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Volumn 58, Issue 1, 2015, Pages 86-97

Ions channels/transporters and chloroplast regulation

Author keywords

Chloroplast envelope; Ions trafficking; Photosynthesis; Proton motive force; Thylakoids

Indexed keywords

ADENOSINE TRIPHOSPHATE; ANION TRANSPORT PROTEIN; CALCIUM ION; CARRIER PROTEIN; CATION CHANNEL; CATION TRANSPORT PROTEIN; ION CHANNEL; ION TRANSPORTER; METAL ION; UNCLASSIFIED DRUG; ARABIDOPSIS PROTEIN; CALCIUM;

EID: 84930539564     PISSN: 01434160     EISSN: 15321991     Source Type: Journal    
DOI: 10.1016/j.ceca.2014.10.002     Document Type: Review
Times cited : (105)

References (154)
  • 2
    • 0041733229 scopus 로고    scopus 로고
    • Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis
    • Froehlich J.E., Wilkerson C.G., Ray W.K., et al. Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis. J. Proteome Res. 2003, 2:413-425.
    • (2003) J. Proteome Res. , vol.2 , pp. 413-425
    • Froehlich, J.E.1    Wilkerson, C.G.2    Ray, W.K.3
  • 3
    • 0348136190 scopus 로고    scopus 로고
    • Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana
    • Ferro M., Salvi D., Brugière S., et al. Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana. Mol. Cell. Proteomics 2003, 2:325-345.
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 325-345
    • Ferro, M.1    Salvi, D.2    Brugière, S.3
  • 4
    • 44349099751 scopus 로고    scopus 로고
    • Sorting signals N-terminal modifications and abundance of the chloroplast proteome
    • Zybailov B., Rutschow H., Friso G., et al. Sorting signals N-terminal modifications and abundance of the chloroplast proteome. PLoS ONE 2008, 3:e1994.
    • (2008) PLoS ONE , vol.3 , pp. e1994
    • Zybailov, B.1    Rutschow, H.2    Friso, G.3
  • 5
    • 77953149231 scopus 로고    scopus 로고
    • AT_CHLORO: a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins
    • Ferro M., Brugière S., Salvi D., et al. AT_CHLORO: a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins. Mol. Cell. Proteomics 2010, 9:1063-1084.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1063-1084
    • Ferro, M.1    Brugière, S.2    Salvi, D.3
  • 6
    • 84905252677 scopus 로고    scopus 로고
    • Deciphering thylakoid sub-compartments using a mass spectrometry-based approach
    • pii: mcp.M114.040923s
    • Tomizioli M., Lazar C., Brugiere S., et al. Deciphering thylakoid sub-compartments using a mass spectrometry-based approach. Mol. Cell. Proteomics 2014, 13:2147-2167. pii: mcp.M114.040923s.
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 2147-2167
    • Tomizioli, M.1    Lazar, C.2    Brugiere, S.3
  • 7
    • 84870195513 scopus 로고    scopus 로고
    • The biosynthetic capacities of the plastids and integration between cytoplasmic and chloroplast processes
    • Rolland N., Curien G., Finazzi G., et al. The biosynthetic capacities of the plastids and integration between cytoplasmic and chloroplast processes. Annu. Rev. Genet. 2012, 46:233-264.
    • (2012) Annu. Rev. Genet. , vol.46 , pp. 233-264
    • Rolland, N.1    Curien, G.2    Finazzi, G.3
  • 8
    • 84896708832 scopus 로고    scopus 로고
    • Function and evolution of channels and transporters in photosynthetic membranes
    • Pfeil B.E., Schoefs B., Spetea C. Function and evolution of channels and transporters in photosynthetic membranes. Cell. Mol. Life Sci. 2014, 71:979-998.
    • (2014) Cell. Mol. Life Sci. , vol.71 , pp. 979-998
    • Pfeil, B.E.1    Schoefs, B.2    Spetea, C.3
  • 9
    • 0344562577 scopus 로고
    • Préparation et activités enzymatiques de l'enveloppe des chloroplastes d'épinard
    • Joyard J., Douce R. Préparation et activités enzymatiques de l'enveloppe des chloroplastes d'épinard. Physiol. Vég. 1976, 14:31-48.
    • (1976) Physiol. Vég. , vol.14 , pp. 31-48
    • Joyard, J.1    Douce, R.2
  • 11
    • 0037781037 scopus 로고    scopus 로고
    • PAA1, a P-type ATPase of Arabidopsis, functions in copper transport in chloroplasts
    • Shikanai T., Müller-Moulé P., Munekage Y., Niyogi K.K., Pilon M. PAA1, a P-type ATPase of Arabidopsis, functions in copper transport in chloroplasts. Plant Cell 2003, 15:1333-1346.
    • (2003) Plant Cell , vol.15 , pp. 1333-1346
    • Shikanai, T.1    Müller-Moulé, P.2    Munekage, Y.3    Niyogi, K.K.4    Pilon, M.5
  • 12
    • 33646153414 scopus 로고    scopus 로고
    • HMA1, a new Cu-ATPase of the chloroplast envelope, is essential for growth under adverse light conditions
    • Seigneurin-Berny D., Gravot A., Auroy P., et al. HMA1, a new Cu-ATPase of the chloroplast envelope, is essential for growth under adverse light conditions. J. Biol. Chem. 2006, 281:2882-2892.
    • (2006) J. Biol. Chem. , vol.281 , pp. 2882-2892
    • Seigneurin-Berny, D.1    Gravot, A.2    Auroy, P.3
  • 13
    • 17644403212 scopus 로고    scopus 로고
    • Two P-Type ATPases are required for copper delivery in Arabidopsis thaliana chloroplasts
    • Abdel-Ghany S.E., Müller-Moulé P., Niyogi K.K., Pilon M., Shikanai T. Two P-Type ATPases are required for copper delivery in Arabidopsis thaliana chloroplasts. Plant Cell 2005, 17:1-19.
    • (2005) Plant Cell , vol.17 , pp. 1-19
    • Abdel-Ghany, S.E.1    Müller-Moulé, P.2    Niyogi, K.K.3    Pilon, M.4    Shikanai, T.5
  • 15
    • 84897429414 scopus 로고    scopus 로고
    • HMA1 and PAA1, two chloroplast-envelope PIB-ATPases, play distinct roles in chloroplast copper homeostasis
    • Boutigny S., Sautron E., Finazzi G., et al. HMA1 and PAA1, two chloroplast-envelope PIB-ATPases, play distinct roles in chloroplast copper homeostasis. J. Exp. Bot. 2014, 65(6):1529-1540.
    • (2014) J. Exp. Bot. , vol.65 , Issue.6 , pp. 1529-1540
    • Boutigny, S.1    Sautron, E.2    Finazzi, G.3
  • 17
    • 66349100468 scopus 로고    scopus 로고
    • AtHMA1 contributes to the detoxification of excess Zn(II) in Arabidopsis
    • Kim Y.Y., Choi H., Segami S., et al. AtHMA1 contributes to the detoxification of excess Zn(II) in Arabidopsis. Plant J. 2009, 58:737-753.
    • (2009) Plant J. , vol.58 , pp. 737-753
    • Kim, Y.Y.1    Choi, H.2    Segami, S.3
  • 18
    • 84869099802 scopus 로고    scopus 로고
    • Barley HvHMA1 is a heavy metal pump involved in mobilizing organellar Zn and Cu and plays a role in metal loading into grains
    • Mikkelsen M.D., Pedas P., Schiller M., et al. Barley HvHMA1 is a heavy metal pump involved in mobilizing organellar Zn and Cu and plays a role in metal loading into grains. PLoS ONE 2012, 7:e49027.
    • (2012) PLoS ONE , vol.7 , pp. e49027
    • Mikkelsen, M.D.1    Pedas, P.2    Schiller, M.3
  • 20
    • 0029010594 scopus 로고
    • Evidence for two catalytically different magnesium-binding sites in acetohydroxy acid isomeroreductase by site-directed mutagenesis
    • Dumas R., Butikofer M.C., Job D., Douce R. Evidence for two catalytically different magnesium-binding sites in acetohydroxy acid isomeroreductase by site-directed mutagenesis. Biochemistry 1995, 34:6026-6036.
    • (1995) Biochemistry , vol.34 , pp. 6026-6036
    • Dumas, R.1    Butikofer, M.C.2    Job, D.3    Douce, R.4
  • 21
    • 0036316780 scopus 로고    scopus 로고
    • Magnesium transport and function in plants: the tip of the iceberg
    • Shaul O. Magnesium transport and function in plants: the tip of the iceberg. Biometals 2002, 15:309-323.
    • (2002) Biometals , vol.15 , pp. 309-323
    • Shaul, O.1
  • 22
    • 84867156481 scopus 로고    scopus 로고
    • 2+ transport by the CorA family of divalent cation transporters
    • 2+ transport by the CorA family of divalent cation transporters. Curr. Top. Membr. 2012, 69:393-414.
    • (2012) Curr. Top. Membr. , vol.69 , pp. 393-414
    • Guskov, A.1    Eshaghi, S.2
  • 23
    • 27144470708 scopus 로고    scopus 로고
    • A putative magnesium transporter AtMRS2-11 is localized to the plant chloroplast envelope membrane system
    • Drummond R.S.M., Tutone A., Li Y.C., Gardner R.C. A putative magnesium transporter AtMRS2-11 is localized to the plant chloroplast envelope membrane system. Plant Sci. 2006, 170:78-89.
    • (2006) Plant Sci. , vol.170 , pp. 78-89
    • Drummond, R.S.M.1    Tutone, A.2    Li, Y.C.3    Gardner, R.C.4
  • 25
    • 34248146824 scopus 로고    scopus 로고
    • PIC1, an ancient permease in Arabidopsis chloroplasts, mediates iron transport
    • Duy D., Wanner G., Meda A.R., von Wirén N., Soll J., Philippar K. PIC1, an ancient permease in Arabidopsis chloroplasts, mediates iron transport. Plant Cell 2007, 19:986-1006.
    • (2007) Plant Cell , vol.19 , pp. 986-1006
    • Duy, D.1    Wanner, G.2    Meda, A.R.3    von Wirén, N.4    Soll, J.5    Philippar, K.6
  • 26
    • 79953692401 scopus 로고    scopus 로고
    • The chloroplast permease PIC1 regulates plant growth and development by directing homeostasis and transport of iron
    • Duy D., Stübe R., Wanner G., Philippar K. The chloroplast permease PIC1 regulates plant growth and development by directing homeostasis and transport of iron. Plant Physiol. 2011, 155:1709-1722.
    • (2011) Plant Physiol. , vol.155 , pp. 1709-1722
    • Duy, D.1    Stübe, R.2    Wanner, G.3    Philippar, K.4
  • 27
    • 70349651782 scopus 로고    scopus 로고
    • Multiple antibiotic resistance in Arabidopsis is conferred by mutations in a chloroplast-localized transport protein
    • Conte S., Stevenson D., Furner I., Lloyd A. Multiple antibiotic resistance in Arabidopsis is conferred by mutations in a chloroplast-localized transport protein. Plant Physiol. 2009, 151:559-573.
    • (2009) Plant Physiol. , vol.151 , pp. 559-573
    • Conte, S.1    Stevenson, D.2    Furner, I.3    Lloyd, A.4
  • 28
    • 77954055112 scopus 로고    scopus 로고
    • Disruption of Nap14, a plastid-localized non-intrinsic ABC protein in Arabidopsis thaliana results in the over-accumulation of transition metals and in aberrant chloroplast structures
    • Shimoni-Shor E., Hassidim M., Yuval-Naeh N., Keren N. Disruption of Nap14, a plastid-localized non-intrinsic ABC protein in Arabidopsis thaliana results in the over-accumulation of transition metals and in aberrant chloroplast structures. Plant Cell Environ. 2010, 33:1029-1038.
    • (2010) Plant Cell Environ. , vol.33 , pp. 1029-1038
    • Shimoni-Shor, E.1    Hassidim, M.2    Yuval-Naeh, N.3    Keren, N.4
  • 29
    • 84876777659 scopus 로고    scopus 로고
    • The Arabidopsis Yellow Stripe Like4 and 6 transporters control iron release from the chloroplast
    • Divol F., Couch D., Conéjéro G., Roschzttardtz H., Mari S., Curie C. The Arabidopsis Yellow Stripe Like4 and 6 transporters control iron release from the chloroplast. Plant Cell 2013, 25:1040-1055.
    • (2013) Plant Cell , vol.25 , pp. 1040-1055
    • Divol, F.1    Couch, D.2    Conéjéro, G.3    Roschzttardtz, H.4    Mari, S.5    Curie, C.6
  • 30
    • 84900819481 scopus 로고    scopus 로고
    • Arabidopsis thaliana yellow stripe1-Like4 and Yellow stripe1-like6 localize to internal cellular membranes and are involved in metal ion homeostasis
    • Conte S.S., Chu H.H., Rodriguez D.C., et al. Arabidopsis thaliana yellow stripe1-Like4 and Yellow stripe1-like6 localize to internal cellular membranes and are involved in metal ion homeostasis. Front. Plant Sci. 2013, 26:283.
    • (2013) Front. Plant Sci. , vol.26 , pp. 283
    • Conte, S.S.1    Chu, H.H.2    Rodriguez, D.C.3
  • 31
    • 0001466980 scopus 로고
    • Ion homeostasis in chloroplasts under salinity and mineral deficiency: I. Solute concentrations in leaves and chloroplasts from spinach plants under NaCl or NaNO(3) salinity
    • Schröppel-Meier G., Kaiser W.M. Ion homeostasis in chloroplasts under salinity and mineral deficiency: I. Solute concentrations in leaves and chloroplasts from spinach plants under NaCl or NaNO(3) salinity. Plant Physiol. 1988, 87:822-827.
    • (1988) Plant Physiol. , vol.87 , pp. 822-827
    • Schröppel-Meier, G.1    Kaiser, W.M.2
  • 33
    • 35848940720 scopus 로고    scopus 로고
    • Two members of the Arabidopsis CLC (chloride channel) family AtCLCe and AtCLCf, are associated with thylakoid and Golgi membranes, respectively
    • Marmagne A., Vinauger-Douard M., Monachello D., et al. Two members of the Arabidopsis CLC (chloride channel) family AtCLCe and AtCLCf, are associated with thylakoid and Golgi membranes, respectively. J. Exp. Bot. 2007, 58:3385-3393.
    • (2007) J. Exp. Bot. , vol.58 , pp. 3385-3393
    • Marmagne, A.1    Vinauger-Douard, M.2    Monachello, D.3
  • 34
    • 79955601703 scopus 로고    scopus 로고
    • Anion channels/transporters in plants: from molecular bases to regulatory networks
    • Barbier-Brygoo H., De Angeli A., Filleur S., et al. Anion channels/transporters in plants: from molecular bases to regulatory networks. Annu. Rev. Plant Biol. 2011, 62:25-51.
    • (2011) Annu. Rev. Plant Biol. , vol.62 , pp. 25-51
    • Barbier-Brygoo, H.1    De Angeli, A.2    Filleur, S.3
  • 35
    • 0000721724 scopus 로고
    • Chloride-selective ion channels in the photosynthetic membrane of a higher plant
    • Schönknecht G., Hedrich R., Junge W., Raschke K. Chloride-selective ion channels in the photosynthetic membrane of a higher plant. Nature 1988, 336:589-592.
    • (1988) Nature , vol.336 , pp. 589-592
    • Schönknecht, G.1    Hedrich, R.2    Junge, W.3    Raschke, K.4
  • 37
    • 34547675939 scopus 로고    scopus 로고
    • A nitrite transporter associated with nitrite uptake by higher plant chloroplasts
    • Sugiura M., Georgescu M.N., Takahashi M. A nitrite transporter associated with nitrite uptake by higher plant chloroplasts. Plant Cell Physiol. 2007, 48:1022-1035.
    • (2007) Plant Cell Physiol. , vol.48 , pp. 1022-1035
    • Sugiura, M.1    Georgescu, M.N.2    Takahashi, M.3
  • 38
    • 0018587160 scopus 로고
    • Sulfate transport across the limiting double membrane or envelope, of spinach chloroplasts
    • Mourioux G., Douce R. Sulfate transport across the limiting double membrane or envelope, of spinach chloroplasts. Biochimie 1979, 61:1283-1292.
    • (1979) Biochimie , vol.61 , pp. 1283-1292
    • Mourioux, G.1    Douce, R.2
  • 39
    • 84874262000 scopus 로고    scopus 로고
    • SULTR3;1 is a chloroplast-localized sulfate transporter in Arabidopsis thaliana
    • Cao M.J., Wang Z., Wirtz M., Hell R., Oliver D.J., Xiang C.B. SULTR3;1 is a chloroplast-localized sulfate transporter in Arabidopsis thaliana. Plant J. 2013, 73:607-616.
    • (2013) Plant J. , vol.73 , pp. 607-616
    • Cao, M.J.1    Wang, Z.2    Wirtz, M.3    Hell, R.4    Oliver, D.J.5    Xiang, C.B.6
  • 40
    • 4344624847 scopus 로고    scopus 로고
    • Plant sulphate transporters: co-ordination of uptake, intracellular and long-distance transport
    • Buchner P., Takahashi H., Hawkesford M.J. Plant sulphate transporters: co-ordination of uptake, intracellular and long-distance transport. J. Exp. Bot. 2004, 55:1765-1773.
    • (2004) J. Exp. Bot. , vol.55 , pp. 1765-1773
    • Buchner, P.1    Takahashi, H.2    Hawkesford, M.J.3
  • 43
    • 84904768348 scopus 로고    scopus 로고
    • The carbon concentrating mechanism in Chlamydomonas reinhardtii: finding the missing pieces
    • Jungnick N., Ma Y., Mukherjee B., et al. The carbon concentrating mechanism in Chlamydomonas reinhardtii: finding the missing pieces. Photosynth. Res. 2014, 121:159-173.
    • (2014) Photosynth. Res. , vol.121 , pp. 159-173
    • Jungnick, N.1    Ma, Y.2    Mukherjee, B.3
  • 44
    • 77956926954 scopus 로고    scopus 로고
    • 2-concentrating mechanism and carbon assimilation
    • Springer, New York
    • 2-concentrating mechanism and carbon assimilation. The Chlamydomonas Sourcebook 2009, vol. 2. Springer, New York.
    • (2009) The Chlamydomonas Sourcebook , vol.2
    • Spalding, M.H.1
  • 45
    • 0031785343 scopus 로고    scopus 로고
    • 2 in Cells and Chloroplasts from the Microalgae Chlamydomonas reinhardtii and Dunaliella tertiolecta
    • 2 in Cells and Chloroplasts from the Microalgae Chlamydomonas reinhardtii and Dunaliella tertiolecta. Plant Physiol. 1998, 116:193-201.
    • (1998) Plant Physiol. , vol.116 , pp. 193-201
    • Amoroso, G.1    Sültemeyer, D.2    Thyssen, C.3    Fock, H.P.4
  • 46
    • 0030733162 scopus 로고    scopus 로고
    • Disruption of the plastid ycf10 open reading frame affects uptake of inorganic carbon in the chloroplast of Chlamydomonas
    • Rolland N., Dorne A.-J., Amoroso G., Sültemeyer D.F., Joyard J., Rochaix J.-D. Disruption of the plastid ycf10 open reading frame affects uptake of inorganic carbon in the chloroplast of Chlamydomonas. EMBO J. 1997, 16:6713-6726.
    • (1997) EMBO J. , vol.16 , pp. 6713-6726
    • Rolland, N.1    Dorne, A.-J.2    Amoroso, G.3    Sültemeyer, D.F.4    Joyard, J.5    Rochaix, J.-D.6
  • 47
    • 0027463403 scopus 로고
    • Chloroplast envelope protein encoded by chloroplast genome
    • Sasaki Y., Sekiguchi K., Nagano Y., Matsuno R. Chloroplast envelope protein encoded by chloroplast genome. FEBS Lett. 1993, 316:93-98.
    • (1993) FEBS Lett. , vol.316 , pp. 93-98
    • Sasaki, Y.1    Sekiguchi, K.2    Nagano, Y.3    Matsuno, R.4
  • 48
    • 0029831325 scopus 로고    scopus 로고
    • Absence of light-induced proton extrusion in a cotA-less mutant of Synechocystis sp. strain PCC6803
    • Katoh A., Sonoda M., Katoh H., Ogawa T. Absence of light-induced proton extrusion in a cotA-less mutant of Synechocystis sp. strain PCC6803. J. Bacteriol. 1996, 178:5452-5455.
    • (1996) J. Bacteriol. , vol.178 , pp. 5452-5455
    • Katoh, A.1    Sonoda, M.2    Katoh, H.3    Ogawa, T.4
  • 49
    • 0033829519 scopus 로고    scopus 로고
    • The Chlamydomonas reinhardtii Nar1 gene encodes a chloroplast membrane protein involved in nitrite transport
    • Rexach J., Fernandez E., Galvan A. The Chlamydomonas reinhardtii Nar1 gene encodes a chloroplast membrane protein involved in nitrite transport. Plant Cell 2000, 12:1441-1453.
    • (2000) Plant Cell , vol.12 , pp. 1441-1453
    • Rexach, J.1    Fernandez, E.2    Galvan, A.3
  • 50
    • 2942681146 scopus 로고    scopus 로고
    • 2-responsive genes regulated by CCM1 controlling a carbon-concentrating mechanism in Chlamydomonas reinhardtii
    • 2-responsive genes regulated by CCM1 controlling a carbon-concentrating mechanism in Chlamydomonas reinhardtii. Plant Physiol. 2004, 135:1595-1607.
    • (2004) Plant Physiol. , vol.135 , pp. 1595-1607
    • Miura, K.1    Yamano, T.2    Yoshioka, S.3
  • 54
    • 0037251317 scopus 로고    scopus 로고
    • Analysis of light and CO(2) regulation in Chlamydomonas reinhardtii using genome-wide approaches
    • Im C.S., Zhang Z., Shrager J., Chang C.W., Grossman A.R. Analysis of light and CO(2) regulation in Chlamydomonas reinhardtii using genome-wide approaches. Photosynth. Res. 2003, 75:111-125.
    • (2003) Photosynth. Res. , vol.75 , pp. 111-125
    • Im, C.S.1    Zhang, Z.2    Shrager, J.3    Chang, C.W.4    Grossman, A.R.5
  • 55
    • 62449323128 scopus 로고    scopus 로고
    • Carbon-concentrating mechanism in a green alga Chlamydomonas reinhardtii, revealed by transcriptome analyses
    • Yamano T., Fukuzawa H. Carbon-concentrating mechanism in a green alga Chlamydomonas reinhardtii, revealed by transcriptome analyses. J. Basic Microbiol. 2009, 49:42-51.
    • (2009) J. Basic Microbiol. , vol.49 , pp. 42-51
    • Yamano, T.1    Fukuzawa, H.2
  • 57
    • 84863104468 scopus 로고    scopus 로고
    • 2-concentrating mechanism regulator CIA5/CCM1
    • 2-concentrating mechanism regulator CIA5/CCM1. Plant Cell 2012, 24:1876-1893.
    • (2012) Plant Cell , vol.24 , pp. 1876-1893
    • Fang, W.1    Si, Y.2    Douglass, S.3
  • 58
    • 84901447887 scopus 로고    scopus 로고
    • High-throughput genotyping of green algal mutants reveals random distribution of mutagenic insertion sites and endonucleolytic cleavage of transforming DNA
    • Zhang R., Patena W., Armbruster U., Gang S.S., Blum S.R., Jonikas M.C. High-throughput genotyping of green algal mutants reveals random distribution of mutagenic insertion sites and endonucleolytic cleavage of transforming DNA. Plant Cell 2014, 26:1398-1409.
    • (2014) Plant Cell , vol.26 , pp. 1398-1409
    • Zhang, R.1    Patena, W.2    Armbruster, U.3    Gang, S.S.4    Blum, S.R.5    Jonikas, M.C.6
  • 59
    • 34047192472 scopus 로고    scopus 로고
    • Characterization and expression analysis of genes encoding α and β carbonic anhydrases in Arabidopsis
    • Fabre N., Reiter I.M., Becuwe-Linka N., Genty B., Rumeau D. Characterization and expression analysis of genes encoding α and β carbonic anhydrases in Arabidopsis. Plant Cell Environ. 2007, 30:617-629.
    • (2007) Plant Cell Environ. , vol.30 , pp. 617-629
    • Fabre, N.1    Reiter, I.M.2    Becuwe-Linka, N.3    Genty, B.4    Rumeau, D.5
  • 60
    • 84857248273 scopus 로고    scopus 로고
    • A basal carbon concentrating mechanism in plants?
    • Zabaleta E., Martin M.V., Braun H.P. A basal carbon concentrating mechanism in plants?. Plant Sci. 2012, 187:97-104.
    • (2012) Plant Sci. , vol.187 , pp. 97-104
    • Zabaleta, E.1    Martin, M.V.2    Braun, H.P.3
  • 64
    • 0000726019 scopus 로고
    • Rate-limiting factors in leaf photosynthesis. I. Carbon fluxes in the Calvin cycle
    • Dietz K., Heber U. Rate-limiting factors in leaf photosynthesis. I. Carbon fluxes in the Calvin cycle. Biochim. Biophys. Acta 1984, 767:432-443.
    • (1984) Biochim. Biophys. Acta , vol.767 , pp. 432-443
    • Dietz, K.1    Heber, U.2
  • 65
    • 0036670270 scopus 로고    scopus 로고
    • A chloroplast phosphate transporter PHT2 influences allocation of phosphate within the plant and phosphate-starvation responses
    • Versaw W.K., Harrison M.J. A chloroplast phosphate transporter PHT2 influences allocation of phosphate within the plant and phosphate-starvation responses. Plant Cell 2002, 14:1751-1766.
    • (2002) Plant Cell , vol.14 , pp. 1751-1766
    • Versaw, W.K.1    Harrison, M.J.2
  • 66
    • 0037143630 scopus 로고    scopus 로고
    • Integral membrane proteins of the chloroplast envelope: identification and subcellular localization of new transporters
    • Ferro M., Salvi D., Riviere-Rolland H., et al. Integral membrane proteins of the chloroplast envelope: identification and subcellular localization of new transporters. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:11487-11492.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 11487-11492
    • Ferro, M.1    Salvi, D.2    Riviere-Rolland, H.3
  • 67
    • 0742267789 scopus 로고    scopus 로고
    • Characterization of a protein of the plastid inner envelope having homology to animal inorganic phosphate, chloride and organic-anion transporters
    • Roth C., Menzel G., Petetot J.M., Rochat-Hacker S., Poirier Y. Characterization of a protein of the plastid inner envelope having homology to animal inorganic phosphate, chloride and organic-anion transporters. Planta 2004, 218:406-416.
    • (2004) Planta , vol.218 , pp. 406-416
    • Roth, C.1    Menzel, G.2    Petetot, J.M.3    Rochat-Hacker, S.4    Poirier, Y.5
  • 68
    • 38949162946 scopus 로고    scopus 로고
    • Functional analysis of the Arabidopsis PHT4 family of intracellular phosphate transporters
    • Guo B., Jin Y., Wussler C., Blancaflor E.B., Motes C.M., Versaw W.K. Functional analysis of the Arabidopsis PHT4 family of intracellular phosphate transporters. New Phytol. 2008, 177:889-898.
    • (2008) New Phytol. , vol.177 , pp. 889-898
    • Guo, B.1    Jin, Y.2    Wussler, C.3    Blancaflor, E.B.4    Motes, C.M.5    Versaw, W.K.6
  • 70
    • 79957501998 scopus 로고    scopus 로고
    • Circadian clock-regulated phosphate transporter PHT4;1 plays an important role in Arabidopsis defense
    • Wang G.Y., Shi J.L., Ng G., Battle S.L., Zhang C., Lu H. Circadian clock-regulated phosphate transporter PHT4;1 plays an important role in Arabidopsis defense. Mol. Plant 2011, 4:516-526.
    • (2011) Mol. Plant , vol.4 , pp. 516-526
    • Wang, G.Y.1    Shi, J.L.2    Ng, G.3    Battle, S.L.4    Zhang, C.5    Lu, H.6
  • 71
    • 82755171849 scopus 로고    scopus 로고
    • The sink-specific plastidic phosphate transporter PHT4;2 influences starch accumulation and leaf size in Arabidopsis
    • Irigoyen S., Karlsson P.M., Kuruvilla J., Spetea C., Versaw W.K. The sink-specific plastidic phosphate transporter PHT4;2 influences starch accumulation and leaf size in Arabidopsis. Plant Physiol. 2011, 157:1765-1777.
    • (2011) Plant Physiol. , vol.157 , pp. 1765-1777
    • Irigoyen, S.1    Karlsson, P.M.2    Kuruvilla, J.3    Spetea, C.4    Versaw, W.K.5
  • 73
    • 0027375852 scopus 로고
    • Characterization of a gene encoding a Ca(2+)-ATPase-like protein in the plastid envelope
    • Huang L., Berkelman T., Franklin A.E., Hoffman N.E. Characterization of a gene encoding a Ca(2+)-ATPase-like protein in the plastid envelope. Proc. Natl. Acad. Sci. U. S. A. 1993, 90:10066-10070.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 10066-10070
    • Huang, L.1    Berkelman, T.2    Franklin, A.E.3    Hoffman, N.E.4
  • 75
    • 67049158006 scopus 로고    scopus 로고
    • An efficient organic solvent based extraction method for the proteomic analysis of Arabidopsis plasma membranes
    • Mitra S.K., Walters B.T., Clouse S.D., Goshe M.B. An efficient organic solvent based extraction method for the proteomic analysis of Arabidopsis plasma membranes. J. Proteome Res. 2009, 8:2752-2767.
    • (2009) J. Proteome Res. , vol.8 , pp. 2752-2767
    • Mitra, S.K.1    Walters, B.T.2    Clouse, S.D.3    Goshe, M.B.4
  • 76
    • 79651471840 scopus 로고    scopus 로고
    • Dual localization of plant glutamate receptor AtGLR3.4 to plastids and plasmamembrane
    • Teardo E., Formentin E., Segalla A., et al. Dual localization of plant glutamate receptor AtGLR3.4 to plastids and plasmamembrane. Biochim. Biophys. Acta 2011, 1807:359-367.
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 359-367
    • Teardo, E.1    Formentin, E.2    Segalla, A.3
  • 77
    • 26644432485 scopus 로고    scopus 로고
    • AtGLR3.4, a glutamate receptor channel-like gene is sensitive to touch and cold
    • Meyerhoff O., Müller K., Roelfsema M.R., et al. AtGLR3.4, a glutamate receptor channel-like gene is sensitive to touch and cold. Planta 2005, 222:418-427.
    • (2005) Planta , vol.222 , pp. 418-427
    • Meyerhoff, O.1    Müller, K.2    Roelfsema, M.R.3
  • 78
    • 30044442533 scopus 로고    scopus 로고
    • MscS-like proteins control plastid size and shape in Arabidopsis thaliana
    • Haswell E.S., Meyerowitz E.M. MscS-like proteins control plastid size and shape in Arabidopsis thaliana. Curr. Biol. 2006, 16:1-11.
    • (2006) Curr. Biol. , vol.16 , pp. 1-11
    • Haswell, E.S.1    Meyerowitz, E.M.2
  • 79
    • 84857993679 scopus 로고    scopus 로고
    • Mechanosensitive channels protect plastids from hypoosmotic stress during normal plant growth
    • Veley K.M., Marshburn S., Clure C.E., Haswell E.S. Mechanosensitive channels protect plastids from hypoosmotic stress during normal plant growth. Curr. Biol. 2012, 22:408-413.
    • (2012) Curr. Biol. , vol.22 , pp. 408-413
    • Veley, K.M.1    Marshburn, S.2    Clure, C.E.3    Haswell, E.S.4
  • 80
    • 84900390014 scopus 로고    scopus 로고
    • Decreased capacity for sodium export out of Arabidopsis chloroplasts impairs salt tolerance, photosynthesis and plant performance
    • Müller M., Kunz H.H., Schroeder J.I., Kemp G., Young H.S., Neuhaus H.E. Decreased capacity for sodium export out of Arabidopsis chloroplasts impairs salt tolerance, photosynthesis and plant performance. Plant J. 2014, 78:646-658.
    • (2014) Plant J. , vol.78 , pp. 646-658
    • Müller, M.1    Kunz, H.H.2    Schroeder, J.I.3    Kemp, G.4    Young, H.S.5    Neuhaus, H.E.6
  • 81
    • 84901020408 scopus 로고    scopus 로고
    • Plastidial transporters KEA1 -2, and -3 are essential for chloroplast osmoregulation, integrity, and pH regulation in Arabidopsis
    • Kunz H.H., Gierth M., Herdean A., et al. Plastidial transporters KEA1 -2, and -3 are essential for chloroplast osmoregulation, integrity, and pH regulation in Arabidopsis. Proc. Natl. Acad. Sci. U. S. A. 2014, 111:7480-7485.
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. 7480-7485
    • Kunz, H.H.1    Gierth, M.2    Herdean, A.3
  • 82
    • 84885667900 scopus 로고    scopus 로고
    • + channel controls photosynthetic light utilization in plants
    • + channel controls photosynthetic light utilization in plants. Science 2013, 342:114-118.
    • (2013) Science , vol.342 , pp. 114-118
    • Carraretto, L.1    Formentin, E.2    Teardo, E.3
  • 83
    • 3042711950 scopus 로고    scopus 로고
    • + exchanger on the chloroplast envelope functions in pH homeostasis and chloroplast development in Arabidopsis thaliana
    • + exchanger on the chloroplast envelope functions in pH homeostasis and chloroplast development in Arabidopsis thaliana. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:10211-10216.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 10211-10216
    • Song, C.P.1    Guo, Y.2    Qiu, Q.3
  • 85
    • 79952286380 scopus 로고    scopus 로고
    • + transporters fail to target ovules in Arabidopsis
    • + transporters fail to target ovules in Arabidopsis. Plant Cell. 2011, 23:81-93.
    • (2011) Plant Cell. , vol.23 , pp. 81-93
    • Lu, Y.1    Chanroj, S.2    Zulkifli, L.3
  • 86
    • 0015821014 scopus 로고
    • Isolation and properties of the envelope of spinach chloroplasts
    • Douce R., Holtz R.B., Benson A.A. Isolation and properties of the envelope of spinach chloroplasts. J. Biol. Chem. 1973, 248:7215-7222.
    • (1973) J. Biol. Chem. , vol.248 , pp. 7215-7222
    • Douce, R.1    Holtz, R.B.2    Benson, A.A.3
  • 87
    • 2642711755 scopus 로고
    • Characterization and localization of the ATPase associated with pea chloroplast envelope membranes
    • McCarty D.R., Keegstra K., Selman B.R. Characterization and localization of the ATPase associated with pea chloroplast envelope membranes. Plant Physiol. 1984, 76:584-588.
    • (1984) Plant Physiol. , vol.76 , pp. 584-588
    • McCarty, D.R.1    Keegstra, K.2    Selman, B.R.3
  • 89
    • 34147149761 scopus 로고    scopus 로고
    • A proteomics dissection of Arabidopsis thaliana vacuoles isolated from cell culture
    • Jaquinod M., Villiers F., Kieffer-Jaquinod S., et al. A proteomics dissection of Arabidopsis thaliana vacuoles isolated from cell culture. Mol. Cell. Proteomics 2007, 6:394-412.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 394-412
    • Jaquinod, M.1    Villiers, F.2    Kieffer-Jaquinod, S.3
  • 91
    • 84901056358 scopus 로고    scopus 로고
    • Lignin, mitochondrial family, and photorespiratory transporter classification as case studies in using co-expression, co-response, and protein locations to aid in identifying transport functions
    • Tohge T., Fernie A.R. Lignin, mitochondrial family, and photorespiratory transporter classification as case studies in using co-expression, co-response, and protein locations to aid in identifying transport functions. Front. Plant Sci. 2014, 5:75.
    • (2014) Front. Plant Sci. , vol.5 , pp. 75
    • Tohge, T.1    Fernie, A.R.2
  • 92
    • 0000400911 scopus 로고
    • Effect of salts and electron transport on the conformation of isolated chloroplasts II. Electron microscopy
    • Izawa S., Good N.E. Effect of salts and electron transport on the conformation of isolated chloroplasts II. Electron microscopy. Plant Physiol. 1966, 41:544-552.
    • (1966) Plant Physiol. , vol.41 , pp. 544-552
    • Izawa, S.1    Good, N.E.2
  • 93
    • 0017410242 scopus 로고
    • Electrical diffuse layers and their influence on photosynthetic processes
    • Barber J., Mills J., Love A. Electrical diffuse layers and their influence on photosynthetic processes. FEBS Lett. 1977, 74:174-181.
    • (1977) FEBS Lett. , vol.74 , pp. 174-181
    • Barber, J.1    Mills, J.2    Love, A.3
  • 94
    • 0019317499 scopus 로고
    • The role of membrane surface charge in the control of photosynthetic processes and the involvement of electrostatic screening
    • Rubin B.T., Barber J. The role of membrane surface charge in the control of photosynthetic processes and the involvement of electrostatic screening. Biochim. Biophys. Acta 1980, 592:87-102.
    • (1980) Biochim. Biophys. Acta , vol.592 , pp. 87-102
    • Rubin, B.T.1    Barber, J.2
  • 95
    • 0019325194 scopus 로고
    • The stacking of chloroplast thylakoids. Effects of cation screening and binding, studied by the digitonin method
    • Chow W.S., Thorne S.W., Duniec J.T., Sculley M.J., Boardman N.K. The stacking of chloroplast thylakoids. Effects of cation screening and binding, studied by the digitonin method. Arch. Biochem. Biophys. 1980, 201:347-355.
    • (1980) Arch. Biochem. Biophys. , vol.201 , pp. 347-355
    • Chow, W.S.1    Thorne, S.W.2    Duniec, J.T.3    Sculley, M.J.4    Boardman, N.K.5
  • 96
    • 0019325194 scopus 로고
    • The stacking of chloroplast thylakoids. Quantitative analysis of the balance of forces between thylakoid membranes of chloroplasts, and the role of divalent cations
    • Sculley M.J., Duniec J.T., Thorne S.W., Chow W.S., Boardman N.K. The stacking of chloroplast thylakoids. Quantitative analysis of the balance of forces between thylakoid membranes of chloroplasts, and the role of divalent cations. Arch. Biochem. Biophys. 1980, 201:339-346.
    • (1980) Arch. Biochem. Biophys. , vol.201 , pp. 339-346
    • Sculley, M.J.1    Duniec, J.T.2    Thorne, S.W.3    Chow, W.S.4    Boardman, N.K.5
  • 97
    • 0001299286 scopus 로고
    • Influence of surface charges on thylakoid structure and function
    • Barber J. Influence of surface charges on thylakoid structure and function. Annu. Rev. Plant Physiol. 1982, 33:261-295.
    • (1982) Annu. Rev. Plant Physiol. , vol.33 , pp. 261-295
    • Barber, J.1
  • 98
    • 0024075788 scopus 로고
    • Biogenesis of thylakoid membranes is controlled by light intensity in the conditional chlorophyll b-deficient CD3 mutant of wheat
    • Allen K.D., Duysen M.E., Staehelin L.A. Biogenesis of thylakoid membranes is controlled by light intensity in the conditional chlorophyll b-deficient CD3 mutant of wheat. J. Cell Biol. 1988, 107:907-919.
    • (1988) J. Cell Biol. , vol.107 , pp. 907-919
    • Allen, K.D.1    Duysen, M.E.2    Staehelin, L.A.3
  • 99
    • 0026069088 scopus 로고
    • Surface charges, the heterogeneous lateral distribution of the two photosystems, and thylakoid stacking
    • Chow W.S., Miller C., Anderson J.M. Surface charges, the heterogeneous lateral distribution of the two photosystems, and thylakoid stacking. Biochim. Biophys. Acta 1991, 1057:69-77.
    • (1991) Biochim. Biophys. Acta , vol.1057 , pp. 69-77
    • Chow, W.S.1    Miller, C.2    Anderson, J.M.3
  • 100
    • 84905241632 scopus 로고    scopus 로고
    • Contribution of galactoglycerolipids to the 3-dimensional architecture of thylakoids
    • Demé B., Cataye C., Block M.A., Maréchal E., Jouhet J. Contribution of galactoglycerolipids to the 3-dimensional architecture of thylakoids. FASEB J. 2014, 10.1096/fj.13-247395.
    • (2014) FASEB J.
    • Demé, B.1    Cataye, C.2    Block, M.A.3    Maréchal, E.4    Jouhet, J.5
  • 101
    • 84883194727 scopus 로고    scopus 로고
    • Arabidopsis CURVATURE THYLAKOID1 proteins modify thylakoid architecture by inducing membrane curvature
    • Ambruster U., Labs M., Pribil M., et al. Arabidopsis CURVATURE THYLAKOID1 proteins modify thylakoid architecture by inducing membrane curvature. Plant Cell 2013, 25:2661-2678.
    • (2013) Plant Cell , vol.25 , pp. 2661-2678
    • Ambruster, U.1    Labs, M.2    Pribil, M.3
  • 102
    • 0027359059 scopus 로고
    • Why do thylakoid membranes from higher plants form grana stacks?
    • Trissl H.-W., Wilhelm C. Why do thylakoid membranes from higher plants form grana stacks?. Trends Biochem. Sci. 1993, 18:415-419.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 415-419
    • Trissl, H.-W.1    Wilhelm, C.2
  • 103
    • 84869215601 scopus 로고    scopus 로고
    • Protein kinases and phosphatases involved in the acclimation of the photosynthetic apparatus to a changing light environment
    • Rochaix J.D., Lemeille S., Shapiguzov A., et al. Protein kinases and phosphatases involved in the acclimation of the photosynthetic apparatus to a changing light environment. Philos. Trans. R. Soc. Lond. B: Biol. Sci. 2012, 367:3466-3474.
    • (2012) Philos. Trans. R. Soc. Lond. B: Biol. Sci. , vol.367 , pp. 3466-3474
    • Rochaix, J.D.1    Lemeille, S.2    Shapiguzov, A.3
  • 104
    • 2642556998 scopus 로고    scopus 로고
    • Cyclic electron flow under saturating excitation of dark-adapted Arabidopsis leaves
    • Joliot P., Beal D., Joliot A. Cyclic electron flow under saturating excitation of dark-adapted Arabidopsis leaves. Biochim. Biophys. Acta 2004, 1656:166-176.
    • (2004) Biochim. Biophys. Acta , vol.1656 , pp. 166-176
    • Joliot, P.1    Beal, D.2    Joliot, A.3
  • 105
    • 84883830638 scopus 로고    scopus 로고
    • Complexities and protein complexes in the antimycin A-sensitive pathway of cyclic electron flow in plants
    • Leister D., Shikanai T. Complexities and protein complexes in the antimycin A-sensitive pathway of cyclic electron flow in plants. Front. Plant Sci. 2013, 4:161.
    • (2013) Front. Plant Sci. , vol.4 , pp. 161
    • Leister, D.1    Shikanai, T.2
  • 106
    • 11044234285 scopus 로고    scopus 로고
    • Supramolecular organization of thylakoid membrane proteins in green plants
    • Dekker J.P., Boekema E.J. Supramolecular organization of thylakoid membrane proteins in green plants. Biochim. Biophys. Acta 2005, 1706:12-39.
    • (2005) Biochim. Biophys. Acta , vol.1706 , pp. 12-39
    • Dekker, J.P.1    Boekema, E.J.2
  • 107
    • 0000765807 scopus 로고
    • Role of light in the regulation of chloroplast enzymes
    • Buchanan B.B. Role of light in the regulation of chloroplast enzymes. Annu. Rev. Plant Physiol. 1980, 31:341-374.
    • (1980) Annu. Rev. Plant Physiol. , vol.31 , pp. 341-374
    • Buchanan, B.B.1
  • 108
    • 0018789833 scopus 로고
    • Energy conversion in the functional membranes of photosynthesis analysis by light pulse and electric pulse methods
    • Witt H.T. Energy conversion in the functional membranes of photosynthesis analysis by light pulse and electric pulse methods. Biochim. Biophys. Acta 1979, 505:355-427.
    • (1979) Biochim. Biophys. Acta , vol.505 , pp. 355-427
    • Witt, H.T.1
  • 109
    • 0028191397 scopus 로고
    • Effects of pH on the kinetics of redox reaction in and around the cytochrome bf complex in an isolated system
    • Hope A.B., Valente P., Matthews D.B. Effects of pH on the kinetics of redox reaction in and around the cytochrome bf complex in an isolated system. Photosynth. Res. 1994, 42:111-120.
    • (1994) Photosynth. Res. , vol.42 , pp. 111-120
    • Hope, A.B.1    Valente, P.2    Matthews, D.B.3
  • 110
    • 0032516449 scopus 로고    scopus 로고
    • In vivo characterization of the electrochemical proton gradient generated in darkness in green algae and its kinetic effects on cytochrome b6f turnover
    • Finazzi G., Rappaport F. In vivo characterization of the electrochemical proton gradient generated in darkness in green algae and its kinetic effects on cytochrome b6f turnover. Biochemistry 1998, 37:9999-10005.
    • (1998) Biochemistry , vol.37 , pp. 9999-10005
    • Finazzi, G.1    Rappaport, F.2
  • 111
    • 0014477179 scopus 로고
    • PH changes in the inner phase of the thylakoids during photosynthesis
    • Rumberg B., Siggel U. pH changes in the inner phase of the thylakoids during photosynthesis. Naturwissenschaften 1969, 56:130-132.
    • (1969) Naturwissenschaften , vol.56 , pp. 130-132
    • Rumberg, B.1    Siggel, U.2
  • 112
    • 84981625721 scopus 로고
    • The kinetics of P700 reduction in leaves: A novel in situ probe of thylakoid functioning
    • Harbinson J., Hedley C. The kinetics of P700 reduction in leaves: A novel in situ probe of thylakoid functioning. Plant Cell Environ. 1989, 12:357-369.
    • (1989) Plant Cell Environ. , vol.12 , pp. 357-369
    • Harbinson, J.1    Hedley, C.2
  • 113
    • 0028852953 scopus 로고
    • Coregulation of electron transport through PS I by Cyt b6f, excitation capture by P700 and acceptor side reduction Time kinetics and electron transport requirement
    • Laisk A., Oja V. Coregulation of electron transport through PS I by Cyt b6f, excitation capture by P700 and acceptor side reduction Time kinetics and electron transport requirement. Photosynth. Res. 1995, 45:11-19.
    • (1995) Photosynth. Res. , vol.45 , pp. 11-19
    • Laisk, A.1    Oja, V.2
  • 114
    • 0031855446 scopus 로고    scopus 로고
    • A diffused-optics flash kinetic spectrophometer (DOFS) for measurements of absorbance changes in intact plants in the steady-state
    • Kramer D.M., Sacksteder C.A. A diffused-optics flash kinetic spectrophometer (DOFS) for measurements of absorbance changes in intact plants in the steady-state. Photosynth. Res. 1998, 56:103-112.
    • (1998) Photosynth. Res. , vol.56 , pp. 103-112
    • Kramer, D.M.1    Sacksteder, C.A.2
  • 115
    • 3042804076 scopus 로고    scopus 로고
    • Dynamic flexibility in the light reactions of photosynthesis governed by both electron and proton transfer reactions
    • Kramer D.M., Avenson T.J., Edwards G.E. Dynamic flexibility in the light reactions of photosynthesis governed by both electron and proton transfer reactions. Trends Plant Sci. 2004, 9:349-357.
    • (2004) Trends Plant Sci. , vol.9 , pp. 349-357
    • Kramer, D.M.1    Avenson, T.J.2    Edwards, G.E.3
  • 116
    • 0000746842 scopus 로고
    • The role of calcium in the pH-dependent control of Photosystem II
    • Krieger A., Weis E. The role of calcium in the pH-dependent control of Photosystem II. Photosynth. Res. 1993, 37:117-130.
    • (1993) Photosynth. Res. , vol.37 , pp. 117-130
    • Krieger, A.1    Weis, E.2
  • 117
    • 0031034274 scopus 로고    scopus 로고
    • Low pH accelerates light-induced damage of Photosystem II by enhancing the probability of the donor-side mechanism of photoinhibition
    • Spetea C., Hidge E., Vass I. Low pH accelerates light-induced damage of Photosystem II by enhancing the probability of the donor-side mechanism of photoinhibition. Biochim. Biophys. Acta 1997, 1318:275-283.
    • (1997) Biochim. Biophys. Acta , vol.1318 , pp. 275-283
    • Spetea, C.1    Hidge, E.2    Vass, I.3
  • 120
    • 84860458817 scopus 로고    scopus 로고
    • Identification of key residues for pH dependent activation of violaxanthin de-epoxidase from Arabidopsis thaliana
    • Fufezan C., Simionato D., Morosinotto T. Identification of key residues for pH dependent activation of violaxanthin de-epoxidase from Arabidopsis thaliana. PLoS ONE 2012, 7:e35669.
    • (2012) PLoS ONE , vol.7 , pp. e35669
    • Fufezan, C.1    Simionato, D.2    Morosinotto, T.3
  • 121
    • 34548756762 scopus 로고    scopus 로고
    • The chloroplast Tat pathway utilizes the transmembrane electric potential as an energy source
    • Braun N.A., Davis A.W., Theg S.M. The chloroplast Tat pathway utilizes the transmembrane electric potential as an energy source. Biophys. J. 2007, 93:1993-1998.
    • (2007) Biophys. J. , vol.93 , pp. 1993-1998
    • Braun, N.A.1    Davis, A.W.2    Theg, S.M.3
  • 122
    • 0343851071 scopus 로고    scopus 로고
    • A pigment-binding protein essential for regulation of photosynthetic light harvesting
    • Li X.P., Björkman O., Shih C., et al. A pigment-binding protein essential for regulation of photosynthetic light harvesting. Nature 2000, 403:391-395.
    • (2000) Nature , vol.403 , pp. 391-395
    • Li, X.P.1    Björkman, O.2    Shih, C.3
  • 123
    • 0001675705 scopus 로고
    • + channels in thylakoid membranes by incorporation of vesicles into planar lipid bilayers
    • + channels in thylakoid membranes by incorporation of vesicles into planar lipid bilayers. Plant Physiol. 1989, 91:249-252.
    • (1989) Plant Physiol. , vol.91 , pp. 249-252
    • Tester, M.1    Blatt, M.R.2
  • 124
    • 84863565372 scopus 로고    scopus 로고
    • Thylakoid potassium channel is required for efficient photosynthesis in cyanobacteria
    • Checchetto V., Segalla A., Allorent G., et al. Thylakoid potassium channel is required for efficient photosynthesis in cyanobacteria. Proc. Natl. Acad. Sci. U. S. A. 2012, 109:11043-11048.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 11043-11048
    • Checchetto, V.1    Segalla, A.2    Allorent, G.3
  • 125
    • 0015904985 scopus 로고
    • Alkalization of the chloroplast stroma caused by light-dependent proton flux into the thylakoid space
    • Heldt H.W., Werdan K., Milovancev M., Geller G. Alkalization of the chloroplast stroma caused by light-dependent proton flux into the thylakoid space. Biochim. Biophys. Acta 1973, 314:224-241.
    • (1973) Biochim. Biophys. Acta , vol.314 , pp. 224-241
    • Heldt, H.W.1    Werdan, K.2    Milovancev, M.3    Geller, G.4
  • 126
    • 0000546107 scopus 로고
    • Stromal pH and photosynthesis are affected by electroneutral K and H exchange through chloroplast envelope ion channels
    • Wu W., Berkowitz G.A. Stromal pH and photosynthesis are affected by electroneutral K and H exchange through chloroplast envelope ion channels. Plant Physiol. 1992, 98:666-672.
    • (1992) Plant Physiol. , vol.98 , pp. 666-672
    • Wu, W.1    Berkowitz, G.A.2
  • 127
    • 0036006057 scopus 로고    scopus 로고
    • Ferrous ion transport across chloroplast inner envelope membranes
    • Shingles R., North M., McCarty R.E. Ferrous ion transport across chloroplast inner envelope membranes. Plant Physiol. 2002, 128:1022-1030.
    • (2002) Plant Physiol. , vol.128 , pp. 1022-1030
    • Shingles, R.1    North, M.2    McCarty, R.E.3
  • 128
    • 80052071456 scopus 로고    scopus 로고
    • A plastidial sodium-dependent pyruvate transporter
    • Furumoto T., Yamaguchi T., Ohshima-Ichie Y. A plastidial sodium-dependent pyruvate transporter. Nature 2011, 476:472-475.
    • (2011) Nature , vol.476 , pp. 472-475
    • Furumoto, T.1    Yamaguchi, T.2    Ohshima-Ichie, Y.3
  • 129
    • 0032827410 scopus 로고    scopus 로고
    • Mitochondrial transport of cations: channels, exchangers, and permeability transition
    • Bernardi P. Mitochondrial transport of cations: channels, exchangers, and permeability transition. Physiol. Rev. 1999, 79:1127-1155.
    • (1999) Physiol. Rev. , vol.79 , pp. 1127-1155
    • Bernardi, P.1
  • 131
    • 37149029370 scopus 로고    scopus 로고
    • Calcium signaling
    • Clapham D.E. Calcium signaling. Cell 2007, 131:1047-1058.
    • (2007) Cell , vol.131 , pp. 1047-1058
    • Clapham, D.E.1
  • 132
    • 84867142601 scopus 로고    scopus 로고
    • The role of calcium in chloroplasts-an intriguing and unresolved puzzle
    • Rocha A.G., Vothknecht U.C. The role of calcium in chloroplasts-an intriguing and unresolved puzzle. Protoplasma 2012, 249:957-966.
    • (2012) Protoplasma , vol.249 , pp. 957-966
    • Rocha, A.G.1    Vothknecht, U.C.2
  • 134
    • 1642331709 scopus 로고    scopus 로고
    • Architecture of the photosynthetic oxygen-evolving center
    • Ferreira K.N., Iverson T.M., Maghlaoui K., Barber J., Iwata S. Architecture of the photosynthetic oxygen-evolving center. Science 2004, 303(5665):1831-1838.
    • (2004) Science , vol.303 , Issue.5665 , pp. 1831-1838
    • Ferreira, K.N.1    Iverson, T.M.2    Maghlaoui, K.3    Barber, J.4    Iwata, S.5
  • 135
    • 84857979132 scopus 로고    scopus 로고
    • Crosstalk between calcium signalling and protein phosphorylation at the thylakoid membrane
    • Stael S., Rocha A.G., Wimberger T., Anrather D., Vothknecht U.C., Teige M. Crosstalk between calcium signalling and protein phosphorylation at the thylakoid membrane. J. Exp. Bot. 2011, 63:1725-1733.
    • (2011) J. Exp. Bot. , vol.63 , pp. 1725-1733
    • Stael, S.1    Rocha, A.G.2    Wimberger, T.3    Anrather, D.4    Vothknecht, U.C.5    Teige, M.6
  • 136
    • 13944253668 scopus 로고    scopus 로고
    • Dynamics of photosystem II: a proteomic approach to thylakoid protein complexes
    • Aro E.-M., Suorsa M., Rokka A., et al. Dynamics of photosystem II: a proteomic approach to thylakoid protein complexes. J. Exp. Bot. 2005, 56:347-356.
    • (2005) J. Exp. Bot. , vol.56 , pp. 347-356
    • Aro, E.-M.1    Suorsa, M.2    Rokka, A.3
  • 137
    • 0019331873 scopus 로고
    • Characterization of the plant nicotinamide adenine dinucleotide kinase activator protein and its identification as calmodulin
    • Anderson J.M., Charbonneau H., Jones H.P., McCann R.O., Cormier M.J. Characterization of the plant nicotinamide adenine dinucleotide kinase activator protein and its identification as calmodulin. Biochemistry 1980, 19:3113-3120.
    • (1980) Biochemistry , vol.19 , pp. 3113-3120
    • Anderson, J.M.1    Charbonneau, H.2    Jones, H.P.3    McCann, R.O.4    Cormier, M.J.5
  • 138
    • 84877757886 scopus 로고    scopus 로고
    • Complementary biochemical approaches applied to the identification of plastidial calmodulin-binding proteins
    • Dell'Aglio E., Giustini C., Salvi D., et al. Complementary biochemical approaches applied to the identification of plastidial calmodulin-binding proteins. Mol. Biosyst. 2013, 9:1234-1248.
    • (2013) Mol. Biosyst. , vol.9 , pp. 1234-1248
    • Dell'Aglio, E.1    Giustini, C.2    Salvi, D.3
  • 139
    • 0019325473 scopus 로고
    • Action of calcium ions on spinach (Spinacia oleracea) chloroplast fructose bisphosphatase and other enzymes of the Calvin cycle
    • Charles S.A., Halliwell B. Action of calcium ions on spinach (Spinacia oleracea) chloroplast fructose bisphosphatase and other enzymes of the Calvin cycle. Biochem. J. 1980, 188:775-779.
    • (1980) Biochem. J. , vol.188 , pp. 775-779
    • Charles, S.A.1    Halliwell, B.2
  • 142
    • 10344242448 scopus 로고    scopus 로고
    • New functions of the thylakoid membrane proteome of Arabidopsis thaliana revealed by a simple, fast, and versatile fractionation strategy
    • Peltier J.-B., Ytterberg A.J., Sun Q., van Wijk K.J. New functions of the thylakoid membrane proteome of Arabidopsis thaliana revealed by a simple, fast, and versatile fractionation strategy. J. Biol. Chem. 2004, 279:49367-49383.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49367-49383
    • Peltier, J.-B.1    Ytterberg, A.J.2    Sun, Q.3    van Wijk, K.J.4
  • 144
    • 33845592044 scopus 로고    scopus 로고
    • Mass spectrometric genomic data mining: novel insights into bioenergetic pathways in Chlamydomonas reinhardtii
    • Allmer J., Naumann B., Markert C., Zhang M., Hippler M. Mass spectrometric genomic data mining: novel insights into bioenergetic pathways in Chlamydomonas reinhardtii. Proteomics 2006, 6:6207-6220.
    • (2006) Proteomics , vol.6 , pp. 6207-6220
    • Allmer, J.1    Naumann, B.2    Markert, C.3    Zhang, M.4    Hippler, M.5
  • 145
    • 77952825427 scopus 로고    scopus 로고
    • Characterizing the anaerobic response of Chlamydomonas reinhardtii by quantitative proteomics
    • Terashima M., Specht M., Naumann B., Hippler M. Characterizing the anaerobic response of Chlamydomonas reinhardtii by quantitative proteomics. Mol. Cell. Proteomics 2010, 9:1514-1532.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1514-1532
    • Terashima, M.1    Specht, M.2    Naumann, B.3    Hippler, M.4
  • 146
    • 0028812274 scopus 로고
    • Stimulusinduced oscillations in guard cell cytosolic free calcium
    • McAinsh M.R., Webb A., Taylor J.E., Hetherington A.M. Stimulusinduced oscillations in guard cell cytosolic free calcium. Plant Cell 1995, 7:1207-1219.
    • (1995) Plant Cell , vol.7 , pp. 1207-1219
    • McAinsh, M.R.1    Webb, A.2    Taylor, J.E.3    Hetherington, A.M.4
  • 148
    • 84555177746 scopus 로고    scopus 로고
    • Calcium-sensing receptor regulates stomatal closure through hydrogen peroxide and nitric oxide in response to extracellular calcium in Arabidopsis
    • Wang W.-H., Yi X.-Q., Han A.-D., et al. Calcium-sensing receptor regulates stomatal closure through hydrogen peroxide and nitric oxide in response to extracellular calcium in Arabidopsis. J. Exp. Bot. 2011, 63:177-190.
    • (2011) J. Exp. Bot. , vol.63 , pp. 177-190
    • Wang, W.-H.1    Yi, X.-Q.2    Han, A.-D.3
  • 149
    • 80053200706 scopus 로고    scopus 로고
    • The chloroplast calcium sensor CAS is required for photoacclimation in Chlamydomonas reinhardtii
    • Petroutsos D., Busch A., Janssen I., et al. The chloroplast calcium sensor CAS is required for photoacclimation in Chlamydomonas reinhardtii. Plant Cell 2011, 23:2950-2963.
    • (2011) Plant Cell , vol.23 , pp. 2950-2963
    • Petroutsos, D.1    Busch, A.2    Janssen, I.3
  • 150
    • 84903993543 scopus 로고    scopus 로고
    • Transcriptional regulation of the stress-responsive light harvesting complex genes in Chlamydomonas reinhardtii
    • Maruyama S., Tokutsu R., Minagawa J. Transcriptional regulation of the stress-responsive light harvesting complex genes in Chlamydomonas reinhardtii. Plant Cell Physiol. 2014, 55:1304-1310.
    • (2014) Plant Cell Physiol. , vol.55 , pp. 1304-1310
    • Maruyama, S.1    Tokutsu, R.2    Minagawa, J.3
  • 151
    • 84867914796 scopus 로고    scopus 로고
    • Calcium-dependent regulation of cyclic photosynthetic electron transfer by a CAS ANR1, and PGRL1 complex
    • Terashima M., Petroutsos D., Hüdig M., et al. Calcium-dependent regulation of cyclic photosynthetic electron transfer by a CAS ANR1, and PGRL1 complex. Proc. Natl. Acad. Sci. U. S. A. 2012, 109:17717-17722.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 17717-17722
    • Terashima, M.1    Petroutsos, D.2    Hüdig, M.3
  • 153
    • 41549103343 scopus 로고    scopus 로고
    • Light regulation of CaS, a novel phosphoprotein in the thylakoid membrane of Arabidopsis thaliana
    • Vainonen J.P., Sakuragi Y., Stael S., et al. Light regulation of CaS, a novel phosphoprotein in the thylakoid membrane of Arabidopsis thaliana. FEBS J. 2008, 275:1767-1777.
    • (2008) FEBS J. , vol.275 , pp. 1767-1777
    • Vainonen, J.P.1    Sakuragi, Y.2    Stael, S.3
  • 154
    • 79961220621 scopus 로고    scopus 로고
    • Comparative phosphoproteome profiling reveals a function of the STN8 kinase in fine-tuning of cyclic electron flow (CEF)
    • Reiland S., Finazzi G., Endler A., et al. Comparative phosphoproteome profiling reveals a function of the STN8 kinase in fine-tuning of cyclic electron flow (CEF). Proc. Natl. Acad. Sci. U. S. A. 2011, 108:12955-12960.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 12955-12960
    • Reiland, S.1    Finazzi, G.2    Endler, A.3


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