메뉴 건너뛰기




Volumn 13, Issue 7, 2014, Pages 3397-3409

A kinase-phosphatase signaling module with Bsk8 and Bsl2 involved in regulation of sucrose-phosphate synthase

Author keywords

Arabidopsis; BSK8 kinase; BSL2 phosphatase; phosphoproteomics; sucrose synthase

Indexed keywords

BRASSINOSTEROID; BRASSINOSTEROID SIGNALING KINASE 8; PHOSPHATASE; PROTEIN KINASE; SUCROSE; SUCROSE PHOSPHATE SYNTHASE; UNCLASSIFIED DRUG; ARABIDOPSIS PROTEIN; BSK8 PROTEIN, ARABIDOPSIS; BSL2 PROTEIN, ARABIDOPSIS; GLUCOSYLTRANSFERASE; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN SERINE THREONINE KINASE; SUCROSE-PHOSPHATE SYNTHASE;

EID: 84903690777     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr5003164     Document Type: Article
Times cited : (32)

References (67)
  • 1
    • 0036099264 scopus 로고    scopus 로고
    • Sucrose metabolism and cellulose biosynthesis in sunflower hypocotyls
    • Kutschera, U.; Heiderich, A. Sucrose metabolism and cellulose biosynthesis in sunflower hypocotyls Physiol. Plant. 2002, 114, 372-379
    • (2002) Physiol. Plant. , vol.114 , pp. 372-379
    • Kutschera, U.1    Heiderich, A.2
  • 2
    • 77955913904 scopus 로고    scopus 로고
    • Sugar input, metabolism, and signaling mediated by invertase: Roles in development, yield potential, and response to drought and heat
    • Ruan, Y. L.; Jin, Y.; Yang, Y. J.; Li, G. J.; Boyer, J. S. Sugar input, metabolism, and signaling mediated by invertase: roles in development, yield potential, and response to drought and heat Mol. Plant 2010, 3, 942-955
    • (2010) Mol. Plant , vol.3 , pp. 942-955
    • Ruan, Y.L.1    Jin, Y.2    Yang, Y.J.3    Li, G.J.4    Boyer, J.S.5
  • 3
    • 4444288688 scopus 로고    scopus 로고
    • Transcriptome profiling of the response of Arabidopsis suspension culture cells to Suc starvation
    • Contento, A. L.; Kim, S. J.; Bassham, D. C. Transcriptome profiling of the response of Arabidopsis suspension culture cells to Suc starvation Plant Physiol. 2004, 135, 2330-2347
    • (2004) Plant Physiol. , vol.135 , pp. 2330-2347
    • Contento, A.L.1    Kim, S.J.2    Bassham, D.C.3
  • 4
    • 14644392198 scopus 로고    scopus 로고
    • Sucrose-induced translational repression of plant bZIP-type transcription factors
    • Wiese, A.; Elzinga, N.; Wobbes, B.; Smeekens, S. Sucrose-induced translational repression of plant bZIP-type transcription factors Biochem. Soc. Trans. 2005, 33, 272-275
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 272-275
    • Wiese, A.1    Elzinga, N.2    Wobbes, B.3    Smeekens, S.4
  • 5
    • 33745530598 scopus 로고    scopus 로고
    • Sugar-induced increases in trehalose 6-phosphate are correlated with redox activation of ADPglucose pyrophosphorylase and higher rates of starch synthesis in Arabidopsis thaliana
    • Lunn, J. E.; Feil, R.; Hendriks, J. H.; Gibon, Y.; Morcuende, R.; Osuna, D.; Scheible, W. R.; Carillo, P.; Hajirezaei, M. R.; Stitt, M. Sugar-induced increases in trehalose 6-phosphate are correlated with redox activation of ADPglucose pyrophosphorylase and higher rates of starch synthesis in Arabidopsis thaliana Biochem. J. 2006, 397, 139-148
    • (2006) Biochem. J. , vol.397 , pp. 139-148
    • Lunn, J.E.1    Feil, R.2    Hendriks, J.H.3    Gibon, Y.4    Morcuende, R.5    Osuna, D.6    Scheible, W.R.7    Carillo, P.8    Hajirezaei, M.R.9    Stitt, M.10
  • 6
    • 0026541075 scopus 로고
    • Sucrose mimics the light induction of Arabidopsis nitrate reductase gene transcription
    • Cheng, C.-L.; Acedo, G. N.; Christinsin, M.; Conkling, M. A. Sucrose mimics the light induction of Arabidopsis nitrate reductase gene transcription Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 1861-1864
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 1861-1864
    • Cheng, C.-L.1    Acedo, G.N.2    Christinsin, M.3    Conkling, M.A.4
  • 8
    • 0032516025 scopus 로고    scopus 로고
    • Sucrose is a signal molecule in assimilate partitioning
    • Chiou, T. J.; Bush, D. R. Sucrose is a signal molecule in assimilate partitioning Proc. Natl. Acad. Sci. U.S.A. 1998, 95, 4784-4788
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 4784-4788
    • Chiou, T.J.1    Bush, D.R.2
  • 9
    • 0032126963 scopus 로고    scopus 로고
    • Sucrose specific signalling represses translation of the Arabidopsis ATB2 bZIP transcription factor gene
    • Rook, F.; Gerrits, N.; Kortsett, A.; van Kampe, M.; Borrias, M. Sucrose specific signalling represses translation of the Arabidopsis ATB2 bZIP transcription factor gene Plant J. 1998, 15, 256-263
    • (1998) Plant J. , vol.15 , pp. 256-263
    • Rook, F.1    Gerrits, N.2    Kortsett, A.3    Van Kampe, M.4    Borrias, M.5
  • 10
    • 2442459991 scopus 로고    scopus 로고
    • Sucrose metabolism: Regulatory mechanisms and pivotal roles in sugar sensing and plant development
    • Koch, K. Sucrose metabolism: regulatory mechanisms and pivotal roles in sugar sensing and plant development Curr. Opin. Plant Biol. 2004, 7, 235-246
    • (2004) Curr. Opin. Plant Biol. , vol.7 , pp. 235-246
    • Koch, K.1
  • 11
    • 77956338820 scopus 로고    scopus 로고
    • Sucrose: Metabolite and signaling molecule
    • Wind, J.; Smeekens, S.; Hanson, J. Sucrose: Metabolite and signaling molecule Phytochemistry 2010, 71 (14-15) 1510-1614
    • (2010) Phytochemistry , vol.71 , Issue.1415 , pp. 1510-1614
    • Wind, J.1    Smeekens, S.2    Hanson, J.3
  • 14
    • 33745908987 scopus 로고    scopus 로고
    • Sugar sensing and signaling in plants: Conserved and novel mechanisms
    • Rolland, F.; Baena-Gonzalez, E.; Sheen, J. Sugar sensing and signaling in plants: Conserved and novel mechanisms Annu. Rev. Plant Biol. 2006, 57, 675-709
    • (2006) Annu. Rev. Plant Biol. , vol.57 , pp. 675-709
    • Rolland, F.1    Baena-Gonzalez, E.2    Sheen, J.3
  • 15
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • Pawson, T.; Nash, P. Assembly of cell regulatory systems through protein interaction domains Science 2003, 300, 445-452
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 16
    • 33745813187 scopus 로고    scopus 로고
    • Reading protein modifications with interaction domains
    • Seet, B. T.; Dikic, I.; Zhou, M. M.; Pawson, T. Reading protein modifications with interaction domains Nat. Rev. Mol. Cell Biol. 2006, 7 (7) 473-483
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , Issue.7 , pp. 473-483
    • Seet, B.T.1    Dikic, I.2    Zhou, M.M.3    Pawson, T.4
  • 17
    • 34547509284 scopus 로고    scopus 로고
    • Phosphoproteomic identification of targets of the Arabidopsis sucrose nonfermenting-like kinase SnRK2.8 reveals a connection to metabolic processes
    • Shin, R.; Alvarez, S.; Burch, A. Y.; Jez, J. M.; Schachtman, D. P. Phosphoproteomic identification of targets of the Arabidopsis sucrose nonfermenting-like kinase SnRK2.8 reveals a connection to metabolic processes Proc. Natl. Acad. Sci. U.S.A. 2007, 104 (15) 6460-6465
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , Issue.15 , pp. 6460-6465
    • Shin, R.1    Alvarez, S.2    Burch, A.Y.3    Jez, J.M.4    Schachtman, D.P.5
  • 18
    • 65449164910 scopus 로고    scopus 로고
    • AKINbeta1 is involved in the regulation of nitrogen metabolism and sugar signaling in Arabidopsis
    • Li, X. F.; Li, Y. J.; An, Y. H.; Xiong, L. J.; Shao, X. H.; Wang, Y.; Sun, Y. AKINbeta1 is involved in the regulation of nitrogen metabolism and sugar signaling in Arabidopsis J. Integr. Plant Biol. 2009, 51 (5) 513-520
    • (2009) J. Integr. Plant Biol. , vol.51 , Issue.5 , pp. 513-520
    • Li, X.F.1    Li, Y.J.2    An, Y.H.3    Xiong, L.J.4    Shao, X.H.5    Wang, Y.6    Sun, Y.7
  • 21
    • 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.; Schulze, W. X. PhosPhAt: A database of phosphorylation sites in Arabidopsis thaliana and a plant-specific phosphorylation site predictor Nucleic Acids Res. 2008, 36, D1015-D1021
    • (2008) Nucleic Acids Res. , vol.36
    • Heazlewood, J.L.1    Durek, P.2    Hummel, J.3    Selbig, J.4    Weckwerth, W.5    Walther, D.6    Schulze, W.X.7
  • 22
    • 84876517560 scopus 로고    scopus 로고
    • PhosPhAt goes kinases-Searchable protein kinase target information in the plant phosphorylation site database PhosPhAt
    • Zulawski, M.; Braginets, R.; Schulze, W. X. PhosPhAt goes kinases-Searchable protein kinase target information in the plant phosphorylation site database PhosPhAt Nucleic Acids Res. 2013, 41 (D1) D1176-1184
    • (2013) Nucleic Acids Res. , vol.41 , Issue.D1 , pp. 1176-1184
    • Zulawski, M.1    Braginets, R.2    Schulze, W.X.3
  • 23
    • 35648996970 scopus 로고    scopus 로고
    • Temporal analysis of sucrose-induced phosphorylation changes in plasma membrane proteins of Arabidopsis
    • Niittylä, T.; Fuglsang, A. T.; Palmgren, M. G.; Frommer, W. B.; Schulze, W. X. Temporal analysis of sucrose-induced phosphorylation changes in plasma membrane proteins of Arabidopsis Mol. Cell. Proteomics 2007, 6 (10) 1711-1726
    • (2007) Mol. Cell. Proteomics , vol.6 , Issue.10 , pp. 1711-1726
    • Niittylä, T.1    Fuglsang, A.T.2    Palmgren, M.G.3    Frommer, W.B.4    Schulze, W.X.5
  • 24
    • 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.; Li, W. H. Comparative analysis of the receptor-like kinase family in Arabidopsis and rice Plant Cell 2004, 16 (5) 1220-1234
    • (2004) Plant Cell , vol.16 , Issue.5 , 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
  • 28
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium -mediated transformation of Arabidopsis thaliana
    • Clough, S. J.; Bent, A. F. Floral dip: a simplified method for Agrobacterium -mediated transformation of Arabidopsis thaliana Plant J. 1998, 16 (6) 735-743
    • (1998) Plant J. , vol.16 , Issue.6 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 29
    • 84980140250 scopus 로고
    • Growth and synthesis of proteins in cell suspensions of a kinetin dependent tobacco
    • Jouanneau, J. P.; Peaud-Lenoel, C. Growth and synthesis of proteins in cell suspensions of a kinetin dependent tobacco Physiol. Plant. 1967, 20, 834-850
    • (1967) Physiol. Plant. , vol.20 , pp. 834-850
    • Jouanneau, J.P.1    Peaud-Lenoel, C.2
  • 30
    • 14744280370 scopus 로고    scopus 로고
    • A Robot-based platform to measure multiple enzyme activities in Arabidopsis using a set of cycling assays: Comparison of changes of enzyme activities and transcript levels during diurnal cycles and in prolonged darkness
    • Gibon, Y.; Bläsing, O. E.; Hannemann, J.; Carillo, P.; Höhne, M.; Hendriks, J. H.; Palacios, N.; Cross, J.; Selbig, J.; Stitt, M. A Robot-based platform to measure multiple enzyme activities in Arabidopsis using a set of cycling assays: comparison of changes of enzyme activities and transcript levels during diurnal cycles and in prolonged darkness Plant Cell 2004, 16 (12) 3304-3325
    • (2004) Plant Cell , vol.16 , Issue.12 , pp. 3304-3325
    • Gibon, Y.1    Bläsing, O.E.2    Hannemann, J.3    Carillo, P.4    Höhne, M.5    Hendriks, J.H.6    Palacios, N.7    Cross, J.8    Selbig, J.9    Stitt, M.10
  • 31
    • 0037317228 scopus 로고    scopus 로고
    • Stop and Go Extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics
    • Rappsilber, J.; Ishihama, Y.; Mann, M. Stop And Go Extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics Anal. Chem. 2003, 75 (3) 663-670
    • (2003) Anal. Chem. , vol.75 , Issue.3 , pp. 663-670
    • Rappsilber, J.1    Ishihama, Y.2    Mann, M.3
  • 32
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichtment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns
    • Larsen, M. R.; Thingholm, T. E.; Jensen, O. N.; Roepstorff, P.; Jorgensen, T. J. D. Highly selective enrichtment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns Mol. Cell. Proteomics 2005, 4 (7) 873-886
    • (2005) Mol. Cell. Proteomics , vol.4 , Issue.7 , pp. 873-886
    • Larsen, M.R.1    Thingholm, T.E.2    Jensen, O.N.3    Roepstorff, P.4    Jorgensen, T.J.D.5
  • 34
    • 3042824849 scopus 로고    scopus 로고
    • A neutral loss activation method for improved phosphopeptide sequence analysis by quadrupole ion trap mass spectrometry
    • Schroeder, M. J.; Shabanowitz, J.; Schwartz, J. C.; Hunt, D. F.; Coon, J. J. A neutral loss activation method for improved phosphopeptide sequence analysis by quadrupole ion trap mass spectrometry Anal. Chem. 2004, 76 (13) 3590-3598
    • (2004) Anal. Chem. , vol.76 , Issue.13 , pp. 3590-3598
    • Schroeder, M.J.1    Shabanowitz, J.2    Schwartz, J.C.3    Hunt, D.F.4    Coon, J.J.5
  • 35
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J.; Mann, M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification Nat. Biotechnol. 2008, 26 (12) 1367-1372
    • (2008) Nat. Biotechnol. , vol.26 , Issue.12 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 36
  • 37
    • 84868316169 scopus 로고    scopus 로고
    • Proteomics wants cRacker: Automated standardized data analysis of LC/MS derived proteomic data
    • Zauber, H.; Schulze, W. X. Proteomics wants cRacker: Automated standardized data analysis of LC/MS derived proteomic data J. Proteome Res. 2012, 11 (11) 5548-5555
    • (2012) J. Proteome Res. , vol.11 , Issue.11 , pp. 5548-5555
    • Zauber, H.1    Schulze, W.X.2
  • 38
    • 84856264733 scopus 로고    scopus 로고
    • Cold acclimation induces changes in Arabidopsis tonoplast protein abundance and activity and alters phosphorylation of tonoplast monosaccharide transporters
    • Schulze, W. X.; Schneider, T.; Starck, S.; Martinoia, E.; Trentmann, O. Cold acclimation induces changes in Arabidopsis tonoplast protein abundance and activity and alters phosphorylation of tonoplast monosaccharide transporters Plant J. 2012, 69 (3) 529-541
    • (2012) Plant J. , vol.69 , Issue.3 , pp. 529-541
    • Schulze, W.X.1    Schneider, T.2    Starck, S.3    Martinoia, E.4    Trentmann, O.5
  • 39
    • 12144291195 scopus 로고    scopus 로고
    • MAPMAN: A user-driven tool to display genomics data sets onto diagrams of metabolic pathways and other biological processes
    • Thimm, O.; Bläsing, O.; Gibon, Y.; Nagel, A.; Meyer, S.; Kruger, P.; Selbig, J.; Muller, L. A.; Rhee, S. Y.; Stitt, M. MAPMAN: a user-driven tool to display genomics data sets onto diagrams of metabolic pathways and other biological processes Plant J. 2004, 37 (6) 914-939
    • (2004) Plant J. , vol.37 , Issue.6 , pp. 914-939
    • Thimm, O.1    Bläsing, O.2    Gibon, Y.3    Nagel, A.4    Meyer, S.5    Kruger, P.6    Selbig, J.7    Muller, L.A.8    Rhee, S.Y.9    Stitt, M.10
  • 40
    • 84876544295 scopus 로고    scopus 로고
    • SUBA3: A database for integrating experimentation and prediction to define the SUBcellular location of proteins in Arabidopsis
    • Tanz, S. K.; Castleden, I.; Hooper, C. M.; Vacher, M.; Small, I.; Millar, H. A. SUBA3: a database for integrating experimentation and prediction to define the SUBcellular location of proteins in Arabidopsis Nucleic Acids Res. 2013, 41, D1185-91
    • (2013) Nucleic Acids Res. , vol.41 , pp. 1185-1191
    • Tanz, S.K.1    Castleden, I.2    Hooper, C.M.3    Vacher, M.4    Small, I.5    Millar, H.A.6
  • 41
    • 0040419081 scopus 로고    scopus 로고
    • Role and regulation of sucrose-phosphate-synthase in higher plants
    • Huber, S. C.; Huber, J. L. Role and regulation of sucrose-phosphate- synthase in higher plants Ann. Rev. Plant Physiol. Plant Mol. Biol. 1996, 47, 431-444
    • (1996) Ann. Rev. Plant Physiol. Plant Mol. Biol. , vol.47 , pp. 431-444
    • Huber, S.C.1    Huber, J.L.2
  • 42
    • 0000117374 scopus 로고
    • Control analysis of photosynthate partitioning. Impact of reduced activity of ADP-glucose pyrophosphorylase or plastid phosphoglucomutase on the fluxes to starch and sucrose in Arabidopsis thaliana (L.) Heynh
    • Neuhaus, H. E.; Stitt, M. Control analysis of photosynthate partitioning. Impact of reduced activity of ADP-glucose pyrophosphorylase or plastid phosphoglucomutase on the fluxes to starch and sucrose in Arabidopsis thaliana (L.) Heynh Planta 1990, 182, 445-454
    • (1990) Planta , vol.182 , pp. 445-454
    • Neuhaus, H.E.1    Stitt, M.2
  • 43
    • 1542318968 scopus 로고    scopus 로고
    • Phosphorylation and 14-3-3 binding of Arabidopsis 6-phosphofructo-2- kinase/fructose-2,6-bisphosphatase
    • Kulma, A.; Villadsen, D.; Campbell, D. G.; Meek, S. E.; Harthill, J. E.; Nielsen, T. H.; MacKintosh, C. Phosphorylation and 14-3-3 binding of Arabidopsis 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase Plant J. 2004, 37, 654-667
    • (2004) Plant J. , vol.37 , pp. 654-667
    • Kulma, A.1    Villadsen, D.2    Campbell, D.G.3    Meek, S.E.4    Harthill, J.E.5    Nielsen, T.H.6    Mackintosh, C.7
  • 45
    • 84876544355 scopus 로고    scopus 로고
    • Characterization and prediction of protein phosphorylation hotspots in Arabidopsis thaliana
    • Christian, J. O.; Braginets, R.; Schulze, W. X.; Walther, D. Characterization and prediction of protein phosphorylation hotspots in Arabidopsis thaliana Front. Plant Sci. 2012, 3, 207
    • (2012) Front. Plant Sci. , vol.3 , pp. 207
    • Christian, J.O.1    Braginets, R.2    Schulze, W.X.3    Walther, D.4
  • 49
    • 84883581715 scopus 로고    scopus 로고
    • PlantLoc: An accurate web server for predicting plant protein subcellular localization by substantiality motif integrating experimentation and prediction to define the SUBcellular location of proteins in Arabidopsis
    • Tang, W.; Li, T.; Cong, P.; Xiong, W.; Wang, Z.; Sun, J. PlantLoc: an accurate web server for predicting plant protein subcellular localization by substantiality motif integrating experimentation and prediction to define the SUBcellular location of proteins in Arabidopsis Nucleic Acids Res. 2013, 31, W441-W446
    • (2013) Nucleic Acids Res. , vol.31
    • Tang, W.1    Li, T.2    Cong, P.3    Xiong, W.4    Wang, Z.5    Sun, J.6
  • 50
    • 78049479360 scopus 로고    scopus 로고
    • Ubiquitin-10 promoter-based vector set for fluorescent protein tagging facilitates temporal stability and native protein distribution in transient and stable expression studies
    • Grefen, C.; Donald, N.; Hashimoto, K.; Kudla, J.; Schumacher, K.; Blatt, M. A. Ubiquitin-10 promoter-based vector set for fluorescent protein tagging facilitates temporal stability and native protein distribution in transient and stable expression studies Plant J. 2010, 64, 355-365
    • (2010) Plant J. , vol.64 , pp. 355-365
    • Grefen, C.1    Donald, N.2    Hashimoto, K.3    Kudla, J.4    Schumacher, K.5    Blatt, M.A.6
  • 51
    • 84890677480 scopus 로고    scopus 로고
    • Stable isotope metabolic labeling-based quantitative phosphoproteomic analysis of Arabidopsis mutants reveals ethylene-regulated time-dependent phosphoproteins and putative substrates of constitutive triple response 1 kinase
    • Yang, Z.; Guo, G.; Zhang, M.; Liu, C. Y.; Hu, Q.; Lam, H.; Cheng, H.; Xue, Y.; Li, J.; Li, N. Stable isotope metabolic labeling-based quantitative phosphoproteomic analysis of Arabidopsis mutants reveals ethylene-regulated time-dependent phosphoproteins and putative substrates of constitutive triple response 1 kinase Mol. Cell. Proteomics 2013, 12 (12) 3559-3582
    • (2013) Mol. Cell. Proteomics , vol.12 , Issue.12 , pp. 3559-3582
    • Yang, Z.1    Guo, G.2    Zhang, M.3    Liu, C.Y.4    Hu, Q.5    Lam, H.6    Cheng, H.7    Xue, Y.8    Li, J.9    Li, N.10
  • 55
    • 0030887842 scopus 로고    scopus 로고
    • Engineering unnatural nucleotide specificity for Rous sarcoma virus tyrosine kinase to uniquely label its direct substrates
    • Shah, K.; Liu, Y.; Deirmengian, C.; Shokat, K. M. Engineering unnatural nucleotide specificity for Rous sarcoma virus tyrosine kinase to uniquely label its direct substrates Proc. Natl. Acad. Sci. U.S.A. 1997, 94 (8) 3565-3570
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , Issue.8 , pp. 3565-3570
    • Shah, K.1    Liu, Y.2    Deirmengian, C.3    Shokat, K.M.4
  • 57
    • 55849147636 scopus 로고    scopus 로고
    • Quantitative phosphoproteome analysis of a mouse liver cell line reveals specificity of phosphatase inhibitors
    • Pan, C.; Gnad, F.; Olsen, J. V.; Mann, M. Quantitative phosphoproteome analysis of a mouse liver cell line reveals specificity of phosphatase inhibitors Proteomics 2008, 8 (21) 4534-4546
    • (2008) Proteomics , vol.8 , Issue.21 , pp. 4534-4546
    • Pan, C.1    Gnad, F.2    Olsen, J.V.3    Mann, M.4
  • 59
    • 3543037605 scopus 로고    scopus 로고
    • Tetratricopeptide repeat cochaperones in steroid receptor complexes
    • Smith, D. F. Tetratricopeptide repeat cochaperones in steroid receptor complexes Cell Stress Chaperones 2004, 9, 102-121
    • (2004) Cell Stress Chaperones , vol.9 , pp. 102-121
    • Smith, D.F.1
  • 60
    • 70349652000 scopus 로고    scopus 로고
    • Brassinosteroid signal transduction from cell-surface receptor kinases to nuclear transcription factors
    • Kim, T. W.; Guan, S.; Sun, Y.; Deng, Z.; Tang, W.; Shang, J. X.; Sun, Y.; Burlingam, A.; Wang, Z. Y. Brassinosteroid signal transduction from cell-surface receptor kinases to nuclear transcription factors Nat. Cell Biol. 2009, 11 (10) 1254-1260
    • (2009) Nat. Cell Biol. , vol.11 , Issue.10 , pp. 1254-1260
    • Kim, T.W.1    Guan, S.2    Sun, Y.3    Deng, Z.4    Tang, W.5    Shang, J.X.6    Sun, Y.7    Burlingam, A.8    Wang, Z.Y.9
  • 61
    • 0000007754 scopus 로고
    • Coarse control of sucrose-phosphate synthase in leaves - Alterations of the kinetic-properties in response to the rate of photosynthesis and the accumulation of sucrose
    • Stitt, M.; Wilke, I.; Feil, R.; Heldt, H. W. Coarse control of sucrose-phosphate synthase in leaves-alterations of the kinetic-properties in response to the rate of photosynthesis and the accumulation of sucrose Planta 1988, 174, 217-230
    • (1988) Planta , vol.174 , pp. 217-230
    • Stitt, M.1    Wilke, I.2    Feil, R.3    Heldt, H.W.4
  • 62
    • 0025271020 scopus 로고
    • Apparent equilibrium constant and mass-action ratio for sucrose-phosphate synthase in seeds of Pisum sativum
    • Lunn, J. E.; ap Rees, T. Apparent equilibrium constant and mass-action ratio for sucrose-phosphate synthase in seeds of Pisum sativum Biochem. J. 1990, 267, 739-743
    • (1990) Biochem. J. , vol.267 , pp. 739-743
    • Lunn, J.E.1    Ap Rees, T.2
  • 63
    • 0032508671 scopus 로고    scopus 로고
    • Site-specific regulatory interaction between spinach leaf sucrose-phosphate synthase and 14-3-3 proteins
    • Toroser, D.; Athwal, G. S.; Huber, S. C. Site-specific regulatory interaction between spinach leaf sucrose-phosphate synthase and 14-3-3 proteins FEBS Lett. 1998, 435 (1) 110-114
    • (1998) FEBS Lett. , vol.435 , Issue.1 , pp. 110-114
    • Toroser, D.1    Athwal, G.S.2    Huber, S.C.3
  • 64
    • 0002591477 scopus 로고
    • Light regulation of sucrose synthesis: Role of protein phosphorylation and possible involvement of cytosolic [Ca2+]
    • Huber, S. C.; McMichael, R. W.; Huber, J. L.; Bachmann, M.; Yamamoto, Y. T.; Conkling, M. A. Light regulation of sucrose synthesis: Role of protein phosphorylation and possible involvement of cytosolic [Ca2+] Curr. Top. Plant Sci. 1995, 13, 35-44
    • (1995) Curr. Top. Plant Sci. , vol.13 , pp. 35-44
    • Huber, S.C.1    McMichael, R.W.2    Huber, J.L.3    Bachmann, M.4    Yamamoto, Y.T.5    Conkling, M.A.6
  • 65
    • 0027133515 scopus 로고
    • Identification of the major regulatory phosphorylation site in sucrose-phosphate synthase
    • Mcmichael, R. W.; Klein, R. R.; Salvucci, M. E.; Huber, S. C. Identification of the major regulatory phosphorylation site in sucrose-phosphate synthase Arch. Biochem. Biophys. 1993, 307, 248-252
    • (1993) Arch. Biochem. Biophys. , vol.307 , pp. 248-252
    • McMichael, R.W.1    Klein, R.R.2    Salvucci, M.E.3    Huber, S.C.4
  • 67
    • 0033134243 scopus 로고    scopus 로고
    • Two SNF1-related protein kinases from spinach leaf phosphorylate and inactivate 3-hydroxy-3-methylglutaryl-coenzyme A reductase, nitrate reductase, and sucrose phosphate synthase in vitro
    • Sugden, C.; Donaghy, P. G.; Halford, N. G.; Hardie, D. G. Two SNF1-related protein kinases from spinach leaf phosphorylate and inactivate 3-hydroxy-3-methylglutaryl-coenzyme A reductase, nitrate reductase, and sucrose phosphate synthase in vitro Plant Physiol. 1999, 120 (1) 257-274-274
    • (1999) Plant Physiol. , vol.120 , Issue.1 , pp. 257
    • Sugden, C.1    Donaghy, P.G.2    Halford, N.G.3    Hardie, D.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.