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Volumn 779, Issue , 2011, Pages 7-52

The age of protein kinases

Author keywords

Cascade; Development; Kinase; Phosphatase; Phosphorylation; Plant; Signalling

Indexed keywords

PROTEIN KINASE;

EID: 80054722817     PISSN: 10643745     EISSN: 19406029     Source Type: Book Series    
DOI: 10.1007/978-1-61779-264-9_2     Document Type: Chapter
Times cited : (40)

References (178)
  • 2
    • 84944000866 scopus 로고
    • Nomenclature of phosphorus-containing compounds of biochemical importance. (Recommendations 1976) IUPAC-IUB Commission on Biochemical Nomenclature
    • IUPAC-IUB Commission on Biochemical Nomenclature (CBN), T
    • IUPAC-IUB Commission on Biochemical Nomenclature (CBN), T. (1977) Nomenclature of phosphorus-containing compounds of biochemical importance. (Recommendations 1976) IUPAC-IUB Commission on Biochemical Nomenclature. Hoppe Seylers Z Physiol Chem 358, 599–616.
    • (1977) Hoppe Seylers Z Physiol Chem , vol.358 , pp. 599-616
  • 4
    • 16344382561 scopus 로고    scopus 로고
    • Functional genomics of protein kinases in plants
    • Chevalier, D., and Walker, J. C. (2005) Functional genomics of protein kinases in plants. Brief Funct Genomic Proteomic 3, 362–71.
    • (2005) Brief Funct Genomic Proteomic , vol.3 , pp. 362-371
    • Chevalier, D.1    Walker, J. C.2
  • 5
    • 0027277098 scopus 로고
    • On target with a new mechanism for the regulation of protein phosphorylation
    • Hubbard, M. J., and Cohen, P. (1993) On target with a new mechanism for the regulation of protein phosphorylation. Trends Biochem Sci 18, 172–7.
    • (1993) Trends Biochem Sci , vol.18 , pp. 172-177
    • Hubbard, M. J.1    Cohen, P.2
  • 6
    • 0035316766 scopus 로고    scopus 로고
    • Toward the phosphoproteome
    • Ahn, N. G., and Resing, K. A. (2001) Toward the phosphoproteome. Nat Biotechnol 19, 317–8.
    • (2001) Nat Biotechnol , vol.19 , pp. 317-318
    • Ahn, N. G.1    Resing, K. A.2
  • 7
    • 0025935237 scopus 로고
    • Chemical properties and separation of phosphoamino acids by thin-layer chromatography and/or electrophoresis
    • Duclos, B., Marcandier, S., and Cozzone, A. J. (1991) Chemical properties and separation of phosphoamino acids by thin-layer chromatography and/or electrophoresis. Methods Enzymol 201, 10–21.
    • (1991) Methods Enzymol , vol.201 , pp. 10-21
    • Duclos, B.1    Marcandier, S.2    Cozzone, A. J.3
  • 8
    • 0029935805 scopus 로고    scopus 로고
    • Tyrosine phosphorylation: past, present and future
    • Hunter, T. (1996) Tyrosine phosphorylation: past, present and future. Biochem Soc Trans 24, 307–27.
    • (1996) Biochem Soc Trans , vol.24 , pp. 307-327
    • Hunter, T.1
  • 9
    • 33846908953 scopus 로고    scopus 로고
    • Quantitative proteomic approaches for studying phosphotyrosine signaling
    • Ding, S.J., Qian, W. J., and Smith, R. D. (2007) Quantitative proteomic approaches for studying phosphotyrosine signaling. Expert Rev Proteomics 4, 13–23.
    • (2007) Expert Rev Proteomics , vol.4 , pp. 13-23
    • Ding, S.J.1    Qian, W. J.2    Smith, R. D.3
  • 10
    • 34250316558 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of phosphotyrosine-mediated cellular signaling networks
    • Zhang, Y., Wolf-Yadlin, A., and White, F.M. (2007) Quantitative proteomic analysis of phosphotyrosine-mediated cellular signaling networks. Methods Mol Biol 359, 203–12.
    • (2007) Methods Mol Biol , vol.359 , pp. 203-212
    • Zhang, Y.1    Wolf-Yadlin, A.2    White, F.M.3
  • 11
    • 33745813187 scopus 로고    scopus 로고
    • Reading protein modifications with interaction domains
    • Seet, B.T., Dikic, I., Zhou, M. M., and Pawson, T. (2006) Reading protein modifications with interaction domains. Nat Rev Mol Cell Biol 7, 473–83.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 473-483
    • Seet, B.T.1    Dikic, I.2    Zhou, M. M.3    Pawson, T.4
  • 15
    • 34347403192 scopus 로고    scopus 로고
    • Phosphopeptide enrichment by ali-phatic hydroxy acid-modified metal oxide chromatography for nano-LC-MS/MS in proteomics applications
    • Sugiyama, N., Masuda, T., Shinoda, K., Nakamura, A., Tomita, M., and Ishihama, Y. (2007) Phosphopeptide enrichment by ali-phatic hydroxy acid-modified metal oxide chromatography for nano-LC-MS/MS in proteomics applications. Mol Cell Proteomics 6, 1103–9.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1103-1109
    • Sugiyama, N.1    Masuda, T.2    Shinoda, K.3    Nakamura, A.4    Tomita, M.5    Ishihama, Y.6
  • 16
    • 33847782587 scopus 로고    scopus 로고
    • Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry
    • Molina, H., Horn, D. M., Tang, N., Mathivanan, S., and Pandey, A. (2007) Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci USA 104, 2199–204.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2199-2204
    • Molina, H.1    Horn, D. M.2    Tang, N.3    Mathivanan, S.4    Pandey, A.5
  • 17
    • 59349086947 scopus 로고    scopus 로고
    • Protein tyrosine phosphorylation in plants: More abundant than expected?
    • de la Fuente van Bentem, S., and Hirt, H. (2009) Protein tyrosine phosphorylation in plants: More abundant than expected? Trends Plant Sci 14, 71–6.
    • (2009) Trends Plant Sci , vol.14 , pp. 71-76
    • de la Fuente van Bentem, S.1    Hirt, H.2
  • 19
    • 0142057022 scopus 로고    scopus 로고
    • Protein phosphatases in plants
    • Luan, S. (2003) Protein phosphatases in plants. Annu Rev Plant Biol 54, 63–92.
    • (2003) Annu Rev Plant Biol , vol.54 , pp. 63-92
    • Luan, S.1
  • 20
    • 0026347515 scopus 로고
    • Identification of phosphohistidine in proteins and purification of protein-histidine kinases
    • Wei, Y. F., and Matthews, H. R. (1991) Identification of phosphohistidine in proteins and purification of protein-histidine kinases. Methods Enzymol 200, 388–414.
    • (1991) Methods Enzymol , vol.200 , pp. 388-414
    • Wei, Y. F.1    Matthews, H. R.2
  • 21
    • 33846671062 scopus 로고    scopus 로고
    • Tuning bulk electrostatics to regulate protein function
    • Serber, Z., and Ferrell, J. E., Jr. (2007) Tuning bulk electrostatics to regulate protein function. Cell 128, 441–4.
    • (2007) Cell , vol.128 , pp. 441-444
    • Serber, Z.1    Ferrell, J. E.2
  • 22
    • 33846686408 scopus 로고    scopus 로고
    • A mechanism for cell-cycle regulation of MAP kinase signaling in a yeast dif ferentiation pathway
    • Strickfaden, S. C., Winters, M. J., Ben-Ari, G., Lamson, R. E., Tyers, M., and Pryciak, P. M. (2007) A mechanism for cell-cycle regulation of MAP kinase signaling in a yeast dif ferentiation pathway. Cell 128, 519–31.
    • (2007) Cell , vol.128 , pp. 519-531
    • Strickfaden, S. C.1    Winters, M. J.2    Ben-Ari, G.3    Lamson, R. E.4    Tyers, M.5    Pryciak, P. M.6
  • 23
    • 0027310848 scopus 로고
    • The effects of phosphorylation on the structure and function of proteins
    • Johnson, L. N., and Barford, D. (1993) The effects of phosphorylation on the structure and function of proteins. Annu Rev Biophys Biomol Struct 22, 199–232.
    • (1993) Annu Rev Biophys Biomol Struct , vol.22 , pp. 199-232
    • Johnson, L. N.1    Barford, D.2
  • 24
    • 33646266474 scopus 로고    scopus 로고
    • Conformational changes in protein loops and helices induced by post-translational phosphorylation
    • Groban, E. S., Narayanan, A., and Jacobson, M. P. (2006) Conformational changes in protein loops and helices induced by post-translational phosphorylation. PLoS Comput Biol 2, e32.
    • (2006) PLoS Comput Biol , vol.2 , pp. e32
    • Groban, E. S.1    Narayanan, A.2    Jacobson, M. P.3
  • 26
    • 0040017910 scopus 로고    scopus 로고
    • Function of WW domains as phos-phoserine-or phosphothreonine-binding modules
    • Lu, P. J., Zhou, X. Z., Shen, M., and Lu, K. P. (1999) Function of WW domains as phos-phoserine-or phosphothreonine-binding modules. Science 283, 1325–8.
    • (1999) Science , vol.283 , pp. 1325-1328
    • Lu, P. J.1    Zhou, X. Z.2    Shen, M.3    Lu, K. P.4
  • 27
    • 28944437358 scopus 로고    scopus 로고
    • Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release
    • Rubin, S. M., Gall, A. L., Zheng, N., and Pavletich, N. P. (2005) Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release. Cell 123, 1093–106.
    • (2005) Cell , vol.123 , pp. 1093-1106
    • Rubin, S. M.1    Gall, A. L.2    Zheng, N.3    Pavletich, N. P.4
  • 28
    • 0029767016 scopus 로고    scopus 로고
    • Structural basis of cyclin-dependent kinase activation by phosphorylation
    • Russo, A. A., Jeffrey, P. D., and Pavletich, N. P. (1996) Structural basis of cyclin-dependent kinase activation by phosphorylation. Nat Struct Biol 3, 696–700.
    • (1996) Nat Struct Biol , vol.3 , pp. 696-700
    • Russo, A. A.1    Jeffrey, P. D.2    Pavletich, N. P.3
  • 31
    • 0025217677 scopus 로고
    • Regulation of isocitrate dehydroge-nase by phosphorylation involves no long-range conformational change in the free enzyme
    • Hurley, J. H., Dean, A. M., Thorsness, P. E., Koshland, D. E., Jr., and Stroud, R. M. (1990) Regulation of isocitrate dehydroge-nase by phosphorylation involves no long-range conformational change in the free enzyme. J Biol Chem 265, 3599–602.
    • (1990) J Biol Chem , vol.265 , pp. 3599-3602
    • Hurley, J. H.1    Dean, A. M.2    Thorsness, P. E.3    Koshland, D. E.4    Stroud, R. M.5
  • 32
    • 0026484261 scopus 로고
    • SH2 and SH3 domains: from structure to function
    • Pawson, T., and Gish, G. D. (1992) SH2 and SH3 domains: from structure to function. Cell 71, 359–62.
    • (1992) Cell , vol.71 , pp. 359-362
    • Pawson, T.1    Gish, G. D.2
  • 33
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson, T. (1995) Protein modules and signalling networks. Nature 373, 573–80.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 34
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling
    • Hunter, T. (1995) Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. Cell 80, 225–36.
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 35
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: structural basis for regulation
    • Johnson, L. N., Noble, M. E., and Owen, D. J. (1996) Active and inactive protein kinases: structural basis for regulation. Cell 85, 149–58.
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L. N.1    Noble, M. E.2    Owen, D. J.3
  • 36
    • 0027159007 scopus 로고
    • Solution structure of the cAMP-dependent protein kinase catalytic subunit and its contraction upon binding the protein kinase inhibitor peptide
    • Olah, G. A., Mitchell, R. D., Sosnick, T. R., Walsh, D. A., and Trewhella, J. (1993) Solution structure of the cAMP-dependent protein kinase catalytic subunit and its contraction upon binding the protein kinase inhibitor peptide. Biochemistry 32, 3649–57.
    • (1993) Biochemistry , vol.32 , pp. 3649-3657
    • Olah, G. A.1    Mitchell, R. D.2    Sosnick, T. R.3    Walsh, D. A.4    Trewhella, J.5
  • 37
    • 33846899405 scopus 로고    scopus 로고
    • Molecular recognition of protein kinase binding pockets for design of potent and selective kinase inhibitors
    • Liao, J. J. (2007) Molecular recognition of protein kinase binding pockets for design of potent and selective kinase inhibitors. J Med Chem 50, 409–24.
    • (2007) J Med Chem , vol.50 , pp. 409-424
    • Liao, J. J.1
  • 38
    • 33745298429 scopus 로고    scopus 로고
    • Rational design of inhibitors that bind to inactive kinase conformations
    • Liu, Y., and Gray, N. S. (2006) Rational design of inhibitors that bind to inactive kinase conformations. Nat Chem Biol 2, 358–64.
    • (2006) Nat Chem Biol , vol.2 , pp. 358-364
    • Liu, Y.1    Gray, N. S.2
  • 39
    • 70349330577 scopus 로고    scopus 로고
    • The regulation of protein phosphorylation
    • Johnson, L. N. (2009) The regulation of protein phosphorylation. Biochem Soc Trans 37, 627–41.
    • (2009) Biochem Soc Trans , vol.37 , pp. 627-641
    • Johnson, L. N.1
  • 40
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse, M., and Kuriyan, J. (2002) The conformational plasticity of protein kinases. Cell 109, 275–82.
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 41
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases; controlling activity through activation segment conformation
    • Nolen, B., Taylor, S., and Ghosh, G. (2004) Regulation of protein kinases; controlling activity through activation segment conformation. Mol Cell 15, 661–75.
    • (2004) Mol Cell , vol.15 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 42
    • 3343024236 scopus 로고    scopus 로고
    • Evolutionary constraints associated with functional specificity of the CMGC protein kinases MAPK, CDK, GSK, SRPK, DYRK, and CK2alpha
    • Kannan, N., and Neuwald, A. F. (2004) Evolutionary constraints associated with functional specificity of the CMGC protein kinases MAPK, CDK, GSK, SRPK, DYRK, and CK2alpha. Protein Sci 13, 2059–77.
    • (2004) Protein Sci , vol.13 , pp. 2059-2077
    • Kannan, N.1    Neuwald, A. F.2
  • 43
    • 0029020282 scopus 로고
    • Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification
    • Hanks, S. K., and Hunter, T. (1995) Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. Faseb J 9, 576–96.
    • (1995) Faseb J , vol.9 , pp. 576-596
    • Hanks, S. K.1    Hunter, T.2
  • 44
    • 0028818886 scopus 로고
    • How do protein kinases discriminate between serine/threonine and tyrosine? Structural insights from the insulin receptor protein-tyrosine kinase
    • Taylor, S. S., Radzio-Andzelm, E., and Hunter, T. (1995) How do protein kinases discriminate between serine/threonine and tyrosine? Structural insights from the insulin receptor protein-tyrosine kinase. Faseb J 9, 1255–66.
    • (1995) Faseb J , vol.9 , pp. 1255-1266
    • Taylor, S. S.1    Radzio-Andzelm, E.2    Hunter, T.3
  • 45
    • 0032560489 scopus 로고    scopus 로고
    • The Eleventh Datta Lecture. The structural basis for substrate recognition and control by protein kinases
    • Johnson, L. N., Lowe, E. D., Noble, M. E., and Owen, D. J. (1998) The Eleventh Datta Lecture. The structural basis for substrate recognition and control by protein kinases. FEBS Lett 430, 1–11.
    • (1998) FEBS Lett , vol.430 , pp. 1-11
    • Johnson, L. N.1    Lowe, E. D.2    Noble, M. E.3    Owen, D. J.4
  • 46
    • 33847352056 scopus 로고    scopus 로고
    • New Science Press Ltd in association with Oxford University Press, London
    • Morgan, D. O. (2007) The cell cycle: principles of control, New Science Press Ltd in association with Oxford University Press, London.
    • (2007) The cell cycle: principles of control
    • Morgan, D. O.1
  • 47
    • 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. (1988) The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 241, 42–52.
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S. K.1    Quinn, A. M.2    Hunter, T.3
  • 48
    • 34250166523 scopus 로고    scopus 로고
    • Evolved to be active: sulfate ions define substrate recognition sites of CK2alpha and emphasise its exceptional role within the CMGC family of eukaryotic protein kinases
    • Niefind, K., Yde, C. W., Ermakova, I., and Issinger, O. G. (2007) Evolved to be active: sulfate ions define substrate recognition sites of CK2alpha and emphasise its exceptional role within the CMGC family of eukaryotic protein kinases. J Mol Biol 370, 427–38.
    • (2007) J Mol Biol , vol.370 , pp. 427-438
    • Niefind, K.1    Yde, C. W.2    Ermakova, I.3    Issinger, O. G.4
  • 49
    • 0029850471 scopus 로고    scopus 로고
    • High-resolution crystal structures of human cyclin-dependent kinase 2 with and without ATP: bound waters and natural ligand as guides for inhibitor design
    • Schulze-Gahmen, U., De Bondt, H. L., and Kim, S. H. (1996) High-resolution crystal structures of human cyclin-dependent kinase 2 with and without ATP: bound waters and natural ligand as guides for inhibitor design. J Med Chem 39, 4540–6.
    • (1996) J Med Chem , vol.39 , pp. 4540-4546
    • Schulze-Gahmen, U.1    De Bondt, H. L.2    Kim, S. H.3
  • 50
    • 0035413606 scopus 로고    scopus 로고
    • Kinetic and catalytic mechanisms of protein kinases
    • Adams, J. A. (2001) Kinetic and catalytic mechanisms of protein kinases. Chem Rev 101, 2271–90.
    • (2001) Chem Rev , vol.101 , pp. 2271-2290
    • Adams, J. A.1
  • 51
    • 0026345394 scopus 로고
    • Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members
    • Hanks, S. K., and Quinn, A. M. (1991) Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Methods Enzymol 200, 38–62.
    • (1991) Methods Enzymol , vol.200 , pp. 38-62
    • Hanks, S. K.1    Quinn, A. M.2
  • 52
    • 0027585031 scopus 로고
    • Targets of cyclin-dependent protein kinases
    • Nigg, E. A. (1993) Targets of cyclin-dependent protein kinases. Curr Opin Cell Biol 5, 187–93.
    • (1993) Curr Opin Cell Biol , vol.5 , pp. 187-193
    • Nigg, E. A.1
  • 54
    • 0030272039 scopus 로고    scopus 로고
    • A conserved motif at the amino termini of MEKs might mediate high-affinity interaction with the cognate MAPKs
    • Bardwell, L., and Thorner, J. (1996) A conserved motif at the amino termini of MEKs might mediate high-affinity interaction with the cognate MAPKs. Trends Biochem Sci 21, 373–4.
    • (1996) Trends Biochem Sci , vol.21 , pp. 373-374
    • Bardwell, L.1    Thorner, J.2
  • 56
    • 0033224309 scopus 로고    scopus 로고
    • The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases
    • Brown, N. R., Noble, M. E., Endicott, J. A., and Johnson, L. N. (1999) The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases. Nat Cell Biol 1, 438–43.
    • (1999) Nat Cell Biol , vol.1 , pp. 438-443
    • Brown, N. R.1    Noble, M. E.2    Endicott, J. A.3    Johnson, L. N.4
  • 58
    • 0028157664 scopus 로고
    • Atomic structure of the MAP kinase ERK2 at 2.3 A resolution
    • Zhang, F., Strand, A., Robbins, D., Cobb, M. H., and Goldsmith, E. J. (1994) Atomic structure of the MAP kinase ERK2 at 2.3 A resolution. Nature 367, 704–11.
    • (1994) Nature , vol.367 , pp. 704-711
    • Zhang, F.1    Strand, A.2    Robbins, D.3    Cobb, M. H.4    Goldsmith, E. J.5
  • 59
    • 0028898390 scopus 로고
    • Phosphorylation modulates catalytic function and regulation in the cAMP-dependent protein kinase
    • Adams, J. A., McGlone, M. L., Gibson, R., and Taylor, S. S. (1995) Phosphorylation modulates catalytic function and regulation in the cAMP-dependent protein kinase. Biochemistry 34, 2447–54.
    • (1995) Biochemistry , vol.34 , pp. 2447-2454
    • Adams, J. A.1    McGlone, M. L.2    Gibson, R.3    Taylor, S. S.4
  • 60
    • 34250786312 scopus 로고    scopus 로고
    • T-loop phosphorylation of Arabidopsis CDKA;1 is required for its function and can be partially substituted by an aspartate residue
    • Dissmeyer, N., Nowack, M. K., Pusch, S., Stals, H., Inze, D., Grini, P. E., and Schnittger, A. (2007) T-loop phosphorylation of Arabidopsis CDKA;1 is required for its function and can be partially substituted by an aspartate residue. Plant Cell 19, 972–85.
    • (2007) Plant Cell , vol.19 , pp. 972-985
    • Dissmeyer, N.1    Nowack, M. K.2    Pusch, S.3    Stals, H.4    Inze, D.5    Grini, P. E.6    Schnittger, A.7
  • 62
    • 0028271690 scopus 로고
    • Protein kinase regulation: insights from crystal structure analysis
    • Morgan, D. O., and De Bondt, H. L. (1994) Protein kinase regulation: insights from crystal structure analysis. Curr Opin Cell Biol 6, 239–46.
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 239-246
    • Morgan, D. O.1    De Bondt, H. L.2
  • 65
    • 34250878954 scopus 로고    scopus 로고
    • Mechanisms of specificity in protein phosphorylation
    • Ubersax, J. A., and Ferrell, J. E., Jr. (2007) Mechanisms of specificity in protein phosphorylation. Nat Rev Mol Cell Biol 8, 530–41.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 530-541
    • Ubersax, J. A.1    Ferrell, J. E.2
  • 66
    • 0036305943 scopus 로고    scopus 로고
    • Sequence and structure classification of kinases
    • Cheek, S., Zhang, H., and Grishin, N. V. (2002) Sequence and structure classification of kinases. J Mol Biol 320, 855–81.
    • (2002) J Mol Biol , vol.320 , pp. 855-881
    • Cheek, S.1    Zhang, H.2    Grishin, N. V.3
  • 68
    • 4143139896 scopus 로고    scopus 로고
    • The mouse kinome: discovery and comparative genomics of all mouse protein kinases
    • Caenepeel, S., Charydczak, G., Sudarsanam, S., Hunter, T., and Manning, G. (2004) The mouse kinome: discovery and comparative genomics of all mouse protein kinases. Proc Natl Acad Sci USA 101, 11707–12.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 11707-11712
    • Caenepeel, S.1    Charydczak, G.2    Sudarsanam, S.3    Hunter, T.4    Manning, G.5
  • 69
    • 33748573639 scopus 로고    scopus 로고
    • Charging it up: global analysis of protein phosphorylation
    • Ptacek, J., and Snyder, M. (2006) Charging it up: global analysis of protein phosphorylation. Trends Genet 22, 545–54.
    • (2006) Trends Genet , vol.22 , pp. 545-554
    • Ptacek, J.1    Snyder, M.2
  • 70
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • The Arabidopsis Genome Initiative
    • The Arabidopsis Genome Initiative. (2000) Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 408, 796–815.
    • (2000) Nature , vol.408 , pp. 796-815
  • 71
    • 84907150192 scopus 로고    scopus 로고
    • The map-based sequence of the rice genome
    • International Rice Genome Sequencing Project
    • International Rice Genome Sequencing Project. (2005) The map-based sequence of the rice genome. Nature 436, 793–800.
    • (2005) Nature , vol.436 , pp. 793-800
  • 72
    • 33747889617 scopus 로고    scopus 로고
    • Genome-wide comparative analyses of domain organisation of repertoires of protein kinases of Arabidopsis thaliana and Oryza sativa
    • Krupa, A., Anamika, K., and Srinivasan, N. (2006) Genome-wide comparative analyses of domain organisation of repertoires of protein kinases of Arabidopsis thaliana and Oryza sativa. Gene 380, 1–13.
    • (2006) Gene , vol.380 , pp. 1-13
    • Krupa, A.1    Anamika, K.2    Srinivasan, N.3
  • 77
    • 0031026008 scopus 로고    scopus 로고
    • The protein kinases of budding yeast: six score and more
    • Hunter, T., and Plowman, G. D. (1997) The protein kinases of budding yeast: six score and more. Trends Biochem Sci 22, 18–22.
    • (1997) Trends Biochem Sci , vol.22 , pp. 18-22
    • Hunter, T.1    Plowman, G. D.2
  • 78
    • 34247234601 scopus 로고    scopus 로고
    • The rice kinase database. A phylogenomic database for the rice kinome
    • Dardick, C., Chen, J., Richter, T., Ouyang, S., and Ronald, P. (2007) The rice kinase database. A phylogenomic database for the rice kinome. Plant Physiol 143, 579–86.
    • (2007) Plant Physiol , vol.143 , pp. 579-586
    • Dardick, C.1    Chen, J.2    Richter, T.3    Ouyang, S.4    Ronald, P.5
  • 79
    • 84864278347 scopus 로고    scopus 로고
    • Using sequence similarity networks for visualization of relationships across diverse protein superfamilies
    • Atkinson, H. J., Morris, J. H., Ferrin, T. E., and Babbitt, P. C. (2009) Using sequence similarity networks for visualization of relationships across diverse protein superfamilies. PLoS One 4, e4345.
    • (2009) PLoS One , vol.4 , pp. e4345
    • Atkinson, H. J.1    Morris, J. H.2    Ferrin, T. E.3    Babbitt, P. C.4
  • 80
    • 0033499326 scopus 로고    scopus 로고
    • PLANT PROTEIN SERINE/THREONINE KINASES: Classification and Functions
    • Hardie, D. G. (1999) PLANT PROTEIN SERINE/THREONINE KINASES: Classification and Functions. Annu Rev Plant Physiol Plant Mol Biol 50, 97–131.
    • (1999) Annu Rev Plant Physiol Plant Mol Biol , vol.50 , pp. 97-131
    • Hardie, D. G.1
  • 81
    • 1542320494 scopus 로고    scopus 로고
    • Reassessing the MAP3K and MAP4K relationships
    • Champion, A., Picaud, A., and Henry, Y. (2004) Reassessing the MAP3K and MAP4K relationships. Trends Plant Sci 9, 123–9.
    • (2004) Trends Plant Sci , vol.9 , pp. 123-129
    • Champion, A.1    Picaud, A.2    Henry, Y.3
  • 82
    • 14644422704 scopus 로고    scopus 로고
    • Global analysis of the core cell cycle regulators of Arabidopsis identifies novel genes, reveals multiple and highly specific profiles of expression and provides a coherent model for plant cell cycle control
    • Menges, M., de Jager, S. M., Gruissem, W., and Murray, J. A. (2005) Global analysis of the core cell cycle regulators of Arabidopsis identifies novel genes, reveals multiple and highly specific profiles of expression and provides a coherent model for plant cell cycle control. Plant J 41, 546–66.
    • (2005) Plant J , vol.41 , pp. 546-566
    • Menges, M.1    de Jager, S. M.2    Gruissem, W.3    Murray, J. A.4
  • 83
    • 68149154791 scopus 로고    scopus 로고
    • MAPK cascade signalling networks in plant defence
    • Pitzschke, A., Schikora, A., and Hirt, H. (2009) MAPK cascade signalling networks in plant defence. Curr Opin Plant Biol 12, 421–6.
    • (2009) Curr Opin Plant Biol , vol.12 , pp. 421-426
    • Pitzschke, A.1    Schikora, A.2    Hirt, H.3
  • 85
    • 75749131083 scopus 로고    scopus 로고
    • Convergence and specificity in the Arabidopsis MAPK nexus
    • Andreasson, E., and Ellis, B. (2010) Convergence and specificity in the Arabidopsis MAPK nexus. Trends Plant Sci 15, 106–113.
    • (2010) Trends Plant Sci , vol.15 , pp. 106-113
    • Andreasson, E.1    Ellis, B.2
  • 88
    • 76749150030 scopus 로고    scopus 로고
    • Genome sequencing and analysis of the model grass Brachypodium distachyon
    • International Brachypodium Initiative, T
    • International Brachypodium Initiative, T. (2010) Genome sequencing and analysis of the model grass Brachypodium distachyon. Nature 463, 763–8.
    • (2010) Nature , vol.463 , pp. 763-768
  • 89
    • 34848886909 scopus 로고    scopus 로고
    • The grapevine genome sequence suggests ancestral hexaploidization in major angiosperm phyla
    • The French-Italian Public Consortium for Grapevine Genome Characterization
    • The French-Italian Public Consortium for Grapevine Genome Characterization. (2007) The grapevine genome sequence suggests ancestral hexaploidization in major angiosperm phyla. Nature 449, 463–467.
    • (2007) Nature , vol.449 , pp. 463-467
  • 90
    • 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. (2001) Receptor-like kinases from Arabidopsis form a monophyletic gene family related to animal receptor kinases. Proc Natl Acad Sci USA 98, 10763–8.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10763-10768
    • Shiu, S. H.1    Bleecker, A. B.2
  • 91
    • 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. (2004) Comparative analysis of the receptor-like kinase family in Arabidopsis and rice. Plant Cell 16, 1220–34.
    • (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
  • 92
    • 33645776778 scopus 로고    scopus 로고
    • Plant and animal pathogen recognition receptors signal through non-RD kinases
    • Dardick, C., and Ronald, P. (2006) Plant and animal pathogen recognition receptors signal through non-RD kinases. PLoS Pathog 2, e2.
    • (2006) PLoS Pathog , vol.2 , pp. e2
    • Dardick, C.1    Ronald, P.2
  • 93
    • 0034644524 scopus 로고    scopus 로고
    • Conservation and innovation in plant signaling pathways
    • McCarty, D. R., and Chory, J. (2000) Conservation and innovation in plant signaling pathways. Cell 103, 201–9.
    • (2000) Cell , vol.103 , pp. 201-209
    • McCarty, D. R.1    Chory, J.2
  • 94
    • 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. (2003) Systematic trans-genomic comparison of protein kinases between Arabidopsis and Saccharomyces cerevisiae. Plant Physiol 132, 2152–65.
    • (2003) Plant Physiol , vol.132 , pp. 2152-2165
    • Wang, D.1    Harper, J. F.2    Gribskov, M.3
  • 95
    • 0037015047 scopus 로고    scopus 로고
    • Tyrosine phosphorylation in plant cell signaling
    • Luan, S. (2002) Tyrosine phosphorylation in plant cell signaling. Proc Natl Acad Sci USA 99, 11567–9.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11567-11569
    • Luan, S.1
  • 96
    • 0036859906 scopus 로고    scopus 로고
    • Comparative proteome bioinformatics: identification of a whole complement of putative protein tyrosine kinases in the model flowering plant Arabidopsis thaliana
    • Carpi, A., Di Maira, G., Vedovato, M., Rossi, V., Naccari, T., Floriduz, M., Terzi, M., and Filippini, F. (2002) Comparative proteome bioinformatics: identification of a whole complement of putative protein tyrosine kinases in the model flowering plant Arabidopsis thaliana. Proteomics 2, 1494–503.
    • (2002) Proteomics , vol.2 , pp. 1494-1503
    • Carpi, A.1    Di Maira, G.2    Vedovato, M.3    Rossi, V.4    Naccari, T.5    Floriduz, M.6    Terzi, M.7    Filippini, F.8
  • 97
    • 31044454762 scopus 로고    scopus 로고
    • Genome-wide analysis and experimentation of plant serine/thre-onine/tyrosine-specific protein kinases
    • Rudrabhatla, P., Reddy, M. M., and Rajasekharan, R. (2006) Genome-wide analysis and experimentation of plant serine/thre-onine/tyrosine-specific protein kinases. Plant Mol Biol 60, 293–319.
    • (2006) Plant Mol Biol , vol.60 , pp. 293-319
    • Rudrabhatla, P.1    Reddy, M. M.2    Rajasekharan, R.3
  • 98
    • 34548808594 scopus 로고    scopus 로고
    • Classification and functional annotation of eukaryotic protein kinases
    • Miranda-Saavedra, D., and Barton, G. J. (2007) Classification and functional annotation of eukaryotic protein kinases. Proteins 68, 893–914.
    • (2007) Proteins , vol.68 , pp. 893-914
    • Miranda-Saavedra, D.1    Barton, G. J.2
  • 99
    • 20444383859 scopus 로고    scopus 로고
    • Protein phosphorylation in signaling – 50 years and counting
    • Pawson, T., and Scott, J. D. (2005) Protein phosphorylation in signaling – 50 years and counting. Trends Biochem Sci 30, 286–90.
    • (2005) Trends Biochem Sci , vol.30 , pp. 286-290
    • Pawson, T.1    Scott, J. D.2
  • 100
    • 0033279836 scopus 로고    scopus 로고
    • SCF and Cullin/Ring H2-based ubiquitin ligases
    • Deshaies, R. J. (1999) SCF and Cullin/Ring H2-based ubiquitin ligases. Annu Rev Cell Dev Biol 15, 435–67.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 435-467
    • Deshaies, R. J.1
  • 101
  • 102
    • 0033544866 scopus 로고    scopus 로고
    • COP9 signalosome-directed c-Jun activation/stabi-lization is independent of JNK
    • Naumann, M., Bech-Otschir, D., Huang, X., Ferrell, K., and Dubiel, W. (1999) COP9 signalosome-directed c-Jun activation/stabi-lization is independent of JNK. J Biol Chem 274, 35297–300.
    • (1999) J Biol Chem , vol.274 , pp. 35297-35300
    • Naumann, M.1    Bech-Otschir, D.2    Huang, X.3    Ferrell, K.4    Dubiel, W.5
  • 103
    • 0035794541 scopus 로고    scopus 로고
    • COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system
    • Bech-Otschir, D., Kraft, R., Huang, X., Henklein, P., Kapelari, B., Pollmann, C., and Dubiel, W. (2001) COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system. Embo J 20, 1630–9.
    • (2001) Embo J , vol.20 , pp. 1630-1639
    • Bech-Otschir, D.1    Kraft, R.2    Huang, X.3    Henklein, P.4    Kapelari, B.5    Pollmann, C.6    Dubiel, W.7
  • 105
    • 0029670193 scopus 로고    scopus 로고
    • Rapid degradation of the G1 cyclin Cln2 induced by CDK-dependent phosphorylation
    • Lanker, S., Valdivieso, M. H., and Wittenberg, C. (1996) Rapid degradation of the G1 cyclin Cln2 induced by CDK-dependent phosphorylation. Science 271, 1597–601.
    • (1996) Science , vol.271 , pp. 1597-1601
    • Lanker, S.1    Valdivieso, M. H.2    Wittenberg, C.3
  • 106
    • 0030847760 scopus 로고    scopus 로고
    • Phosphorylation-dependent degradation of the cyclin-dependent kinase inhibitor p27
    • Vlach, J., Hennecke, S., and Amati, B. (1997) Phosphorylation-dependent degradation of the cyclin-dependent kinase inhibitor p27. Embo J 16, 5334–44.
    • (1997) Embo J , vol.16 , pp. 5334-5344
    • Vlach, J.1    Hennecke, S.2    Amati, B.3
  • 108
    • 29444454751 scopus 로고    scopus 로고
    • A positive signal from the fertilization of the egg cell sets off endosperm proliferation in angiosperm embryogenesis
    • Nowack, M. K., Grini, P. E., Jakoby, M. J., Lafos, M., Koncz, C., and Schnittger, A. (2006) A positive signal from the fertilization of the egg cell sets off endosperm proliferation in angiosperm embryogenesis. Nat Genet 38, 63–7.
    • (2006) Nat Genet , vol.38 , pp. 63-67
    • Nowack, M. K.1    Grini, P. E.2    Jakoby, M. J.3    Lafos, M.4    Koncz, C.5    Schnittger, A.6
  • 109
    • 33644858006 scopus 로고    scopus 로고
    • Arabidopsis CDKA;1, a cdc2 homo-logue, controls proliferation of generative cells in male gametogenesis
    • Iwakawa, H., Shinmyo, A., and Sekine, M. (2006) Arabidopsis CDKA;1, a cdc2 homo-logue, controls proliferation of generative cells in male gametogenesis. Plant J 45, 819–31.
    • (2006) Plant J , vol.45 , pp. 819-831
    • Iwakawa, H.1    Shinmyo, A.2    Sekine, M.3
  • 111
    • 34248650674 scopus 로고    scopus 로고
    • Stomatal development and patterning are regulated by environmentally responsive mitogen-activated protein kinases in Arabidopsis
    • Wang, H., Ngwenyama, N., Liu, Y., Walker, J. C., and Zhang, S. (2007) Stomatal development and patterning are regulated by environmentally responsive mitogen-activated protein kinases in Arabidopsis. Plant Cell 19, 63–73.
    • (2007) Plant Cell , vol.19 , pp. 63-73
    • Wang, H.1    Ngwenyama, N.2    Liu, Y.3    Walker, J. C.4    Zhang, S.5
  • 112
    • 56449126420 scopus 로고    scopus 로고
    • Arabidopsis stomatal initiation is controlled by MAPK-mediated regulation of the bHLH SPEECHLESS
    • Lampard, G. R., Macalister, C. A., and Bergmann, D. C. (2008) Arabidopsis stomatal initiation is controlled by MAPK-mediated regulation of the bHLH SPEECHLESS. Science 322, 1113–6.
    • (2008) Science , vol.322 , pp. 1113-1116
    • Lampard, G. R.1    Macalister, C. A.2    Bergmann, D. C.3
  • 113
    • 0035208670 scopus 로고    scopus 로고
    • MAPK cascades in plant defense signaling
    • Zhang, S., and Klessig, D. F. (2001) MAPK cascades in plant defense signaling. Trends Plant Sci 6, 520–7.
    • (2001) Trends Plant Sci , vol.6 , pp. 520-527
    • Zhang, S.1    Klessig, D. F.2
  • 114
    • 0036779407 scopus 로고    scopus 로고
    • Complexity, cross talk and integration of plant MAP kinase signalling
    • Jonak, C., Okresz, L., Bogre, L., and Hirt, H. (2002) Complexity, cross talk and integration of plant MAP kinase signalling. Curr Opin Plant Biol 5, 415–24.
    • (2002) Curr Opin Plant Biol , vol.5 , pp. 415-424
    • Jonak, C.1    Okresz, L.2    Bogre, L.3    Hirt, H.4
  • 115
    • 0034865417 scopus 로고    scopus 로고
    • Protein kinases in the plant defence response
    • Romeis, T. (2001) Protein kinases in the plant defence response. Curr Opin Plant Biol 4, 407–14.
    • (2001) Curr Opin Plant Biol , vol.4 , pp. 407-414
    • Romeis, T.1
  • 116
    • 66049110566 scopus 로고    scopus 로고
    • Flg22 regulates the release of an ethylene response factor substrate from MAP kinase 6 in Arabidopsis thaliana via ethylene signaling
    • Bethke, G., Unthan, T., Uhrig, J. F., Poschl, Y., Gust, A. A., Scheel, D., and Lee, J. (2009) Flg22 regulates the release of an ethylene response factor substrate from MAP kinase 6 in Arabidopsis thaliana via ethylene signaling. Proc Natl Acad Sci USA 106, 8067–72.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 8067-8072
    • Bethke, G.1    Unthan, T.2    Uhrig, J. F.3    Poschl, Y.4    Gust, A. A.5    Scheel, D.6    Lee, J.7
  • 117
    • 40949092722 scopus 로고    scopus 로고
    • MAPK phosphorylation-induced stabilization of ACS6 protein is mediated by the non-catalytic C-terminal domain, which also contains the cis-determinant for rapid degradation by the 26S proteasome pathway
    • Joo, S., Liu, Y., Lueth, A., and Zhang, S. (2008) MAPK phosphorylation-induced stabilization of ACS6 protein is mediated by the non-catalytic C-terminal domain, which also contains the cis-determinant for rapid degradation by the 26S proteasome pathway. Plant J 54, 129–40.
    • (2008) Plant J , vol.54 , pp. 129-140
    • Joo, S.1    Liu, Y.2    Lueth, A.3    Zhang, S.4
  • 118
    • 39149095565 scopus 로고    scopus 로고
    • Dual control of nuclear EIN3 by bifurcate MAPK cascades in C2H4 signalling
    • Yoo, S. D., Cho, Y. H., Tena, G., Xiong, Y., and Sheen, J. (2008) Dual control of nuclear EIN3 by bifurcate MAPK cascades in C2H4 signalling. Nature 451, 789–95.
    • (2008) Nature , vol.451 , pp. 789-795
    • Yoo, S. D.1    Cho, Y. H.2    Tena, G.3    Xiong, Y.4    Sheen, J.5
  • 119
    • 0030116870 scopus 로고    scopus 로고
    • The Arabidopsis ERECTA gene encodes a putative receptor protein kinase with extracellular leucine-rich repeats
    • Torii, K. U., Mitsukawa, N., Oosumi, T., Matsuura, Y., Yokoyama, R., Whittier, R. F., and Komeda, Y. (1996) The Arabidopsis ERECTA gene encodes a putative receptor protein kinase with extracellular leucine-rich repeats. Plant Cell 8, 735–46.
    • (1996) Plant Cell , vol.8 , pp. 735-746
    • Torii, K. U.1    Mitsukawa, N.2    Oosumi, T.3    Matsuura, Y.4    Yokoyama, R.5    Whittier, R. F.6    Komeda, Y.7
  • 120
    • 0030729445 scopus 로고    scopus 로고
    • The CLAVATA1 gene encodes a putative receptor kinase that controls shoot and floral meristem size in Arabidopsis
    • Clark, S. E., Williams, R. W., and Meyerowitz, E. M. (1997) The CLAVATA1 gene encodes a putative receptor kinase that controls shoot and floral meristem size in Arabidopsis. Cell 89, 575–85.
    • (1997) Cell , vol.89 , pp. 575-585
    • Clark, S. E.1    Williams, R. W.2    Meyerowitz, E. M.3
  • 121
    • 0027752777 scopus 로고
    • The Tousled gene in A. thaliana encodes a protein kinase homolog that is required for leaf and flower development
    • Roe, J. L., Rivin, C. J., Sessions, R. A., Feldmann, K. A., and Zambryski, P. C. (1993) The Tousled gene in A. thaliana encodes a protein kinase homolog that is required for leaf and flower development. Cell 75, 939–50.
    • (1993) Cell , vol.75 , pp. 939-950
    • Roe, J. L.1    Rivin, C. J.2    Sessions, R. A.3    Feldmann, K. A.4    Zambryski, P. C.5
  • 122
    • 0033957459 scopus 로고    scopus 로고
    • HAESA, an Arabidopsis leucine-rich repeat receptor kinase, controls floral organ abscission
    • Jinn, T. L., Stone, J. M., and Walker, J. C. (2000) HAESA, an Arabidopsis leucine-rich repeat receptor kinase, controls floral organ abscission. Genes Dev 14, 108–17.
    • (2000) Genes Dev , vol.14 , pp. 108-117
    • Jinn, T. L.1    Stone, J. M.2    Walker, J. C.3
  • 123
    • 0033827884 scopus 로고    scopus 로고
    • Receptor kinase activation and signal transduction in plants: an emerging picture
    • Torii, K. U. (2000) Receptor kinase activation and signal transduction in plants: an emerging picture. Curr Opin Plant Biol 3, 361–7.
    • (2000) Curr Opin Plant Biol , vol.3 , pp. 361-367
    • Torii, K. U.1
  • 124
    • 77952507231 scopus 로고    scopus 로고
    • Brassinosteroid Signal Transduction from Receptor Kinases to Transcription Factors
    • 24
    • Kim, T. W., and Wang, Z. Y. (2010) Brassinosteroid Signal Transduction from Receptor Kinases to Transcription Factors. Annu Rev Plant Biol 61, 1–23.24.
    • (2010) Annu Rev Plant Biol , vol.61 , pp. 1-23
    • Kim, T. W.1    Wang, Z. Y.2
  • 125
    • 0033828022 scopus 로고    scopus 로고
    • Cell-cell signaling in the self-incompatibility response
    • Nasrallah, J. B. (2000) Cell-cell signaling in the self-incompatibility response. Curr Opin Plant Biol 3, 368–73.
    • (2000) Curr Opin Plant Biol , vol.3 , pp. 368-373
    • Nasrallah, J. B.1
  • 126
    • 0036439235 scopus 로고    scopus 로고
    • Receptor kinase signaling in plant development
    • Becraft, P. W. (2002) Receptor kinase signaling in plant development. Annu Rev Cell Dev Biol 18, 163–92.
    • (2002) Annu Rev Cell Dev Biol , vol.18 , pp. 163-192
    • Becraft, P. W.1
  • 127
    • 44149086357 scopus 로고    scopus 로고
    • Novel receptor kinases involved in growth regulation
    • Hematy, K., and Hofte, H. (2008) Novel receptor kinases involved in growth regulation. Curr Opin Plant Biol 11, 321–8.
    • (2008) Curr Opin Plant Biol , vol.11 , pp. 321-328
    • Hematy, K.1    Hofte, H.2
  • 128
    • 0027380220 scopus 로고
    • Arabidopsis eth-ylene-response gene ETR1: similarity of product to two-component regulators
    • Chang, C., Kwok, S. F., Bleecker, A. B., and Meyerowitz, E. M. (1993) Arabidopsis eth-ylene-response gene ETR1: similarity of product to two-component regulators. Science 262, 539–44.
    • (1993) Science , vol.262 , pp. 539-544
    • Chang, C.1    Kwok, S. F.2    Bleecker, A. B.3    Meyerowitz, E. M.4
  • 130
    • 0032563147 scopus 로고    scopus 로고
    • Ethylene responses are negatively regulated by a receptor gene family in Arabidopsis thaliana
    • Hua, J., and Meyerowitz, E. M. (1998) Ethylene responses are negatively regulated by a receptor gene family in Arabidopsis thaliana. Cell 94, 261–71.
    • (1998) Cell , vol.94 , pp. 261-271
    • Hua, J.1    Meyerowitz, E. M.2
  • 131
    • 0036914930 scopus 로고    scopus 로고
    • Effect of ethylene pathway mutations upon expression of the ethylene receptor ETR1 from Arabidopsis
    • Zhao, X. C., Qu, X., Mathews, D. E., and Schaller, G. E. (2002) Effect of ethylene pathway mutations upon expression of the ethylene receptor ETR1 from Arabidopsis. Plant Physiol 130, 1983–91.
    • (2002) Plant Physiol , vol.130 , pp. 1983-1991
    • Zhao, X. C.1    Qu, X.2    Mathews, D. E.3    Schaller, G. E.4
  • 132
    • 0037422588 scopus 로고    scopus 로고
    • Canonical histidine kinase activity of the transmitter domain of the ETR1 ethylene receptor from Arabidopsis is not required for signal transmission
    • Wang, W., Hall, A. E., O’Malley, R., and Bleecker, A. B. (2003) Canonical histidine kinase activity of the transmitter domain of the ETR1 ethylene receptor from Arabidopsis is not required for signal transmission. Proc Natl Acad Sci USA 100, 352–7.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 352-357
    • Wang, W.1    Hall, A. E.2    O’Malley, R.3    Bleecker, A. B.4
  • 133
    • 77953214257 scopus 로고    scopus 로고
    • Arabidopsis Histidine Kinase CKI1 Acts Upstream of HISTIDINE PHOSPHOTRANSFER PROTEINS to Regulate Female Gametophyte Development and Vegetative Growth
    • tpc.108.065128
    • Deng, Y., Dong, H., Mu, J., Ren, B., Zheng, B., Ji, Z., Yang, W.-C., Liang, Y., and Zuo, J. (2010) Arabidopsis Histidine Kinase CKI1 Acts Upstream of HISTIDINE PHOSPHOTRANSFER PROTEINS to Regulate Female Gametophyte Development and Vegetative Growth. Plant Cell, tpc.108.065128.
    • (2010) Plant Cell
    • Deng, Y.1    Dong, H.2    Mu, J.3    Ren, B.4    Zheng, B.5    Ji, Z.6    Yang, W.-C.7    Liang, Y.8    Zuo, J.9
  • 134
    • 0034614490 scopus 로고    scopus 로고
    • Signaling – 2000 and beyond
    • Hunter, T. (2000) Signaling – 2000 and beyond. Cell 100, 113–27.
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 137
    • 33645765762 scopus 로고    scopus 로고
    • The dictyostelium kinome – analysis of the protein kinases from a simple model organism
    • Goldberg, J. M., Manning, G., Liu, A., Fey, P., Pilcher, K. E., Xu, Y., and Smith, J. L. (2006) The dictyostelium kinome – analysis of the protein kinases from a simple model organism. PLoS Genet 2, e38.
    • (2006) PLoS Genet , vol.2 , pp. e38
    • Goldberg, J. M.1    Manning, G.2    Liu, A.3    Fey, P.4    Pilcher, K. E.5    Xu, Y.6    Smith, J. L.7
  • 139
    • 0033598830 scopus 로고    scopus 로고
    • The protein kinases of Caenorhabditis elegans: a model for signal transduction in multicellular organisms
    • Plowman, G. D., Sudarsanam, S., Bingham, J., Whyte, D., and Hunter, T. (1999) The protein kinases of Caenorhabditis elegans: a model for signal transduction in multicellular organisms. Proc Natl Acad Sci USA 96, 13603–10.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13603-13610
    • Plowman, G. D.1    Sudarsanam, S.2    Bingham, J.3    Whyte, D.4    Hunter, T.5
  • 140
    • 38549135536 scopus 로고    scopus 로고
    • Genomic overview of protein kinases
    • Manning, G. (2005) Genomic overview of protein kinases. WormBook, 1–19.
    • (2005) WormBook , pp. 1-19
    • Manning, G.1
  • 141
    • 0032509302 scopus 로고    scopus 로고
    • Genome sequence of the nematode C. elegans: a platform for investigating biology
    • C. elegans Sequencing Consortium, T
    • C. elegans Sequencing Consortium, T. (1998) Genome sequence of the nematode C. elegans: a platform for investigating biology. Science 282, 2012–8.
    • (1998) Science , vol.282 , pp. 2012-2018
  • 146
    • 4544291080 scopus 로고    scopus 로고
    • Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database
    • Nuhse, T. S., Stensballe, A., Jensen, O. N., and Peck, S. C. (2004) Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database. Plant Cell 16, 2394–405.
    • (2004) Plant Cell , vol.16 , pp. 2394-2405
    • Nuhse, T. S.1    Stensballe, A.2    Jensen, O. N.3    Peck, S. C.4
  • 149
    • 37549018044 scopus 로고    scopus 로고
    • Functional flexibility of human cyclin-dependent kinase-2 and its evolutionary conservation
    • Bartova, I., Koca, J., and Otyepka, M. (2008) Functional flexibility of human cyclin-dependent kinase-2 and its evolutionary conservation. Protein Sci 17, 22–33.
    • (2008) Protein Sci , vol.17 , pp. 22-33
    • Bartova, I.1    Koca, J.2    Otyepka, M.3
  • 150
    • 38549127781 scopus 로고    scopus 로고
    • PhosPhAt: a database of phosphorylation sites in Arabidopsis thaliana and a plant-specific phosphorylation site predictor
    • Heazlewood, J. L., Durek, P., Hummel, J., Selbig, J., Weckwerth, W., Walther, D., and Schulze, W. X. (2008) PhosPhAt: a database of phosphorylation sites in Arabidopsis thaliana and a plant-specific phosphorylation site predictor. Nucleic Acids Res 36, D1015–21.
    • (2008) Nucleic Acids Res , vol.36 , pp. D1015-D1021
    • Heazlewood, J. L.1    Durek, P.2    Hummel, J.3    Selbig, J.4    Weckwerth, W.5    Walther, D.6    Schulze, W. X.7
  • 152
    • 40349091686 scopus 로고    scopus 로고
    • An “Electronic Fluorescent Pictograph” browser for exploring and analyzing large-scale biological data sets
    • Winter, D., Vinegar, B., Nahal, H., Ammar, R., Wilson, G. V., and Provart, N. J. (2007) An “Electronic Fluorescent Pictograph” browser for exploring and analyzing large-scale biological data sets. PLoS One 2, e718.
    • (2007) PLoS One , vol.2 , pp. e718
    • Winter, D.1    Vinegar, B.2    Nahal, H.3    Ammar, R.4    Wilson, G. V.5    Provart, N. J.6
  • 157
    • 3042602443 scopus 로고    scopus 로고
    • TILLING. Traditional mutagenesis meets functional genomics
    • Henikoff, S., Till, B. J., and Comai, L. (2004) TILLING. Traditional mutagenesis meets functional genomics. Plant Physiol 135, 630–6.
    • (2004) Plant Physiol , vol.135 , pp. 630-636
    • Henikoff, S.1    Till, B. J.2    Comai, L.3
  • 158
  • 159
    • 58149193245 scopus 로고    scopus 로고
    • Kinomer v. 1.0: a database of systematically classified eukaryotic protein kinases
    • Martin, D. M., Miranda-Saavedra, D., and Barton, G. J. (2009) Kinomer v. 1.0: a database of systematically classified eukaryotic protein kinases. Nucleic Acids Res 37, D244–50.
    • (2009) Nucleic Acids Res , vol.37 , pp. D244-D250
    • Martin, D. M.1    Miranda-Saavedra, D.2    Barton, G. J.3
  • 166
    • 0029410712 scopus 로고
    • Mapping the transition state for ATP hydrolysis: implications for enzymatic catalysis
    • Admiraal, S. J., and Herschlag, D. (1995) Mapping the transition state for ATP hydrolysis: implications for enzymatic catalysis. Chem Biol 2, 729–39.
    • (1995) Chem Biol , vol.2 , pp. 729-739
    • Admiraal, S. J.1    Herschlag, D.2
  • 167
    • 0028262202 scopus 로고
    • Crystal structures of rat acid phosphatase complexed with the transition-state analogs vanadate and molybdate. Implications for the reaction mechanism
    • Lindqvist, Y., Schneider, G., and Vihko, P. (1994) Crystal structures of rat acid phosphatase complexed with the transition-state analogs vanadate and molybdate. Implications for the reaction mechanism. Eur J Biochem 221, 139–42.
    • (1994) Eur J Biochem , vol.221 , pp. 139-142
    • Lindqvist, Y.1    Schneider, G.2    Vihko, P.3
  • 168
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu, W., Harrison, S. C., and Eck, M. J. (1997) Three-dimensional structure of the tyrosine kinase c-Src. Nature 385, 595–602.
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S. C.2    Eck, M. J.3
  • 173
    • 14644402341 scopus 로고    scopus 로고
    • Inclining the purine base binding plane in protein kinase CK2 by exchanging the flanking side-chains generates a preference for ATP as a cosubstrate
    • Yde, C. W., Ermakova, I., Issinger, O. G., and Niefind, K. (2005) Inclining the purine base binding plane in protein kinase CK2 by exchanging the flanking side-chains generates a preference for ATP as a cosubstrate. J Mol Biol 347, 399–414.
    • (2005) J Mol Biol , vol.347 , pp. 399-414
    • Yde, C. W.1    Ermakova, I.2    Issinger, O. G.3    Niefind, K.4
  • 174
    • 0030866897 scopus 로고    scopus 로고
    • Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
    • Canagarajah, B. J., Khokhlatchev, A., Cobb, M. H., and Goldsmith, E. J. (1997) Activation mechanism of the MAP kinase ERK2 by dual phosphorylation. Cell 90, 859–69.
    • (1997) Cell , vol.90 , pp. 859-869
    • Canagarajah, B. J.1    Khokhlatchev, A.2    Cobb, M. H.3    Goldsmith, E. J.4
  • 175
    • 0033567706 scopus 로고    scopus 로고
    • The structure of phosphorylated p38gamma is mono-meric and reveals a conserved activation-loop conformation
    • Bellon, S., Fitzgibbon, M. J., Fox, T., Hsiao, H. M., and Wilson, K. P. (1999) The structure of phosphorylated p38gamma is mono-meric and reveals a conserved activation-loop conformation. Structure 7, 1057–65.
    • (1999) Structure , vol.7 , pp. 1057-1065
    • Bellon, S.1    Fitzgibbon, M. J.2    Fox, T.3    Hsiao, H. M.4    Wilson, K. P.5
  • 176
    • 0035875098 scopus 로고    scopus 로고
    • Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition
    • Dajani, R., Fraser, E., Roe, S. M., Young, N., Good, V., Dale, T. C., and Pearl, L. H. (2001) Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition. Cell 105, 721–32.
    • (2001) Cell , vol.105 , pp. 721-732
    • Dajani, R.1    Fraser, E.2    Roe, S. M.3    Young, N.4    Good, V.5    Dale, T. C.6    Pearl, L. H.7
  • 177
    • 17144385867 scopus 로고    scopus 로고
    • Structure and inhibition of the human cell cycle checkpoint kinase, Wee1A kinase: an atypical tyrosine kinase with a key role in CDK1 regulation
    • Squire, C. J., Dickson, J. M., Ivanovic, I., and Baker, E. N. (2005) Structure and inhibition of the human cell cycle checkpoint kinase, Wee1A kinase: an atypical tyrosine kinase with a key role in CDK1 regulation. Structure 13, 541–50.
    • (2005) Structure , vol.13 , pp. 541-550
    • Squire, C. J.1    Dickson, J. M.2    Ivanovic, I.3    Baker, E. N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.