메뉴 건너뛰기




Volumn 8, Issue 10, 2003, Pages 505-512

Calcium/calmodulin-mediated signal network in plants

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; ARABIDOPSIS; EUKARYOTA;

EID: 0142245708     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tplants.2003.09.004     Document Type: Review
Times cited : (484)

References (77)
  • 1
    • 0034304906 scopus 로고    scopus 로고
    • The versatility and universality of calcium signalling
    • Berridge, M.J. et al. (2000) The versatility and universality of calcium signalling. Nat. Rev. Mol. Cell Biol. 1, 11-21
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , pp. 11-21
    • Berridge, M.J.1
  • 3
    • 0035797949 scopus 로고    scopus 로고
    • Combining genetics and cell biology to crack the code of plant cell calcium signaling
    • Allen, G.J. and Schroeder, J.I. (2001) Combining genetics and cell biology to crack the code of plant cell calcium signaling. Sci. STKE 1, RE13
    • (2001) Sci. STKE , vol.1
    • Allen, G.J.1    Schroeder, J.I.2
  • 4
    • 0033990432 scopus 로고    scopus 로고
    • Calcium signaling during abiotic stress in plants
    • Knight, H. (2000) Calcium signaling during abiotic stress in plants. Int. Rev. Cytol. 195, 269-324
    • (2000) Int. Rev. Cytol. , vol.195 , pp. 269-324
    • Knight, H.1
  • 5
    • 0036269927 scopus 로고    scopus 로고
    • Calcium at the crossroads of signaling
    • Sanders, D. et al. (2002) Calcium at the crossroads of signaling. Plant Cell 14 (Suppl. 1), S401-S417
    • (2002) Plant Cell , vol.14 , Issue.1 SUPPL.
    • Sanders, D.1
  • 6
    • 0034863998 scopus 로고    scopus 로고
    • Calcium oscillations in higher plants
    • Evans, N.H. et al. (2001) Calcium oscillations in higher plants. Curr. Opin. Plant Biol. 4, 415-420
    • (2001) Curr. Opin. Plant Biol. , vol.4 , pp. 415-420
    • Evans, N.H.1
  • 7
    • 0035809014 scopus 로고    scopus 로고
    • Calcium: Silver bullet in signaling
    • Reddy, A.S. (2001) Calcium: silver bullet in signaling. Plant Sci. 160, 381-404
    • (2001) Plant Sci. , vol.160 , pp. 381-404
    • Reddy, A.S.1
  • 8
    • 0034660508 scopus 로고    scopus 로고
    • Control of free calcium in plant cell nuclei
    • Pauly, N. et al. (2000) Control of free calcium in plant cell nuclei. Nature 405, 754-755
    • (2000) Nature , vol.405 , pp. 754-755
    • Pauly, N.1
  • 9
    • 0034945001 scopus 로고    scopus 로고
    • Calmodulin as a versatile calcium signal transducer in plants
    • Snedden, W. and Fromm, H. (2001) Calmodulin as a versatile calcium signal transducer in plants. New Physiol. 151, 35-66
    • (2001) New Physiol. , vol.151 , pp. 35-66
    • Snedden, W.1    Fromm, H.2
  • 11
    • 0037163398 scopus 로고    scopus 로고
    • Analysis of EF-hand-containing proteins in Arabidopsis
    • RESEARCH0056
    • Day, I.S. et al. (2002) Analysis of EF-hand-containing proteins in Arabidopsis. Genome Biol. 3, RESEARCH0056 (http://genomebiology. com/2002/3/10/RESEARCH/0056)
    • (2002) Genome Biol. , vol.3
    • Day, I.S.1
  • 14
    • 0035983609 scopus 로고    scopus 로고
    • Calcium signaling through protein kinases. The Arabidopsis calcium-dependent protein kinase gene family
    • Cheng, S.H. et al. (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.H.1
  • 15
    • 0036276574 scopus 로고    scopus 로고
    • Calmodulins and calcineurin B-like proteins: Calcium sensors for specific signal response coupling in plants
    • Luan, S. et al. (2002) Calmodulins and calcineurin B-like proteins: calcium sensors for specific signal response coupling in plants. Plant Cell 14, S389-S400
    • (2002) Plant Cell , vol.14
    • Luan, S.1
  • 16
    • 0034864883 scopus 로고    scopus 로고
    • Molecular evolution of calmodulin-like domain protein kinases (CDPKs) in plants and protists
    • Zhang, X. and Choi, J. (2001) Molecular evolution of calmodulin-like domain protein kinases (CDPKs) in plants and protists. J. Mol. Evol. 53, 214-224
    • (2001) J. Mol. Evol. , vol.53 , pp. 214-224
    • Zhang, X.1    Choi, J.2
  • 17
    • 0024396312 scopus 로고
    • Crystal structure of the helix-loop-helix calcium-binding proteins
    • Natalie, C. et al. (1989) Crystal structure of the helix-loop-helix calcium-binding proteins. Annu. Rev. Biochem. 58, 951-958
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 951-958
    • Natalie, C.1
  • 18
    • 0037155689 scopus 로고    scopus 로고
    • Calmodulin in action: Diversity in target recognition and activation mechanisms
    • Hoeflich, K.P. and Ikura, M. (2002) Calmodulin in action: diversity in target recognition and activation mechanisms. Cell 108, 739-742
    • (2002) Cell , vol.108 , pp. 739-742
    • Hoeflich, K.P.1    Ikura, M.2
  • 19
    • 0034681912 scopus 로고    scopus 로고
    • A novel type of calmodulin interaction in the inhibition of basic helix-loop-helix transcription factors
    • Onions, J. et al. (2000) A novel type of calmodulin interaction in the inhibition of basic helix-loop-helix transcription factors. Biochemistry 39, 4366-4374
    • (2000) Biochemistry , vol.39 , pp. 4366-4374
    • Onions, J.1
  • 20
    • 0034256090 scopus 로고    scopus 로고
    • Calmodulin: A prototypical calcium sensor
    • Chin, D. and Means, A.R. (2000) Calmodulin: a prototypical calcium sensor. Trends Cell Biol. 10, 322-328
    • (2000) Trends Cell Biol. , vol.10 , pp. 322-328
    • Chin, D.1    Means, A.R.2
  • 21
    • 0037165139 scopus 로고    scopus 로고
    • Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin
    • Drum, C. et al. (2002) Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin. Nature 415, 396-402
    • (2002) Nature , vol.415 , pp. 396-402
    • Drum, C.1
  • 22
    • 0035953757 scopus 로고    scopus 로고
    • 2+/calmodulin
    • 2+/calmodulin. Nature 410, 1120-1124
    • (2001) Nature , vol.410 , pp. 1120-1124
    • Schumacher, M.1
  • 23
    • 0037453258 scopus 로고    scopus 로고
    • Structural basis for simultaneous binding of two carboxy-terminal peptides of plant glutamate decarboxylase to calmodulin
    • Yap, K. et al. (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.1
  • 24
    • 0029999946 scopus 로고    scopus 로고
    • Characterization of the calmodulin gene family in wheat: Structure, chromosomal location, and evolutionary aspects
    • Yang, T. et al. (1996) Characterization of the calmodulin gene family in wheat: structure, chromosomal location, and evolutionary aspects. Mol. Gen. Genet. 252, 684-694
    • (1996) Mol. Gen. Genet. , vol.252 , pp. 684-694
    • Yang, T.1
  • 25
    • 0034613277 scopus 로고    scopus 로고
    • A calmodulin-related protein that suppresses posttranscriptional gene silencing in plants
    • Anandalakshmi, R. et al. (2000) A calmodulin-related protein that suppresses posttranscriptional gene silencing in plants. Science 290, 142-144
    • (2000) Science , vol.290 , pp. 142-144
    • Anandalakshmi, R.1
  • 26
    • 0028534793 scopus 로고
    • 2+ binding protein and shows environmentally induced and tissue-specific regulation
    • 2+ binding protein and shows environmentally induced and tissue-specific regulation. Plant Cell 6, 1553-1565
    • (1994) Plant Cell , vol.6 , pp. 1553-1565
    • Sistrunk, M.1
  • 27
    • 0036010640 scopus 로고    scopus 로고
    • Calmodulin as a potential negative regulator of Arabidopsis COR gene expression
    • Townley, H.E. and Knight, M.R. (2002) Calmodulin as a potential negative regulator of Arabidopsis COR gene expression. Plant Physiol. 128, 1169-1172
    • (2002) Plant Physiol. , vol.128 , pp. 1169-1172
    • Townley, H.E.1    Knight, M.R.2
  • 28
    • 0038715263 scopus 로고    scopus 로고
    • Calmodulin is involved in heat shock signal transduction in wheat
    • Liu, H. et al. (2003) Calmodulin is involved in heat shock signal transduction in wheat. Plant Physiol. 132, 1186-1195
    • (2003) Plant Physiol. , vol.132 , pp. 1186-1195
    • Liu, H.1
  • 29
    • 0038414032 scopus 로고    scopus 로고
    • Differential expression of genes encoding calmodulin-binding proteins in response to bacterial pathogens and inducers of defense responses
    • Ali, G. et al. (2003) Differential expression of genes encoding calmodulin-binding proteins in response to bacterial pathogens and inducers of defense responses. Plant Mol. Biol. 51, 803-815
    • (2003) Plant Mol. Biol. , vol.51 , pp. 803-815
    • Ali, G.1
  • 30
    • 0032061003 scopus 로고    scopus 로고
    • Developmentally regulated organ-, tissue-, and cell-specific expression of calmodulin genes in common wheat
    • Yang, T. et al. (1998) Developmentally regulated organ-, tissue-, and cell-specific expression of calmodulin genes in common wheat. Plant Mol. Biol. 37, 109-120
    • (1998) Plant Mol. Biol. , vol.37 , pp. 109-120
    • Yang, T.1
  • 31
    • 0038157340 scopus 로고    scopus 로고
    • Differential expression and functional analysis of three calmodulin isoforms in germinating pea (Pisum sativum L.) seeds
    • Duval, F. et al. (2002) Differential expression and functional analysis of three calmodulin isoforms in germinating pea (Pisum sativum L.) seeds. Plant J. 32, 481-493
    • (2002) Plant J. , vol.32 , pp. 481-493
    • Duval, F.1
  • 32
    • 0033230738 scopus 로고    scopus 로고
    • Distinct calcium signaling pathways regulate calmodulin gene expression in tobacco
    • van Der Luit, A.H. et al. (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
  • 33
    • 0037133690 scopus 로고    scopus 로고
    • Hydrogen peroxide homeostasis: Activation of plant catalase by calcium/calmodulin
    • Yang, T. and Poovaiah, B.W. (2002) Hydrogen peroxide homeostasis: activation of plant catalase by calcium/calmodulin. Proc. Natl. Acad. Sci. U. S. A. 99, 4097-4102
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 4097-4102
    • Yang, T.1    Poovaiah, B.W.2
  • 34
    • 0032697003 scopus 로고    scopus 로고
    • The presence of a heterotrimeric G protein and its role in signal transduction of extracellular calmodulin in pollen germination and tube growth
    • Ma, L. et al. (1999) The presence of a heterotrimeric G protein and its role in signal transduction of extracellular calmodulin in pollen germination and tube growth. Plant Cell 11, 1351-1364
    • (1999) Plant Cell , vol.11 , pp. 1351-1364
    • Ma, L.1
  • 35
    • 0034490131 scopus 로고    scopus 로고
    • Carboxyl-methylation of prenylated calmodulin CaM53 is required for efficient plasma membrane targeting of the protein
    • Rodriguez-Concepcion, M. et al. (2000) Carboxyl-methylation of prenylated calmodulin CaM53 is required for efficient plasma membrane targeting of the protein. Plant J. 24, 775-784
    • (2000) Plant J. , vol.24 , pp. 775-784
    • Rodriguez-Concepcion, M.1
  • 36
    • 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. et al. (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
  • 37
    • 0034663566 scopus 로고    scopus 로고
    • 2+ concentration
    • 2+ concentration. Biochem. J. 350, 299-306
    • (2000) Biochem. J. , vol.350 , pp. 299-306
    • Lee, S.H.1
  • 38
    • 0037077216 scopus 로고    scopus 로고
    • Identification of calmodulin isoform-specific binding peptides from a phage-displayed random 22-mer peptide library
    • Choi, J.Y. et al. (2002) Identification of calmodulin isoform-specific binding peptides from a phage-displayed random 22-mer peptide library. J. Biol. Chem. 277, 21630-21638
    • (2002) J. Biol. Chem. , vol.277 , pp. 21630-21638
    • Choi, J.Y.1
  • 39
    • 0033615738 scopus 로고    scopus 로고
    • Interaction of a kinesin-like protein with calmodulin isoforms from Arabidopsis
    • Reddy, V. et al. (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.1
  • 40
    • 0033582172 scopus 로고    scopus 로고
    • Involvement of specific calmodulin isoforms in salicylic acid-independent activation of plant disease resistance responses
    • Heo, W.D. et al. (1999) Involvement of specific calmodulin isoforms in salicylic acid-independent activation of plant disease resistance responses. Proc. Natl. Acad. Sci. U. S. A. 96, 766-771
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 766-771
    • Heo, W.D.1
  • 41
    • 0037155853 scopus 로고    scopus 로고
    • Genes encoding calmodulin-binding proteins in the Arabidopsis genome
    • Reddy, V.S. et al. (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
  • 42
    • 0036009056 scopus 로고    scopus 로고
    • Deletion of the C-terminal 138 amino acids of the wheat FKBP73 abrogates calmodulin binding, dimerization and male fertility in transgenic rice
    • Kurek, I. et al. (2002) Deletion of the C-terminal 138 amino acids of the wheat FKBP73 abrogates calmodulin binding, dimerization and male fertility in transgenic rice. Plant Mol. Biol. 48, 369-381
    • (2002) Plant Mol. Biol. , vol.48 , pp. 369-381
    • Kurek, I.1
  • 43
    • 0033213367 scopus 로고    scopus 로고
    • 2+ hypersensitivity in transgenic plants
    • 2+ hypersensitivity in transgenic plants. Plant J. 20, 171-182
    • (1999) Plant J. , vol.20 , pp. 171-182
    • Arazi, T.1
  • 45
    • 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
  • 46
    • 0037077285 scopus 로고    scopus 로고
    • A novel family of calmodulin-binding transcription activators in multicellular organisms
    • Bouche, N. et al. (2002) A novel family of calmodulin-binding transcription activators in multicellular organisms. J. Biol. Chem. 277, 21851-21861
    • (2002) J. Biol. Chem. , vol.277 , pp. 21851-21861
    • Bouche, N.1
  • 47
    • 0035127215 scopus 로고    scopus 로고
    • Molecular motors and their functions in plants
    • Reddy, A.S. (2001) Molecular motors and their functions in plants. Int. Rev. Cytol. 204, 97-178
    • (2001) Int. Rev. Cytol. , vol.204 , pp. 97-178
    • Reddy, A.S.1
  • 48
    • 0037187626 scopus 로고    scopus 로고
    • Calmodulin interacts with MLO protein to regulate defence against mildew in barley
    • Kim, M.C. et al. (2002) Calmodulin interacts with MLO protein to regulate defence against mildew in barley. Nature 416, 447-451
    • (2002) Nature , vol.416 , pp. 447-451
    • Kim, M.C.1
  • 49
    • 0034603001 scopus 로고    scopus 로고
    • Molecular and biochemical evidence for the involvement of calcium/calmodulin in auxin action
    • Yang, T. and Poovaiah, B.W. (2000) Molecular and biochemical evidence for the involvement of calcium/calmodulin in auxin action. J. Biol. Chem. 275, 3137-3143
    • (2000) J. Biol. Chem. , vol.275 , pp. 3137-3143
    • Yang, T.1    Poovaiah, B.W.2
  • 50
    • 0034634639 scopus 로고    scopus 로고
    • A pollen-specific novel calmodulin-binding protein with tetratricopeptide repeats
    • Safadi, F. et al. (2000) A pollen-specific novel calmodulin-binding protein with tetratricopeptide repeats. J. Biol. Chem. 275, 35457-35470
    • (2000) J. Biol. Chem. , vol.275 , pp. 35457-35470
    • Safadi, F.1
  • 51
    • 0038050772 scopus 로고    scopus 로고
    • Calmodulin-binding protein kinases in plants
    • Zhang, L. and Lu, Y. (2003) Calmodulin-binding protein kinases in plants. Trends Plant Sci. 8, 123-127
    • (2003) Trends Plant Sci. , vol.8 , pp. 123-127
    • Zhang, L.1    Lu, Y.2
  • 52
    • 0034730245 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase. Role of the neural visinin-like domain in regulating autophosphorylation and calmodulin affinity
    • 2+/ calmodulin-dependent protein kinase. Role of the neural visinin-like domain in regulating autophosphorylation and calmodulin affinity. J. Biol. Chem. 275, 30417-30422
    • (2000) J. Biol. Chem. , vol.275 , pp. 30417-30422
    • Sathyanarayanan, P.V.1
  • 53
    • 0035980012 scopus 로고    scopus 로고
    • Calcium-stimulated autophosphorylation site of plant chimeric calcium/calmodulin-dependent protein kinase
    • Sathyanarayanan, P.V. et al. (2001) Calcium-stimulated autophosphorylation site of plant chimeric calcium/calmodulin-dependent protein kinase. J. Biol. Chem. 276, 32940-32947
    • (2001) J. Biol. Chem. , vol.276 , pp. 32940-32947
    • Sathyanarayanan, P.V.1
  • 54
    • 0036111767 scopus 로고    scopus 로고
    • Autophosphorylation-dependent inactivation of plant chimeric calcium/calmodulin-dependent protein kinase
    • Sathyanarayanan, P.V. and Poovaiah, B.W. (2002) Autophosphorylation- dependent inactivation of plant chimeric calcium/calmodulin-dependent protein kinase. Eur. J. Biochem. 269, 2457-2463
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2457-2463
    • Sathyanarayanan, P.V.1    Poovaiah, B.W.2
  • 55
    • 0033180038 scopus 로고    scopus 로고
    • Developmental regulation of the gene for chimeric calcium/calmodulin- dependent protein kinase in anthers
    • Poovaiah, B. et al. (1999) Developmental regulation of the gene for chimeric calcium/calmodulin-dependent protein kinase in anthers. Planta 209, 161-171
    • (1999) Planta , vol.209 , pp. 161-171
    • Poovaiah, B.1
  • 56
    • 0034624051 scopus 로고    scopus 로고
    • An early ethylene up-regulated gene encoding a calmodulin-binding protein involved in plant senescence and death
    • Yang, T. and Poovaiah, B.W. (2000) An early ethylene up-regulated gene encoding a calmodulin-binding protein involved in plant senescence and death. J. Biol. Chem. 275, 38467-38473
    • (2000) J. Biol. Chem. , vol.275 , pp. 38467-38473
    • Yang, T.1    Poovaiah, B.W.2
  • 57
    • 0034731413 scopus 로고    scopus 로고
    • A calmodulin binding protein from Arabidopsis is induced by ethylene and contains a DNA-binding motif
    • Reddy, A.S. et al. (2000) A calmodulin binding protein from Arabidopsis is induced by ethylene and contains a DNA-binding motif. Biochem. Biophys. Res. Commun. 279, 762-769
    • (2000) Biochem. Biophys. Res. Commun. , vol.279 , pp. 762-769
    • Reddy, A.S.1
  • 58
    • 0037040290 scopus 로고    scopus 로고
    • Isolation and characterization of a novel calmodulin-binding protein from potato
    • Reddy, A.S. et al. (2002) Isolation and characterization of a novel calmodulin-binding protein from potato. J. Biol. Chem. 277, 4206-4214
    • (2002) J. Biol. Chem. , vol.277 , pp. 4206-4214
    • Reddy, A.S.1
  • 59
    • 0242585456 scopus 로고    scopus 로고
    • DRL1, a homolog of the yeast TOT4/KTI12 protein, has a function in meristem activity and organ growth in plants
    • Nelissen, H. et al. (2003) DRL1, a homolog of the yeast TOT4/KTI12 protein, has a function in meristem activity and organ growth in plants. Plant Cell 15, 639-654
    • (2003) Plant Cell , vol.15 , pp. 639-654
    • Nelissen, H.1
  • 60
    • 0035213374 scopus 로고    scopus 로고
    • Dissecting calcium oscillators in plant cells
    • Harper, J.F. (2001) Dissecting calcium oscillators in plant cells. Trends Plant Sci. 6, 395-397
    • (2001) Trends Plant Sci. , vol.6 , pp. 395-397
    • Harper, J.F.1
  • 61
    • 0034144402 scopus 로고    scopus 로고
    • Regulatory role of the N terminus of the vacuolar calcium-ATPase in cauliflower
    • Malmstrom, S. et al. (2000) Regulatory role of the N terminus of the vacuolar calcium-ATPase in cauliflower. Plant Physiol. 122, 517-526
    • (2000) Plant Physiol. , vol.122 , pp. 517-526
    • Malmstrom, S.1
  • 62
    • 0033117288 scopus 로고    scopus 로고
    • 2+-ATPase in the endoplasmic reticulum
    • 2+-ATPase in the endoplasmic reticulum. Plant Physiol. 119, 1165-1176
    • (1999) Plant Physiol. , vol.119 , pp. 1165-1176
    • Hong, B.1
  • 63
    • 0033827635 scopus 로고    scopus 로고
    • 2+-ATPase (SCA1) that is located in the plasma membrane
    • 2+-ATPase (SCA1) that is located in the plasma membrane. Plant Cell 12, 1393-1407
    • (2000) Plant Cell , vol.12 , pp. 1393-1407
    • Chung, W.S.1
  • 64
    • 85047682135 scopus 로고    scopus 로고
    • Electrophysiological analysis of cloned cyclic nucleotide-gated ion channels
    • Leng, Q. et al. (2002) Electrophysiological analysis of cloned cyclic nucleotide-gated ion channels. Plant Physiol. 128, 400-410
    • (2002) Plant Physiol. , vol.128 , pp. 400-410
    • Leng, Q.1
  • 65
    • 0033624546 scopus 로고    scopus 로고
    • 2+/calmodulin-regulated channels in plants: Targets for manipulating heavy-metal tolerance, and possible physiological roles
    • 2+/calmodulin- regulated channels in plants: targets for manipulating heavy-metal tolerance, and possible physiological roles. Biochem. Soc. Trans. 28, 471-475
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 471-475
    • Arazi, T.1
  • 66
    • 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
  • 67
    • 0034545464 scopus 로고    scopus 로고
    • 2+ tolerance
    • 2+ tolerance. Plant J. 24, 533-542
    • (2000) Plant J. , vol.24 , pp. 533-542
    • Sunkar, R.1
  • 68
    • 0034255488 scopus 로고    scopus 로고
    • The Arabidopsis dnd1 "defense, no death" gene encodes a mutated cyclic nucleotide-gated ion channel
    • Clough, S. et al. (2000) The Arabidopsis dnd1 "defense, no death" gene encodes a mutated cyclic nucleotide-gated ion channel. Proc. Natl. Acad. Sci. U. S. A. 97, 9323-9328
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 9323-9328
    • Clough, S.1
  • 69
    • 0034571237 scopus 로고    scopus 로고
    • Regulation of a recombinant pea nuclear apyrase by calmodulin and casein kinase II
    • Hsieh, H. et al. (2000) Regulation of a recombinant pea nuclear apyrase by calmodulin and casein kinase II. Biochim. Biophys. Acta 1494, 248-255
    • (2000) Biochim. Biophys. Acta , vol.1494 , pp. 248-255
    • Hsieh, H.1
  • 70
    • 0037205430 scopus 로고    scopus 로고
    • Mlo, a modulator of plant defense and cell death, is a novel calmodulin-binding protein. Isolation and characterization of a rice Mlo homologue
    • Kim, M.C. et al. (2002) Mlo, a modulator of plant defense and cell death, is a novel calmodulin-binding protein. Isolation and characterization of a rice Mlo homologue. J. Biol. Chem. 277, 19304-19314
    • (2002) J. Biol. Chem. , vol.277 , pp. 19304-19314
    • Kim, M.C.1
  • 71
    • 0037391711 scopus 로고    scopus 로고
    • Disruption of apyrases inhibits pollen germination in Arabidopsis
    • Steinebrunner, I. et al. (2003) Disruption of apyrases inhibits pollen germination in Arabidopsis. Plant Physiol. 131, 1638-1647
    • (2003) Plant Physiol. , vol.131 , pp. 1638-1647
    • Steinebrunner, I.1
  • 72
    • 0036943959 scopus 로고    scopus 로고
    • Characterization of three new members of the Arabidopsis thaliana calmodulin gene family: Conserved and highly diverged members of the gene family functionally complement a yeast calmodulin null
    • Zielinski, R.E. (2002) Characterization of three new members of the Arabidopsis thaliana calmodulin gene family: conserved and highly diverged members of the gene family functionally complement a yeast calmodulin null. Planta 214, 446-455
    • (2002) Planta , vol.214 , pp. 446-455
    • Zielinski, R.E.1
  • 73
    • 0034212418 scopus 로고    scopus 로고
    • The role of calcium and activated oxygens as signals for controlling cross-tolerance
    • Bowler, C. and Fluhr, R. (2000) The role of calcium and activated oxygens as signals for controlling cross-tolerance. Trends Plant Sci. 5, 241-246
    • (2000) Trends Plant Sci. , vol.5 , pp. 241-246
    • Bowler, C.1    Fluhr, R.2
  • 74
    • 0032004154 scopus 로고    scopus 로고
    • 2+ binding motifs
    • 2+ binding motifs. Plant Cell 10, 255-266
    • (1998) Plant Cell , vol.10 , pp. 255-266
    • Keller, T.1
  • 75
    • 0030907241 scopus 로고    scopus 로고
    • Transgenic tobacco expressing a foreign calmodulin gene shows an enhanced production of active oxygen species
    • Harding, S. et al. (1997) Transgenic tobacco expressing a foreign calmodulin gene shows an enhanced production of active oxygen species. EMBO J. 16, 1137-1144
    • (1997) EMBO J. , vol.16 , pp. 1137-1144
    • Harding, S.1
  • 76
    • 0033671250 scopus 로고    scopus 로고
    • Alternative splicing of a novel diacylglycerol kinase in tomato leads to a calmodulin-binding isoform
    • Snedden, W. and Blumwald, E. (2000) Alternative splicing of a novel diacylglycerol kinase in tomato leads to a calmodulin-binding isoform. Plant J. 24, 317-326
    • (2000) Plant J. , vol.24 , pp. 317-326
    • Snedden, W.1    Blumwald, E.2
  • 77
    • 0030140041 scopus 로고    scopus 로고
    • Early genes and auxin action
    • Abel, S. and Theologis, A. (1996) Early genes and auxin action. Plant Physiol. 111, 9-17
    • (1996) Plant Physiol. , vol.111 , pp. 9-17
    • Abel, S.1    Theologis, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.