1989) Bergey's Manual of Systematic Bacteriology , vol.3 , pp. 1842-1858
    • Kelly, D.1    Harrison, A.2
  • 111
    • 0034065246 scopus 로고    scopus 로고
    • Reclassification of some species of Thiobacillus to the newly designated genera Acidithiobacillus gen. nov., Halothiobacillus gen. nov. and Thermithiobacillus gen. nov.
    • Kelly DP, Wood AP. 2000. Reclassification of some species of Thiobacillus to the newly designated genera Acidithiobacillus gen. nov., Halothiobacillus gen. nov and Thermithiobacillus gen. nov. Int. J. Syst. Evol. Microbiol. 50:511-516. (Pubitemid 30167492)
    • (2000) International Journal of Systematic and Evolutionary Microbiology , vol.50 , Issue.2 , pp. 511-516
    • Kelly, D.P.1    Wood, A.P.2
  • 112
    • 84857065808 scopus 로고    scopus 로고
    • Isolation and characterization of the Prochlorococcus carboxysome reveal the presence of the novel shell protein CsoS1D
    • Roberts EW, Cai F, Kerfeld CA, Cannon GC, Heinhorst S. 2012. Isolation and characterization of the Prochlorococcus carboxysome reveal the presence of the novel shell protein CsoS1D. J. Bacteriol. 194:787-795.
    • (2012) J. Bacteriol , vol.194 , pp. 787-795
    • Roberts, E.W.1    Cai, F.2    Kerfeld, C.A.3    Cannon, G.C.4    Heinhorst, S.5
  • 113
    • 84856963458 scopus 로고    scopus 로고
    • Comparative analysis of carboxysome shell proteins
    • Kinney JN, Axen SD, Kerfeld CA. 2011. Comparative analysis of carboxysome shell proteins. Photosynth. Res. 109:21-32.
    • (2011) Photosynth. Res , vol.109 , pp. 21-32
    • Kinney, J.N.1    Axen, S.D.2    Kerfeld, C.A.3
  • 115
  • 116
    • 77952945226 scopus 로고    scopus 로고
    • Bacterial microcompartment organelles: Protein shell structure and evolution
    • Yeates T, Crowley C, Tanaka S. 2010. Bacterial microcompartment organelles: protein shell structure and evolution. Annu. Rev. Biophys. 39:185-205.
    • (2010) Annu. Rev. Biophys , vol.39 , pp. 185-205
    • Yeates, T.1    Crowley, C.2    Tanaka, S.3
  • 117
    • 58149456903 scopus 로고    scopus 로고
    • Insights from multiple structures of the shell proteins from the -carboxysome
    • Tanaka S, Sawaya M, Phillips M, Yeates T. 2009. Insights from multiple structures of the shell proteins from the -carboxysome. Protein Sci. 18:108-120.
    • (2009) Protein Sci , vol.18 , pp. 108-120
    • Tanaka, S.1    Sawaya, M.2    Phillips, M.3    Yeates, T.4
  • 118
    • 34250347772 scopus 로고    scopus 로고
    • Structural analysis of CsoS1A and the protein shell of the Halothiobacillus neapolitanus carboxysome
    • DOI 10.1371/journal.pbio.0050144
    • Tsai Y, Sawaya MR, Cannon GC, Cai F, Williams EB, Heinhorst S, Kerfeld CA, Yeates TO. 2007. Structural analysis of CsoS1A and the protein shell of the Halothiobacillus neapolitanus carboxysome. PLoS Biol. 5:e144. doi:10.1371/journal.pbio.0050144. (Pubitemid 46919953)
    • (2007) PLoS Biology , vol.5 , Issue.6 , pp. 1345-1354
    • Tsai, Y.1    Sawaya, M.R.2    Cannon, G.C.3    Cai, F.4    Williams, E.B.5    Heinhorst, S.6    Kerfeld, C.A.7    Yeates, T.O.8
  • 119
    • 69949153137 scopus 로고    scopus 로고
    • Analysis of lattice-translocation disorder in the layered hexagonal structure of carboxysome shell protein CsoS1C. Acta Crystallogr
    • Tsai Y, Sawaya MR, Yeates TO. 2009. Analysis of lattice-translocation disorder in the layered hexagonal structure of carboxysome shell protein CsoS1C. Acta Crystallogr. D Biol. Crystallogr. 65:980-988.
    • (2009) D Biol. Crystallogr , vol.65 , pp. 980-988
    • Tsai, Y.1    Sawaya, M.R.2    Yeates, T.O.3
  • 120
    • 68949220061 scopus 로고    scopus 로고
    • Identification and structural analysis of a novel carboxysome shell protein with implications for metabolite transport
    • Klein MG, Zwart P, Bagby SC, Cai F, Chisholm SW, Heinhorst S, Cannon GC, Kerfeld CA. 2009. Identification and structural analysis of a novel carboxysome shell protein with implications for metabolite transport. J. Mol. Biol. 392:319-333.
    • (2009) J. Mol. Biol , vol.392 , pp. 319-333
    • Klein, M.G.1    Zwart, P.2    Bagby, S.C.3    Cai, F.4    Chisholm, S.W.5    Heinhorst, S.6    Cannon, G.C.7    Kerfeld, C.A.8
  • 121
    • 55849129963 scopus 로고    scopus 로고
    • Halothiobacillus neapolitanus carboxysomes sequester heterologous and chimeric RubisCO species
    • doi:10.1371/journal.pone.0003570
    • Menon BB, Dou Z, Heinhorst S, Shively JM, Cannon GC. 2008. Halothiobacillus neapolitanus carboxysomes sequester heterologous and chimeric RubisCO species. PLoS One 3:e3570. doi:10.1371/journal.pone .0003570.
    • (2008) PLoS One , vol.3
    • Menon, B.B.1    Dou, Z.2    Heinhorst, S.3    Shively, J.M.4    Cannon, G.C.5
  • 128
    • 74649083831 scopus 로고    scopus 로고
    • Organization, structure, and assembly of alpha-carboxysomes determined by electron cryotomography of intact cells
    • Iancu CV, Morris DM, Dou ZC, Heinhorst S, Cannon GC, Jensen GJ. 2010. Organization, structure, and assembly of alpha-carboxysomes determined by electron cryotomography of intact cells. J. Mol. Biol. 396:105-117.
    • (2010) J. Mol. Biol , vol.396 , pp. 105-117
    • Iancu, C.V.1    Morris, D.M.2    Dou, Z.C.3    Heinhorst, S.4    Cannon, G.C.5    Jensen, G.J.6
  • 129
    • 34548276117 scopus 로고    scopus 로고
    • The Structure of Isolated Synechococcus Strain WH8102 Carboxysomes as Revealed by Electron Cryotomography
    • DOI 10.1016/j.jmb.2007.06.059, PII S0022283607008662
    • Iancu CV, Ding HJ, Morris DM, Dias DP, Gonzales AD, Martino A, Jensen GJ. 2007. The structure of isolated Synechococcus strain WH8102 carboxysomes as revealed by electron cryotomography. J. Mol. Biol. 372:764-773. (Pubitemid 47321793)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 764-773
    • Iancu, C.V.1    Ding, H.J.2    Morris, D.M.3    Dias, D.P.4    Gonzales, A.D.5    Martino, A.6    Jensen, G.J.7
  • 130
    • 0032886650 scopus 로고    scopus 로고
    • The correlation of the gene csoS2 of the carboxysome operon with two polypeptides of the carboxysome in Thiobacillus neapolitanus
    • DOI 10.1007/s002030050765
    • Baker SH, Lorbach SC, Rodriguez-Buey M, Williams DS, Aldrich HC, Shively JM. 1999. The correlation of the gene csoS2 of the carboxysome operon with two polypeptides of the carboxysome in Thiobacillus neapolitanus. Arch. Microbiol. 172:233-239. (Pubitemid 29470800)
    • (1999) Archives of Microbiology , vol.172 , Issue.4 , pp. 233-239
    • Baker, S.H.1    Lorbach, S.C.2    Rodriguez-Buey, M.3    Williams, D.S.4    Aldrich, H.C.5    Shively, J.M.6
  • 132
    • 1642500161 scopus 로고    scopus 로고
    • A Novel Evolutionary Lineage of Carbonic Anhydrase (epsilon Class) Is a Component of the Carboxysome Shell
    • DOI 10.1128/JB.186.3.623-630.2004
    • So AKC, Espie GS, Williams EB, Shively JM, Heinhorst S, Cannon GC. 2004. A novel evolutionary lineage of carbonic anhydrase (epsilon class) is a component of the carboxysome shell. J. Bacteriol. 186:623-630. (Pubitemid 38129638)
    • (2004) Journal of Bacteriology , vol.186 , Issue.3 , pp. 623-630
    • So, A.K.-C.1    Espie, G.S.2    Williams, E.B.3    Shively, J.M.4    Heinhorst, S.5    Cannon, G.C.6
  • 133
    • 33646365079 scopus 로고    scopus 로고
    • The structure of β-carbonic anhydrase from the carboxysomal shell reveals a distinct subclass with one active site for the price of two
    • DOI 10.1074/jbc.M510464200
    • Sawaya MR, Cannon GC, Heinhorst S, Tanaka S, Williams EB, Yeates TO, Kerfeld CA. 2006. The structure of beta-carbonic anhydrase from the carboxysomal shell reveals a distinct subclass with one active site for the price of two. J. Biol. Chem. 281:7546-7555. (Pubitemid 43847525)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.11 , pp. 7546-7555
    • Sawaya, M.R.1    Cannon, G.C.2    Heinhorst, S.3    Tanaka, S.4    Williams, E.B.5    Yeates, T.O.6    Kerfeld, C.A.7
  • 135
    • 84875723302 scopus 로고    scopus 로고
    • Cyanobacterialbased approaches to improving photosynthesis in plants
    • Zarzycki J, Axen SD, Kinney JN, Kerfeld CA. 2013. Cyanobacterialbased approaches to improving photosynthesis in plants. J. Exp. Bot. 64:787-798.
    • (2013) J. Exp. Bot , vol.64 , pp. 787-798
    • Zarzycki, J.1    Axen, S.D.2    Kinney, J.N.3    Kerfeld, C.A.4
  • 136
    • 0000066404 scopus 로고    scopus 로고
    • 2 concentrating mechanism in several cyanobacterial strains: A review of general physiological characteristics, genes, proteins, and recent advances
    • 2 concentrating mechanism in several cyanobacterial strains-a review of general physiological characteristics, genes, proteins, and recent advances. Can. J. Bot. 76:973-1002. (Pubitemid 29042833)
    • (1998) Canadian Journal of Botany , vol.76 , Issue.6 , pp. 973-1002
    • Price, G.D.1    Sultemeyer, D.2    Klughammer, B.3    Ludwig, M.4    Badger, M.R.5
  • 137
    • 29144484138 scopus 로고    scopus 로고
    • Proteomic assessment of an established technique for carboxysome enrichment from Synechococcus PCC7942
    • DOI 10.1139/b05-058
    • Long BM, Price GD, Badger MR. 2005. Proteomic assessment of an established technique for carboxysome enrichment from Synechococcus PCC7942. Can. J. Bot. 83:746-757. (Pubitemid 41806438)
    • (2005) Canadian Journal of Botany , vol.83 , Issue.7 , pp. 746-757
    • Long, B.M.1    Price, G.D.2    Badger, M.R.3
  • 140
    • 0027223239 scopus 로고
    • Analysis of a genomic DNA region from the cyanobacterium Synechococcus sp strain PCC7942 involved in carboxysome assembly and function
    • Price GD, Howitt SM, Harrison K, Badger MR. 1993. Analysis of a genomic DNA region from the cyanobacterium Synechococcus sp. strain PCC 7942 involved in carboxysome assembly and function. J. Bacteriol. 175:2871-2879. (Pubitemid 23148719)
    • (1993) Journal of Bacteriology , vol.175 , Issue.10 , pp. 2871-2879
    • Price, G.D.1    Howitt, S.M.2    Harrison, K.3    Badger, M.R.4
  • 141
    • 0034490454 scopus 로고    scopus 로고
    • Isolation of ccmKLMN genes from the marine cyanobacterium, Synechococcus sp. PCC7002 (Cyanophyceae), and evidence that CcmM is essential for carboxysome assembly
    • Ludwig M, Sültemeyer D, Price G. 2000. Isolation of ccmKLMN genes from the marine cyanobacterium, Synechococcus sp. PCC7002 (Cyanophyceae), and evidence that CcmM is essential for carboxysome assembly. J. Phycol. 36:1109-1119.
    • (2000) J. Phycol , vol.36 , pp. 1109-1119
    • Ludwig, M.1    Sültemeyer, D.2    Price, G.3
  • 142
    • 0028065840 scopus 로고
    • Isolation and characterization of the ccmM gene required by the cyanobacterium Synechocystis PCC6803 for inorganic carbon utilization
    • Ogawa T, Amichay D, Gurevitz M. 1994. Isolation and characterization of the ccmM gene required by the cyanobacterium Synechocystis PCC6803 for inorganic carbon utilization. Photosynth. Res. 39:183-190. (Pubitemid 2059110)
    • (1994) Photosynthesis Research , vol.39 , Issue.2 , pp. 183-190
    • Ogawa, T.1    Amichay, D.2    Gurevitz, M.3
  • 143
    • 84861208627 scopus 로고    scopus 로고
    • Elucidating essential role of conserved carboxysomal protein CcmN reveals common feature of bacterial microcompartment assembly
    • Kinney JN, Salmeen A, Cai F, Kerfeld CA. 2012. Elucidating essential role of conserved carboxysomal protein CcmN reveals common feature of bacterial microcompartment assembly. J. Biol. Chem. 287:17729-17736.
    • (2012) J. Biol. Chem , vol.287 , pp. 17729-17736
    • Kinney, J.N.1    Salmeen, A.2    Cai, F.3    Kerfeld, C.A.4
  • 144
    • 30744456312 scopus 로고    scopus 로고
    • Intact carboxysomes in a cyanobacterial cell visualized by Hilbert differential contrast transmission electron microscopy
    • DOI 10.1128/JB.188.2.805-808.2006
    • Kaneko Y, Danev R, Nagayama K, Nakamoto H. 2006. Intact carboxysomes in a cyanobacterial cell visualized by Hilbert differential contrast transmission electron microscopy. J. Bacteriol. 188:805-808. (Pubitemid 43100568)
    • (2006) Journal of Bacteriology , vol.188 , Issue.2 , pp. 805-808
    • Kaneko, Y.1    Danev, R.2    Nagayama, K.3    Nakamoto, H.4
  • 145
    • 0031992162 scopus 로고    scopus 로고
    • Chimeric Arabidopsis thaliana Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Containing a Pea Small Subunit Protein Is Compromised in Carbamylation
    • Getzoff TP, Zhu GH, Bohnert HJ, Jensen RG. 1998. Chimeric Arabidopsis thaliana ribulose-1,5-bisphosphate carboxylase/oxygenase containing a pea small subunit protein is compromised in carbamylation. Plant Physiol. 116:695-702. (Pubitemid 128482297)
    • (1998) Plant Physiology , vol.116 , Issue.2 , pp. 695-702
    • Getzoff, T.P.1    Zhu, G.2    Bohnert, H.J.3    Jensen, R.G.4
  • 146
    • 0027433039 scopus 로고
    • The X-ray structure of Synechococcus ribulose-bisphosphate carboxylase/oxygenase-activated quaternary complex at 2.2-A resolution
    • Newman J, Gutteridge S. 1993. The X-ray structure of Synechococcus ribulose-bisphosphate carboxylase oxygenase-activated quaternary complex at 2.2-angstrom resolution. J. Biol. Chem. 268:25876-25886. (Pubitemid 23358206)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.34 , pp. 25876-25886
    • Newman, J.1    Gutteridge, S.2
  • 147
    • 23244439942 scopus 로고    scopus 로고
    • Microbiology: Protein structures forming the shell of primitive bacterial organelles
    • DOI 10.1126/science.1113397
    • Kerfeld C, Sawaya M, Tanaka S, Nguyen C, Phillips M, Beeby M, Yeates T. 2005. Protein structures forming the shell of primitive bacterial organelles. Science 309:936-938. (Pubitemid 41099930)
    • (2005) Science , vol.309 , Issue.5736 , pp. 936-938
    • Kerfeld, C.A.1    Sawaya, M.R.2    Tanaka, S.3    Nguyen, C.V.4    Phillips, M.5    Beeby, M.6    Yeates, T.O.7
  • 151
    • 0027368491 scopus 로고
    • Rubisco but not Rubisco activase is clustered in the carboxysomes of the cyanobacterium Synechococcus sp. PCC 7942: Mud-induced carboxysomeless mutants
    • Friedberg D, Jager KM, Kessel M, Silman NJ, Bergman B. 1993. Rubisco but not Rubisco activase is clustered in the carboxysomes of the cyanobacterium Synechococcus sp. PCC 7942: mud-induced carboxysomeless mutants. Mol. Microbiol. 9:1193-1201. (Pubitemid 23286250)
    • (1993) Molecular Microbiology , vol.9 , Issue.6 , pp. 1193-1201
    • Friedberg, D.1    Jager, K.M.2    Kessel, M.3    Silman, N.J.4    Bergman, B.5
  • 152
    • 0001301352 scopus 로고
    • Is there a role for the 42 kilodalton polypeptide in inorganic carbon uptake by cyanobacteria?
    • Schwarz R, Friedberg D, Kaplan A. 1988. Is there a role for the 42 kilodalton polypeptide in inorganic carbon uptake by cyanobacteria? Plant Physiol. 88:284-288.
    • (1988) Plant Physiol , vol.88 , pp. 284-288
    • Schwarz, R.1    Friedberg, D.2    Kaplan, A.3
  • 155
    • 0032408245 scopus 로고    scopus 로고
    • Sequence homologs of the carboxysomal polypeptide CsoS1 of the thiobacilli are present in cyanobacteria and enteric bacteria that form carboxysomes - Polyhedral bodies
    • Shively JM, Bradburne CE, Aldrich HC, Bobik TA, Mehlman JL, Jin S, Baker SH. 1998. Sequence homologs of the carboxysomal polypeptide csoS1 of the Thiobacilli are present in cyanobacteria and enteric bacteria that form carboxysomes-polyhedral bodies. Can. J. Bot. 76:906-916. (Pubitemid 29042826)
    • (1998) Canadian Journal of Botany , vol.76 , Issue.6 , pp. 906-916
    • Shively, J.M.1    Bradburne, C.E.2    Aldrich, H.C.3    Bobik, T.A.4    Mehlman, J.L.5    Jin, S.6    Baker, S.H.7
  • 158
    • 1642459127 scopus 로고    scopus 로고
    • Four Novel Genes Required for Optimal Photoautotrophic Growth of the Cyanobacterium Synechocystis sp. Strain PCC 6803 Identified by In Vitro Transposon Mutagenesis
    • DOI 10.1128/JB.186.3.875-879.2004
    • Zhang SL, Laborde SM, Frankel LK, Bricker TA. 2004. Four novel genes required for optimal photoautotrophic growth of the cyanobacterium Synechocystis sp strain PCC 6803 identified by in vitro transposon mutagenesis. J. Bacteriol. 186:875-879. (Pubitemid 38129668)
    • (2004) Journal of Bacteriology , vol.186 , Issue.3 , pp. 875-879
    • Zhang, S.1    Laborde, S.M.2    Frankel, L.K.3    Bricker, T.M.4
  • 159
    • 84865191456 scopus 로고    scopus 로고
    • Structural determinants of the outer shell of β-carboxysomes in Synechococcus elongatus PCC 7942: Roles for CcmK2, K3-K4, CcmO, and CcmL
    • doi:10.1371/journal.pone.0043871
    • Rae BD, Long BM, Badger MR, Price GD. 2012. Structural determinants of the outer shell of β-carboxysomes in Synechococcus elongatus PCC 7942: roles for CcmK2, K3-K4, CcmO, and CcmL. PLoS One 7:e43871. doi:10.1371/journal. pone.0043871.
    • (2012) PLoS One , vol.7
    • Rae, B.D.1    Long, B.M.2    Badger, M.R.3    Price, G.D.4
  • 160
    • 84864863698 scopus 로고    scopus 로고
    • A dodecameric CcmK2 structure suggests β-carboxysomal shell facets have a double-layered organization
    • Samborska B, Kimber MS. 2012. A dodecameric CcmK2 structure suggests β-carboxysomal shell facets have a double-layered organization. Structure 20:1353-1362.
    • (2012) Structure , vol.20 , pp. 1353-1362
    • Samborska, B.1    Kimber, M.S.2
  • 161
    • 84865189935 scopus 로고    scopus 로고
    • Bioinformatic identification and structural characterization of a new carboxysome shell protein
    • Burnap R, VermaasW(ed), Springer, Dordrecht, Netherlands
    • Cai F, Kerfeld CA, Sandh G. 2012. Bioinformatic identification and structural characterization of a new carboxysome shell protein, p 345-356. In Burnap R, VermaasW(ed), Functional genomics and evolution of photosynthetic systems, vol 33. Springer, Dordrecht, Netherlands.
    • (2012) Functional Genomics and Evolution of Photosynthetic Systems , vol.33 , pp. 345-356
    • Cai, F.1    Kerfeld, C.A.2    Sandh, G.3
  • 162
    • 0030793384 scopus 로고    scopus 로고
    • Carboxysomal diffusion resistance to ribulose 1,5-bisphosphate and 3-phosphoglycerate in the cyanobacterium Synechococcus PCC7942
    • Satoh R, Himeno M, Wadano A. 1997. Carboxysomal diffusion resistance to ribulose 1,5-bisphosphate and 3-phosphoglycerate in the cyanobacterium Synechococcus PCC7942. Plant Cell Physiol. 38:769-775. (Pubitemid 27347759)
    • (1997) Plant and Cell Physiology , vol.38 , Issue.7 , pp. 769-775
    • Satoh, R.1    Himeno, M.2    Wadano, A.3
  • 165
    • 78549246253 scopus 로고    scopus 로고
    • Structural insight into the mechanisms of transport across the Salmonella enterica Pdu microcompartment shell
    • Crowley CS, Cascio D, Sawaya MR, Kopstein JS, Bobik TA, Yeates TO. 2010. Structural insight into the mechanisms of transport across the Salmonella enterica Pdu microcompartment shell. J. Biol. Chem. 285:37838-37846.
    • (2010) J. Biol. Chem , vol.285 , pp. 37838-37846
    • Crowley, C.S.1    Cascio, D.2    Sawaya, M.R.3    Kopstein, J.S.4    Bobik, T.A.5    Yeates, T.O.6
  • 166
    • 67049117718 scopus 로고    scopus 로고
    • Crystal structure of the EutL shell protein of the ethanolamine ammonia lyase microcompartment
    • Sagermann M, Ohtaki A, Nikolakakis K. 2009. Crystal structure of the EutL shell protein of the ethanolamine ammonia lyase microcompartment. Proc. Natl. Acad. Sci. U. S. A. 106:8883-8887.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 8883-8887
    • Sagermann, M.1    Ohtaki, A.2    Nikolakakis, K.3
  • 167
    • 29144463619 scopus 로고    scopus 로고
    • Cyanobacterial carbonic anhydrases
    • DOI 10.1139/b05-057
    • So AKC, Espie GS. 2005. Cyanobacterial carbonic anhydrases. Can. J. Bot. 83:721-734. (Pubitemid 41806436)
    • (2005) Canadian Journal of Botany , vol.83 , Issue.7 , pp. 721-734
    • So, A.K.-C.1    Espie, G.S.2
  • 168
    • 33751562111 scopus 로고    scopus 로고
    • Characterization of the carboxysomal carbonic anhydrase CsoSCA from Halothiobacillus neapolitanus
    • DOI 10.1128/JB.00990-06
    • Heinhorst S, Williams E, Cai F, Murin C, Shively J, Cannon G. 2006. Characterization of the carboxysomal carbonic anhydrase CsoSCA from Halothiobacillus neapolitanus. J. Bacteriol. 188:8087-8094. (Pubitemid 44845678)
    • (2006) Journal of Bacteriology , vol.188 , Issue.23 , pp. 8087-8094
    • Heinhorst, S.1    Williams, E.B.2    Cai, F.3    Murin, C.D.4    Shively, J.M.5    Cannon, G.C.6
  • 170
    • 0001202065 scopus 로고
    • Isolation of a putative carboxysomal carbonic anhydrase gene from the cyanobacterium Synechococcus PCC7942
    • Yu JW, Price GD, Song L, Badger MR. 1992. Isolation of a putative carboxysomal carbonic anhydrase gene from the cyanobacterium Synechococcus PCC7942. Plant Physiol. 100:794.
    • (1992) Plant Physiol , vol.100 , pp. 794
    • Yu, J.W.1    Price, G.D.2    Song, L.3    Badger, M.R.4
  • 171
    • 0026539278 scopus 로고
    • A gene homologous to chloroplast carbonic anhydrase (icfA) is essential to photosynthetic carbon dioxide fixation by Synechococcus PCC7942
    • Fukuzawa H, Suzuki E, Komukai Y, Miyachi S. 1992. A gene homologous to chloroplast carbonic anhydrase (icfA) is essential to photosynthetic carbon dioxide fixation by Synechococcus PCC7942. Proc. Natl. Acad. Sci. U. S. A. 89:4437-4441.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 4437-4441
    • Fukuzawa, H.1    Suzuki, E.2    Komukai, Y.3    Miyachi, S.4
  • 172
    • 0032080510 scopus 로고    scopus 로고
    • Cloning, characterization and expression of carbonic anhydrase from the cyanobacterium Synechocystis PCC6803
    • DOI 10.1023/A:1005959200390
    • So AKC, Espie GS. 1998. Cloning, characterization and expression of carbonic anhydrase from the cyanobacterium Synechocystis PCC6803. Plant Mol. Biol. 37:205-215. (Pubitemid 28209584)
    • (1998) Plant Molecular Biology , vol.37 , Issue.2 , pp. 205-215
    • So, A.K.C.1    Espie, G.S.2
  • 173
    • 0036326616 scopus 로고    scopus 로고
    • Characterization of the C-terminal extension of carboxysomal carbonic anhydrase from Synechocystis sp. PCC6803
    • So AKC, Cot SSW, Espie GS. 2002. Characterization of the C-terminal extension of carboxysomal carbonic anhydrase from Synechocystis sp PCC6803. Funct. Plant Biol. 29:183-194. (Pubitemid 34853355)
    • (2002) Functional Plant Biology , vol.29 , Issue.2-3 , pp. 183-194
    • So, A.K.-C.1    Cot, S.S.-W.2    Espie, G.S.3
  • 174
    • 0036941660 scopus 로고    scopus 로고
    • Characterization of a mutant lacking carboxysomal carbonic anhydrase from the cyanobacterium Synechocystis PCC6803
    • DOI 10.1007/s004250100638
    • So AKC, John-McKay M, Espie GS. 2002. Characterization of a mutant lacking carboxysomal carbonic anhydrase from the cyanobacterium Synechocystis PCC6803. Planta 214:456-467. (Pubitemid 36072670)
    • (2002) Planta , vol.214 , Issue.3 , pp. 456-467
    • So, A.K.C.1    John-McKay, M.2    Espie, G.S.3
  • 175
    • 0142039047 scopus 로고    scopus 로고
    • 2 concentrating mechanisms
    • 2 concentrating mechanisms. Photosynth Res. 77:83-94.
    • (2003) Photosynth Res , vol.77 , pp. 83-94
    • Badger, M.R.1
  • 176
    • 0024713252 scopus 로고
    • A cyanobacterial mutant requiring the expression of ribulose bisphosphate carboxylase from a photosynthetic anaerobe
    • Pierce J, Carlson TJ, Williams JG. 1989. A cyanobacterial mutant requiring the expression of ribulose bisphosphate carboxylase from a photosynthetic anaerobe. Proc. Natl. Acad. Sci. U. S. A. 86:5753-5757.
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 5753-5757
    • Pierce, J.1    Carlson, T.J.2    Williams, J.G.3
  • 177
    • 0029146875 scopus 로고
    • Use of electroporation to generate a Thiobacillus neapolitanus carboxysome mutant
    • English RS, Jin S, Shively JM. 1995. Use of electroporation to generate a Thiobacillus neapolitanus carboxysome mutant. Appl. Environ. Microbiol. 61:3256-3260.
    • (1995) Appl. Environ. Microbiol , vol.61 , pp. 3256-3260
    • English, R.S.1    Jin, S.2    Shively, J.M.3
  • 178
    • 0029167899 scopus 로고
    • Biogenesis and ultrastructure of carboxysomes from wild type and mutants of Synechococcus sp strain PCC 7942
    • Orus MI, Rodriguez ML, Martinez F, Marco E. 1995. Biogenesis and ultrastructure of carboxysomes from wild type and mutants of Synechococcus sp strain PCC 7942. Plant Physiol. 107:1159-1166.
    • (1995) Plant Physiol , vol.107 , pp. 1159-1166
    • Orus, M.I.1    Rodriguez, M.L.2    Martinez, F.3    Marco, E.4
  • 180
    • 84866280237 scopus 로고    scopus 로고
    • Interactions between the termini of lumen enzymes and shell proteins mediate enzyme encapsulation into bacterial microcompartments
    • Fan CG, Cheng SQ, Sinha S, Bobik TA. 2012. Interactions between the termini of lumen enzymes and shell proteins mediate enzyme encapsulation into bacterial microcompartments. Proc. Natl. Acad. Sci. U. S. A. 109:14995-15000.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 14995-15000
    • Fan, C.G.1    Cheng, S.Q.2    Sinha, S.3    Bobik, T.A.4
  • 181
    • 77749264485 scopus 로고    scopus 로고
    • Spatially ordered dynamics of the bacterial carbon fixation machinery
    • Savage D, Afonso B, Chen A, Silver P. 2010. Spatially ordered dynamics of the bacterial carbon fixation machinery. Science 327:1258.
    • (2010) Science , vol.327 , pp. 1258
    • Savage, D.1    Afonso, B.2    Chen, A.3    Silver, P.4
  • 182
    • 0017120255 scopus 로고
    • The fine structure of a microplatemicrotubule array, microfilaments and polyhedral body associated microtubules in several species of Anabaena
    • Jensen TE, Ayala RP. 1976. The fine structure of a microplatemicrotubule array, microfilaments and polyhedral body associated microtubules in several species of Anabaena. Arch. Microbiol. 111:1-6.
    • (1976) Arch. Microbiol , vol.111 , pp. 1-6
    • Jensen, T.E.1    Ayala, R.P.2
  • 183
    • 82555165967 scopus 로고    scopus 로고
    • ParA ATPases can move and position DNA and subcellular structures
    • Szardenings F, Guymer D, Gerdes K. 2011. ParA ATPases can move and position DNA and subcellular structures. Curr. Opin. Microbiol. 14:712-718.
    • (2011) Curr. Opin. Microbiol , vol.14 , pp. 712-718
    • Szardenings, F.1    Guymer, D.2    Gerdes, K.3
  • 184
    • 77956069180 scopus 로고    scopus 로고
    • Protein subcellular localization in bacteria
    • doi:10.1101/cshperspect.a000307
    • Rudner DZ, Losick R. 2010. Protein subcellular localization in bacteria. Cold Spring Harb. Perspect. Biol. 2:a000307. doi:10.1101/cshperspect .a000307.
    • (2010) Cold Spring Harb. Perspect. Biol , vol.2
    • Rudner, D.Z.1    Losick, R.2
  • 185
    • 0000301525 scopus 로고
    • Characteristics of two marine nitrite oxidizing bacteria, Nitrospina gracilis nov. gen. nov. sp. and Nitrococcus mobilis nov. gen. nov. sp
    • Watson SW, Waterbury JB. 1971. Characteristics of two marine nitrite oxidizing bacteria, Nitrospina gracilis nov. gen. nov. sp. and Nitrococcus mobilis nov. gen. nov. sp. Arch. Microbiol. 77:203-230.
    • (1971) Arch. Microbiol , vol.77 , pp. 203-230
    • Watson, S.W.1    Waterbury, J.B.2
  • 186
    • 77950906711 scopus 로고    scopus 로고
    • Synthesis of empty bacterial microcompartments, directed organelle protein incorporation, and evidence of filamentassociated organelle movement
    • Parsons JB, Frank S, Bhella D, Liang MZ, Prentice MB, Mulvihill DP, Warren MJ. 2010. Synthesis of empty bacterial microcompartments, directed organelle protein incorporation, and evidence of filamentassociated organelle movement. Mol. Cell 38:305-315.
    • (2010) Mol. Cell , vol.38 , pp. 305-315
    • Parsons, J.B.1    Frank, S.2    Bhella, D.3    Liang, M.Z.4    Prentice, M.B.5    Mulvihill, D.P.6    Warren, M.J.7
  • 187
    • 79952367508 scopus 로고    scopus 로고
    • Genetic analysis of the protein shell of the microcompartments involved in coenzyme B12- dependent 1,2-propanediol degradation by Salmonella
    • Cheng S, Sinha S, Fan C, Liu Y, Bobik TA. 2011. Genetic analysis of the protein shell of the microcompartments involved in coenzyme B12- dependent 1,2-propanediol degradation by Salmonella. J. Bacteriol. 193:1385-1392.
    • (2011) J. Bacteriol , vol.193 , pp. 1385-1392
    • Cheng, S.1    Sinha, S.2    Fan, C.3    Liu, Y.4    Bobik, T.A.5
  • 188
    • 0347682442 scopus 로고    scopus 로고
    • 2-Concentrating Mechanism in Synechococcus sp. PCC7942 through a Redox-Independent Pathway
    • DOI 10.1104/pp.103.029728
    • 2-concentrating mechanism in Synechococcus sp. PCC7942 through a redox-independent pathway. Plant Physiol. 133:2069-2080. (Pubitemid 38047333)
    • (2003) Plant Physiology , vol.133 , Issue.4 , pp. 2069-2080
    • Woodger, F.J.1    Badger, M.R.2    Price, G.D.3
  • 189
    • 34247640781 scopus 로고    scopus 로고
    • 2-concentrating mechanism in a euryhaline, coastal marine cyanobacteriurn, Synechococcus sp strain PCC 7002: Role of NdhR/CcmR
    • DOI 10.1128/JB.01745-06
    • 2-concentrating mechanism in a euryhaline, coastal marine cyanobacterium, Synechococcus sp strain PCC 7002: role of NdhR/CcmR. J. Bacteriol. 189:3335-3347. (Pubitemid 46668798)
    • (2007) Journal of Bacteriology , vol.189 , Issue.9 , pp. 3335-3347
    • Woodger, F.J.1    Bryant, D.A.2    Price, G.D.3
  • 191
    • 1242339627 scopus 로고    scopus 로고
    • Alterations in Global Patterns of Gene Expression in Synechocystis sp. PCC 6803 in Response to Inorganic Carbon Limitation and the Inactivation of ndhR, a LysR Family Regulator
    • DOI 10.1074/jbc.M311336200
    • Wang HL, Postier BL, Burnap RL. 2004. Alterations in global patterns of gene expression in Synechocystis sp PCC 6803 in response to inorganic carbon limitation and the inactivation of ndhR, a LysR family regulator. J. Biol. Chem. 279:5739-5751. (Pubitemid 38220604)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.7 , pp. 5739-5751
    • Wang, H.-L.1    Postier, B.L.2    Burnap, R.L.3
  • 192
    • 0027234991 scopus 로고
    • Effect of dissolved inorganic carbon on the expression of carboxysomes, localization of Rubisco and the mode of inorganic carbon transport in cells of the cyanobacterium Synechococcus UTEX 625
    • McKay RML, Gibbs SP, Espie GS. 1993. Effect of dissolved inorganic carbon on the expression of carboxysomes, localization of Rubisco and the mode of inorganic carbon transport in cells of the cyanobacterium Synechococcus UTEX 625. Arch. Microbiol. 159:21-29.
    • (1993) Arch. Microbiol , vol.159 , pp. 21-29
    • McKay, R.M.L.1    Gibbs, S.P.2    Espie, G.S.3
  • 193
    • 0030724104 scopus 로고    scopus 로고
    • 2 assimilation genes in autotrophic bacteria
    • DOI 10.1016/S0168-6445(97)00054-5, PII S0168644597000545
    • 2 assimilation genes in autotrophic bacteria. FEMS Microbiol. Rev. 21:135-155. (Pubitemid 27455842)
    • (1997) FEMS Microbiology Reviews , vol.21 , Issue.2 , pp. 135-155
    • Kusian, B.1    Bowien, B.2
  • 194
    • 2642524290 scopus 로고    scopus 로고
    • 2 assimilation, nitrogen fixation, hydrogen metabolism and energy generation
    • DOI 10.1016/j.femsre.2004.01.002, PII S0168644504000130
    • 2 assimilation, nitrogen fixation, hydrogen metabolism and energy generation. FEMS Microbiol. Rev. 28:353-376. (Pubitemid 38721409)
    • (2004) FEMS Microbiology Reviews , vol.28 , Issue.3 , pp. 353-376
    • Dubbs, J.M.1    Tabita, F.R.2
  • 195
    • 36048943681 scopus 로고    scopus 로고
    • Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin
    • DOI 10.1002/pmic.200700410
    • Mata-Cabana A, Florencio FJ, Lindahl M. 2007. Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin. Proteomics 7:3953-3963. (Pubitemid 350100011)
    • (2007) Proteomics , vol.7 , Issue.21 , pp. 3953-3963
    • Mata-Cabana, A.1    Florencio, F.J.2    Lindahl, A.M.3
  • 197
    • 79952802915 scopus 로고    scopus 로고
    • The cyanobacterial hepatotoxin microcystin binds to proteins and increases the fitness of Microcystis under oxidative stress conditions
    • doi:10.1371/journal.pone.0017615
    • Zilliges Y, Kehr J, Meissner S, Ishida K, Mikkat S, Hagemann M, Kaplan A, Börner T, Dittmann E. 2011. The cyanobacterial hepatotoxin microcystin binds to proteins and increases the fitness of Microcystis under oxidative stress conditions. PLoS One 6:e17615. doi:10.1371 /journal.pone.0017615.
    • (2011) PLoS One , vol.6
    • Zilliges, Y.1    Kehr, J.2    Meissner, S.3    Ishida, K.4    Mikkat, S.5    Hagemann, M.6    Kaplan, A.7    Börner, T.8    Dittmann, E.9
  • 198
    • 31344443358 scopus 로고    scopus 로고
    • An advanced technique for immuno-labelling of microcystins in cryosectioned cells of Microcystis aeruginosa PCC 7806 (cyanobacteria): Implementations of an experiment with varying light scenarios and culture densities
    • DOI 10.1016/j.toxicon.2005.10.019, PII S0041010105003764
    • Gerbersdorf SU. 2006. An advanced technique for immuno-labelling of microcystins in cryosectioned cells of Microcystis aeruginosa PCC 7806 (cyanobacteria): implementations of an experiment with varying light scenarios and culture densities. Toxicon 47:218-228. (Pubitemid 43143230)
    • (2006) Toxicon , vol.47 , Issue.2 , pp. 218-228
    • Gerbersdorf, S.U.1
  • 199
    • 35948934722 scopus 로고    scopus 로고
    • Impact of inorganic carbon availability on microcystin production by Microcystis aeruginosa PCC 7806
    • DOI 10.1128/AEM.01253-07
    • Jähnichen S, Ihle T, Petzoldt T, Benndorf J. 2007. Impact of inorganic carbon availability on microcystin production by Microcystis aeruginosa PCC 7806. Appl. Environ. Microbiol. 73:6994-7002. (Pubitemid 350076821)
    • (2007) Applied and Environmental Microbiology , vol.73 , Issue.21 , pp. 6994-7002
    • Jahrlichen, S.1    Ihle, T.2    Petzoldt, T.3    Benndorf, J.4
  • 200
    • 59649115168 scopus 로고    scopus 로고
    • Bioactive compounds produced by cyanobacteria
    • Herrero A, Flores E (ed), Caister Academic Press, Norfolk, United Kingdom
    • Sivonen K, Börner T. 2008. Bioactive compounds produced by cyanobacteria, p 159-197. In Herrero A, Flores E (ed), The cyanobacteria: molecular biology, genomics and evolution, vol 1. Caister Academic Press, Norfolk, United Kingdom.
    • (2008) The Cyanobacteria: Molecular Biology, Genomics and Evolution , vol.1 , pp. 159-197
    • Sivonen, K.1    Börner, T.2
  • 201
    • 0035158449 scopus 로고    scopus 로고
    • Cellular microcystin content in N-limited Microcystis aeruginosa can be predicted from growth rate
    • DOI 10.1128/AEM.67.1.278-283.2001
    • Long BM, Jones GJ, Orr PT. 2001. Cellular microcystin content in N-limited Microcystis aeruginosa can be predicted from growth rate. Appl. Environ. Microbiol. 67:278-283. (Pubitemid 32044429)
    • (2001) Applied and Environmental Microbiology , vol.67 , Issue.1 , pp. 278-283
    • Long, B.M.1    Jones, G.J.2    Orr, P.T.3
  • 202
    • 70449523106 scopus 로고    scopus 로고
    • Relationship between photosynthetic processes and microcystin in Microcystis aeruginosa grown under different photon irradiances
    • Deblois CP, Juneau P. 2010. Relationship between photosynthetic processes and microcystin in Microcystis aeruginosa grown under different photon irradiances. Harmful Algae 9:18-24.
    • (2010) Harmful Algae , vol.9 , pp. 18-24
    • Deblois, C.P.1    Juneau, P.2
  • 203
    • 0032819399 scopus 로고    scopus 로고
    • 2 to increase the efficiency of photosynthetic carbon fixation?
    • 2 to increase the efficiency of photosynthetic carbon fixation? Plant Physiol. 119:9-16. (Pubitemid 29384575)
    • (1999) Plant Physiology , vol.119 , Issue.1 , pp. 9-16
    • Moroney, J.V.1    Somanchi, A.2
  • 204
    • 0029904551 scopus 로고    scopus 로고
    • A pyrenoid-based carbon-concentrating mechanism is present in terrestrial bryophytes of the class Anthocerotae
    • Smith EC, Griffiths H. 1996. A pyrenoid-based carbon-concentrating mechanism is present in terrestrial bryophytes of the class Anthocerotae. Planta 200:203-212. (Pubitemid 26407058)
    • (1996) Planta , vol.200 , Issue.2 , pp. 203-212
    • Smith, E.C.1    Griffiths, H.2
  • 205
    • 0003112935 scopus 로고
    • The pyrenoid
    • Griffiths D. 1970. The pyrenoid. Bot. Rev. 36:29-58.
    • (1970) Bot. Rev , vol.36 , pp. 29-58
    • Griffiths, D.1
  • 206
    • 0030021966 scopus 로고    scopus 로고
    • 2-concentrating mechanism and carbon isotope discrimination in lichens and bryophytes
    • 2-concentrating mechanism and carbon isotope discrimination in lichens and bryophytes. Planta 198:6-16.
    • (1996) Planta , vol.198 , pp. 6-16
    • Smith, E.C.1    Griffiths, H.2
  • 207
    • 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 Physiol. 116:1585-1591. (Pubitemid 128500549)
    • (1998) Plant Physiology , vol.116 , Issue.4 , pp. 1585-1591
    • Borkhsenious, O.N.1    Mason, C.B.2    Moroney, J.V.3
  • 208
    • 20444389072 scopus 로고    scopus 로고
    • 2 concentrating mechanisms in algae: Mechanisms, environmental modulation, and evolution
    • DOI 10.1146/annurev.arplant.56.032604.144052
    • 2 concentrating mechanisms in algae: mechanisms, environmental modulation, and evolution. Annu. Rev. Plant Biol. 56:99-131. (Pubitemid 40802405)
    • (2005) Annual Review of Plant Biology , vol.56 , pp. 99-131
    • Giordano, M.1    Beardall, J.2    Raven, J.A.3
  • 209
    • 68249158101 scopus 로고    scopus 로고
    • Chloroplast structure of diatoms of different classes
    • Bedoshvili Y, Popkova T, Likhoshway Y. 2009. Chloroplast structure of diatoms of different classes. Cell Tissue Biol. 3:297-310.
    • (2009) Cell Tissue Biol , vol.3 , pp. 297-310
    • Bedoshvili, Y.1    Popkova, T.2    Likhoshway, Y.3
  • 212
    • 70449427293 scopus 로고    scopus 로고
    • Distribution and functional role of carbonic anhydrase Cah3 associated with thylakoid membranes in the chloroplast and pyrenoid of Chlamydomonas reinhardtii
    • Markelova AG, Sinetova MP, Kupriyanova EV, Pronina NA. 2009. Distribution and functional role of carbonic anhydrase Cah3 associated with thylakoid membranes in the chloroplast and pyrenoid of Chlamydomonas reinhardtii. Russ. J. Plant Physiol. 56:761-768.
    • (2009) Russ. J. Plant Physiol , vol.56 , pp. 761-768
    • Markelova, A.G.1    Sinetova, M.P.2    Kupriyanova, E.V.3    Pronina, N.A.4
  • 213
    • 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. Biochim. Biophys. Acta Bioenerg. 1817:1248-1255.
    • (2012) Biochim. Biophys. Acta Bioenerg , 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
  • 214
    • 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. J. Biol. Chem. 285:19833-19841.
    • (2010) J. Biol. Chem , vol.285 , pp. 19833-19841
    • Genkov, T.1    Meyer, M.2    Griffiths, H.3    Spreitzer, R.J.4
  • 215
    • 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 Physiol. 156:884-896.
    • (2011) Plant Physiol , vol.156 , pp. 884-896
    • Ma, Y.1    Pollock, S.V.2    Xiao, Y.3    Cunnusamy, K.4    Moroney, J.V.5
  • 216
    • 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. J. Cell Sci. 5:251-269.
    • (1969) J. Cell Sci , vol.5 , pp. 251-269
    • Kowallik, K.1
  • 217
    • 0015004904 scopus 로고
    • Fine structure and light microscopy of a new species of Chrysochromulina (C acantha)
    • Leadbeater BSC, Manton I. 1971. Fine structure and light microscopy of a new species of Chrysochromulina (C. acantha). Arch. Microbiol. 78:58-69.
    • (1971) Arch. Microbiol , vol.78 , pp. 58-69
    • Leadbeater, B.S.C.1    Manton, I.2
  • 218
    • 0014878175 scopus 로고
    • An ultrastructural study of pyrenoids from Chlorella pyrenoidosa
    • Bertagnolli BL, Nadakavukaren MJ. 1970. An ultrastructural study of pyrenoids from Chlorella pyrenoidosa. J. Cell Sci. 7:623-630.
    • (1970) J. Cell Sci , vol.7 , pp. 623-630
    • Bertagnolli, B.L.1    Nadakavukaren, M.J.2
  • 219
    • 84980210245 scopus 로고
    • Chloroplast inclusions in zoospores of Oedocladium
    • Markowitz MM, Hoffman LR. 1974. Chloroplast inclusions in zoospores of Oedocladium. J. Phycol. 10:308-315.
    • (1974) J. Phycol , vol.10 , pp. 308-315
    • Markowitz, M.M.1    Hoffman, L.R.2
  • 220
    • 0028190940 scopus 로고
    • 2-concentrating mechanism is correlated with the formation of the starch sheath around the pyrenoid of Chlamydomonas reinhardtii
    • 2-concentrating mechanism is correlated with the formation of the starch sheath around the pyrenoid of Chlamydomonas reinhardtii. Planta 195:210-216.
    • (1994) Planta , vol.195 , pp. 210-216
    • Ramazanov, Z.1    Rawat, M.2    Henk, M.C.3    Mason, C.B.4    Matthews, S.W.5    Moroney, J.V.6
  • 222
    • 0034019405 scopus 로고    scopus 로고
    • Evolutionary and ecological perspectives on carbon acquisition in phytoplankton
    • Tortell PD. 2000. Evolutionary and ecological perspectives on carbon acquisition in phytoplankton. Limnol. Oceanogr. 45:744-750. (Pubitemid 30247486)
    • (2000) Limnology and Oceanography , vol.45 , Issue.3 , pp. 744-750
    • Tortell, P.D.1
  • 223
    • 0032822281 scopus 로고    scopus 로고
    • 12-dependent 1,2-propanediol degradation
    • Bobik TA, Havemann GD, Busch RJ, Williams DS, Aldrich HC. 1999. The propanediol utilization (pdu) operon of Salmonella enterica serovar Typhimurium LT2 includes genes necessary for formation of polyhedral organelles involved in coenzyme B-12-dependent 1,2-propanediol degradation. J. Bacteriol. 181:5967-5975. (Pubitemid 29459906)
    • (1999) Journal of Bacteriology , vol.181 , Issue.19 , pp. 5967-5975
    • Bobik, T.A.1    Havemann, G.D.2    Busch, R.J.3    Williams, D.S.4    Aldrich, H.C.5
  • 224
    • 0027934799 scopus 로고
    • The control region of the pdu/cob regulon in Salmonella typhimurium
    • Chen P, Andersson DI, Roth JR. 1994. The control region of the pdu/ cob regulon in Salmonella typhimurium. J. Bacteriol. 176:5474-5482. (Pubitemid 24273538)
    • (1994) Journal of Bacteriology , vol.176 , Issue.17 , pp. 5474-5482
    • Chen, P.1    Andersson, D.I.2    Roth, J.R.3
  • 225
    • 0028944586 scopus 로고
    • Ethanolamine utilization in Salmonella typhimurium: Nucleotide sequence, protein expression, and mutational analysis of the cchA cchB eutE eutJ eutG eutH gene cluster
    • Stojiljkovic I, Baumler AJ, Heffron F. 1995. Ethanolamine utilization in Salmonella typhimurium: nucleotide sequence, protein expression, and mutational analysis of the cchA cchB eutE eutJ eutG eutH gene cluster. J. Bacteriol. 177:1357-1366.
    • (1995) J. Bacteriol , vol.177 , pp. 1357-1366
    • Stojiljkovic, I.1    Baumler, A.J.2    Heffron, F.3
  • 226
    • 0032851358 scopus 로고    scopus 로고
    • The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes five homologues of carboxysome shell proteins
    • Kofoid E, Rappleye C, Stojiljkovic I, Roth J. 1999. The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes five homologues of carboxysome shell proteins. J. Bacteriol. 181:5317-5329. (Pubitemid 29416352)
    • (1999) Journal of Bacteriology , vol.181 , Issue.17 , pp. 5317-5329
    • Kofoid, E.1    Rappleye, C.2    Stojiljkovic, I.3    Roth, J.4
  • 227
    • 33645723005 scopus 로고    scopus 로고
    • Polyhedral organelles compartmenting bacterial metabolic processes
    • Bobik TA. 2006. Polyhedral organelles compartmenting bacterial metabolic processes. Appl. Microbiol. Biotechnol. 70:517-525.
    • (2006) Appl. Microbiol. Biotechnol , vol.70 , pp. 517-525
    • Bobik, T.A.1
  • 228
    • 33645964606 scopus 로고    scopus 로고
    • Conserving a volatile metabolite: A role for carboxysome-like organelles in Salmonella enterica
    • Penrod JT, Roth JR. 2006. Conserving a volatile metabolite: a role for carboxysome-like organelles in Salmonella enterica. J. Bacteriol. 188:2865-2874.
    • (2006) J. Bacteriol , vol.188 , pp. 2865-2874
    • Penrod, J.T.1    Roth, J.R.2
  • 232
    • 55649110049 scopus 로고    scopus 로고
    • A simple, fast, and accurate method of phylogenomic inference
    • doi:10.1186/gb-2008-9-10-r151
    • Wu M, Eisen J. 2008. A simple, fast, and accurate method of phylogenomic inference. Genome Biol. 9:R151. doi:10.1186/gb-2008-9-10-r151.
    • (2008) Genome Biol , vol.9
    • Wu, M.1    Eisen, J.2
  • 233
    • 0034849408 scopus 로고    scopus 로고
    • MRBAYES: Bayesian inference of phylogenetic trees
    • Huelsenbeck JP, Ronquist F. 2001. MRBAYES: Bayesian inference of phylogenetic trees. Bioinformatics 17:754-755. (Pubitemid 32851390)
    • (2001) Bioinformatics , vol.17 , Issue.8 , pp. 754-755
    • Huelsenbeck, J.P.1    Ronquist, F.2
  • 234
    • 0041386108 scopus 로고    scopus 로고
    • MrBayes 3: Bayesian phylogenetic inference under mixed models
    • DOI 10.1093/bioinformatics/btg180
    • Ronquist F, Huelsenbeck JP. 2003. MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 19:1572-1574. (Pubitemid 37038874)
    • (2003) Bioinformatics , vol.19 , Issue.12 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 235
    • 74549125386 scopus 로고    scopus 로고
    • SeaView version 4: A multiplatform graphical user interface for sequence alignment and phylogenetic tree building
    • Gouy M, Guindon S, Gascuel O. 2010. SeaView version 4: a multiplatform graphical user interface for sequence alignment and phylogenetic tree building. Mol. Biol. Evol. 27:221-224.
    • (2010) Mol. Biol. Evol , vol.27 , pp. 221-224
    • Gouy, M.1    Guindon, S.2    Gascuel, O.3
  • 236
    • 0034043778 scopus 로고    scopus 로고
    • Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis
    • Castresana J. 2000. Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis. Mol. Biol. Evol. 17:540-552. (Pubitemid 30210700)
    • (2000) Molecular Biology and Evolution , vol.17 , Issue.4 , pp. 540-552
    • Castresana, J.1
  • 238
  • 239
    • 0019264651 scopus 로고
    • Ecophysiological studies on Spirulina platensis. Effect of temperature, light intensity and nitrate concentration on growth and ultrastructure
    • van Eykelenburg C. 1980. Ecophysiological studies on Spirulina platensis. Effect of temperature, light intensity and nitrate concentration on growth and ultrastructure. Antonie Van Leeuwenhoek 46:113-127.
    • (1980) Antonie Van Leeuwenhoek , vol.46 , pp. 113-127
    • Van Eykelenburg, C.1
  • 240
    • 77957352833 scopus 로고    scopus 로고
    • Jmol - A paradigm shift in crystallographic visualization
    • Hanson R. 2010. Jmol-a paradigm shift in crystallographic visualization. J. Appl. Crystallogr. 43:1250-1260.
    • (2010) J. Appl. Crystallogr , vol.43 , pp. 1250-1260
    • Hanson, R.1
  • 241
    • 0029004590 scopus 로고
    • Protein modeling by e-mail
    • Peitsch MC. 1995. Protein modeling by e-mail. Nat. Biotechnol. 13:658-660.
    • (1995) Nat. Biotechnol , vol.13 , pp. 658-660
    • Peitsch, M.C.1
  • 242
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • DOI 10.1093/bioinformatics/bti770
    • Arnold K, Bordoli L, Kopp J, Schwede T. 2006. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22:195-201. (Pubitemid 43205406)
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 244
    • 0000528384 scopus 로고
    • Structure determination and refinement of ribulose 1,5-bisphosphate carboxylase/oxygenase from Synechococcus PCC6301
    • Newman J, Branden C-I, Jones TA. 1993. Structure determination and refinement of ribulose 1,5-bisphosphate carboxylase/oxygenase from Synechococcus PCC6301. Acta Crystallogr. D Biol. Crystallogr. 49:548-560.
    • (1993) Acta Crystallogr. D Biol. Crystallogr , vol.49 , pp. 548-560
    • Newman, J.1    Branden, C.-I.2    Jones, T.A.3
  • 245
    • 0034599484 scopus 로고    scopus 로고
    • The active site architecture of Pisum sativum β-carbonic anhydrase is a mirror image of that of α-carbonic anhydrases
    • Kimber MS, Pai EF. 2000. The active site architecture of Pisum sativum beta-carbonic anhydrase is a mirror image of that of alpha-carbonic anhydrases. EMBO J. 19:1407-1418. (Pubitemid 30182148)
    • (2000) EMBO Journal , vol.19 , Issue.7 , pp. 1407-1418
    • Kimber, M.S.1    Pai, E.F.2
  • 246
    • 0025859290 scopus 로고
    • 2-requiring mutant of the cyanobacterium, Synechococcus sp. PCC7942
    • 2-requiring mutant of the cyanobacterium, Synechococcus sp. PCC7942. Mol. Gen. Genet. 226:401-408.
    • (1991) Mol. Gen. Genet , vol.226 , pp. 401-408
    • Suzuki, E.1    Fukuzawa, H.2    Miyachi, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.