메뉴 건너뛰기




Volumn 23, Issue 8, 2011, Pages 2950-2963

The chloroplast calcium sensor CAS is required for photoacclimation in Chlamydomonas reinhardtii

Author keywords

[No Author keywords available]

Indexed keywords

CHLAMYDOMONAS REINHARDTII; CHLOROPHYTA; TRACHEOPHYTA;

EID: 80053200706     PISSN: 10404651     EISSN: 1532298X     Source Type: Journal    
DOI: 10.1105/tpc.111.087973     Document Type: Article
Times cited : (127)

References (64)
  • 1
    • 77954627020 scopus 로고    scopus 로고
    • Physcomitrella patens mutants affected on heat dissipation clarify the evolution of photoprotection mechanisms upon land colonization
    • Alboresi, A., Gerotto, C., Giacometti, G.M., Bassi, R., and Morosinotto, T. (2010). Physcomitrella patens mutants affected on heat dissipation clarify the evolution of photoprotection mechanisms upon land colonization. Proc. Natl. Acad. Sci. USA 107: 11128-11133.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 11128-11133
    • Alboresi, A.1    Gerotto, C.2    Giacometti, G.M.3    Bassi, R.4    Morosinotto, T.5
  • 2
    • 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., and Hippler, M. (2006). Mass spectrometric genomic data mining: Novel insights into bioenergetic pathways in Chlamydomonas reinhardtii. Proteomics 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
  • 3
    • 0024453294 scopus 로고
    • Inositol phosphates and cell signalling
    • Berridge, M.J., and Irvine, R.F. (1989). Inositol phosphates and cell signalling. Nature 341: 197-205.
    • (1989) Nature , vol.341 , pp. 197-205
    • Berridge, M.J.1    Irvine, R.F.2
  • 4
    • 57349151754 scopus 로고    scopus 로고
    • Channelrhodopsin-1 initiates phototaxis and photophobic responses in chlamydomonas by immediate lightinduced depolarization
    • Berthold, P., Tsunoda, S.P., Ernst, O.P., Mages, W., Gradmann, D., and Hegemann, P. (2008). Channelrhodopsin-1 initiates phototaxis and photophobic responses in chlamydomonas by immediate lightinduced depolarization. Plant Cell 20: 1665-1677.
    • (2008) Plant Cell , vol.20 , pp. 1665-1677
    • Berthold, P.1    Tsunoda, S.P.2    Ernst, O.P.3    Mages, W.4    Gradmann, D.5    Hegemann, P.6
  • 5
    • 0037077285 scopus 로고    scopus 로고
    • A novel family of calmodulin-binding transcription activators in multicellular organisms
    • Bouché, N., Scharlat, A., Snedden, W., Bouchez, D., and Fromm, H. (2002). A novel family of calmodulin-binding transcription activators in multicellular organisms. J. Biol. Chem. 277: 21851-21861.
    • (2002) J. Biol. Chem , vol.277 , pp. 21851-21861
    • Bouché, N.1    Scharlat, A.2    Snedden, W.3    Bouchez, D.4    Fromm, H.5
  • 6
    • 0025807316 scopus 로고
    • Measuring detection limits in inductively coupled plasma emission spectrometry using the "SBR-RSDB approach"- 1. A tutorial discussion of the theory
    • Boumans, P.W. (1991). Measuring detection limits in inductively coupled plasma emission spectrometry using the "SBR-RSDB approach"- 1. A tutorial discussion of the theory. Spectrochimica Acta 46B: 431-445.
    • (1991) Spectrochimica Acta , vol.46 B , pp. 431-445
    • Boumans, P.W.1
  • 7
    • 33744539625 scopus 로고
    • Measuring detection limits in inductively coupled plasma emission spectrometry-II. Experimental data and their interpretation
    • Boumans, P.W., Ivaldi, J., and Slavin, W. (1991). Measuring detection limits in inductively coupled plasma emission spectrometry-II. Experimental data and their interpretation. Spectrochimica Acta 46B: 641-665.
    • (1991) Spectrochimica Acta , vol.46 B , pp. 641-665
    • Boumans, P.W.1    Ivaldi, J.2    Slavin, W.3
  • 8
    • 0024425920 scopus 로고
    • EPR signals from modified charge accumulation states of the oxygen evolving enzyme in Ca2+-deficient photosystem II
    • Boussac, A., Zimmermann, J.L., and Rutherford, A.W. (1989). EPR signals from modified charge accumulation states of the oxygen evolving enzyme in Ca2+-deficient photosystem II. Biochemistry 28: 8984-8989.
    • (1989) Biochemistry , vol.28 , pp. 8984-8989
    • Boussac, A.1    Zimmermann, J.L.2    Rutherford, A.W.3
  • 9
    • 70450170969 scopus 로고    scopus 로고
    • Calcium regulation in endosymbiotic organelles of plants
    • Bussemer, J., Vothknecht, U.C., and Chigri, F. (2009). Calcium regulation in endosymbiotic organelles of plants. Plant Signal. Behav. 4: 805-808.
    • (2009) Plant Signal. Behav , vol.4 , pp. 805-808
    • Bussemer, J.1    Vothknecht, U.C.2    Chigri, F.3
  • 11
    • 21244451176 scopus 로고    scopus 로고
    • Calcium regulation of chloroplast protein import
    • Chigri, F., Soll, J., and Vothknecht, U.C. (2005). Calcium regulation of chloroplast protein import. Plant J. 42: 821-831.
    • (2005) Plant J , vol.42 , pp. 821-831
    • Chigri, F.1    Soll, J.2    Vothknecht, U.C.3
  • 12
    • 77951869322 scopus 로고    scopus 로고
    • Pcdp1 is a central apparatus protein that binds Ca(2+)-calmodulin and regulates ciliary motility
    • DiPetrillo, C.G., and Smith, E.F. (2010). Pcdp1 is a central apparatus protein that binds Ca(2+)-calmodulin and regulates ciliary motility. J. Cell Biol. 189: 601-612.
    • (2010) J. Cell Biol , vol.189 , pp. 601-612
    • Dipetrillo, C.G.1    Smith, E.F.2
  • 14
    • 66449131193 scopus 로고    scopus 로고
    • Roles for Arabidopsis CAMTA transcription factors in coldregulated gene expression and freezing tolerance
    • Doherty, C.J., Van Buskirk, H.A., Myers, S.J., and Thomashow, M.F. (2009). Roles for Arabidopsis CAMTA transcription factors in coldregulated gene expression and freezing tolerance. Plant Cell 21: 972-984.
    • (2009) Plant Cell , vol.21 , pp. 972-984
    • Doherty, C.J.1    van Buskirk, H.A.2    Myers, S.J.3    Thomashow, M.F.4
  • 15
    • 0032806829 scopus 로고    scopus 로고
    • Identification of a Ca2+/H+ antiport in the plant chloroplast thylakoid membrane
    • Ettinger, W.F., Clear, A.M., Fanning, K.J., and Peck, M.L. (1999). Identification of a Ca2+/H+ antiport in the plant chloroplast thylakoid membrane. Plant Physiol. 119: 1379-1386.
    • (1999) Plant Physiol , vol.119 , pp. 1379-1386
    • Ettinger, W.F.1    Clear, A.M.2    Fanning, K.J.3    Peck, M.L.4
  • 16
    • 1642331709 scopus 로고    scopus 로고
    • Architecture of the photosynthetic oxygen-evolving center
    • Ferreira, K.N., Iverson, T.M., Maghlaoui, K., Barber, J., and Iwata, S. (2004). Architecture of the photosynthetic oxygen-evolving center. Science 303: 1831-1838.
    • (2004) Science , vol.303 , pp. 1831-1838
    • Ferreira, K.N.1    Iverson, T.M.2    Maghlaoui, K.3    Barber, J.4    Iwata, S.5
  • 17
    • 0000981541 scopus 로고
    • Calcium reconstitutes high rates of oxygen evolution in polypeptide depleted photosystem II preparations
    • Ghanotakis, D.F., Babcock, G.T., and Yocum, C.F. (1984). Calcium reconstitutes high rates of oxygen evolution in polypeptide depleted photosystem II preparations. FEBS Lett. 167: 127-130.
    • (1984) FEBS Lett , vol.167 , pp. 127-130
    • Ghanotakis, D.F.1    Babcock, G.T.2    Yocum, C.F.3
  • 18
    • 33745621580 scopus 로고    scopus 로고
    • Nodulation independent of rhizobia induced by a calcium-activated kinase lacking autoinhibition
    • Gleason, C., Chaudhuri, S., Yang, T., Muñoz, A., Poovaiah, B.W., and Oldroyd, G.E. (2006). Nodulation independent of rhizobia induced by a calcium-activated kinase lacking autoinhibition. Nature 441: 1149-1152.
    • (2006) Nature , vol.441 , pp. 1149-1152
    • Gleason, C.1    Chaudhuri, S.2    Yang, T.3    Muñoz, A.4    Poovaiah, B.W.5    Oldroyd, G.E.6
  • 19
    • 0141496283 scopus 로고    scopus 로고
    • A cell surface receptor mediates extracellular Ca(2+) sensing in guard cells
    • Han, S., Tang, R., Anderson, L.K., Woerner, T.E., and Pei, Z.M. (2003). A cell surface receptor mediates extracellular Ca(2+) sensing in guard cells. Nature 425: 196-200.
    • (2003) Nature , vol.425 , pp. 196-200
    • Han, S.1    Tang, R.2    Anderson, L.K.3    Woerner, T.E.4    Pei, Z.M.5
  • 21
    • 0343374101 scopus 로고
    • N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide, a calmodulin antagonist, inhibits cell proliferation
    • Hidaka, H., Sasaki, Y., Tanaka, T., Endo, T., Ohno, S., Fujii, Y., and Nagata, T. (1981). N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide, a calmodulin antagonist, inhibits cell proliferation. Proc. Natl. Acad. Sci. USA 78: 4354-4357.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4354-4357
    • Hidaka, H.1    Sasaki, Y.2    Tanaka, T.3    Endo, T.4    Ohno, S.5    Fujii, Y.6    Nagata, T.7
  • 22
    • 0025193034 scopus 로고
    • Regulation of Gi and Go by mastoparan, related amphiphilic peptides, and hydrophobic amines. Mechanism and structural determinants of activity
    • Higashijima, T., Burnier, J., and Ross, E.M. (1990). Regulation of Gi and Go by mastoparan, related amphiphilic peptides, and hydrophobic amines. Mechanism and structural determinants of activity. J. Biol. Chem. 265: 14176-14186.
    • (1990) J. Biol. Chem , vol.265 , pp. 14176-14186
    • Higashijima, T.1    Burnier, J.2    Ross, E.M.3
  • 23
    • 0035543903 scopus 로고    scopus 로고
    • Towards functional proteomics of membrane protein complexes: Analysis of thylakoid membranes from Chlamydomonas reinhardtii
    • Hippler, M., Klein, J., Fink, A., Allinger, T., and Hoerth, P. (2001). Towards functional proteomics of membrane protein complexes: Analysis of thylakoid membranes from Chlamydomonas reinhardtii. Plant J. 28: 595-606.
    • (2001) Plant J , vol.28 , pp. 595-606
    • Hippler, M.1    Klein, J.2    Fink, A.3    Allinger, T.4    Hoerth, P.5
  • 24
    • 33750989900 scopus 로고    scopus 로고
    • Rapid transcriptome changes induced by cytosolic Ca2+ transients reveal ABRE-related sequences as Ca2 +-responsive cis-elements in Arabidopsis
    • Kaplan, B., Davydov, O., Knight, H., Galon, Y., Knight, M.R., Fluhr, R., and Fromm, H. (2006). Rapid transcriptome changes induced by cytosolic Ca2+ transients reveal ABRE-related sequences as Ca2 +-responsive cis-elements in Arabidopsis. Plant Cell 18: 2733-2748.
    • (2006) Plant Cell , vol.18 , pp. 2733-2748
    • Kaplan, B.1    Davydov, O.2    Knight, H.3    Galon, Y.4    Knight, M.R.5    Fluhr, R.6    Fromm, H.7
  • 25
    • 0024791910 scopus 로고
    • Stable nuclear transformation of Chlamydomonas using the Chlamydomonas gene for nitrate reductase
    • Kindle, K.L., Schnell, R.A., Fernández, E., and Lefebvre, P.A. (1989). Stable nuclear transformation of Chlamydomonas using the Chlamydomonas gene for nitrate reductase. J. Cell Biol. 109: 2589-2601.
    • (1989) J. Cell Biol , vol.109 , pp. 2589-2601
    • Kindle, K.L.1    Schnell, R.A.2    Fernández, E.3    Lefebvre, P.A.4
  • 26
    • 0027442393 scopus 로고
    • Low-Ph-induced Ca2+ ion release in the water-splitting system is accompanied by a shift in the midpoint redox potential of the primary quinone acceptor-Q(a)
    • Krieger, A., Weis, E., and Demeter, S. (1993). Low-Ph-induced Ca2+ ion release in the water-splitting system is accompanied by a shift in the midpoint redox potential of the primary quinone acceptor-Q(a). Biochim. Biophys. Acta 1144: 411-418.
    • (1993) Biochim. Biophys. Acta , vol.1144 , pp. 411-418
    • Krieger, A.1    Weis, E.2    Demeter, S.3
  • 27
    • 0024965007 scopus 로고
    • Mutation at the Chlamydomonas nuclear NAC2 locus specifically affects stability of the chloroplast psbD transcript encoding polypeptide D2 of PS II
    • Kuchka, M.R., Goldschmidt-Clermont, M., van Dillewijn, J., and Rochaix, J.D. (1989). Mutation at the Chlamydomonas nuclear NAC2 locus specifically affects stability of the chloroplast psbD transcript encoding polypeptide D2 of PS II. Cell 58: 869-876.
    • (1989) Cell , vol.58 , pp. 869-876
    • Kuchka, M.R.1    Goldschmidt-Clermont, M.2    van Dillewijn, J.3    Rochaix, J.D.4
  • 28
    • 77953184082 scopus 로고    scopus 로고
    • Calcium signals: The lead currency of plant information processing
    • Kudla, J., Batistic, O., and Hashimoto, K. (2010). Calcium signals: The lead currency of plant information processing. Plant Cell 22: 541-563.
    • (2010) Plant Cell , vol.22 , pp. 541-563
    • Kudla, J.1    Batistic, O.2    Hashimoto, K.3
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0343851071 scopus 로고    scopus 로고
    • A pigment-binding protein essential for regulation of photosynthetic light harvesting
    • Li, X.P., Björkman, O., Shih, C., Grossman, A.R., Rosenquist, M., Jansson, S., and Niyogi, K.K. (2000). A pigment-binding protein essential for regulation of photosynthetic light harvesting. Nature 403: 391-395.
    • (2000) Nature , vol.403 , pp. 391-395
    • Li, X.P.1    Björkman, O.2    Shih, C.3    Grossman, A.R.4    Rosenquist, M.5    Jansson, S.6    Niyogi, K.K.7
  • 32
    • 57649171349 scopus 로고    scopus 로고
    • Shaping the calcium signature
    • McAinsh, M.R., and Pittman, J.K. (2009). Shaping the calcium signature. New Phytol. 181: 275-294.
    • (2009) New Phytol , vol.181 , pp. 275-294
    • McAinsh, M.R.1    Pittman, J.K.2
  • 33
    • 63349090914 scopus 로고    scopus 로고
    • Highly specific gene silencing by artificial microRNAs in the unicellular alga Chlamydomonas reinhardtii
    • Molnar, A., Bassett, A., Thuenemann, E., Schwach, F., Karkare, S., Ossowski, S., Weigel, D., and Baulcombe, D. (2009). Highly specific gene silencing by artificial microRNAs in the unicellular alga Chlamydomonas reinhardtii. Plant J. 58: 165-174.
    • (2009) Plant J , vol.58 , pp. 165-174
    • Molnar, A.1    Bassett, A.2    Thuenemann, E.3    Schwach, F.4    Karkare, S.5    Ossowski, S.6    Weigel, D.7    Baulcombe, D.8
  • 36
    • 58249110509 scopus 로고    scopus 로고
    • Agriculture and the new challenges for photosynthesis research
    • Murchie, E.H., Pinto, M., and Horton, P. (2009). Agriculture and the new challenges for photosynthesis research. New Phytol. 181: 532-552.
    • (2009) New Phytol , vol.181 , pp. 532-552
    • Murchie, E.H.1    Pinto, M.2    Horton, P.3
  • 38
    • 36048942406 scopus 로고    scopus 로고
    • Comparative quantitative proteomics to investigate the remodeling of bioenergetic pathways under iron deficiency in Chlamydomonas reinhardtii
    • Naumann, B., Busch, A., Allmer, J., Ostendorf, E., Zeller, M., Kirchhoff, H., and Hippler, M. (2007). Comparative quantitative proteomics to investigate the remodeling of bioenergetic pathways under iron deficiency in Chlamydomonas reinhardtii. Proteomics 7: 3964-3979.
    • (2007) Proteomics , vol.7 , pp. 3964-3979
    • Naumann, B.1    Busch, A.2    Allmer, J.3    Ostendorf, E.4    Zeller, M.5    Kirchhoff, H.6    Hippler, M.7
  • 39
    • 20144382680 scopus 로고    scopus 로고
    • N-terminal processing of Lhca3 is a key step in remodeling of the photosystem I-light-harvesting complex under iron deficiency in Chlamydomonas reinhardtii
    • Naumann, B., Stauber, E.J., Busch, A., Sommer, F., and Hippler, M. (2005). N-terminal processing of Lhca3 is a key step in remodeling of the photosystem I-light-harvesting complex under iron deficiency in Chlamydomonas reinhardtii. J. Biol. Chem. 280: 20431-20441.
    • (2005) J. Biol. Chem , vol.280 , pp. 20431-20441
    • Naumann, B.1    Stauber, E.J.2    Busch, A.3    Sommer, F.4    Hippler, M.5
  • 40
    • 2642672010 scopus 로고    scopus 로고
    • Chlamydomonas xanthophyll cycle mutants identified by video imaging of chlorophyll fluorescence quenching
    • Niyogi, K.K., Bjorkman, O., and Grossman, A.R. (1997). Chlamydomonas xanthophyll cycle mutants identified by video imaging of chlorophyll fluorescence quenching. Plant Cell 9: 1369-1380.
    • (1997) Plant Cell , vol.9 , pp. 1369-1380
    • Niyogi, K.K.1    Bjorkman, O.2    Grossman, A.R.3
  • 41
    • 40549107148 scopus 로고    scopus 로고
    • Evidence for chloroplast control of external Ca2+-induced cytosolic Ca2+ transients and stomatal closure
    • Nomura, H., Komori, T., Kobori, M., Nakahira, Y., and Shiina, T. (2008). Evidence for chloroplast control of external Ca2+-induced cytosolic Ca2+ transients and stomatal closure. Plant J. 53: 988-998.
    • (2008) Plant J , vol.53 , pp. 988-998
    • Nomura, H.1    Komori, T.2    Kobori, M.3    Nakahira, Y.4    Shiina, T.5
  • 42
    • 38949151063 scopus 로고    scopus 로고
    • Gene silencing in plants using artificial microRNAs and other small RNAs
    • Ossowski, S., Schwab, R., and Weigel, D. (2008). Gene silencing in plants using artificial microRNAs and other small RNAs. Plant J. 53: 674-690.
    • (2008) Plant J , vol.53 , pp. 674-690
    • Ossowski, S.1    Schwab, R.2    Weigel, D.3
  • 43
    • 3343025478 scopus 로고    scopus 로고
    • Flagellar radial spokes contain a Ca2+-stimulated nucleoside diphosphate kinase
    • Patel-King, R.S., Gorbatyuk, O., Takebe, S., and King, S.M. (2004). Flagellar radial spokes contain a Ca2+-stimulated nucleoside diphosphate kinase. Mol. Biol. Cell 15: 3891-3902.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3891-3902
    • Patel-King, R.S.1    Gorbatyuk, O.2    Takebe, S.3    King, S.M.4
  • 45
    • 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., and van Wijk, K.J. (2004). New functions of the thylakoid membrane proteome of Arabidopsis thaliana revealed by a simple, fast, and versatile fractionation strategy. J. Biol. Chem. 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
  • 46
    • 0026537581 scopus 로고
    • Inositol phospholipid metabolism may trigger flagellar excision in Chlamydomonas reinhardtii
    • Quarmby, L.M., Yueh, Y.G., Cheshire, J.L., Keller, L.R., Snell, W.J., and Crain, R.C. (1992). Inositol phospholipid metabolism may trigger flagellar excision in Chlamydomonas reinhardtii. J.CellBiol. 116: 737-744.
    • (1992) J.CellBiol , vol.116 , pp. 737-744
    • Quarmby, L.M.1    Yueh, Y.G.2    Cheshire, J.L.3    Keller, L.R.4    Snell, W.J.5    Crain, R.C.6
  • 47
    • 0032472375 scopus 로고    scopus 로고
    • A systematic survey of conserved histidines in the core subunits of Photosystem I by sitedirected mutagenesis reveals the likely axial ligands of P700
    • Redding, K., MacMillan, F., Leibl, W., Brettel, K., Hanley, J., Rutherford, A.W., Breton, J., and Rochaix, J.D. (1998). A systematic survey of conserved histidines in the core subunits of Photosystem I by sitedirected mutagenesis reveals the likely axial ligands of P700. EMBO J. 17: 50-60.
    • (1998) EMBO J , vol.17 , pp. 50-60
    • Redding, K.1    Macmillan, F.2    Leibl, W.3    Brettel, K.4    Hanley, J.5    Rutherford, A.W.6    Breton, J.7    Rochaix, J.D.8
  • 48
    • 0001226199 scopus 로고    scopus 로고
    • Direct measurement of calcium transport across chloroplast innerenvelope vesicles
    • Roh, M.H., Shingles, R., Cleveland, M.J., and McCarty, R.E. (1998). Direct measurement of calcium transport across chloroplast innerenvelope vesicles. Plant Physiol. 118: 1447-1454.
    • (1998) Plant Physiol , vol.118 , pp. 1447-1454
    • Roh, M.H.1    Shingles, R.2    Cleveland, M.J.3    McCarty, R.E.4
  • 49
    • 8444222059 scopus 로고    scopus 로고
    • Tandem inverted repeat system for selection of effective transgenic RNAi strains in Chlamydomonas
    • Rohr, J., Sarkar, N., Balenger, S., Jeong, B.R., and Cerutti, H. (2004). Tandem inverted repeat system for selection of effective transgenic RNAi strains in Chlamydomonas. Plant J. 40: 611-621.
    • (2004) Plant J , vol.40 , pp. 611-621
    • Rohr, J.1    Sarkar, N.2    Balenger, S.3    Jeong, B.R.4    Cerutti, H.5
  • 50
    • 0035983843 scopus 로고    scopus 로고
    • Dark-stimulated calcium ion fluxes in the chloroplast stroma and cytosol
    • Sai, J., and Johnson, C.H. (2002). Dark-stimulated calcium ion fluxes in the chloroplast stroma and cytosol. Plant Cell 14: 1279-1291.
    • (2002) Plant Cell , vol.14 , pp. 1279-1291
    • Sai, J.1    Johnson, C.H.2
  • 51
    • 77956182394 scopus 로고    scopus 로고
    • An inducible artificial microRNA system for Chlamydomonas reinhardtii confirms a key role for heat shock factor 1 in regulating thermotolerance
    • Schmollinger, S., Strenkert, D., and Schroda, M. (2010). An inducible artificial microRNA system for Chlamydomonas reinhardtii confirms a key role for heat shock factor 1 in regulating thermotolerance. Curr. Genet. 56: 383-389.
    • (2010) Curr. Genet , vol.56 , pp. 383-389
    • Schmollinger, S.1    Strenkert, D.2    Schroda, M.3
  • 53
    • 65549119270 scopus 로고    scopus 로고
    • The use of ESI-MS to probe the binding of divalent cations to calmodulin
    • Shirran, S.L., and Barran, P.E. (2009). The use of ESI-MS to probe the binding of divalent cations to calmodulin. J. Am. Soc. Mass Spectrom. 20: 1159-1171.
    • (2009) J. Am. Soc. Mass Spectrom , vol.20 , pp. 1159-1171
    • Shirran, S.L.1    Barran, P.E.2
  • 54
    • 0036732941 scopus 로고    scopus 로고
    • Regulation of flagellar dynein by calcium and a role for an axonemal calmodulin and calmodulin-dependent kinase
    • Smith, E.F. (2002). Regulation of flagellar dynein by calcium and a role for an axonemal calmodulin and calmodulin-dependent kinase. Mol. Biol. Cell 13: 3303-3313.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3303-3313
    • Smith, E.F.1
  • 55
    • 34548235325 scopus 로고    scopus 로고
    • Expression, assembly and auxiliary functions of photosystem II oxygen-evolving proteins in higher plants
    • Suorsa, M., and Aro, E.M. (2007). Expression, assembly and auxiliary functions of photosystem II oxygen-evolving proteins in higher plants. Photosynth. Res. 93: 89-100.
    • (2007) Photosynth. Res , vol.93 , pp. 89-100
    • Suorsa, M.1    Aro, E.M.2
  • 56
    • 77952825427 scopus 로고    scopus 로고
    • Characterizing the anaerobic response of Chlamydomonas reinhardtii by quantitative proteomics
    • Terashima, M., Specht, M., Naumann, B., and Hippler, M. (2010). Characterizing the anaerobic response of Chlamydomonas reinhardtii by quantitative proteomics. Mol. Cell. Proteomics 9: 1514-1532.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1514-1532
    • Terashima, M.1    Specht, M.2    Naumann, B.3    Hippler, M.4
  • 57
    • 0029064203 scopus 로고
    • Targeted disruption of mouse EGF receptor: Effect of genetic background on mutant phenotype
    • Threadgill, D.W., et al. (1995). Targeted disruption of mouse EGF receptor: Effect of genetic background on mutant phenotype. Science 269: 230-234.
    • (1995) Science , vol.269 , pp. 230-234
    • Threadgill, D.W.1
  • 58
    • 33646684841 scopus 로고    scopus 로고
    • Deregulation of a Ca2+/calmodulin-dependent kinase leads to spontaneous nodule development
    • Tirichine, L., et al. (2006). Deregulation of a Ca2+/calmodulin-dependent kinase leads to spontaneous nodule development. Nature 441: 1153-1156.
    • (2006) Nature , vol.441 , pp. 1153-1156
    • Tirichine, L.1
  • 59
    • 34547679867 scopus 로고    scopus 로고
    • Inhibitors in the functional dissection of the photosynthetic electron transport system
    • Trebst, A. (2007). Inhibitors in the functional dissection of the photosynthetic electron transport system. Photosynth. Res. 92: 217-224.
    • (2007) Photosynth. Res , vol.92 , pp. 217-224
    • Trebst, A.1
  • 62
    • 50349089617 scopus 로고    scopus 로고
    • Ca2+ signalling in plants and green algae-Changing channels
    • Wheeler, G.L., and Brownlee, C. (2008). Ca2+ signalling in plants and green algae-Changing channels. Trends Plant Sci. 13: 506-514.
    • (2008) Trends Plant Sci , vol.13 , pp. 506-514
    • Wheeler, G.L.1    Brownlee, C.2
  • 63
    • 38649120238 scopus 로고    scopus 로고
    • Rapid spatiotemporal patterning of cytosolic Ca2+ underlies flagellar excision in Chlamydomonas reinhardtii
    • Wheeler, G.L., Joint, I., and Brownlee, C. (2008). Rapid spatiotemporal patterning of cytosolic Ca2+ underlies flagellar excision in Chlamydomonas reinhardtii. Plant J. 53: 401-413.
    • (2008) Plant J , vol.53 , pp. 401-413
    • Wheeler, G.L.1    Joint, I.2    Brownlee, C.3
  • 64
    • 33748751106 scopus 로고    scopus 로고
    • The PsbQ protein is required in Arabidopsis for photosystem II assembly/stability and photoautotrophy under low light conditions
    • Yi, X., Hargett, S.R., Frankel, L.K., and Bricker, T.M. (2006). The PsbQ protein is required in Arabidopsis for photosystem II assembly/stability and photoautotrophy under low light conditions. J. Biol. Chem. 281: 26260-26267.
    • (2006) J. Biol. Chem , vol.281 , pp. 26260-26267
    • Yi, X.1    Hargett, S.R.2    Frankel, L.K.3    Bricker, T.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.