메뉴 건너뛰기




Volumn 4, Issue JUN, 2013, Pages

Fluorescent protein tagging as a tool to define the subcellular distribution of proteins in plants

Author keywords

Arabidopsis; Database; FP tagging; Subcellular localization; Subcellular proteomics

Indexed keywords


EID: 84887555324     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2013.00214     Document Type: Review
Times cited : (65)

References (89)
  • 1
    • 2342525212 scopus 로고    scopus 로고
    • A mutation of the CRUMPLED LEAF gene that encodes a protein localized in the outer envelope membrane of plastids affects the pattern of cell division, cell differentiation, and plastid division in Arabidopsis
    • doi: 10.1111/j.1365-313X.2004.02057.x
    • Asano, T., Yoshioka, Y., Kurei, S., Sakamoto, W., and Machida, Y. (2004). A mutation of the CRUMPLED LEAF gene that encodes a protein localized in the outer envelope membrane of plastids affects the pattern of cell division, cell differentiation, and plastid division in Arabidopsis. Plant J. 38, 448-459. doi: 10.1111/j.1365-313X.2004.02057.x
    • (2004) Plant J. , vol.38 , pp. 448-459
    • Asano, T.1    Yoshioka, Y.2    Kurei, S.3    Sakamoto, W.4    McHida, Y.5
  • 2
    • 0345167799 scopus 로고    scopus 로고
    • Local, efflux-dependent auxin gradients as a common module for plant organ formation
    • doi: 10.1016/S0092-8674(03)00924-3
    • Benkova, E., Michniewicz, M., Sauer, M., Teichmann, T., Seifertova, D., Jurgens, G., et al. (2003). Local, efflux-dependent auxin gradients as a common module for plant organ formation. Cell 115, 591-602. doi: 10.1016/S0092-8674(03)00924-3
    • (2003) Cell , vol.115 , pp. 591-602
    • Benkova, E.1    Michniewicz, M.2    Sauer, M.3    Teichmann, T.4    Seifertova, D.5    Jurgens, G.6
  • 3
    • 37249058912 scopus 로고    scopus 로고
    • Fluorescent protein applications in plants
    • doi: 10.1016/S0091-679X(08)85008-X
    • Berg, R. H., and Beachy, R. N. (2008). Fluorescent protein applications in plants. Method Cell Biol. 85, 153-177. doi: 10.1016/S0091-679X(08)85008-X
    • (2008) Method Cell Biol. , vol.85 , pp. 153-177
    • Berg, R.H.1    Beachy, R.N.2
  • 4
    • 77954274687 scopus 로고    scopus 로고
    • YLoc-an interpretable web server for predicting subcellular localization
    • doi: 10.1093/nar/gkq477
    • Briesemeister, S., Rahnenfuhrer, J., and Kohlbacher, O. (2010). YLoc-an interpretable web server for predicting subcellular localization. Nucleic Acids Res. 38, W497-W502. doi: 10.1093/nar/gkq477
    • (2010) Nucleic Acids Res. , vol.38
    • Briesemeister, S.1    Rahnenfuhrer, J.2    Kohlbacher, O.3
  • 5
    • 3242773053 scopus 로고    scopus 로고
    • The hydrophobic proteome of mitochondrial membranes from Arabidopsis cell suspensions
    • doi: 10.1016/j.phytochem.2004.03.028
    • Brugiere, S., Kowalski, S., Ferro, M., Seigneurin-Berny, D., Miras, S., Salvi, D., et al. (2004). The hydrophobic proteome of mitochondrial membranes from Arabidopsis cell suspensions. Phytochemistry 65, 1693-1707. doi: 10.1016/j.phytochem.2004.03.028
    • (2004) Phytochemistry , vol.65 , pp. 1693-1707
    • Brugiere, S.1    Kowalski, S.2    Ferro, M.3    Seigneurin-Berny, D.4    Miras, S.5    Salvi, D.6
  • 6
    • 62149097250 scopus 로고    scopus 로고
    • Approaches to defining dual-targeted proteins in Arabidopsis
    • doi: 10.1111/j.1365-313X.2008.03745.x
    • Carrie, C., Kuhn, K., Murcha, M. W., Duncan, O., Small, I. D., O'Toole, N., et al. (2009). Approaches to defining dual-targeted proteins in Arabidopsis. Plant J. 57, 1128-1139. doi: 10.1111/j.1365-313X.2008.03745.x
    • (2009) Plant J. , vol.57 , pp. 1128-1139
    • Carrie, C.1    Kuhn, K.2    Murcha, M.W.3    Duncan, O.4    Small, I.D.5    O'Toole, N.6
  • 7
    • 49649083497 scopus 로고    scopus 로고
    • Type II NAD(P)H dehydrogenases are targeted to mitochondria and chloroplasts or peroxisomes in Arabidopsis thaliana
    • doi: 10.1016/j.febslet.2008.07.061
    • Carrie, C., Murcha, M. W., Kuehn, K., Duncan, O., Barthet, M., Smith, P. M., et al. (2008). Type II NAD(P)H dehydrogenases are targeted to mitochondria and chloroplasts or peroxisomes in Arabidopsis thaliana. FEBS Lett. 582, 3073-3079. doi: 10.1016/j.febslet.2008.07.061
    • (2008) FEBS Lett. , vol.582 , pp. 3073-3079
    • Carrie, C.1    Murcha, M.W.2    Kuehn, K.3    Duncan, O.4    Barthet, M.5    Smith, P.M.6
  • 8
    • 84871779194 scopus 로고    scopus 로고
    • A reevaluation of dual-targeting of proteins to mitochondria and chloroplasts
    • doi: 10.1016/j.bbamcr.2012.05.029
    • Carrie, C., and Small, I. (2012). A reevaluation of dual-targeting of proteins to mitochondria and chloroplasts. Biochim. Biophys. Acta. 1833, 253-259. doi: 10.1016/j.bbamcr.2012.05.029
    • (2012) Biochim. Biophys. Acta. , vol.1833 , pp. 253-259
    • Carrie, C.1    Small, I.2
  • 9
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • doi: 10.1126/science.8303295
    • Chalfie, M., Tu, Y., Euskirchen, G., Ward, W. W., and Prasher, D. C. (1994). Green fluorescent protein as a marker for gene expression. Science 263, 802-805. doi: 10.1126/science.8303295
    • (1994) Science , vol.263 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 10
    • 0033602387 scopus 로고    scopus 로고
    • Structural elements required for the localization of ASH1 mRNA and of a green fluorescent protein reporter particle in vivo
    • doi: 10.1016/S0960-9822(99)80144-4
    • Chartrand, P., Meng, X. H., Singer, R. H., and Long, R. M. (1999). Structural elements required for the localization of ASH1 mRNA and of a green fluorescent protein reporter particle in vivo. Curr. Biol. 9, 333-336. doi: 10.1016/S0960-9822(99)80144-4
    • (1999) Curr. Biol. , vol.9 , pp. 333-336
    • Chartrand, P.1    Meng, X.H.2    Singer, R.H.3    Long, R.M.4
  • 11
    • 1642532372 scopus 로고    scopus 로고
    • A plant outer mitochondrial membrane protein with high amino acid sequence identity to a chloroplast protein import receptor
    • doi: 10.1016/S0014-5793(03)01457-1
    • Chew, O., Lister, R., Qbadou, S., Heazlewood, J. L., Soll, J., Schleiff, E., et al. (2004). A plant outer mitochondrial membrane protein with high amino acid sequence identity to a chloroplast protein import receptor. FEBS Lett. 557, 109-114. doi: 10.1016/S0014-5793(03)01457-1
    • (2004) FEBS Lett. , vol.557 , pp. 109-114
    • Chew, O.1    Lister, R.2    Qbadou, S.3    Heazlewood, J.L.4    Soll, J.5    Schleiff, E.6
  • 12
    • 0346669752 scopus 로고    scopus 로고
    • Characterization of the targeting signal of dual-targeted pea glutathione reductase
    • doi: 10.1023/B:PLAN.0000006939.87660.4f
    • Chew, O., Rudhe, C., Glaser, E., and Whelan, J. (2003). Characterization of the targeting signal of dual-targeted pea glutathione reductase. Plant Mol. Biol. 53, 341-356. doi: 10.1023/B:PLAN.0000006939.87660.4f
    • (2003) Plant Mol. Biol. , vol.53 , pp. 341-356
    • Chew, O.1    Rudhe, C.2    Glaser, E.3    Whelan, J.4
  • 13
    • 77956199192 scopus 로고    scopus 로고
    • Plant-mPLoc: A top-down strategy to augment the power for predicting plant protein subcellular localization
    • doi: 10.1371/journal.pone.0011335
    • Chou, K. C., and Shen, H. B. (2010). Plant-mPLoc: a top-down strategy to augment the power for predicting plant protein subcellular localization. PLoS ONE 5:e11335. doi: 10.1371/journal.pone.0011335
    • (2010) PLoS ONE , vol.5
    • Chou, K.C.1    Shen, H.B.2
  • 14
    • 0034724178 scopus 로고    scopus 로고
    • Random GFP: CDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at a high frequency
    • doi: 10.1073/pnas.97.7.3718
    • Cutler, S. R., Ehrhardt, D. W., Griffitts, J. S., and Somerville, C. R. (2000). Random GFP: cDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at a high frequency. Proc. Natl. Acad. Sci. U.S.A. 97, 3718-3723. doi: 10.1073/pnas.97.7.3718
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 3718-3723
    • Cutler, S.R.1    Ehrhardt, D.W.2    Griffitts, J.S.3    Somerville, C.R.4
  • 15
    • 77951985351 scopus 로고    scopus 로고
    • Illuminating plant biology: Using fluorescent proteins for high-throughput analysis of protein localization and function in plants
    • doi: 10.1093/bfgp/elp060
    • Deblasio, S. L., Sylvester, A. W., and Jackson, D. (2010). Illuminating plant biology: using fluorescent proteins for high-throughput analysis of protein localization and function in plants. Brief. Funct. Genom. 9, 129-138. doi: 10.1093/bfgp/elp060
    • (2010) Brief. Funct. Genom. , vol.9 , pp. 129-138
    • Deblasio, S.L.1    Sylvester, A.W.2    Jackson, D.3
  • 16
    • 33644853883 scopus 로고    scopus 로고
    • Using intrinsically fluorescent proteins for plant cell imaging
    • doi: 10.1111/j.1365-313X.2006.02658.x
    • Dixit, R., Cyr, R., and Gilroy, S. (2006). Using intrinsically fluorescent proteins for plant cell imaging. Plant J. 45, 599-615. doi: 10.1111/j.1365-313X.2006.02658.x
    • (2006) Plant J. , vol.45 , pp. 599-615
    • Dixit, R.1    Cyr, R.2    Gilroy, S.3
  • 17
    • 28044436758 scopus 로고    scopus 로고
    • Dual targeting is the rule for organellar aminoacyl-tRNA synthetases in Arabidopsis thaliana
    • doi: 10.1073/pnas.0504682102
    • Duchene, A. M., Giritch, A., Hoffmann, B., Cognat, V., Lancelin, D., Peeters, N. M., et al. (2005). Dual targeting is the rule for organellar aminoacyl-tRNA synthetases in Arabidopsis thaliana. Proc. Natl. Acad. Sci. U.S.A. 102, 16484-16489. doi: 10.1073/pnas.0504682102
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 16484-16489
    • Duchene, A.M.1    Giritch, A.2    Hoffmann, B.3    Cognat, V.4    Lancelin, D.5    Peeters, N.M.6
  • 18
    • 0344531517 scopus 로고    scopus 로고
    • GFP technology for live cell imaging
    • doi: 10.1016/j.pbi.2003.09.014
    • Ehrhardt, D. (2003). GFP technology for live cell imaging. Curr. Opin. Plant Biol. 6, 622-628. doi: 10.1016/j.pbi.2003.09.014
    • (2003) Curr. Opin. Plant Biol. , vol.6 , pp. 622-628
    • Ehrhardt, D.1
  • 19
    • 0038381715 scopus 로고    scopus 로고
    • High-throughput viral expression of cDNA-green fluorescent protein fusions reveals novel subcellular addresses and identifies unique proteins that interact with plasmodesmata
    • doi: 10.1105/tpc.013284
    • Escobar, N. M., Haupt, S., Thow, G., Boevink, P., Chapman, S., and Oparka, K. (2003). High-throughput viral expression of cDNA-green fluorescent protein fusions reveals novel subcellular addresses and identifies unique proteins that interact with plasmodesmata. Plant Cell. 15, 1507-1523. doi: 10.1105/tpc.013284
    • (2003) Plant Cell. , vol.15 , pp. 1507-1523
    • Escobar, N.M.1    Haupt, S.2    Thow, G.3    Boevink, P.4    Chapman, S.5    Oparka, K.6
  • 20
    • 57749104780 scopus 로고    scopus 로고
    • Novel proteins, putative membrane transporters, and an integrated metabolic network are revealed by quantitative proteomic analysis of Arabidopsis cell culture peroxisomes
    • doi: 10.1104/pp.108.129999
    • Eubel, H., Meyer, E. H., Taylor, N. L., Bussell, J. D., O'Toole, N., Heazlewood, J. L., et al. (2008). Novel proteins, putative membrane transporters, and an integrated metabolic network are revealed by quantitative proteomic analysis of Arabidopsis cell culture peroxisomes. Plant Physiol. 148, 1809-1829. doi: 10.1104/pp.108.129999
    • (2008) Plant Physiol. , vol.148 , pp. 1809-1829
    • Eubel, H.1    Meyer, E.H.2    Taylor, N.L.3    Bussell, J.D.4    O'Toole, N.5    Heazlewood, J.L.6
  • 21
    • 77953149231 scopus 로고    scopus 로고
    • AT_CHLORO, a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins
    • doi: 10.1074/mcp.M900325-MCP200
    • Ferro, M., Brugiere, S., Salvi, D., Seigneurin-Berny, D., Court, M., Moyet, L., et al. (2010). AT_CHLORO, a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins. Mol. Cell Proteome. 9, 1063-1084. doi: 10.1074/mcp.M900325-MCP200
    • (2010) Mol. Cell Proteome. , vol.9 , pp. 1063-1084
    • Ferro, M.1    Brugiere, S.2    Salvi, D.3    Seigneurin-Berny, D.4    Court, M.5    Moyet, L.6
  • 22
    • 33745941352 scopus 로고    scopus 로고
    • Quantitative fluorescence microscopy: From art to science
    • doi: 10.1146/annurev.arplant.57.032905.105239
    • Fricker, M., Runions, J., and Moore, I. (2006). Quantitative fluorescence microscopy: from art to science. Annu. Rev. Plant Biol. 57, 79-107. doi: 10.1146/annurev.arplant.57.032905.105239
    • (2006) Annu. Rev. Plant Biol. , vol.57 , pp. 79-107
    • Fricker, M.1    Runions, J.2    Moore, I.3
  • 23
    • 1042279117 scopus 로고    scopus 로고
    • In-depth analysis of the thylakoid membrane proteome of Arabidopsis thaliana chloroplasts: New proteins, new functions, and a plastid proteome database
    • doi: 10.1105/tpc.017814
    • Friso, G., Giacomelli, L., Ytterberg, A. J., Peltier, J. B., Rudella, A., Sun, Q., et al. (2004). In-depth analysis of the thylakoid membrane proteome of Arabidopsis thaliana chloroplasts: new proteins, new functions, and a plastid proteome database. Plant Cell 16, 478-499. doi: 10.1105/tpc.017814
    • (2004) Plant Cell , vol.16 , pp. 478-499
    • Friso, G.1    Giacomelli, L.2    Ytterberg, A.J.3    Peltier, J.B.4    Rudella, A.5    Sun, Q.6
  • 24
    • 0041733229 scopus 로고    scopus 로고
    • Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis
    • doi: 10.1021/pr034025j
    • Froehlich, J. E., Wilkerson, C. G., Ray, W. K., McAndrew, R. S., Osteryoung, K. W., Gage, D. A., et al. (2003). Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis. J. Proteome. Res. 2, 413-425. doi: 10.1021/pr034025j
    • (2003) J. Proteome. Res. , vol.2 , pp. 413-425
    • Froehlich, J.E.1    Wilkerson, C.G.2    Ray, W.K.3    McAndrew, R.S.4    Osteryoung, K.W.5    Gage, D.A.6
  • 25
    • 0037389632 scopus 로고    scopus 로고
    • ARC5, a cytosolic dynamin-like protein from plants, is part of the chloroplast division machinery
    • doi: 10.1073/pnas.0530206100
    • Gao, H., Kadirjan-Kalbach, D., Froehlich, J. E., and Osteryoung, K. W. (2003). ARC5, a cytosolic dynamin-like protein from plants, is part of the chloroplast division machinery. Proc. Natl. Acad. Sci. U.S.A. 100, 4328-4333. doi: 10.1073/pnas.0530206100
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 4328-4333
    • Gao, H.1    Kadirjan-Kalbach, D.2    Froehlich, J.E.3    Osteryoung, K.W.4
  • 26
    • 0042972780 scopus 로고    scopus 로고
    • Control of cellulose synthase complex localization in developing xylem
    • doi: 10.1105/tpc.012815
    • Gardiner, J. C., Taylor, N. G., and Turner, S. R. (2003). Control of cellulose synthase complex localization in developing xylem. Plant Cell 15, 1740-1748. doi: 10.1105/tpc.012815
    • (2003) Plant Cell , vol.15 , pp. 1740-1748
    • Gardiner, J.C.1    Taylor, N.G.2    Turner, S.R.3
  • 27
    • 33745659672 scopus 로고    scopus 로고
    • High light response of the thylakoid proteome in arabidopsis wild type and the ascorbate-deficient mutant vtc2-2. A comparative proteomics study
    • doi: 10.1104/pp.106.080150
    • Giacomelli, L., Rudella, A., and Van Wijk, K. J. (2006). High light response of the thylakoid proteome in arabidopsis wild type and the ascorbate-deficient mutant vtc2-2. A comparative proteomics study. Plant Physiol. 141, 685-701. doi: 10.1104/pp.106.080150
    • (2006) Plant Physiol. , vol.141 , pp. 685-701
    • Giacomelli, L.1    Rudella, A.2    Van Wijk, K.J.3
  • 28
    • 79961005037 scopus 로고    scopus 로고
    • Clustering of MS spectra for improved protein identification rate and screening for protein variants and modifications by MALDI-MS/MS
    • doi: 10.1016/j.jprot.2011.04.008
    • Granlund, I., Kieselbach, T., Alm, R., Schroder, W. P., and Emanuelsson, C. (2011). Clustering of MS spectra for improved protein identification rate and screening for protein variants and modifications by MALDI-MS/MS. J. Proteom. 74, 1190-1200. doi: 10.1016/j.jprot.2011.04.008
    • (2011) J. Proteom. , vol.74 , pp. 1190-1200
    • Granlund, I.1    Kieselbach, T.2    Alm, R.3    Schroder, W.P.4    Emanuelsson, C.5
  • 29
    • 79953081860 scopus 로고    scopus 로고
    • An Arabidopsis dual-localized pentatricopeptide repeat protein interacts with nuclear proteins involved in gene expression regulation
    • doi: 10.1105/tpc.110.081638
    • Hammani, K., Gobert, A., Hleibieh, K., Choulier, L., Small, I., and Giege, P. (2011). An Arabidopsis dual-localized pentatricopeptide repeat protein interacts with nuclear proteins involved in gene expression regulation. Plant Cell 23, 730-740. doi: 10.1105/tpc.110.081638
    • (2011) Plant Cell , vol.23 , pp. 730-740
    • Hammani, K.1    Gobert, A.2    Hleibieh, K.3    Choulier, L.4    Small, I.5    Giege, P.6
  • 30
    • 0034971120 scopus 로고    scopus 로고
    • GFP imaging: Methodology and application to investigate cellular compartmentation in plants
    • doi: 10.1093/jexbot/52.356.529
    • Hanson, M. R., and Kohler, R. H. (2001). GFP imaging: methodology and application to investigate cellular compartmentation in plants. J. Exp. Bot. 52, 529-539. doi: 10.1093/jexbot/52.356.529
    • (2001) J. Exp. Bot. , vol.52 , pp. 529-539
    • Hanson, M.R.1    Kohler, R.H.2
  • 31
    • 0030989517 scopus 로고    scopus 로고
    • Removal of a cryptic intron and subcellular localization of green fluorescent protein are required to mark transgenic Arabidopsis plants brightly
    • doi: 10.1073/pnas.94.6.2122
    • Haseloff, J., Siemering, K. R., Prasher, D. C., and Hodge, S. (1997). Removal of a cryptic intron and subcellular localization of green fluorescent protein are required to mark transgenic Arabidopsis plants brightly. Proc. Natl. Acad. Sci. U.S.A. 94, 2122-2127. doi: 10.1073/pnas.94.6.2122
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 2122-2127
    • Haseloff, J.1    Siemering, K.R.2    Prasher, D.C.3    Hodge, S.4
  • 32
    • 33644649331 scopus 로고    scopus 로고
    • Combining experimental and predicted datasets for determination of the subcellular location of proteins in Arabidopsis
    • doi: 10.1104/pp.105.065532
    • Heazlewood, J. L., Tonti-Filippini, J., Verboom, R. E., and Millar, A. H. (2005). Combining experimental and predicted datasets for determination of the subcellular location of proteins in Arabidopsis. Plant Physiol. 139, 598-609. doi: 10.1104/pp.105.065532
    • (2005) Plant Physiol. , vol.139 , pp. 598-609
    • Heazlewood, J.L.1    Tonti-Filippini, J.2    Verboom, R.E.3    Millar, A.H.4
  • 34
    • 0025181843 scopus 로고
    • The sn-1, 2-diacylglycerol cholinephosphotransferase of Saccharomyces cerevisiae. Nucleotide sequence, transcriptional mapping, and gene product analysis of the CPT1 gene
    • Hjelmstad, R. H., and Bell, R. M. (1990). The sn-1, 2-diacylglycerol cholinephosphotransferase of Saccharomyces cerevisiae. Nucleotide sequence, transcriptional mapping, and gene product analysis of the CPT1 gene. J. Biol. Chem. 265, 1755-1764.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1755-1764
    • Hjelmstad, R.H.1    Bell, R.M.2
  • 35
    • 84866872610 scopus 로고    scopus 로고
    • GFP-tagging of Arabidopsis acyl-activating enzymes raises the issue of peroxisome-chloroplast import competition versus dual localization
    • doi: 10.1016/j.jplph.2012.05.026
    • Hooks, K. B., Turner, J. E., Graham, I. A., Runions, J., and Hooks, M. A. (2012). GFP-tagging of Arabidopsis acyl-activating enzymes raises the issue of peroxisome-chloroplast import competition versus dual localization. J. Plant Physiol. 169, 1631-1638. doi: 10.1016/j.jplph.2012.05.026
    • (2012) J. Plant Physiol. , vol.169 , pp. 1631-1638
    • Hooks, K.B.1    Turner, J.E.2    Graham, I.A.3    Runions, J.4    Hooks, M.A.5
  • 37
    • 0142184341 scopus 로고    scopus 로고
    • Global analysis of protein localization in budding yeast
    • doi: 10.1038/nature02026
    • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., et al. (2003). Global analysis of protein localization in budding yeast. Nature 425, 686-691. doi: 10.1038/nature02026
    • (2003) Nature , vol.425 , pp. 686-691
    • Huh, W.K.1    Falvo, J.V.2    Gerke, L.C.3    Carroll, A.S.4    Howson, R.W.5    Weissman, J.S.6
  • 38
    • 79953708576 scopus 로고    scopus 로고
    • Analysis of the Arabidopsis cytosolic proteome highlights subcellular partitioning of central plant metabolism
    • doi: 10.1021/pr1009433
    • Ito, J., Batth, T. S., Petzold, C. J., Redding-Johanson, A. M., Mukhopadhyay, A., Verboom, R., et al. (2011). Analysis of the Arabidopsis cytosolic proteome highlights subcellular partitioning of central plant metabolism. J. Proteome Res. 10, 1571-1582. doi: 10.1021/pr1009433
    • (2011) J. Proteome Res. , vol.10 , pp. 1571-1582
    • Ito, J.1    Batth, T.S.2    Petzold, C.J.3    Redding-Johanson, A.M.4    Mukhopadhyay, A.5    Verboom, R.6
  • 39
    • 34147149761 scopus 로고    scopus 로고
    • A proteomics dissection of Arabidopsis thaliana vacuoles isolated from cell culture
    • doi: 10.1074/mcp.M600250-MCP200
    • Jaquinod, M., Villiers, F., Kieffer-Jaquinod, S., Hugouvieux, V., Bruley, C., Garin, J., et al. (2007). A proteomics dissection of Arabidopsis thaliana vacuoles isolated from cell culture. Mol. Cell Proteom. 6, 394-412. doi: 10.1074/mcp.M600250-MCP200
    • (2007) Mol. Cell Proteom. , vol.6 , pp. 394-412
    • Jaquinod, M.1    Villiers, F.2    Kieffer-Jaquinod, S.3    Hugouvieux, V.4    Bruley, C.5    Garin, J.6
  • 40
    • 0141502074 scopus 로고    scopus 로고
    • Developmental regulation and significance of KNOX protein trafficking in Arabidopsis
    • doi: 10.1242/dev.00618
    • Kim, J. Y., Yuan, Z., and Jackson, D. (2003). Developmental regulation and significance of KNOX protein trafficking in Arabidopsis. Development 130, 4351-4362. doi: 10.1242/dev.00618
    • (2003) Development , vol.130 , pp. 4351-4362
    • Kim, J.Y.1    Yuan, Z.2    Jackson, D.3
  • 41
    • 1842432608 scopus 로고    scopus 로고
    • The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions
    • doi: 10.1016/j.cub.2004.02.039
    • Kleffmann, T., Russenberger, D., Von Zychlinski, A., Christopher, W., Sjolander, K., Gruissem, W., et al. (2004). The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions. Curr. Biol. 14, 354-362. doi: 10.1016/j.cub.2004.02.039
    • (2004) Curr. Biol. , vol.14 , pp. 354-362
    • Kleffmann, T.1    Russenberger, D.2    Von Zychlinski, A.3    Christopher, W.4    Sjolander, K.5    Gruissem, W.6
  • 42
    • 80053594838 scopus 로고    scopus 로고
    • Defining the protein complex proteome of plant mitochondria
    • doi: 10.1104/pp.111.182352
    • Klodmann, J., Senkler, M., Rode, C., and Braun, H. P. (2011). Defining the protein complex proteome of plant mitochondria. Plant Physiol. 157, 587-598. doi: 10.1104/pp.111.182352
    • (2011) Plant Physiol. , vol.157 , pp. 587-598
    • Klodmann, J.1    Senkler, M.2    Rode, C.3    Braun, H.P.4
  • 43
    • 11144287643 scopus 로고    scopus 로고
    • High-throughput protein localization in Arabidopsis using Agrobacterium-mediated transient expression of GFP-ORF fusions
    • doi: 10.1111/j.1365-313X.2004.02281.x
    • Koroleva, O. A., Tomlinson, M. L., Leader, D., Shaw, P., and Doonan, J. H. (2005). High-throughput protein localization in Arabidopsis using Agrobacterium-mediated transient expression of GFP-ORF fusions. Plant J. 41, 162-174. doi: 10.1111/j.1365-313X.2004.02281.x
    • (2005) Plant J. , vol.41 , pp. 162-174
    • Koroleva, O.A.1    Tomlinson, M.L.2    Leader, D.3    Shaw, P.4    Doonan, J.H.5
  • 44
    • 0032750815 scopus 로고    scopus 로고
    • Viral movement proteins as probes for intracellular and intercellular trafficking in plants
    • Lazarowitz, S. G., and Beachy, R. N. (1999). Viral movement proteins as probes for intracellular and intercellular trafficking in plants. Plant Cell 11, 535-548.
    • (1999) Plant Cell , vol.11 , pp. 535-548
    • Lazarowitz, S.G.1    Beachy, R.N.2
  • 45
    • 79958172874 scopus 로고    scopus 로고
    • Combining proteomics of root and shoot mitochondria and transcript analysis to define constitutive and variable components in plant mitochondria
    • doi: 10.1016/j.phytochem.2010.12.004
    • Lee, C. P., Eubel, H., O'Toole, N., and Millar, A. H. (2011). Combining proteomics of root and shoot mitochondria and transcript analysis to define constitutive and variable components in plant mitochondria. Phytochemistry 72, 1092-1108. doi: 10.1016/j.phytochem.2010.12.004
    • (2011) Phytochemistry , vol.72 , pp. 1092-1108
    • Lee, C.P.1    Eubel, H.2    O'Toole, N.3    Millar, A.H.4
  • 46
    • 84857950653 scopus 로고    scopus 로고
    • The functional network of the Arabidopsis plastoglobule proteome based on quantitative proteomics and genome-wide coexpression analysis
    • doi: 10.1104/pp.111.193144
    • Lundquist, P. K., Poliakov, A., Bhuiyan, N. H., Zybailov, B., Sun, Q., and Van Wijk, K. J. (2012). The functional network of the Arabidopsis plastoglobule proteome based on quantitative proteomics and genome-wide coexpression analysis. Plant Physiol. 158, 1172-1192. doi: 10.1104/pp.111.193144
    • (2012) Plant Physiol. , vol.158 , pp. 1172-1192
    • Lundquist, P.K.1    Poliakov, A.2    Bhuiyan, N.H.3    Zybailov, B.4    Sun, Q.5    Van Wijk, K.J.6
  • 47
    • 4043172772 scopus 로고    scopus 로고
    • Genome-wide analysis of Arabidopsis pentatricopeptide repeat proteins reveals their essential role in organelle biogenesis
    • doi: 10.1105/tpc.104.022236
    • Lurin, C., Andres, C., Aubourg, S., Bellaoui, M., Bitton, F., Bruyere, C., et al. (2004). Genome-wide analysis of Arabidopsis pentatricopeptide repeat proteins reveals their essential role in organelle biogenesis. Plant Cell 16, 2089-2103. doi: 10.1105/tpc.104.022236
    • (2004) Plant Cell , vol.16 , pp. 2089-2103
    • Lurin, C.1    Andres, C.2    Aubourg, S.3    Bellaoui, M.4    Bitton, F.5    Bruyere, C.6
  • 48
    • 2342539053 scopus 로고    scopus 로고
    • An Arabidopsis dynamin-related protein, DRP3A, controls both peroxisomal and mitochondrial division
    • doi: 10.1111/j.1365-313X.2004.02063.x
    • Mano, S., Nakamori, C., Kondo, M., Hayashi, M., and Nishimura, M. (2004). An Arabidopsis dynamin-related protein, DRP3A, controls both peroxisomal and mitochondrial division. Plant J. 38, 487-498. doi: 10.1111/j.1365-313X.2004.02063.x
    • (2004) Plant J. , vol.38 , pp. 487-498
    • Mano, S.1    Nakamori, C.2    Kondo, M.3    Hayashi, M.4    Nishimura, M.5
  • 49
    • 52649132375 scopus 로고    scopus 로고
    • Systematic analysis of protein subcellular localization and interaction using high-throughput transient transformation of Arabidopsis seedlings
    • doi: 10.1111/j.1365-313X.2008.03596.x
    • Marion, J., Bach, L., Bellec, Y., Meyer, C., Gissot, L., and Faure, J. D. (2008). Systematic analysis of protein subcellular localization and interaction using high-throughput transient transformation of Arabidopsis seedlings. Plant J. 56, 169-179. doi: 10.1111/j.1365-313X.2008.03596.x
    • (2008) Plant J. , vol.56 , pp. 169-179
    • Marion, J.1    Bach, L.2    Bellec, Y.3    Meyer, C.4    Gissot, L.5    Faure, J.D.6
  • 50
    • 39749155929 scopus 로고    scopus 로고
    • Resolving and identifying protein components of plant mitochondrial respiratory complexes using three dimensions of gel electrophoresis
    • doi: 10.1021/pr700595p
    • Meyer, E. H., Taylor, N. L., and Millar, A. H. (2008). Resolving and identifying protein components of plant mitochondrial respiratory complexes using three dimensions of gel electrophoresis. J. Proteome Res. 7, 786-794. doi: 10.1021/pr700595p
    • (2008) J. Proteome Res. , vol.7 , pp. 786-794
    • Meyer, E.H.1    Taylor, N.L.2    Millar, A.H.3
  • 51
    • 38449110969 scopus 로고    scopus 로고
    • Transient expression of fluorescent fusion proteins in protoplasts of suspension cultured cells
    • doi: 10.1038/nprot.2007.360
    • Miao, Y., and Jiang, L. (2007). Transient expression of fluorescent fusion proteins in protoplasts of suspension cultured cells. Nat. Protoc. 2, 2348-2353. doi: 10.1038/nprot.2007.360
    • (2007) Nat. Protoc. , vol.2 , pp. 2348-2353
    • Miao, Y.1    Jiang, L.2
  • 52
    • 0142152465 scopus 로고    scopus 로고
    • Arabidopsis genes encoding mitochondrial type II NAD(P)H dehydrogenases have different evolutionary origin and show distinct responses to light
    • doi: 10.1104/pp.103.024208
    • Michalecka, A. M., Svensson, A. S., Johansson, F. I., Agius, S. C., Johanson, U., Brennicke, A., et al. (2003). Arabidopsis genes encoding mitochondrial type II NAD(P)H dehydrogenases have different evolutionary origin and show distinct responses to light. Plant Physiol. 133, 642-652. doi: 10.1104/pp.103.024208
    • (2003) Plant Physiol. , vol.133 , pp. 642-652
    • Michalecka, A.M.1    Svensson, A.S.2    Johansson, F.I.3    Agius, S.C.4    Johanson, U.5    Brennicke, A.6
  • 53
    • 70349254021 scopus 로고    scopus 로고
    • Exploring the function-location nexus: Using multiple lines of evidence in defining the subcellular location of plant proteins
    • doi: 10.1105/tpc.109.066019
    • Millar, A. H., Carrie, C., Pogson, B., and Whelan, J. (2009). Exploring the function-location nexus: using multiple lines of evidence in defining the subcellular location of plant proteins. Plant Cell 21, 1625-1631. doi: 10.1105/tpc.109.066019
    • (2009) Plant Cell , vol.21 , pp. 1625-1631
    • Millar, A.H.1    Carrie, C.2    Pogson, B.3    Whelan, J.4
  • 54
    • 0030175064 scopus 로고    scopus 로고
    • The same Arabidopsis gene encodes both cytosolic and mitochondrial alanyl-tRNA synthetases
    • Mireau, H., Lancelin, D., and Small, I. D. (1996). The same Arabidopsis gene encodes both cytosolic and mitochondrial alanyl-tRNA synthetases. Plant Cell 8, 1027-1039.
    • (1996) Plant Cell , vol.8 , pp. 1027-1039
    • Mireau, H.1    Lancelin, D.2    Small, I.D.3
  • 55
    • 67049158006 scopus 로고    scopus 로고
    • An efficient organic solvent based extraction method for the proteomic analysis of Arabidopsis plasma membranes
    • doi: 10.1021/pr801044y
    • Mitra, S. K., Walters, B. T., Clouse, S. D., and Goshe, M. B. (2009). An efficient organic solvent based extraction method for the proteomic analysis of Arabidopsis plasma membranes. J. Proteome Res. 8, 2752-2767. doi: 10.1021/pr801044y
    • (2009) J. Proteome Res. , vol.8 , pp. 2752-2767
    • Mitra, S.K.1    Walters, B.T.2    Clouse, S.D.3    Goshe, M.B.4
  • 56
    • 66649095648 scopus 로고    scopus 로고
    • Prediction of dual protein targeting to plant organelles
    • doi: 10.1111/j.1469-8137.2009.02832.x
    • Mitschke, J., Fuss, J., Blum, T., Hoglund, A., Reski, R., Kohlbacher, O., et al. (2009). Prediction of dual protein targeting to plant organelles. New Phytol. 183, 224-235. doi: 10.1111/j.1469-8137.2009.02832.x
    • (2009) New Phytol. , vol.183 , pp. 224-235
    • Mitschke, J.1    Fuss, J.2    Blum, T.3    Hoglund, A.4    Reski, R.5    Kohlbacher, O.6
  • 57
    • 33846391338 scopus 로고    scopus 로고
    • Characterization of the preprotein and amino acid transporter gene family in Arabidopsis
    • doi: 10.1104/pp.106.090688
    • Murcha, M. W., Elhafez, D., Lister, R., Tonti-Filippini, J., Baumgartner, M., Philippar, K., et al. (2007). Characterization of the preprotein and amino acid transporter gene family in Arabidopsis. Plant Physiol 143, 199-212. doi: 10.1104/pp.106.090688
    • (2007) Plant Physiol , vol.143 , pp. 199-212
    • Murcha, M.W.1    Elhafez, D.2    Lister, R.3    Tonti-Filippini, J.4    Baumgartner, M.5    Philippar, K.6
  • 58
    • 34548487513 scopus 로고    scopus 로고
    • A multicolored set of in vivo organelle markers for co-localization studies in Arabidopsis and other plants
    • doi: 10.1111/j.1365-313X.2007.03212.x
    • Nelson, B. K., Cai, X., and Nebenfuhr, A. (2007). A multicolored set of in vivo organelle markers for co-localization studies in Arabidopsis and other plants. Plant J. 51, 1126-1136. doi: 10.1111/j.1365-313X.2007.03212.x
    • (2007) Plant J. , vol.51 , pp. 1126-1136
    • Nelson, B.K.1    Cai, X.2    Nebenfuhr, A.3
  • 59
    • 77954711237 scopus 로고    scopus 로고
    • Megadalton complexes in the chloroplast stroma of Arabidopsis thaliana characterized by size exclusion chromatography, mass spectrometry, and hierarchical clustering
    • doi: 10.1074/mcp.M000038-MCP201
    • Olinares, P. D., Ponnala, L., and Van Wijk, K. J. (2010). Megadalton complexes in the chloroplast stroma of Arabidopsis thaliana characterized by size exclusion chromatography, mass spectrometry, and hierarchical clustering. Mol. Cell Proteom. 9, 1594-1615. doi: 10.1074/mcp.M000038-MCP201
    • (2010) Mol. Cell Proteom. , vol.9 , pp. 1594-1615
    • Olinares, P.D.1    Ponnala, L.2    Van Wijk, K.J.3
  • 60
    • 71449120312 scopus 로고    scopus 로고
    • Molecular identification and functional characterization of Arabidopsis thaliana mitochondrial and chloroplastic NAD+ carrier proteins
    • doi: 10.1074/jbc.M109.041830
    • Palmieri, F., Rieder, B., Ventrella, A., Blanco, E., Do, P. T., Nunes-Nesi, A., et al. (2009). Molecular identification and functional characterization of Arabidopsis thaliana mitochondrial and chloroplastic NAD+ carrier proteins. J. Biol. Chem. 284, 31249-31259. doi: 10.1074/jbc.M109.041830
    • (2009) J. Biol. Chem. , vol.284 , pp. 31249-31259
    • Palmieri, F.1    Rieder, B.2    Ventrella, A.3    Blanco, E.4    Do, P.T.5    Nunes-Nesi, A.6
  • 61
    • 0037725392 scopus 로고    scopus 로고
    • Manipulation of Rubisco: The amount, activity, function and regulation
    • doi: 10.1093/jxb/erg141
    • Parry, M. A., Andralojc, P. J., Mitchell, R. A., Madgwick, P. J., and Keys, A. J. (2003). Manipulation of Rubisco: the amount, activity, function and regulation. J. Exp. Bot. 54, 1321-1333. doi: 10.1093/jxb/erg141
    • (2003) J. Exp. Bot. , vol.54 , pp. 1321-1333
    • Parry, M.A.1    Andralojc, P.J.2    Mitchell, R.A.3    Madgwick, P.J.4    Keys, A.J.5
  • 62
    • 0035852247 scopus 로고    scopus 로고
    • Dual targeting to mitochondria and chloroplasts
    • doi: 10.1016/S0167-4889(01)00146-X
    • Peeters, N., and Small, I. (2001). Dual targeting to mitochondria and chloroplasts. Biochim. Biophys. Acta 1541, 54-63. doi: 10.1016/S0167-4889(01)00146-X
    • (2001) Biochim. Biophys. Acta , vol.1541 , pp. 54-63
    • Peeters, N.1    Small, I.2
  • 63
    • 31644438575 scopus 로고    scopus 로고
    • The oligomeric stromal proteome of Arabidopsis thaliana chloroplasts
    • doi: 10.1074/mcp.M500180-MCP200
    • Peltier, J. B., Cai, Y., Sun, Q., Zabrouskov, V., Giacomelli, L., Rudella, A., et al. (2006). The oligomeric stromal proteome of Arabidopsis thaliana chloroplasts. Mol. Cell Proteom. 5, 114-133. doi: 10.1074/mcp.M500180-MCP200
    • (2006) Mol. Cell Proteom. , vol.5 , pp. 114-133
    • Peltier, J.B.1    Cai, Y.2    Sun, Q.3    Zabrouskov, V.4    Giacomelli, L.5    Rudella, A.6
  • 64
    • 10344242448 scopus 로고    scopus 로고
    • New functions of the thylakoid membrane proteome of Arabidopsis thaliana revealed by a simple, fast, and versatile fractionation strategy
    • doi: 10.1074/jbc.M406763200
    • Peltier, J. B., Ytterberg, A. J., Sun, Q., and Van Wijk, K. J. (2004). New functions of the thylakoid membrane proteome of Arabidopsis thaliana revealed by a simple, fast, and versatile fractionation strategy. J. Biol. Chem. 279, 49367-49383. doi: 10.1074/jbc.M406763200
    • (2004) J. Biol. Chem. , vol.279 , pp. 49367-49383
    • Peltier, J.B.1    Ytterberg, A.J.2    Sun, Q.3    Van Wijk, K.J.4
  • 65
    • 79955030496 scopus 로고    scopus 로고
    • Toward a definition of the complete proteome of plant peroxisomes: Where experimental proteomics must be complemented by bioinformatics
    • doi: 10.1002/pmic.201000681
    • Reumann, S. (2011). Toward a definition of the complete proteome of plant peroxisomes: where experimental proteomics must be complemented by bioinformatics. Proteomics 11, 1764-1779. doi: 10.1002/pmic.201000681
    • (2011) Proteomics , vol.11 , pp. 1764-1779
    • Reumann, S.1
  • 66
    • 37249016441 scopus 로고    scopus 로고
    • Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting peptides, metabolic pathways, and defense mechanisms
    • doi: 10.1105/tpc.107.050989
    • Reumann, S., Babujee, L., Ma, C., Wienkoop, S., Siemsen, T., Antonicelli, G. E., et al. (2007). Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting peptides, metabolic pathways, and defense mechanisms. Plant Cell 19, 3170-3193. doi: 10.1105/tpc.107.050989
    • (2007) Plant Cell , vol.19 , pp. 3170-3193
    • Reumann, S.1    Babujee, L.2    Ma, C.3    Wienkoop, S.4    Siemsen, T.5    Antonicelli, G.E.6
  • 67
    • 66149148256 scopus 로고    scopus 로고
    • In-depth proteome analysis of Arabidopsis leaf peroxisomes combined with in vivo subcellular targeting verification indicates novel metabolic and regulatory functions of peroxisomes
    • doi: 10.1104/pp.109.137703
    • Reumann, S., Quan, S., Aung, K., Yang, P., Manandhar-Shrestha, K., Holbrook, D., et al. (2009). In-depth proteome analysis of Arabidopsis leaf peroxisomes combined with in vivo subcellular targeting verification indicates novel metabolic and regulatory functions of peroxisomes. Plant Physiol. 150, 125-143. doi: 10.1104/pp.109.137703
    • (2009) Plant Physiol. , vol.150 , pp. 125-143
    • Reumann, S.1    Quan, S.2    Aung, K.3    Yang, P.4    Manandhar-Shrestha, K.5    Holbrook, D.6
  • 68
    • 1642276286 scopus 로고    scopus 로고
    • An improved prediction of chloroplast proteins reveals diversities and commonalities in the chloroplast proteomes of Arabidopsis and rice
    • doi: 10.1016/j.gene.2004.01.008
    • Richly, E., and Leister, D. (2004). An improved prediction of chloroplast proteins reveals diversities and commonalities in the chloroplast proteomes of Arabidopsis and rice. Gene 329, 11-16. doi: 10.1016/j.gene.2004.01.008
    • (2004) Gene , vol.329 , pp. 11-16
    • Richly, E.1    Leister, D.2
  • 69
    • 0031127382 scopus 로고    scopus 로고
    • Enhanced expression in tobacco of the gene encoding green fluorescent protein by modification of its codon usage
    • doi: 10.1023/A:1005740823703
    • Rouwendal, G. J., Mendes, O., Wolbert, E. J., and Douwe De Boer, A. (1997). Enhanced expression in tobacco of the gene encoding green fluorescent protein by modification of its codon usage. Plant Mol. Biol. 33, 989-999. doi: 10.1023/A:1005740823703
    • (1997) Plant Mol. Biol. , vol.33 , pp. 989-999
    • Rouwendal, G.J.1    Mendes, O.2    Wolbert, E.J.3    Douwe De Boer, A.4
  • 70
    • 0035999898 scopus 로고    scopus 로고
    • A novel in vitro system for simultaneous import of precursor proteins into mitochondria and chloroplasts
    • doi: 10.1046/j.1365-313X.2002.01280.x
    • Rudhe, C., Chew, O., Whelan, J., and Glaser, E. (2002). A novel in vitro system for simultaneous import of precursor proteins into mitochondria and chloroplasts. Plant J. 30, 213-220. doi: 10.1046/j.1365-313X.2002.01280.x
    • (2002) Plant J. , vol.30 , pp. 213-220
    • Rudhe, C.1    Chew, O.2    Whelan, J.3    Glaser, E.4
  • 71
    • 55549091437 scopus 로고    scopus 로고
    • Quantitative proteomics of a chloroplast SRP54 sorting mutant and its genetic interactions with CLPC1 in Arabidopsis
    • doi: 10.1104/pp.108.124545
    • Rutschow, H., Ytterberg, A. J., Friso, G., Nilsson, R., and Van Wijk, K. J. (2008). Quantitative proteomics of a chloroplast SRP54 sorting mutant and its genetic interactions with CLPC1 in Arabidopsis. Plant Physiol. 148, 156-175. doi: 10.1104/pp.108.124545
    • (2008) Plant Physiol. , vol.148 , pp. 156-175
    • Rutschow, H.1    Ytterberg, A.J.2    Friso, G.3    Nilsson, R.4    Van Wijk, K.J.5
  • 72
    • 0035984061 scopus 로고    scopus 로고
    • The Arabidopsis SKU5 gene encodes an extracellular glycosyl phosphatidylinositol-anchored glycoprotein involved in directional root growth
    • doi: 10.1105/tpc.002360
    • Sedbrook, J. C., Carroll, K. L., Hung, K. F., Masson, P. H., and Somerville, C. R. (2002). The Arabidopsis SKU5 gene encodes an extracellular glycosyl phosphatidylinositol-anchored glycoprotein involved in directional root growth. Plant Cell 14, 1635-1648. doi: 10.1105/tpc.002360
    • (2002) Plant Cell , vol.14 , pp. 1635-1648
    • Sedbrook, J.C.1    Carroll, K.L.2    Hung, K.F.3    Masson, P.H.4    Somerville, C.R.5
  • 73
    • 78650990021 scopus 로고    scopus 로고
    • Plastids contain a second sec translocase system with essential functions
    • doi: 10.1104/pp.110.166546
    • Skalitzky, C. A., Martin, J. R., Harwood, J. H., Beirne, J. J., Adamczyk, B. J., Heck, G. R., et al. (2011). Plastids contain a second sec translocase system with essential functions. Plant Physiol. 155, 354-369. doi: 10.1104/pp.110.166546
    • (2011) Plant Physiol. , vol.155 , pp. 354-369
    • Skalitzky, C.A.1    Martin, J.R.2    Harwood, J.H.3    Beirne, J.J.4    Adamczyk, B.J.5    Heck, G.R.6
  • 74
    • 0032168849 scopus 로고    scopus 로고
    • Two birds with one stone: Genes that encode products targeted to two or more compartments
    • doi: 10.1023/A:1006081903354
    • Small, I., Wintz, H., Akashi, K., and Mireau, H. (1998). Two birds with one stone: genes that encode products targeted to two or more compartments. Plant Mol. Biol. 38, 265-277. doi: 10.1023/A:1006081903354
    • (1998) Plant Mol. Biol. , vol.38 , pp. 265-277
    • Small, I.1    Wintz, H.2    Akashi, K.3    Mireau, H.4
  • 75
    • 0033573157 scopus 로고    scopus 로고
    • Characterization of two bifunctional Arabdopsis thaliana genes coding for mitochondrial and cytosolic forms of valyl-tRNA synthetase and threonyl-tRNA synthetase by alternative use of two in-frame AUGs
    • doi: 10.1046/j.1432-1327.1999.00922.x
    • Souciet, G., Menand, B., Ovesna, J., Cosset, A., Dietrich, A., and Wintz, H. (1999). Characterization of two bifunctional Arabdopsis thaliana genes coding for mitochondrial and cytosolic forms of valyl-tRNA synthetase and threonyl-tRNA synthetase by alternative use of two in-frame AUGs. Eur. J. Biochem. 266, 848-854. doi: 10.1046/j.1432-1327.1999.00922.x
    • (1999) Eur. J. Biochem. , vol.266 , pp. 848-854
    • Souciet, G.1    Menand, B.2    Ovesna, J.3    Cosset, A.4    Dietrich, A.5    Wintz, H.6
  • 76
    • 77949497673 scopus 로고    scopus 로고
    • The stromal chloroplast Deg7 protease participates in the repair of photosystem II after photoinhibition in Arabidopsis
    • doi: 10.1104/pp.109.150722
    • Sun, X., Fu, T., Chen, N., Guo, J., Ma, J., Zou, M., et al. (2010). The stromal chloroplast Deg7 protease participates in the repair of photosystem II after photoinhibition in Arabidopsis. Plant Physiol. 152, 1263-1273. doi: 10.1104/pp.109.150722
    • (2010) Plant Physiol. , vol.152 , pp. 1263-1273
    • Sun, X.1    Fu, T.2    Chen, N.3    Guo, J.4    Ma, J.5    Zou, M.6
  • 77
    • 84876544295 scopus 로고    scopus 로고
    • SUBA3: A database for integrating experimentation and prediction to define the SUBcellular location of proteins in Arabidopsis
    • doi: 10.1093/nar/gks1151
    • Tanz, S. K., Castleden, I., Hooper, C. M., Vacher, M., Small, I., and Millar, H. A. (2013). SUBA3: a database for integrating experimentation and prediction to define the SUBcellular location of proteins in Arabidopsis. Nucleic Acids Res. 41, D1185-D1191. doi: 10.1093/nar/gks1151
    • (2013) Nucleic Acids Res. , vol.41
    • Tanz, S.K.1    Castleden, I.2    Hooper, C.M.3    Vacher, M.4    Small, I.5    Millar, H.A.6
  • 78
    • 80052946099 scopus 로고    scopus 로고
    • In silico methods for identifying organellar and suborganellar targeting peptides in Arabidopsis chloroplast proteins and for predicting the topology of membrane proteins
    • doi: 10.1007/978-1-61779-234-2_16
    • Tanz, S. K., and Small, I. (2011). In silico methods for identifying organellar and suborganellar targeting peptides in Arabidopsis chloroplast proteins and for predicting the topology of membrane proteins. Method Mol. Biol. 774, 243-280. doi: 10.1007/978-1-61779-234-2_16
    • (2011) Method Mol. Biol. , vol.774 , pp. 243-280
    • Tanz, S.K.1    Small, I.2
  • 79
    • 79955022171 scopus 로고    scopus 로고
    • The Arabidopsis thaliana 2-D gel mitochondrial proteome: Refining the value of reference maps for assessing protein abundance, contaminants and post-translational modifications
    • doi: 10.1002/pmic.201000620
    • Taylor, N. L., Heazlewood, J. L., and Millar, A. H. (2011). The Arabidopsis thaliana 2-D gel mitochondrial proteome: refining the value of reference maps for assessing protein abundance, contaminants and post-translational modifications. Proteomics 11, 1720-1733. doi: 10.1002/pmic.201000620
    • (2011) Proteomics , vol.11 , pp. 1720-1733
    • Taylor, N.L.1    Heazlewood, J.L.2    Millar, A.H.3
  • 80
    • 2442708120 scopus 로고    scopus 로고
    • High-throughput fluorescent tagging of full-length Arabidopsis gene products in planta
    • doi: 10.1104/pp.104.040139
    • Tian, G. W., Mohanty, A., Chary, S. N., Li, S., Paap, B., Drakakaki, G., et al. (2004). High-throughput fluorescent tagging of full-length Arabidopsis gene products in planta. Plant Physiol. 135, 25-38. doi: 10.1104/pp.104.040139
    • (2004) Plant Physiol. , vol.135 , pp. 25-38
    • Tian, G.W.1    Mohanty, A.2    Chary, S.N.3    Li, S.4    Paap, B.5    Drakakaki, G.6
  • 81
    • 84856690949 scopus 로고    scopus 로고
    • An efficient Agrobacterium-mediated transient transformation of Arabidopsis
    • doi: 10.1111/j.1365-313X.2011.04819.x
    • Tsuda, K., Qi, Y., Nguyen Le, V., Bethke, G., Tsuda, Y., Glazebrook, J., and Katagiri, F. (2012). An efficient Agrobacterium-mediated transient transformation of Arabidopsis. Plant J. 69, 713-719. doi: 10.1111/j.1365-313X.2011.04819.x
    • (2012) Plant J. , vol.69 , pp. 713-719
    • Tsuda, K.1    Qi, Y.2    Nguyen Le, V.3    Bethke, G.4    Tsuda, Y.5    Glazebrook, J.6    Katagiri, F.7
  • 82
    • 80053486846 scopus 로고    scopus 로고
    • To gate, or not to gate: Regulatory mechanisms for intercellular protein transport and virus movement in plants
    • doi: 10.1093/mp/ssr060
    • Ueki, S., and Citovsky, V. (2011). To gate, or not to gate: regulatory mechanisms for intercellular protein transport and virus movement in plants. Mol. Plant 4, 782-793. doi: 10.1093/mp/ssr060
    • (2011) Mol. Plant , vol.4 , pp. 782-793
    • Ueki, S.1    Citovsky, V.2
  • 83
    • 0033931375 scopus 로고    scopus 로고
    • In vivo analysis of plant promoters and transcription factors by agroinfiltration of tobacco leaves
    • doi: 10.1046/j.1365-313x.2000.00760.x
    • Yang, Y., Li, R., and Qi, M. (2000). In vivo analysis of plant promoters and transcription factors by agroinfiltration of tobacco leaves. Plant J. 22, 543-551. doi: 10.1046/j.1365-313x.2000.00760.x
    • (2000) Plant J. , vol.22 , pp. 543-551
    • Yang, Y.1    Li, R.2    Qi, M.3
  • 84
    • 34447099171 scopus 로고    scopus 로고
    • Arabidopsis mesophyll protoplasts: A versatile cell system for transient gene expression analysis
    • doi: 10.1038/nprot.2007.199
    • Yoo, S. D., Cho, Y. H., and Sheen, J. (2007). Arabidopsis mesophyll protoplasts: a versatile cell system for transient gene expression analysis. Nat. Protoc. 2, 1565-1572. doi: 10.1038/nprot.2007.199
    • (2007) Nat. Protoc. , vol.2 , pp. 1565-1572
    • Yoo, S.D.1    Cho, Y.H.2    Sheen, J.3
  • 85
    • 57749111990 scopus 로고    scopus 로고
    • Mutations in SUPPRESSOR OF VARIEGATION1, a factor required for normal chloroplast translation, suppress var2-mediated leaf variegation in Arabidopsis
    • doi: 10.1105/tpc.107.054965
    • Yu, F., Liu, X., Alsheikh, M., Park, S., and Rodermel, S. (2008). Mutations in SUPPRESSOR OF VARIEGATION1, a factor required for normal chloroplast translation, suppress var2-mediated leaf variegation in Arabidopsis. Plant Cell 20, 1786-1804. doi: 10.1105/tpc.107.054965
    • (2008) Plant Cell , vol.20 , pp. 1786-1804
    • Yu, F.1    Liu, X.2    Alsheikh, M.3    Park, S.4    Rodermel, S.5
  • 86
    • 33644623648 scopus 로고    scopus 로고
    • Molecular biology and mutation of green fluorescent protein
    • Zacharias, D. A., and Tsien, R. Y. (2006). Molecular biology and mutation of green fluorescent protein. Method Biochem. Anal. 47, 83-120.
    • (2006) Method Biochem. Anal. , vol.47 , pp. 83-120
    • Zacharias, D.A.1    Tsien, R.Y.2
  • 87
    • 79955045326 scopus 로고    scopus 로고
    • Simplified enrichment of plasma membrane proteins for proteomic analyses in Arabidopsis thaliana
    • doi: 10.1002/pmic.201000648
    • Zhang, Z. J., and Peck, S. C. (2011). Simplified enrichment of plasma membrane proteins for proteomic analyses in Arabidopsis thaliana. Proteomics 11, 1780-1788. doi: 10.1002/pmic.201000648
    • (2011) Proteomics , vol.11 , pp. 1780-1788
    • Zhang, Z.J.1    Peck, S.C.2
  • 88
    • 79955809131 scopus 로고    scopus 로고
    • A recombineering-based gene tagging system for Arabidopsis
    • doi: 10.1111/j.1365-313X.2011.04524.x
    • Zhou, R., Benavente, L. M., Stepanova, A. N., and Alonso, J. M. (2011). A recombineering-based gene tagging system for Arabidopsis. Plant J. 66, 712-723. doi: 10.1111/j.1365-313X.2011.04524.x
    • (2011) Plant J. , vol.66 , pp. 712-723
    • Zhou, R.1    Benavente, L.M.2    Stepanova, A.N.3    Alonso, J.M.4
  • 89
    • 44349099751 scopus 로고    scopus 로고
    • Sorting signals, N-terminal modifications and abundance of the chloroplast proteome
    • doi: 10.1371/journal.pone.0001994
    • Zybailov, B., Rutschow, H., Friso, G., Rudella, A., Emanuelsson, O., Sun, Q., et al. (2008). Sorting signals, N-terminal modifications and abundance of the chloroplast proteome. PLoS ONE 3:e1994. doi: 10.1371/journal.pone.0001994
    • (2008) PLoS ONE , vol.3
    • Zybailov, B.1    Rutschow, H.2    Friso, G.3    Rudella, A.4    Emanuelsson, O.5    Sun, Q.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.