메뉴 건너뛰기




Volumn 1, Issue , 2015, Pages

Protein turnover in plant biology

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84936790069     PISSN: None     EISSN: 20550278     Source Type: Journal    
DOI: 10.1038/nplants.2015.17     Document Type: Review
Times cited : (75)

References (76)
  • 1
    • 84876287130 scopus 로고    scopus 로고
    • Glucose-TOR signalling reprograms the transcriptome and activates meristems
    • Xiong, Y. et al. Glucose-TOR signalling reprograms the transcriptome and activates meristems. Nature 496, 181-186 (2013).
    • (2013) Nature , vol.496 , pp. 181-186
    • Xiong, Y.1
  • 2
    • 78649488563 scopus 로고    scopus 로고
    • The developmental dynamics of the maize leaf transcriptome
    • Li, P. et al. The developmental dynamics of the maize leaf transcriptome. Nature Genet. 42, 1060-1067 (2010).
    • (2010) Nature Genet. , vol.42 , pp. 1060-1067
    • Li, P.1
  • 3
    • 84893427735 scopus 로고    scopus 로고
    • In vivo genome-wide profiling of RNA secondary structure reveals novel regulatory features
    • Ding, Y. et al. In vivo genome-wide profiling of RNA secondary structure reveals novel regulatory features. Nature 505, 696-700 (2014).
    • (2014) Nature , vol.505 , pp. 696-700
    • Ding, Y.1
  • 4
    • 84897571308 scopus 로고    scopus 로고
    • Poly(A)-tail profiling reveals an embryonic switch in translational control
    • Subtelny, A. O., Eichhorn, S. W., Chen, G. R., Sive, H., Bartel, D. P. Poly(A)-tail profiling reveals an embryonic switch in translational control. Nature 508, 66-71 (2014).
    • (2014) Nature , vol.508 , pp. 66-71
    • Subtelny, A.O.1    Eichhorn, S.W.2    Chen, G.R.3    Sive, H.4    Bartel, D.P.5
  • 5
    • 84891945795 scopus 로고    scopus 로고
    • Translational dynamics revealed by genome-wide profiling of ribosome footprints in Arabidopsis
    • Juntawong, P., Girke, T., Bazin, J., Bailey-Serres, J. Translational dynamics revealed by genome-wide profiling of ribosome footprints in Arabidopsis. Proc. Natl Acad. Sci. USA 111, E203-E212 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. E203-E212
    • Juntawong, P.1    Girke, T.2    Bazin, J.3    Bailey-Serres, J.4
  • 6
    • 84879732934 scopus 로고    scopus 로고
    • Diurnal changes of polysome loading track sucrose content in the rosette of wild-type arabidopsis and the starchless pgm mutant
    • Pal, S. K. et al. Diurnal changes of polysome loading track sucrose content in the rosette of wild-type arabidopsis and the starchless pgm mutant. Plant Physiol. 162, 1246-1265 (2013).
    • (2013) Plant Physiol. , vol.162 , pp. 1246-1265
    • Pal, S.K.1
  • 7
    • 79955536138 scopus 로고    scopus 로고
    • The dynamic state of protein turnover: It's about time
    • Hinkson, I. V., Elias, J. E. The dynamic state of protein turnover: It's about time. Trends Cell Biol. 21, 293-303 (2011).
    • (2011) Trends Cell Biol. , vol.21 , pp. 293-303
    • Hinkson, I.V.1    Elias, J.E.2
  • 8
    • 84857963102 scopus 로고    scopus 로고
    • A quantitative spatial proteomics analysis of proteome turnover in human cells
    • Boisvert, F. M. et al. A quantitative spatial proteomics analysis of proteome turnover in human cells. Mol. Cell Proteomics 11, M111. 011429 (2012).
    • (2012) Mol. Cell Proteomics , vol.11 , pp. M111011429
    • Boisvert, F.M.1
  • 9
    • 84905457938 scopus 로고    scopus 로고
    • Arabidopsis della protein degradation is controlled by a type-one protein phosphatase TOPP4
    • Qin, Q. et al. Arabidopsis DELLA protein degradation is controlled by a type-one protein phosphatase, TOPP4. PLoS Genet. 10, e1004464 (2014).
    • (2014) PLoS Genet. , vol.10 , pp. e1004464
    • Qin, Q.1
  • 10
    • 84928895757 scopus 로고    scopus 로고
    • Protein maturation and proteolysis in plant plastids, mitochondria, and peroxisomes
    • van Wijk, K. J. Protein maturation and proteolysis in plant plastids, mitochondria, and peroxisomes. Annu. Rev. Plant Biol. (2015).
    • (2015) Annu. Rev. Plant Biol.
    • Van Wijk, K.J.1
  • 11
    • 84864387284 scopus 로고    scopus 로고
    • Accumulation of newly synthesized F1 in vivo in Arabidopsis mitochondria provides evidence for modular assembly of the plant F1Fo ATP synthase
    • Li, L., Carrie, C., Nelson, C., Whelan, J., Millar, A. H. Accumulation of newly synthesized F1 in vivo in Arabidopsis mitochondria provides evidence for modular assembly of the plant F1Fo ATP synthase. J. Biol. Chem. 287, 25749-25757 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 25749-25757
    • Li, L.1    Carrie, C.2    Nelson, C.3    Whelan, J.4    Millar, A.H.5
  • 12
    • 84865778296 scopus 로고    scopus 로고
    • Rapid phosphoproteomic and transcriptomic changes in the rhizobia-legume symbiosis
    • Rose, C. M. et al. Rapid phosphoproteomic and transcriptomic changes in the rhizobia-legume symbiosis. Mol. Cell Proteomics 11, 724-744 (2012).
    • (2012) Mol. Cell Proteomics , vol.11 , pp. 724-744
    • Rose, C.M.1
  • 13
    • 44249091879 scopus 로고    scopus 로고
    • Genome-scale proteomics reveals Arabidopsis thaliana gene models and proteome dynamics
    • Baerenfaller, K. et al. Genome-scale proteomics reveals Arabidopsis thaliana gene models and proteome dynamics. Science 320, 938-941 (2008).
    • (2008) Science , vol.320 , pp. 938-941
    • Baerenfaller, K.1
  • 14
    • 78650882578 scopus 로고    scopus 로고
    • Structural and metabolic transitions of C4 leaf development and differentiation defined by microscopy and quantitative proteomics in maize
    • Majeran, W. et al. Structural and metabolic transitions of C4 leaf development and differentiation defined by microscopy and quantitative proteomics in maize. Plant Cell 22, 3509-3542 (2010).
    • (2010) Plant Cell , vol.22 , pp. 3509-3542
    • Majeran, W.1
  • 15
    • 84866650808 scopus 로고    scopus 로고
    • Quantifying ATP turnover in anoxic coleoptiles of rice (Oryza sativa) demonstrates preferential allocation of energy to protein synthesis
    • Edwards, J. M., Roberts, T. H., Atwell, B. J. Quantifying ATP turnover in anoxic coleoptiles of rice (Oryza sativa) demonstrates preferential allocation of energy to protein synthesis. J. Exp. Bot. 63, 4389-4402 (2012).
    • (2012) J. Exp. Bot. , vol.63 , pp. 4389-4402
    • Edwards, J.M.1    Roberts, T.H.2    Atwell, B.J.3
  • 16
    • 84887341869 scopus 로고    scopus 로고
    • Expression changes of ribosomal proteins in phosphate-and iron-deficient Arabidopsis roots predict stress-specific alterations in ribosome composition
    • Wang, J. et al. Expression changes of ribosomal proteins in phosphate-and iron-deficient Arabidopsis roots predict stress-specific alterations in ribosome composition. BMC Genom. 14, 783 (2013).
    • (2013) BMC Genom. , vol.14 , pp. 783
    • Wang, J.1
  • 17
    • 84900851871 scopus 로고    scopus 로고
    • The link between transcript regulation and de novo protein synthesis in the retrograde high light acclimation response of Arabidopsis thaliana
    • Oelze, M. L., Muthuramalingam, M., Vogel, M. O., Dietz, K. J. The link between transcript regulation and de novo protein synthesis in the retrograde high light acclimation response of Arabidopsis thaliana. BMC Genom. 15, 320 (2014).
    • (2014) BMC Genom. , vol.15 , pp. 320
    • Oelze, M.L.1    Muthuramalingam, M.2    Vogel, M.O.3    Dietz, K.J.4
  • 18
    • 84868228819 scopus 로고    scopus 로고
    • Chloroplast biogenesis is regulated by direct action of the ubiquitin-proteasome system
    • Ling, Q., Huang, W., Baldwin, A., Jarvis, P. Chloroplast biogenesis is regulated by direct action of the ubiquitin-proteasome system. Science 338, 655-659 (2012).
    • (2012) Science , vol.338 , pp. 655-659
    • Ling, Q.1    Huang, W.2    Baldwin, A.3    Jarvis, P.4
  • 19
    • 84898768916 scopus 로고    scopus 로고
    • Plant ubiquitin ligases as signaling hubs
    • Shabek, N., Zheng, N. Plant ubiquitin ligases as signaling hubs. Nature Struct. Mol. Biol. 21, 293-296 (2014).
    • (2014) Nature Struct. Mol. Biol. , vol.21 , pp. 293-296
    • Shabek, N.1    Zheng, N.2
  • 20
    • 84887251616 scopus 로고    scopus 로고
    • Proteomics analysis reveals a highly heterogeneous proteasome composition and the post-translational regulation of peptidase activity under pathogen signaling in plants
    • Sun, H. H. et al. Proteomics analysis reveals a highly heterogeneous proteasome composition and the post-translational regulation of peptidase activity under pathogen signaling in plants. J. Proteome Res. 12, 5084-5095 (2013).
    • (2013) J. Proteome Res. , vol.12 , pp. 5084-5095
    • Sun, H.H.1
  • 21
    • 75149157140 scopus 로고    scopus 로고
    • The ubiquitin/26S proteasome system in plant-pathogen interactions: A never-ending hide-and-seek game
    • Dielen, A. S., Badaoui, S., Candresse, T., German-Retana, S. The ubiquitin/26S proteasome system in plant-pathogen interactions: a never-ending hide-and-seek game. Mol. Plant Pathol. 11, 293-308 (2010).
    • (2010) Mol. Plant Pathol. , vol.11 , pp. 293-308
    • Dielen, A.S.1    Badaoui, S.2    Candresse, T.3    German-Retana, S.4
  • 22
    • 84902310414 scopus 로고    scopus 로고
    • The Arabidopsis mitochondrial membrane-bound ubiquitin protease UBP27 contributes to mitochondrial morphogenesis
    • Pan, R., Kaur, N., Hu, J. The Arabidopsis mitochondrial membrane-bound ubiquitin protease UBP27 contributes to mitochondrial morphogenesis. Plant J. 78, 1047-1059 (2014).
    • (2014) Plant J. , vol.78 , pp. 1047-1059
    • Pan, R.1    Kaur, N.2    Hu, J.3
  • 23
    • 84875713765 scopus 로고    scopus 로고
    • Autophagy contributes to nighttime energy availability for growth in Arabidopsis
    • Izumi, M., Hidema, J., Makino, A., Ishida, H. Autophagy contributes to nighttime energy availability for growth in Arabidopsis. Plant Physiol. 161, 1682-1693 (2013).
    • (2013) Plant Physiol. , vol.161 , pp. 1682-1693
    • Izumi, M.1    Hidema, J.2    Makino, A.3    Ishida, H.4
  • 24
    • 77957966789 scopus 로고    scopus 로고
    • New insights into the types and function of proteases in plastids
    • Kato, Y., Sakamoto, W. New insights into the types and function of proteases in plastids. Int. Rev. Cell Mol. Biol. 280, 185-218 (2010).
    • (2010) Int. Rev. Cell Mol. Biol. , vol.280 , pp. 185-218
    • Kato, Y.1    Sakamoto, W.2
  • 26
    • 84891789094 scopus 로고    scopus 로고
    • Dynamic proteomics emphasizes the importance of selective mRNA translation and protein turnover during Arabidopsis seed germination
    • Galland, M. et al. Dynamic proteomics emphasizes the importance of selective mRNA translation and protein turnover during Arabidopsis seed germination. Mol. Cell Proteomics 13, 252-268 (2014).
    • (2014) Mol. Cell Proteomics , vol.13 , pp. 252-268
    • Galland, M.1
  • 27
    • 84879740822 scopus 로고    scopus 로고
    • Moving beyond translation: Glucose-TOR signaling in the transcriptional control of cell cycle
    • Xiong, Y., Sheen, J. Moving beyond translation: glucose-TOR signaling in the transcriptional control of cell cycle. Cell Cycle 12, 1989-1990 (2013).
    • (2013) Cell Cycle , vol.12 , pp. 1989-1990
    • Xiong, Y.1    Sheen, J.2
  • 28
    • 84893498683 scopus 로고    scopus 로고
    • The role of target of rapamycin signaling networks in plant growth and metabolism
    • Xiong, Y., Sheen, J. The role of target of rapamycin signaling networks in plant growth and metabolism. Plant Physiol. 164, 499-512 (2014).
    • (2014) Plant Physiol. , vol.164 , pp. 499-512
    • Xiong, Y.1    Sheen, J.2
  • 29
    • 84906898355 scopus 로고    scopus 로고
    • Coordinated regulation of protein synthesis and degradation by mTORC1
    • Zhang, Y. et al. Coordinated regulation of protein synthesis and degradation by mTORC1. Nature, 513, 440-443 (2014).
    • (2014) Nature , vol.513 , pp. 440-443
    • Zhang, Y.1
  • 30
    • 84908478523 scopus 로고    scopus 로고
    • The eukaryotic N-end rule pathway: Conserved mechanisms and diverse functions
    • Gibbs, D. J., Bacardit, J., Bachmair, A., Holdsworth, M. J. The eukaryotic N-end rule pathway: conserved mechanisms and diverse functions. Trends Cell Biol. 24, 603-611 (2014).
    • (2014) Trends Cell Biol. , vol.24 , pp. 603-611
    • Gibbs, D.J.1    Bacardit, J.2    Bachmair, A.3    Holdsworth, M.J.4
  • 31
    • 84862338914 scopus 로고    scopus 로고
    • Determining degradation and synthesis rates of Arabidopsis proteins using the kinetics of progressive 15N labeling of two-dimensional gel-separated protein spots
    • Li, L., Nelson, C. J., Solheim, C., Whelan, J., Millar, A. H. Determining degradation and synthesis rates of Arabidopsis proteins using the kinetics of progressive 15N labeling of two-dimensional gel-separated protein spots. Mol. Cell Proteomics 11, M111 010025 (2012).
    • (2012) Mol. Cell Proteomics , vol.11 , pp. M111010025
    • Li, L.1    Nelson, C.J.2    Solheim, C.3    Whelan, J.4    Millar, A.H.5
  • 32
    • 84907058339 scopus 로고    scopus 로고
    • Proteins with high turnover rate in barley leaves estimated by proteome analysis combined with in planta isotope labelling
    • Nelson, C. J., Alexova, R., Jacoby, R. P., Millar, A. H. Proteins with high turnover rate in barley leaves estimated by proteome analysis combined with in planta isotope labelling. Plant Physiol. 166, 91-108 (2014).
    • (2014) Plant Physiol. , vol.166 , pp. 91-108
    • Nelson, C.J.1    Alexova, R.2    Jacoby, R.P.3    Millar, A.H.4
  • 33
    • 0036692065 scopus 로고    scopus 로고
    • Dynamics of protein turnover, a missing dimension in proteomics
    • Pratt, J. M. et al. Dynamics of protein turnover, a missing dimension in proteomics. Mol. Cell Proteomics 1, 579-591 (2002).
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 579-591
    • Pratt, J.M.1
  • 35
    • 77957813967 scopus 로고    scopus 로고
    • Advances in protein turnover analysis at the global level and biological insights
    • Li, Q. Advances in protein turnover analysis at the global level and biological insights. Mass Spectrom. Rev. 29, 717-736 (2010).
    • (2010) Mass Spectrom. Rev. , vol.29 , pp. 717-736
    • Li, Q.1
  • 36
    • 84879953097 scopus 로고    scopus 로고
    • Degradation rate of mitochondrial proteins in Arabidopsis thaliana cells
    • Nelson, C. J., Li, L., Jacoby, R. P., Millar, A. H. Degradation rate of mitochondrial proteins in Arabidopsis thaliana cells. J. Proteome Res. 12, 3449-3459 (2013).
    • (2013) J. Proteome Res. , vol.12 , pp. 3449-3459
    • Nelson, C.J.1    Li, L.2    Jacoby, R.P.3    Millar, A.H.4
  • 37
    • 62549094876 scopus 로고    scopus 로고
    • Functional proteomics of Arabidopsis thaliana guard cells uncovers new stomatal signaling pathways
    • Zhao, Z., Zhang, W., Stanley, B. A., Assmann, S. M. Functional proteomics of Arabidopsis thaliana guard cells uncovers new stomatal signaling pathways. Plant Cell 20, 3210-3226 (2008).
    • (2008) Plant Cell , vol.20 , pp. 3210-3226
    • Zhao, Z.1    Zhang, W.2    Stanley, B.A.3    Assmann, S.M.4
  • 38
    • 66149152316 scopus 로고    scopus 로고
    • Functional differentiation of Brassica napus guard cells and mesophyll cells revealed by comparative proteomics
    • Zhu, M., Dai, S., McClung, S., Yan, X., Chen, S. Functional differentiation of Brassica napus guard cells and mesophyll cells revealed by comparative proteomics. Mol. Cell Proteomics 8, 752-766 (2009).
    • (2009) Mol. Cell Proteomics , vol.8 , pp. 752-766
    • Zhu, M.1    Dai, S.2    McClung, S.3    Yan, X.4    Chen, S.5
  • 39
    • 33645960112 scopus 로고    scopus 로고
    • Functional differentiation of bundle sheath and mesophyll maize chloroplasts determined by comparative proteomics
    • Majeran, W., Cai, Y., Sun, Q., van Wijk, K. J. Functional differentiation of bundle sheath and mesophyll maize chloroplasts determined by comparative proteomics. Plant Cell 17, 3111-3140 (2005).
    • (2005) Plant Cell , vol.17 , pp. 3111-3140
    • Majeran, W.1    Cai, Y.2    Sun, Q.3    Van Wijk, K.J.4
  • 40
    • 52649096494 scopus 로고    scopus 로고
    • Consequences of C4 differentiation for chloroplast membrane proteomes in maize mesophyll and bundle sheath cells
    • Majeran, W. et al. Consequences of C4 differentiation for chloroplast membrane proteomes in maize mesophyll and bundle sheath cells. Mol. Cell Proteomics 7, 1609-1638 (2008).
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 1609-1638
    • Majeran, W.1
  • 41
    • 67650091977 scopus 로고    scopus 로고
    • Differential turnover of the photosystem II reaction centre D1 protein in mesophyll and bundle sheath chloroplasts of maize
    • Pokorska, B., Zienkiewicz, M., Powikrowska, M., Drozak, A., Romanowska, E. Differential turnover of the photosystem II reaction centre D1 protein in mesophyll and bundle sheath chloroplasts of maize. Biochim. Biophys. Acta 1787, 1161-1169 (2009).
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1161-1169
    • Pokorska, B.1    Zienkiewicz, M.2    Powikrowska, M.3    Drozak, A.4    Romanowska, E.5
  • 42
    • 36248951584 scopus 로고    scopus 로고
    • Transcriptomic and proteomic analyses of pericycle cells of the maize primary root
    • Dembinsky, D. et al. Transcriptomic and proteomic analyses of pericycle cells of the maize primary root. Plant Physiol. 145, 575-588 (2007).
    • (2007) Plant Physiol. , vol.145 , pp. 575-588
    • Dembinsky, D.1
  • 43
    • 17644411695 scopus 로고    scopus 로고
    • Proteomic analysis of soybean root hairs after infection by Bradyrhizobium japonicum
    • Wan, J. et al. Proteomic analysis of soybean root hairs after infection by Bradyrhizobium japonicum. Mol. Plant Microbe Interact. 18, 458-467 (2005).
    • (2005) Mol. Plant Microbe Interact. , vol.18 , pp. 458-467
    • Wan, J.1
  • 44
    • 37249082491 scopus 로고    scopus 로고
    • Cell wall proteome in the maize primary root elongation zone. II. Region-specific changes in water soluble and lightly ionically bound proteins under water deficit
    • Zhu, J. et al. Cell wall proteome in the maize primary root elongation zone. II. Region-specific changes in water soluble and lightly ionically bound proteins under water deficit. Plant Physiol. 145, 1533-1548 (2007).
    • (2007) Plant Physiol. , vol.145 , pp. 1533-1548
    • Zhu, J.1
  • 45
    • 74049155841 scopus 로고    scopus 로고
    • Expression profiling and proteomic analysis of isolated photosynthetic cells of the non-Kranz C4 species Bienertia sinuspersici
    • Park, J., Okita, T. W., Edwards, G. E. Expression profiling and proteomic analysis of isolated photosynthetic cells of the non-Kranz C4 species Bienertia sinuspersici. Funct. Plant Biol. 37, 1-13 (2010).
    • (2010) Funct. Plant Biol. , vol.37 , pp. 1-13
    • Park, J.1    Okita, T.W.2    Edwards, G.E.3
  • 46
    • 84874292317 scopus 로고    scopus 로고
    • Subcomplexes of ancestral respiratory complex i subunits rapidly turn over in vivo as productive assembly intermediates in Arabidopsis
    • Li, L. et al. Subcomplexes of ancestral respiratory complex I subunits rapidly turn over in vivo as productive assembly intermediates in Arabidopsis. J. Biol. Chem. 288, 5707-5717 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 5707-5717
    • Li, L.1
  • 47
    • 84907354412 scopus 로고    scopus 로고
    • Glutamate dehydrogenase isoenzyme 3 (GDH3) of Arabidopsis thaliana is less thermostable than GDH1 and GDH2 isoenzymes
    • Marchi, L., Polverini, E., Degola, F., Baruffini, E., Restivo, F. M. Glutamate dehydrogenase isoenzyme 3 (GDH3) of Arabidopsis thaliana is less thermostable than GDH1 and GDH2 isoenzymes. Plant Physiol. Biochem. 83, 225-231 (2014).
    • (2014) Plant Physiol. Biochem. , vol.83 , pp. 225-231
    • Marchi, L.1    Polverini, E.2    Degola, F.3    Baruffini, E.4    Restivo, F.M.5
  • 48
    • 84905014771 scopus 로고    scopus 로고
    • COP1 and phyB Physically interact with PIL1 to regulate its stability and photomorphogenic development in Arabidopsis
    • Luo, Q. et al. COP1 and phyB Physically interact with PIL1 to regulate its stability and photomorphogenic development in Arabidopsis. Plant Cell 26, 2441-2456 (2014).
    • (2014) Plant Cell , vol.26 , pp. 2441-2456
    • Luo, Q.1
  • 49
    • 0025284693 scopus 로고
    • Chlorophyll regulates accumulation of the plastid-encoded chlorophyll apoproteins CP43 and D1 by increasing apoprotein stability
    • Mullet, J. E., Klein, P. G., Klein, R. R. Chlorophyll regulates accumulation of the plastid-encoded chlorophyll apoproteins CP43 and D1 by increasing apoprotein stability. Proc. Natl Acad. Sci. USA 87, 4038-4042 (1990).
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 4038-4042
    • Mullet, J.E.1    Klein, P.G.2    Klein, R.R.3
  • 50
    • 0028824766 scopus 로고
    • Contribution of the FAD binding site residue tyrosine 308 to the stability of pea ferredoxin-NADP+ oxidoreductase
    • Calcaterra, N. B. et al. Contribution of the FAD binding site residue tyrosine 308 to the stability of pea ferredoxin-NADP+ oxidoreductase. Biochemistry 34, 12842-12848 (1995).
    • (1995) Biochemistry , vol.34 , pp. 12842-12848
    • Calcaterra, N.B.1
  • 51
    • 0022972973 scopus 로고
    • Rapid degradation of apoplastocyanin in Cu(II)-deficient cells of Chlamydomonas reinhardtii
    • Merchant, S., Bogorad, L. Rapid degradation of apoplastocyanin in Cu(II)-deficient cells of Chlamydomonas reinhardtii. J Biol Chem 261, 15850-15853 (1986).
    • (1986) J Biol Chem , vol.261 , pp. 15850-15853
    • Merchant, S.1    Bogorad, L.2
  • 52
    • 0028783872 scopus 로고
    • Degradation of the D1-and D2-proteins of photosystem II in higher plants is regulated by reversible phosphorylation
    • Koivuniemi, A., Aro, E. M., Andersson, B. Degradation of the D1-and D2-proteins of photosystem II in higher plants is regulated by reversible phosphorylation. Biochemistry 34, 16022-16029 (1995).
    • (1995) Biochemistry , vol.34 , pp. 16022-16029
    • Koivuniemi, A.1    Aro, E.M.2    Andersson, B.3
  • 53
    • 82755187237 scopus 로고    scopus 로고
    • Thylakoid protein phosphorylation in dynamic regulation of photosystem II in higher plants
    • Tikkanen, M., Aro, E. M. Thylakoid protein phosphorylation in dynamic regulation of photosystem II in higher plants. Biochim. Biophys. Acta 1817, 232-238 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 232-238
    • Tikkanen, M.1    Aro, E.M.2
  • 54
    • 84879478354 scopus 로고    scopus 로고
    • Advanced proteomic analyses yield a deep catalog of ubiquitylation targets in Arabidopsis
    • Kim, D. Y., Scalf, M., Smith, L. M., Vierstra, R. D. Advanced proteomic analyses yield a deep catalog of ubiquitylation targets in Arabidopsis. Plant Cell 25, 1523-1540 (2013).
    • (2013) Plant Cell , vol.25 , pp. 1523-1540
    • Kim, D.Y.1    Scalf, M.2    Smith, L.M.3    Vierstra, R.D.4
  • 55
    • 84901929460 scopus 로고    scopus 로고
    • Protein abundance changes and ubiquitylation targets identified after inhibition of the proteasome with syringolin A
    • Svozil, J., Hirsch-Hoffmann, M., Dudler, R., Gruissem, W., Baerenfaller, K. Protein abundance changes and ubiquitylation targets identified after inhibition of the proteasome with syringolin A. Mol. Cell Proteomics 13, 1523-1536 (2014).
    • (2014) Mol. Cell Proteomics , vol.13 , pp. 1523-1536
    • Svozil, J.1    Hirsch-Hoffmann, M.2    Dudler, R.3    Gruissem, W.4    Baerenfaller, K.5
  • 56
    • 84874050141 scopus 로고    scopus 로고
    • Quantitative proteomics reveals factors regulating RNA biology as dynamic targets of stress-induced SUMOylation in Arabidopsis
    • Miller, M. J. et al. Quantitative proteomics reveals factors regulating RNA biology as dynamic targets of stress-induced SUMOylation in Arabidopsis. Mol. Cell Proteomics 12, 449-463 (2013).
    • (2013) Mol. Cell Proteomics , vol.12 , pp. 449-463
    • Miller, M.J.1
  • 57
    • 20344377809 scopus 로고    scopus 로고
    • Proteomic identification of S-nitrosylated proteins in Arabidopsis
    • Lindermayr, C., Saalbach, G., Durner, J. Proteomic identification of S-nitrosylated proteins in Arabidopsis. Plant Physiol. 137, 921-930 (2005).
    • (2005) Plant Physiol. , vol.137 , pp. 921-930
    • Lindermayr, C.1    Saalbach, G.2    Durner, J.3
  • 58
    • 84896731136 scopus 로고    scopus 로고
    • E3 ubiquitin ligase CHIP and NBR1-mediated selective autophagy protect additively against proteotoxicity in plant stress responses
    • Zhou, J. et al. E3 ubiquitin ligase CHIP and NBR1-mediated selective autophagy protect additively against proteotoxicity in plant stress responses. PLoS Genet. 10, e1004116 (2014).
    • (2014) PLoS Genet. , vol.10 , pp. e1004116
    • Zhou, J.1
  • 59
    • 34250849635 scopus 로고    scopus 로고
    • Oxidative modifications to cellular components in plants
    • Moller, I. M., Jensen, P. E., Hansson, A. Oxidative modifications to cellular components in plants. Annu. Rev. Plant Biol. 58, 459-481 (2007).
    • (2007) Annu. Rev. Plant Biol. , vol.58 , pp. 459-481
    • Moller, I.M.1    Jensen, P.E.2    Hansson, A.3
  • 60
    • 77957222651 scopus 로고    scopus 로고
    • Modification-specific proteomics in plant biology
    • Ytterberg, A. J., Jensen, O. N. Modification-specific proteomics in plant biology. J. Proteomics 73, 2249-2266 (2010).
    • (2010) J. Proteomics , vol.73 , pp. 2249-2266
    • Ytterberg, A.J.1    Jensen, O.N.2
  • 61
    • 77955679608 scopus 로고    scopus 로고
    • Measuring the turnover rates of Arabidopsis proteins using deuterium oxide: An auxin signaling case study
    • Yang, X. Y. et al. Measuring the turnover rates of Arabidopsis proteins using deuterium oxide: an auxin signaling case study. Plant J. 63, 680-695 (2010).
    • (2010) Plant J. , vol.63 , pp. 680-695
    • Yang, X.Y.1
  • 62
    • 84903638180 scopus 로고    scopus 로고
    • Repression of jasmonate-dependent defenses by shade involves differential regulation of protein stability of MYC transcription factors and their JAZ repressors in Arabidopsis
    • Chico, J. M. et al. Repression of jasmonate-dependent defenses by shade involves differential regulation of protein stability of MYC transcription factors and their JAZ repressors in Arabidopsis. Plant Cell 26, 1967-1980 (2014).
    • (2014) Plant Cell , vol.26 , pp. 1967-1980
    • Chico, J.M.1
  • 63
    • 34548675558 scopus 로고    scopus 로고
    • A bacterial transgene for catalase protects translation of d1 protein during exposure of salt-stressed tobacco leaves to strong light
    • Al-Taweel, K. et al. A bacterial transgene for catalase protects translation of d1 protein during exposure of salt-stressed tobacco leaves to strong light. Plant Physiol. 145, 258-265 (2007).
    • (2007) Plant Physiol. , vol.145 , pp. 258-265
    • Al-Taweel, K.1
  • 64
    • 0036006859 scopus 로고    scopus 로고
    • Molecular and physiological approaches to maize improvement for drought tolerance
    • Bruce, W. B., Edmeades, G. O., Barker, T. C. Molecular and physiological approaches to maize improvement for drought tolerance. J. Exp. Bot. 53, 13-25 (2002).
    • (2002) J. Exp. Bot. , vol.53 , pp. 13-25
    • Bruce, W.B.1    Edmeades, G.O.2    Barker, T.C.3
  • 65
    • 84921296789 scopus 로고    scopus 로고
    • Drought adaptation of stay-green sorghum is associated with canopy development, leaf anatomy, root growth, and water uptake
    • Borrell, A. K. et al. Drought adaptation of stay-green sorghum is associated with canopy development, leaf anatomy, root growth, and water uptake. J. Exp. Bot. 65, 6251-6263 (2014).
    • (2014) J. Exp. Bot. , vol.65 , pp. 6251-6263
    • Borrell, A.K.1
  • 67
    • 84856264198 scopus 로고    scopus 로고
    • Comparative proteomic study reveals dynamic proteome changes between superhybrid rice LYP9 and its parents at different developmental stages
    • Zhang, C. Y. et al. Comparative proteomic study reveals dynamic proteome changes between superhybrid rice LYP9 and its parents at different developmental stages. J. Plant Physiol. 169, 387-398 (2012).
    • (2012) J. Plant Physiol. , vol.169 , pp. 387-398
    • Zhang, C.Y.1
  • 68
    • 84872135198 scopus 로고    scopus 로고
    • Source-sink dynamics and proteomic reprogramming under elevated night temperature and their impact on rice yield and grain quality
    • Shi, W. J. et al. Source-sink dynamics and proteomic reprogramming under elevated night temperature and their impact on rice yield and grain quality. New Phytol. 197, 825-837 (2013).
    • (2013) New Phytol. , vol.197 , pp. 825-837
    • Shi, W.J.1
  • 69
    • 84896781265 scopus 로고    scopus 로고
    • Quantitative proteomics reveals the role of protein phosphorylation in rice embryos during early stages of germination
    • Han, C., Yang, P. F., Sakata, K., Komatsu, S. Quantitative proteomics reveals the role of protein phosphorylation in rice embryos during early stages of germination. J. Proteome Res. 13, 1766-1782 (2014).
    • (2014) J. Proteome Res. , vol.13 , pp. 1766-1782
    • Han, C.1    Yang, P.F.2    Sakata, K.3    Komatsu, S.4
  • 70
    • 84911868356 scopus 로고    scopus 로고
    • A proteomic analysis of rice seed germination as affected by high temperature and ABA treatment
    • Liu, S. J. et al. A proteomic analysis of rice seed germination as affected by high temperature and ABA treatment. Physiol. Plant (2014).
    • (2014) Physiol. Plant
    • Liu, S.J.1
  • 71
    • 70450173107 scopus 로고    scopus 로고
    • Proteasome regulation, plant growth and stress tolerance
    • Kurepa, J., Wang, S., Li, Y., Smalle, J. Proteasome regulation, plant growth and stress tolerance. Plant Signal. Behav. 4, 924-927 (2009).
    • (2009) Plant Signal. Behav. , vol.4 , pp. 924-927
    • Kurepa, J.1    Wang, S.2    Li, Y.3    Smalle, J.4
  • 72
    • 84903177385 scopus 로고    scopus 로고
    • The membrane proteome of Medicago truncatula roots displays qualitative and quantitative changes in response to arbuscular mycorrhizal symbiosis
    • Abdallah, C. et al. The membrane proteome of Medicago truncatula roots displays qualitative and quantitative changes in response to arbuscular mycorrhizal symbiosis. J. Proteomics 108, 354-368 (2014).
    • (2014) J. Proteomics , vol.108 , pp. 354-368
    • Abdallah, C.1
  • 73
    • 84905044798 scopus 로고    scopus 로고
    • Drought stress provokes the down-regulation of methionine and ethylene biosynthesis pathways in Medicago truncatula roots and nodules
    • Larrainzar, E. et al. Drought stress provokes the down-regulation of methionine and ethylene biosynthesis pathways in Medicago truncatula roots and nodules. Plant Cell Environ. 37, 2051-2063 (2014).
    • (2014) Plant Cell Environ. , vol.37 , pp. 2051-2063
    • Larrainzar, E.1
  • 74
    • 84904910775 scopus 로고    scopus 로고
    • Metaproteomic identification of diazotrophic methanotrophs and their localization in root tissues of field-grown rice plants
    • Bao, Z. et al. Metaproteomic identification of diazotrophic methanotrophs and their localization in root tissues of field-grown rice plants. Appl. Environ. Microbiol. 80, 5043-5052 (2014).
    • (2014) Appl. Environ. Microbiol. , vol.80 , pp. 5043-5052
    • Bao, Z.1
  • 75
    • 84885113180 scopus 로고    scopus 로고
    • Emerging roles for diverse intramembrane proteases in plant biology
    • Adam, Z. Emerging roles for diverse intramembrane proteases in plant biology. Biochim. Biophys. Acta 1828, 2933-2936 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 2933-2936
    • Adam, Z.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.