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Volumn 17, Issue , 2010, Pages 17-54

Calcium: Not just another ion

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EID: 79960035204     PISSN: 18611370     EISSN: 18611362     Source Type: Book Series    
DOI: 10.1007/978-3-642-10613-2_2     Document Type: Article
Times cited : (24)

References (315)
  • 3
    • 0025129252 scopus 로고
    • 2+ channels in isolated red beet root vacuole membrane by inositol 1, 4, 5-trisphosphate
    • 2+ channels in isolated red beet root vacuole membrane by inositol 1, 4, 5-trisphosphate. Nature 343:567-570
    • (1990) Nature , vol.343 , pp. 567-570
    • Alexandre, J.1
  • 4
    • 29344449722 scopus 로고    scopus 로고
    • Expression of plant cyclic nucleotide-gated cation channels in yeast
    • Ali R, Zielinski RE, Berkowitz GA (2006) Expression of plant cyclic nucleotide-gated cation channels in yeast. J Exp Bot 57:125-138
    • (2006) J Exp Bot , vol.57 , pp. 125-138
    • Ali, R.1    Zielinski, R.E.2    Berkowitz, G.A.3
  • 5
    • 34250741057 scopus 로고    scopus 로고
    • Death don't have no mercy and neither does calcium: Arabidopsis CYCLIC NUCLEOTIDE GATED CHANNEL2 and innate immunity
    • Ali R, Ma W, Lemtiri-Chlieh F, Tsaltas D, Leng Q, von Bodman S, Berkowitz GA (2007) Death don't have no mercy and neither does calcium: Arabidopsis CYCLIC NUCLEOTIDE GATED CHANNEL2 and innate immunity. Plant Cell 19:1081-1095
    • (2007) Plant Cell , vol.19 , pp. 1081-1095
    • Ali, R.1    Ma, W.2    Lemtiri-Chlieh, F.3    Tsaltas, D.4    Leng, Q.5    von Bodman, S.6    Berkowitz, G.A.7
  • 6
    • 0028056889 scopus 로고
    • Two Voltage-Gated, Calcium Release Channels Coreside in the Vacuolar Membrane of Broad Bean Guard Cells
    • Allen GJ, Sanders D (1994) Two Voltage-Gated, Calcium Release Channels Coreside in the Vacuolar Membrane of Broad Bean Guard Cells. Plant Cell 6:685-694
    • (1994) Plant Cell , vol.6 , pp. 685-694
    • Allen, G.J.1    Sanders, D.2
  • 7
    • 0028989065 scopus 로고
    • 2+ from individual plant vacuoles by both InsP3 and cyclic ADP-ribose
    • 2+ from individual plant vacuoles by both InsP3 and cyclic ADP-ribose. Science 268:735-737
    • (1995) Science , vol.268 , pp. 735-737
    • Allen, G.J.1    Muir, S.R.2    Sanders, D.3
  • 12
    • 0001401761 scopus 로고
    • Involvement of Plasma Membrane Calcium Influx in Bacterial Induction of the K/H and Hypersensitive Responses in Tobacco
    • Atkinson MM, Keppler LD, Orlandi EW, Baker CJ, Mischke CF (1990) Involvement of Plasma Membrane Calcium Influx in Bacterial Induction of the K/H and Hypersensitive Responses in Tobacco. Plant Physiol 92:215-221
    • (1990) Plant Physiol , vol.92 , pp. 215-221
    • Atkinson, M.M.1    Keppler, L.D.2    Orlandi, E.W.3    Baker, C.J.4    Mischke, C.F.5
  • 13
    • 0037327025 scopus 로고    scopus 로고
    • HLM1, an essential signaling component in the hypersensitive response, is a member of the cyclic nucleotide-gated channel ion channel family
    • Balague C, Lin B, Alcon C, Flottes G, Malmstrom S, Kohler C, Neuhaus G, Pelletier G, Gaymard F, Roby D (2003) HLM1, an essential signaling component in the hypersensitive response, is a member of the cyclic nucleotide-gated channel ion channel family. Plant Cell 15:365-379
    • (2003) Plant Cell , vol.15 , pp. 365-379
    • Balague, C.1    Lin, B.2    Alcon, C.3    Flottes, G.4    Malmstrom, S.5    Kohler, C.6    Neuhaus, G.7    Pelletier, G.8    Gaymard, F.9    Roby, D.10
  • 14
    • 7044226261 scopus 로고    scopus 로고
    • Integration and channeling of calcium signaling through the CBL calcium sensor/CIPK protein kinase network
    • Batistic O, Kudla J (2004) Integration and channeling of calcium signaling through the CBL calcium sensor/CIPK protein kinase network. Planta 219:915-924
    • (2004) Planta , vol.219 , pp. 915-924
    • Batistic, O.1    Kudla, J.2
  • 15
    • 67349229820 scopus 로고    scopus 로고
    • Plant calcineurin B-like proteins and their interacting protein kinases
    • Batistic O, Kudla J (2009) Plant calcineurin B-like proteins and their interacting protein kinases. Biochim Biophys Acta 1793:985-992
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 985-992
    • Batistic, O.1    Kudla, J.2
  • 17
    • 73849141867 scopus 로고    scopus 로고
    • CBL-mediated targeting of CIPKs facilitates the decoding of calcium signals emanating from distinct cellular stores
    • doi: 10.1111/j.1365-1313X.2009.04045.x
    • Batistic O, Waadt R, Steinhorst L, Held K, Kudla J (2009) CBL-mediated targeting of CIPKs facilitates the decoding of calcium signals emanating from distinct cellular stores. Plant J, doi: 10.1111/j.1365-1313X.2009.04045.x
    • (2009) Plant J
    • Batistic, O.1    Waadt, R.2    Steinhorst, L.3    Held, K.4    Kudla, J.5
  • 20
    • 33751032385 scopus 로고    scopus 로고
    • Calcium microdomains: Organization and function
    • Berridge MJ (2006) Calcium microdomains: organization and function. Cell Calcium 40:405-412
    • (2006) Cell Calcium , vol.40 , pp. 405-412
    • Berridge, M.J.1
  • 22
    • 0033827628 scopus 로고    scopus 로고
    • Receptor-mediated increase in cytoplasmic free calcium required for activation of pathogen defense in parsley
    • Blume B, Nurnberger T, Nass N, Scheel D (2000) Receptor-mediated increase in cytoplasmic free calcium required for activation of pathogen defense in parsley. Plant Cell 12:1425-1440
    • (2000) Plant Cell , vol.12 , pp. 1425-1440
    • Blume, B.1    Nurnberger, T.2    Nass, N.3    Scheel, D.4
  • 23
    • 0033841214 scopus 로고    scopus 로고
    • At ACA8 encodes a plasma membrane-localized calcium-ATPase of Arabidopsis with a calmodulinbinding domain at the N terminus
    • Bonza MC, Morandini P, Luoni L, Geisler M, Palmgren MG, De Michelis MI (2000) At ACA8 encodes a plasma membrane-localized calcium-ATPase of Arabidopsis with a calmodulinbinding domain at the N terminus. Plant Physiol 123:1495-1506
    • (2000) Plant Physiol , vol.123 , pp. 1495-1506
    • Bonza, M.C.1    Morandini, P.2    Luoni, L.3    Geisler, M.4    Palmgren, M.G.5    de Michelis, M.I.6
  • 25
    • 0034506541 scopus 로고    scopus 로고
    • Arabidopsis mutants resistant to S(+)-beta-methyl-alpha, beta-diaminopropionic acid, a cycadderived glutamate receptor agonist
    • Brenner ED, Martinez-Barboza N, Clark AP, Liang QS, Stevenson DW, Coruzzi GM (2000) Arabidopsis mutants resistant to S(+)-beta-methyl-alpha, beta-diaminopropionic acid, a cycadderived glutamate receptor agonist. Plant Physiol 124:1615-1624
    • (2000) Plant Physiol , vol.124 , pp. 1615-1624
    • Brenner, E.D.1    Martinez-Barboza, N.2    Clark, A.P.3    Liang, Q.S.4    Stevenson, D.W.5    Coruzzi, G.M.6
  • 26
    • 0003506909 scopus 로고    scopus 로고
    • Physiology and biochemistry of plant cell walls
    • Chapman & Hall, London
    • Brett C, Waldron K (1996) Physiology and biochemistry of plant cell walls, second editionth edn. Chapman & Hall, London
    • (1996) Second Editionth Edn
    • Brett, C.1    Waldron, K.2
  • 29
    • 0002424966 scopus 로고
    • Regulation of cytosolic calcium in plants
    • Bush DS (1993) Regulation of cytosolic calcium in plants. Plant Physiol 103:7-13
    • (1993) Plant Physiol , vol.103 , pp. 7-13
    • Bush, D.S.1
  • 30
    • 0006203382 scopus 로고    scopus 로고
    • Effects of gibberellic acid and environmental factors on cytosloic calcium in wheat aleurone cells
    • Bush DS (1996) Effects of gibberellic acid and environmental factors on cytosloic calcium in wheat aleurone cells. Planta 199:89-99
    • (1996) Planta , vol.199 , pp. 89-99
    • Bush, D.S.1
  • 32
    • 0024971705 scopus 로고
    • The calcium requirement for stability and enzymatic activity of two isoforms of barley aleurone alpha-amylase
    • Bush DS, Sticher L, van Huystee R, Wagner D, Jones RL (1989b) The calcium requirement for stability and enzymatic activity of two isoforms of barley aleurone alpha-amylase. J Biol Chem 264:19392-19398
    • (1989) J Biol Chem , vol.264 , pp. 19392-19398
    • Bush, D.S.1    Sticher, L.2    van Huystee, R.3    Wagner, D.4    Jones, R.L.5
  • 33
    • 0001428133 scopus 로고
    • 2+ transport in the endomembrane system of the barley aleurone
    • 2+ transport in the endomembrane system of the barley aleurone. Planta 189:507-515
    • (1993) Planta , vol.189 , pp. 507-515
    • Bush, D.S.1    Biswas, A.K.2    Jones, R.L.3
  • 34
    • 84982066482 scopus 로고
    • Die Entwicklung von Calcium-Mangelsymptomen
    • Bussler W (1962) Die Entwicklung von Calcium-Mangelsymptomen. Z Pflanzenernahr Dung Bodenkde 100:53-58
    • (1962) Z Pflanzenernahr Dung Bodenkde , vol.100 , pp. 53-58
    • Bussler, W.1
  • 35
    • 0017929402 scopus 로고
    • Mitochondria and the control of intracellular calcium
    • Bygrave FL (1978) Mitochondria and the control of intracellular calcium. Biol Rev Camb Philos Soc 53:43-79
    • (1978) Biol Rev Camb Philos Soc , vol.53 , pp. 43-79
    • Bygrave, F.L.1
  • 39
    • 0038797073 scopus 로고    scopus 로고
    • A cyclic nucleotide-gated ion channel, CNGC2, is crucial for plant development and adaptation to calcium stress
    • Chan CW, Schorrak LM, Smith RK, Bent AF, Sussman MR (2003) A cyclic nucleotide-gated ion channel, CNGC2, is crucial for plant development and adaptation to calcium stress. Plant Physiol 132:728-731
    • (2003) Plant Physiol , vol.132 , pp. 728-731
    • Chan, C.W.1    Schorrak, L.M.2    Smith, R.K.3    Bent, A.F.4    Sussman, M.R.5
  • 40
    • 62549165187 scopus 로고    scopus 로고
    • Lotus japonicus CASTOR and POLLUX Are Ion Channels Essential for Perinuclear Calcium Spiking in Legume Root Endosymbiosis
    • Charpentier M, Bredemeier R, Wanner G, Takeda N, Schleiff E, Parniske M (2008) Lotus japonicus CASTOR and POLLUX Are Ion Channels Essential for Perinuclear Calcium Spiking in Legume Root Endosymbiosis. Plant Cell 20:3467-3479
    • (2008) Plant Cell , vol.20 , pp. 3467-3479
    • Charpentier, M.1    Bredemeier, R.2    Wanner, G.3    Takeda, N.4    Schleiff, E.5    Parniske, M.6
  • 41
    • 0031105943 scopus 로고    scopus 로고
    • 2+ in the gibberellin-dependent signaling pathway in aleurone cells
    • 2+ in the gibberellin-dependent signaling pathway in aleurone cells. Plant J 11:363-371
    • (1997) Plant J , vol.11 , pp. 363-371
    • Chen, X.1    Chang, M.2    Wang, B.3    Wu, B.4
  • 42
    • 0037458588 scopus 로고    scopus 로고
    • Cloning and characterization of CXIP1, a novel PICOT domaincontaining Arabidopsis protein that associates with CAX1
    • Cheng NH, Hirschi KD (2003) Cloning and characterization of CXIP1, a novel PICOT domaincontaining Arabidopsis protein that associates with CAX1. J Biol Chem 278:6503-6509
    • (2003) J Biol Chem , vol.278 , pp. 6503-6509
    • Cheng, N.H.1    Hirschi, K.D.2
  • 44
    • 0035983609 scopus 로고    scopus 로고
    • Calcium signaling through protein kinases. The Arabidopsis calcium-dependent protein kinase gene family
    • Cheng SH, Willmann MR, Chen HC, Sheen J (2002b) Calcium signaling through protein kinases. The Arabidopsis calcium-dependent protein kinase gene family. Plant Physiol 129:469-485
    • (2002) Plant Physiol , vol.129 , pp. 469-485
    • Cheng, S.H.1    Willmann, M.R.2    Chen, H.C.3    Sheen, J.4
  • 45
    • 0037329942 scopus 로고    scopus 로고
    • The Arabidopsis cax1 mutant exhibits impaired ion homeostasis, development, and hormonal responses and reveals interplay among vacuolar transporters
    • Cheng NH, Pittman JK, Barkla BJ, Shigaki T, Hirschi KD (2003) The Arabidopsis cax1 mutant exhibits impaired ion homeostasis, development, and hormonal responses and reveals interplay among vacuolar transporters. Plant Cell 15:347-364
    • (2003) Plant Cell , vol.15 , pp. 347-364
    • Cheng, N.H.1    Pittman, J.K.2    Barkla, B.J.3    Shigaki, T.4    Hirschi, K.D.5
  • 49
    • 0041920602 scopus 로고    scopus 로고
    • CBL1, a calcium sensor that differentially regulates salt, drought, and cold responses in Arabidopsis
    • Cheong YH, Kim KN, Pandey GK, Gupta R, Grant JJ, Luan S (2003) CBL1, a calcium sensor that differentially regulates salt, drought, and cold responses in Arabidopsis. Plant Cell 15:1833-1845
    • (2003) Plant Cell , vol.15 , pp. 1833-1845
    • Cheong, Y.H.1    Kim, K.N.2    Pandey, G.K.3    Gupta, R.4    Grant, J.J.5    Luan, S.6
  • 50
    • 35148841967 scopus 로고    scopus 로고
    • Two calcineurin B-like calcium sensors, interacting with protein kinase CIPK23, regulate leaf transpiration and root potassium uptake in Arabidopsis
    • Cheong YH, Pandey GK, Grant JJ, Batistic O, Li L, Kim BG, Lee SC, Kudla J, Luan S (2007) Two calcineurin B-like calcium sensors, interacting with protein kinase CIPK23, regulate leaf transpiration and root potassium uptake in Arabidopsis. Plant J 52:223-239
    • (2007) Plant J , vol.52 , pp. 223-239
    • Cheong, Y.H.1    Pandey, G.K.2    Grant, J.J.3    Batistic, O.4    Li, L.5    Kim, B.G.6    Lee, S.C.7    Kudla, J.8    Luan, S.9
  • 51
    • 0034256090 scopus 로고    scopus 로고
    • Calmodulin: A prototypical calcium sensor
    • Chin D, Means AR (2000) Calmodulin: a prototypical calcium sensor. Trends Cell Biol 10: 322-328
    • (2000) Trends Cell Biol , vol.10 , pp. 322-328
    • Chin, D.1    Means, A.R.2
  • 52
    • 31444445016 scopus 로고    scopus 로고
    • Arabidopsis calcium-dependent protein kinase AtCPK32 interacts with ABF4, a transcriptional regulator of abscisic acid-responsive gene expression, and modulates its activity
    • Choi HI, Park HJ, Park JH, Kim S, Im MY, Seo HH, Kim YW, Hwang I, Kim SY (2005) Arabidopsis calcium-dependent protein kinase AtCPK32 interacts with ABF4, a transcriptional regulator of abscisic acid-responsive gene expression, and modulates its activity. Plant Physiol 139:1750-1761
    • (2005) Plant Physiol , vol.139 , pp. 1750-1761
    • Choi, H.I.1    Park, H.J.2    Park, J.H.3    Kim, S.4    Im, M.Y.5    Seo, H.H.6    Kim, Y.W.7    Hwang, I.8    Kim, S.Y.9
  • 54
    • 0028831997 scopus 로고
    • Calcium signaling
    • Clapham DE (1995) Calcium signaling. Cell 80:259-268
    • (1995) Cell , vol.80 , pp. 259-268
    • Clapham, D.E.1
  • 57
    • 0026411492 scopus 로고
    • Stretch-activated chloride, potassium, and calcium channels coexisting in plasma membranes of guard cells of Vicia faba L
    • Cosgrove DJ, Hedrich R (1991) Stretch-activated chloride, potassium, and calcium channels coexisting in plasma membranes of guard cells of Vicia faba L. Planta 186:143-153
    • (1991) Planta , vol.186 , pp. 143-153
    • Cosgrove, D.J.1    Hedrich, R.2
  • 60
    • 0001455309 scopus 로고    scopus 로고
    • Where does all the calcium go? Evidence of an important regulatory role for trichomes in two calcicoles
    • De Silva DLR, Hetherington AM, Mansfield TA (1996) Where does all the calcium go? Evidence of an important regulatory role for trichomes in two calcicoles. Plant Cell Environ 19:880-886
    • (1996) Plant Cell Environ , vol.19 , pp. 880-886
    • de Silva, D.L.R.1    Hetherington, A.M.2    Mansfield, T.A.3
  • 61
    • 0032510478 scopus 로고    scopus 로고
    • Translocation of calmodulin to the nucleus supports CREB phosphorylation in hippocampal neurons
    • Deisseroth K, Heist EK, Tsien RW (1998) Translocation of calmodulin to the nucleus supports CREB phosphorylation in hippocampal neurons. Nature 392:198-202
    • (1998) Nature , vol.392 , pp. 198-202
    • Deisseroth, K.1    Heist, E.K.2    Tsien, R.W.3
  • 63
    • 34447515608 scopus 로고    scopus 로고
    • Physiological roles of nonselective cation channels in plants: From salt stress to signalling and development
    • Demidchik V, Maathuis FJ (2007) Physiological roles of nonselective cation channels in plants: from salt stress to signalling and development. New Phytol 175:387-404
    • (2007) New Phytol , vol.175 , pp. 387-404
    • Demidchik, V.1    Maathuis, F.J.2
  • 64
    • 85047684549 scopus 로고    scopus 로고
    • Sodium fluxes through nonselective cation channels in the plasma membrane of protoplasts from Arabidopsis roots
    • Demidchik V, Tester M (2002) Sodium fluxes through nonselective cation channels in the plasma membrane of protoplasts from Arabidopsis roots. Plant Physiol 128:379-387
    • (2002) Plant Physiol , vol.128 , pp. 379-387
    • Demidchik, V.1    Tester, M.2
  • 69
    • 33750515671 scopus 로고    scopus 로고
    • Imaging single-channel calcium microdomains
    • Demuro A, Parker I (2006) Imaging single-channel calcium microdomains. Cell Calcium 40:413-422
    • (2006) Cell Calcium , vol.40 , pp. 413-422
    • Demuro, A.1    Parker, I.2
  • 70
    • 0034520161 scopus 로고    scopus 로고
    • Glutamate-gated calcium fluxes in Arabidopsis
    • Dennison KL, Spalding EP (2000) Glutamate-gated calcium fluxes in Arabidopsis. Plant Physiol 124:1511-1514
    • (2000) Plant Physiol , vol.124 , pp. 1511-1514
    • Dennison, K.L.1    Spalding, E.P.2
  • 71
    • 0002603461 scopus 로고
    • 2+ transport in mitochondiral and microsomal fraction from higher plants
    • 2+ transport in mitochondiral and microsomal fraction from higher plants. Planta 150:1-8
    • (1980) Planta , vol.150 , pp. 1-8
    • Dieter, P.1    Marme, D.2
  • 72
    • 0010524378 scopus 로고
    • The effect of calmodulin and far-red light on the kinetic properties of the mitochondrial and microsomal calcium-ion transport system from corn
    • Dieter P, Marmé D (1983) The effect of calmodulin and far-red light on the kinetic properties of the mitochondrial and microsomal calcium-ion transport system from corn. Planta 159:277-281
    • (1983) Planta , vol.159 , pp. 277-281
    • Dieter, P.1    Marmé, D.2
  • 73
    • 0030864749 scopus 로고    scopus 로고
    • First evidence of a calcium transient in flowering plants at fertilization
    • Digonnet C, Aldon D, Leduc N, Dumas C, Rougier M (1997) First evidence of a calcium transient in flowering plants at fertilization. Development 124:2867-2874
    • (1997) Development , vol.124 , pp. 2867-2874
    • Digonnet, C.1    Aldon, D.2    Leduc, N.3    Dumas, C.4    Rougier, M.5
  • 76
    • 26944439512 scopus 로고    scopus 로고
    • 2+/calmodulin is critical for brassinosteroid biosynthesis and plant growth
    • 2+/calmodulin is critical for brassinosteroid biosynthesis and plant growth. Nature 437:741-745
    • (2005) Nature , vol.437 , pp. 741-745
    • Du, L.1    Poovaiah, B.W.2
  • 78
    • 3542995708 scopus 로고    scopus 로고
    • Identification and characterization of stretch-activated ion channels in pollen protoplasts
    • Dutta R, Robinson KR (2004) Identification and characterization of stretch-activated ion channels in pollen protoplasts. Plant Physiol 135:1398-1406
    • (2004) Plant Physiol , vol.135 , pp. 1398-1406
    • Dutta, R.1    Robinson, K.R.2
  • 79
    • 0029895156 scopus 로고    scopus 로고
    • Calcium spiking in plant root hairs responding to Rhizobium nodulation signals
    • Ehrhardt DW, Wais R, Long SR (1996) Calcium spiking in plant root hairs responding to Rhizobium nodulation signals. Cell 85:673-681
    • (1996) Cell , vol.85 , pp. 673-681
    • Ehrhardt, D.W.1    Wais, R.2    Long, S.R.3
  • 80
    • 0000398148 scopus 로고
    • The essential role of calcium in selective cation transport by plant cells
    • Epstein E (1961) The essential role of calcium in selective cation transport by plant cells. Plant Physiol 36:437-444
    • (1961) Plant Physiol , vol.36 , pp. 437-444
    • Epstein, E.1
  • 81
    • 0032546814 scopus 로고    scopus 로고
    • How calcium enhances plant salt tolerance
    • Epstein E (1998) How calcium enhances plant salt tolerance. Science 280:1906-1907
    • (1998) Science , vol.280 , pp. 1906-1907
    • Epstein, E.1
  • 82
    • 0028588657 scopus 로고
    • Cloning and characterization of a maize pollen-specific calcium-dependent calmodulin-independent protein kinase
    • Estruch JJ, Kadwell S, Merlin E, Crossland L (1994) Cloning and characterization of a maize pollen-specific calcium-dependent calmodulin-independent protein kinase. Proc Natl Acad Sci USA 91:8837-8841
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8837-8841
    • Estruch, J.J.1    Kadwell, S.2    Merlin, E.3    Crossland, L.4
  • 85
    • 0026610965 scopus 로고
    • 2+ through K+ channels in the plasma membrane of Vicia faba guard cells
    • 2+ through K+ channels in the plasma membrane of Vicia faba guard cells. J Membr Biol 128:103-113
    • (1992) J Membr Biol , vol.128 , pp. 103-113
    • Fairley-Grenot, K.A.1    Assmann, S.M.2
  • 86
    • 0032712165 scopus 로고    scopus 로고
    • Calcium and phospholipid activation of a recombinant calciumdependent protein kinase (DcCPK1) from carrot (Daucus carota L.)
    • Farmer PK, Choi JH (1999) Calcium and phospholipid activation of a recombinant calciumdependent protein kinase (DcCPK1) from carrot (Daucus carota L.). Biochim Biophys Acta 1434:6-17
    • (1999) Biochim Biophys Acta , vol.1434 , pp. 6-17
    • Farmer, P.K.1    Choi, J.H.2
  • 87
    • 0036071639 scopus 로고    scopus 로고
    • Ionic signaling in plant responses to gravity and touch
    • Fasano JM, Massa GD, Gilroy S (2002) Ionic signaling in plant responses to gravity and touch. J Plant Growth Regul 21:71-88
    • (2002) J Plant Growth Regul , vol.21 , pp. 71-88
    • Fasano, J.M.1    Massa, G.D.2    Gilroy, S.3
  • 88
    • 0028297761 scopus 로고
    • An in Vitro System for Adhesion and Fusion of Maize Gametes
    • Faure JE, Digonnet C, Dumas C (1994) An in Vitro System for Adhesion and Fusion of Maize Gametes. Science 263:1598-1600
    • (1994) Science , vol.263 , pp. 1598-1600
    • Faure, J.E.1    Digonnet, C.2    Dumas, C.3
  • 89
    • 7144261208 scopus 로고
    • Auxin causes oscillation of cytosolic free calcium and pH in Zea mays coleoptiles
    • Felle H (1988) Auxin causes oscillation of cytosolic free calcium and pH in Zea mays coleoptiles. Planta 174:495-499
    • (1988) Planta , vol.174 , pp. 495-499
    • Felle, H.1
  • 92
    • 0000351423 scopus 로고
    • The self-incompatibiity response in Papaver rhoeas is mediated by cytosolic free calcium
    • Franklin-Tong VE, Ride JP, Read ND, Trewavas A, Franklin FCH (1993) The self-incompatibiity response in Papaver rhoeas is mediated by cytosolic free calcium. Plant J 4:163-177
    • (1993) Plant J , vol.4 , pp. 163-177
    • Franklin-Tong, V.E.1    Ride, J.P.2    Read, N.D.3    Trewavas, A.4    Franklin, F.C.H.5
  • 95
    • 67651116950 scopus 로고    scopus 로고
    • An autophosphorylation site of the protein kinase SOS2 is important for salt tolerance in Arabidopsis
    • Fujii H, Zhu JK (2009) An autophosphorylation site of the protein kinase SOS2 is important for salt tolerance in Arabidopsis. Mol Plant 2:183-190
    • (2009) Mol Plant , vol.2 , pp. 183-190
    • Fujii, H.1    Zhu, J.K.2
  • 97
    • 0025702395 scopus 로고
    • Phototropism and geotropism in maize coleoptiles are spatially correlated with increases in cytosolic free calcium
    • Gehring CA, Williams DA, Cody SH, Parish RW (1990) Phototropism and geotropism in maize coleoptiles are spatially correlated with increases in cytosolic free calcium. Nature 345:528-530
    • (1990) Nature , vol.345 , pp. 528-530
    • Gehring, C.A.1    Williams, D.A.2    Cody, S.H.3    Parish, R.W.4
  • 98
    • 0034529989 scopus 로고    scopus 로고
    • The ACA4 gene of Arabidopsis encodes a vacuolar membrane calcium pump that improves salt tolerance in yeast
    • Geisler M, Frangne N, Gomes E, Martinoia E, Palmgren MG (2000) The ACA4 gene of Arabidopsis encodes a vacuolar membrane calcium pump that improves salt tolerance in yeast. Plant Physiol 124:1814-1827
    • (2000) Plant Physiol , vol.124 , pp. 1814-1827
    • Geisler, M.1    Frangne, N.2    Gomes, E.3    Martinoia, E.4    Palmgren, M.G.5
  • 99
    • 38949110087 scopus 로고    scopus 로고
    • 2+-ATPase regulates adult vegetative development and inflorescence architecture in Arabidopsis
    • 2+-ATPase regulates adult vegetative development and inflorescence architecture in Arabidopsis. Plant Physiol 146:716-728
    • (2008) Plant Physiol , vol.146 , pp. 716-728
    • George, L.1    Romanowsky, S.M.2    Harper, J.F.3    Sharrock, R.A.4
  • 100
    • 0026534659 scopus 로고
    • Gibberellic acid and abscisic acid coordinately regulate cytoplasmic calcium and secretory activity in barley aleurone protoplasts
    • Gilroy S, Jones RL (1992) Gibberellic acid and abscisic acid coordinately regulate cytoplasmic calcium and secretory activity in barley aleurone protoplasts. Proc Natl Acad Sci USA 89:3591-3595
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3591-3595
    • Gilroy, S.1    Jones, R.L.2
  • 101
    • 0025713332 scopus 로고
    • Elevation of cytoplasmic calcium by caged calcium or caged inositol triphosphate initiates stomatal closure
    • Gilroy S, Read ND, Trewavas AJ (1990) Elevation of cytoplasmic calcium by caged calcium or caged inositol triphosphate initiates stomatal closure. Nature 346:769-771
    • (1990) Nature , vol.346 , pp. 769-771
    • Gilroy, S.1    Read, N.D.2    Trewavas, A.J.3
  • 103
    • 0033842313 scopus 로고    scopus 로고
    • The RPM1 plant disease resistance gene facilitates a rapid and sustained increase in cytosolic calcium that is necessary for the oxidative burst and hypersensitive cell death
    • Grant M, Brown I, Adams S, Knight M, Ainslie A, Mansfield J (2000) The RPM1 plant disease resistance gene facilitates a rapid and sustained increase in cytosolic calcium that is necessary for the oxidative burst and hypersensitive cell death. Plant J 23:441-450
    • (2000) Plant J , vol.23 , pp. 441-450
    • Grant, M.1    Brown, I.2    Adams, S.3    Knight, M.4    Ainslie, A.5    Mansfield, J.6
  • 104
    • 0035910259 scopus 로고    scopus 로고
    • 2+-binding protein involved in cryptochrome and phytochrome coaction
    • 2+-binding protein involved in cryptochrome and phytochrome coaction. Science 291:487-490
    • (2001) Science , vol.291 , pp. 487-490
    • Guo, H.1    Mockler, T.2    Duong, H.3    Lin, C.4
  • 105
    • 0034949516 scopus 로고    scopus 로고
    • Molecular characterization of functional domains in the protein kinase SOS2 that is required for plant salt tolerance
    • Guo Y, Halfter U, Ishitani M, Zhu JK (2001b) Molecular characterization of functional domains in the protein kinase SOS2 that is required for plant salt tolerance. Plant Cell 13:1383-1400
    • (2001) Plant Cell , vol.13 , pp. 1383-1400
    • Guo, Y.1    Halfter, U.2    Ishitani, M.3    Zhu, J.K.4
  • 108
    • 0034724180 scopus 로고    scopus 로고
    • The Arabidopsis SOS2 protein kinase physically interacts with and is activated by the calcium-binding protein SOS3
    • Halfter U, Ishitani M, Zhu JK (2000) The Arabidopsis SOS2 protein kinase physically interacts with and is activated by the calcium-binding protein SOS3. Proc Natl Acad Sci USA 97:3735-3740
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3735-3740
    • Halfter, U.1    Ishitani, M.2    Zhu, J.K.3
  • 109
    • 0034712588 scopus 로고    scopus 로고
    • 2+ channels at the plasma membrane of stomatal guard cells are activated by hyperpolarization and abscisic acid
    • 2+ channels at the plasma membrane of stomatal guard cells are activated by hyperpolarization and abscisic acid. Proc Natl Acad Sci USA 97:4967-4972
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 4967-4972
    • Hamilton, D.W.1    Hills, A.2    Kohler, B.3    Blatt, M.R.4
  • 115
    • 0000283706 scopus 로고
    • Cytoplasmic calcium regulates voltage-dependent ion channels in plant vacuoles
    • Hedrich R, Neher E (1987) Cytoplasmic calcium regulates voltage-dependent ion channels in plant vacuoles. Nature 329:833-836
    • (1987) Nature , vol.329 , pp. 833-836
    • Hedrich, R.1    Neher, E.2
  • 116
    • 0343749685 scopus 로고
    • Calcium Deficiency of Dark-grown Seedlings of Phaseolus vulgaris L
    • Helms K (1971) Calcium Deficiency of Dark-grown Seedlings of Phaseolus vulgaris L. Plant Physiol 47:799-804
    • (1971) Plant Physiol , vol.47 , pp. 799-804
    • Helms, K.1
  • 117
    • 27744579268 scopus 로고    scopus 로고
    • Calcium: A central regulator of plant growth and development
    • Hepler PK (2005) Calcium: a central regulator of plant growth and development. Plant Cell 17:2142-2155
    • (2005) Plant Cell , vol.17 , pp. 2142-2155
    • Hepler, P.K.1
  • 120
    • 0033231267 scopus 로고    scopus 로고
    • Expression of Arabidopsis CAX1 in tobacco: Altered calcium homeostasis and increased stress sensitivity
    • Hirschi KD (1999) Expression of Arabidopsis CAX1 in tobacco: altered calcium homeostasis and increased stress sensitivity. Plant Cell 11:2113-2122
    • (1999) Plant Cell , vol.11 , pp. 2113-2122
    • Hirschi, K.D.1
  • 121
    • 11844257472 scopus 로고    scopus 로고
    • The calcium conundrum. Both versatile nutrient and specific signal
    • Hirschi KD (2004) The calcium conundrum. Both versatile nutrient and specific signal. Plant Physiol 136:2438-2442
    • (2004) Plant Physiol , vol.136 , pp. 2438-2442
    • Hirschi, K.D.1
  • 122
    • 0033833640 scopus 로고    scopus 로고
    • Expression of arabidopsis CAX2 in tobacco. Altered metal accumulation and increased manganese tolerance
    • Hirschi KD, Korenkov VD, Wilganowski NL, Wagner GJ (2000) Expression of arabidopsis CAX2 in tobacco. Altered metal accumulation and increased manganese tolerance. Plant Physiol 124:125-133
    • (2000) Plant Physiol , vol.124 , pp. 125-133
    • Hirschi, K.D.1    Korenkov, V.D.2    Wilganowski, N.L.3    Wagner, G.J.4
  • 123
    • 17144394175 scopus 로고    scopus 로고
    • A cellular hypothesis for the induction of blossom-end rot in tomato fruit
    • Ho LC, White PJ (2005) A cellular hypothesis for the induction of blossom-end rot in tomato fruit. Ann Bot (Lond) 95:571-581
    • (2005) Ann Bot (Lond) , vol.95 , pp. 571-581
    • Ho, L.C.1    White, P.J.2
  • 124
    • 0030925241 scopus 로고    scopus 로고
    • 2+/GTP-binding protein-controlled exocytosis in a plant cell
    • 2+/GTP-binding protein-controlled exocytosis in a plant cell. Proc Natl Acad Sci USA 94:6565-6570
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6565-6570
    • Homann, U.1    Tester, M.2
  • 126
    • 58349088076 scopus 로고    scopus 로고
    • AtCIPK8, a CBL-interacting protein kinase, regulates the lowaffinity phase of the primary nitrate response
    • Hu HC, Wang YY, Tsay YF (2009) AtCIPK8, a CBL-interacting protein kinase, regulates the lowaffinity phase of the primary nitrate response. Plant J 57:264-278
    • (2009) Plant J , vol.57 , pp. 264-278
    • Hu, H.C.1    Wang, Y.Y.2    Tsay, Y.F.3
  • 127
    • 0038715131 scopus 로고    scopus 로고
    • Plants do it differently. A new basis for potassium/sodium selectivity in the pore of an ion channel
    • Hua BG, Mercier RW, Leng Q, Berkowitz GA (2003a) Plants do it differently. A new basis for potassium/sodium selectivity in the pore of an ion channel. Plant Physiol 132:1353-1361
    • (2003) Plant Physiol , vol.132 , pp. 1353-1361
    • Hua, B.G.1    Mercier, R.W.2    Leng, Q.3    Berkowitz, G.A.4
  • 128
    • 0344496699 scopus 로고    scopus 로고
    • Functional interaction of calmodulin with a plant cyclic nucleotide gated cation channel
    • Hua BG, Mercier RW, Zielinski RE, Berkowitz GA (2003b) Functional interaction of calmodulin with a plant cyclic nucleotide gated cation channel. Plant Physiol Biochem 41:945-954
    • (2003) Plant Physiol Biochem , vol.41 , pp. 945-954
    • Hua, B.G.1    Mercier, R.W.2    Zielinski, R.E.3    Berkowitz, G.A.4
  • 130
    • 0034705147 scopus 로고    scopus 로고
    • 2+ pump (ACA2) located in the endoplasmic reticulum of Arabidopsis
    • 2+ pump (ACA2) located in the endoplasmic reticulum of Arabidopsis. Proc Natl Acad Sci USA 97:6224-6229
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6224-6229
    • Hwang, I.1    Sze, H.2    Harper, J.F.3
  • 131
    • 0026542897 scopus 로고
    • Changes in cytosolic pH and calcium of guard cells precede stomatal movements
    • Irving HR, Gehring CA, Parish RW (1992) Changes in cytosolic pH and calcium of guard cells precede stomatal movements. Proc Natl Acad Sci USA 89:1790-1794
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 1790-1794
    • Irving, H.R.1    Gehring, C.A.2    Parish, R.W.3
  • 132
    • 62549090194 scopus 로고    scopus 로고
    • A tobacco Calcium-dependent protein kinase, CDPK1, regulates the transcription factor REPRESSION OF SHOOT GROWTH in response to gibberellins
    • Ishida S, Yuasa T, Nakata M, Takahashi Y (2008) A tobacco Calcium-dependent protein kinase, CDPK1, regulates the transcription factor REPRESSION OF SHOOT GROWTH in response to gibberellins. Plant Cell 20:3273-3288
    • (2008) Plant Cell , vol.20 , pp. 3273-3288
    • Ishida, S.1    Yuasa, T.2    Nakata, M.3    Takahashi, Y.4
  • 133
    • 0033793156 scopus 로고    scopus 로고
    • SOS3 function in plant salt tolerance requires N-myristoylation and calcium binding
    • Ishitani M, Liu J, Halfter U, Kim CS, Shi W, Zhu JK (2000) SOS3 function in plant salt tolerance requires N-myristoylation and calcium binding. Plant Cell 12:1667-1678
    • (2000) Plant Cell , vol.12 , pp. 1667-1678
    • Ishitani, M.1    Liu, J.2    Halfter, U.3    Kim, C.S.4    Shi, W.5    Zhu, J.K.6
  • 135
    • 0034842948 scopus 로고    scopus 로고
    • Calcium - how and why?
    • Jaiswal JK (2001) Calcium - how and why? J Biosci 26:357-363
    • (2001) J Biosci , vol.26 , pp. 357-363
    • Jaiswal, J.K.1
  • 136
    • 16644366421 scopus 로고    scopus 로고
    • Evidence of a novel cell signaling role for extracellular adenosine triphosphates and diphosphates in Arabidopsis
    • Jeter CR, Tang W, Henaff E, Butterfield T, Roux SJ (2004) Evidence of a novel cell signaling role for extracellular adenosine triphosphates and diphosphates in Arabidopsis. Plant Cell 16:2652-2664
    • (2004) Plant Cell , vol.16 , pp. 2652-2664
    • Jeter, C.R.1    Tang, W.2    Henaff, E.3    Butterfield, T.4    Roux, S.J.5
  • 138
    • 0030027680 scopus 로고    scopus 로고
    • Extracellular calmodulin-binding proteins in plants: Purification of a 21-kDa calmodulin-binding protein
    • Jun T, Wu S, Bai J, Sun D (1996) Extracellular calmodulin-binding proteins in plants: purification of a 21-kDa calmodulin-binding protein. Planta 198:510-516
    • (1996) Planta , vol.198 , pp. 510-516
    • Jun, T.1    Wu, S.2    Bai, J.3    Sun, D.4
  • 139
    • 34248190722 scopus 로고    scopus 로고
    • Cyclic nucleotide-gated channels in plants
    • Kaplan B, Sherman T, Fromm H (2007) Cyclic nucleotide-gated channels in plants. FEBS Lett 581:2237-2246
    • (2007) FEBS Lett , vol.581 , pp. 2237-2246
    • Kaplan, B.1    Sherman, T.2    Fromm, H.3
  • 140
    • 0025196294 scopus 로고
    • + antiporter in plasma membrane vesicles isolated by aqueous two-phase partitioning from corn leaves
    • + antiporter in plasma membrane vesicles isolated by aqueous two-phase partitioning from corn leaves. J Membr Biol 114:133-142
    • (1990) J Membr Biol , vol.114 , pp. 133-142
    • Kasai, M.1    Muto, S.2
  • 141
    • 0002798136 scopus 로고
    • Some aspects of Calcium-dependent regulation in plant metabolism
    • Kauss H (1987) Some aspects of Calcium-dependent regulation in plant metabolism. Ann Rev Plant Physiol 38:47-72
    • (1987) Ann Rev Plant Physiol , vol.38 , pp. 47-72
    • Kauss, H.1
  • 142
    • 0031850816 scopus 로고    scopus 로고
    • Salicylic acid induces extracellular superoxide generation followed by an increase in cytosolic calcium ion in tobacco suspension culture: The earliest events in salicylic acid signal transduction
    • Kawano T, Sahashi N, Takahashi K, Uozumi N, Muto S (1998) Salicylic acid induces extracellular superoxide generation followed by an increase in cytosolic calcium ion in tobacco suspension culture: the earliest events in salicylic acid signal transduction. Plant Cell Physiol 39:721-730
    • (1998) Plant Cell Physiol , vol.39 , pp. 721-730
    • Kawano, T.1    Sahashi, N.2    Takahashi, K.3    Uozumi, N.4    Muto, S.5
  • 144
    • 0033884980 scopus 로고    scopus 로고
    • Cell-type-specific calcium responses to drought, salt and cold in the Arabidopsis root
    • Kiegle E, Moore CA, Haseloff J, Tester MA, Knight MR (2000) Cell-type-specific calcium responses to drought, salt and cold in the Arabidopsis root. Plant J 23:267-278
    • (2000) Plant J , vol.23 , pp. 267-278
    • Kiegle, E.1    Moore, C.A.2    Haseloff, J.3    Tester, M.A.4    Knight, M.R.5
  • 145
    • 0037329951 scopus 로고    scopus 로고
    • CIPK3, a calcium sensor associated protein kinase that regulates abscisic acid and cold signal transduction in Arabidopsis
    • Kim KN, Cheong YH, Grant JJ, Pandey GK, Luan S (2003) CIPK3, a calcium sensor associated protein kinase that regulates abscisic acid and cold signal transduction in Arabidopsis. Plant Cell 15:411-423
    • (2003) Plant Cell , vol.15 , pp. 411-423
    • Kim, K.N.1    Cheong, Y.H.2    Grant, J.J.3    Pandey, G.K.4    Luan, S.5
  • 148
    • 0346668129 scopus 로고    scopus 로고
    • Convergence of calcium signaling pathways of pathogenic elicitors and abscisic acid in Arabidopsis guard cells
    • Klusener B, Young JJ, Murata Y, Allen GJ, Mori IC, Hugouvieux V, Schroeder JI (2002) Convergence of calcium signaling pathways of pathogenic elicitors and abscisic acid in Arabidopsis guard cells. Plant Physiol 130:2152-2163
    • (2002) Plant Physiol , vol.130 , pp. 2152-2163
    • Klusener, B.1    Young, J.J.2    Murata, Y.3    Allen, G.J.4    Mori, I.C.5    Hugouvieux, V.6    Schroeder, J.I.7
  • 149
    • 0026419945 scopus 로고
    • Transgenic plant aequorin reports the effects of touch and cold-shock and elicitors on cytoplasmic calcium
    • Knight MR, Campbell AK, Smith SM, Trewavas AJ (1991) Transgenic plant aequorin reports the effects of touch and cold-shock and elicitors on cytoplasmic calcium. Nature 352: 524-526
    • (1991) Nature , vol.352 , pp. 524-526
    • Knight, M.R.1    Campbell, A.K.2    Smith, S.M.3    Trewavas, A.J.4
  • 150
    • 0031279985 scopus 로고    scopus 로고
    • Calcium signalling in Arabidopsis thaliana responding to drought and salinity
    • Knight H, Trewavas AJ, Knight MR (1997) Calcium signalling in Arabidopsis thaliana responding to drought and salinity. Plant J 12:1067-1078
    • (1997) Plant J , vol.12 , pp. 1067-1078
    • Knight, H.1    Trewavas, A.J.2    Knight, M.R.3
  • 151
    • 0032447027 scopus 로고    scopus 로고
    • A history of stress alters drought calcium signaling pathways in Arabidopsis
    • Knight H, Brandt S, Knight MR (1998) A history of stress alters drought calcium signaling pathways in Arabidopsis. Plant J 16:681-687
    • (1998) Plant J , vol.16 , pp. 681-687
    • Knight, H.1    Brandt, S.2    Knight, M.R.3
  • 152
    • 0842328861 scopus 로고    scopus 로고
    • Calcium sensors and their interacting protein kinases: Genomics of the Arabidopsis and rice CBL-CIPK signaling networks
    • Kolukisaoglu U, Weinl S, Blazevic D, Batistic O, Kudla J (2004) Calcium sensors and their interacting protein kinases: genomics of the Arabidopsis and rice CBL-CIPK signaling networks. Plant Physiol 134:43-58
    • (2004) Plant Physiol , vol.134 , pp. 43-58
    • Kolukisaoglu, U.1    Weinl, S.2    Blazevic, D.3    Batistic, O.4    Kudla, J.5
  • 154
    • 0001635360 scopus 로고
    • Stromal Free Calcium Concentration and Light-Mediated Activation of Chloroplast Fructose-1, 6-Bisphosphatase
    • Kreimer G, Melkonian M, Holtum JA, Latzko E (1988) Stromal Free Calcium Concentration and Light-Mediated Activation of Chloroplast Fructose-1, 6-Bisphosphatase. Plant Physiol 86:423-428
    • (1988) Plant Physiol , vol.86 , pp. 423-428
    • Kreimer, G.1    Melkonian, M.2    Holtum, J.A.3    Latzko, E.4
  • 155
    • 0033551073 scopus 로고    scopus 로고
    • Genes for calcineurin B-like proteins in Arabidopsis are differentially regulated by stress signals
    • Kudla J, Xu Q, Harter K, Gruissem W, Luan S (1999) Genes for calcineurin B-like proteins in Arabidopsis are differentially regulated by stress signals. Proc Natl Acad Sci USA 96:4718-4723
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4718-4723
    • Kudla, J.1    Xu, Q.2    Harter, K.3    Gruissem, W.4    Luan, S.5
  • 156
    • 57649203470 scopus 로고    scopus 로고
    • Calmodulin7 plays an important role as transcriptional regulator in Arabidopsis seedling development
    • Kushwaha R, Singh A, Chattopadhyay S (2008) Calmodulin7 plays an important role as transcriptional regulator in Arabidopsis seedling development. Plant Cell 20:1747-1759
    • (2008) Plant Cell , vol.20 , pp. 1747-1759
    • Kushwaha, R.1    Singh, A.2    Chattopadhyay, S.3
  • 160
    • 85047683937 scopus 로고    scopus 로고
    • Protection against heat stress-induced oxidative damage in Arabidopsis involves calcium, abscisic acid, ethylene, and salicylic acid
    • Larkindale J, Knight MR (2002) Protection against heat stress-induced oxidative damage in Arabidopsis involves calcium, abscisic acid, ethylene, and salicylic acid. Plant Physiol 128:682-695
    • (2002) Plant Physiol , vol.128 , pp. 682-695
    • Larkindale, J.1    Knight, M.R.2
  • 162
    • 0033432828 scopus 로고    scopus 로고
    • Serine/threonine phosphorylation of calmodulin modulates its interaction with the binding domains of target enzymes
    • Leclerc E, Corti C, Schmid H, Vetter S, James P, Carafoli E (1999) Serine/threonine phosphorylation of calmodulin modulates its interaction with the binding domains of target enzymes. Biochem J 344(Pt 2):403-411
    • (1999) Biochem J , vol.344 , Issue.Pt 2 , pp. 403-411
    • Leclerc, E.1    Corti, C.2    Schmid, H.3    Vetter, S.4    James, P.5    Carafoli, E.6
  • 163
    • 0036802255 scopus 로고    scopus 로고
    • Analysis and effects of cytosolic free calcium increases in response to elicitors in Nicotiana plumbaginifolia cells
    • Lecourieux D, Mazars C, Pauly N, Ranjeva R, Pugin A (2002) Analysis and effects of cytosolic free calcium increases in response to elicitors in Nicotiana plumbaginifolia cells. Plant Cell 14:2627-2641
    • (2002) Plant Cell , vol.14 , pp. 2627-2641
    • Lecourieux, D.1    Mazars, C.2    Pauly, N.3    Ranjeva, R.4    Pugin, A.5
  • 164
    • 27744462058 scopus 로고    scopus 로고
    • Proteinaceous and oligosaccharidic elicitors induce different calcium signatures in the nucleus of tobacco cells
    • Lecourieux D, Lamotte O, Bourque S, Wendehenne D, Mazars C, Ranjeva R, Pugin A (2005) Proteinaceous and oligosaccharidic elicitors induce different calcium signatures in the nucleus of tobacco cells. Cell Calcium 38:527-538
    • (2005) Cell Calcium , vol.38 , pp. 527-538
    • Lecourieux, D.1    Lamotte, O.2    Bourque, S.3    Wendehenne, D.4    Mazars, C.5    Ranjeva, R.6    Pugin, A.7
  • 165
    • 0020584018 scopus 로고
    • Reversible Loss of Gravitropic Sensitivity in Maize Roots After Tip Application of Calcium Chelators
    • Lee JS, Mulkey TJ, Evans ML (1983) Reversible Loss of Gravitropic Sensitivity in Maize Roots After Tip Application of Calcium Chelators. Science 220:1375-1376
    • (1983) Science , vol.220 , pp. 1375-1376
    • Lee, J.S.1    Mulkey, T.J.2    Evans, M.L.3
  • 167
    • 0032510705 scopus 로고    scopus 로고
    • Kinetic and calcium-binding properties of three calciumdependent protein kinase isoenzymes from soybean
    • Lee JY, Yoo BC, Harmon AC (1998) Kinetic and calcium-binding properties of three calciumdependent protein kinase isoenzymes from soybean. Biochemistry 37:6801-6809
    • (1998) Biochemistry , vol.37 , pp. 6801-6809
    • Lee, J.Y.1    Yoo, B.C.2    Harmon, A.C.3
  • 172
    • 0030113929 scopus 로고    scopus 로고
    • Calcium-mediated apoptosis in a plant hypersensitive disease resistance response
    • Levine A, Pennell RI, Alvarez ME, Palmer R, Lamb C (1996) Calcium-mediated apoptosis in a plant hypersensitive disease resistance response. Curr Biol 6:427-437
    • (1996) Curr Biol , vol.6 , pp. 427-437
    • Levine, A.1    Pennell, R.I.2    Alvarez, M.E.3    Palmer, R.4    Lamb, C.5
  • 176
    • 0141787893 scopus 로고    scopus 로고
    • Mitochondrial and cytosolic calcium dynamics are differentially regulated in plants
    • Logan DC, Knight MR (2003) Mitochondrial and cytosolic calcium dynamics are differentially regulated in plants. Plant Physiol 133:21-24
    • (2003) Plant Physiol , vol.133 , pp. 21-24
    • Logan, D.C.1    Knight, M.R.2
  • 177
    • 0032297190 scopus 로고    scopus 로고
    • Involvement of plasma membrane redox activity and calcium homeostasis in the UV-B and UV-A/blue light induction of gene expression in Arabidopsis
    • Long JC, Jenkins GI (1998) Involvement of plasma membrane redox activity and calcium homeostasis in the UV-B and UV-A/blue light induction of gene expression in Arabidopsis. Plant Cell 10:2077-2086
    • (1998) Plant Cell , vol.10 , pp. 2077-2086
    • Long, J.C.1    Jenkins, G.I.2
  • 178
    • 1842813395 scopus 로고    scopus 로고
    • Circadian and diurnal calcium oscillations encode photoperiodic information in Arabidopsis
    • Love J, Dodd AN, Webb AA (2004) Circadian and diurnal calcium oscillations encode photoperiodic information in Arabidopsis. Plant Cell 16:956-966
    • (2004) Plant Cell , vol.16 , pp. 956-966
    • Love, J.1    Dodd, A.N.2    Webb, A.A.3
  • 179
    • 0036006051 scopus 로고    scopus 로고
    • An Arabidopsis calcium-dependent protein kinase is associated with the endoplasmic reticulum
    • Lu SX, Hrabak EM (2002) An Arabidopsis calcium-dependent protein kinase is associated with the endoplasmic reticulum. Plant Physiol 128:1008-1021
    • (2002) Plant Physiol , vol.128 , pp. 1008-1021
    • Lu, S.X.1    Hrabak, E.M.2
  • 181
    • 27644527841 scopus 로고    scopus 로고
    • A putative plasma membrane cation/proton antiporter from soybean confers salt tolerance in Arabidopsis
    • Luo GZ, Wang HW, Huang J, Tian AG, Wang YJ, Zhang JS, Chen SY (2005) A putative plasma membrane cation/proton antiporter from soybean confers salt tolerance in Arabidopsis. Plant Mol Biol 59:809-820
    • (2005) Plant Mol Biol , vol.59 , pp. 809-820
    • Luo, G.Z.1    Wang, H.W.2    Huang, J.3    Tian, A.G.4    Wang, Y.J.5    Zhang, J.S.6    Chen, S.Y.7
  • 182
    • 0001208576 scopus 로고
    • Salinity Stress Increases Cytoplasmic Ca Activity in Maize Root Protoplasts
    • Lynch J, Polito VS, Lauchli A (1989) Salinity Stress Increases Cytoplasmic Ca Activity in Maize Root Protoplasts. Plant Physiol 90:1271-1274
    • (1989) Plant Physiol , vol.90 , pp. 1271-1274
    • Lynch, J.1    Polito, V.S.2    Lauchli, A.3
  • 183
    • 35348959564 scopus 로고    scopus 로고
    • AtCPK23 functions in Arabidopsis responses to drought and salt stresses
    • Ma SY, Wu WH (2007) AtCPK23 functions in Arabidopsis responses to drought and salt stresses. Plant Mol Biol 65:511-518
    • (2007) Plant Mol Biol , vol.65 , pp. 511-518
    • Ma, S.Y.1    Wu, W.H.2
  • 184
    • 0032697003 scopus 로고    scopus 로고
    • The presence of a heterotrimeric G protein and its role in signal transduction of extracellular calmodulin in pollen germination and tube growth
    • Ma L, Xu X, Cui S, Sun D (1999) The presence of a heterotrimeric G protein and its role in signal transduction of extracellular calmodulin in pollen germination and tube growth. Plant Cell 11:1351-1364
    • (1999) Plant Cell , vol.11 , pp. 1351-1364
    • Ma, L.1    Xu, X.2    Cui, S.3    Sun, D.4
  • 185
    • 57749110482 scopus 로고    scopus 로고
    • 2+ elevation is linked to downstream nitric oxide generation through the action of calmodulin or a calmodulin-like protein
    • 2+ elevation is linked to downstream nitric oxide generation through the action of calmodulin or a calmodulin-like protein. Plant Physiol 148:818-828
    • (2008) Plant Physiol , vol.148 , pp. 818-828
    • Ma, W.1    Smigel, A.2    Tsai, Y.C.3    Braam, J.4    Berkowitz, G.A.5
  • 186
    • 0001224614 scopus 로고
    • Calcium influx at the plasmalemma of isolated guard cells of Commelina communis
    • MacRobbie EA (1989) Calcium influx at the plasmalemma of isolated guard cells of Commelina communis. Planta 178:231-241
    • (1989) Planta , vol.178 , pp. 231-241
    • Macrobbie, E.A.1
  • 187
    • 58149232499 scopus 로고    scopus 로고
    • Mutations in AtCML9, a calmodulin-like protein from Arabidopsis thaliana, alter plant responses to abiotic stress and abscisic acid
    • Magnan F, Ranty B, Charpenteau M, Sotta B, Galaud JP, Aldon D (2008) Mutations in AtCML9, a calmodulin-like protein from Arabidopsis thaliana, alter plant responses to abiotic stress and abscisic acid. Plant J 56:575-589
    • (2008) Plant J , vol.56 , pp. 575-589
    • Magnan, F.1    Ranty, B.2    Charpenteau, M.3    Sotta, B.4    Galaud, J.P.5    Aldon, D.6
  • 188
    • 34249933061 scopus 로고    scopus 로고
    • How synaptotagmin promotes membrane fusion
    • Martens S, Kozlov MM, McMahon HT (2007) How synaptotagmin promotes membrane fusion. Science 316:1205-1208
    • (2007) Science , vol.316 , pp. 1205-1208
    • Martens, S.1    Kozlov, M.M.2    McMahon, H.T.3
  • 189
    • 0034548365 scopus 로고    scopus 로고
    • Membrane localization of a rice calcium-dependent protein kinase (CDPK) is mediated by myristoylation and palmitoylation
    • Martin ML, Busconi L (2000) Membrane localization of a rice calcium-dependent protein kinase (CDPK) is mediated by myristoylation and palmitoylation. Plant J 24:429-435
    • (2000) Plant J , vol.24 , pp. 429-435
    • Martin, M.L.1    Busconi, L.2
  • 190
    • 0033833714 scopus 로고    scopus 로고
    • Subcellular localization of a high affinity binding site for D-myo-inositol 1, 4, 5-trisphosphate from Chenopodium rubrum
    • Martinec J, Feltl T, Scanlon CH, Lumsden PJ, Machackova I (2000) Subcellular localization of a high affinity binding site for D-myo-inositol 1, 4, 5-trisphosphate from Chenopodium rubrum. Plant Physiol 124:475-483
    • (2000) Plant Physiol , vol.124 , pp. 475-483
    • Martinec, J.1    Feltl, T.2    Scanlon, C.H.3    Lumsden, P.J.4    Machackova, I.5
  • 194
    • 0042466588 scopus 로고    scopus 로고
    • Calmodulins and related potential calcium sensors of Arabidopsis
    • McCormack E, Braam J (2003) Calmodulins and related potential calcium sensors of Arabidopsis. New Phyt 159:585-598
    • (2003) New Phyt , vol.159 , pp. 585-598
    • McCormack, E.1    Braam, J.2
  • 195
    • 23044471508 scopus 로고    scopus 로고
    • Handling calcium signaling: Arabidopsis CaMs and CMLs
    • McCormack E, Tsai YC, Braam J (2005) Handling calcium signaling: Arabidopsis CaMs and CMLs. Trends Plant Sci 10:383-389
    • (2005) Trends Plant Sci , vol.10 , pp. 383-389
    • McCormack, E.1    Tsai, Y.C.2    Braam, J.3
  • 196
    • 3242716121 scopus 로고    scopus 로고
    • The calcium-dependent protein kinase HvCDPK1 mediates the gibberellic acid response of the barley aleurone through regulation of vacuolar function
    • McCubbin AG, Ritchie SM, Swanson SJ, Gilroy S (2004) The calcium-dependent protein kinase HvCDPK1 mediates the gibberellic acid response of the barley aleurone through regulation of vacuolar function. Plant J 39:206-218
    • (2004) Plant J , vol.39 , pp. 206-218
    • McCubbin, A.G.1    Ritchie, S.M.2    Swanson, S.J.3    Gilroy, S.4
  • 197
    • 0029124281 scopus 로고
    • Granal photosystem II complexes contain only the high redox potential form of cytochrome b-559 which is stabilized by the ligation of calcium
    • McNamara VP, Gounaris K (1995) Granal photosystem II complexes contain only the high redox potential form of cytochrome b-559 which is stabilized by the ligation of calcium. Biochim Biophys Acta 1231:289-296
    • (1995) Biochim Biophys Acta , vol.1231 , pp. 289-296
    • McNamara, V.P.1    Gounaris, K.2
  • 200
  • 201
    • 47249137786 scopus 로고    scopus 로고
    • Two voltagedependent calcium channels co-exist in the apical plasma membrane of Arabidopsis thaliana root hairs
    • Miedema H, Demidchik V, Very AA, Bothwell JH, Brownlee C, Davies JM (2008) Two voltagedependent calcium channels co-exist in the apical plasma membrane of Arabidopsis thaliana root hairs. New Phytol 179:378-385
    • (2008) New Phytol , vol.179 , pp. 378-385
    • Miedema, H.1    Demidchik, V.2    Very, A.A.3    Bothwell, J.H.4    Brownlee, C.5    Davies, J.M.6
  • 202
    • 0023090515 scopus 로고
    • Depletion of cytosolic free calcium induced by photosynthesis
    • Miller AJ, Sanders D (1987) Depletion of cytosolic free calcium induced by photosynthesis. Nature 326:397-400
    • (1987) Nature , vol.326 , pp. 397-400
    • Miller, A.J.1    Sanders, D.2
  • 209
    • 0031200791 scopus 로고    scopus 로고
    • 2+ release across nonvacuolar membranes in cauliflower
    • 2+ release across nonvacuolar membranes in cauliflower. Plant Physiol 114:1511-1521
    • (1997) Plant Physiol , vol.114 , pp. 1511-1521
    • Muir, S.R.1    Sanders, D.2
  • 210
    • 33751285390 scopus 로고
    • Mineral nutrition of plants
    • Mulder EG (1950) Mineral nutrition of plants. Annu Rev Plant Physiol 1:1-24
    • (1950) Annu Rev Plant Physiol , vol.1 , pp. 1-24
    • Mulder, E.G.1
  • 211
    • 0142242192 scopus 로고    scopus 로고
    • The crystal structure of the novel calcium-binding protein AtCBL2 from Arabidopsis thaliana
    • Nagae M, Nozawa A, Koizumi N, Sano H, Hashimoto H, Sato M, Shimizu T (2003) The crystal structure of the novel calcium-binding protein AtCBL2 from Arabidopsis thaliana. J Biol Chem 278:42240-42246
    • (2003) J Biol Chem , vol.278 , pp. 42240-42246
    • Nagae, M.1    Nozawa, A.2    Koizumi, N.3    Sano, H.4    Hashimoto, H.5    Sato, M.6    Shimizu, T.7
  • 213
    • 0034682499 scopus 로고    scopus 로고
    • Calcium release from the endoplasmic reticulum of higher plants elicited by the NADP metabolite nicotinic acid adenine dinucleotide phosphate
    • Navazio L, Bewell MA, Siddiqua A, Dickinson GD, Galione A, Sanders D (2000) Calcium release from the endoplasmic reticulum of higher plants elicited by the NADP metabolite nicotinic acid adenine dinucleotide phosphate. Proc Natl Acad Sci USA 97:8693-8698
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8693-8698
    • Navazio, L.1    Bewell, M.A.2    Siddiqua, A.3    Dickinson, G.D.4    Galione, A.5    Sanders, D.6
  • 214
    • 0034744461 scopus 로고    scopus 로고
    • 2+ by cyclic ADP-ribose from the endoplasmic reticulum of cauliflower florets
    • 2+ by cyclic ADP-ribose from the endoplasmic reticulum of cauliflower florets. Plant Physiol 125:2129-2138
    • (2001) Plant Physiol , vol.125 , pp. 2129-2138
    • Navazio, L.1    Mariani, P.2    Sanders, D.3
  • 215
    • 38349091117 scopus 로고    scopus 로고
    • Calcium efflux as a component of the hypersensitive response of Nicotiana benthamiana to Pseudomonas syringae
    • Nemchinov LG, Shabala L, Shabala S (2008) Calcium efflux as a component of the hypersensitive response of Nicotiana benthamiana to Pseudomonas syringae. Plant Cell Physiol 49:40-46
    • (2008) Plant Cell Physiol , vol.49 , pp. 40-46
    • Nemchinov, L.G.1    Shabala, L.2    Shabala, S.3
  • 216
    • 0027156395 scopus 로고
    • Calcium/calmodulin-dependent and independent phytochrome signal transduction pathways
    • Neuhaus G, Bowler C, Kern R, Chua NH (1993) Calcium/calmodulin-dependent and independent phytochrome signal transduction pathways. Cell 73:937-952
    • (1993) Cell , vol.73 , pp. 937-952
    • Neuhaus, G.1    Bowler, C.2    Kern, R.3    Chua, N.H.4
  • 217
    • 0035967125 scopus 로고    scopus 로고
    • Drought-induced guard cell signal transduction involves sphingosine-1-phosphate
    • Ng CK, Carr K, McAinsh MR, Powell B, Hetherington AM (2001) Drought-induced guard cell signal transduction involves sphingosine-1-phosphate. Nature 410:596-599
    • (2001) Nature , vol.410 , pp. 596-599
    • Ng, C.K.1    Carr, K.2    McAinsh, M.R.3    Powell, B.4    Hetherington, A.M.5
  • 219
    • 0003772435 scopus 로고
    • Why Calcium?
    • Ochiai E-I (1991) Why Calcium? J Chem Educ 68:10-12
    • (1991) J Chem Educ , vol.68 , pp. 10-12
    • Ochiai, E.-I.1
  • 220
    • 0039791752 scopus 로고
    • Analysis of the State of Posttranslational Calmodulin Methylation in Developing Pea Plants
    • Oh SH, Roberts DM (1990) Analysis of the State of Posttranslational Calmodulin Methylation in Developing Pea Plants. Plant Physiol 93:880-887
    • (1990) Plant Physiol , vol.93 , pp. 880-887
    • Oh, S.H.1    Roberts, D.M.2
  • 221
    • 0141593530 scopus 로고    scopus 로고
    • A novel domain in the protein kinase SOS2 mediates interaction with the protein phosphatase 2C ABI2
    • Ohta M, Guo Y, Halfter U, Zhu JK (2003) A novel domain in the protein kinase SOS2 mediates interaction with the protein phosphatase 2C ABI2. Proc Natl Acad Sci USA 100:11771-11776
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11771-11776
    • Ohta, M.1    Guo, Y.2    Halfter, U.3    Zhu, J.K.4
  • 223
    • 0035215715 scopus 로고    scopus 로고
    • The nucleus together with the cytosol generates patterns of specific cellular calcium signatures in tobacco suspension culture cells
    • Pauly N, Knight MR, Thuleau P, Graziana A, Muto S, Ranjeva R, Mazars C (2001) The nucleus together with the cytosol generates patterns of specific cellular calcium signatures in tobacco suspension culture cells. Cell Calcium 30:413-421
    • (2001) Cell Calcium , vol.30 , pp. 413-421
    • Pauly, N.1    Knight, M.R.2    Thuleau, P.3    Graziana, A.4    Muto, S.5    Ranjeva, R.6    Mazars, C.7
  • 230
    • 23644458923 scopus 로고    scopus 로고
    • Calcium: Just another regulator in the machinery of life?
    • Plieth C (2005) Calcium: just another regulator in the machinery of life? Ann Bot (Lond) 96:1-8
    • (2005) Ann Bot (Lond) , vol.96 , pp. 1-8
    • Plieth, C.1
  • 231
    • 0033152627 scopus 로고    scopus 로고
    • Temperature sensing by plants: The primary characteristics of signal perception and calcium response
    • Plieth C, Hansen UP, Knight H, Knight MR (1999) Temperature sensing by plants: the primary characteristics of signal perception and calcium response. Plant J 18:491-497
    • (1999) Plant J , vol.18 , pp. 491-497
    • Plieth, C.1    Hansen, U.P.2    Knight, H.3    Knight, M.R.4
  • 232
    • 34248363651 scopus 로고    scopus 로고
    • Differential binding of calmodulin-related proteins to their targets revealed through high-density Arabidopsis protein microarrays
    • Popescu SC, Popescu GV, Bachan S, Zhang Z, Seay M, Gerstein M, Snyder M, Dinesh Kumar SP (2007) Differential binding of calmodulin-related proteins to their targets revealed through high-density Arabidopsis protein microarrays. Proc Natl Acad Sci USA 104:4730-4735
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 4730-4735
    • Popescu, S.C.1    Popescu, G.V.2    Bachan, S.3    Zhang, Z.4    Seay, M.5    Gerstein, M.6    Snyder, M.7    Dinesh, K.S.P.8
  • 233
    • 0017145035 scopus 로고
    • Light-dependent changes of the Mg2+ concentration in the stroma in relation to the Mg2+ dependency of CO2 fixation in intact chloroplasts
    • Portis AR Jr, Heldt HW (1976) Light-dependent changes of the Mg2+ concentration in the stroma in relation to the Mg2+ dependency of CO2 fixation in intact chloroplasts. Biochim Biophys Acta 449:434-436
    • (1976) Biochim Biophys Acta , vol.449 , pp. 434-436
    • Portis Jr., A.R.1    Heldt, H.W.2
  • 234
  • 237
    • 33751106422 scopus 로고    scopus 로고
    • Calcium entry mediated by GLR3.3, an Arabidopsis glutamate receptor with a broad agonist profile
    • Qi Z, Stephens NR, Spalding EP (2006) Calcium entry mediated by GLR3.3, an Arabidopsis glutamate receptor with a broad agonist profile. Plant Physiol 142:963-971
    • (2006) Plant Physiol , vol.142 , pp. 963-971
    • Qi, Z.1    Stephens, N.R.2    Spalding, E.P.3
  • 240
    • 0037173054 scopus 로고    scopus 로고
    • Reconstitution in yeast of the Arabidopsis SOS signaling pathway for Na+ homeostasis
    • Quintero FJ, Ohta M, Shi H, Zhu JK, Pardo JM (2002) Reconstitution in yeast of the Arabidopsis SOS signaling pathway for Na+ homeostasis. Proc Natl Acad Sci USA 99:9061-9066
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9061-9066
    • Quintero, F.J.1    Ohta, M.2    Shi, H.3    Zhu, J.K.4    Pardo, J.M.5
  • 243
    • 0001630250 scopus 로고
    • Calcium Requirement for Ethylene-Dependent Responses
    • Raz V, Fluhr R (1992) Calcium Requirement for Ethylene-Dependent Responses. Plant Cell 4:1123-1130
    • (1992) Plant Cell , vol.4 , pp. 1123-1130
    • Raz, V.1    Fluhr, R.2
  • 244
    • 0037155853 scopus 로고    scopus 로고
    • Genes encoding calmodulin-binding proteins in the Arabidopsis genome
    • Reddy VS, Ali GS, Reddy AS (2002) Genes encoding calmodulin-binding proteins in the Arabidopsis genome. J Biol Chem 277:9840-9852
    • (2002) J Biol Chem , vol.277 , pp. 9840-9852
    • Reddy, V.S.1    Ali, G.S.2    Reddy, A.S.3
  • 245
    • 3543003536 scopus 로고    scopus 로고
    • Oxidative stress-induced calcium signaling in Arabidopsis
    • Rentel MC, Knight MR (2004) Oxidative stress-induced calcium signaling in Arabidopsis. Plant Physiol 135:1471-1479
    • (2004) Plant Physiol , vol.135 , pp. 1471-1479
    • Rentel, M.C.1    Knight, M.R.2
  • 246
    • 0034037554 scopus 로고    scopus 로고
    • Resistance gene-dependent activation of a calcium dependent protein kinase in the plant defense response
    • Romeis T, Piedras P, Jones JD (2000) Resistance gene-dependent activation of a calcium dependent protein kinase in the plant defense response. Plant Cell 12:803-816
    • (2000) Plant Cell , vol.12 , pp. 803-816
    • Romeis, T.1    Piedras, P.2    Jones, J.D.3
  • 247
    • 0035886699 scopus 로고    scopus 로고
    • Calcium-dependent protein kinases play an essential role in a plant defence response
    • Romeis T, Ludwig AA, Martin R, Jones JD (2001) Calcium-dependent protein kinases play an essential role in a plant defence response. Embo J 20:5556-5567
    • (2001) Embo J , vol.20 , pp. 5556-5567
    • Romeis, T.1    Ludwig, A.A.2    Martin, R.3    Jones, J.D.4
  • 249
    • 0035983843 scopus 로고    scopus 로고
    • Dark-stimulated calcium ion fluxes in the chloroplast stroma and cytosol
    • Sai J, Johnson CH (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
  • 250
    • 0033624156 scopus 로고    scopus 로고
    • 2+- dependent protein kinase confers both cold and salt/drought tolerance on rice plants
    • 2+- dependent protein kinase confers both cold and salt/drought tolerance on rice plants. Plant J 23:319-327
    • (2000) Plant J , vol.23 , pp. 319-327
    • Saijo, Y.1    Hata, S.2    Kyozuka, J.3    Shimamoto, K.4    Izui, K.5
  • 251
    • 0027788911 scopus 로고
    • 2+ localization in the dividing cells of the maize root tip
    • 2+ localization in the dividing cells of the maize root tip. Cell Struct Funct 18:389-397
    • (1993) Cell Struct Funct , vol.18 , pp. 389-397
    • Sakai-Wada, A.1    Yagi, S.2
  • 252
    • 11844292846 scopus 로고    scopus 로고
    • The structure of the Arabidopsis thaliana SOS3: Molecular mechanism of sensing calcium for salt stress response
    • Sanchez-Barrena MJ, Martinez-Ripoll M, Zhu JK, Albert A (2005) The structure of the Arabidopsis thaliana SOS3: molecular mechanism of sensing calcium for salt stress response. J Mol Biol 345:1253-1264
    • (2005) J Mol Biol , vol.345 , pp. 1253-1264
    • Sanchez-Barrena, M.J.1    Martinez-Ripoll, M.2    Zhu, J.K.3    Albert, A.4
  • 253
    • 34247627317 scopus 로고    scopus 로고
    • The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3
    • Sanchez-Barrena MJ, Fujii H, Angulo I, Martinez-Ripoll M, Zhu JK, Albert A (2007) The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3. Mol Cell 26:427-435
    • (2007) Mol Cell , vol.26 , pp. 427-435
    • Sanchez-Barrena, M.J.1    Fujii, H.2    Angulo, I.3    Martinez-Ripoll, M.4    Zhu, J.K.5    Albert, A.6
  • 255
    • 0032146404 scopus 로고    scopus 로고
    • Unusual membrane-associated protein kinases in higher plants
    • Satterlee JS, Sussman MR (1998) Unusual membrane-associated protein kinases in higher plants. J Membr Biol 164:205-213
    • (1998) J Membr Biol , vol.164 , pp. 205-213
    • Satterlee, J.S.1    Sussman, M.R.2
  • 256
    • 0026576535 scopus 로고
    • Characterization of a calcium- and lipid dependent protein kinase associated with the plasma membrane of oat
    • Schaller GE, Harmon AC, Sussman MR (1992) Characterization of a calcium- and lipid dependent protein kinase associated with the plasma membrane of oat. Biochemistry 31:1721-1727
    • (1992) Biochemistry , vol.31 , pp. 1721-1727
    • Schaller, G.E.1    Harmon, A.C.2    Sussman, M.R.3
  • 259
    • 0039795372 scopus 로고
    • Cytosolic calcium regulates ion channels in the plasma membrane of Vicia faba guard cells
    • Schroeder JI, Hagiwara S (1989) Cytosolic calcium regulates ion channels in the plasma membrane of Vicia faba guard cells. Nature 338:427-430
    • (1989) Nature , vol.338 , pp. 427-430
    • Schroeder, J.I.1    Hagiwara, S.2
  • 260
    • 0023664149 scopus 로고
    • 2+ from vacuolar membrane vesicles of oat roots
    • 2+ from vacuolar membrane vesicles of oat roots. J Biol Chem 262:3944-3946
    • (1987) J Biol Chem , vol.262 , pp. 3944-3946
    • Schumaker, K.S.1    Sze, H.2
  • 263
    • 0026644789 scopus 로고
    • Cytosolic free calcium mediates red light induced photomorphogenesis
    • Shacklock PS, Read ND, Trewavas A (1992) Cytosolic free calcium mediates red light induced photomorphogenesis. Nature 358:753-755
    • (1992) Nature , vol.358 , pp. 753-755
    • Shacklock, P.S.1    Read, N.D.2    Trewavas, A.3
  • 265
    • 0033388972 scopus 로고    scopus 로고
    • Novel protein kinases associated with calcineurin B-like calcium sensors in Arabidopsis
    • Shi J, Kim KN, Ritz O, Albrecht V, Gupta R, Harter K, Luan S, Kudla J (1999) Novel protein kinases associated with calcineurin B-like calcium sensors in Arabidopsis. Plant Cell 11:2393-2405
    • (1999) Plant Cell , vol.11 , pp. 2393-2405
    • Shi, J.1    Kim, K.N.2    Ritz, O.3    Albrecht, V.4    Gupta, R.5    Harter, K.6    Luan, S.7    Kudla, J.8
  • 266
    • 33845363673 scopus 로고    scopus 로고
    • Identification of three distinct phylogenetic groups of CAX cation/proton antiporters
    • Shigaki T, Rees I, Nakhleh L, Hirschi KD (2006) Identification of three distinct phylogenetic groups of CAX cation/proton antiporters. J Mol Evol 63:815-825
    • (2006) J Mol Evol , vol.63 , pp. 815-825
    • Shigaki, T.1    Rees, I.2    Nakhleh, L.3    Hirschi, K.D.4
  • 267
    • 0036809394 scopus 로고    scopus 로고
    • A vacuolar sorting receptor PV72 on the membrane of vesicles that accumulate precursors of seed storage proteins (PAC vesicles)
    • Shimada T, Watanabe E, Tamura K, Hayashi Y, Nishimura M, Hara-Nishimura I (2002) A vacuolar sorting receptor PV72 on the membrane of vesicles that accumulate precursors of seed storage proteins (PAC vesicles). Plant Cell Physiol 43:1086-1095
    • (2002) Plant Cell Physiol , vol.43 , pp. 1086-1095
    • Shimada, T.1    Watanabe, E.2    Tamura, K.3    Hayashi, Y.4    Nishimura, M.5    Hara-Nishimura, I.6
  • 268
    • 84985417765 scopus 로고
    • The symptoms of calcium deficiency in plants
    • Simon EW (1978) The symptoms of calcium deficiency in plants. New Phytol 80:1-15
    • (1978) New Phytol , vol.80 , pp. 1-15
    • Simon, E.W.1
  • 269
    • 0033574009 scopus 로고    scopus 로고
    • Abscisic acid induces oscillations in guard-cell cytosolic free calcium that involve phosphoinositidespecific phospholipase C
    • Staxen II, Pical C, Montgomery LT, Gray JE, Hetherington AM, McAinsh MR (1999) Abscisic acid induces oscillations in guard-cell cytosolic free calcium that involve phosphoinositidespecific phospholipase C. Proc Natl Acad Sci USA 96:1779-1784
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1779-1784
    • Staxen, I.I.1    Pical, C.2    Montgomery, L.T.3    Gray, J.E.4    Hetherington, A.M.5    McAinsh, M.R.6
  • 270
    • 0037417812 scopus 로고    scopus 로고
    • Blue light activates calciumpermeable channels in Arabidopsis mesophyll cells via the phototropin signaling pathway
    • Stoelzle S, Kagawa T, Wada M, Hedrich R, Dietrich P (2003) Blue light activates calciumpermeable channels in Arabidopsis mesophyll cells via the phototropin signaling pathway. Proc Natl Acad Sci USA 100:1456-1461
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 1456-1461
    • Stoelzle, S.1    Kagawa, T.2    Wada, M.3    Hedrich, R.4    Dietrich, P.5
  • 271
    • 0024396312 scopus 로고
    • Crystal structures of the helix-loop-helix calcium binding proteins
    • Strynadka NC, James MN (1989) Crystal structures of the helix-loop-helix calcium binding proteins. Annu Rev Biochem 58:951-998
    • (1989) Annu Rev Biochem , vol.58 , pp. 951-998
    • Strynadka, N.C.1    James, M.N.2
  • 272
    • 0028674859 scopus 로고
    • Elevation of cytosolic calcium precedes anoxic gene expression in maize suspension-cultured cells
    • Subbaiah CC, Bush DS, Sachs MM (1994) Elevation of cytosolic calcium precedes anoxic gene expression in maize suspension-cultured cells. Plant Cell 6:1747-1762
    • (1994) Plant Cell , vol.6 , pp. 1747-1762
    • Subbaiah, C.C.1    Bush, D.S.2    Sachs, M.M.3
  • 274
    • 0029168714 scopus 로고
    • The effects of CaM on cell wall regeneration and cell division of protoplasts
    • Sun DY, Bian YQ, Zhao BH, Zhao LY (1995) The effects of CaM on cell wall regeneration and cell division of protoplasts. Plant Cell Physiol 36:133-138
    • (1995) Plant Cell Physiol , vol.36 , pp. 133-138
    • Sun, D.Y.1    Bian, Y.Q.2    Zhao, B.H.3    Zhao, L.Y.4
  • 281
    • 0032033745 scopus 로고    scopus 로고
    • Plasma membrane depolarization-activated calcium channels, stimulated by microtubule depolymerizing drugs in wild-type Arabidopsis thaliana protoplasts, display constitutively large activities and a longer half-life in ton 2 mutant cells affected in the organization of cortical microtubules
    • Thion L, Mazars C, Nacry P, Bouchez D, Moreau M, Ranjeva R, Thuleau P (1998) Plasma membrane depolarization-activated calcium channels, stimulated by microtubule depolymerizing drugs in wild-type Arabidopsis thaliana protoplasts, display constitutively large activities and a longer half-life in ton 2 mutant cells affected in the organization of cortical microtubules. Plant J 13:603-610
    • (1998) Plant J , vol.13 , pp. 603-610
    • Thion, L.1    Mazars, C.2    Nacry, P.3    Bouchez, D.4    Moreau, M.5    Ranjeva, R.6    Thuleau, P.7
  • 282
    • 0032868542 scopus 로고    scopus 로고
    • Le calcium, C'est la vie: Calcium makes waves
    • Trewavas A (1999) Le calcium, C'est la vie: calcium makes waves. Plant Physiol 120:1-6
    • (1999) Plant Physiol , vol.120 , pp. 1-6
    • Trewavas, A.1
  • 283
    • 66249109963 scopus 로고    scopus 로고
    • CIPK6, a CBL interacting protein kinase is required for development and salt tolerance in plant
    • Tripathi V, Parasuraman B, Laxmi A, Chattopadhyay D (2009) CIPK6, a CBL interacting protein kinase is required for development and salt tolerance in plant. Plant J 58:778-790
    • (2009) Plant J , vol.58 , pp. 778-790
    • Tripathi, V.1    Parasuraman, B.2    Laxmi, A.3    Chattopadhyay, D.4
  • 284
    • 0034633775 scopus 로고    scopus 로고
    • Arabidopsis basic leucine zipper transcription factors involved in an abscisic acid-dependent signal transduction pathway under drought and high-salinity conditions
    • Uno Y, Furihata T, Abe H, Yoshida R, Shinozaki K, Yamaguchi-Shinozaki K (2000) Arabidopsis basic leucine zipper transcription factors involved in an abscisic acid-dependent signal transduction pathway under drought and high-salinity conditions. Proc Natl Acad Sci USA 97:11632-11637
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 11632-11637
    • Uno, Y.1    Furihata, T.2    Abe, H.3    Yoshida, R.4    Shinozaki, K.5    Yamaguchi-Shinozaki, K.6
  • 287
    • 0033230738 scopus 로고    scopus 로고
    • Distinct calcium signaling pathways regulate calmodulin gene expression in tobacco
    • van Der Luit AH, Olivari C, Haley A, Knight MR, Trewavas AJ (1999) Distinct calcium signaling pathways regulate calmodulin gene expression in tobacco. Plant Physiol 121:705-714
    • (1999) Plant Physiol , vol.121 , pp. 705-714
    • van Der, L.A.H.1    Olivari, C.2    Haley, A.3    Knight, M.R.4    Trewavas, A.J.5
  • 288
    • 84981583887 scopus 로고
    • Redistribution of potassium, calcium, magnesium, and manganese in the plant
    • van Goor BJ, Wiersma D (1974) Redistribution of potassium, calcium, magnesium, and manganese in the plant. Physiol Plant 31:163-168
    • (1974) Physiol Plant , vol.31 , pp. 163-168
    • van Goor, B.J.1    Wiersma, D.2
  • 289
    • 0001569619 scopus 로고    scopus 로고
    • Second messengers mediate increases in cytosolic calcium in tobacco protoplasts
    • Volotovski ID, Sokolovsky SG, Molchan OV, Knight MR (1998) Second messengers mediate increases in cytosolic calcium in tobacco protoplasts. Plant Physiol 117:1023-1030
    • (1998) Plant Physiol , vol.117 , pp. 1023-1030
    • Volotovski, I.D.1    Sokolovsky, S.G.2    Molchan, O.V.3    Knight, M.R.4
  • 290
    • 0040126360 scopus 로고
    • X-ray microanalysis and chlorotetracycline staining of calcium vesicles in the green alg Mougeotia
    • Wagner G, Rossbacher R (1980) X-ray microanalysis and chlorotetracycline staining of calcium vesicles in the green alg Mougeotia. Planta 149:298-305
    • (1980) Planta , vol.149 , pp. 298-305
    • Wagner, G.1    Rossbacher, R.2
  • 292
    • 0037040987 scopus 로고    scopus 로고
    • Calciummediated association of a putative vacuolar sorting receptor PV72 with a propeptide of 2S albumin
    • Watanabe E, Shimada T, Kuroyanagi M, Nishimura M, Hara-Nishimura I (2002) Calciummediated association of a putative vacuolar sorting receptor PV72 with a propeptide of 2S albumin. J Biol Chem 277:8708-8715
    • (2002) J Biol Chem , vol.277 , pp. 8708-8715
    • Watanabe, E.1    Shimada, T.2    Kuroyanagi, M.3    Nishimura, M.4    Hara-Nishimura, I.5
  • 293
  • 294
    • 0031397713 scopus 로고    scopus 로고
    • Properties of Two Outward-Rectifying Channels in Root Xylem Parenchyma Cells Suggest a Role in K+ Homeostasis and Long-Distance Signaling
    • Wegner LH, De Boer AH (1997) Properties of Two Outward-Rectifying Channels in Root Xylem Parenchyma Cells Suggest a Role in K+ Homeostasis and Long-Distance Signaling. Plant Physiol 115:1707-1719
    • (1997) Plant Physiol , vol.115 , pp. 1707-1719
    • Wegner, L.H.1    de Boer, A.H.2
  • 296
    • 50349089617 scopus 로고    scopus 로고
    • 2+ signalling in plants and green algae-changing channels
    • 2+ 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
  • 299
    • 0018936475 scopus 로고
    • 2+-containing antimonate precipitates during mitosis
    • 2+-containing antimonate precipitates during mitosis. J Cell Biol 86:500-513
    • (1980) J Cell Biol , vol.86 , pp. 500-513
    • Wick, S.M.1    Hepler, P.K.2
  • 300
    • 37049121132 scopus 로고
    • The biochemistry of sodium, potassium, magnesium, and calcium
    • Williams RJP (1970) The biochemistry of sodium, potassium, magnesium, and calcium. Quart Rev Chem Soc 24:331-365
    • (1970) Quart Rev Chem Soc , vol.24 , pp. 331-365
    • Williams, R.J.P.1
  • 301
    • 3242781053 scopus 로고    scopus 로고
    • Signalling: Basics and evolution
    • Williams RJ (2004) Signalling: basics and evolution. Acta Biochim Pol 51:281-298
    • (2004) Acta Biochim Pol , vol.51 , pp. 281-298
    • Williams, R.J.1
  • 304
    • 5144224895 scopus 로고    scopus 로고
    • Isolated plant nuclei as mechanical and thermal sensors involved in calcium signalling
    • Xiong TC, Jauneau A, Ranjeva R, Mazars C (2004) Isolated plant nuclei as mechanical and thermal sensors involved in calcium signalling. Plant J 40:12-21
    • (2004) Plant J , vol.40 , pp. 12-21
    • Xiong, T.C.1    Jauneau, A.2    Ranjeva, R.3    Mazars, C.4
  • 305
    • 0031742853 scopus 로고    scopus 로고
    • Role of calcium in signal transduction during the hypersensitive response caused by basidiospore-derived infection of the cowpea rust fungus
    • Xu H, Heath MC (1998) Role of calcium in signal transduction during the hypersensitive response caused by basidiospore-derived infection of the cowpea rust fungus. Plant Cell 10:585-598
    • (1998) Plant Cell , vol.10 , pp. 585-598
    • Xu, H.1    Heath, M.C.2
  • 306
    • 33745251949 scopus 로고    scopus 로고
    • A protein kinase, interacting with two calcineurin B-like proteins, regulates K+ transporter AKT1 in Arabidopsis
    • Xu J, Li HD, Chen LQ, Wang Y, Liu LL, He L, Wu WH (2006) A protein kinase, interacting with two calcineurin B-like proteins, regulates K+ transporter AKT1 in Arabidopsis. Cell 125:1347-1360
    • (2006) Cell , vol.125 , pp. 1347-1360
    • Xu, J.1    Li, H.D.2    Chen, L.Q.3    Wang, Y.4    Liu, L.L.5    He, L.6    Wu, W.H.7
  • 308
    • 62549127319 scopus 로고    scopus 로고
    • Calcium-Dependent Freezing Tolerance in Arabidopsis Involves Membrane Resealing via Synaptotagmin SYT1
    • Yamazaki T, Kawamura Y, Minami A, Uemura M (2008) Calcium-Dependent Freezing Tolerance in Arabidopsis Involves Membrane Resealing via Synaptotagmin SYT1. Plant Cell 20:3389-3404
    • (2008) Plant Cell , vol.20 , pp. 3389-3404
    • Yamazaki, T.1    Kawamura, Y.2    Minami, A.3    Uemura, M.4
  • 309
    • 0142245708 scopus 로고    scopus 로고
    • Calcium/calmodulin-mediated signal network in plants
    • Yang T, Poovaiah BW (2003) Calcium/calmodulin-mediated signal network in plants. Trends Plant Sci 8:505-512
    • (2003) Trends Plant Sci , vol.8 , pp. 505-512
    • Yang, T.1    Poovaiah, B.W.2
  • 310
    • 33745471970 scopus 로고    scopus 로고
    • Calcium-dependent protein kinase isoforms in Petunia have distinct functions in pollen tube growth, including regulating polarity
    • Yoon GM, Dowd PE, Gilroy S, McCubbin AG (2006) Calcium-dependent protein kinase isoforms in Petunia have distinct functions in pollen tube growth, including regulating polarity. Plant Cell 18:867-878
    • (2006) Plant Cell , vol.18 , pp. 867-878
    • Yoon, G.M.1    Dowd, P.E.2    Gilroy, S.3    McCubbin, A.G.4
  • 311
    • 33646824849 scopus 로고    scopus 로고
    • The chimeric Arabidopsis CYCLIC NUCLEOTIDE-GATED ION CHANNEL11/12 activates multiple pathogen resistance responses
    • Yoshioka K, Moeder W, Kang HG, Kachroo P, Masmoudi K, Berkowitz G, Klessig DF (2006) The chimeric Arabidopsis CYCLIC NUCLEOTIDE-GATED ION CHANNEL11/12 activates multiple pathogen resistance responses. Plant Cell 18:747-763
    • (2006) Plant Cell , vol.18 , pp. 747-763
    • Yoshioka, K.1    Moeder, W.2    Kang, H.G.3    Kachroo, P.4    Masmoudi, K.5    Berkowitz, G.6    Klessig, D.F.7
  • 312
    • 0032560508 scopus 로고    scopus 로고
    • Gene-for-gene disease resistance without the hypersensitive response in Arabidopsis dnd1 mutant
    • Yu IC, Parker J, Bent AF (1998) Gene-for-gene disease resistance without the hypersensitive response in Arabidopsis dnd1 mutant. Proc Natl Acad Sci USA 95:7819-7824
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7819-7824
    • Yu, I.C.1    Parker, J.2    Bent, A.F.3


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