메뉴 건너뛰기




Volumn 11, Issue , 2011, Pages

Identification and analysis of phosphorylation status of proteins in dormant terminal buds of poplar

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; POPULUS SIMONII;

EID: 81055148229     PISSN: None     EISSN: 14712229     Source Type: Journal    
DOI: 10.1186/1471-2229-11-158     Document Type: Article
Times cited : (21)

References (113)
  • 1
    • 40049101580 scopus 로고    scopus 로고
    • Gene expression during the induction, maintenance, and release of dormancy in apical buds of poplar
    • Rohde A, Ruttink T, Hostyn V, Sterck L, Van Driessche K, Boerjan W. Gene expression during the induction, maintenance, and release of dormancy in apical buds of poplar. J Exp Bot 2007, 58:4047-4060.
    • (2007) J Exp Bot , vol.58 , pp. 4047-4060
    • Rohde, A.1    Ruttink, T.2    Hostyn, V.3    Sterck, L.4    Van Driessche, K.5    Boerjan, W.6
  • 2
    • 0141680392 scopus 로고    scopus 로고
    • Induction and Release of Bud Dormancy in Woody perennials: A science Comes of Age
    • Rajeev Arora LJR, Tanino K. Induction and Release of Bud Dormancy in Woody perennials: A science Comes of Age. Hortscience 2003, 38:911-921.
    • (2003) Hortscience , vol.38 , pp. 911-921
    • Rajeev Arora, L.J.R.1    Tanino, K.2
  • 4
    • 34248221558 scopus 로고    scopus 로고
    • Plant dormancy in the perennial context
    • Rohde A, Bhalerao R. Plant dormancy in the perennial context. Trends Plant Sci 2007, 12:217-223.
    • (2007) Trends Plant Sci , vol.12 , pp. 217-223
    • Rohde, A.1    Bhalerao, R.2
  • 6
    • 0038422257 scopus 로고    scopus 로고
    • A current review on the regulation of dormancy in vegetative buds
    • Anderson J, Chao W, Horvath D, USDA A. A current review on the regulation of dormancy in vegetative buds. Weed Sci 2001, 49:581-589.
    • (2001) Weed Sci , vol.49 , pp. 581-589
    • Anderson, J.1    Chao, W.2    Horvath, D.3    USDA, A.4
  • 7
    • 34248561474 scopus 로고    scopus 로고
    • Environmental and hormonal regulation of the activity-dormancy cycle in the cambial meristem involves stage-specific modulation of transcriptional and metabolic networks
    • Druart N, Johansson A, Baba K, Schrader J, Sj din A, Bhalerao R, Resman L, Trygg J, Moritz T, Bhalerao R. Environmental and hormonal regulation of the activity-dormancy cycle in the cambial meristem involves stage-specific modulation of transcriptional and metabolic networks. Plant J 2007, 50:557-573.
    • (2007) Plant J , vol.50 , pp. 557-573
    • Druart, N.1    Johansson, A.2    Baba, K.3    Schrader, J.4    Sj din, A.5    Bhalerao, R.6    Resman, L.7    Trygg, J.8    Moritz, T.9    Bhalerao, R.10
  • 8
    • 52349106848 scopus 로고    scopus 로고
    • Dormancy in potato tuber meristems: chemically induced cessation in dormancy matches the natural process based on transcript profiles
    • Campbell M, Segear E, Beers L, Knauber D, Suttle J. Dormancy in potato tuber meristems: chemically induced cessation in dormancy matches the natural process based on transcript profiles. Funct Integr Genomics 2008, 8:317-328.
    • (2008) Funct Integr Genomics , vol.8 , pp. 317-328
    • Campbell, M.1    Segear, E.2    Beers, L.3    Knauber, D.4    Suttle, J.5
  • 11
    • 61349162295 scopus 로고    scopus 로고
    • Transcript profiling in Vitis riparia during chilling requirement fulfillment reveals coordination of gene expression patterns with optimized bud break
    • Mathiason K, He D, Grimplet J, Venkateswari J, Galbraith D, Or E, Fennell A. Transcript profiling in Vitis riparia during chilling requirement fulfillment reveals coordination of gene expression patterns with optimized bud break. Funct Integr Genomics 2009, 9:81-96.
    • (2009) Funct Integr Genomics , vol.9 , pp. 81-96
    • Mathiason, K.1    He, D.2    Grimplet, J.3    Venkateswari, J.4    Galbraith, D.5    Or, E.6    Fennell, A.7
  • 13
    • 52049110575 scopus 로고    scopus 로고
    • Advances in the Analysis of Protein Phosphorylation
    • Paradela A, Albar J. Advances in the Analysis of Protein Phosphorylation. J Proteome Res 2008, 7:1809-1818.
    • (2008) J Proteome Res , vol.7 , pp. 1809-1818
    • Paradela, A.1    Albar, J.2
  • 14
    • 77955873040 scopus 로고    scopus 로고
    • Proteomics approaches to understand protein phosphorylation in pathway modulation
    • Schulze W. Proteomics approaches to understand protein phosphorylation in pathway modulation. Curr Opin Plant Biol 2010, 13:280-287.
    • (2010) Curr Opin Plant Biol , vol.13 , pp. 280-287
    • Schulze, W.1
  • 15
    • 49549116189 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of signaling network dynamics
    • White FM. Quantitative phosphoproteomic analysis of signaling network dynamics. Curr Opin Biotechnol 2008, 19:404-409.
    • (2008) Curr Opin Biotechnol , vol.19 , pp. 404-409
    • White, F.M.1
  • 17
    • 0036605185 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome
    • Mann M, Ong S, Grønborg M, Steen H, Jensen O, Pandey A. Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome. Trends Biotechnol 2002, 20:261-268.
    • (2002) Trends Biotechnol , vol.20 , pp. 261-268
    • Mann, M.1    Ong, S.2    Grønborg, M.3    Steen, H.4    Jensen, O.5    Pandey, A.6
  • 18
    • 33746730389 scopus 로고    scopus 로고
    • Phosphoproteomic approaches to elucidate cellular signaling networks
    • Schmelzle K, White FM. Phosphoproteomic approaches to elucidate cellular signaling networks. Curr Opin Biotechnol 2006, 17:406-414.
    • (2006) Curr Opin Biotechnol , vol.17 , pp. 406-414
    • Schmelzle, K.1    White, F.M.2
  • 20
    • 34548459741 scopus 로고    scopus 로고
    • Using phosphoproteomics to reveal signalling dynamics in plants
    • de la Fuente van Bentem S, Hirt H. Using phosphoproteomics to reveal signalling dynamics in plants. Trends Plant Sci 2007, 12:404-411.
    • (2007) Trends Plant Sci , vol.12 , pp. 404-411
    • de la Fuente van Bentem, S.1    Hirt, H.2
  • 21
    • 33646271601 scopus 로고    scopus 로고
    • Phosphoproteomics in Arabidopsis: moving from empirical to predictive science
    • Peck S. Phosphoproteomics in Arabidopsis: moving from empirical to predictive science. J Exp Bot 2006, 57:1523-1527.
    • (2006) J Exp Bot , vol.57 , pp. 1523-1527
    • Peck, S.1
  • 23
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold R, Mann M. Mass spectrometry-based proteomics. Nature 2003, 422:198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 24
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • Zhou H, Watts J, Aebersold R. A systematic approach to the analysis of protein phosphorylation. Nat Biotechnol 2001, 19:375-378.
    • (2001) Nat Biotechnol , vol.19 , pp. 375-378
    • Zhou, H.1    Watts, J.2    Aebersold, R.3
  • 25
    • 24944519450 scopus 로고    scopus 로고
    • Highly Selective Enrichment of Phosphorylated Peptides from Peptide Mixtures Using Titanium Dioxide Microcolumns
    • Larsen M, Thingholm T, Jensen O, Roepstorff P, Jorgensen T. Highly Selective Enrichment of Phosphorylated Peptides from Peptide Mixtures Using Titanium Dioxide Microcolumns*. Mol Cell Proteomics 2005, 4:873-886.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 873-886
    • Larsen, M.1    Thingholm, T.2    Jensen, O.3    Roepstorff, P.4    Jorgensen, T.5
  • 26
    • 33845992932 scopus 로고    scopus 로고
    • Evaluation of the titanium dioxide approach for MS analysis of phosphopeptides
    • Klemm C, Otto S, Wolf C, Haseloff R, Beyermann M, Krause E. Evaluation of the titanium dioxide approach for MS analysis of phosphopeptides. J Mass Spectrom 2006, 41:1623-1632.
    • (2006) J Mass Spectrom , vol.41 , pp. 1623-1632
    • Klemm, C.1    Otto, S.2    Wolf, C.3    Haseloff, R.4    Beyermann, M.5    Krause, E.6
  • 27
    • 3042761083 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation by mass spectrometry
    • Areces LB, Matafora V, Bachi A. Analysis of protein phosphorylation by mass spectrometry. Eur J Mass Spectrom 2004, 10:383-392.
    • (2004) Eur J Mass Spectrom , vol.10 , pp. 383-392
    • Areces, L.B.1    Matafora, V.2    Bachi, A.3
  • 28
    • 34248640261 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides using titanium dioxide
    • Thingholm TE, Jorgensen TJD, Jensen ON, Larsen MR. Highly selective enrichment of phosphorylated peptides using titanium dioxide. Nat Protoc 2006, 1:1929-1935.
    • (2006) Nat Protoc , vol.1 , pp. 1929-1935
    • Thingholm, T.E.1    Jorgensen, T.J.D.2    Jensen, O.N.3    Larsen, M.R.4
  • 29
    • 11444263845 scopus 로고    scopus 로고
    • Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry
    • Nühse T, Stensballe A, Jensen O, Peck S. Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry. Mol Cell Proteomics 2003, 2:1234-1243.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 1234-1243
    • Nühse, T.1    Stensballe, A.2    Jensen, O.3    Peck, S.4
  • 30
    • 4544291080 scopus 로고    scopus 로고
    • Phosphoproteomics of the Arabidopsis Plasma Membrane and a New Phosphorylation Site Database
    • Nühse T, Stensballe A, Jensen O, Peck S. Phosphoproteomics of the Arabidopsis Plasma Membrane and a New Phosphorylation Site Database. Plant Cell 2004, 16:2394-2405.
    • (2004) Plant Cell , vol.16 , pp. 2394-2405
    • Nühse, T.1    Stensballe, A.2    Jensen, O.3    Peck, S.4
  • 31
    • 34548128405 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of plasma membrane proteins reveals regulatory mechanisms of plant innate immune responses
    • Nühse T, Bottrill A, Jones A, Peck S. Quantitative phosphoproteomic analysis of plasma membrane proteins reveals regulatory mechanisms of plant innate immune responses. Plant J 2007, 51:931-940.
    • (2007) Plant J , vol.51 , pp. 931-940
    • Nühse, T.1    Bottrill, A.2    Jones, A.3    Peck, S.4
  • 34
    • 63049130982 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of ethylene-regulated protein phosphorylation in etiolated seedlings of Arabidopsis mutant ein2 using two-dimensional separations coupled with a hybrid quadrupole time-of-flight mass spectrometer
    • Li H, Wong WS, Zhu L, Guo HW, Ecker J, Li N. Phosphoproteomic analysis of ethylene-regulated protein phosphorylation in etiolated seedlings of Arabidopsis mutant ein2 using two-dimensional separations coupled with a hybrid quadrupole time-of-flight mass spectrometer. Proteomics 2009, 9:1646-1661.
    • (2009) Proteomics , vol.9 , pp. 1646-1661
    • Li, H.1    Wong, W.S.2    Zhu, L.3    Guo, H.W.4    Ecker, J.5    Li, N.6
  • 36
    • 39749142082 scopus 로고    scopus 로고
    • Analysis of the Arabidopsis cytosolic ribosome proteome provides detailed insights into its components and their post-translational modification
    • Carroll AJ, Heazlewood JL, Ito J, Millar AH. Analysis of the Arabidopsis cytosolic ribosome proteome provides detailed insights into its components and their post-translational modification. Mol Cell Proteomics 2008, 7:347-369.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 347-369
    • Carroll, A.J.1    Heazlewood, J.L.2    Ito, J.3    Millar, A.H.4
  • 37
    • 35648996970 scopus 로고    scopus 로고
    • Temporal analysis of sucrose-induced phosphorylation changes in plasma membrane proteins of Arabidopsis
    • Niittyla T, Fuglsang AT, Palmgren MG, Frommer WB, Schulze WX. Temporal analysis of sucrose-induced phosphorylation changes in plasma membrane proteins of Arabidopsis. Mol Cell Proteomics 2007, 6:1711-1726.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1711-1726
    • Niittyla, T.1    Fuglsang, A.T.2    Palmgren, M.G.3    Frommer, W.B.4    Schulze, W.X.5
  • 38
    • 84890499160 scopus 로고    scopus 로고
    • Combining metal oxide affinity chromatography (MOAC) and selective mass spectrometry for robust identification of in vivo protein phosphorylation sites
    • Wolschin F, Weckwerth W. Combining metal oxide affinity chromatography (MOAC) and selective mass spectrometry for robust identification of in vivo protein phosphorylation sites. Plant Methods 2005, 1:1-9.
    • (2005) Plant Methods , vol.1 , pp. 1-9
    • Wolschin, F.1    Weckwerth, W.2
  • 41
    • 33751401609 scopus 로고    scopus 로고
    • Large scale identification and quantitative profiling of phosphoproteins expressed during seed filling in oilseed rape
    • Agrawal G, Thelen J. Large scale identification and quantitative profiling of phosphoproteins expressed during seed filling in oilseed rape. Mol Cell Proteomics 2006, 5:2044-2059.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 2044-2059
    • Agrawal, G.1    Thelen, J.2
  • 42
    • 52649124306 scopus 로고    scopus 로고
    • A proteomic and phosphoproteomic analysis of Oryza sativa plasma membrane and vacuolar membrane
    • Whiteman SA, Nuhse TS, Ashford DA, Sanders D, Maathuis FJ. A proteomic and phosphoproteomic analysis of Oryza sativa plasma membrane and vacuolar membrane. Plant J 2008, 56:146-156.
    • (2008) Plant J , vol.56 , pp. 146-156
    • Whiteman, S.A.1    Nuhse, T.S.2    Ashford, D.A.3    Sanders, D.4    Maathuis, F.J.5
  • 43
    • 60349118495 scopus 로고    scopus 로고
    • In vivo phosphorylation sites of barley tonoplast proteins identified by a phosphoproteomic approach
    • Endler A, Reiland S, Gerrits B, Schmidt UG, Baginsky S, Martinoia E. In vivo phosphorylation sites of barley tonoplast proteins identified by a phosphoproteomic approach. Proteomics 2009, 9:310-321.
    • (2009) Proteomics , vol.9 , pp. 310-321
    • Endler, A.1    Reiland, S.2    Gerrits, B.3    Schmidt, U.G.4    Baginsky, S.5    Martinoia, E.6
  • 44
    • 55849083914 scopus 로고    scopus 로고
    • A shotgun phosphoproteomics analysis of embryos in germinated maize seeds
    • Lu T, Meng L, Yang C, Liu G, Liu G, Ma W, Wang B. A shotgun phosphoproteomics analysis of embryos in germinated maize seeds. Planta 2008, 228:1029-1041.
    • (2008) Planta , vol.228 , pp. 1029-1041
    • Lu, T.1    Meng, L.2    Yang, C.3    Liu, G.4    Liu, G.5    Ma, W.6    Wang, B.7
  • 45
    • 76049094327 scopus 로고    scopus 로고
    • Phosphoproteomic identification and phylogenetic analysis of ribosomal P-proteins in Populus dormant terminal buds
    • Liu C-C, Lu T-C, Li H-H, Wang H-X, Liu G-F, Ma L, Yang C-P, Wang B-C. Phosphoproteomic identification and phylogenetic analysis of ribosomal P-proteins in Populus dormant terminal buds. Planta 2010, 231:571-581.
    • (2010) Planta , vol.231 , pp. 571-581
    • Liu, C.-.C.1    Lu, T.-.C.2    Li, H.-.H.3    Wang, H.-.X.4    Liu, G.-.F.5    Ma, L.6    Yang, C.-.P.7    Wang, B.-.C.8
  • 46
    • 0029310678 scopus 로고
    • Plant protein kinase families and signal transduction
    • Stone J, Walker J. Plant protein kinase families and signal transduction. Plant Physiol 1995, 108:451-457.
    • (1995) Plant Physiol , vol.108 , pp. 451-457
    • Stone, J.1    Walker, J.2
  • 48
    • 71249130462 scopus 로고    scopus 로고
    • The chloroplast kinase network: new insights from large-scale phosphoproteome profiling
    • Baginsky S, Gruissem W. The chloroplast kinase network: new insights from large-scale phosphoproteome profiling. Mol Plant 2009, 2:1141-1153.
    • (2009) Mol Plant , vol.2 , pp. 1141-1153
    • Baginsky, S.1    Gruissem, W.2
  • 51
    • 59349086947 scopus 로고    scopus 로고
    • Protein tyrosine phosphorylation in plants: more abundant than expected?
    • van Bentem SD, Hirt H. Protein tyrosine phosphorylation in plants: more abundant than expected?. Trends Plant Sci 2009, 14:71-76.
    • (2009) Trends Plant Sci , vol.14 , pp. 71-76
    • van Bentem, S.D.1    Hirt, H.2
  • 52
    • 49849096720 scopus 로고    scopus 로고
    • Development of phosphopeptide enrichment techniques for phosphoproteome analysis
    • Han G, Ye M, Zou H. Development of phosphopeptide enrichment techniques for phosphoproteome analysis. Analyst 2008, 133:1128-1138.
    • (2008) Analyst , vol.133 , pp. 1128-1138
    • Han, G.1    Ye, M.2    Zou, H.3
  • 53
    • 73849110528 scopus 로고    scopus 로고
    • Techniques for phosphopeptide enrichment prior to analysis by mass spectrometry
    • Dunn JD, Reid GE, Bruening ML. Techniques for phosphopeptide enrichment prior to analysis by mass spectrometry. Mass Spectrom Rev 2010, 29:29-54.
    • (2010) Mass Spectrom Rev , vol.29 , pp. 29-54
    • Dunn, J.D.1    Reid, G.E.2    Bruening, M.L.3
  • 57
    • 24644503098 scopus 로고    scopus 로고
    • Blast2GO: a universal tool for annotation, visualization and analysis in functional genomics research
    • Conesa A, Gotz S, Garcia-Gomez JM, Terol J, Talon M, Robles M. Blast2GO: a universal tool for annotation, visualization and analysis in functional genomics research. Bioinformatics 2005, 21:3674-3676.
    • (2005) Bioinformatics , vol.21 , pp. 3674-3676
    • Conesa, A.1    Gotz, S.2    Garcia-Gomez, J.M.3    Terol, J.4    Talon, M.5    Robles, M.6
  • 58
    • 27944499451 scopus 로고    scopus 로고
    • An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets
    • Schwartz D, Gygi S. An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets. Nat Biotechnol 2005, 23:1391-1398.
    • (2005) Nat Biotechnol , vol.23 , pp. 1391-1398
    • Schwartz, D.1    Gygi, S.2
  • 59
    • 0035957331 scopus 로고    scopus 로고
    • 14-3-3 protein is a regulator of the mitochondrial and chloroplast ATP synthase
    • Bunney T, van Walraven H, de Boer A. 14-3-3 protein is a regulator of the mitochondrial and chloroplast ATP synthase. Proc Natl Acad Sci 2001, 98:4249-4254.
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 4249-4254
    • Bunney, T.1    van Walraven, H.2    de Boer, A.3
  • 61
    • 77950948851 scopus 로고    scopus 로고
    • Identification of genes associated with growth cessation and bud dormancy entrance using a dormancy-incapable tree mutant
    • Jimenez S, Li Z, Reighard G, Bielenberg D. Identification of genes associated with growth cessation and bud dormancy entrance using a dormancy-incapable tree mutant. BMC Plant Biol 2010, 10:25.
    • (2010) BMC Plant Biol , vol.10 , pp. 25
    • Jimenez, S.1    Li, Z.2    Reighard, G.3    Bielenberg, D.4
  • 62
    • 42049096330 scopus 로고    scopus 로고
    • Transcriptional profiles of the annual growth cycle in Populus deltoides
    • Park S, Keathley DE, Han KH. Transcriptional profiles of the annual growth cycle in Populus deltoides. Tree Physiol 2008, 28:321-329.
    • (2008) Tree Physiol , vol.28 , pp. 321-329
    • Park, S.1    Keathley, D.E.2    Han, K.H.3
  • 63
    • 33745210178 scopus 로고    scopus 로고
    • Subtractive cDNA libraries identify differentially expressed genes in dormant and growing buds of leafy spurge (Euphorbia esula)
    • Jia Y, Anderson JV, Horvath DP, Gu YQ, Lym RG, Chao WS. Subtractive cDNA libraries identify differentially expressed genes in dormant and growing buds of leafy spurge (Euphorbia esula). Plant Mol Biol 2006, 61:329-344.
    • (2006) Plant Mol Biol , vol.61 , pp. 329-344
    • Jia, Y.1    Anderson, J.V.2    Horvath, D.P.3    Gu, Y.Q.4    Lym, R.G.5    Chao, W.S.6
  • 64
    • 33746873661 scopus 로고    scopus 로고
    • Analysis of gene expression during bud burst initiation in Norway spruce via ESTs from subtracted cDNA libraries
    • Yakovlev IA, Fossdal CG, Junttila O, Skr ppa T. Analysis of gene expression during bud burst initiation in Norway spruce via ESTs from subtracted cDNA libraries. Tree Genet Genomes 2006, 2:39-52.
    • (2006) Tree Genet Genomes , vol.2 , pp. 39-52
    • Yakovlev, I.A.1    Fossdal, C.G.2    Junttila, O.3    Skr ppa, T.4
  • 65
    • 33845309449 scopus 로고    scopus 로고
    • Transcriptome analysis of leafy spurge (Euphorbia esula) crown buds during shifts in well-defined phases of dormancy
    • Horvath DP, Anderson JV, Soto-Suarez M, Chao WS. Transcriptome analysis of leafy spurge (Euphorbia esula) crown buds during shifts in well-defined phases of dormancy. Weed Sci 2006, 821-827.
    • (2006) Weed Sci , pp. 821-827
    • Horvath, D.P.1    Anderson, J.V.2    Soto-Suarez, M.3    Chao, W.S.4
  • 66
    • 57949085178 scopus 로고    scopus 로고
    • Transcriptome analysis identifies novel responses and potential regulatory genes involved in seasonal dormancy transitions of leafy spurge (Euphorbia esula L.)
    • Horvath D, Chao W, Suttle J, Thimmapuram J, Anderson J. Transcriptome analysis identifies novel responses and potential regulatory genes involved in seasonal dormancy transitions of leafy spurge (Euphorbia esula L.). BMC Genomics 2008, 9:536.
    • (2008) BMC Genomics , vol.9 , pp. 536
    • Horvath, D.1    Chao, W.2    Suttle, J.3    Thimmapuram, J.4    Anderson, J.5
  • 69
    • 0028233382 scopus 로고
    • A protein phosphatase 2C involved in ABA signal transduction in Arabidopsis thaliana
    • Meyer K, Leube MP, Grill E. A protein phosphatase 2C involved in ABA signal transduction in Arabidopsis thaliana. Science 1994, 264:1452-1455.
    • (1994) Science , vol.264 , pp. 1452-1455
    • Meyer, K.1    Leube, M.P.2    Grill, E.3
  • 71
    • 29544438751 scopus 로고    scopus 로고
    • Leucine-rich repeat receptor-like kinase1 is a key membrane-bound regulator of abscisic acid early signaling in Arabidopsis
    • Osakabe Y, Maruyama K, Seki M, Satou M, Shinozaki K, Yamaguchi-Shinozaki K. Leucine-rich repeat receptor-like kinase1 is a key membrane-bound regulator of abscisic acid early signaling in Arabidopsis. Plant Cell 2005, 17:1105-1119.
    • (2005) Plant Cell , vol.17 , pp. 1105-1119
    • Osakabe, Y.1    Maruyama, K.2    Seki, M.3    Satou, M.4    Shinozaki, K.5    Yamaguchi-Shinozaki, K.6
  • 72
    • 0031131635 scopus 로고    scopus 로고
    • The Arabidopsis ABSCISIC ACID-INSENSITIVE2 (ABI2) and ABI1 genes encode homologous protein phosphatases 2C involved in abscisic acid signal transduction
    • Leung J, Merlot S, Giraudat J. The Arabidopsis ABSCISIC ACID-INSENSITIVE2 (ABI2) and ABI1 genes encode homologous protein phosphatases 2C involved in abscisic acid signal transduction. Plant Cell 1997, 9:759-771.
    • (1997) Plant Cell , vol.9 , pp. 759-771
    • Leung, J.1    Merlot, S.2    Giraudat, J.3
  • 73
    • 67849103829 scopus 로고    scopus 로고
    • Calcium and calmodulin-mediated regulation of gene expression in plants
    • Kim MC, Chung WS, Yun DJ, Cho MJ. Calcium and calmodulin-mediated regulation of gene expression in plants. Mol Plant 2009, 2:13-21.
    • (2009) Mol Plant , vol.2 , pp. 13-21
    • Kim, M.C.1    Chung, W.S.2    Yun, D.J.3    Cho, M.J.4
  • 74
    • 42149156023 scopus 로고    scopus 로고
    • The development of a genetic linkage map of blackcurrant (Ribes nigrum L.) and the identification of regions associated with key fruit quality and agronomic traits
    • Brennan R, Jorgensen L, Hackett C, Woodhead M, Gordon S, Russell J. The development of a genetic linkage map of blackcurrant (Ribes nigrum L.) and the identification of regions associated with key fruit quality and agronomic traits. Euphytica 2008, 161:19-34.
    • (2008) Euphytica , vol.161 , pp. 19-34
    • Brennan, R.1    Jorgensen, L.2    Hackett, C.3    Woodhead, M.4    Gordon, S.5    Russell, J.6
  • 75
    • 54049100716 scopus 로고    scopus 로고
    • Genes associated with the release of dormant buds in tree peonies (Paeonia suffruticosa)
    • Huang X, Xue T, Dai S, Gai S, Zheng C, Zheng G. Genes associated with the release of dormant buds in tree peonies (Paeonia suffruticosa). Acta Physiol Plant 2008, 30:797-806.
    • (2008) Acta Physiol Plant , vol.30 , pp. 797-806
    • Huang, X.1    Xue, T.2    Dai, S.3    Gai, S.4    Zheng, C.5    Zheng, G.6
  • 76
    • 33745186397 scopus 로고    scopus 로고
    • Seasonal shifts in dormancy status, carbohydrate metabolism, and related gene expression in crown buds of leafy spurge
    • Anderson JV, Gesch RW, Jia Y, Chao WS, Horvath DP. Seasonal shifts in dormancy status, carbohydrate metabolism, and related gene expression in crown buds of leafy spurge. Plant Cell Environ 2005, 28:1567-1578.
    • (2005) Plant Cell Environ , vol.28 , pp. 1567-1578
    • Anderson, J.V.1    Gesch, R.W.2    Jia, Y.3    Chao, W.S.4    Horvath, D.P.5
  • 77
    • 77950465225 scopus 로고    scopus 로고
    • Differential floral development and gene expression in grapevines during long and short photoperiods suggests a role for floral genes in dormancy transitioning
    • Sreekantan L, Mathiason K, Grimplet J, Schlauch K, Dickerson JA, Fennell AY. Differential floral development and gene expression in grapevines during long and short photoperiods suggests a role for floral genes in dormancy transitioning. Plant Mol Biol 2010, 73:191-205.
    • (2010) Plant Mol Biol , vol.73 , pp. 191-205
    • Sreekantan, L.1    Mathiason, K.2    Grimplet, J.3    Schlauch, K.4    Dickerson, J.A.5    Fennell, A.Y.6
  • 78
    • 41149160719 scopus 로고    scopus 로고
    • Resetting of FLOWERING LOCUS C expression after epigenetic repression by vernalization
    • Sheldon C, Hills M, Lister C, Dean C, Dennis E, Peacock W. Resetting of FLOWERING LOCUS C expression after epigenetic repression by vernalization. Proc Natl Acad Sci 2008, 105:2214-2219.
    • (2008) Proc Natl Acad Sci , vol.105 , pp. 2214-2219
    • Sheldon, C.1    Hills, M.2    Lister, C.3    Dean, C.4    Dennis, E.5    Peacock, W.6
  • 79
    • 0036733292 scopus 로고    scopus 로고
    • The VERNALIZATION INDEPENDENCE 4 gene encodes a novel regulator of FLOWERING LOCUS C
    • Zhang H, Van Nocker S. The VERNALIZATION INDEPENDENCE 4 gene encodes a novel regulator of FLOWERING LOCUS C. Plant J 2002, 31:663-673.
    • (2002) Plant J , vol.31 , pp. 663-673
    • Zhang, H.1    Van Nocker, S.2
  • 80
    • 33646837086 scopus 로고    scopus 로고
    • The Arabidopsis-mei2-like genes play a role in meiosis and vegetative growth in Arabidopsis
    • Kaur J, Sebastian J, Siddiqi I. The Arabidopsis-mei2-like genes play a role in meiosis and vegetative growth in Arabidopsis. Plant Cell 2006, 18:545-559.
    • (2006) Plant Cell , vol.18 , pp. 545-559
    • Kaur, J.1    Sebastian, J.2    Siddiqi, I.3
  • 81
    • 0030498675 scopus 로고    scopus 로고
    • Dehydrins: emergence of a biochemical role of a family of plant dehydration proteins
    • Close T. Dehydrins: emergence of a biochemical role of a family of plant dehydration proteins. Physiol Plant 1996, 97:795-803.
    • (1996) Physiol Plant , vol.97 , pp. 795-803
    • Close, T.1
  • 83
    • 34247573081 scopus 로고    scopus 로고
    • The role of dehydrins in plant response to cold
    • Kosova K, Vitamvas P, Prásil I. The role of dehydrins in plant response to cold. Biol Plant 2007, 51:601-617.
    • (2007) Biol Plant , vol.51 , pp. 601-617
    • Kosova, K.1    Vitamvas, P.2    Prásil, I.3
  • 84
    • 34548460796 scopus 로고    scopus 로고
    • The continuing conundrum of the LEA proteins
    • Tunnacliffe A, Wise M. The continuing conundrum of the LEA proteins. Naturwissenschaften 2007, 94:791-812.
    • (2007) Naturwissenschaften , vol.94 , pp. 791-812
    • Tunnacliffe, A.1    Wise, M.2
  • 85
    • 33847140438 scopus 로고    scopus 로고
    • Plant dehydrins-tissue location, structure and function
    • Rorat T. Plant dehydrins-tissue location, structure and function. Cell Mol Biol Lett 2006, 11:536-556.
    • (2006) Cell Mol Biol Lett , vol.11 , pp. 536-556
    • Rorat, T.1
  • 86
    • 0031822739 scopus 로고    scopus 로고
    • Onset of freezing tolerance in birch (Betula pubescens Ehrh.) involves LEA proteins and osmoregulation and is impaired in an ABA-deficient genotype
    • Rinne P, Welling A, Kaikuranta P. Onset of freezing tolerance in birch (Betula pubescens Ehrh.) involves LEA proteins and osmoregulation and is impaired in an ABA-deficient genotype. Plant Cell Environ 1998, 21:601-611.
    • (1998) Plant Cell Environ , vol.21 , pp. 601-611
    • Rinne, P.1    Welling, A.2    Kaikuranta, P.3
  • 87
    • 0032701931 scopus 로고    scopus 로고
    • Dehydrins in cold-acclimated apices of birch (Betula pubescens Ehrh.): production, localization and potential role in rescuing enzyme function during dehydration
    • Rinne PLH, Kaikuranta PLM, van der Plas LHW, van der Schoot C. Dehydrins in cold-acclimated apices of birch (Betula pubescens Ehrh.): production, localization and potential role in rescuing enzyme function during dehydration. Planta 1999, 209:377-388.
    • (1999) Planta , vol.209 , pp. 377-388
    • Rinne, P.L.H.1    Kaikuranta, P.L.M.2    van der Plas, L.H.W.3    van der Schoot, C.4
  • 88
    • 16644378940 scopus 로고    scopus 로고
    • Short-day potentiation of low temperature-induced gene expression of a C-repeat-binding factor-controlled gene during cold acclimation in silver birch
    • Puhakainen T, Li C, Boije-Malm M, Kangasj rvi J, Heino P, Palva ET. Short-day potentiation of low temperature-induced gene expression of a C-repeat-binding factor-controlled gene during cold acclimation in silver birch. Plant Physiol 2004, 136:4299-4307.
    • (2004) Plant Physiol , vol.136 , pp. 4299-4307
    • Puhakainen, T.1    Li, C.2    Boije-Malm, M.3    Kangasj rvi, J.4    Heino, P.5    Palva, E.T.6
  • 90
    • 0032033115 scopus 로고    scopus 로고
    • Phosphorylation mediates the nuclear targeting of the maize Rab17 protein
    • Jensen AB, Goday A, Figueras M, Jessop AC, Pages M. Phosphorylation mediates the nuclear targeting of the maize Rab17 protein. Plant J 1998, 13:691-697.
    • (1998) Plant J , vol.13 , pp. 691-697
    • Jensen, A.B.1    Goday, A.2    Figueras, M.3    Jessop, A.C.4    Pages, M.5
  • 91
    • 3042709455 scopus 로고    scopus 로고
    • Protein kinase CK2 modulates developmental functions of the abscisic acid responsive protein Rab17 from maize
    • Riera M, Figueras M, Lopez C, Goday A, Pages M. Protein kinase CK2 modulates developmental functions of the abscisic acid responsive protein Rab17 from maize. Proc Natl Acad Sci 2004, 101:9879-9884.
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 9879-9884
    • Riera, M.1    Figueras, M.2    Lopez, C.3    Goday, A.4    Pages, M.5
  • 92
    • 2442445139 scopus 로고    scopus 로고
    • Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response
    • Wang W, Vinocur B, Shoseyov O, Altman A. Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response. Trends Plant Sci 2004, 9:244-252.
    • (2004) Trends Plant Sci , vol.9 , pp. 244-252
    • Wang, W.1    Vinocur, B.2    Shoseyov, O.3    Altman, A.4
  • 93
    • 80052005396 scopus 로고    scopus 로고
    • Transcriptome analysis of chestnut (Castanea sativa) tree buds suggests a putative role for epigenetic control of bud dormancy
    • Santamaria ME, Rodriguez R, Ca al MJ, Toorop PE. Transcriptome analysis of chestnut (Castanea sativa) tree buds suggests a putative role for epigenetic control of bud dormancy. Ann Bot 2011, 108:485-498.
    • (2011) Ann Bot , vol.108 , pp. 485-498
    • Santamaria, M.E.1    Rodriguez, R.2    Ca al, M.J.3    Toorop, P.E.4
  • 94
    • 0030883042 scopus 로고    scopus 로고
    • Effects of near-lethal heat stress on bud break, heat-shock proteins and ubiquitin in dormant poplar (Populus nigra Charkowiensis × P. nigra incrassata)
    • Wisniewski M, Sauter J, Fuchigami L, Stepien V. Effects of near-lethal heat stress on bud break, heat-shock proteins and ubiquitin in dormant poplar (Populus nigra Charkowiensis × P. nigra incrassata). Tree Physiol 1997, 17:453-460.
    • (1997) Tree Physiol , vol.17 , pp. 453-460
    • Wisniewski, M.1    Sauter, J.2    Fuchigami, L.3    Stepien, V.4
  • 96
    • 46049100082 scopus 로고    scopus 로고
    • Function, structure and regulation of the vacuolar (H+)-ATPases
    • Jefferies KC, Cipriano DJ, Forgac M. Function, structure and regulation of the vacuolar (H+)-ATPases. Arch Biochem Biophys 2008, 476:33-42.
    • (2008) Arch Biochem Biophys , vol.476 , pp. 33-42
    • Jefferies, K.C.1    Cipriano, D.J.2    Forgac, M.3
  • 97
    • 62149096105 scopus 로고    scopus 로고
    • The plant plasma membrane proton pump ATPase: a highly regulated P-type ATPase with multiple physiological roles
    • Duby G, Boutry M. The plant plasma membrane proton pump ATPase: a highly regulated P-type ATPase with multiple physiological roles. Pflugers Arch 2009, 457:645-655.
    • (2009) Pflugers Arch , vol.457 , pp. 645-655
    • Duby, G.1    Boutry, M.2
  • 98
    • 0035781086 scopus 로고    scopus 로고
    • Plant plasma membrane H+-ATPases: powerhouses for nutrient uptake
    • Palmgren MG. Plant plasma membrane H+-ATPases: powerhouses for nutrient uptake. Annu Rev Plant Biol 2001, 52:817-845.
    • (2001) Annu Rev Plant Biol , vol.52 , pp. 817-845
    • Palmgren, M.G.1
  • 101
    • 77950505008 scopus 로고    scopus 로고
    • Proteomic approach to analyze dormancy breaking of tree seeds
    • Paw owski TA. Proteomic approach to analyze dormancy breaking of tree seeds. Plant Mol Biol 2010, 73:15-25.
    • (2010) Plant Mol Biol , vol.73 , pp. 15-25
    • Paw owski, T.A.1
  • 102
    • 55549092088 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 5A is involved in pathogen-induced cell death and development of disease symptoms in Arabidopsis
    • Hopkins M, Lampi Y, Wang T, Liu Z, Thompson J. Eukaryotic translation initiation factor 5A is involved in pathogen-induced cell death and development of disease symptoms in Arabidopsis. Plant Physiol 2008, 148:479-489.
    • (2008) Plant Physiol , vol.148 , pp. 479-489
    • Hopkins, M.1    Lampi, Y.2    Wang, T.3    Liu, Z.4    Thompson, J.5
  • 103
    • 34447130270 scopus 로고    scopus 로고
    • Functional characterization of the Arabidopsis eukaryotic translation initiation factor 5A-2 that plays a crucial role in plant growth and development by regulating cell division, cell growth, and cell death
    • Feng H, Chen Q, Feng J, Zhang J, Yang X, Zuo J. Functional characterization of the Arabidopsis eukaryotic translation initiation factor 5A-2 that plays a crucial role in plant growth and development by regulating cell division, cell growth, and cell death. Plant Physiol 2007, 144:1531-1545.
    • (2007) Plant Physiol , vol.144 , pp. 1531-1545
    • Feng, H.1    Chen, Q.2    Feng, J.3    Zhang, J.4    Yang, X.5    Zuo, J.6
  • 105
    • 77949712407 scopus 로고    scopus 로고
    • A Structural Domain Mediates Attachment of Ethanolamine Phosphoglycerol to Eukaryotic Elongation Factor 1A in Trypanosoma brucei
    • Greganova E, Heller M, Bütikofer P. A Structural Domain Mediates Attachment of Ethanolamine Phosphoglycerol to Eukaryotic Elongation Factor 1A in Trypanosoma brucei. PLoS ONE 2010, 5:e9486.
    • (2010) PLoS ONE , vol.5
    • Greganova, E.1    Heller, M.2    Bütikofer, P.3
  • 106
    • 26944487335 scopus 로고    scopus 로고
    • Translation elongation factor 1A is essential for regulation of the actin cytoskeleton and cell morphology
    • Gross S, Kinzy T. Translation elongation factor 1A is essential for regulation of the actin cytoskeleton and cell morphology. Nat Struct Mol Biol 2005, 12:772-778.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 772-778
    • Gross, S.1    Kinzy, T.2
  • 107
    • 0028892669 scopus 로고    scopus 로고
    • Phosphorylation of elongation factor 1 (EF-1) by protein kinase C stimulates GDP/GTP-exchange activity
    • Peters H, Chang Y, Traugh J. Phosphorylation of elongation factor 1 (EF-1) by protein kinase C stimulates GDP/GTP-exchange activity. Eur J Biochem 2004, 234:550-556.
    • (2004) Eur J Biochem , vol.234 , pp. 550-556
    • Peters, H.1    Chang, Y.2    Traugh, J.3
  • 108
    • 33645779695 scopus 로고    scopus 로고
    • Novel protein phosphorylation site identification in spinach stroma membranes by titanium dioxide microcolumns and tandem mass spectrometry
    • Rinalducci S, Larsen M, Mohammed S, Zolla L. Novel protein phosphorylation site identification in spinach stroma membranes by titanium dioxide microcolumns and tandem mass spectrometry. J Proteome Res 2006, 5:973-982.
    • (2006) J Proteome Res , vol.5 , pp. 973-982
    • Rinalducci, S.1    Larsen, M.2    Mohammed, S.3    Zolla, L.4
  • 109
    • 33646945632 scopus 로고    scopus 로고
    • Abundantly and rarely expressed Lhc protein genes exhibit distinct regulation patterns in plants
    • Klimmek F, Sjodin A, Noutsos C, Leister D, Jansson S. Abundantly and rarely expressed Lhc protein genes exhibit distinct regulation patterns in plants. Plant Physiol 2006, 140:793-804.
    • (2006) Plant Physiol , vol.140 , pp. 793-804
    • Klimmek, F.1    Sjodin, A.2    Noutsos, C.3    Leister, D.4    Jansson, S.5
  • 110
    • 1842546738 scopus 로고    scopus 로고
    • Identification of three previously unknown in vivo protein phosphorylation sites in thylakoid membranes of Arabidopsis thaliana
    • Hansson M, Vener A. Identification of three previously unknown in vivo protein phosphorylation sites in thylakoid membranes of Arabidopsis thaliana. Mol Cell Proteomics 2003, 2:550-559.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 550-559
    • Hansson, M.1    Vener, A.2
  • 112
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn MP, Wolters D, Yates JR. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol 2001, 19:242-247.
    • (2001) Nat Biotechnol , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.