메뉴 건너뛰기




Volumn , Issue , 2007, Pages 141-182

Integration of Ca2+ in plant drought and salt stress signal transduction pathways

Author keywords

abiotic stress; calcium sensor; calcium signaling; signal transduction

Indexed keywords


EID: 79955636621     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-1-4020-5578-2_7     Document Type: Chapter
Times cited : (5)

References (205)
  • 1
    • 16644366650 scopus 로고    scopus 로고
    • OsCDPK13, a calcium-dependent protein kinase gene from rice, is induced by cold and gibberellin in rice leaf sheath
    • Abbasi, F., Onodera, H., Toki, S., Tanaka, H. and Komatsu, S. (2004). OsCDPK13, a calcium-dependent protein kinase gene from rice, is induced by cold and gibberellin in rice leaf sheath. Plant Mol. Biol. 55, 541-552.
    • (2004) Plant Mol. Biol. , vol.55 , pp. 541-552
    • Abbasi, F.1    Onodera, H.2    Toki, S.3    Tanaka, H.4    Komatsu, S.5
  • 6
    • 0033197614 scopus 로고    scopus 로고
    • Cameleon calcium indicator reports cytoplasmic calcium dynamics in Arabidopsis guard cells
    • Allen, G.J., Kwak, J.M., Chu, S.P., Llopis, J., Tsien, R.Y., Harper, J.F., and Schroeder, J.I. (1999). Cameleon calcium indicator reports cytoplasmic calcium dynamics in Arabidopsis guard cells. Plant J. 19, 735-747.
    • (1999) Plant J. , vol.19 , pp. 735-747
    • Allen, G.J.1    Kwak, J.M.2    Chu, S.P.3    Llopis, J.4    Tsien, R.Y.5    Harper, J.F.6    Schroeder, J.I.7
  • 7
    • 0034012321 scopus 로고    scopus 로고
    • A high-affinity calmodulin-binding site in a tobacco plasma-membrane channel protein coincides with a characteristic element of cyclic nucleotide-binding domains
    • Arazi, T., Kaplan, B., and Fromm, H. (2000). A high-affinity calmodulin-binding site in a tobacco plasma-membrane channel protein coincides with a characteristic element of cyclic nucleotide-binding domains. Plant Mol. Biol. 42, 591-601.
    • (2000) Plant Mol. Biol. , vol.42 , pp. 591-601
    • Arazi, T.1    Kaplan, B.2    Fromm, H.3
  • 9
    • 0034976968 scopus 로고    scopus 로고
    • Inventory of the superfamily of P-type ion pumps in Arabidopsis
    • Axelsen, K.B. and Palmgren, M.G. (2001). Inventory of the superfamily of P-type ion pumps in Arabidopsis. Plant Physiol. 126, 696-706.
    • (2001) Plant Physiol. , vol.126 , pp. 696-706
    • Axelsen, K.B.1    Palmgren, M.G.2
  • 11
    • 7044226261 scopus 로고    scopus 로고
    • Integration and channeling of calcium signaling through the CBL calcium sensor/CIPK protein kinase network
    • Batistic, O. and 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
  • 12
    • 0030983727 scopus 로고    scopus 로고
    • Cycloheximide induces a subset of low temperature-inducible genes in maize
    • Berberich, T. and Kusano, T. (1997). Cycloheximide induces a subset of low temperature-inducible genes in maize. Mol. Gen. Genet. 254, 275-283.
    • (1997) Mol. Gen. Genet. , vol.254 , pp. 275-283
    • Berberich, T.1    Kusano, T.2
  • 15
    • 0034068684 scopus 로고    scopus 로고
    • 2+ signalling and control of guard-cell volume in stomatal movements
    • 2+ signalling and control of guard-cell volume in stomatal movements. Curr. Opin. Plant Biol. 3, 196-204.
    • (2000) Curr. Opin. Plant Biol. , vol.3 , pp. 196-204
    • Blatt, M.R.1
  • 16
    • 84900759868 scopus 로고    scopus 로고
    • The cyclic nucleotide-gated calmodulin-binding channel AtCNGC10 localizes to the plasma membrane and influences numerous growth responses and starch accumulation in Arabidopsis thaliana
    • 2006 Aug 31 (Epub)
    • Borsics, T., Webb, D., Andeme-Ondzighi, C., Staehelin, L.A. and Christopher, D.A. (2006). The cyclic nucleotide-gated calmodulin-binding channel AtCNGC10 localizes to the plasma membrane and influences numerous growth responses and starch accumulation in Arabidopsis thaliana. Planta 2006 Aug 31 (Epub).
    • (2006) Planta
    • Borsics, T.1    Webb, D.2    Andeme-Ondzighi, C.3    Staehelin, L.A.4    Christopher, D.A.5
  • 17
    • 0030108468 scopus 로고    scopus 로고
    • Calcium-dependent protein kinase gene expression in response to physical and chemical stimuli in mungbean (Vigna radiata)
    • Botella, J.R., Arteca, J.M., Somodevilla, M. and Arteca, R.N. (1996). Calcium-dependent protein kinase gene expression in response to physical and chemical stimuli in mungbean (Vigna radiata). Plant Mol. Biol. 30, 1129-1137.
    • (1996) Plant Mol. Biol. , vol.30 , pp. 1129-1137
    • Botella, J.R.1    Arteca, J.M.2    Somodevilla, M.3    Arteca, R.N.4
  • 21
    • 0031251227 scopus 로고    scopus 로고
    • Two homologous low-temperature-inducible genes from Arabidopsis encode highly hydrophobic proteins
    • Capel, J., Jarillo, J.A., Salinas, J. and Martinez-Zapater, J.M. (1997). Two homologous low-temperature-inducible genes from Arabidopsis encode highly hydrophobic proteins. Plant Physiol. 115, 569-576.
    • (1997) Plant Physiol. , vol.115 , pp. 569-576
    • Capel, J.1    Jarillo, J.A.2    Salinas, J.3    Martinez-Zapater, J.M.4
  • 23
    • 0038797073 scopus 로고    scopus 로고
    • A cyclic nucleotide-gated ion channel, CNGC2, is crucial for plant development and adaptation to calcium stress
    • Chan, C.W., Schorrak, L.M., Smith, R.K. Jr., Bent, A.F. and Sussman, M.R. (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 Jr., R.K.3    Bent, A.F.4    Sussman, M.R.5
  • 25
    • 3543017369 scopus 로고    scopus 로고
    • Autophosphory-lation and subcellular localization dynamics of a salt-and water deficit-induced calcium-dependent protein kinase from ice plant
    • Chehab, E.W., Patharkar, O.R., Hegeman, A.D., Taybi, T. and Cushman, J.C. (2004). Autophosphory-lation and subcellular localization dynamics of a salt-and water deficit-induced calcium-dependent protein kinase from ice plant. Plant Physiol. 135, 1430-1446.
    • (2004) Plant Physiol. , vol.135 , pp. 1430-1446
    • Chehab, E.W.1    Patharkar, O.R.2    Hegeman, A.D.3    Taybi, T.4    Cushman, J.C.5
  • 26
    • 0037329942 scopus 로고    scopus 로고
    • The Arabidopsis cax1 mutant exhibits impaired ion homeostasis, development, and hormonal responses and reveals interplay among vacuolar transporters
    • Cheng, N.H., Pitman, J.K., Barkla, B.J., Shigaki, T. and Hirschi, K.D. (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    Pitman, J.K.2    Barkla, B.J.3    Shigaki, T.4    Hirschi, K.D.5
  • 30
    • 0035983609 scopus 로고    scopus 로고
    • Calcium signaling through protein kinases: The Arabidopsis calcium-dependent protein kinase gene family
    • Cheng, S., Willmann, M.R., Chen, H. and Sheen, J. (2002), 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.1    Willmann, M.R.2    Chen, H.3    Sheen, J.4
  • 31
    • 0041920602 scopus 로고    scopus 로고
    • CBL1, a calcium sensor that differentially regulates salt, drought, and cold responses in Arabidopsis
    • Cheong, Y.H., Kim, K.N., Pandey, G.K., Gupta, R., Grant, J.J. and 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
  • 32
    • 0034695679 scopus 로고    scopus 로고
    • ABFs, a family of ABA-responsive element binding factors
    • Choi, H., Hong, J., Ha, J., Kang, J. and Kim, S.Y. (2000). ABFs, a family of ABA-responsive element binding factors. J. Biol. Chem. 275, 1723-1730.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1723-1730
    • Choi, H.1    Hong, J.2    Ha, J.3    Kang, J.4    Kim, S.Y.5
  • 33
    • 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, H.I., Park, H.J., Park, J.H., Kim, S., Im, M.Y., Seo, H.H., Kim, Y.W., Hwang, I. and Kim, S.Y. (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
  • 35
    • 0028831997 scopus 로고
    • Calcium signaling
    • Clapham, D.E. (1995). Calcium signaling. Cell 80, 259-268.
    • (1995) Cell , vol.80 , pp. 259-268
    • Clapham, D.E.1
  • 36
    • 0034255488 scopus 로고    scopus 로고
    • The Arabidopsis dnd1 defense, no death gene encodes a mutated cyclic nucleotide-gated ion channel
    • Clough, S.J., Fengler, K.A., Yu, I.C., Lippok, B., Smith, R.K., and Bent, A.F. (2000). The Arabidopsis dnd1 "defense, no death" gene encodes a mutated cyclic nucleotide-gated ion channel. Proc. Natl. Acad. Sci. USA 97, 9323-9328.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9323-9328
    • Clough, S.J.1    Fengler, K.A.2    Yu, I.C.3    Lippok, B.4    Smith, R.K.5    Bent, A.F.6
  • 37
    • 0029149085 scopus 로고
    • Molecular and structural basis of target recognition by calmodulin
    • Crivici, A. and Ikura, M. (1995). Molecular and structural basis of target recognition by calmodulin. Annu. Rev. Biophys. Biomol. Struct. 24, 85-116.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 85-116
    • Crivici, A.1    Ikura, M.2
  • 38
    • 0242355632 scopus 로고    scopus 로고
    • Calcineurin signaling in Saccharomyces cerevisiae: How yeast go crazy in response to stress
    • Cyert, M.S. (2003). Calcineurin signaling in Saccharomyces cerevisiae: how yeast go crazy in response to stress. Biochem. Biophys. Res. Commun. 311, 1143-1150.
    • (2003) Biochem. Biophys. Res. Commun. , vol.311 , pp. 1143-1150
    • Cyert, M.S.1
  • 40
    • 0037163398 scopus 로고    scopus 로고
    • Analysis of EF-hand-containing proteins in Arabidopsis
    • Day, I., Reddy, V.S., Shad Ali, G. and Reddy, A.S.N. (2002). Analysis of EF-hand-containing proteins in Arabidopsis. Genome Biol. 3, 1-24.
    • (2002) Genome Biol. , vol.3 , pp. 1-24
    • Day, I.1    Reddy, V.S.2    Shad Ali, G.3    Reddy, A.S.N.4
  • 42
    • 0030799188 scopus 로고    scopus 로고
    • Structure and functions of annexins in plants
    • Delmer, D.P. and Potikha, T.S. (1997). Structure and functions of annexins in plants. Cell. Mol. Life Sci. 53, 546-553.
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 546-553
    • Delmer, D.P.1    Potikha, T.S.2
  • 44
    • 0037033784 scopus 로고    scopus 로고
    • 2+ release in yeast is triggered by hypertonic shock and mediated by a TRP channel homologue
    • 2+ release in yeast is triggered by hypertonic shock and mediated by a TRP channel homologue. J.Cell Biol. 156, 29-34.
    • (2002) J.Cell Biol. , vol.156 , pp. 29-34
    • Denis, V.1    Cyert, M.S.2
  • 46
    • 4444325076 scopus 로고    scopus 로고
    • 2+/calmodulin-binding proteins involved in transcriptional regulation: Interaction with fsh/Ring3 class transcription activators
    • 2+/calmodulin-binding proteins involved in transcriptional regulation: interaction with fsh/Ring3 class transcription activators. Plant Mol. Biol. 54, 549-569.
    • (2004) Plant Mol. Biol. , vol.54 , pp. 549-569
    • Du, L.1    Poovaiah, B.W.2
  • 47
    • 0026655047 scopus 로고
    • Depolarization of alfalfa root hair membrane potential by Rhizobium meliloti Nod factors
    • Ehrhardt, D.W., Atkinson, E.M. and Long, S.R. (1992). Depolarization of alfalfa root hair membrane potential by Rhizobium meliloti Nod factors. Science 256, 998-1000.
    • (1992) Science , vol.256 , pp. 998-1000
    • Ehrhardt, D.W.1    Atkinson, E.M.2    Long, S.R.3
  • 48
    • 0032999165 scopus 로고    scopus 로고
    • Cloning, expression and N-terminal myristoylation of CpCPK1, a calcium-dependent protein kinase from zucchini (Cucurbita pepo L.)
    • Ellard-Ivey, M., Hopkins, R.B., White, T. and Lomax, T.L. (1999). Cloning, expression and N-terminal myristoylation of CpCPK1, a calcium-dependent protein kinase from zucchini (Cucurbita pepo L.). Plant Mol. Biol. 39, 199-208.
    • (1999) Plant Mol. Biol. , vol.39 , pp. 199-208
    • Ellard-Ivey, M.1    Hopkins, R.B.2    White, T.3    Lomax, T.L.4
  • 50
    • 0032578026 scopus 로고    scopus 로고
    • P-type calcium ATPases in higher plants-biochemical, molecular and functional properties
    • Evans, D.E, and Williams, L.E. (1998). P-type calcium ATPases in higher plants-biochemical, molecular and functional properties. Biochim. Biophy. Acta. 1376, 1-25.
    • (1998) Biochim. Biophy. Acta. , vol.1376 , pp. 1-25
    • Evans, D.E.1    Williams, L.E.2
  • 52
    • 7144261208 scopus 로고
    • Auxin causes oscillations of cytosolic free calcium and pH in Zea mays coleoptiles
    • Felle, H. (1988). Auxin causes oscillations of cytosolic free calcium and pH in Zea mays coleoptiles. Planta 174, 495-499.
    • (1988) Planta , vol.174 , pp. 495-499
    • Felle, H.1
  • 56
    • 0034771863 scopus 로고    scopus 로고
    • Plant cells express several stress calcium ATPases but apparently no sodium ATPase
    • Garciadeblas, B., Benito, B. and Rodríguez-Navarro, A. (2001). Plant cells express several stress calcium ATPases but apparently no sodium ATPase. Plant Soil 235, 181-192.
    • (2001) Plant Soil , vol.235 , pp. 181-192
    • Garciadeblas, B.1    Benito, B.2    Rodríguez-Navarro, A.3
  • 57
  • 58
    • 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., and Palmgren, M.G. (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
  • 59
    • 0034652341 scopus 로고    scopus 로고
    • Elemental propagation of calcium signals in response-specific patterns determined by environmental stimulus strength
    • Goddard, H., Manison, N.F.H., Tomos, D., and Brownlee, C. (2000). Elemental propagation of calcium signals in response-specific patterns determined by environmental stimulus strength. Proc. Natl. Acad. Sci. USA 97, 1932-1937.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1932-1937
    • Goddard, H.1    Manison, N.F.H.2    Tomos, D.3    Brownlee, C.4
  • 60
    • 0037008783 scopus 로고    scopus 로고
    • Biochemical and functional characterization of PKS11, a novel Arabidopsis protein kinase
    • Gong, D., Gong, Z., Guo, Y., Chen, X. and Zhu, J.K. (2002c). Biochemical and functional characterization of PKS11, a novel Arabidopsis protein kinase. J. Biol. Chem. 277, 28340-28350.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28340-28350
    • Gong, D.1    Gong, Z.2    Guo, Y.3    Chen, X.4    Zhu, J.K.5
  • 61
    • 0036000036 scopus 로고    scopus 로고
    • Expression, activation, and biochemical properties of a novel Arabidopsis protein kinase
    • Gong, D., Gong, Z., Guo, Y. and Zhu, J.K. (2002b). Expression, activation, and biochemical properties of a novel Arabidopsis protein kinase. Plant Physiol. 129, 225-234.
    • (2002) Plant Physiol. , vol.129 , pp. 225-234
    • Gong, D.1    Gong, Z.2    Guo, Y.3    Zhu, J.K.4
  • 62
    • 0036740915 scopus 로고    scopus 로고
    • Biochemical characterization of the Arabidopsis protein kinase SOS2 that functions in salt tolerance
    • Gong, D., Guo, Y., Jagendorf, A.T. and Zhu, J.K. (2002a). Biochemical characterization of the Arabidopsis protein kinase SOS2 that functions in salt tolerance. Plant Physiol. 130, 256-264.
    • (2002) Plant Physiol. , vol.130 , pp. 256-264
    • Gong, D.1    Guo, Y.2    Jagendorf, A.T.3    Zhu, J.K.4
  • 63
    • 0032516044 scopus 로고    scopus 로고
    • 2+ increases with abscisic acid in stomatal guard cells
    • 2+ increases with abscisic acid in stomatal guard cells. Proc. Natl. Acad. Sci. USA 95, 4778-4783.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4778-4783
    • Grabov, A.1    Blatt, M.R.2
  • 64
    • 0032516044 scopus 로고    scopus 로고
    • 2+ increases with abscisic acid in stomatal guard cells
    • 2+ increases with abscisic acid in stomatal guard cells. Proc. Natl. Acad. Sci. USA 95, 4778-4783.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4778-4783
    • Grabov, A.1    Blatt, M.R.2
  • 66
    • 1042290710 scopus 로고    scopus 로고
    • Transgenic evaluation of activated mutant alleles of SOS2 reveals a critical requirement for its kinase activity and C-terminal regulatory domain for salt tolerance in Arabidopsis thaliana
    • Guo, Y., Qiu, Q., Quintero, F.J., Pardo, J.M., Ohta, M., Zhang, C., Schumaker, K.S. and Zhu, J.K. (2004). Transgenic evaluation of activated mutant alleles of SOS2 reveals a critical requirement for its kinase activity and C-terminal regulatory domain for salt tolerance in Arabidopsis thaliana. Plant Cell 16, 435-449.
    • (2004) Plant Cell , vol.16 , pp. 435-449
    • Guo, Y.1    Qiu, Q.2    Quintero, F.J.3    Pardo, J.M.4    Ohta, M.5    Zhang, C.6    Schumaker, K.S.7    Zhu, J.K.8
  • 67
    • 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., and Zhu, J.K. (2001). 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
  • 68
    • 0036696407 scopus 로고    scopus 로고
    • A calcium sensor and its interacting protein kinase are global regulators of abscisic acid signaling in Arabidopsis
    • Guo, Y., Xiong, L., Song, C.-P., Gong, D., Halfter, U., and Zhu, J.K. (2002). A calcium sensor and its interacting protein kinase are global regulators of abscisic acid signaling in Arabidopsis. Dev. Cell 3, 233-244.
    • (2002) Dev. Cell , vol.3 , pp. 233-244
    • Guo, Y.1    Xiong, L.2    Song, C.-P.3    Gong, D.4    Halfter, U.5    Zhu, J.K.6
  • 69
    • 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. and Zhu, J.K. (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
  • 71
    • 0028247009 scopus 로고
    • Pseudosubstrate inhibition of CDPK, a protein kinase with a calmodulin-like domain
    • Harmon, A.C., Yoo, B-C. and McCaffery, C. (1994). Pseudosubstrate inhibition of CDPK, a protein kinase with a calmodulin-like domain. Biochemistry 33, 7278-7287.
    • (1994) Biochemistry , vol.33 , pp. 7278-7287
    • Harmon, A.C.1    Yoo, B.-C.2    McCaffery, C.3
  • 74
    • 0034747345 scopus 로고    scopus 로고
    • 2+ transport: Who's directing the traffic?
    • 2+ transport: Who's directing the traffic? Trends Plant Sci. 6, 100-104.
    • (2001) Trends Plant Sci. , vol.6 , pp. 100-104
    • Hirschi, K.1
  • 75
    • 0033231267 scopus 로고    scopus 로고
    • Expression of Arabidopsis CAX1 in tobacco: Altered calcium homeostasis and increased stress sensitivity
    • Hirschi, K.D. (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
  • 77
    • 35448964846 scopus 로고    scopus 로고
    • Calcium-dependent protein kinases and their relatives
    • Hrabak, E.M. (2000). Calcium-dependent protein kinases and their relatives. Adv. Bot. Res. 32, 185-223.
    • (2000) Adv. Bot. Res. , vol.32 , pp. 185-223
    • Hrabak, E.M.1
  • 78
    • 0344496699 scopus 로고    scopus 로고
    • Functional interaction of calmodulin with a plant cyclic nucleotide gated cation channel
    • Hua, B.G., Mercier, R.W., Zielinski, R.E., Berkowitz, G.A. (2003). 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
  • 79
    • 1842788502 scopus 로고    scopus 로고
    • A tobacco calmodulin-binding protein kinase (NtCBK2) induced by high-salt/GA treatment and its expression during floral development and embryogenesis
    • Hua, W., Li, R.J., Wang, L. and Lu, Y.T. (2004). A tobacco calmodulin-binding protein kinase (NtCBK2) induced by high-salt/GA treatment and its expression during floral development and embryogenesis. Plant Sci. 166, 1253-1259.
    • (2004) Plant Sci. , vol.166 , pp. 1253-1259
    • Hua, W.1    Li, R.J.2    Wang, L.3    Lu, Y.T.4
  • 80
    • 27244437132 scopus 로고    scopus 로고
    • A gibberellin-regulated calcineurin B in rice localizes to the tonoplast and is implicated in vacuole function
    • Hwang, Y.S., Bethke, P.C., Cheong, Y.H., Chang, H.S., Zhu, T. and Jones, R.L. (2005). A gibberellin-regulated calcineurin B in rice localizes to the tonoplast and is implicated in vacuole function. Plant Physiol. 138, 1347-1358.
    • (2005) Plant Physiol. , vol.138 , pp. 1347-1358
    • Hwang, Y.S.1    Bethke, P.C.2    Cheong, Y.H.3    Chang, H.S.4    Zhu, T.5    Jones, R.L.6
  • 81
    • 0033793156 scopus 로고    scopus 로고
    • SOS3 function in plant salt tolerance requires N-myristoylation and calcium-binding
    • Ishitani, M., Liu, J., Halfter, U., Kim, C.-S., Shi, W., and Zhu, J.K. (2000). SOS3 function in plant salt tolerance requires N-myristoylation and calcium-binding. Plant Cell 12, 1667-1677.
    • (2000) Plant Cell , vol.12 , pp. 1667-1677
    • Ishitani, M.1    Liu, J.2    Halfter, U.3    Kim, C.-S.4    Shi, W.5    Zhu, J.K.6
  • 82
    • 3142700162 scopus 로고    scopus 로고
    • Evidence for differing roles for each lobe of the calmodulin-like domain in a calcium-dependent protein kinase
    • Christodoulou, J., Malmendal, A., Harper, J.F. and Chazin, W.J. (2004). Evidence for differing roles for each lobe of the calmodulin-like domain in a calcium-dependent protein kinase, J. Biol. Chem. 279, 29092-29100.
    • (2004) J. Biol. Chem. , vol.279 , pp. 29092-29100
    • Christodoulou, J.1    Malmendal, A.2    Harper, J.F.3    Chazin, W.J.4
  • 83
    • 0028464370 scopus 로고
    • Two related low-temperature-inducible genes of Arabidopsis encode proteins showing high homology to 14-3-3 proteins, a family of putative kinase regulators
    • Jarillo, J.A., Capel, J., Leyva, A., Martinez-Zapater, J.M. and Salinas, J. (1994). Two related low-temperature-inducible genes of Arabidopsis encode proteins showing high homology to 14-3-3 proteins, a family of putative kinase regulators. Plant Mol. Biol. 25, 693-704.
    • (1994) Plant Mol. Biol. , vol.25 , pp. 693-704
    • Jarillo, J.A.1    Capel, J.2    Leyva, A.3    Martinez-Zapater, J.M.4    Salinas, J.5
  • 84
    • 0036779407 scopus 로고    scopus 로고
    • Complexity, cross talk and integration of plant MAP kinase signaling
    • Jonak, C., Okresz L., Bogre L. and Hirt, H. (2002). complexity, cross talk and integration of plant MAP kinase signaling. Curr. Opin. Plant Biol. 5, 415-424.
    • (2002) Curr. Opin. Plant Biol. , vol.5 , pp. 415-424
    • Jonak, C.1    Okresz, L.2    Bogre, L.3    Hirt, H.4
  • 85
    • 0036301043 scopus 로고    scopus 로고
    • Cyclic nucleotide-gated ion channels
    • Kaupp, U.B. and Seifert, R. (2002). Cyclic nucleotide-gated ion channels. Physiol. Rev. 82, 769-824.
    • (2002) Physiol. Rev. , vol.82 , pp. 769-824
    • Kaupp, U.B.1    Seifert, R.2
  • 87
    • 0034522759 scopus 로고    scopus 로고
    • Interaction specificity of Arabidopsis calcineurin B-like calcium sensors and their target kinases
    • Kim, K.N., Cheong, Y.H., Gupta, R. and Luan, S. (2000). Interaction specificity of Arabidopsis calcineurin B-like calcium sensors and their target kinases. Plant Physiol. 124, 1844-1853.
    • (2000) Plant Physiol. , vol.124 , pp. 1844-1853
    • Kim, K.N.1    Cheong, Y.H.2    Gupta, R.3    Luan, S.4
  • 88
    • 0342749255 scopus 로고    scopus 로고
    • Characterisation of calmodulin binding to cyclic nucleotide-gated ion channels from Arabidopsis thaliana
    • Kohler, C., and Neuhaus, G. (2000). Characterisation of calmodulin binding to cyclic nucleotide-gated ion channels from Arabidopsis thaliana. FEBS Lett. 471, 133-136.
    • (2000) FEBS Lett. , vol.471 , pp. 133-136
    • Kohler, C.1    Neuhaus, G.2
  • 89
    • 0037693763 scopus 로고    scopus 로고
    • Gelsolin domains 4-6 in active, actin-free conformation identifies sites of regulatory calcium ions
    • Kolappan, S., Gooch, J.T., Weeds, A.G. and McLaughlin, P.J. (2003). Gelsolin domains 4-6 in active, actin-free conformation identifies sites of regulatory calcium ions. J. Mol. Biol. 329, 85-92.
    • (2003) J. Mol. Biol. , vol.329 , pp. 85-92
    • Kolappan, S.1    Gooch, J.T.2    Weeds, A.G.3    McLaughlin, P.J.4
  • 90
    • 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. and 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
  • 91
    • 0035745741 scopus 로고    scopus 로고
    • Modulation of cyclic-nucleotide-gated channels and regulation of vertebrate phototransduction
    • Kramer, R.H, and Molokanova, E. (2001). Modulation of cyclic-nucleotide-gated channels and regulation of vertebrate phototransduction. J. Exp. Biol. 204, 2921-2931.
    • (2001) J. Exp. Biol. , vol.204 , pp. 2921-2931
    • Kramer, R.H.1    Molokanova, E.2
  • 92
    • 0015919772 scopus 로고
    • Carp muscle calcium-binding protein. II. Structure determination and general description
    • Kretsinger, R.H. and Nockolds, C.E. (1973). Carp muscle calcium-binding protein. II. Structure determination and general description. J. Biol. Chem. 248, 3313-3326.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3313-3326
    • Kretsinger, R.H.1    Nockolds, C.E.2
  • 93
    • 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. and 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
  • 94
    • 20244374796 scopus 로고    scopus 로고
    • The identity of plant glutamate receptors
    • Lacombe, B., et al. (2001). The identity of plant glutamate receptors. Science 292, 1486-1487.
    • (2001) Science , vol.292 , pp. 1486-1487
    • Lacombe, B.1
  • 95
    • 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. and 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
  • 96
    • 0032510705 scopus 로고    scopus 로고
    • Kinetic and calcium-binding properties of three calcium-dependent protein kinase isoenzymes from soybean
    • Lee, J-Y., Yoo, B-C. and Harmon, A.C. (1998). Kinetic and calcium-binding properties of three calcium-dependent 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
  • 97
    • 0028339956 scopus 로고
    • Arabidopsis ABA response gene ABI1: Features of a calcium-modulated protein phosphatase
    • Leung, J., Bouvier-Durand, M., Morris, P.C., Guerrier, D., Chefdor, F. and Giraudat, J. (1994). Arabidopsis ABA response gene ABI1: features of a calcium-modulated protein phosphatase. Science 264, 1448-1452.
    • (1994) Science , vol.264 , pp. 1448-1452
    • Leung, J.1    Bouvier-Durand, M.2    Morris, P.C.3    Guerrier, D.4    Chefdor, F.5    Giraudat, J.6
  • 98
    • 0034964668 scopus 로고    scopus 로고
    • Time course of cell biological events evoked in legume root hairs by Rhizobium Nod factors: State of the art
    • Lhuissier, F.G.P., De Ruijter, N.C.A., Sieberer, B.J., Esseling, J.J. and Emons, A.M.C. (2001). Time course of cell biological events evoked in legume root hairs by Rhizobium Nod factors: state of the art. Ann. Bot. 87, 289-302.
    • (2001) Ann. Bot. , vol.87 , pp. 289-302
    • Lhuissier, F.G.P.1    De Ruijter, N.C.A.2    Sieberer, B.J.3    Esseling, J.J.4    Emons, A.M.C.5
  • 100
    • 23844442496 scopus 로고    scopus 로고
    • Arabidopsis AtCNGC10 rescues potassium channel mutants of E. coli, yeast and Arabidopsis and is regulated by calcium/calmodulin and cyclic GMP in E. coli
    • Li, X-L., Borsics, T., Harrington, H.M. and Christopher, D.A. (2005). Arabidopsis AtCNGC10 rescues potassium channel mutants of E. coli, yeast and Arabidopsis and is regulated by calcium/calmodulin and cyclic GMP in E. coli. Funct. Plant Biol. 32, 643-653.
    • (2005) Funct. Plant Biol. , vol.32 , pp. 643-653
    • Li, X.-L.1    Borsics, T.2    Harrington, H.M.3    Christopher, D.A.4
  • 101
    • 0030063768 scopus 로고    scopus 로고
    • Differential stimulation of NAD kinase and binding of peptide substrates by wild-type and mutant plant calmodulin isoforms
    • Liao, B., Gawienowski, M.C. and Zielinski, R.E. (1996). Differential stimulation of NAD kinase and binding of peptide substrates by wild-type and mutant plant calmodulin isoforms. Archives of Biochemistry and Biphysics 327, 53-60.
    • (1996) Archives of Biochemistry and Biphysics , vol.327 , pp. 53-60
    • Liao, B.1    Gawienowski, M.C.2    Zielinski, R.E.3
  • 102
    • 0027597441 scopus 로고
    • Isolation of an Arabidopsis cDNA sequence encoding a 22 kDa calcium-binding protein (CaBP-22) related to calmodulin
    • Ling, V. and Zielinski, R.E. (1993). Isolation of an Arabidopsis cDNA sequence encoding a 22 kDa calcium-binding protein (CaBP-22) related to calmodulin. Plant Mol. Biol.22, 207-214.
    • (1993) Plant Mol. Biol. , vol.22 , pp. 207-214
    • Ling, V.1    Zielinski, R.E.2
  • 103
    • 0031153925 scopus 로고    scopus 로고
    • Proline accumulation and salt-stress-induced gene expression in a salt-hypersensitive mutant of Arabidopsis
    • Liu, J. and Zhu, J.-K. (1997). Proline accumulation and salt-stress-induced gene expression in a salt-hypersensitive mutant of Arabidopsis. Plant Physiol. 114, 591-596.
    • (1997) Plant Physiol. , vol.114 , pp. 591-596
    • Liu, J.1    Zhu, J.-K.2
  • 104
    • 0032546821 scopus 로고    scopus 로고
    • A calcium sensor homolog required for plant salt tolerance
    • Liu, J. and Zhu, J.-K. (1998). A calcium sensor homolog required for plant salt tolerance. Science 280, 1943-1945.
    • (1998) Science , vol.280 , pp. 1943-1945
    • Liu, J.1    Zhu, J.-K.2
  • 105
    • 0034724210 scopus 로고    scopus 로고
    • The Arabidopsis thaliana SOS2 gene encodes a protein kinase that is required for salt tolerance
    • Liu, J., Ishitani, M., Halfter, U., Kim, C.-S. and Zhu, J.K. (2000). The Arabidopsis thaliana SOS2 gene encodes a protein kinase that is required for salt tolerance. Proc. Natl. Acad. Sci. USA 97, 3730-3734.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3730-3734
    • Liu, J.1    Ishitani, M.2    Halfter, U.3    Kim, C.-S.4    Zhu, J.K.5
  • 106
    • 0036793334 scopus 로고    scopus 로고
    • A novel cold-inducible gene from Arabidopsis, RCI3, encodes a peroxidase that constitutes a component for stress tolerance
    • Llorente, F., Lopez-Cobollo, R.M., Catala, R., Martinez-Zapater, J.M. and Salinas, J. (2002). A novel cold-inducible gene from Arabidopsis, RCI3, encodes a peroxidase that constitutes a component for stress tolerance. Plant J. 32, 13-24.
    • (2002) Plant J. , vol.32 , pp. 13-24
    • Llorente, F.1    Lopez-Cobollo, R.M.2    Catala, R.3    Martinez-Zapater, J.M.4    Salinas, J.5
  • 107
    • 0036006051 scopus 로고    scopus 로고
    • An Arabidopsis calcium-dependent protein kinase is associated with the endoplasmic reticulum
    • Lu, S.X. and Hrabak, E.M. (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
  • 109
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin, Nature Struct
    • Zhang, M., Tanaka, T. and Ikura, M. (1995). Calcium-induced conformational transition revealed by the solution structure of apo calmodulin, Nature Struct. Biol. 2, 758-767.
    • (1995) Biol. , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3
  • 110
    • 0038714319 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase cascades in plants: A new nomenclature
    • (Ichimura et al.,)
    • MAPK Group (Ichimura et al.,) (2002). Mitogen-activated protein kinase cascades in plants: a new nomenclature. Trends Plant Sci. 7, 301-308.
    • (2002) Trends Plant Sci. , vol.7 , pp. 301-308
  • 111
    • 0034548365 scopus 로고    scopus 로고
    • Membrane localization of a rice calcium-dependent protein kinase (CDPK) is mediated by myristoylation and palmitoylation
    • Martin, M. and 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.1    Busconi, L.2
  • 112
    • 0037853748 scopus 로고    scopus 로고
    • Phylogenetic relationships within cation transporter families of Arabidopsis
    • Maser, P., et al. (2001). Phylogenetic relationships within cation transporter families of Arabidopsis. Plant Physiol. 126, 1646-1667.
    • (2001) Plant Physiol. , vol.126 , pp. 1646-1667
    • Maser, P.1
  • 113
    • 0031451194 scopus 로고    scopus 로고
    • Tcn1p/Crz1p, a calcineurin-dependent transcription factor that differentially regulates gene expression in Saccharomyces cerevisiae
    • Matheos, D.P., Kingsbury, T.J., Ahsan, U.S. and Cunningham, K.W. (1997). Tcn1p/Crz1p, a calcineurin-dependent transcription factor that differentially regulates gene expression in Saccharomyces cerevisiae. Genes Dev. 11, 3445-3458.
    • (1997) Genes Dev. , vol.11 , pp. 3445-3458
    • Matheos, D.P.1    Kingsbury, T.J.2    Ahsan, U.S.3    Cunningham, K.W.4
  • 114
    • 0028812274 scopus 로고
    • Stimulus-induced oscillations in guard cell cytoplasmic free calcium
    • McAinsh, M.R., Webb, A.A.R., Taylor, J.E., and Hetherington, A.M. (1995). Stimulus-induced oscillations in guard cell cytoplasmic free calcium. Plant Cell 7, 1207-1219.
    • (1995) Plant Cell , vol.7 , pp. 1207-1219
    • McAinsh, M.R.1    Webb, A.A.R.2    Taylor, J.E.3    Hetherington, A.M.4
  • 115
    • 0042466588 scopus 로고    scopus 로고
    • Calmodulins and related potential calcium sensors in Arabidopsis
    • McCormack, E. and Braam, J. (2003). Calmodulins and related potential calcium sensors in Arabidopsis. New Phytol. 159, 585-598.
    • (2003) New Phytol. , vol.159 , pp. 585-598
    • McCormack, E.1    Braam, J.2
  • 116
    • 23044471508 scopus 로고    scopus 로고
    • Handling calcium signaling: Arabidopsis CaMs and CMLs
    • McCormack, E., Tsai, Y.C. and 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
  • 117
    • 0028286249 scopus 로고
    • The protein phosphatase calcineurin is essential for NaCl tolerance of Saccharomyces cerevisiae
    • Mendoza, I., Rubio, F., Rodriguez-Navarro, A. and Pardo, J.M. (1994). The protein phosphatase calcineurin is essential for NaCl tolerance of Saccharomyces cerevisiae. J. Biol. Chem. 269, 8792-8796.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8792-8796
    • Mendoza, I.1    Rubio, F.2    Rodriguez-Navarro, A.3    Pardo, J.M.4
  • 118
    • 33745193104 scopus 로고    scopus 로고
    • The Arabidopsis AtDi19 gene family encodes a novel type of Cys2/His2 zinc-finger protein implicated in ABA-independent dehydration, high-salinity stress and light signaling pathways
    • Milla, M.A., Townsend, J., Chang, I.F. and Cushman, J.C. (2006). The Arabidopsis AtDi19 gene family encodes a novel type of Cys2/His2 zinc-finger protein implicated in ABA-independent dehydration, high-salinity stress and light signaling pathways. Plant Mol. Biol. 61, 13-30.
    • (2006) Plant Mol. Biol. , vol.61 , pp. 13-30
    • Milla, M.A.1    Townsend, J.2    Chang, I.F.3    Cushman, J.C.4
  • 119
    • 0029039937 scopus 로고
    • The dynamic role of palmitoylation in signal trans-duction
    • Milligan, G., Parenti, M. and Magee, A.I. (1995). The dynamic role of palmitoylation in signal trans-duction. Trends Biol. Sci. 20, 181-186.
    • (1995) Trends Biol. Sci. , vol.20 , pp. 181-186
    • Milligan, G.1    Parenti, M.2    Magee, A.I.3
  • 120
    • 0029257293 scopus 로고
    • Low-temperature signal transduction: Induction of cold acclimation-specific genes of alfalfa by calcium at 25 C
    • Monroy, A.F. and Dhindsa, R.S. (1995). Low-temperature signal transduction: induction of cold acclimation-specific genes of alfalfa by calcium at 25 C. Plant Cell 7, 321-331.
    • (1995) Plant Cell , vol.7 , pp. 321-331
    • Monroy, A.F.1    Dhindsa, R.S.2
  • 121
    • 0035209746 scopus 로고    scopus 로고
    • 2+ channels in guard cells requires cytosolic NAD(P)H and is differentially disrupted upstream and downstream of reactive oxygen species production in abi1-1 and abi2-1 protein phosphatase 2C mutants
    • 2+ channels in guard cells requires cytosolic NAD(P)H and is differentially disrupted upstream and downstream of reactive oxygen species production in abi1-1 and abi2-1 protein phosphatase 2C mutants. Plant Cell 13, 2513-2523.
    • (2001) Plant Cell , vol.13 , pp. 2513-2523
    • Murata, Y.1    Pei, Z.M.2    Mori, I.C.3    Schroeder, J.4
  • 122
    • 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. and 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
  • 123
    • 0027385382 scopus 로고
    • Protein phosphatase type 2B (calcineurin)-mediated, FK506-sensitive regulation of intracellular ions in yeast is an important determinant for adaptation to high salt stress conditions
    • Nakamura, T., Liu, Y., Hirata, D., Namba, H., Harada, S., Hirokawa, T. and Miyakawa, T. (1993). Protein phosphatase type 2B (calcineurin)-mediated, FK506-sensitive regulation of intracellular ions in yeast is an important determinant for adaptation to high salt stress conditions. EMBO J. 12, 4063-4071.
    • (1993) EMBO J. , vol.12 , pp. 4063-4071
    • Nakamura, T.1    Liu, Y.2    Hirata, D.3    Namba, H.4    Harada, S.5    Hirokawa, T.6    Miyakawa, T.7
  • 124
    • 0035967125 scopus 로고    scopus 로고
    • Drought-induced guard cell signal transduction involves sphingosine-1-phosphate
    • Ng, C.K.Y., Carr, K., McAinsh, M.R., Powell, B., and Hetherington, A.M. (2001). Drought-induced guard cell signal transduction involves sphingosine-1-phosphate. Nature 410, 596-598.
    • (2001) Nature , vol.410 , pp. 596-598
    • Ng, C.K.Y.1    Carr, K.2    McAinsh, M.R.3    Powell, B.4    Hetherington, A.M.5
  • 125
    • 0034787999 scopus 로고    scopus 로고
    • An Arabidopsis SNF1-related protein kinase, AtSR1, interacts with a calcium-binding protein, AtCBL2, of which transcripts respond to light
    • Nozawa, A., Koizumi, N. and Sano, H. (2001). An Arabidopsis SNF1-related protein kinase, AtSR1, interacts with a calcium-binding protein, AtCBL2, of which transcripts respond to light. Plant Cell Physiol. 42:976-981.
    • (2001) Plant Cell Physiol. , vol.42 , pp. 976-981
    • Nozawa, A.1    Koizumi, N.2    Sano, H.3
  • 126
    • 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. and Zhu, J.K. (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
  • 127
    • 0036749309 scopus 로고    scopus 로고
    • 2+ and membrane potential during hypotonic turgor regulation in a brackish water Charophyte Lampro-thamnium succinctum
    • 2+ and membrane potential during hypotonic turgor regulation in a brackish water Charophyte Lampro-thamnium succinctum. Plant Cell Physiol. 43, 1027-1035.
    • (2002) Plant Cell Physiol. , vol.43 , pp. 1027-1035
    • Okazaki, Y.1    Ishigami, M.2    Iwasaki, N.3
  • 129
    • 0034517719 scopus 로고    scopus 로고
    • A stress-inducible calcium-dependent protein kinase from Mesembryanthemum crystallinum phosphorylates a two-component pseudo-response regulator
    • Patharkar, O.R. and Cushman, J.C. (2000) A stress-inducible calcium-dependent protein kinase from Mesembryanthemum crystallinum phosphorylates a two-component pseudo-response regulator. Plant J. 24, 679-691.
    • (2000) Plant J. , vol.24 , pp. 679-691
    • Patharkar, O.R.1    Cushman, J.C.2
  • 130
    • 33750988242 scopus 로고    scopus 로고
    • A novel coiled-coil protein co-localizes and interacts with a calcium-dependent protein kinase in the common ice plant during low-humidity stress
    • Jun 14 (Epub)
    • Patharkar, O.R. and Cushman, J.C. (2006). A novel coiled-coil protein co-localizes and interacts with a calcium-dependent protein kinase in the common ice plant during low-humidity stress. Planta Jun 14 (Epub).
    • (2006) Planta
    • Patharkar, O.R.1    Cushman, J.C.2
  • 131
    • 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, M.R., Thuleau, P., Graziana, A., Muto, S., Ranjeva, R., and 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
  • 132
    • 0034680090 scopus 로고    scopus 로고
    • Calcium channels activated by hydrogen peroxide mediate abscisic acid signalling in guard cells
    • Pei, Z.M., Murata, Y., Benning, G., Thomine, S., Klusener, B., Allen, G.J., Grill, E., and Schroeder, J.I. (2000). Calcium channels activated by hydrogen peroxide mediate abscisic acid signalling in guard cells. Nature 406, 731-734.
    • (2000) Nature , vol.406 , pp. 731-734
    • Pei, Z.M.1    Murata, Y.2    Benning, G.3    Thomine, S.4    Klusener, B.5    Allen, G.J.6    Grill, E.7    Schroeder, J.I.8
  • 133
    • 0032710213 scopus 로고    scopus 로고
    • Magnesium sensitizes slow vacuolar channels to physiological cytosolic calcium and inhibits fast vacuolar channels in fava bean guard cell vacuoles
    • Pei, Z.M., Ward, J.M., and Schroeder, J.I. (1999). Magnesium sensitizes slow vacuolar channels to physiological cytosolic calcium and inhibits fast vacuolar channels in fava bean guard cell vacuoles. Plant Physiol. 121, 977-986.
    • (1999) Plant Physiol. , vol.121 , pp. 977-986
    • Pei, Z.M.1    Ward, J.M.2    Schroeder, J.I.3
  • 134
    • 0026892430 scopus 로고
    • Structure and expression of the Arabidopsis CaM-3 calmodulin gene
    • Perera, I.Y. and Zielinski, R.E. (1992). Structure and expression of the Arabidopsis CaM-3 calmodulin gene. Plant Mol. Biol. 19, 649-664.
    • (1992) Plant Mol. Biol. , vol.19 , pp. 649-664
    • Perera, I.Y.1    Zielinski, R.E.2
  • 136
    • 2342559182 scopus 로고    scopus 로고
    • A novel calmodulin-binding protein functions as a negative regulator of osmotic stress tolerance in Arabidopsis thaliana seedlings
    • Perruc, E., Charpenteau, M., Ramirez, B.C., Jauneau, A., Galaud, J.P. et al. (2004). A novel calmodulin-binding protein functions as a negative regulator of osmotic stress tolerance in Arabidopsis thaliana seedlings. Plant J. 38, 410-420.
    • (2004) Plant J. , vol.38 , pp. 410-420
    • Perruc, E.1    Charpenteau, M.2    Ramirez, B.C.3    Jauneau, A.4    Galaud, J.P.5
  • 137
    • 29844452097 scopus 로고    scopus 로고
    • Calcium signaling-mediated and differential induction of calmodulin gene expression by stress in Oryza sativa L
    • Phean-O-Pas, S., Punteeranurak, P. and Buaboocha, T. (2005). Calcium signaling-mediated and differential induction of calmodulin gene expression by stress in Oryza sativa L. J. Biochem. Mol. Biol. 38, 432-439.
    • (2005) J. Biochem. Mol. Biol. , vol.38 , pp. 432-439
    • Phean-O-Pas, S.1    Punteeranurak, P.2    Buaboocha, T.3
  • 139
    • 0035201584 scopus 로고    scopus 로고
    • + antiporter. Identification of an N-terminal autoinhibitory domain
    • + antiporter. Identification of an N-terminal autoinhibitory domain. Plant Physiol. 127, 1020-1029.
    • (2001) Plant Physiol. , vol.127 , pp. 1020-1029
    • Pittman, J.K.1    Hirschi, K.D.2
  • 143
    • 0037155853 scopus 로고    scopus 로고
    • Genes encoding calmodulin-binding proteins in the Arabidopsis genome
    • Reddy, V.S., Ali, G.S. and Reddy, A.S.N. (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.N.3
  • 144
    • 3242768512 scopus 로고    scopus 로고
    • Proteomics of calcium-signaling components in plants
    • Reddy, V.S. and Reddy, A.S.N. (2004). Proteomics of calcium-signaling components in plants. Phyto-chemistry 65, 1745-1776.
    • (2004) Phyto-chemistry , vol.65 , pp. 1745-1776
    • Reddy, V.S.1    Reddy, A.S.N.2
  • 145
    • 0033615738 scopus 로고    scopus 로고
    • Interaction of a kinesin-like protein with calmodulin isoforms from Arabidopsis
    • Reddy, V.S., Safadi, F., Zielinski, R.E. and Reddy, A.S.N. (1999). Interaction of a kinesin-like protein with calmodulin isoforms from Arabidopsis. J. Biol. Chem. 274, 31727-31733.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31727-31733
    • Reddy, V.S.1    Safadi, F.2    Zielinski, R.E.3    Reddy, A.S.N.4
  • 146
    • 3543003536 scopus 로고    scopus 로고
    • Oxidative stress-induced calcium signaling in Arabidopsis
    • Rentel, M.C. and Knight, M.R. (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
  • 147
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh, M.D. (1999). Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta 1451, 1-16.
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 150
    • 0033779701 scopus 로고    scopus 로고
    • Calcineurin: Form and function
    • Rusnak, F. and Mertz, P. (2000). Calcineurin: form and function. Physiol. Rev. 80, 1483-1521.
    • (2000) Physiol. Rev. , vol.80 , pp. 1483-1521
    • Rusnak, F.1    Mertz, P.2
  • 151
    • 0034954408 scopus 로고    scopus 로고
    • Superoxide production by plant homologues of the gp91(phox) NADPH oxidase. Modulation of activity by calcium and by tobacco mosaic virus infection
    • Sagi, M. and Fluhr, R. (2001). Superoxide production by plant homologues of the gp91(phox) NADPH oxidase. Modulation of activity by calcium and by tobacco mosaic virus infection. Plant Physiol. 126, 1281-1290.
    • (2001) Plant Physiol. , vol.126 , pp. 1281-1290
    • Sagi, M.1    Fluhr, R.2
  • 152
    • 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
  • 153
    • 11844292846 scopus 로고    scopus 로고
    • The structure of the Arabidopsis thaliana SOS3: Molecular mechanism of sensing calcium for salt stress response
    • Sanchez-Barrena, M.J., Martinez-Ripoll, M., Zhu, J.K. and 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
  • 156
    • 0035107803 scopus 로고    scopus 로고
    • Monitoring the expression pattern of 1300 Arabidopsis genes under drought and cold stresses by using a full-length cDNA microarray
    • Seki, M., Narusaka, M., Abe, H., Kasuga, M., Yamaguchi-Shinozaki, K., Carninci, P., Hayashizaki, Y. and Shinozaki, K. (2001). Monitoring the expression pattern of 1300 Arabidopsis genes under drought and cold stresses by using a full-length cDNA microarray. Plant Cell. 13, 61-72.
    • (2001) Plant Cell. , vol.13 , pp. 61-72
    • Seki, M.1    Narusaka, M.2    Abe, H.3    Kasuga, M.4    Yamaguchi-Shinozaki, K.5    Carninci, P.6    Hayashizaki, Y.7    Shinozaki, K.8
  • 157
    • 0030300175 scopus 로고    scopus 로고
    • 2+-dependent protein kinases and stress signal transduction in plants
    • 2+-dependent protein kinases and stress signal transduction in plants. Science 274, 1900-1902.
    • (1996) Science , vol.274 , pp. 1900-1902
    • Sheen, J.1
  • 160
    • 0036791468 scopus 로고    scopus 로고
    • + antiporter gene AtNHX1 expression by salt stress and abscisic acid
    • + antiporter gene AtNHX1 expression by salt stress and abscisic acid. Plant Mol Biol. 50, 543-550.
    • (2002) Plant Mol Biol. , vol.50 , pp. 543-550
    • Shi, H.1    Zhu, J.K.2
  • 161
    • 0033388972 scopus 로고    scopus 로고
    • Novel protein kinases associated with calcineurin B-like calcium sensors in Arabidopsis
    • Shi, J., Kim, K.N., Ritz, O., Albrecht, V., Gupta, R., Harter, K., Luan, S. and 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
  • 164
    • 0029761681 scopus 로고    scopus 로고
    • Role of kinases and the phosphatase calcineurin in the nuclear shuttling of transcription factor NF-AT4
    • Shibasaki, F., Price, E.R., Milan, D. and McKeon, F. (1996). Role of kinases and the phosphatase calcineurin in the nuclear shuttling of transcription factor NF-AT4. Nature 382, 370-373.
    • (1996) Nature , vol.382 , pp. 370-373
    • Shibasaki, F.1    Price, E.R.2    Milan, D.3    McKeon, F.4
  • 166
    • 0345598942 scopus 로고    scopus 로고
    • Genetic engineering of the glyoxalase pathway in tobacco leads to enhanced salinity tolerance
    • Singla-Pareek, S.L., Reddy, M.K. and Sopory, S.K. (2003). Genetic engineering of the glyoxalase pathway in tobacco leads to enhanced salinity tolerance. Proc. Natl. Acad. Sci. USA 100, 14672-14677.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14672-14677
    • Singla-Pareek, S.L.1    Reddy, M.K.2    Sopory, S.K.3
  • 167
    • 0034945001 scopus 로고    scopus 로고
    • Calmodulin as a versatile calcium signal transducer in plants
    • Snedden, W.A. and Fromm, H. (2001). Calmodulin as a versatile calcium signal transducer in plants. New Phytol. 151, 35-66.
    • (2001) New Phytol. , vol.151 , pp. 35-66
    • Snedden, W.A.1    Fromm, H.2
  • 168
    • 0031438164 scopus 로고    scopus 로고
    • Calcineurin acts through the CRZ1/TCN1-encoded transcription factor to regulate gene expression in yeast
    • Stathopoulos, A.M. and Cyert, M.S. (1997). Calcineurin acts through the CRZ1/TCN1-encoded transcription factor to regulate gene expression in yeast. Genes Dev. 11, 3432-3444.
    • (1997) Genes Dev. , vol.11 , pp. 3432-3444
    • Stathopoulos, A.M.1    Cyert, M.S.2
  • 173
    • 1842426646 scopus 로고    scopus 로고
    • Calmodulin-binding proteins in bryophytes: Identification of abscisic acid-, cold-, and osmotic stress-induced genes encoding novel membrane-bound transporterlike proteins
    • Takezawa, D. and Minami, A. (2004). Calmodulin-binding proteins in bryophytes: identification of abscisic acid-, cold-, and osmotic stress-induced genes encoding novel membrane-bound transporterlike proteins. Biochem. Biophys. Res. Commun. 317, 428-436.
    • (2004) Biochem. Biophys. Res. Commun. , vol.317 , pp. 428-436
    • Takezawa, D.1    Minami, A.2
  • 174
    • 0038607573 scopus 로고    scopus 로고
    • CNGCs: Prime targets of plant cyclic nucleotide signalling?
    • Talke, I.N., Blaudez, D., Maathuis, F.J. and Sanders, D. (2003). CNGCs: prime targets of plant cyclic nucleotide signalling? Trends Plant Sci. 8, 286-293.
    • (2003) Trends Plant Sci. , vol.8 , pp. 286-293
    • Talke, I.N.1    Blaudez, D.2    Maathuis, F.J.3    Sanders, D.4
  • 176
    • 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 ton2 mutant cells affected in the organization of cortical microtubules
    • Thion, L., Mazars, C., Nacry, P., Bouchez, D., Moreau, M., Ranjeva, R. and 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 ton2 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
  • 177
    • 0025298551 scopus 로고
    • The glyoxalase system: New developments towards functional characterization of a metabolic pathway fundamental to biological life
    • Thornalley, P.J. (1990). The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life. Biochem. J. 269, 1-11.
    • (1990) Biochem. J. , vol.269 , pp. 1-11
    • Thornalley, P.J.1
  • 178
    • 20444458715 scopus 로고    scopus 로고
    • Functions of the respiratory burst oxidase in biotic interactions, abiotic stress and development
    • Torres, M.A. and Dangl, J.L. (2005). Functions of the respiratory burst oxidase in biotic interactions, abiotic stress and development. Curr. Opin. Plant Biol. 8, 397-403.
    • (2005) Curr. Opin. Plant Biol. , vol.8 , pp. 397-403
    • Torres, M.A.1    Dangl, J.L.2
  • 179
    • 18744393379 scopus 로고    scopus 로고
    • Distinct regulation of salinity and genotoxic stress responses by Arabidopsis MAP kinase phosphatase 1
    • Ulm, R., Ichimura, K., Mizoguchi, T., Peck, S.C., Zhu, T., Wang, X., Shinozaki, K. and Paszkowski, J. (2002). Distinct regulation of salinity and genotoxic stress responses by Arabidopsis MAP kinase phosphatase 1. EMBO J. 21, 6483-6493.
    • (2002) EMBO J. , vol.21 , pp. 6483-6493
    • Ulm, R.1    Ichimura, K.2    Mizoguchi, T.3    Peck, S.C.4    Zhu, T.5    Wang, X.6    Shinozaki, K.7    Paszkowski, J.8
  • 180
    • 0035868754 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase phosphatase is required for genotoxic stress relief in Arabidopsis
    • Ulm, R., Revenkova, E., di Sansebastiano, G.P., Bechtold, N. and Paszkowski, J. (2001). Mitogen-activated protein kinase phosphatase is required for genotoxic stress relief in Arabidopsis. Genes Dev. 15, 699-709.
    • (2001) Genes Dev. , vol.15 , pp. 699-709
    • Ulm, R.1    Revenkova, E.2    Di Sansebastiano, G.P.3    Bechtold, N.4    Paszkowski, J.5
  • 182
    • 0034636116 scopus 로고    scopus 로고
    • 2+-dependent protein kinase is disrupted by insertions in the tether that connects the calmodulin-like domain to the kinase
    • 2+-dependent protein kinase is disrupted by insertions in the tether that connects the calmodulin-like domain to the kinase. Biochemistry 39, 4004-4011.
    • (2000) Biochemistry , vol.39 , pp. 4004-4011
    • Vitart, V.1    Christodoulou, J.2    Huang, J.F.3    Chazin, W.J.4    Harper, J.F.5
  • 183
    • 0033230738 scopus 로고    scopus 로고
    • Distinct calcium signaling pathways regulate calmodulin gene expression in tobacco
    • van der Luit, A.H., Olivari, C., Haley, A., Knight, M.R., and Trewavas, A.J. (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 Luit, A.H.1    Olivari, C.2    Haley, A.3    Knight, M.R.4    Trewavas, A.J.5
  • 184
    • 84941102391 scopus 로고    scopus 로고
    • Calmodulin and calcium signal transduction: An introduction
    • van Eldik L.J., Watterson, M.D., eds, New York, USA: Academic Press
    • Van Eldik, L.J. and Watterson, M.D. (1998). Calmodulin and calcium signal transduction: an introduction. In: van Eldik, L.J., Watterson, M.D., eds. Calmodulin and signal transduction. New York, USA: Academic Press, 1-15.
    • (1998) Calmodulin and Signal Transduction , pp. 1-15
    • Van Eldik, L.J.1    Watterson, M.D.2
  • 185
    • 0033082685 scopus 로고    scopus 로고
    • Glyoxalase i from Brassica juncea: Molecular cloning, regulation and its over-expression confer tolerance in transgenic tobacco under stress
    • Veena, Reddy, V.S. and Sopory, S.K. (1999). Glyoxalase I from Brassica juncea: molecular cloning, regulation and its over-expression confer tolerance in transgenic tobacco under stress. Plant J. 17, 385-395.
    • (1999) Plant J. , vol.17 , pp. 385-395
    • Veena Reddy, V.S.1    Sopory, S.K.2
  • 186
    • 31844454590 scopus 로고    scopus 로고
    • Regulatory functions of phospholipase D and phosphatidic acid in plant growth, development, and stress responses
    • Wang, X. (2005). Regulatory functions of phospholipase D and phosphatidic acid in plant growth, development, and stress responses. Plant Physiol. 139, 566-573.
    • (2005) Plant Physiol. , vol.139 , pp. 566-573
    • Wang, X.1
  • 187
  • 188
    • 0037206128 scopus 로고    scopus 로고
    • Genes for calcium-permeable channels in the plasma membrane of plant root cells
    • White, P.J., Bowen, H.C., Demidchik, V., Nichols, C. and Davies, J.M. (2002). Genes for calcium-permeable channels in the plasma membrane of plant root cells. Biochim. Biophys. Acta 1564, 299-309.
    • (2002) Biochim. Biophys. Acta , vol.1564 , pp. 299-309
    • White, P.J.1    Bowen, H.C.2    Demidchik, V.3    Nichols, C.4    Davies, J.M.5
  • 189
    • 0034194710 scopus 로고    scopus 로고
    • Calcium channels in higher plants
    • White, P.J. (2000). Calcium channels in higher plants. Biochim. Biophys. Acta 1465, 171-189.
    • (2000) Biochim. Biophys. Acta , vol.1465 , pp. 171-189
    • White, P.J.1
  • 191
    • 0033670905 scopus 로고    scopus 로고
    • The characterization of differential calcium signalling in tobacco guard cells
    • Wood, N.T., Allan, A.C., Haley, A., Viry-Moussaid, M., and Trewavas, A.J. (2000). The characterization of differential calcium signalling in tobacco guard cells. Plant J. 24, 335-344.
    • (2000) Plant J. , vol.24 , pp. 335-344
    • Wood, N.T.1    Allan, A.C.2    Haley, A.3    Viry-Moussaid, M.4    Trewavas, A.J.5
  • 192
    • 0038949224 scopus 로고    scopus 로고
    • SOS1, a genetic locus essential for salt tolerance and potassium acquisition
    • Wu, S.-J., Lei, D., and Zhu, J.-K. (1996). SOS1, a genetic locus essential for salt tolerance and potassium acquisition. Plant Cell 8, 617-627.
    • (1996) Plant Cell , vol.8 , pp. 617-627
    • Wu, S.-J.1    Lei, D.2    Zhu, J.-K.3
  • 193
    • 0036273511 scopus 로고    scopus 로고
    • Cell signaling for cold, drought, and salt stresses
    • Xiong, L., Schumaker, K.S. and Zhu, J.-K. (2002). Cell signaling for cold, drought, and salt stresses. Plant Cell 14(suppl), S165-183.
    • (2002) Plant Cell , vol.14 , Issue.SUPPL.
    • Xiong, L.1    Schumaker, K.S.2    Zhu, J.-K.3
  • 198
    • 0037160040 scopus 로고    scopus 로고
    • A calmodulin-binding/CGCG box DNA-binding protein family involved in multiple signaling pathways in plants
    • Yang, T. and Poovaiah, B.W. (2002). A calmodulin-binding/CGCG box DNA-binding protein family involved in multiple signaling pathways in plants. J. Biol. Chem. 277, 45049-45058.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45049-45058
    • Yang, T.1    Poovaiah, B.W.2
  • 199
    • 13544256637 scopus 로고    scopus 로고
    • Direct interaction of a divergent CaM isoform and the transcription factor, MYB2, enhances salt tolerance in Arabidopsis
    • Yoo, J.H., Park, C.Y., Kim, J.C., Heo, W.D., Cheong, M.S. et al. (2005). Direct interaction of a divergent CaM isoform and the transcription factor, MYB2, enhances salt tolerance in Arabidopsis. J. Biol. Chem. 280, 3697-3706.
    • (2005) J. Biol. Chem. , vol.280 , pp. 3697-3706
    • Yoo, J.H.1    Park, C.Y.2    Kim, J.C.3    Heo, W.D.4    Cheong, M.S.5
  • 200
    • 0037163129 scopus 로고    scopus 로고
    • Genome-wide analysis of gene expression regulated by the calcineurin/Crz1p signaling pathway in Saccharomyces cerevisiae
    • Yoshimoto, H., Saltsman, K., Gasch, A.P., Li, H.X., Ogawa, N., Botstein, D., Brown, P.O. and Cyert, M.S. (2002). Genome-wide analysis of gene expression regulated by the calcineurin/Crz1p signaling pathway in Saccharomyces cerevisiae. J. Biol. Chem. 277, 31079-31088.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31079-31088
    • Yoshimoto, H.1    Saltsman, K.2    Gasch, A.P.3    Li, H.X.4    Ogawa, N.5    Botstein, D.6    Brown, P.O.7    Cyert, M.S.8
  • 201
    • 23944479121 scopus 로고    scopus 로고
    • Phospholipase D in the signaling networks of plant response to abscisic acid and reactive oxygen species
    • Zhang, W., Yu, L., Zhang, Y. and Wang, X. (2005). Phospholipase D in the signaling networks of plant response to abscisic acid and reactive oxygen species. Biochim. Biophys. Acta 1736, 1-9.
    • (2005) Biochim. Biophys. Acta , vol.1736 , pp. 1-9
    • Zhang, W.1    Yu, L.2    Zhang, Y.3    Wang, X.4
  • 202
    • 0034872870 scopus 로고    scopus 로고
    • Hydrogen peroxide is involved in abscisic acid-induced stomatal closure in Vicia faba
    • Zhang, X., Zhang, L., Dong, F.C., Gao, J.F., Galbraith, D.W. and Song, C.P. (2001). Hydrogen peroxide is involved in abscisic acid-induced stomatal closure in Vicia faba. Plant Physiol. 126, 1438-1448.
    • (2001) Plant Physiol. , vol.126 , pp. 1438-1448
    • Zhang, X.1    Zhang, L.2    Dong, F.C.3    Gao, J.F.4    Galbraith, D.W.5    Song, C.P.6
  • 203
    • 0036999615 scopus 로고    scopus 로고
    • Salt and drought stress signal transduction in plants
    • Zhu J.K. (2002). Salt and drought stress signal transduction in plants. Annu. Rev. Plant Biol. 53, 247-273.
    • (2002) Annu. Rev. Plant Biol. , vol.53 , pp. 247-273
    • Zhu, J.K.1
  • 204
    • 0032125095 scopus 로고    scopus 로고
    • Genetic analysis of salt tolerance in Arabidopsis thaliana: Evidence of a critical role for potassium nutrition
    • Zhu, J.K., Liu, J. and Xiong, L. (1998). Genetic analysis of salt tolerance in Arabidopsis thaliana: evidence of a critical role for potassium nutrition. Plant Cell 10, 1181-1192.
    • (1998) Plant Cell , vol.10 , pp. 1181-1192
    • Zhu, J.K.1    Liu, J.2    Xiong, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.