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Volumn 380, Issue 1, 2006, Pages 1-13

Genome-wide comparative analyses of domain organisation of repertoires of protein kinases of Arabidopsis thaliana and Oryza sativa

Author keywords

Domain organisation; Genome analysis; Phosphorylation; Protein kinases

Indexed keywords

ARABIDOPSIS PROTEIN; CALCIUM PROTEIN KINASE; CASEIN KINASE I; CASEIN KINASE II; CYCLIC NUCLEOTIDE DEPENDENT PROTEIN KINASE; CYCLIN DEPENDENT KINASE; GLYCOGEN SYNTHASE KINASE; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE; PHOSPHOTRANSFERASE; PROTEIN KINASE; PROTEIN NIMA; PROTEIN SERINE THREONINE KINASE; PROTEIN TYROSINE KINASE; RAF PROTEIN; TRANSLATION REGULATORY KINASE; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

EID: 33747889617     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2006.05.016     Document Type: Review
Times cited : (38)

References (97)
  • 1
    • 0029310578 scopus 로고
    • A rice membrane calcium-dependent protein kinase is induced by gibberellin
    • Abo-el-Saad M., and Wu R. A rice membrane calcium-dependent protein kinase is induced by gibberellin. Plant Physiol. 108 (1995) 787-793
    • (1995) Plant Physiol. , vol.108 , pp. 787-793
    • Abo-el-Saad, M.1    Wu, R.2
  • 2
    • 0035282892 scopus 로고    scopus 로고
    • The NAF domain defines a novel protein-protein interaction module conserved in Ca2+-regulated kinases
    • Albrecht V., Ritz O., Linder S., Harter K., and Kudla J. The NAF domain defines a novel protein-protein interaction module conserved in Ca2+-regulated kinases. EMBO J. 20 (2001) 1051-1063
    • (2001) EMBO J. , vol.20 , pp. 1051-1063
    • Albrecht, V.1    Ritz, O.2    Linder, S.3    Harter, K.4    Kudla, J.5
  • 3
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • Altschul S.F., et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucl. Acids Res. 25 (1997) 3389-3402
    • (1997) Nucl. Acids Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1
  • 5
    • 0036774056 scopus 로고    scopus 로고
    • Structure and interactions of PAS kinase N-terminal PAS domain: model for intramolecular kinase regulation
    • Amezcua C.A., Harper S.M., Rutter J., and Gardner K.H. Structure and interactions of PAS kinase N-terminal PAS domain: model for intramolecular kinase regulation. Structure (Camb.) 10 (2002) 1349-1361
    • (2002) Structure (Camb.) , vol.10 , pp. 1349-1361
    • Amezcua, C.A.1    Harper, S.M.2    Rutter, J.3    Gardner, K.H.4
  • 6
    • 10844221661 scopus 로고    scopus 로고
    • A genomic perspective of protein kinases in Plasmodium falciparum
    • Anamika, Srinivasan N., and Krupa A. A genomic perspective of protein kinases in Plasmodium falciparum. Proteins 58 (2005) 180-189
    • (2005) Proteins , vol.58 , pp. 180-189
    • Anamika1    Srinivasan, N.2    Krupa, A.3
  • 7
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • Arabidopsis Genome Initiative. Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 408 (2000) 796-815
    • (2000) Nature , vol.408 , pp. 796-815
    • Arabidopsis Genome Initiative1
  • 8
    • 0033907240 scopus 로고    scopus 로고
    • Alternative transcript initiation and novel post-transcriptional processing of a leucine-rich repeat receptor-like protein kinase gene that responds to short-day photoperiodic floral induction in morning glory (Ipomoea nil)
    • Bassett C.L., Nickerson M.L., Cohen R.A., and Rajeevan M.S. Alternative transcript initiation and novel post-transcriptional processing of a leucine-rich repeat receptor-like protein kinase gene that responds to short-day photoperiodic floral induction in morning glory (Ipomoea nil). Plant Mol. Biol. 43 (2000) 43-58
    • (2000) Plant Mol. Biol. , vol.43 , pp. 43-58
    • Bassett, C.L.1    Nickerson, M.L.2    Cohen, R.A.3    Rajeevan, M.S.4
  • 9
    • 9144257886 scopus 로고    scopus 로고
    • The Pfam protein families database
    • Bateman A., et al. The Pfam protein families database. Nucleic Acids Res. 32 (2004) D138-D141
    • (2004) Nucleic Acids Res. , vol.32
    • Bateman, A.1
  • 10
    • 0031662772 scopus 로고    scopus 로고
    • Receptor kinases in plant development
    • Becraft P.W. Receptor kinases in plant development. Trends Plant Sci. 3 (1998) 384-388
    • (1998) Trends Plant Sci. , vol.3 , pp. 384-388
    • Becraft, P.W.1
  • 11
    • 0036439235 scopus 로고    scopus 로고
    • Receptor kinase signaling in plant development
    • Becraft P.W. Receptor kinase signaling in plant development. Annu. Rev. Cell Dev. Biol. 18 (2002) 163-192
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 163-192
    • Becraft, P.W.1
  • 12
    • 0037255072 scopus 로고    scopus 로고
    • The SWISS-PROT protein knowledge base and its supplement TrEMBL in 2003
    • Boeckmann B., et al. The SWISS-PROT protein knowledge base and its supplement TrEMBL in 2003. Nucleic Acids Res. 31 (2003) 365-370
    • (2003) Nucleic Acids Res. , vol.31 , pp. 365-370
    • Boeckmann, B.1
  • 13
    • 0141503468 scopus 로고    scopus 로고
    • Growth signalling pathways in Arabidopsis and the AGC protein kinases
    • Bogre L., Okresz L., Henriques R., and Anthony R.G. Growth signalling pathways in Arabidopsis and the AGC protein kinases. Trends Plant Sci. 8 (2003) 424-431
    • (2003) Trends Plant Sci. , vol.8 , pp. 424-431
    • Bogre, L.1    Okresz, L.2    Henriques, R.3    Anthony, R.G.4
  • 14
    • 85047671892 scopus 로고    scopus 로고
    • Plant transmembrane receptors: new pieces in the signaling puzzle
    • Braun D.M., and Walker J.C. Plant transmembrane receptors: new pieces in the signaling puzzle. Trends Biochem Sci. 21 (1996) 70-73
    • (1996) Trends Biochem Sci. , vol.21 , pp. 70-73
    • Braun, D.M.1    Walker, J.C.2
  • 15
    • 4644255309 scopus 로고    scopus 로고
    • The novel yeast PAS kinase Rim15 orchestrates G(0)-associated antioxidant defense mechanisms
    • Cameroni E., Hulo N., Roosen J., Winderickx J., and De Virgilio C. The novel yeast PAS kinase Rim15 orchestrates G(0)-associated antioxidant defense mechanisms. Cell Cycle 4 (2004) 462-468
    • (2004) Cell Cycle , vol.4 , pp. 462-468
    • Cameroni, E.1    Hulo, N.2    Roosen, J.3    Winderickx, J.4    De Virgilio, C.5
  • 16
    • 1642547018 scopus 로고    scopus 로고
    • Sensitization of defense responses and activation of programmed cell death by a pathogen-induced receptor-like protein kinase in Arabidopsis
    • Chen K., Du L., and Chen Z. Sensitization of defense responses and activation of programmed cell death by a pathogen-induced receptor-like protein kinase in Arabidopsis. Plant Mol. Biol. 53 (2003) 61-74
    • (2003) Plant Mol. Biol. , vol.53 , pp. 61-74
    • Chen, K.1    Du, L.2    Chen, Z.3
  • 17
    • 0036852939 scopus 로고    scopus 로고
    • Arabidopsis brassinosteroid-insensitive dwarf12 mutants are semidominant and defective in a glycogen synthase kinase 3beta-like kinase
    • Choe S., et al. Arabidopsis brassinosteroid-insensitive dwarf12 mutants are semidominant and defective in a glycogen synthase kinase 3beta-like kinase. Plant Physiol. 130 (2002) 1506-1515
    • (2002) Plant Physiol. , vol.130 , pp. 1506-1515
    • Choe, S.1
  • 18
    • 0035945523 scopus 로고    scopus 로고
    • Signal transduction mechanisms in plants: an overview
    • Clark G.B., Thompson Jr. G., and Roux S.J. Signal transduction mechanisms in plants: an overview. Curr Sci. 80 (2001) 170-177
    • (2001) Curr Sci. , vol.80 , pp. 170-177
    • Clark, G.B.1    Thompson Jr., G.2    Roux, S.J.3
  • 20
    • 0033136469 scopus 로고    scopus 로고
    • Characterization of an Arabidopsis thaliana receptor-like protein kinase gene activated by oxidative stress and pathogen attack
    • Czernic P., et al. Characterization of an Arabidopsis thaliana receptor-like protein kinase gene activated by oxidative stress and pathogen attack. Plant J. 18 (1999) 321-327
    • (1999) Plant J. , vol.18 , pp. 321-327
    • Czernic, P.1
  • 21
    • 1542267790 scopus 로고    scopus 로고
    • CK2 phosphorylation of CCA1 is necessary for its circadian oscillator function in Arabidopsis
    • Daniel X., Sugano S., and Tobin E.M. CK2 phosphorylation of CCA1 is necessary for its circadian oscillator function in Arabidopsis. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 3292-3297
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 3292-3297
    • Daniel, X.1    Sugano, S.2    Tobin, E.M.3
  • 22
    • 0030738539 scopus 로고    scopus 로고
    • Light-repressible receptor protein kinase: a novel photo-regulated gene from Arabidopsis thaliana
    • Deeken R., and Kaldenhoff R. Light-repressible receptor protein kinase: a novel photo-regulated gene from Arabidopsis thaliana. Planta 202 (1997) 479-486
    • (1997) Planta , vol.202 , pp. 479-486
    • Deeken, R.1    Kaldenhoff, R.2
  • 23
    • 0036143156 scopus 로고    scopus 로고
    • Systematic identification of novel protein domain families associated with nuclear functions
    • Doerks T., Copley R.R., Schultz J., Ponting C.P., and Bork P. Systematic identification of novel protein domain families associated with nuclear functions. Genome Res. 12 (2002) 47-56
    • (2002) Genome Res. , vol.12 , pp. 47-56
    • Doerks, T.1    Copley, R.R.2    Schultz, J.3    Ponting, C.P.4    Bork, P.5
  • 24
    • 0034029658 scopus 로고    scopus 로고
    • Arabidopsis thaliana SHAGGY-related protein kinases (AtSK11 and 12) function in perianth and gynoecium development
    • Dornelas M.C., Van Lammeren A.A., and Kreis M. Arabidopsis thaliana SHAGGY-related protein kinases (AtSK11 and 12) function in perianth and gynoecium development. Plant J. 21 (2000) 419-429
    • (2000) Plant J. , vol.21 , pp. 419-429
    • Dornelas, M.C.1    Van Lammeren, A.A.2    Kreis, M.3
  • 25
    • 0034486764 scopus 로고    scopus 로고
    • Identification of genes encoding receptor-like protein kinases as possible targets of pathogen- and salicylic acid-induced WRKY DNA-binding proteins in Arabidopsis
    • Du L., and Chen Z. Identification of genes encoding receptor-like protein kinases as possible targets of pathogen- and salicylic acid-induced WRKY DNA-binding proteins in Arabidopsis. Plant J. 24 (2000) 837-847
    • (2000) Plant J. , vol.24 , pp. 837-847
    • Du, L.1    Chen, Z.2
  • 26
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • Eddy S.R. Profile hidden Markov models. Bioinformatics 14 (1998) 755-763
    • (1998) Bioinformatics , vol.14 , pp. 755-763
    • Eddy, S.R.1
  • 28
    • 0033394112 scopus 로고    scopus 로고
    • Cyclic AMP-dependent protein phosphorylation in guard cell protoplasts of Vicia faba L
    • Friedrich P., Curvetto N., and Giusto N. Cyclic AMP-dependent protein phosphorylation in guard cell protoplasts of Vicia faba L. Biocell 23 (1999) 203-209
    • (1999) Biocell , vol.23 , pp. 203-209
    • Friedrich, P.1    Curvetto, N.2    Giusto, N.3
  • 29
    • 0042330161 scopus 로고    scopus 로고
    • Nucleotide binding site/leucine-rich repeats, Pto-like and receptor-like kinases related to disease resistance in grapevine
    • Gaspero D.G., and Cipriani G. Nucleotide binding site/leucine-rich repeats, Pto-like and receptor-like kinases related to disease resistance in grapevine. Mol. Genet. Genomics 269 (2003) 612-623
    • (2003) Mol. Genet. Genomics , vol.269 , pp. 612-623
    • Gaspero, D.G.1    Cipriani, G.2
  • 30
    • 0037023349 scopus 로고    scopus 로고
    • A draft sequence of the rice genome (Oryza sativa L. ssp. japonica)
    • Goff S.A., et al. A draft sequence of the rice genome (Oryza sativa L. ssp. japonica). Science 296 (2002) 92-100
    • (2002) Science , vol.296 , pp. 92-100
    • Goff, S.A.1
  • 31
    • 0027225936 scopus 로고
    • Serum-induced translocation of mitogen-activated protein kinase to the cell surface ruffling membrane and the nucleus
    • Gonzalez F.A., Seth A., Raden D.L., Bowman D.S., Fay F.S., and Davis R.J. Serum-induced translocation of mitogen-activated protein kinase to the cell surface ruffling membrane and the nucleus. J. Cell Biol. 122 (1993) 1089-1101
    • (1993) J. Cell Biol. , vol.122 , pp. 1089-1101
    • Gonzalez, F.A.1    Seth, A.2    Raden, D.L.3    Bowman, D.S.4    Fay, F.S.5    Davis, R.J.6
  • 32
    • 0035173417 scopus 로고    scopus 로고
    • PlantsP: a functional genomics database for plant phosphorylation
    • Gribskov M., et al. PlantsP: a functional genomics database for plant phosphorylation. Nucleic Acids Res. 29 (2001) 111-113
    • (2001) Nucleic Acids Res. , vol.29 , pp. 111-113
    • Gribskov, M.1
  • 33
    • 0023885305 scopus 로고
    • The protein kinase family: conserved features and deduced phylogeny of the catalytic domains
    • Hanks S.K., Quinn A.M., and Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 241 (1988) 42-52
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 34
    • 0033499326 scopus 로고    scopus 로고
    • Plant protein serine/threonine kinases: classification and functions
    • Hardie D.G. Plant protein serine/threonine kinases: classification and functions. Annu. Rev. Plant Physiol. Plant Mol. Biol. 50 (1999) 97-131
    • (1999) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.50 , pp. 97-131
    • Hardie, D.G.1
  • 37
    • 0033120343 scopus 로고    scopus 로고
    • A cluster of five cell wall-associated receptor kinase genes, Wak1-5, are expressed in specific organs of Arabidopsis
    • He Z.H., Cheeseman I., He D., and Kohorn B.D. A cluster of five cell wall-associated receptor kinase genes, Wak1-5, are expressed in specific organs of Arabidopsis. Plant Mol. Biol. 39 (1999) 1189-1196
    • (1999) Plant Mol. Biol. , vol.39 , pp. 1189-1196
    • He, Z.H.1    Cheeseman, I.2    He, D.3    Kohorn, B.D.4
  • 38
    • 0033102999 scopus 로고    scopus 로고
    • Characterization of the Arabidopsis lecRK-a genes: members of a superfamily encoding putative receptors with an extracellular domain homologous to legume lectins
    • Herve C., et al. Characterization of the Arabidopsis lecRK-a genes: members of a superfamily encoding putative receptors with an extracellular domain homologous to legume lectins. Plant Mol. Biol. 39 (1999) 671-682
    • (1999) Plant Mol. Biol. , vol.39 , pp. 671-682
    • Herve, C.1
  • 40
    • 0031026008 scopus 로고    scopus 로고
    • The protein kinases of budding yeast: six score and more
    • Hunter T., and Plowman G.D. The protein kinases of budding yeast: six score and more. Trends Biochem. Sci. 22 (1997) 18-22
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 18-22
    • Hunter, T.1    Plowman, G.D.2
  • 41
    • 0034705147 scopus 로고    scopus 로고
    • A calcium-dependent protein kinase can inhibit a calmodulin-stimulated Ca2+ pump (ACA2) located in the endoplasmic reticulum of Arabidopsis
    • Hwang I., Sze H., and Harper J.F. A calcium-dependent protein kinase can inhibit a calmodulin-stimulated Ca2+ pump (ACA2) located in the endoplasmic reticulum of Arabidopsis. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 6224-6229
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6224-6229
    • Hwang, I.1    Sze, H.2    Harper, J.F.3
  • 42
    • 0038714319 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase cascades in plants: a new nomenclature
    • Ichimura K., et al. Mitogen-activated protein kinase cascades in plants: a new nomenclature. Trends Plant Sci. 7 (2002) 301-308
    • (2002) Trends Plant Sci. , vol.7 , pp. 301-308
    • Ichimura, K.1
  • 43
    • 50149107431 scopus 로고    scopus 로고
    • The maize CR4 receptor-like kinase mediates a growth factor-like differentiation response
    • Jin P., Guo T., and Becraft P.W. The maize CR4 receptor-like kinase mediates a growth factor-like differentiation response. Genesis 27 (2000) 104-116
    • (2000) Genesis , vol.27 , pp. 104-116
    • Jin, P.1    Guo, T.2    Becraft, P.W.3
  • 44
    • 0036777092 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3/SHAGGY-like kinases in plants: an emerging family with novel functions
    • Jonak C., and Hirt H. Glycogen synthase kinase 3/SHAGGY-like kinases in plants: an emerging family with novel functions. Trends Plant Sci. 7 (2002) 457-461
    • (2002) Trends Plant Sci. , vol.7 , pp. 457-461
    • Jonak, C.1    Hirt, H.2
  • 45
    • 0033776984 scopus 로고    scopus 로고
    • CDK-related protein kinases in plants
    • Joubes J., et al. CDK-related protein kinases in plants. Plant Mol. Biol. 43 (2000) 607-620
    • (2000) Plant Mol. Biol. , vol.43 , pp. 607-620
    • Joubes, J.1
  • 46
    • 0036273591 scopus 로고    scopus 로고
    • Self-incompatibility in the Brassicaceae: receptor-ligand signaling and cell-to-cell communication
    • Kachroo A., Nasrallah M.E., and Nasrallah J.B. Self-incompatibility in the Brassicaceae: receptor-ligand signaling and cell-to-cell communication. Plant Cell 14 (2002) S227-S238
    • (2002) Plant Cell , vol.14
    • Kachroo, A.1    Nasrallah, M.E.2    Nasrallah, J.B.3
  • 47
    • 0035983678 scopus 로고    scopus 로고
    • The complement of protein phosphatase catalytic subunits encoded in the genome of Arabidopsis
    • Kerk D., Bulgrien J., Smith D.W., Barsam B., Veretnik S., and Gribskov M. The complement of protein phosphatase catalytic subunits encoded in the genome of Arabidopsis. Plant Physiol. 129 (2002) 908-925
    • (2002) Plant Physiol. , vol.129 , pp. 908-925
    • Kerk, D.1    Bulgrien, J.2    Smith, D.W.3    Barsam, B.4    Veretnik, S.5    Gribskov, M.6
  • 48
    • 0037353618 scopus 로고    scopus 로고
    • Arabidopsis proteins containing similarity to the universal stress protein domain of bacteria
    • Kerk D., Bulgrien J., Smith D.W., and Gribskov M. Arabidopsis proteins containing similarity to the universal stress protein domain of bacteria. Plant Physiol. 131 (2003) 1209-1219
    • (2003) Plant Physiol. , vol.131 , pp. 1209-1219
    • Kerk, D.1    Bulgrien, J.2    Smith, D.W.3    Gribskov, M.4
  • 49
    • 0030972075 scopus 로고    scopus 로고
    • Insulin regulation of mitogen-activated protein kinase kinase (MEK), mitogen-activated protein kinase and casein kinase in the cell nucleus: a possible role in the regulation of gene expression
    • Kim S.J., and Kahn C.R. Insulin regulation of mitogen-activated protein kinase kinase (MEK), mitogen-activated protein kinase and casein kinase in the cell nucleus: a possible role in the regulation of gene expression. Biochem. J. 323 (1997) 621-627
    • (1997) Biochem. J. , vol.323 , pp. 621-627
    • Kim, S.J.1    Kahn, C.R.2
  • 50
    • 0038376835 scopus 로고    scopus 로고
    • Arabidopsis D-type cyclin CYCD4;1 is a novel cyclin partner of B2-type cyclin-dependent kinase
    • Kono A., Umeda-Hara C., Lee J., Ito M., Uchimiya H., and Umeda M. Arabidopsis D-type cyclin CYCD4;1 is a novel cyclin partner of B2-type cyclin-dependent kinase. Plant Physiol. 132 (2003) 1315-1321
    • (2003) Plant Physiol. , vol.132 , pp. 1315-1321
    • Kono, A.1    Umeda-Hara, C.2    Lee, J.3    Ito, M.4    Uchimiya, H.5    Umeda, M.6
  • 51
    • 0037158810 scopus 로고    scopus 로고
    • Human members of the eukaryotic protein kinase family
    • (RESEARCH0043. Electronic publication 2002 Aug 22)
    • Kostich M., et al. Human members of the eukaryotic protein kinase family. Genome Biol. 3 (2002) (RESEARCH0043. Electronic publication 2002 Aug 22)
    • (2002) Genome Biol. , vol.3
    • Kostich, M.1
  • 52
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • Krogh A., Larsson B., von Heijne G., and Sonnhammer E.L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305 (2001) 567-580
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 53
    • 0038549051 scopus 로고    scopus 로고
    • The repertoire of protein kinases encoded in the draft version of the human genome: atypical variations and uncommon domain combinations
    • (RESEARCH0066.1-14)
    • Krupa A., and Srinivasan N. The repertoire of protein kinases encoded in the draft version of the human genome: atypical variations and uncommon domain combinations. Genome Biol. 3 (2002) (RESEARCH0066.1-14)
    • (2002) Genome Biol. , vol.3
    • Krupa, A.1    Srinivasan, N.2
  • 54
    • 25444460385 scopus 로고    scopus 로고
    • Diversity in domain architectures of Ser/Thr kinases and their homologues in prokaryotes
    • Krupa A., and Srinivasan N. Diversity in domain architectures of Ser/Thr kinases and their homologues in prokaryotes. BMC Genomics 6 (2005) 129
    • (2005) BMC Genomics , vol.6 , pp. 129
    • Krupa, A.1    Srinivasan, N.2
  • 55
    • 3042584697 scopus 로고    scopus 로고
    • Structural modes of stabilization of permissive phosphorylation sites in protein kinases: distinct strategies in Ser/Thr and Tyr kinases
    • Krupa A., Preethi G., and Srinivasan N. Structural modes of stabilization of permissive phosphorylation sites in protein kinases: distinct strategies in Ser/Thr and Tyr kinases. J. Mol. Biol. 339 (2004) 1025-1039
    • (2004) J. Mol. Biol. , vol.339 , pp. 1025-1039
    • Krupa, A.1    Preethi, G.2    Srinivasan, N.3
  • 57
    • 0035669594 scopus 로고    scopus 로고
    • The role of protein kinases in the regulation of plant growth and development
    • Laurie S., and Halford N.G. The role of protein kinases in the regulation of plant growth and development. Plant Growth Regul. 34 (2001) 253-265
    • (2001) Plant Growth Regul. , vol.34 , pp. 253-265
    • Laurie, S.1    Halford, N.G.2
  • 58
    • 0038531125 scopus 로고    scopus 로고
    • Cell cycle function of a rice B2-type cyclin interacting with a B-type cyclin-dependent kinase
    • Lee J., et al. Cell cycle function of a rice B2-type cyclin interacting with a B-type cyclin-dependent kinase. Plant J. 34 (2003) 417-425
    • (2003) Plant J. , vol.34 , pp. 417-425
    • Lee, J.1
  • 59
    • 0142134236 scopus 로고    scopus 로고
    • Roles of OsCKI1, a rice casein kinase I, in root development and plant hormone sensitivity
    • Liu W., Xu Z.H., Luo D., and Xue H.W. Roles of OsCKI1, a rice casein kinase I, in root development and plant hormone sensitivity. Plant J. 36 (2003) 189-202
    • (2003) Plant J. , vol.36 , pp. 189-202
    • Liu, W.1    Xu, Z.H.2    Luo, D.3    Xue, H.W.4
  • 60
    • 0036006051 scopus 로고    scopus 로고
    • An Arabidopsis calcium-dependent protein kinase is associated with the endoplasmic reticulum
    • Lu S.X., and Hrabak E.M. An Arabidopsis calcium-dependent protein kinase is associated with the endoplasmic reticulum. Plant Physiol. 128 (2002) 1008-1021
    • (2002) Plant Physiol. , vol.128 , pp. 1008-1021
    • Lu, S.X.1    Hrabak, E.M.2
  • 61
    • 0142104972 scopus 로고    scopus 로고
    • A receptor kinase gene of the LysM type is involved in legume perception of rhizobial signals
    • Madsen E.B., et al. A receptor kinase gene of the LysM type is involved in legume perception of rhizobial signals. Nature 425 (2003) 637-640
    • (2003) Nature , vol.425 , pp. 637-640
    • Madsen, E.B.1
  • 63
    • 0037252683 scopus 로고    scopus 로고
    • CDD: a curated Entrez database of conserved domain alignments
    • Marchler-Bauer A., et al. CDD: a curated Entrez database of conserved domain alignments. Nucleic Acids Res. 31 (2003) 383-387
    • (2003) Nucleic Acids Res. , vol.31 , pp. 383-387
    • Marchler-Bauer, A.1
  • 64
    • 0035106056 scopus 로고    scopus 로고
    • A rice membrane-bound calcium-dependent protein kinase is activated in response to low temperature
    • Martin M.L., and Busconi L. A rice membrane-bound calcium-dependent protein kinase is activated in response to low temperature. Plant Physiol. 125 (2001) 1442-1449
    • (2001) Plant Physiol. , vol.125 , pp. 1442-1449
    • Martin, M.L.1    Busconi, L.2
  • 65
    • 0030922083 scopus 로고    scopus 로고
    • A novel mechanism of JNK1 activation. Nuclear translocation and activation of JNK1 during ischemia and reperfusion
    • Mizukami Y., Yoshioka K., Morimoto S., and Yoshida K. A novel mechanism of JNK1 activation. Nuclear translocation and activation of JNK1 during ischemia and reperfusion. J. Biol. Chem. 272 (1997) 16657-16662
    • (1997) J. Biol. Chem. , vol.272 , pp. 16657-16662
    • Mizukami, Y.1    Yoshioka, K.2    Morimoto, S.3    Yoshida, K.4
  • 66
    • 0037230334 scopus 로고    scopus 로고
    • Pathogen derived elicitors: searching for receptors in plants
    • Montesano M., Brader G., and Palva E.T. Pathogen derived elicitors: searching for receptors in plants. Mol. Plant Pathol. 4 (2003) 73-79
    • (2003) Mol. Plant Pathol. , vol.4 , pp. 73-79
    • Montesano, M.1    Brader, G.2    Palva, E.T.3
  • 67
    • 0042572077 scopus 로고    scopus 로고
    • Receptor-like protein kinases: the keys to response
    • Morris E.R., and Walker J.C. Receptor-like protein kinases: the keys to response. Curr. Opin. Plant Biol. 6 (2003) 339-342
    • (2003) Curr. Opin. Plant Biol. , vol.6 , pp. 339-342
    • Morris, E.R.1    Walker, J.C.2
  • 68
    • 0034710302 scopus 로고    scopus 로고
    • Protein kinases and phosphatases in Drosophila genome
    • Morrsison D.K., Murakami M.S., and Cleghon V. Protein kinases and phosphatases in Drosophila genome. J. Cell Biol. 150 (2000) F57-F62
    • (2000) J. Cell Biol. , vol.150
    • Morrsison, D.K.1    Murakami, M.S.2    Cleghon, V.3
  • 69
    • 1542377395 scopus 로고    scopus 로고
    • A membrane-anchored protein kinase involved in Brassica self-incompatibility signaling
    • Murase K., et al. A membrane-anchored protein kinase involved in Brassica self-incompatibility signaling. Science 303 (2004) 1516-1519
    • (2004) Science , vol.303 , pp. 1516-1519
    • Murase, K.1
  • 70
    • 0032029231 scopus 로고    scopus 로고
    • Pollen tube localization implies a role in pollen-pistil interactions for the tomato receptor-like protein kinases LePRK1 and LePRK2
    • Muschietti J., Eyal Y., and McCormick S. Pollen tube localization implies a role in pollen-pistil interactions for the tomato receptor-like protein kinases LePRK1 and LePRK2. Plant Cell 10 (1998) 319-330
    • (1998) Plant Cell , vol.10 , pp. 319-330
    • Muschietti, J.1    Eyal, Y.2    McCormick, S.3
  • 71
    • 0025140432 scopus 로고
    • Regulation of phosphoenolpyruvate carboxylase: an example of signal transduction via protein phosphorylation in higher plants
    • Nimmo H.G., Carter P.J., Fewson C.A., McNaughton G.A., Nimmo G.A., and Wilkins M.B. Regulation of phosphoenolpyruvate carboxylase: an example of signal transduction via protein phosphorylation in higher plants. Adv. Enzyme Regul. 30 (1990) 121-131
    • (1990) Adv. Enzyme Regul. , vol.30 , pp. 121-131
    • Nimmo, H.G.1    Carter, P.J.2    Fewson, C.A.3    McNaughton, G.A.4    Nimmo, G.A.5    Wilkins, M.B.6
  • 72
    • 0036408233 scopus 로고    scopus 로고
    • Requirements for activation of the signal-transduction network that leads to regulatory phosphorylation of leaf guard-cell phosphoenolpyruvate carboxylase during fusicoccin-stimulated stomatal opening
    • Outlaw Jr. W.H., Du Z., Xia Meng F., Aghoram K., Riddle K.A., and Chollet R. Requirements for activation of the signal-transduction network that leads to regulatory phosphorylation of leaf guard-cell phosphoenolpyruvate carboxylase during fusicoccin-stimulated stomatal opening. Arch. Biochem. Biophys. 407 (2002) 63-71
    • (2002) Arch. Biochem. Biophys. , vol.407 , pp. 63-71
    • Outlaw Jr., W.H.1    Du, Z.2    Xia Meng, F.3    Aghoram, K.4    Riddle, K.A.5    Chollet, R.6
  • 73
    • 0033598830 scopus 로고    scopus 로고
    • The protein kinase of Caenorhabditis elegans: a model for signal transduction in multicellular organisms
    • Plowman G.D., Sudarsanam S., Bingham J., Whyte D., and Hunter T. The protein kinase of Caenorhabditis elegans: a model for signal transduction in multicellular organisms. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 13603-13610
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13603-13610
    • Plowman, G.D.1    Sudarsanam, S.2    Bingham, J.3    Whyte, D.4    Hunter, T.5
  • 74
    • 0142041483 scopus 로고    scopus 로고
    • Plant recognition of symbiotic bacteria requires two LysM receptor-like kinases
    • Radutoiu S., et al. Plant recognition of symbiotic bacteria requires two LysM receptor-like kinases. Nature 425 (2003) 585-592
    • (2003) Nature , vol.425 , pp. 585-592
    • Radutoiu, S.1
  • 75
    • 0036267255 scopus 로고    scopus 로고
    • Expression of an Arabidopsis lectin kinase gene, lecRKa1 is induced during senescence, wound-healing and in response to oligogalacturonic acids
    • Riou C., Herve C., Dabos P., Pacquit V., and Lescure B. Expression of an Arabidopsis lectin kinase gene, lecRKa1 is induced during senescence, wound-healing and in response to oligogalacturonic acids. Plant Physiol. Biochem. 40 (2002) 431-438
    • (2002) Plant Physiol. Biochem. , vol.40 , pp. 431-438
    • Riou, C.1    Herve, C.2    Dabos, P.3    Pacquit, V.4    Lescure, B.5
  • 76
    • 0032146404 scopus 로고    scopus 로고
    • Unusual membrane-associated protein kinases in higher plants
    • Satterlee J.S., and Sussman M.R. Unusual membrane-associated protein kinases in higher plants. J. Membr. Biol. 164 (1998) 205-213
    • (1998) J. Membr. Biol. , vol.164 , pp. 205-213
    • Satterlee, J.S.1    Sussman, M.R.2
  • 77
    • 0033998566 scopus 로고    scopus 로고
    • The ethylene-inducible PK12 kinase mediates the phosphorylation of SR splicing factors
    • Savaldi-Goldstein S., Sessa G., and Fluhr R. The ethylene-inducible PK12 kinase mediates the phosphorylation of SR splicing factors. Plant J. 21 (2000) 91-96
    • (2000) Plant J. , vol.21 , pp. 91-96
    • Savaldi-Goldstein, S.1    Sessa, G.2    Fluhr, R.3
  • 78
    • 0036718810 scopus 로고    scopus 로고
    • The CRK1 receptor-like kinase gene of tobacco is negatively regulated by cytokinin
    • Schafer S., and Schmulling T. The CRK1 receptor-like kinase gene of tobacco is negatively regulated by cytokinin. Plant Mol. Biol. 50 (2002) 155-166
    • (2002) Plant Mol. Biol. , vol.50 , pp. 155-166
    • Schafer, S.1    Schmulling, T.2
  • 79
    • 0028951187 scopus 로고
    • The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase
    • Schuller D.J., Grant G.A., and Banaszak L.J. The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase. Nat. Struct. Biol. 2 (1995) 69-76
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 69-76
    • Schuller, D.J.1    Grant, G.A.2    Banaszak, L.J.3
  • 80
    • 0035845575 scopus 로고    scopus 로고
    • Receptor-like kinases from Arabidopsis form a monophyletic gene family related to animal receptor kinases
    • Shiu S.H., and Bleecker A.B. Receptor-like kinases from Arabidopsis form a monophyletic gene family related to animal receptor kinases. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 10763-10768
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 10763-10768
    • Shiu, S.H.1    Bleecker, A.B.2
  • 81
    • 0038460040 scopus 로고    scopus 로고
    • Expansion of the receptor-like kinase/Pelle gene family and receptor-like proteins in Arabidopsis
    • Shiu S.H., and Bleecker A.B. Expansion of the receptor-like kinase/Pelle gene family and receptor-like proteins in Arabidopsis. Plant Physiol. 132 (2003) 530-543
    • (2003) Plant Physiol. , vol.132 , pp. 530-543
    • Shiu, S.H.1    Bleecker, A.B.2
  • 82
    • 2442591728 scopus 로고    scopus 로고
    • Comparative analysis of the receptor-like kinase family in Arabidopsis and rice
    • Shiu S.H., Karlowski W.M., Pan R., Tzeng Y.H., Mayer K.F., and Li W.H. Comparative analysis of the receptor-like kinase family in Arabidopsis and rice. Plant Cell 16 (2004) 1220-1234
    • (2004) Plant Cell , vol.16 , pp. 1220-1234
    • Shiu, S.H.1    Karlowski, W.M.2    Pan, R.3    Tzeng, Y.H.4    Mayer, K.F.5    Li, W.H.6
  • 83
    • 0032478537 scopus 로고    scopus 로고
    • Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran
    • Stewart M., Kent H.M., and McCoy A.J. Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran. J. Mol. Biol. 277 (1998) 635-646
    • (1998) J. Mol. Biol. , vol.277 , pp. 635-646
    • Stewart, M.1    Kent, H.M.2    McCoy, A.J.3
  • 84
    • 0029310678 scopus 로고
    • Plant protein kinase families and signal transduction
    • Stone J.M., and Walker J.C. Plant protein kinase families and signal transduction. Plant Physiol. 108 (1995) 451-457
    • (1995) Plant Physiol. , vol.108 , pp. 451-457
    • Stone, J.M.1    Walker, J.C.2
  • 85
    • 25144466936 scopus 로고    scopus 로고
    • Positively selected sites in the Arabidopsis receptor-like kinase gene family
    • Strain E., and Muse S.V. Positively selected sites in the Arabidopsis receptor-like kinase gene family. J. Mol. Evol. 61 (2005) 325-332
    • (2005) J. Mol. Evol. , vol.61 , pp. 325-332
    • Strain, E.1    Muse, S.V.2
  • 86
    • 0034874729 scopus 로고    scopus 로고
    • Plant mitogen-activated protein kinase signaling cascades
    • Tena G., Asai T., Chiu W.L., and Sheen J. Plant mitogen-activated protein kinase signaling cascades. Curr. Opin. Plant Biol. 4 (2001) 392-400
    • (2001) Curr. Opin. Plant Biol. , vol.4 , pp. 392-400
    • Tena, G.1    Asai, T.2    Chiu, W.L.3    Sheen, J.4
  • 87
    • 0033498862 scopus 로고    scopus 로고
    • Plant cold acclimation: freezing tolerance genes and regulatory mechanisms
    • Thomashow M.F. Plant cold acclimation: freezing tolerance genes and regulatory mechanisms. Annu. Rev. Plant Physiol. Plant Mol. Biol. 50 (1999) 571-599
    • (1999) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.50 , pp. 571-599
    • Thomashow, M.F.1
  • 88
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 89
    • 0033827884 scopus 로고    scopus 로고
    • Receptor kinase activation and signal transduction in plants: an emerging picture
    • Torii K.U. Receptor kinase activation and signal transduction in plants: an emerging picture. Curr. Opin. Plant Biol. 3 (2000) 361-367
    • (2000) Curr. Opin. Plant Biol. , vol.3 , pp. 361-367
    • Torii, K.U.1
  • 90
    • 0032873026 scopus 로고    scopus 로고
    • Differential expression of genes for cyclin-dependent protein kinases in rice plants
    • Umeda M., Umeda-Hara C., Yamaguchi M., Hashimoto J., and Uchimiya H. Differential expression of genes for cyclin-dependent protein kinases in rice plants. Plant Physiol. 119 (1999) 31-40
    • (1999) Plant Physiol. , vol.119 , pp. 31-40
    • Umeda, M.1    Umeda-Hara, C.2    Yamaguchi, M.3    Hashimoto, J.4    Uchimiya, H.5
  • 92
    • 0035983616 scopus 로고    scopus 로고
    • The cell wall-associated kinase (WAK) and WAK-like kinase gene family
    • Verica J.A., and He Z.H. The cell wall-associated kinase (WAK) and WAK-like kinase gene family. Plant Physiol. 129 (2002) 455-459
    • (2002) Plant Physiol. , vol.129 , pp. 455-459
    • Verica, J.A.1    He, Z.H.2
  • 93
    • 0042510537 scopus 로고    scopus 로고
    • Systematic trans-genomic comparison of protein kinases between Arabidopsis and Saccharomyces cerevisiae
    • Wang D., Harper J.F., and Gribskov M. Systematic trans-genomic comparison of protein kinases between Arabidopsis and Saccharomyces cerevisiae. Plant Physiol. 132 (2003) 2152-2165
    • (2003) Plant Physiol. , vol.132 , pp. 2152-2165
    • Wang, D.1    Harper, J.F.2    Gribskov, M.3
  • 94
    • 0032076826 scopus 로고    scopus 로고
    • Xa21D encodes a receptor-like molecule with a leucine-rich repeat domain that determines race-specific recognition and is subject to adaptive evolution
    • Wang G.L., et al. Xa21D encodes a receptor-like molecule with a leucine-rich repeat domain that determines race-specific recognition and is subject to adaptive evolution. Plant Cell 10 (1998) 765-779
    • (1998) Plant Cell , vol.10 , pp. 765-779
    • Wang, G.L.1
  • 95
    • 9144258616 scopus 로고    scopus 로고
    • Protein kinases of the human malaria parasite Plasmodium falciparum: the kinome of a divergent eukaryote
    • Ward P., Equinet L., Packer J., and Doerig C. Protein kinases of the human malaria parasite Plasmodium falciparum: the kinome of a divergent eukaryote. BMC Genomics 5 (2004) 79
    • (2004) BMC Genomics , vol.5 , pp. 79
    • Ward, P.1    Equinet, L.2    Packer, J.3    Doerig, C.4
  • 96
    • 0032830481 scopus 로고    scopus 로고
    • Evolution of aminoacyl-tRNA synthetases-analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events
    • Wolf Y.I., Aravind L., Grishin N.V., and Koonin E.V. Evolution of aminoacyl-tRNA synthetases-analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. Genome Res. 9 (1999) 689-710
    • (1999) Genome Res. , vol.9 , pp. 689-710
    • Wolf, Y.I.1    Aravind, L.2    Grishin, N.V.3    Koonin, E.V.4
  • 97
    • 0034763215 scopus 로고    scopus 로고
    • MAP kinase pathways: how many and what for?
    • Wrzaczek M., and Hirt H. MAP kinase pathways: how many and what for?. Biol. Cell 93 (2001) 81-87
    • (2001) Biol. Cell , vol.93 , pp. 81-87
    • Wrzaczek, M.1    Hirt, H.2


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