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Volumn 56, Issue , 2005, Pages 435-466

Plant-specific calmodulin-binding proteins

Author keywords

Arabidopsis; Calcium; Environmental stress; Signal transduction

Indexed keywords

CALCIUM; CALMODULIN BINDING PROTEIN; VEGETABLE PROTEIN;

EID: 20444376563     PISSN: 15435008     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.arplant.56.032604.144224     Document Type: Review
Times cited : (360)

References (199)
  • 1
    • 0035977492 scopus 로고    scopus 로고
    • Rice (Oryza sativa) contains a novel isoform of glutamate decarboxylase that lacks an authentic calmodulin-binding domain at the C-terminus
    • Akama K, Akihiro T, Kitagawa M, Takaiwa F. 2001. Rice (Oryza sativa) contains a novel isoform of glutamate decarboxylase that lacks an authentic calmodulin-binding domain at the C-terminus. Biochim. Biophys. Acta 1522:143-50
    • (2001) Biochim. Biophys. Acta , vol.1522 , pp. 143-150
    • Akama, K.1    Akihiro, T.2    Kitagawa, M.3    Takaiwa, F.4
  • 2
    • 0038414032 scopus 로고    scopus 로고
    • Differential expression of genes encoding calmodulin-binding proteins in response to bacterial pathogens and inducers of defense responses
    • Ali GS, Reddy VS, Lindgren PB, Jakobek JL, Reddy AS. 2003. Differential expression of genes encoding calmodulin-binding proteins in response to bacterial pathogens and inducers of defense responses. Plant Mol. Biol. 51:803-15
    • (2003) Plant Mol. Biol. , vol.51 , pp. 803-815
    • Ali, G.S.1    Reddy, V.S.2    Lindgren, P.B.3    Jakobek, J.L.4    Reddy, A.S.5
  • 3
    • 0035963337 scopus 로고    scopus 로고
    • A defined range of guard cell calcium oscillation parameters encodes stomatal movements
    • Allen GJ, Chu SP, Harrington CL, Schumacher K, Hoffmann T, et al. 2001. A defined range of guard cell calcium oscillation parameters encodes stomatal movements. Nature 411:1053-57
    • (2001) Nature , vol.411 , pp. 1053-1057
    • Allen, G.J.1    Chu, S.P.2    Harrington, C.L.3    Schumacher, K.4    Hoffmann, T.5
  • 4
    • 0034730610 scopus 로고    scopus 로고
    • Alteration of stimulus-specific guard cell calcium oscillations and stomatal closing in Arabidopsis det3 mutant
    • Allen GJ, Chu SP, Schumacher K, Shimazaki CT, Vafeados D, et al. 2000. Alteration of stimulus-specific guard cell calcium oscillations and stomatal closing in Arabidopsis det3 mutant. Science 289:2338-42
    • (2000) Science , vol.289 , pp. 2338-2342
    • Allen, G.J.1    Chu, S.P.2    Schumacher, K.3    Shimazaki, C.T.4    Vafeados, D.5
  • 5
    • 67649240085 scopus 로고    scopus 로고
    • Combining genetics and cell biology to crack the code of plant cell calcium signaling
    • Allen GJ, Schroeder JI. 2001. Combining genetics and cell biology to crack the code of plant cell calcium signaling. Sciences STKE 13:1-7
    • (2001) Sciences STKE , vol.13 , pp. 1-7
    • Allen, G.J.1    Schroeder, J.I.2
  • 6
    • 0034613277 scopus 로고    scopus 로고
    • A calmodulin-related protein that suppresses posttranscriptional gene silencing in plants
    • Anandalakshmi R, Marathe R, Ge X, Herr JMJ, Mau C, et al. 2000. A calmodulin-related protein that suppresses posttranscriptional gene silencing in plants. Science 290:142-44
    • (2000) Science , vol.290 , pp. 142-144
    • Anandalakshmi, R.1    Marathe, R.2    Ge, X.3    Herr, J.M.J.4    Mau, C.5
  • 7
    • 3242715114 scopus 로고    scopus 로고
    • Reactive oxygen species: Metabolism, oxidative stress, and signal transduction
    • Apel K, Hirt H. 2004. Reactive oxygen species: metabolism, oxidative stress, and signal transduction. Annu. Rev. Plant Physiol. Plant Mol. Biol. 55:373-99
    • (2004) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.55 , pp. 373-399
    • Apel, K.1    Hirt, H.2
  • 8
    • 0029310677 scopus 로고
    • Molecular and biochemical analysis of calmodulin interactions with the calmodulin-binding domain of plant glutamate decarboxylase
    • Arazi T, Baum G, Snedden WA, Shelp BJ, Fromm H. 1995. Molecular and biochemical analysis of calmodulin interactions with the calmodulin-binding domain of plant glutamate decarboxylase. Plant Physiol. 108:551-61
    • (1995) Plant Physiol. , vol.108 , pp. 551-561
    • Arazi, T.1    Baum, G.2    Snedden, W.A.3    Shelp, B.J.4    Fromm, H.5
  • 9
    • 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, 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
  • 10
    • 0033624546 scopus 로고    scopus 로고
    • Cyclic nucleotide- and calcium/calmodulin-regulated channels in plants: Targets for manipulating heavy metal tolerance, and possible physiological roles
    • Arazi T, Kaplan B, Sunkar R, Dolev D, Fromm H. 2000. Cyclic nucleotide- and calcium/calmodulin-regulated channels in plants: targets for manipulating heavy metal tolerance, and possible physiological roles. Biochem. Soc. Trans. 28:471-75
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 471-475
    • Arazi, T.1    Kaplan, B.2    Sunkar, R.3    Dolev, D.4    Fromm, H.5
  • 12
    • 0029177391 scopus 로고
    • Involvement of calcium and calmodulin in protein and amino-acid metabolism in rice roots under anoxia
    • Aurisano N, Bertani A, Reggiani R. 1995. Involvement of calcium and calmodulin in protein and amino-acid metabolism in rice roots under anoxia. Plant Cell Physiol. 36:1525-29
    • (1995) Plant Cell Physiol. , vol.36 , pp. 1525-1529
    • Aurisano, N.1    Bertani, A.2    Reggiani, R.3
  • 14
    • 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
    • Balagué C, Lin B, Alcon C, Flottes G, Malmstrom S, et al. 2003. HLM1, an essential signaling component in the hypersensitive response, is a member of the cyclic nucleotide-gated channel ion channel family. Plant Cell 15:365-79
    • (2003) Plant Cell , vol.15 , pp. 365-379
    • Balagué, C.1    Lin, B.2    Alcon, C.3    Flottes, G.4    Malmstrom, S.5
  • 15
    • 0027203970 scopus 로고
    • A plant glutamate decarboxylase containing a calmodulin binding domain. Cloning, sequence, and functional analysis
    • Baum G, Chen Y, Arazi T, Takatsuji H, Fromm H. 1993. A plant glutamate decarboxylase containing a calmodulin binding domain. Cloning, sequence, and functional analysis. J. Biol. Chem. 268:19610-17
    • (1993) J. Biol. Chem. , vol.268 , pp. 19610-19617
    • Baum, G.1    Chen, Y.2    Arazi, T.3    Takatsuji, H.4    Fromm, H.5
  • 16
    • 0030014203 scopus 로고    scopus 로고
    • Calmodulin binding to glutamate decarboxylase is required for regulation of glutamate and GABA metabolism and normal development in plants
    • Baum G, Lev-Yadun S, Fridmann Y, Arazi T, Katsnelson H, et al. 1996. Calmodulin binding to glutamate decarboxylase is required for regulation of glutamate and GABA metabolism and normal development in plants. EMBO J. 15:2988-96
    • (1996) EMBO J. , vol.15 , pp. 2988-2996
    • Baum, G.1    Lev-Yadun, S.2    Fridmann, Y.3    Arazi, T.4    Katsnelson, H.5
  • 17
    • 0033167033 scopus 로고    scopus 로고
    • Wound- and systemin-inducible calmodulin gene expression in tomato leaves
    • Bergey DR, Ryan CA. 1999. Wound- and systemin-inducible calmodulin gene expression in tomato leaves. Plant Mol. Biol. 40:815-23
    • (1999) Plant Mol. Biol. , vol.40 , pp. 815-823
    • Bergey, D.R.1    Ryan, C.A.2
  • 18
    • 0034598910 scopus 로고    scopus 로고
    • Signal transduction: The calcium entry pas de deux
    • Berridge MJ, Lipp P, Bootman MD. 2000. Signal transduction: the calcium entry pas de deux. Science 287:1604-5
    • (2000) Science , vol.287 , pp. 1604-1605
    • Berridge, M.J.1    Lipp, P.2    Bootman, M.D.3
  • 19
    • 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 12:1425-40
    • (2000) Plant Cell , vol.12 , pp. 1425-1440
    • Blume, B.1    Nurnberger, T.2    Nass, N.3    Scheel, D.4
  • 20
    • 0028387457 scopus 로고
    • Differential expression of two calmodulin genes in response to physical and chemical stimuli
    • Botella JR, Arteca RN. 1994. Differential expression of two calmodulin genes in response to physical and chemical stimuli. Plant Mol. Biol. 24:757-66
    • (1994) Plant Mol. Biol. , vol.24 , pp. 757-766
    • Botella, J.R.1    Arteca, R.N.2
  • 21
    • 0037636431 scopus 로고    scopus 로고
    • Mitochondrial succinic-semialdehyde dehydrogenase of the γ-aminobutyrate shunt is required to restrict levels of reactive oxygen intermediates in plants
    • Bouché N, Fait A, Bouchez D, Møller SG, Fromm H. 2003. Mitochondrial succinic-semialdehyde dehydrogenase of the γ-aminobutyrate shunt is required to restrict levels of reactive oxygen intermediates in plants. Proc. Natl. Acad. Sci. USA 100:6843-48
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6843-6848
    • Bouché, N.1    Fait, A.2    Bouchez, D.3    Møller, S.G.4    Fromm, H.5
  • 22
    • 16544368713 scopus 로고    scopus 로고
    • The root-specific glutamate decarboxylase (GAD1) is essential for sustaining GABA levels in Arabidopsis
    • Bouché N, Fait A, Zik M, Fromm H. 2004. The root-specific glutamate decarboxylase (GAD1) is essential for sustaining GABA levels in Arabidopsis. Plant Mol. Biol. 55:315-25
    • (2004) Plant Mol. Biol. , vol.55 , pp. 315-325
    • Bouché, N.1    Fait, A.2    Zik, M.3    Fromm, H.4
  • 23
    • 1542290398 scopus 로고    scopus 로고
    • GABA in plants: Just a metabolite?
    • Bouché N, Fromm H. 2004. GABA in plants: just a metabolite? Trends Plant Sci. 9:110-15
    • (2004) Trends Plant Sci. , vol.9 , pp. 110-115
    • Bouché, N.1    Fromm, H.2
  • 24
    • 0037077285 scopus 로고    scopus 로고
    • A novel family of calmodulin-binding transcription activators in multicellular organisms
    • Bouché N, Scharlat A, Snedden W, Bouchez D, Fromm H. 2002. A novel family of calmodulin-binding transcription activators in multicellular organisms. J. Biol. Chem. 277:21851-61
    • (2002) J. Biol. Chem. , vol.277 , pp. 21851-21861
    • Bouché, N.1    Scharlat, A.2    Snedden, W.3    Bouchez, D.4    Fromm, H.5
  • 25
    • 0037008175 scopus 로고    scopus 로고
    • Insect footsteps on leaves stimulate the accumulation of 4-aminobutyrate and can be visualized through increased chlorophyll fluorescence and superoxide production
    • Bown AW, Hall DE, MacGregor KB. 2002. Insect footsteps on leaves stimulate the accumulation of 4-aminobutyrate and can be visualized through increased chlorophyll fluorescence and superoxide production. Plant Physiol. 129:1430-34
    • (2002) Plant Physiol. , vol.129 , pp. 1430-1434
    • Bown, A.W.1    Hall, D.E.2    MacGregor, K.B.3
  • 26
    • 0025162096 scopus 로고
    • Rain-, wind-, and touch-induced expression of calmodulin and calmodulin-related genes in Arabidopsis
    • Braam J, Davis RW. 1990. Rain-, wind-, and touch-induced expression of calmodulin and calmodulin-related genes in Arabidopsis. Cell 60:357-64
    • (1990) Cell , vol.60 , pp. 357-364
    • Braam, J.1    Davis, R.W.2
  • 29
    • 20444387434 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 30
    • 20444362586 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 31
    • 0023039744 scopus 로고
    • Characterization of nucleoside triphosphatase activity in isolated pea nuclei and its photoreversible regulation by light
    • Chen YR, Roux SJ. 1986. Characterization of nucleoside triphosphatase activity in isolated pea nuclei and its photoreversible regulation by light. Plant Physiol. 81:609-13
    • (1986) Plant Physiol. , vol.81 , pp. 609-613
    • Chen, Y.R.1    Roux, S.J.2
  • 32
    • 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. 2002. Calcium signaling through protein kinases. The Arabidopsis calcium-dependent protein kinase gene family. Plant Physiol. 129:469-85
    • (2002) Plant Physiol. , vol.129 , pp. 469-485
    • Cheng, S.H.1    Willmann, M.R.2    Chen, H.C.3    Sheen, J.4
  • 33
    • 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 15:1833-45
    • (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
  • 34
    • 0032506166 scopus 로고    scopus 로고
    • Reciprocal regulation of mammalian nitric oxide synthase and calcineurin by plant calmodulin isoforms
    • Cho MJ, Vaghy PL, Kondo R, Lee SH, Davis JP, et al. 1998. Reciprocal regulation of mammalian nitric oxide synthase and calcineurin by plant calmodulin isoforms. Biochemistry 37:15593-97
    • (1998) Biochemistry , vol.37 , pp. 15593-15597
    • Cho, M.J.1    Vaghy, P.L.2    Kondo, R.3    Lee, S.H.4    Davis, J.P.5
  • 35
    • 0037077216 scopus 로고    scopus 로고
    • Identification of calmodulin isoform-specific binding peptides from a phage-displayed random 22-mer peptide library
    • Choi JY, Lee SH, Park CY, Heo WD, Kim JC, et al. 2002. Identification of calmodulin isoform-specific binding peptides from a phage-displayed random 22-mer peptide library. J. Biol. Chem. 277:21630-38
    • (2002) J. Biol. Chem. , vol.277 , pp. 21630-21638
    • Choi, J.Y.1    Lee, S.H.2    Park, C.Y.3    Heo, W.D.4    Kim, J.C.5
  • 39
    • 0029149085 scopus 로고
    • Molecular and structural basis of target recognition by calmodulin
    • Crivici A, 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
  • 40
    • 0035859020 scopus 로고    scopus 로고
    • Plant pathogens and integrated defence responses to infection
    • Dangl JL, Jones JD. 2001. Plant pathogens and integrated defence responses to infection. Nature 411:826-33
    • (2001) Nature , vol.411 , pp. 826-833
    • Dangl, J.L.1    Jones, J.D.2
  • 41
    • 0031058901 scopus 로고    scopus 로고
    • Characterization of the basic amphiphilic α-helix calmodulin-binding domain of a 61.5 kDa tobacco calmodulin-binding protein
    • Dash S, Niemaczura W, Harrington HM. 1997. Characterization of the basic amphiphilic α-helix calmodulin-binding domain of a 61.5 kDa tobacco calmodulin-binding protein. Biochemistry 36:2025-29
    • (1997) Biochemistry , vol.36 , pp. 2025-2029
    • Dash, S.1    Niemaczura, W.2    Harrington, H.M.3
  • 43
    • 0034608071 scopus 로고    scopus 로고
    • Interaction of a kinesin-like calmodulin-binding protein with a protein kinase
    • Day IS, Miller C, Golovkin M, Reddy AS. 2000. Interaction of a kinesin-like calmodulin-binding protein with a protein kinase. J. Biol. Chem. 275:13737-45
    • (2000) J. Biol. Chem. , vol.275 , pp. 13737-13745
    • Day, I.S.1    Miller, C.2    Golovkin, M.3    Reddy, A.S.4
  • 45
    • 0242669365 scopus 로고    scopus 로고
    • Expression profiling of the host response to bacterial infection: The transition from basal to induced defence responses in RPM1-mediated resistance
    • de Torres M, Sanchez P, Fernandez-Delmond I, Grant M. 2003. Expression profiling of the host response to bacterial infection: the transition from basal to induced defence responses in RPM1-mediated resistance. Plant J. 33:665-76
    • (2003) Plant J. , vol.33 , pp. 665-676
    • De Torres, M.1    Sanchez, P.2    Fernandez-Delmond, I.3    Grant, M.4
  • 47
    • 0032490943 scopus 로고    scopus 로고
    • Nitric oxide functions as a signal in plant disease resistance
    • Delledonne M, Xia Y, Dixon RA, Lamb C. 1998. Nitric oxide functions as a signal in plant disease resistance. Nature 394:585-88
    • (1998) Nature , vol.394 , pp. 585-588
    • Delledonne, M.1    Xia, Y.2    Dixon, R.A.3    Lamb, C.4
  • 48
    • 0035818606 scopus 로고    scopus 로고
    • Signal interactions between nitric oxide and reactive oxygen intermediates in the plant hypersensitive disease resistance response
    • Delledonne M, Zeier J, Marocco A, Lamb C. 2001. Signal interactions between nitric oxide and reactive oxygen intermediates in the plant hypersensitive disease resistance response. Proc. Natl. Acad. Sci. USA 98:13454-59
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13454-13459
    • Delledonne, M.1    Zeier, J.2    Marocco, A.3    Lamb, C.4
  • 49
    • 0342424183 scopus 로고    scopus 로고
    • Effects of short-term NaCl stress on calmodulin transcript levels and calmodulin-dependent NAD kinase activity in two species of tomato
    • Delumeau O, Morere-Le Paven M-C, Montrichard F, Laval-Martin DL. 2000. Effects of short-term NaCl stress on calmodulin transcript levels and calmodulin-dependent NAD kinase activity in two species of tomato. Plant Cell Environ. 23:329-36
    • (2000) Plant Cell Environ. , vol.23 , pp. 329-336
    • Delumeau, O.1    Morere-Le Paven, M.-C.2    Montrichard, F.3    Laval-Martin, D.L.4
  • 50
    • 0032580202 scopus 로고    scopus 로고
    • Calcium oscillations increase the efficiency and specificity of gene expression
    • Dolmetsch RE, Xu K, Lewis RS. 1998. Calcium oscillations increase the efficiency and specificity of gene expression. Nature 392:933-41
    • (1998) Nature , vol.392 , pp. 933-941
    • Dolmetsch, R.E.1    Xu, K.2    Lewis, R.S.3
  • 51
    • 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. 54:549-69
    • (2004) Plant Mol. Biol. , vol.54 , pp. 549-569
    • Du, L.1    Poovaiah, B.W.2
  • 52
    • 0032544005 scopus 로고    scopus 로고
    • Defense gene induction in tobacco by nitric oxide, cyclic GMP, and cyclic ADP-ribose
    • Durner J, Wendehenne D, Klessig DF. 1998. Defense gene induction in tobacco by nitric oxide, cyclic GMP, and cyclic ADP-ribose. Proc. Natl. Acad. Sci. USA 95:10328-33
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10328-10333
    • Durner, J.1    Wendehenne, D.2    Klessig, D.F.3
  • 53
    • 0033948456 scopus 로고    scopus 로고
    • cDNA-AFLP reveals a striking overlap in race-specific resistance and wound response gene expression profiles
    • Durrant WE, Rowland O, Piedras P, Hammond-Kosack KE, Jones JD. 2000. cDNA-AFLP reveals a striking overlap in race-specific resistance and wound response gene expression profiles. Plant Cell 12:963-77
    • (2000) Plant Cell , vol.12 , pp. 963-977
    • Durrant, W.E.1    Rowland, O.2    Piedras, P.3    Hammond-Kosack, K.E.4    Jones, J.D.5
  • 55
    • 18344374007 scopus 로고    scopus 로고
    • The cell morphogenesis gene ANGUSTIFOLIA encodes a CtBP/BARS-like protein and is involved in the control of the microtubule cytoskeleton
    • Folkers U, Kirik V, Schobinger U, Falk S, Krishnakumar S, et al. 2002. The cell morphogenesis gene ANGUSTIFOLIA encodes a CtBP/BARS-like protein and is involved in the control of the microtubule cytoskeleton. EMBO J. 21:1280-88
    • (2002) EMBO J. , vol.21 , pp. 1280-1288
    • Folkers, U.1    Kirik, V.2    Schobinger, U.3    Falk, S.4    Krishnakumar, S.5
  • 56
    • 51249167396 scopus 로고
    • 35S labeled recombinant calmodulin as a probe
    • 35S labeled recombinant calmodulin as a probe. Plant Mol. Biol. Rep. 10:199-206
    • (1992) Plant Mol. Biol. Rep. , vol.10 , pp. 199-206
    • Fromm, H.1    Chua, N.-H.2
  • 59
    • 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. 124:1814-27
    • (2000) Plant Physiol. , vol.124 , pp. 1814-1827
    • Geisler, M.1    Frangne, N.2    Gomes, E.3    Martinoia, E.4    Palmgren, M.G.5
  • 60
    • 3042723172 scopus 로고    scopus 로고
    • Arabidopsis immunophilin-like TWD1 functionally interacts with vacuolar ABC transporters
    • Geisler M, Girin M, Brandt S, Vincenzetti V, Plaza S, et al. 2004. Arabidopsis immunophilin-like TWD1 functionally interacts with vacuolar ABC transporters. Mol. Biol. Cell 15:3393-405
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3393-3405
    • Geisler, M.1    Girin, M.2    Brandt, S.3    Vincenzetti, V.4    Plaza, S.5
  • 61
    • 10744223685 scopus 로고    scopus 로고
    • TWISTED DWARF1, a unique plasma membrane-anchored immunophilin-like protein, interacts with Arabidopsis multidrug resistance-like transporters AtPGP1 and AtPGP19
    • Geisler M, Kolukisaoglu HU, Bouchard R, Billion K, Berger J, et al. 2003. TWISTED DWARF1, a unique plasma membrane-anchored immunophilin-like protein, interacts with Arabidopsis multidrug resistance-like transporters AtPGP1 and AtPGP19. Mol. Biol. Cell. 14:4238-49
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 4238-4249
    • Geisler, M.1    Kolukisaoglu, H.U.2    Bouchard, R.3    Billion, K.4    Berger, J.5
  • 63
    • 0041335543 scopus 로고    scopus 로고
    • A calmodulin-binding protein from Arabidopsis has an essential role in pollen germination
    • Golovkin M, Reddy ASN. 2003. A calmodulin-binding protein from Arabidopsis has an essential role in pollen germination. Proc. Natl. Acad. Sci. USA 100:10558-63
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10558-10563
    • Golovkin, M.1    Reddy, A.S.N.2
  • 64
    • 1642465539 scopus 로고    scopus 로고
    • The SOS3 family of calcium sensors and SOS2 family of protein kinases in Arabidopsis
    • Gong D, Guo Y, Schumaker KS, Zhu JK. 2004. The SOS3 family of calcium sensors and SOS2 family of protein kinases in Arabidopsis. Plant Physiol. 134:919-26
    • (2004) Plant Physiol. , vol.134 , pp. 919-926
    • Gong, D.1    Guo, Y.2    Schumaker, K.S.3    Zhu, J.K.4
  • 65
    • 0028872394 scopus 로고
    • Involvement of calcium and calmodulin in the acquisition of heat shock induced thermotolerance in maize
    • Gong M, Li Z-G. 1995. Involvement of calcium and calmodulin in the acquisition of heat shock induced thermotolerance in maize. Phytochemistry 40:1335-39
    • (1995) Phytochemistry , vol.40 , pp. 1335-1339
    • Gong, M.1    Li, Z.-G.2
  • 66
    • 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. 23:441-50
    • (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
  • 67
    • 0141531067 scopus 로고    scopus 로고
    • Identification of a plant nitric oxide synthase gene involved in hormonal signaling
    • Guo F-Q, Okamoto M, Crawford NM. 2003. Identification of a plant nitric oxide synthase gene involved in hormonal signaling. Science 302:100-3
    • (2003) Science , vol.302 , pp. 100-103
    • Guo, F.-Q.1    Okamoto, M.2    Crawford, N.M.3
  • 68
    • 0035910259 scopus 로고    scopus 로고
    • 2+-binding protein involved in cryptochrome and phytochrome coaction
    • 2+-binding protein involved in cryptochrome and phytochrome coaction. Science 291:487-90
    • (2001) Science , vol.291 , pp. 487-490
    • Guo, H.1    Mockler, T.2    Duong, H.3    Lin, C.4
  • 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, 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 97:3735-40
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3735-3740
    • Halfter, U.1    Ishitani, M.2    Zhu, J.-K.3
  • 70
    • 0030907241 scopus 로고    scopus 로고
    • Transgenic tobacco expressing a foreign calmodulin gene shows an enhanced production of active oxygen species
    • Harding SA, Oh SH, Roberts DM. 1997. Transgenic tobacco expressing a foreign calmodulin gene shows an enhanced production of active oxygen species. EMBO J. 16:1137-44
    • (1997) EMBO J. , vol.16 , pp. 1137-1144
    • Harding, S.A.1    Oh, S.H.2    Roberts, D.M.3
  • 71
    • 0032454145 scopus 로고    scopus 로고
    • Nuclear calcium: A key regulator of gene expression
    • Hardingham GE, Bading H. 1998. Nuclear calcium: a key regulator of gene expression. BioMetals 11:345-58
    • (1998) BioMetals , vol.11 , pp. 345-358
    • Hardingham, G.E.1    Bading, H.2
  • 72
    • 0142025055 scopus 로고    scopus 로고
    • Calcium-regulated protein kinases of plants
    • Harmon AC. 2003. Calcium-regulated protein kinases of plants. Gravit. Space Biol. Bull. 16:83-90
    • (2003) Gravit. Space Biol. Bull. , vol.16 , pp. 83-90
    • Harmon, A.C.1
  • 74
    • 0035209361 scopus 로고    scopus 로고
    • FKBPs: At the crossroads of folding and transduction
    • Harrar Y, Bellini C, Faure JD. 2001. FKBPs: at the crossroads of folding and transduction. Trends Plant Sci. 6:426-31
    • (2001) Trends Plant Sci. , vol.6 , pp. 426-431
    • Harrar, Y.1    Bellini, C.2    Faure, J.D.3
  • 75
    • 0033582172 scopus 로고    scopus 로고
    • Involvement of specific calmodulin isoforms in salicylic acid-independent activation of plant disease resistance responses
    • Heo WD, Lee SH, Kim MC, Kim JC, Chung WS, et al. 1999. Involvement of specific calmodulin isoforms in salicylic acid-independent activation of plant disease resistance responses. Proc. Natl. Acad. Sci. USA 96:766-71
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 766-771
    • Heo, W.D.1    Lee, S.H.2    Kim, M.C.3    Kim, J.C.4    Chung, W.S.5
  • 77
    • 0037155689 scopus 로고    scopus 로고
    • Calmodulin in action: Diversity in target recognition and activation mechanisms
    • Hoeflich KP, Ikura M. 2004. Calmodulin in action: diversity in target recognition and activation mechanisms. Cell 108:739-42
    • (2004) Cell , vol.108 , pp. 739-742
    • Hoeflich, K.P.1    Ikura, M.2
  • 78
    • 0041966088 scopus 로고    scopus 로고
    • Control of pollen tube growth: Role of ion gradients and fluxes
    • Holdaway-Clarke TL, Hepler PK. 2003. Control of pollen tube growth: role of ion gradients and fluxes. New Phytol. 159:539-63
    • (2003) New Phytol. , vol.159 , pp. 539-563
    • Holdaway-Clarke, T.L.1    Hepler, P.K.2
  • 79
    • 0034571237 scopus 로고    scopus 로고
    • Regulation of a recombinant pea nuclear apyrase by calmodulin and casein kinase II
    • Hsieh H-L, Song CJ, Roux SJ. 2000. Regulation of a recombinant pea nuclear apyrase by calmodulin and casein kinase II. Biochim. Biophys. Acta 1494:248-55
    • (2000) Biochim. Biophys. Acta , vol.1494 , pp. 248-255
    • Hsieh, H.-L.1    Song, C.J.2    Roux, S.J.3
  • 80
    • 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. 2003. Functional interaction of calmodulin with a plant cyclic nucleotide gated cation channel. Plant Physiol. Biochem. 41:945-54
    • (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
  • 81
    • 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, 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 Science 166:1253-59
    • (2004) Plant Science , vol.166 , pp. 1253-1259
    • Hua, W.1    Li, R.-J.2    Wang, L.3    Lu, Y.-T.4
  • 82
    • 0345256489 scopus 로고    scopus 로고
    • A tobacco (Nicotiana tabaccum) calmodulin-binding protein kinase, NtCBK2, is regulated differentially by calmodulin isoforms
    • Hua W, Liang S, Lu Y. 2003. A tobacco (Nicotiana tabaccum) calmodulin-binding protein kinase, NtCBK2, is regulated differentially by calmodulin isoforms. Biochem J. 376:291-302
    • (2003) Biochem J. , vol.376 , pp. 291-302
    • Hua, W.1    Liang, S.2    Lu, Y.3
  • 83
    • 0033180073 scopus 로고    scopus 로고
    • A bean cDNA expressed during a hypersensitive reaction encodes a putative calcium-binding protein
    • Jakobek JL, Smith-Becker JA, Lindgren PB. 1999. A bean cDNA expressed during a hypersensitive reaction encodes a putative calcium-binding protein. Mol. Plant-Microbe Int. 12:712-19
    • (1999) Mol. Plant-Microbe Int. , vol.12 , pp. 712-719
    • Jakobek, J.L.1    Smith-Becker, J.A.2    Lindgren, P.B.3
  • 85
    • 0038381561 scopus 로고    scopus 로고
    • Isolation and analyses of genes preferentially expressed during early cotton fiber development by subtractive PCR and cDNA array
    • Ji SJ, Lu YC, Feng JX, Wei G, Li J, et al. 2003. Isolation and analyses of genes preferentially expressed during early cotton fiber development by subtractive PCR and cDNA array. Nucleic Acids Res. 31:2534-43
    • (2003) Nucleic Acids Res. , vol.31 , pp. 2534-2543
    • Ji, S.J.1    Lu, Y.C.2    Feng, J.X.3    Wei, G.4    Li, J.5
  • 86
    • 0036847334 scopus 로고    scopus 로고
    • Characterization of Arabidopsis thaliana AtFKBP42 that is membrane-bound and interacts with Hsp90
    • Kamphausen T, Fanghanel J, Neumann D, Schulz B, Rahfeld JU. 2002. Characterization of Arabidopsis thaliana AtFKBP42 that is membrane-bound and interacts with Hsp90. Plant J. 32:263-76
    • (2002) Plant J. , vol.32 , pp. 263-276
    • Kamphausen, T.1    Fanghanel, J.2    Neumann, D.3    Schulz, B.4    Rahfeld, J.U.5
  • 87
    • 3042656678 scopus 로고    scopus 로고
    • Identification and characterization of FLJ10737 and CAMTA1 genes on the commonly deleted region of neuroblastoma at human chromosome 1p36.31-p36.23
    • Katoh M. 2003. Identification and characterization of FLJ10737 and CAMTA1 genes on the commonly deleted region of neuroblastoma at human chromosome 1p36.31-p36.23. Int. J. Oncol. 23:1219-24
    • (2003) Int. J. Oncol. , vol.23 , pp. 1219-1224
    • Katoh, M.1
  • 88
    • 0036301043 scopus 로고    scopus 로고
    • Cyclic nucleotide-gated ion channels
    • Kaupp UB, 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
  • 89
    • 0037205430 scopus 로고    scopus 로고
    • Mlo, a modulator of plant defense and cell death, is a novel calmodulin-binding protein. Isolation and characterization of rice Mlo homologue
    • Kim MC, Lee SH, Kim JK, Chun HJ, Choi MS, et al. 2002. Mlo, a modulator of plant defense and cell death, is a novel calmodulin-binding protein. Isolation and characterization of rice Mlo homologue. J. Biol. Chem. 277:19304-14
    • (2002) J. Biol. Chem. , vol.277 , pp. 19304-19314
    • Kim, M.C.1    Lee, S.H.2    Kim, J.K.3    Chun, H.J.4    Choi, M.S.5
  • 90
    • 0037187626 scopus 로고    scopus 로고
    • Calmodulin interacts with MLO protein to regulate defence against mildew in barley
    • Kim MC, Panstruga R, Elliott C, Muller J, Devoto A, et al. 2002. Calmodulin interacts with MLO protein to regulate defence against mildew in barley. Nature 416:447-51
    • (2002) Nature , vol.416 , pp. 447-451
    • Kim, M.C.1    Panstruga, R.2    Elliott, C.3    Muller, J.4    Devoto, A.5
  • 92
    • 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, et al. 2002. Convergence of calcium signaling pathways of pathogenic elicitors and abscisic acid in Arabidopsis guard cells. Plant Physiol. 130:2152-63
    • (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
  • 93
    • 0038267403 scopus 로고    scopus 로고
    • The auxin-induced maize gene ZmSAUR2 encodes a short-lived nuclear protein expressed in elongating tissues
    • Knauss S, Rohrmeier T, Lehle L. 2003. The auxin-induced maize gene ZmSAUR2 encodes a short-lived nuclear protein expressed in elongating tissues. J. Biol. Chem. 278:23936-43
    • (2003) J. Biol. Chem. , vol.278 , pp. 23936-23943
    • Knauss, S.1    Rohrmeier, T.2    Lehle, L.3
  • 94
    • 0035206163 scopus 로고    scopus 로고
    • Abiotic stress signalling pathways: Specificity and cross-talk
    • Knight H, Knight MR. 2001. Abiotic stress signalling pathways: specificity and cross-talk. Trends Plant Sci. 6:262-67
    • (2001) Trends Plant Sci. , vol.6 , pp. 262-267
    • Knight, H.1    Knight, M.R.2
  • 95
    • 0033579561 scopus 로고    scopus 로고
    • A point mutation in a plant calmodulin is responsible for its inhibition of nitric-oxide synthase
    • Kondo R, Tikunova SB, Cho MJ, Johnson JD. 1999. A point mutation in a plant calmodulin is responsible for its inhibition of nitric-oxide synthase. J. Biol. Chem. 274:36213-18
    • (1999) J. Biol. Chem. , vol.274 , pp. 36213-36218
    • Kondo, R.1    Tikunova, S.B.2    Cho, M.J.3    Johnson, J.D.4
  • 96
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wüthrich K. 1996. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 14:51-55
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 97
    • 0033080475 scopus 로고    scopus 로고
    • The wheat peptidyl prolyl cis-trans-isomerase FKBP77 is heat induced and developmentally regulated
    • Kurek I, Aviezer K, Erel N, Herman E, Breiman A. 1999. The wheat peptidyl prolyl cis-trans-isomerase FKBP77 is heat induced and developmentally regulated. Plant Physiol. 119:693-704
    • (1999) Plant Physiol. , vol.119 , pp. 693-704
    • Kurek, I.1    Aviezer, K.2    Erel, N.3    Herman, E.4    Breiman, A.5
  • 98
    • 0347297339 scopus 로고    scopus 로고
    • Wheat FKBP73 functions in vitro as a molecular chaperone independently of its peptidyl prolyl cis-trans isomerase activity
    • Kurek I, Pirkl F, Fischer E, Buchner J, Breiman A. 2002. Wheat FKBP73 functions in vitro as a molecular chaperone independently of its peptidyl prolyl cis-trans isomerase activity. Planta 215:119-26
    • (2002) Planta , vol.215 , pp. 119-126
    • Kurek, I.1    Pirkl, F.2    Fischer, E.3    Buchner, J.4    Breiman, A.5
  • 99
    • 0036702494 scopus 로고    scopus 로고
    • Overexpression of the wheat FK506-binding protein 73 (FKBP73) and the heat-induced wheat FKBP77 in transgenic wheat reveals different functions of the two isoforms
    • Kurek I, Stoger E, Dulberger R, Christou P, Breiman A. 2002. Overexpression of the wheat FK506-binding protein 73 (FKBP73) and the heat-induced wheat FKBP77 in transgenic wheat reveals different functions of the two isoforms. Transgenic Res. 11:373-79
    • (2002) Transgenic Res. , vol.11 , pp. 373-379
    • Kurek, I.1    Stoger, E.2    Dulberger, R.3    Christou, P.4    Breiman, A.5
  • 101
    • 2442664337 scopus 로고    scopus 로고
    • Analysis of nitric oxide signaling functions in tobacco cells challenged by the elicitor cryptogein
    • Lamotte O, Gould K, Lecourieux D, Sequeira-Legrand A, Lebrun-Garcia A, et al. 2004. Analysis of nitric oxide signaling functions in tobacco cells challenged by the elicitor cryptogein. Plant Physiol. 135:516-29
    • (2004) Plant Physiol. , vol.135 , pp. 516-529
    • Lamotte, O.1    Gould, K.2    Lecourieux, D.3    Sequeira-Legrand, A.4    Lebrun-Garcia, A.5
  • 102
    • 2042437650 scopus 로고    scopus 로고
    • Initial sequencing and analysis of the human genome
    • Lander ES, Linton LM, Birren B, Nusbaum C, Zody MC, et al. International Human Genome Sequencing Consortium. 2001. Initial sequencing and analysis of the human genome. Nature 409:860-921
    • (2001) Nature , vol.409 , pp. 860-921
    • Lander, E.S.1    Linton, L.M.2    Birren, B.3    Nusbaum, C.4    Zody, M.C.5
  • 103
    • 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. 128:682-95
    • (2002) Plant Physiol. , vol.128 , pp. 682-695
    • Larkindale, J.1    Knight, M.R.2
  • 104
    • 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 14:2627-41
    • (2002) Plant Cell , vol.14 , pp. 2627-2641
    • Lecourieux, D.1    Mazars, C.2    Pauly, N.3    Ranjeva, R.4    Pugin, A.5
  • 105
    • 2942677358 scopus 로고    scopus 로고
    • Proteomic identification of annexins, calcium-dependent membrane binding proteins that mediate osmotic stress and abscisic acid signal transduction in Arabidopsis
    • Lee EJ, Yang EJ, Lee JE, Park AR, Song WH, Park OK. 2004. Proteomic identification of annexins, calcium-dependent membrane binding proteins that mediate osmotic stress and abscisic acid signal transduction in Arabidopsis. Plant Cell 16:1378-91
    • (2004) Plant Cell , vol.16 , pp. 1378-1391
    • Lee, E.J.1    Yang, E.J.2    Lee, J.E.3    Park, A.R.4    Song, W.H.5    Park, O.K.6
  • 106
    • 0035010868 scopus 로고    scopus 로고
    • A harpin binding site in tobacco plasma membranes mediates activation of the pathogenesis-related gene HIN1 independent of extracellular calcium but dependent on mitogen-activated protein kinase activity
    • Lee J, Klessig DF, Nurnberger T. 2001. A harpin binding site in tobacco plasma membranes mediates activation of the pathogenesis-related gene HIN1 independent of extracellular calcium but dependent on mitogen-activated protein kinase activity. Plant Cell 13:1079-93
    • (2001) Plant Cell , vol.13 , pp. 1079-1093
    • Lee, J.1    Klessig, D.F.2    Nurnberger, T.3
  • 108
    • 0032813204 scopus 로고    scopus 로고
    • Competitive binding of calmodulin isoforms to calmodulin-binding proteins: Implication for the function of calmodulin isoforms in plants
    • Lee SH, Kim MC, Heo WD, Kim JC, Chung WS, et al. 1999. Competitive binding of calmodulin isoforms to calmodulin-binding proteins: implication for the function of calmodulin isoforms in plants. Biochim. Biophys. Acta 1433:56-67
    • (1999) Biochim. Biophys. Acta , vol.1433 , pp. 56-67
    • Lee, S.H.1    Kim, M.C.2    Heo, W.D.3    Kim, J.C.4    Chung, W.S.5
  • 109
    • 0001281471 scopus 로고    scopus 로고
    • Differential activation of NAD kinase by plant calmodulin isoforms. The critical role of domain I
    • Lee SH, Seo HY, Kim JC, Heo WD, Chung WS, et al. 1997. Differential activation of NAD kinase by plant calmodulin isoforms. The critical role of domain I. J. Biol. Chem. 272:9252-59
    • (1997) J. Biol. Chem. , vol.272 , pp. 9252-9259
    • Lee, S.H.1    Seo, H.Y.2    Kim, J.C.3    Heo, W.D.4    Chung, W.S.5
  • 110
    • 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. 6:427-37
    • (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
  • 111
    • 0029441618 scopus 로고
    • Production of recombinant plant calmodulin and its use to detect calmodulin-binding proteins
    • Liao B, Zielinski RE. 1995. Production of recombinant plant calmodulin and its use to detect calmodulin-binding proteins. Methods Cell Biol. 49:487-500
    • (1995) Methods Cell Biol. , vol.49 , pp. 487-500
    • Liao, B.1    Zielinski, R.E.2
  • 112
    • 0028486212 scopus 로고
    • Analysis of a soluble calmodulin binding protein from fava bean roots: Identification of glutamate decarboxylase as a calmodulin-activated enzyme
    • Ling V, Snedden WA, Shelp BJ, Assmann SM. 1994. Analysis of a soluble calmodulin binding protein from fava bean roots: identification of glutamate decarboxylase as a calmodulin-activated enzyme. Plant Cell 6:1135-43
    • (1994) Plant Cell , vol.6 , pp. 1135-1143
    • Ling, V.1    Snedden, W.A.2    Shelp, B.J.3    Assmann, S.M.4
  • 113
    • 0038715263 scopus 로고    scopus 로고
    • Calmodulin is involved in heat shock signal transduction in wheat
    • Liu HT, Li B, Shang ZL, Li XZ, Mu RL, et al. 2003. Calmodulin is involved in heat shock signal transduction in wheat. Plant Physiol. 132:1186-95
    • (2003) Plant Physiol. , vol.132 , pp. 1186-1195
    • Liu, H.T.1    Li, B.2    Shang, Z.L.3    Li, X.Z.4    Mu, R.L.5
  • 114
    • 0028007935 scopus 로고
    • Isolation of tobacco cDNA clones encoding calmodulin-binding proteins and characterization of a known calmodulin-binding domain
    • Lu Y-T, Harrington HM. 1994. Isolation of tobacco cDNA clones encoding calmodulin-binding proteins and characterization of a known calmodulin-binding domain. Plant Physiol. Biochem. 32:413-22
    • (1994) Plant Physiol. Biochem. , vol.32 , pp. 413-422
    • Lu, Y.-T.1    Harrington, H.M.2
  • 115
    • 0029328290 scopus 로고
    • Characterization of a cDNA encoding a novel heat-shock protein that binds to calmodulin
    • Lu YT, Dharmasiri MA, Harrington HM. 1995. Characterization of a cDNA encoding a novel heat-shock protein that binds to calmodulin. Plant Physiol. 108:1197-202
    • (1995) Plant Physiol. , vol.108 , pp. 1197-1202
    • Lu, Y.T.1    Dharmasiri, M.A.2    Harrington, H.M.3
  • 116
    • 0036276574 scopus 로고    scopus 로고
    • Calmodulins and calcineurin B-like proteins: Calcium sensors for specific signal response coupling in plants
    • Luan S, Kudla J, Rodriguez-Concepcion M, Yalovsky S, Gruissem W. 2002. Calmodulins and calcineurin B-like proteins: calcium sensors for specific signal response coupling in plants. Plant Cell 14:S389-400
    • (2002) Plant Cell , vol.14
    • Luan, S.1    Kudla, J.2    Rodriguez-Concepcion, M.3    Yalovsky, S.4    Gruissem, W.5
  • 117
    • 1642564016 scopus 로고    scopus 로고
    • CDPK-mediated signalling pathways: Specificity and cross-talk
    • Ludwig AA, Romeis T, Jones JD. 2004. CDPK-mediated signalling pathways: specificity and cross-talk. J. Exp. Bot. 55:181-88
    • (2004) J. Exp. Bot. , vol.55 , pp. 181-188
    • Ludwig, A.A.1    Romeis, T.2    Jones, J.D.3
  • 118
    • 0141455272 scopus 로고    scopus 로고
    • Overexpression of glutamate decarboxylase in transgenic tobacco plants deters feeding by phytophagous insect larvae
    • MacGregor KB, Shelp BJ, Peiris S, Bown AW. 2003. Overexpression of glutamate decarboxylase in transgenic tobacco plants deters feeding by phytophagous insect larvae. J. Chem. Ecol. 29:2177-82
    • (2003) J. Chem. Ecol. , vol.29 , pp. 2177-2182
    • MacGregor, K.B.1    Shelp, B.J.2    Peiris, S.3    Bown, A.W.4
  • 119
    • 0037853748 scopus 로고    scopus 로고
    • Phylogenetic relationships within cation transporter families of Arabidopsis
    • Maser P, Thomine S, Schroeder JI, Ward JM, Hirschi K, et al. 2001. Phylogenetic relationships within cation transporter families of Arabidopsis. Plant Physiol. 126:1646-67
    • (2001) Plant Physiol. , vol.126 , pp. 1646-1667
    • Maser, P.1    Thomine, S.2    Schroeder, J.I.3    Ward, J.M.4    Hirschi, K.5
  • 120
    • 0042466588 scopus 로고    scopus 로고
    • Calmodulins and related potential calcium sensors in Arabidopsis
    • McCormack E, Braam J. 2003. Calmodulins and related potential calcium sensors in Arabidopsis. New Phytol. 159:585-98
    • (2003) New Phytol. , vol.159 , pp. 585-598
    • McCormack, E.1    Braam, J.2
  • 121
    • 1842532201 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase required for symbiotic nodule development: Gene identification by transcript-based cloning
    • 2+/calmodulin-dependent protein kinase required for symbiotic nodule development: gene identification by transcript-based cloning. Proc. Natl. Acad. Sci. USA 101:4701-5
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4701-4705
    • Mitra, R.M.1    Gleason, C.A.2    Edwards, A.3    Hadfield, J.4    Downie, J.A.5
  • 123
    • 0036845182 scopus 로고    scopus 로고
    • Comprehensive transcript profiling of Pto- and Prf-mediated host defense responses to infection by Pseudomonas syringae pv. tomato
    • Mysore KS, Crasta OR, Tuori RP, Folkerts O, Swirsky PB, Martin GB. 2002. Comprehensive transcript profiling of Pto- and Prf-mediated host defense responses to infection by Pseudomonas syringae pv. tomato. Plant J. 32:299-315
    • (2002) Plant J. , vol.32 , pp. 299-315
    • Mysore, K.S.1    Crasta, O.R.2    Tuori, R.P.3    Folkerts, O.4    Swirsky, P.B.5    Martin, G.B.6
  • 124
    • 12944282356 scopus 로고    scopus 로고
    • Cell cycle-dependent transcriptional regulation of calmodulin-binding transcription activator 1 in neuroblastoma cells
    • Nakatani K, Nishioka J, Itakura T, Nakanishi Y, Horinouchi J, et al. 2004. Cell cycle-dependent transcriptional regulation of calmodulin-binding transcription activator 1 in neuroblastoma cells. Int. J. Oncol. 24:1407-12
    • (2004) Int. J. Oncol. , vol.24 , pp. 1407-1412
    • Nakatani, K.1    Nishioka, J.2    Itakura, T.3    Nakanishi, Y.4    Horinouchi, J.5
  • 125
    • 0001939211 scopus 로고    scopus 로고
    • Evolution of EF-hand proteins
    • ed. E Carafoli, J Krebs New York: Springer
    • Nakayama S, Kawasaki H, Krestinger R. 2000. Evolution of EF-hand proteins. In Calcium Homeostasis, ed. E Carafoli, J Krebs. pp. 29-58. New York: Springer
    • (2000) Calcium Homeostasis , pp. 29-58
    • Nakayama, S.1    Kawasaki, H.2    Krestinger, R.3
  • 126
    • 0024396312 scopus 로고
    • Crystal structure of the helix-loop-helix calcium-binding proteins
    • Natalie C, Strynadka J, James MNG. 1989. Crystal structure of the helix-loop-helix calcium-binding proteins. Annu. Rev. Biochem. 58:951-58
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 951-958
    • Natalie, C.1    Strynadka, J.2    James, M.N.G.3
  • 128
    • 1542389625 scopus 로고    scopus 로고
    • Encoding specificity in plant calcium signalling: Hot-spotting the ups and downs and waves
    • Ng CK-Y, Mc Ainsh MR. 2003. Encoding specificity in plant calcium signalling: hot-spotting the ups and downs and waves. Ann. Bot. 92:477-85
    • (2003) Ann. Bot. , vol.92 , pp. 477-485
    • Ng, C.K.-Y.1    Mc Ainsh, M.R.2
  • 130
    • 0028266837 scopus 로고
    • Diverse essential functions revealed by complementing yeast calmodulin mutants
    • Ohya Y, Botstein D. 1994. Diverse essential functions revealed by complementing yeast calmodulin mutants. Science 263:963-66
    • (1994) Science , vol.263 , pp. 963-966
    • Ohya, Y.1    Botstein, D.2
  • 131
    • 1942477681 scopus 로고    scopus 로고
    • Expression of bovine calmodulin in tobacco plants confers faster germination on saline media
    • Olsson P, Yilmaz JL, Sommarin M, Persson S, Bulow L. 2004. Expression of bovine calmodulin in tobacco plants confers faster germination on saline media. Plant Sci. 166:1595-604
    • (2004) Plant Sci. , vol.166 , pp. 1595-1604
    • Olsson, P.1    Yilmaz, J.L.2    Sommarin, M.3    Persson, S.4    Bulow, L.5
  • 132
    • 0038446879 scopus 로고    scopus 로고
    • Pollen tube growth and guidance is regulated by POP2, an Arabidopsis gene that controls GABA levels
    • Palanivelu R, Brass L, Edlund AF, Preuss D. 2003. Pollen tube growth and guidance is regulated by POP2, an Arabidopsis gene that controls GABA levels. Cell 114:47-59
    • (2003) Cell , vol.114 , pp. 47-59
    • Palanivelu, R.1    Brass, L.2    Edlund, A.F.3    Preuss, D.4
  • 134
    • 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 BC, Jauneau A, Galaud JP, et al. 2004. A novel calmodulin-binding protein functions as a negative regulator of osmotic stress tolerance in Arabidopsis thaliana seedlings. Plant J. 38:410-20
    • (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
  • 135
    • 0037986719 scopus 로고    scopus 로고
    • The cotton kinesin-like calmodulin-binding protein associates with cortical microtubules in cotton fibers
    • Preuss ML, Delmer DP, Liu B. 2003. The cotton kinesin-like calmodulin-binding protein associates with cortical microtubules in cotton fibers. Plant Physiol. 132:154-60
    • (2003) Plant Physiol. , vol.132 , pp. 154-160
    • Preuss, M.L.1    Delmer, D.P.2    Liu, B.3
  • 136
    • 0031420922 scopus 로고    scopus 로고
    • Early events induced by the elicitor cryptogein in tobacco cells: Involvement of a plasma membrane NADPH oxidase and activation of glycolysis and the pentose phosphate pathway
    • Pugin A, Frachisse JM, Tavernier E, Bligny R, Gout E, et al. 1997. Early events induced by the elicitor cryptogein in tobacco cells: involvement of a plasma membrane NADPH oxidase and activation of glycolysis and the pentose phosphate pathway. Plant Cell 9:2077-91
    • (1997) Plant Cell , vol.9 , pp. 2077-2091
    • Pugin, A.1    Frachisse, J.M.2    Tavernier, E.3    Bligny, R.4    Gout, E.5
  • 138
    • 2942708089 scopus 로고    scopus 로고
    • Calmodulin activity and cAMP signalling modulate growth and apical secretion in pollen tubes
    • Rato C, Monteiro D, Hepler PK, Malho R. 2004. Calmodulin activity and cAMP signalling modulate growth and apical secretion in pollen tubes. Plant J. 38:887-97
    • (2004) Plant J. , vol.38 , pp. 887-897
    • Rato, C.1    Monteiro, D.2    Hepler, P.K.3    Malho, R.4
  • 139
    • 0034486236 scopus 로고    scopus 로고
    • The role of the cytoskeleton and a molecular motor in trichome morphogenesis
    • Reddy AS, Day IS. 2000. The role of the cytoskeleton and a molecular motor in trichome morphogenesis. Trends Plant Sci. 5:503-5
    • (2000) Trends Plant Sci. , vol.5 , pp. 503-505
    • Reddy, A.S.1    Day, I.S.2
  • 140
    • 0034731413 scopus 로고    scopus 로고
    • A calmodulin binding protein from Arabidopsis is induced by ethylene and contains a DNA-binding motif
    • Reddy AS, Reddy VS, Golovkin M. 2000. A calmodulin binding protein from Arabidopsis is induced by ethylene and contains a DNA-binding motif. Biochem. Biophys. Res. Commun. 279:762-69
    • (2000) Biochem. Biophys. Res. Commun. , vol.279 , pp. 762-769
    • Reddy, A.S.1    Reddy, V.S.2    Golovkin, M.3
  • 141
    • 0032245891 scopus 로고    scopus 로고
    • High-molecular-weight FK506-binding proteins are components of heat-shock protein 90 heterocomplexes in wheat germ lysate
    • Reddy RK, Kurek I, Silverstein AM, Chinkers M, Breiman A, Krishna P. 1998. High-molecular-weight FK506-binding proteins are components of heat-shock protein 90 heterocomplexes in wheat germ lysate. Plant Physiol. 118:1395-401
    • (1998) Plant Physiol. , vol.118 , pp. 1395-1401
    • Reddy, R.K.1    Kurek, I.2    Silverstein, A.M.3    Chinkers, M.4    Breiman, A.5    Krishna, P.6
  • 143
    • 0037155853 scopus 로고    scopus 로고
    • Genes encoding calmodulin-binding proteins in the Arabidopsis genome
    • Reddy VS, Ali GS, Reddy ASN. 2002. Genes encoding calmodulin-binding proteins in the Arabidopsis genome. J. Biol. Chem. 277:9840-52
    • (2002) J. Biol. Chem. , vol.277 , pp. 9840-9852
    • Reddy, V.S.1    Ali, G.S.2    Reddy, A.S.N.3
  • 144
    • 0842334764 scopus 로고    scopus 로고
    • 2+ binding protein with one EF-hand motif, interacts with a microtubule motor protein and regulates trichome morphogenesis
    • 2+ binding protein with one EF-hand motif, interacts with a microtubule motor protein and regulates trichome morphogenesis. Plant Cell 16:185-200
    • (2004) Plant Cell , vol.16 , pp. 185-200
    • Reddy, V.S.1    Day, I.S.2    Thomas, T.3    Reddy, A.S.4
  • 145
    • 0037073731 scopus 로고    scopus 로고
    • 2+-calmodulin regulation to animal plus- and minus-end kinesins
    • 2+-calmodulin regulation to animal plus- and minus-end kinesins. J. Biol. Chem. 277:48058-65
    • (2002) J. Biol. Chem. , vol.277 , pp. 48058-48065
    • Reddy, V.S.1    Reddy, A.S.2
  • 146
    • 3242768512 scopus 로고    scopus 로고
    • Proteomics of calcium-signaling components in plants
    • Reddy VS, Reddy ASN. 2004. Proteomics of calcium-signaling components in plants. Phytochemistry 65:1745-76
    • (2004) Phytochemistry , vol.65 , pp. 1745-1776
    • Reddy, V.S.1    Reddy, A.S.N.2
  • 147
    • 3543003536 scopus 로고    scopus 로고
    • Oxidative stress-induced calcium signaling in Arabidopsis thaliana
    • Rentel MR, Knight MR. 2004. Oxidative stress-induced calcium signaling in Arabidopsis thaliana. Plant Physiol. 135:1471-79
    • (2004) Plant Physiol. , vol.135 , pp. 1471-1479
    • Rentel, M.R.1    Knight, M.R.2
  • 148
    • 0041896859 scopus 로고    scopus 로고
    • The prenylation status of a novel plant calmodulin directs plasma membrane or nuclear localization of the protein
    • Rodriguez-Concepcion M, Yalovsky S, Zik M, Fromm H, Gruissem W. 1999. The prenylation status of a novel plant calmodulin directs plasma membrane or nuclear localization of the protein. EMBO J. 18:1996-2007
    • (1999) EMBO J. , vol.18 , pp. 1996-2007
    • Rodriguez-Concepcion, M.1    Yalovsky, S.2    Zik, M.3    Fromm, H.4    Gruissem, W.5
  • 149
    • 0033585135 scopus 로고    scopus 로고
    • Identification of kinesin-C, a calmodulin-binding carboxy-terminal kinesin in animal (Strongylocentrotus purpuratus) cells
    • Rogers GC, Hart CL, Wedaman KP, Scholey JM. 1999. Identification of kinesin-C, a calmodulin-binding carboxy-terminal kinesin in animal (Strongylocentrotus purpuratus) cells. J. Mol. Biol. 294:1-8
    • (1999) J. Mol. Biol. , vol.294 , pp. 1-8
    • Rogers, G.C.1    Hart, C.L.2    Wedaman, K.P.3    Scholey, J.M.4
  • 150
    • 0034634639 scopus 로고    scopus 로고
    • A pollen-specific novel calmodulin-binding protein with tetratricopeptide repeats
    • Safadi F, Reddy VS, Reddy ASN. 2000. A pollen-specific novel calmodulin-binding protein with tetratricopeptide repeats. J. Biol. Chem. 275:35457-70
    • (2000) J. Biol. Chem. , vol.275 , pp. 35457-35470
    • Safadi, F.1    Reddy, V.S.2    Reddy, A.S.N.3
  • 152
    • 0032731314 scopus 로고    scopus 로고
    • Metabolism and functions of gamma-aminobutyric acid
    • Shelp BJ, Bown AW, McLean MD. 1999. Metabolism and functions of gamma-aminobutyric acid. Trends Plant Sci. 4:446-52
    • (1999) Trends Plant Sci. , vol.4 , pp. 446-452
    • Shelp, B.J.1    Bown, A.W.2    McLean, M.D.3
  • 153
    • 0033601331 scopus 로고    scopus 로고
    • Different regions of the immunophilin FKBP52 determine its association with the glucocorticoid receptor, hsp90, and cytoplasmic dynein
    • Silverstein AM, Galigniana MD, Kanelakis KC, Radanyi C, Renoir JM, Pratt WB. 1999. Different regions of the immunophilin FKBP52 determine its association with the glucocorticoid receptor, hsp90, and cytoplasmic dynein. J. Biol. Chem. 274:36980-86
    • (1999) J. Biol. Chem. , vol.274 , pp. 36980-36986
    • Silverstein, A.M.1    Galigniana, M.D.2    Kanelakis, K.C.3    Radanyi, C.4    Renoir, J.M.5    Pratt, W.B.6
  • 154
    • 0028830815 scopus 로고
    • Calcium/calmodulin activation of soybean glutamate decarboxylase
    • Snedden WA, Arazi T, Fromm H, Shelp BJ. 1995. Calcium/calmodulin activation of soybean glutamate decarboxylase. Plant Physiol. 108:543-49
    • (1995) Plant Physiol. , vol.108 , pp. 543-549
    • Snedden, W.A.1    Arazi, T.2    Fromm, H.3    Shelp, B.J.4
  • 155
    • 0001863779 scopus 로고    scopus 로고
    • Regulation of the γ-aminobutyrate-synthesizing enzyme, glutamate decarboxylase, by calcium-calmodulin: A mechanism for rapid activation in response to stress
    • ed. HR Lerner, New York: Marcel Dekker
    • Snedden WA, Fromm H. 1999. Regulation of the γ-aminobutyrate- synthesizing enzyme, glutamate decarboxylase, by calcium-calmodulin: a mechanism for rapid activation in response to stress. In Plant Responses to Environmental Stresses: From Phytohormones to Genome Reorganization, ed. HR Lerner, pp. 549-74 . New York: Marcel Dekker
    • (1999) Plant Responses to Environmental Stresses: from Phytohormones to Genome Reorganization , pp. 549-574
    • Snedden, W.A.1    Fromm, H.2
  • 156
    • 0034945001 scopus 로고    scopus 로고
    • Calmodulin as a versatile calcium signal transducer in plants
    • Snedden WA, 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
  • 157
    • 0030060208 scopus 로고    scopus 로고
    • Activation of a recombinant petunia glutamate decarboxylase by calcium/calmodulin or by a monoclonal antibody which recognizes the calmodulin binding domain
    • Snedden WA, Koutsia N, Baum G, Fromm H. 1996. Activation of a recombinant petunia glutamate decarboxylase by calcium/calmodulin or by a monoclonal antibody which recognizes the calmodulin binding domain. J. Biol. Chem. 271:4148-53
    • (1996) J. Biol. Chem. , vol.271 , pp. 4148-4153
    • Snedden, W.A.1    Koutsia, N.2    Baum, G.3    Fromm, H.4
  • 158
    • 0034496345 scopus 로고    scopus 로고
    • Molecular and biochemical comparison of two different apyrases from Arabidopsis thaliana
    • Steinebrunner I, Jeter C, Song C, Roux SJ. 2000. Molecular and biochemical comparison of two different apyrases from Arabidopsis thaliana. Plant Physiol. Biochem. 38:913-22
    • (2000) Plant Physiol. Biochem. , vol.38 , pp. 913-922
    • Steinebrunner, I.1    Jeter, C.2    Song, C.3    Roux, S.J.4
  • 159
    • 0037391711 scopus 로고    scopus 로고
    • Disruption of apyrases inhibits pollen germination in Arabidopsis
    • Steinebrunner I, Wu J, Sun Y, Corbett A, Roux SJ. 2003. Disruption of apyrases inhibits pollen germination in Arabidopsis. Plant Physiol. 131:1638-47
    • (2003) Plant Physiol. , vol.131 , pp. 1638-1647
    • Steinebrunner, I.1    Wu, J.2    Sun, Y.3    Corbett, A.4    Roux, S.J.5
  • 160
    • 0033949661 scopus 로고    scopus 로고
    • Binding of the maize cytosolic Hsp70 to calmodulin, and identification of calmodulin-binding site in Hsp70
    • Sun XT, Li B, Zhou GM, Tang WQ, Bai J, et al. 2000. Binding of the maize cytosolic Hsp70 to calmodulin, and identification of calmodulin-binding site in Hsp70. Plant Physiol. 41:804-10
    • (2000) Plant Physiol. , vol.41 , pp. 804-810
    • Sun, X.T.1    Li, B.2    Zhou, G.M.3    Tang, W.Q.4    Bai, J.5
  • 162
    • 1842426646 scopus 로고    scopus 로고
    • Calmodulin-binding proteins in bryophytes: Identification of abscisic acid-, cold-, and osmotic stress-induced genes encoding novel membrane-bound transporter-like proteins
    • Takezawa D, Minami A. 2004. Calmodulin-binding proteins in bryophytes: identification of abscisic acid-, cold-, and osmotic stress-induced genes encoding novel membrane-bound transporter-like proteins. Biochem. Biophys. Res. Commun. 317:428-36
    • (2004) Biochem. Biophys. Res. Commun. , vol.317 , pp. 428-436
    • Takezawa, D.1    Minami, A.2
  • 165
    • 0036010640 scopus 로고    scopus 로고
    • Calmodulin as a potential negative regulator of Arabidopsis COR gene expression
    • Townley HE, Knight MR. 2002. Calmodulin as a potential negative regulator of Arabidopsis COR gene expression. Plant Physiol. 128:1169-72
    • (2002) Plant Physiol. , vol.128 , pp. 1169-1172
    • Townley, H.E.1    Knight, M.R.2
  • 166
    • 0041589199 scopus 로고    scopus 로고
    • Intracellular coupling via limiting calmodulin
    • Tran QK, Black DJ, Persechini A. 2003. Intracellular coupling via limiting calmodulin. J. Biol. Chem. 278:24247-50
    • (2003) J. Biol. Chem. , vol.278 , pp. 24247-24250
    • Tran, Q.K.1    Black, D.J.2    Persechini, A.3
  • 168
    • 0032135219 scopus 로고    scopus 로고
    • Characterization of two glutamate decarboxylase cDNA clones from Arabidopsis
    • Turano FJ, Fang TK, 1998. Characterization of two glutamate decarboxylase cDNA clones from Arabidopsis. Plant Physiol. 117:1411-21
    • (1998) Plant Physiol. , vol.117 , pp. 1411-1421
    • Turano, F.J.1    Fang, T.K.2
  • 169
    • 3543001681 scopus 로고    scopus 로고
    • Cloning and characterization of two NAD kinases from Arabidopsis: Identification of a calmodulin binding isoform
    • Turner WL, Waller JC, Vanderbeld B, Snedden WA. 2004. Cloning and characterization of two NAD kinases from Arabidopsis: identification of a calmodulin binding isoform. Plant Physiol. 135:1243-55
    • (2004) Plant Physiol. , vol.135 , pp. 1243-1255
    • Turner, W.L.1    Waller, J.C.2    Vanderbeld, B.3    Snedden, W.A.4
  • 171
    • 0142245606 scopus 로고    scopus 로고
    • Interaction of calmodulin, a sorting nexin and kinase-associated protein phosphatase with the Brassica oleracea S locus receptor kinase
    • Vanoosthuyse V, Tichtinsky G, Dumas C, Gaude T, Cock JM. 2003. Interaction of calmodulin, a sorting nexin and kinase-associated protein phosphatase with the Brassica oleracea S locus receptor kinase. Plant Physiol. 133:919-29
    • (2003) Plant Physiol. , vol.133 , pp. 919-929
    • Vanoosthuyse, V.1    Tichtinsky, G.2    Dumas, C.3    Gaude, T.4    Cock, J.M.5
  • 172
    • 0037318056 scopus 로고    scopus 로고
    • Novel aspects of calmodulin target recognition and activation
    • Vetter SW, Leclerc E. 2003. Novel aspects of calmodulin target recognition and activation. Eur. J. Biochem. 270:404-14
    • (2003) Eur. J. Biochem. , vol.270 , pp. 404-414
    • Vetter, S.W.1    Leclerc, E.2
  • 174
    • 20444419242 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 177
    • 0037382949 scopus 로고    scopus 로고
    • Multiherbicide tolerance conferred by AtPgp1 and apyrase overexpression in Arabidopsis thaliana
    • Windsor B, Roux SJ, Lloyd A. 2003. Multiherbicide tolerance conferred by AtPgp1 and apyrase overexpression in Arabidopsis thaliana. Nat. Biotechnol. 21:428-33
    • (2003) Nat. Biotechnol. , vol.21 , pp. 428-433
    • Windsor, B.1    Roux, S.J.2    Lloyd, A.3
  • 178
    • 0036582580 scopus 로고    scopus 로고
    • Towards genomic and proteomic studies of protein phosphorylation in plant-pathogen interactions
    • Xing T, Ouellet T, Miki BL. 2002. Towards genomic and proteomic studies of protein phosphorylation in plant-pathogen interactions. Trends Plant Sci. 7:224-30
    • (2002) Trends Plant Sci. , vol.7 , pp. 224-230
    • Xing, T.1    Ouellet, T.2    Miki, B.L.3
  • 179
    • 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 10:585-98
    • (1998) Plant Cell , vol.10 , pp. 585-598
    • Xu, H.1    Heath, M.C.2
  • 181
    • 0034835238 scopus 로고    scopus 로고
    • Transcriptionally and post-transcriptionally regulated response of 13 calmodulin genes to tobacco mosaic virus-induced cell death and wounding in tobacco plant
    • Yamakawa H, Mitsuhara I, Ito N, Seo S, Kamada H, Ohashi Y. 2001. Transcriptionally and post-transcriptionally regulated response of 13 calmodulin
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3916-3929
    • Yamakawa, H.1    Mitsuhara, I.2    Ito, N.3    Seo, S.4    Kamada, H.5    Ohashi, Y.6
  • 182
    • 1942496481 scopus 로고    scopus 로고
    • Calmodulin's flexibility allows for promiscuity in its interactions with target proteins and peptides
    • Yamniuk AP, Vogel HJ. 2004. Calmodulin's flexibility allows for promiscuity in its interactions with target proteins and peptides. Mol. Biotechnol. 27:33-57
    • (2004) Mol. Biotechnol. , vol.27 , pp. 33-57
    • Yamniuk, A.P.1    Vogel, H.J.2
  • 183
    • 0034726456 scopus 로고    scopus 로고
    • Arabidopsis chloroplast chaperonin 10 is a calmodulin-binding protein
    • Yang T, Poovaiah BW. 2000. Arabidopsis chloroplast chaperonin 10 is a calmodulin-binding protein. Biochem. Biophys. Res. Commun. 275:601-7
    • (2000) Biochem. Biophys. Res. Commun. , vol.275 , pp. 601-607
    • Yang, T.1    Poovaiah, B.W.2
  • 184
    • 0034624051 scopus 로고    scopus 로고
    • An early ethylene up-regulated gene encoding a calmodulin-binding protein involved in plant senescence and death
    • Yang T, Poovaiah BW. 2000. An early ethylene up-regulated gene encoding a calmodulin-binding protein involved in plant senescence and death. J. Biol. Chem. 275:38467-73
    • (2000) J. Biol. Chem. , vol.275 , pp. 38467-38473
    • Yang, T.1    Poovaiah, B.W.2
  • 185
    • 0034603001 scopus 로고    scopus 로고
    • Molecular and biochemical evidence for the involvement of calcium/calmodulin in auxin action
    • Yang T, Poovaiah BW. 2000. Molecular and biochemical evidence for the involvement of calcium/calmodulin in auxin action. J. Biol. Chem. 275:3137-43
    • (2000) J. Biol. Chem. , vol.275 , pp. 3137-3143
    • Yang, T.1    Poovaiah, B.W.2
  • 186
    • 0037160040 scopus 로고    scopus 로고
    • A calmodulin-binding/CGCG box DNA-binding protein family involved in multiple signaling pathways in plants
    • Yang T, Poovaiah BW. 2002. A calmodulin-binding/CGCG box DNA-binding protein family involved in multiple signaling pathways in plants. J. Biol. Chem. 277:45049-58
    • (2002) J. Biol. Chem. , vol.277 , pp. 45049-45058
    • Yang, T.1    Poovaiah, B.W.2
  • 187
    • 0037133690 scopus 로고    scopus 로고
    • Hydrogen peroxide homeostasis: Activation of plant catalase by calcium/calmodulin
    • Yang T, Poovaiah BW. 2002. Hydrogen peroxide homeostasis: activation of plant catalase by calcium/calmodulin. Proc. Natl. Acad. Sci. USA 99:4097-102
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 4097-4102
    • Yang, T.1    Poovaiah, B.W.2
  • 188
    • 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. 8:505-12
    • (2003) Trends Plant Sci. , vol.8 , pp. 505-512
    • Yang, T.1    Poovaiah, B.W.2
  • 189
    • 0029999946 scopus 로고    scopus 로고
    • Characterization of the calmodulin gene family in wheat: Structure, chromosomal location, and evolutionary aspects
    • Yang T, Segal G, Abbo S, Feldman M, Fromm H. 1996. Characterization of the calmodulin gene family in wheat: structure, chromosomal location, and evolutionary aspects. Mol. Gen. Genet. 252:684-94
    • (1996) Mol. Gen. Genet. , vol.252 , pp. 684-694
    • Yang, T.1    Segal, G.2    Abbo, S.3    Feldman, M.4    Fromm, H.5
  • 190
    • 0037453258 scopus 로고    scopus 로고
    • Structural basis for simultaneous binding of two carboxy-terminal peptides of plant glutamate decarboxylase to calmodulin
    • Yap KL, Yuan T, Mal TK, Vogel HJ, Ikura M. 2003. Structural basis for simultaneous binding of two carboxy-terminal peptides of plant glutamate decarboxylase to calmodulin. J. Mol. Biol. 328:193-204
    • (2003) J. Mol. Biol. , vol.328 , pp. 193-204
    • Yap, K.L.1    Yuan, T.2    Mal, T.K.3    Vogel, H.J.4    Ikura, M.5
  • 192
    • 0032580023 scopus 로고    scopus 로고
    • Cloning and characterization of a tobacco cDNA encoding calcium/calmodulin-dependent glutamate decarboxylase
    • Yun SJ, Oh SH. 1998. Cloning and characterization of a tobacco cDNA encoding calcium/calmodulin-dependent glutamate decarboxylase. Mol. Cells 8:125-29
    • (1998) Mol. Cells , vol.8 , pp. 125-129
    • Yun, S.J.1    Oh, S.H.2
  • 193
    • 8144225726 scopus 로고    scopus 로고
    • Innate immunity in Arabidopsis thaliana: Lipopolysaccharides activate nitric oxide synthase (NOS) and induce defense genes
    • 191a. Zeidler D, Zahringer U, Gerber I, Dubery I, Hartung T, et al. 2004. Innate immunity in Arabidopsis thaliana: Lipopolysaccharides activate nitric oxide synthase (NOS) and induce defense genes. Proc. Natl. Acad. Sci. USA 101:15811-16
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15811-15816
    • Zeidler, D.1    Zahringer, U.2    Gerber, I.3    Dubery, I.4    Hartung, T.5
  • 194
    • 0035860499 scopus 로고    scopus 로고
    • Global analysis of protein activities using proteome chips
    • Zhu H, Bilgin M, Bangham R, Hall D, Casamayor A, et al. 2001. Global analysis of protein activities using proteome chips. Science 293:2101-5
    • (2001) Science , vol.293 , pp. 2101-2105
    • Zhu, H.1    Bilgin, M.2    Bangham, R.3    Hall, D.4    Casamayor, A.5
  • 195
    • 0036999615 scopus 로고    scopus 로고
    • Salt and drought stress signal transduction in plants
    • Zhu JK. 2002. Salt and drought stress signal transduction in plants. Annu. Rev. Plant Biol. 53:247-73
    • (2002) Annu. Rev. Plant Biol. , vol.53 , pp. 247-273
    • Zhu, J.K.1
  • 196
    • 0141502038 scopus 로고    scopus 로고
    • Regulation of ion homeostasis under salt stress
    • Zhu JK. 2003. Regulation of ion homeostasis under salt stress. Curr. Opin. Plant Biol. 6:441-45
    • (2003) Curr. Opin. Plant Biol. , vol.6 , pp. 441-445
    • Zhu, J.K.1
  • 198
    • 0032146950 scopus 로고    scopus 로고
    • Two isoforms of glutamate decarboxylase in Arabidopsis are regulated by calcium/calmodulin and differ in organ distribution
    • Zik M, Arazi T, Snedden WA, Fromm H. 1998. Two isoforms of glutamate decarboxylase in Arabidopsis are regulated by calcium/calmodulin and differ in organ distribution. Plant Mol. Biol. 37:967-75
    • (1998) Plant Mol. Biol. , vol.37 , pp. 967-975
    • Zik, M.1    Arazi, T.2    Snedden, W.A.3    Fromm, H.4


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