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Volumn 10, Issue 11, 2010, Pages 2123-2137

Proteomic analysis of Medicago truncatula root plastids

Author keywords

Defence related proteins; GeLC MS; Membrane proteins; MS; Plant organelles; Plant proteomics

Indexed keywords

CARBOHYDRATE; NITROGEN; NUCLEIC ACID;

EID: 77952981094     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200900345     Document Type: Article
Times cited : (29)

References (108)
  • 3
    • 0037534915 scopus 로고    scopus 로고
    • Glutamate synthesis in barley roots: The role of the plastidic glucose-6-phosphate dehydrogenase
    • Esposito, S., Massaro, G.., Vona, V., Rigano, V. D. et al., Glutamate synthesis in barley roots: the role of the plastidic glucose-6-phosphate dehydrogenase. Planta 2003, 216, 639-647.
    • (2003) Planta , vol.216 , pp. 639-647
    • Esposito, S.1    Massaro, G.2    Vona, V.3    Rigano, V.D.4
  • 4
    • 2642563865 scopus 로고    scopus 로고
    • Metabolic control analysis and regulation of the conversion of sucrose to starch in growing potato tubers
    • DOI 10.1111/j.1365-3040.2004.01183.x
    • Geigenberger, P., Stitt, M., Fernie, A. R., Metabolic control analysis and regulation of the conversion of sucrose to starch in growing potato tubers. Plant Cell Environ. 2004, 27, 655-673. (Pubitemid 38708676)
    • (2004) Plant, Cell and Environment , vol.27 , Issue.6 , pp. 655-673
    • Geigenberger, P.1    Stitt, M.2    Fernie, A.R.3
  • 5
    • 0036139124 scopus 로고    scopus 로고
    • Carbon flux and fatty acid synthesis in plants
    • DOI 10.1016/S0163-7827(01)00023-6, PII S0163782701000236
    • Rawsthorne, S., Carbon flux and fatty acid synthesis in plants. Progress Lipid Res. 2002, 41, 182-196. (Pubitemid 34037870)
    • (2002) Progress in Lipid Research , vol.41 , Issue.2 , pp. 182-196
    • Rawsthorne, S.1
  • 6
    • 33845957146 scopus 로고    scopus 로고
    • Plastid biogenesis, between light and shadows
    • López-Juez, E., Plastid biogenesis, between light and shadows. J. Exp. Bot. 2007, 58, 11-26.
    • (2007) J. Exp. Bot. , vol.58 , pp. 11-26
    • López-Juez, E.1
  • 7
    • 0025135468 scopus 로고
    • A conserved cleavage-site motif in chloroplast transit peptides
    • DOI 10.1016/0014-5793(90)80614-O
    • Gavel, Y., Vonheijne, G., A conserved cleavage-site motif in chloroplast transit peptides FEBS Lett. 1990, 261, 455-458. (Pubitemid 20075016)
    • (1990) FEBS Letters , vol.261 , Issue.2 , pp. 455-458
    • Gavel, Y.1    Von Heijne, G.2
  • 8
    • 0029856727 scopus 로고    scopus 로고
    • Transit peptides play a major role in the preferential import of proteins into leucoplasts and chloroplasts
    • DOI 10.1074/jbc.271.49.31227
    • Wan, J. X., Blakeley, S. D., Dennis, D. T., Ko, K., Transit peptides play a major role in the preferential import of proteins into leucoplasts and chloroplasts. J. Biol. Chem. 1996, 271, 31227-31233. (Pubitemid 26408568)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.49 , pp. 31227-31233
    • Wan, J.1    Blakeley, S.D.2    Dennis, D.T.3    Ko, K.4
  • 9
    • 41549112931 scopus 로고    scopus 로고
    • The amyloplast proteome of potato tuber
    • Stensballe, A., Hald, S., Bauw, G., Blennow, A. et al., The amyloplast proteome of potato tuber. FEBS J. 2008, 275, 1723-1741.
    • (2008) FEBS J. , vol.275 , pp. 1723-1741
    • Stensballe, A.1    Hald, S.2    Bauw, G.3    Blennow, A.4
  • 10
    • 57749094259 scopus 로고    scopus 로고
    • Arabidopsis nuclear-encoded plastid transit peptides contain multiple sequence subgroups with distinctive chloroplast-targeting sequence motifs
    • DOI 10.1105/tpc.108.060541
    • Lee, D. W., Kim, J. K., Lee, S., Choi, S. et al., Arabidopsis nuclear-encoded plastid transit peptides contain multiple sequence subgroups with distinctive chloroplast-targeting sequence motifs. Plant Cell 2008, 20, 1603-1662. (Pubitemid 352844166)
    • (2008) Plant Cell , vol.20 , Issue.6 , pp. 1603-1622
    • Dong, W.L.1    Jong, K.K.2    Lee, S.3    Choi, S.4    Kim, S.5    Hwang, I.6
  • 11
    • 33644637941 scopus 로고    scopus 로고
    • The function and diversity of plastid protein import pathways: A multilane GTPase highway into plastids
    • DOI 10.1111/j.1600-0854.2005.00382.x
    • Kessler, F., Schnell, D. J., The function and diversity of plastid protein import pathways: a multilane GTPase highway into plastids. Traffic 2006, 7, 248-257. (Pubitemid 43323953)
    • (2006) Traffic , vol.7 , Issue.3 , pp. 248-257
    • Kessler, F.1    Schnell, D.J.2
  • 12
    • 36348955545 scopus 로고    scopus 로고
    • A prediction of the size and evolutionary origin of the proteome of chloro plasts of Arabidopsis
    • Abdallah, F., Salamini, F., Leister, D., A prediction of the size and evolutionary origin of the proteome of chloro plasts of Arabidopsis. Trends Plant Sci. 2000, 5, 141-142.
    • (2000) Trends Plant Sci. , vol.5 , pp. 141-142
    • Abdallah, F.1    Salamini, F.2    Leister, D.3
  • 13
    • 0037213560 scopus 로고    scopus 로고
    • Chloroplast research in the genomic age
    • Leister, D., Chloroplast research in the genomic age. Trends Genet. 2003, 19, 47-56.
    • (2003) Trends Genet. , vol.19 , pp. 47-56
    • Leister, D.1
  • 15
    • 35349011536 scopus 로고    scopus 로고
    • Differential gene expression and subcellular targeting of Arabidopsis glutathione S-transferase F8 is achieved through alternative transcription start sites
    • Thatcher, L. F., Carrie, C., Andersson, C. R., Sivasithamparam, K. et al., Differential gene expression and subcellular targeting of Arabidopsis glutathione S-transferase F8 is achieved through alternative transcription start sites. J. Biol. Chem. 2007, 282, 28915-28928.
    • (2007) J. Biol. Chem. , vol.282 , pp. 28915-28928
    • Thatcher, L.F.1    Carrie, C.2    Andersson, C.R.3    Sivasithamparam, K.4
  • 17
    • 33749624260 scopus 로고    scopus 로고
    • Recent surprises in protein targeting to mitochondria and plastids
    • DOI 10.1016/j.pbi.2006.09.002, PII S1369526606001439
    • Millar, A. H., Whelan, J., Small, I., Recent surprises in protein targeting to mitochondria and plastids. Curr. Opin. Plant Biol. 2006, 9, 610-615. (Pubitemid 44540403)
    • (2006) Current Opinion in Plant Biology , vol.9 , Issue.6 , pp. 610-615
    • Millar, A.H.1    Whelan, J.2    Small, I.3
  • 20
    • 33845700051 scopus 로고    scopus 로고
    • Proteome analysis of bell pepper (Capsicum annuum L.) chromoplasts
    • DOI 10.1093/pcp/pcl033
    • Siddique, M. A., Grossmann, J., Gruissem, W., Baginsky, S., Proteome analysis of bell pepper (Capsicum annuum L.) chromoplasts. Plant Cell Physiol. 2006, 47, 1663-1673. (Pubitemid 44968261)
    • (2006) Plant and Cell Physiology , vol.47 , Issue.12 , pp. 1663-1673
    • Siddique, M.A.1    Grossmann, J.2    Gruissem, W.3    Baginsky, S.4
  • 23
    • 0348136190 scopus 로고    scopus 로고
    • Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana
    • Ferro,M., Salvi, D., Brugiere, S.,Miras, S. et al., Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana. Mol. Cell. Proteomics 2003, 2, 325-345.
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 325-345
    • Salvi, D.1    Brugiere, S.2    Miras, S.3
  • 24
    • 33646902709 scopus 로고    scopus 로고
    • Protein profiling of plastoglobules in chloroplasts and chromoplasts. a surprising site for differential accumulation of metabolic enzymes
    • Ytterberg, A. J., Peltier, J. B., van Wijk, K. J., Protein profiling of plastoglobules in chloroplasts and chromoplasts. A surprising site for differential accumulation of metabolic enzymes. Plant Physiol. 2006, 140, 984-997.
    • (2006) Plant Physiol. , vol.140 , pp. 984-997
    • Ytterberg, A.J.1    Peltier, J.B.2    Van Wijk, K.J.3
  • 25
    • 0036746523 scopus 로고    scopus 로고
    • Proteomic characterization of wheat amyloplasts using identification of proteins by tandem mass spectrometry
    • Andon, N. L., Hollingworth, S., Koller, A., Greenland, A. J. et al., Proteomic characterization of wheat amyloplasts using identification of proteins by tandem mass spectrometry. Proteomics 2002, 2, 1156-1168.
    • (2002) Proteomics , vol.2 , pp. 1156-1168
    • Andon, N.L.1    Hollingworth, S.2    Koller, A.3    Greenland, A.J.4
  • 26
    • 33646261644 scopus 로고    scopus 로고
    • Proteome of amyloplasts isolated from developing wheat endosperm presents evidence of broad metabolic capability
    • Balmer, Y., Vensel, W. H., DuPont, F. M., Buchanan, B. B. et al., Proteome of amyloplasts isolated from developing wheat endosperm presents evidence of broad metabolic capability. J. Exp. Bot. 2006, 57, 1591-1602.
    • (2006) J. Exp. Bot. , vol.57 , pp. 1591-1602
    • Balmer, Y.1    Vensel, W.H.2    Dupont, F.M.3    Buchanan, B.B.4
  • 28
    • 11144348652 scopus 로고    scopus 로고
    • Proteome analysis of tobacco bright yellow-2 (BY-2) cell culture plastids as a model for undifferentiated heterotrophic plastids
    • DOI 10.1021/pr0499186
    • Baginsky, S., Siddique, A., Gruissem, W., Proteome analysis of tobacco bright yellow-2 (BY-2) cell culture plastids as a model for undifferentiated heterotrophic plastids. J. Proteome Res. 2004, 3, 1128-1137. (Pubitemid 40040366)
    • (2004) Journal of Proteome Research , vol.3 , Issue.6 , pp. 1128-1137
    • Baginsky, S.1    Siddique, A.2    Gruissem, W.3
  • 30
    • 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. et al., Sorting signals, N-terminal modifications and abundance of the chloroplast proteome. PLoS ONE 2008, 23, doi: 10.1371/journal.pone.0001994.
    • (2008) PLoS ONE , pp. 23
    • Zybailov, B.1    Rutschow, H.2    Friso, G.3    Rudella, A.4
  • 31
    • 0029801858 scopus 로고    scopus 로고
    • The effect of nitrogen nutrition on the cellular localization of glutamine synthetase isoforms in barley roots
    • Peat, L. J., Tobin, A. K., The effect of nitrogen nutrition on the cellular localization of glutamine synthetase isoforms in barley roots. Plant Physiol. 1996, 111, 1109-1117.
    • (1996) Plant Physiol. , vol.111 , pp. 1109-1117
    • Peat, L.J.1    Tobin, A.K.2
  • 32
    • 0034976820 scopus 로고    scopus 로고
    • Cellular compartmentation of ammonium assimilation in rice and barley
    • Tobin, A. K., Yamaya, T., Cellular compartmentation of ammonium assimilation in rice and barley. J. Exp. Bot. 2001, 52, 591-604. (Pubitemid 32533259)
    • (2001) Journal of Experimental Botany , vol.52 , Issue.356 , pp. 591-604
    • Tobin, A.K.1    Yamaya, T.2
  • 33
    • 60649097712 scopus 로고    scopus 로고
    • Evolution of organelle-associated protein profiling
    • Yan, W., Aebersold, R., Raines, E. W., Evolution of organelle-associated protein profiling. J. Proteomics 2009, 72, 4-11.
    • (2009) J. Proteomics , vol.72 , pp. 4-11
    • Yan, W.1    Aebersold, R.2    Raines, E.W.3
  • 34
    • 33745851905 scopus 로고    scopus 로고
    • Toward the complete yeast mitochondrial proteome: Multidimensional separation techniques for mitochondrial proteomics
    • DOI 10.1021/pr050477f
    • Reinders, J., Zahedi, R. P., Pfanner, N., Meisinger, C. et al., The complete yeast mitochondrial proteome: Multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 2006, 5, 1543-1554. (Pubitemid 44036128)
    • (2006) Journal of Proteome Research , vol.5 , Issue.7 , pp. 1543-1554
    • Reinders, J.1    Zahedi, R.P.2    Pfanner, N.3    Meisinger, C.4    Sickmann, A.5
  • 35
    • 20444450912 scopus 로고    scopus 로고
    • Legumes as a model plant family. Genomics for food and feed report of the cross-legume advances through genomics conference
    • DOI 10.1104/pp.105.060871
    • Gepts, P., Beavis, W. D., Brummer, E. C., Shoemaker, R. C. et al., Legumes as a model plant family. Genomics for food and feed report of the cross-legume advances through genomics conference. Plant Physiol. 2005, 137, 1228-1235. (Pubitemid 43119324)
    • (2005) Plant Physiology , vol.137 , Issue.4 , pp. 1228-1235
    • Gepts, P.1    Beavis, W.D.2    Brummer, E.C.3    Shoemaker, R.C.4    Stalker, H.T.5    Weeden, N.E.6    Young, N.D.7
  • 36
    • 52049107644 scopus 로고    scopus 로고
    • Arbuscular mycorrhiza: The mother of plant root endosymbioses
    • Parniske, M., Arbuscular mycorrhiza: the mother of plant root endosymbioses. Nat. Rev. Microbiol. 2008, 26, 763-775.
    • (2008) Nat. Rev. Microbiol. , vol.26 , pp. 763-775
    • Parniske, M.1
  • 37
    • 62449226168 scopus 로고    scopus 로고
    • TRUNCATULIX-a data warehouse for the legume community
    • Henckel, K., Runte, K. J., Bekel, T., Dondrup, M. et al., TRUNCATULIX-a data warehouse for the legume community. BCM Plant Biol. 2009, 11, 9-19.
    • (2009) BCM Plant Biol. , vol.11 , pp. 9-19
    • Henckel, K.1    Runte, K.J.2    Bekel, T.3    Dondrup, M.4
  • 38
    • 33644805025 scopus 로고    scopus 로고
    • Organization and metabolism of plastids and mitochondria in arbuscular mycorrhizal roots of Medicago truncatula
    • DOI 10.1104/pp.105.061457
    • Lohse, S., Schliemann, W., Ammer, C., Kopka, J. et al., Organization and metabolism of plastids and mitochondria in arbuscular mycorrhizal roots of Medicago truncatula. Plant Physiol. 2005, 139, 329-340. (Pubitemid 43951616)
    • (2005) Plant Physiology , vol.139 , Issue.1 , pp. 329-340
    • Lohse, S.1    Schliemann, W.2    Ammer, C.3    Kopka, J.4    Strack, D.5    Fester, T.6
  • 39
    • 0033965855 scopus 로고    scopus 로고
    • The TIGR Gene Indices: Reconstruction and representation of expressed gene sequences
    • Quackenbush, J., Liang, F., Holt, I., Pertea, G. et al., The TIGR Gene Indices: reconstruction and representation of expressed gene sequences. Nucleic Acids Res. 2000, 28, 141-145. (Pubitemid 30047738)
    • (2000) Nucleic Acids Research , vol.28 , Issue.1 , pp. 141-145
    • Quackenbush, J.1    Liang, F.2    Holt, I.3    Pertea, G.4    Upton, J.5
  • 40
    • 0037115831 scopus 로고    scopus 로고
    • Exploring root symbiotic programs in the model legume Medicago truncatula using EST analysis
    • Journet, E. P., van Tuinen, D., Gouzy, J., Crespeau, H. et al., Exploring root symbiotic programs in the model legume Medicago truncatula using EST analysis. Nucleic Acids Res. 2002, 30, 5579-5592.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 5579-5592
    • Journet, E.P.1    Van Tuinen, D.2    Gouzy, J.3    Crespeau, H.4
  • 41
    • 0036150104 scopus 로고    scopus 로고
    • Proteome analysis and identification of symbiosis-related proteins from Medicago truncatula Gaertn. by two-dimensional electrophoresis and mass spectrometry
    • Bestel-Corre, G., Dumas-Gaudot, E., Poinsot, V., Dieu, M. et al., Proteome analysis and identification of symbiosis-related proteins from Medicago truncatula Gaertn. by two-dimensional electrophoresis and mass spectrometry. Electrophoresis 2002, 23, 122-137.
    • (2002) Electrophoresis , vol.23 , pp. 122-137
    • Bestel-Corre, G.1    Dumas-Gaudot, E.2    Poinsot, V.3    Dieu, M.4
  • 42
    • 0028055837 scopus 로고
    • Chitinase isoforms in roots of various pea genotypes infected with arbuscular mycorrhizal fungi
    • DOI 10.1016/0168-9452(94)90117-1
    • Dumas-Gaudot, E., Asselin, A., Gianinazzi-Pearson, V., Gollotte, A. et al., Chitinase isoforms in roots of various pea genotypes infected with arbuscular mycorrhizal fungi. Plant Sci. 1994, 99, 27-37. (Pubitemid 2090364)
    • (1994) Plant Science , vol.99 , Issue.1 , pp. 27-37
    • Dumas-Gaudot, E.1    Asselin, A.2    Gianinazzi-Pearson, V.3    Gollotte, A.4    Gianinazzi, S.5
  • 43
    • 0001552084 scopus 로고
    • Nitrite reduction and carbohydrate metabolism in plastids purified from roots of Pisum sativum L
    • Bowsher C. G., Hucklesby, D. P., Emes, M. J., Nitrite reduction and carbohydrate metabolism in plastids purified from roots of Pisum sativum L. Planta 1989, 177, 359-366.
    • (1989) Planta , vol.177 , pp. 359-366
    • Bowsher, C.G.1    Hucklesby, D.P.2    Emes, M.J.3
  • 44
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M., A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem.1976, 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 46
    • 54449100342 scopus 로고    scopus 로고
    • Exploring the nuclear proteome of Medicago truncatula at the switch towards seed filling
    • Repetto, O., Rogniaux, H., Firnhaber, C., Zuber, H. et al., Exploring the nuclear proteome of Medicago truncatula at the switch towards seed filling. Plant J. 2008, 56, 398-410.
    • (2008) Plant J. , vol.56 , pp. 398-410
    • Repetto, O.1    Rogniaux, H.2    Firnhaber, C.3    Zuber, H.4
  • 47
    • 33746762097 scopus 로고    scopus 로고
    • A mass spectrometric approach to identify arbuscular mycorrhiza-related proteins in root plasma membrane fractions
    • Valot, B., Negroni, L., Zivy, M., Gianinazzi, S. et al., A mass spectrometric approach to identify arbuscular mycorrhiza-related proteins in root plasma membrane fractions. Proteomics 2006, 6, S145-S155.
    • (2006) Proteomics , vol.6
    • Valot, B.1    Negroni, L.2    Zivy, M.3    Gianinazzi, S.4
  • 48
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 49
    • 0035525061 scopus 로고    scopus 로고
    • Establishment of a root proteome reference map for the model legume Medicago truncatula using the expressed sequence tag database for peptide mass fingerprinting
    • Mathesius, U., Keijzers, G., Natera, S. H. A., Weinman, J. J. et al., Establishment of a root proteome reference map for the model legume Medicago truncatula using the expressed sequence tag database for peptide mass fingerprinting. Proteomics 2001, 1, 1424-1440.
    • (2001) Proteomics , vol.1 , pp. 1424-1440
    • Mathesius, U.1    Keijzers, G.2    Natera, S.H.A.3    Weinman, J.J.4
  • 50
    • 60449097009 scopus 로고    scopus 로고
    • On the mechanisms of cadmium stress alleviation in Medicago truncatula by arbuscular mycorrhizal symbiosis: A root proteomic study
    • Aloui, A., Recorbet, G., Gollotte, A., Robert, F. et al., On the mechanisms of cadmium stress alleviation in Medicago truncatula by arbuscular mycorrhizal symbiosis: a root proteomic study. Proteomics 2009, 9, 420-433.
    • (2009) Proteomics , vol.9 , pp. 420-433
    • Aloui, A.1    Recorbet, G.2    Gollotte, A.3    Robert, F.4
  • 51
    • 0036891705 scopus 로고    scopus 로고
    • Sequence conserved for subcellular localization
    • Nair, R., Rost, B., Sequence conserved for subcellular localization. Protein Sci. 2002, 11, 2836-2847.
    • (2002) Protein Sci. , vol.11 , pp. 2836-2847
    • Nair, R.1    Rost, B.2
  • 52
    • 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, PII S0378111904000150
    • Richly, E., Leister, D., An improved prediction of chloroplast proteins reveals diversities and commonalities in the chloroplast proteomes of Arabidopsis and rice. Gene 2004, 329: 11-16. (Pubitemid 38366490)
    • (2004) Gene , vol.329 , Issue.1-2 , pp. 11-16
    • Richly, E.1    Leister, D.2
  • 53
    • 24044513966 scopus 로고    scopus 로고
    • Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations
    • DOI 10.1038/nmeth785
    • Elias, J. E., Haas, W., Faherty, B. K., Gygi, S. P., Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations. Nat. Methods 2005, 2, 667-675. (Pubitemid 41223093)
    • (2005) Nature Methods , vol.2 , Issue.9 , pp. 667-675
    • Elias, J.E.1    Haas, W.2    Faherty, B.K.3    Gygi, S.P.4
  • 54
    • 33750971117 scopus 로고    scopus 로고
    • Multidimensional proteomic analysis of the soluble subproteome of the emerging nosocomial pathogen Ochrobactrum anthropi
    • Graham, R. L. J., Pollock, C. E., O'Loughlin, S. N., Ternan, N. G. et al., Multidimensional proteomic analysis of the soluble subproteome of the emerging nosocomial pathogen Ochrobactrum anthropi. J. Proteome Res. 2006, 5, 3145-3153.
    • (2006) J. Proteome Res. , vol.5 , pp. 3145-3153
    • Graham, R.L.J.1    Pollock, C.E.2    O'Loughlin, S.N.3    Ternan, N.G.4
  • 55
    • 33846640661 scopus 로고    scopus 로고
    • Multidimensional analysis of the insoluble subproteome of Oceanobacillus iheyensis HTE831, an alkaliphilic and halotolerant deep-sea bacterium isolated from the Iheya ridge
    • Graham, R. L. J., Pollock, C. E., O'Loughlin, S. N., Ternan, N. G. et al., Multidimensional analysis of the insoluble subproteome of Oceanobacillus iheyensis HTE831, an alkaliphilic and halotolerant deep-sea bacterium isolated from the Iheya ridge. Proteomics 2007, 7, 82-91.
    • (2007) Proteomics , vol.7 , pp. 82-91
    • Graham, R.L.J.1    Pollock, C.E.2    O'Loughlin, S.N.3    Ternan, N.G.4
  • 56
    • 27644555055 scopus 로고    scopus 로고
    • Interpretation of shotgun proteomic data: The protein inference problem
    • DOI 10.1074/mcp.R500012-MCP200
    • Nesvizhskii, A. I., Aebersold, R., Interpretation of shotgun proteomic data-The protein inference problem. Mol. Cell. Proteomics 2005, 4, 1419-1440. (Pubitemid 41555469)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.10 , pp. 1419-1440
    • Nesvizhskii, A.I.1    Aebersold, R.2
  • 57
    • 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., Millar, A. H., Combining experimental and predicted datasets for determination of the subcellular location of proteins in Arabidopsis. Plant Physiol. 2005, 139, 598-609. (Pubitemid 43907090)
    • (2005) Plant Physiology , vol.139 , Issue.2 , pp. 598-609
    • Heazlewood, J.L.1    Tonti-Filippini, J.2    Verboom, R.E.3    Millar, A.H.4
  • 58
    • 33644876911 scopus 로고    scopus 로고
    • MitoP2: The mitochondrial proteome database-now including mouse data
    • Prokisch, H., Andreoli, C., Ahting, U., Heiss, K. et al., MitoP2: the mitochondrial proteome database-now including mouse data. Nucleic Acids Res. 2006, 34, D705-D711.
    • (2006) Nucleic Acids Res. , vol.34
    • Prokisch, H.1    Andreoli, C.2    Ahting, U.3    Heiss, K.4
  • 61
    • 0036007390 scopus 로고    scopus 로고
    • Interaction of plant mitochondrial and chloroplast signal peptides with the Hsp70 molecular chaperone
    • DOI 10.1016/S1360-1385(01)02180-X, PII S136013850102180X
    • Zhang, X. P., Glaser, E., Interaction of plant mitochondrial and chloroplast signal peptides with the Hsp70 molecular chaperone. Trends Plant Sci. 2002, 7, 14-21. (Pubitemid 34108194)
    • (2002) Trends in Plant Science , vol.7 , Issue.1 , pp. 14-21
    • Zhang, X.-P.1    Glaser, E.2
  • 62
    • 2942589051 scopus 로고    scopus 로고
    • Predotar: A tool for rapidly screening proteomes for N-terminal targeting sequences
    • DOI 10.1002/pmic.200300776
    • Small, I., Peeters, N., Legeai, F., Lurin, C., Predotar: A tool for rapidly screening proteomes for N-terminal targeting sequences. Proteomics 2004, 4, 1581-1590. (Pubitemid 38738317)
    • (2004) Proteomics , vol.4 , Issue.6 , pp. 1581-1590
    • Small, I.1    Peeters, N.2    Legeai, F.3    Lurin, C.4
  • 63
    • 34248676824 scopus 로고    scopus 로고
    • Comparative survey of plastid and mitochondrial targeting properties of transcription factors in Arabidopsis and rice
    • DOI 10.1007/s00438-007-0214-4
    • Schwacke, R., Fischer, K., Ketelsen, B., Krupinska, K. et al., Comparative survey of plastid and mitochondrial targeting properties of transcription factors in Arabidopsis and rice. Mol. Gen. Genomics 2007, 277, 631-646. (Pubitemid 46776594)
    • (2007) Molecular Genetics and Genomics , vol.277 , Issue.6 , pp. 631-646
    • Schwacke, R.1    Fischer, K.2    Ketelsen, B.3    Krupinska, K.4    Krause, K.5
  • 65
    • 57749092770 scopus 로고    scopus 로고
    • Peroxisomal localization of Arabidopsis isopentenyl diphosphate isomerases suggests that part of the plant isoprenoid mevalonic acid pathway is compartmentalized to peroxisomes
    • Sapir-Mir, M., Mettt, A., Belausov, E., Tal-Meshulam, S. et al., Peroxisomal localization of Arabidopsis isopentenyl diphosphate isomerases suggests that part of the plant isoprenoid mevalonic acid pathway is compartmentalized to peroxisomes. Plant Physiol. 2008, 148, 1219-1228.
    • (2008) Plant Physiol. , vol.148 , pp. 1219-1228
    • Sapir-Mir, M.1    Mettt, A.2    Belausov, E.3    Tal-Meshulam, S.4
  • 66
    • 15744385479 scopus 로고    scopus 로고
    • The vegetative vacuole proteome of Arabidopsis thaliana reveals predicted and unexpected proteins
    • DOI 10.1105/tpc.104.027078
    • Carter, C, Pan, S. Q., Jan, Z. H., Avila, E. L. et al., The vegetative vacuole proteorne of Arabidopsis thaliana reveals predicted and unexpected proteins. Plant Cell 2004, 16, 3285-3303. (Pubitemid 41096007)
    • (2004) Plant Cell , vol.16 , Issue.12 , pp. 3285-3303
    • Carter, C.1    Pan, S.2    Zouhar, J.3    Avila, E.L.4    Girke, T.5    Raikhel, N.V.6
  • 67
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • DOI 10.1038/nprot.2007.131, PII NPROT.2007.131
    • Emanuelsson, O., Brunak, S., von Heijne, G., Nielsen, H., Locating proteins in the cell using TargetP, SignalP and related tools. Nat. Protocols 2007, 2, 953-971. (Pubitemid 46745592)
    • (2007) Nature Protocols , vol.2 , Issue.4 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 69
    • 43949127723 scopus 로고    scopus 로고
    • Metabolic pathways of the wheat (Triticum aestivum) endosperm amyloplast revealed by proteomics
    • Dupont, F., Metabolic pathways of the wheat (Triticum aestivum) endosperm amyloplast revealed by proteomics. BMC Plant Biol. 2008, 8, 39-57.
    • (2008) BMC Plant Biol. , vol.8 , pp. 39-57
    • Dupont, F.1
  • 70
    • 20444385506 scopus 로고    scopus 로고
    • Solute transporters of the plastid envelope membrane
    • DOI 10.1146/annurev.arplant.56.032604.144228
    • Weber, A. P. M., Schwacke, R., Flugge, U. I., Solute transporters of the plastid envelope membrane. Annu. Rev. Plant Biol. 2005, 56, 133-164. (Pubitemid 40802406)
    • (2005) Annual Review of Plant Biology , vol.56 , pp. 133-164
    • Weber, A.P.M.1    Schwacke, R.2    Flugge, U.-I.3
  • 71
    • 0030850950 scopus 로고    scopus 로고
    • The expression of subunits of the mitochondrial complex I-homologous NAD(P)H-plastoquinone-oxidoreductase during plastid development
    • Fischer, M., Funk, E., Steinmuller, K., The expression of subunits of the mitochondrial complex I-homologous NAD(P)H-plastoquinone-oxidoreductase during plastid development. Z. Naturforsch. C 1997, 52, 481-486. (Pubitemid 27378074)
    • (1997) Zeitschrift fur Naturforschung Section C - Journal of Biosciences , vol.52 , Issue.7-8 , pp. 481-486
    • Fischer, M.1    Funk, E.2    Steinmuller, K.3
  • 72
    • 34247235591 scopus 로고    scopus 로고
    • The effect of G1c6P uptake and its subsequent oxidation within pea root plastids on nitrite reduction and glutamate synthesis
    • Bowsher, C. G., Lacey, A. E., Hanke, G. T., Clarkson, D. T. et al., The effect of G1c6P uptake and its subsequent oxidation within pea root plastids on nitrite reduction and glutamate synthesis. J. Exp. Bot. 2007, 58, 1109-1118.
    • (2007) J. Exp. Bot. , vol.58 , pp. 1109-1118
    • Bowsher, C.G.1    Lacey, A.E.2    Hanke, G.T.3    Clarkson, D.T.4
  • 73
    • 33745645551 scopus 로고    scopus 로고
    • Protein degradation machineries in plastids
    • Sakamoto, W., Protein degradation machineries in plastids. Annu. Rev. Plant Biol. 2006, 57, 599-621
    • (2006) Annu. Rev. Plant Biol. , vol.57 , pp. 599-621
    • Sakamoto, W.1
  • 74
    • 50249088759 scopus 로고    scopus 로고
    • Stress induces the assembly of RNA granules in the chloroplast of Chlamydomonas reinhardtii
    • Uniacke, J., Zerges, W., Stress induces the assembly of RNA granules in the chloroplast of Chlamydomonas reinhardtii. J. Cell Biol. 2008, 182, 641-646.
    • (2008) J. Cell Biol. , vol.182 , pp. 641-646
    • Uniacke, J.1    Zerges, W.2
  • 75
    • 0018375639 scopus 로고
    • Transport of proteins into mitochondria and chloroplasts
    • Chua, N. H., Schmidt, G. W., Transport of proteins into mitochondria and chloroplasts. J. Cell Biol. 1979, 81, 461-483.
    • (1979) J. Cell Biol. , vol.81 , pp. 461-483
    • Chua, N.H.1    Schmidt, G.W.2
  • 76
    • 33646261158 scopus 로고    scopus 로고
    • Tandem affinity purification tagging of fatty acid biosynthetic enzymes in Synechocystis sp. PCC6803 and Arabidopsis thaliana
    • Brown, A. P., Affleck, V., Fawcett,T., Slabas, A. R., Tandem affinity purification tagging of fatty acid biosynthetic enzymes in Synechocystis sp. PCC6803 and Arabidopsis thaliana. J. Exp. Bot. 2006, 57, 1563-1571.
    • (2006) J. Exp. Bot. , vol.57 , pp. 1563-1571
    • Brown, A.P.1    Affleck, V.2    Fawcett, T.3    Slabas, A.R.4
  • 78
    • 0039057706 scopus 로고
    • Immunological evidence for the presence of proteins of the photosynthetic membrane in etiolated leaves of Phaseolus vulgaris
    • Dujardin, E., Bertrand, M., Radunz, A., Schmid, G. H., Immunological evidence for the presence of proteins of the photosynthetic membrane in etiolated leaves of Phaseolus vulgaris. J. Plant Physiol. 1987, 128, 95-107.
    • (1987) J. Plant Physiol. , vol.128 , pp. 95-107
    • Dujardin, E.1    Bertrand, M.2    Radunz, A.3    Schmid, G.H.4
  • 79
    • 33645698674 scopus 로고    scopus 로고
    • The early responses of Arabidopsis thaliana cells to cadmium exposure explored by protein and metabolite profiling analyses
    • Sarry, J. E., Kuhn, L., Ducruix, C., Lafaye, A. et al., The early responses of Arabidopsis thaliana cells to cadmium exposure explored by protein and metabolite profiling analyses. Proteomics 2006, 6, 2180-2198.
    • (2006) Proteomics , vol.6 , pp. 2180-2198
    • Sarry, J.E.1    Kuhn, L.2    Ducruix, C.3    Lafaye, A.4
  • 80
    • 66149131103 scopus 로고    scopus 로고
    • Overexpression of GmAKR1, a stress-induced aldo/keto reductase from soybean, retards nodule development
    • Hur, Y., Shin, K., Kim, S., Nam, K. et al., Overexpression of GmAKR1, a stress-induced aldo/keto reductase from soybean, retards nodule development. Mol. Cells 2009, 27, 217-223.
    • (2009) Mol. Cells , vol.27 , pp. 217-223
    • Hur, Y.1    Shin, K.2    Kim, S.3    Nam, K.4
  • 82
    • 0141564568 scopus 로고    scopus 로고
    • Transcript profiling coupled with spatial expression analyses reveals genes involved in distinct developmental stages of an arbuscular mycorrhizal symbiosis
    • DOI 10.1105/tpc.014183
    • Liu, J. Y., Blaylock, L. A., Endre, G., Cho, J. et al., Transcript profiling coupled with spatial expression analyses reveals genes involved in distinct developmental stages of an arbuscular mycorrhizal symbiosis. Plant Cell 2003, 15, 2106-2123. (Pubitemid 37144064)
    • (2003) Plant Cell , vol.15 , Issue.9 , pp. 2106-2123
    • Liu, J.1    Blaylock, L.A.2    Endre, G.3    Cho, J.4    Town, C.D.5    Vandenbosch, K.A.6    Harrison, M.J.7
  • 83
    • 26944432679 scopus 로고    scopus 로고
    • Expression patterns of purple acid phosphatase genes in Arabidopsis organs and functional analysis of AtPAP23 predominantly transcribed in flower
    • Zhu, H. F., Qian, W. Q., Lu, X. Z., Li, D. P. et al., Expression patterns of purple acid phosphatase genes in Arabidopsis organs and functional analysis of AtPAP23 predominantly transcribed in flower. Plant Mol. Biol. 2005, 59, 581-594.
    • (2005) Plant Mol. Biol. , vol.59 , pp. 581-594
    • Zhu, H.F.1    Qian, W.Q.2    Lu, X.Z.3    Li, D.P.4
  • 84
    • 0031664911 scopus 로고    scopus 로고
    • Uclacyanins, stellacyanins, and plantacyanins are distinct subfamilies of phytocyanins: Plant-specific mononuclear blue copper proteins
    • Nersissian, A. M., Immoos, C., Hill, M. G., Hart, P. J. et al., Uclacyanins, stellacyanins, and plantacyanins ape distinct subfamilies of phytocyanins: Plant-specific mononuclear blue copper proteins. Prot. Sci. 1998, 7, 1915-1929. (Pubitemid 28432432)
    • (1998) Protein Science , vol.7 , Issue.9 , pp. 1915-1929
    • Nersissian, A.M.1    Immoos, C.2    Hill, M.G.3    Hart, P.J.4    Williams, G.5    Herrmann, R.G.6    Valentine, J.S.7
  • 85
    • 5844327992 scopus 로고    scopus 로고
    • Gene expression under water deficit in loblolly pine (Pinus taeda): Isolation and characterization of cDNA clones
    • Chang, S. J., Puryear, J. D., Dias, M., Funkhouser, E. A. et al., Gene expression under water deficit in loblolly pine (Pinus taeda): Isolation and characterization of cDNA clones. Physiol. Plant. 1996, 97, 139-148. (Pubitemid 126616889)
    • (1996) Physiologia Plantarum , vol.97 , Issue.1 , pp. 139-148
    • Chang, S.1    Puryear, J.D.2    Dias, M.A.D.L.3    Funkhouser, E.A.4    Newton, R.J.5    Cairney, J.6
  • 86
    • 0028247854 scopus 로고
    • Isolation and characterization of a pea pod cDNA-encoding a putative blue copper protein correlated with lignin deposition
    • Drew, J. E., Gatehouse, J.A., Isolation and characterization of a pea pod cDNA-encoding a putative blue copper protein correlated with lignin deposition. J. Exp. Bot. 1994, 45, 1873-1884.
    • (1994) J. Exp. Bot. , vol.45 , pp. 1873-1884
    • Drew, J.E.1    Gatehouse, J.A.2
  • 87
    • 47549112273 scopus 로고    scopus 로고
    • Identification of stress-induced genes from the drought tolerant semi-arid legume crop horsegram (Macrotyloma uniflorum (Lam.) Verdc.) through analysis of subtracted expressed sequence tags
    • Reddy, P. C. O., Sairanganayakulu, G., Thippeswamy, M., Reddy, P. S. et al., Identification of stress-induced genes from the drought tolerant semi-arid legume crop horsegram (Macrotyloma uniflorum (Lam.) Verdc.) through analysis of subtracted expressed sequence tags. Plant Sci. 2008, 175, 372-384.
    • (2008) Plant Sci. , vol.175 , pp. 372-384
    • Reddy, P.C.O.1    Sairanganayakulu, G.2    Thippeswamy, M.3    Reddy, P.S.4
  • 88
    • 0036008974 scopus 로고    scopus 로고
    • Local and systemic wound-induction of RNase and nuclease activities in Arabidopsis: RNS1 as a marker for a JA-independent systemic signaling pathway
    • LeBrasseur, N. D., MacIntosh, G. C., Perez-Amador, M. A., Saito, H. M. et al., Local and systemic wound-induction of RNase and nuclease activities in Arabidopsis: RNS1 as a marker for a JA-independent systemic signaling pathway. Plant J. 2002, 29, 393-403.
    • (2002) Plant J. , vol.29 , pp. 393-403
    • Lebrasseur, N.D.1    MacIntosh, G.C.2    Perez-Amador, M.A.3    Saito, H.M.4
  • 90
    • 27744602589 scopus 로고    scopus 로고
    • Identification of Arabidopsis salt and osmotic stress responsive proteins using two-dimensional difference gel electrophoresis and mass spectrometry
    • DOI 10.1002/pmic.200401282
    • Ndimba, B. K., Chivasa, S., Simon, W. J., Slabas, A. R., Identification of Arabidopsis salt and osmotic stress responsive proteins using two-dimensional difference gel electrophoresis and mass spectrometry. Proteomics 2005, 5, 4185-4196. (Pubitemid 41626086)
    • (2005) Proteomics , vol.5 , Issue.16 , pp. 4185-4196
    • Ndimba, B.K.1    Chivasa, S.2    Simon, W.J.3    Slabas, A.R.4
  • 91
    • 67349093845 scopus 로고    scopus 로고
    • Genome-wide identification of BURP domain-containing genes in rice reveals a gene family with diverse structures and responses to abiotic stresses
    • Ding, X., Hou, X., Xie, K., Xiong, L., Genome-wide identification of BURP domain-containing genes in rice reveals a gene family with diverse structures and responses to abiotic stresses. Planta 2009, 230, 149-163.
    • (2009) Planta , vol.230 , pp. 149-163
    • Ding, X.1    Hou, X.2    Xie, K.3    Xiong, L.4
  • 92
    • 32044466069 scopus 로고    scopus 로고
    • Dirigent proteins in conifer defense: Gene discovery, phylogeny, and differential wound- and insect-induced expression of a family of DIR and DIR-like genes in spruce (Picea spp.)
    • Ralph, S., Park, J. Y., Bohlmann, J., Mansfield, S. D., Dirigent proteins in conifer defense: gene discovery, phylogeny, and differential wound- and insect-induced expression of a family of DIR and DIR-like genes in spruce (Picea spp.). Plant Mol. Biol. 2006, 60, 21-40.
    • (2006) Plant Mol. Biol. , vol.60 , pp. 21-40
    • Ralph, S.1    Park, J.Y.2    Bohlmann, J.3    Mansfield, S.D.4
  • 93
    • 66449122161 scopus 로고    scopus 로고
    • Proteomic analysis of chicory root identifies proteins typically involved in cold acclimation
    • Degand, H., Faber, A., Dauchot, N., Mingeot, D. et al., Proteomic analysis of chicory root identifies proteins typically involved in cold acclimation. Proteomics 2009, 29, 2903-2907.
    • (2009) Proteomics , vol.29 , pp. 2903-2907
    • Degand, H.1    Faber, A.2    Dauchot, N.3    Mingeot, D.4
  • 95
    • 58849094608 scopus 로고    scopus 로고
    • Ripening and genotype control stilbene accumulation in healthy grapes
    • Gatto, P., Vrhovsek, U., Muth, J., Segala, C. et al., Ripening and genotype control stilbene accumulation in healthy grapes. J. Agric. Food Chem. 2008, 56, 11773-11785.
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 11773-11785
    • Gatto, P.1    Vrhovsek, U.2    Muth, J.3    Segala, C.4
  • 97
    • 37249025796 scopus 로고    scopus 로고
    • Insights into the role and structure of plant ureases
    • DOI 10.1016/j.phytochem.2007.06.034, PII S0031942207004396
    • Follmer, C., Insights into the role and structure of plant ureases. Phytochemistry 2008, 69, 18-28. (Pubitemid 350262817)
    • (2008) Phytochemistry , vol.69 , Issue.1 , pp. 18-28
    • Follmer, C.1
  • 98
    • 0030609539 scopus 로고    scopus 로고
    • Regulation of protease inhibitors and plant defense
    • DOI 10.1016/S1360-1385(97)01107-2
    • Koiwa, H., Bressan, R. A., Hasegawa, P. M., Regulation of protease inhibitors and plant defense. Trends Plant Sci. 1997, 2, 379-384. (Pubitemid 27403191)
    • (1997) Trends in Plant Science , vol.2 , Issue.10 , pp. 379-384
    • Koiwa, H.1    Bressan, R.A.2    Hasegawa, P.M.3
  • 99
    • 0033179482 scopus 로고    scopus 로고
    • The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins
    • van Loon, L. C., van Strien, E. A., The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins. Physiol. Mol. Plant Pathol. 1999, 55, 85-97.
    • (1999) Physiol. Mol. Plant Pathol. , vol.55 , pp. 85-97
    • Van Loon, L.C.1    Van Strien, E.A.2
  • 101
    • 51649097090 scopus 로고    scopus 로고
    • Retrograde signaling and plant stress: Plastid signals initiate cellular stress responses
    • Piňas Fernandez, A., Strand, A., Retrograde signaling and plant stress: plastid signals initiate cellular stress responses. Curr. Opin. Plant Biol. 2008, 11, 509-513.
    • (2008) Curr. Opin. Plant Biol. , vol.11 , pp. 509-513
    • Piňas Fernandez, A.1    Strand, A.2
  • 102
    • 20444507261 scopus 로고    scopus 로고
    • Overlaps in the transcriptional profiles of Medicago truncatula roots inoculated with two different Glomus fungi provide insights into the genetic program activated during arbuscular mycorrhiza
    • Hohnjec, N., Vieweg, M. E., Pühler, A., Becker, A. et al., Overlaps in the transcriptional profiles of Medicago truncatula roots inoculated with two different Glomus fungi provide insights into the genetic program activated during arbuscular mycorrhiza. Plant Physiol. 2005, 137, 1283-1301.
    • (2005) Plant Physiol. , vol.137 , pp. 1283-1301
    • Hohnjec, N.1    Vieweg, M.E.2    Pühler, A.3    Becker, A.4
  • 103
    • 26844444697 scopus 로고    scopus 로고
    • Proteomic profiling unravels insights into the molecular background underlying increased Aphanomyces euteiches-tolerance of Medicago truncatula
    • DOI 10.1007/s11103-005-0184-z
    • Colditz, F., Braun, H. P., Jacquet, C., Niehaus, K. et al., Proteomic profiling unravels insights into the molecular background underlying increased Aphanomyces euteiches tolerance of Medicago truncatula. Plant Mol. Biol. 2005, 59, 387-406. (Pubitemid 41464661)
    • (2005) Plant Molecular Biology , vol.59 , Issue.3 , pp. 387-406
    • Colditz, F.1    Braun, H.-P.2    Jacquet, C.3    Niehaus, K.4    Krajinski, F.5
  • 104
    • 33747478283 scopus 로고    scopus 로고
    • Mutations in DMI3 and SUNN modify the appressorium-responsive root proteome in arbuscular mycorrhiza
    • DOI 10.1094/MPMI-19-0988
    • Amiour, N., Recorbet, G., Robert , F., Gianinazzi, S. et al., Mutations in DMI3 and SUNN modify the appressorium-responsive root proteome in arbuscular mycorrhiza. Mol. Plant Microbe Interact. 2006, 19, 988-997. (Pubitemid 44260241)
    • (2006) Molecular Plant-Microbe Interactions , vol.19 , Issue.9 , pp. 988-997
    • Amiour, N.1    Recorbet, G.2    Robert, F.3    Gianinazzi, S.4    Dumas-Gaudot, E.5
  • 105
    • 33644839378 scopus 로고    scopus 로고
    • Suppression of allene oxide cyclase in hairy roots of Medicago truncatula reduces jasmonate levels and the degree of mycorrhization with Glomus intraradices
    • DOI 10.1104/pp.105.069054
    • Isayenkov, S., Mrosk, C., Stenzel, I., Strack, D. et al., Suppression of allene oxide cyclase in hairy roots of Medicago truncatula reduces jasmonate levels and the degree of mycorrhization with Glomus intraradices. Plant Physiol. 2005, 139, 1401-1410. (Pubitemid 43786840)
    • (2005) Plant Physiology , vol.139 , Issue.3 , pp. 1401-1410
    • Isayenkov, S.1    Mrosk, C.2    Stenzel, I.3    Strack, D.4    Hause, B.5
  • 106
    • 33747605292 scopus 로고    scopus 로고
    • Isoprenoid metabolism and plastid reorganization in arbuscular mycorrhizal roots
    • DOI 10.1111/j.1469-8137.2006.01837.x
    • Strack, D., Fester, T., Isoprenoid metabolism and plastid reorganization in arbuscular mycorrhizal roots. New Phytol. 2006, 172, 22-34. (Pubitemid 44268110)
    • (2006) New Phytologist , vol.172 , Issue.1 , pp. 22-34
    • Strack, D.1    Fester, T.2
  • 107
    • 52649114325 scopus 로고    scopus 로고
    • Knock-down of the MEP pathway isogene 1-deoxy-D-xylulose 5-phosphate synthase 2 inhibits formation of arbuscular mycorrhiza-induced apocarotenoids, and abolishes normal expression of mycorrhiza-specific plant marker genes
    • Floß, D. S., Hause, B., Lange, P. R., Küster, H. et al., Knock-down of the MEP pathway isogene 1-deoxy-D-xylulose 5-phosphate synthase 2 inhibits formation of arbuscular mycorrhiza-induced apocarotenoids, and abolishes normal expression of mycorrhiza-specific plant marker genes. Plant J. 2008, 56, 86-100.
    • (2008) Plant J. , vol.56 , pp. 86-100
    • Floß, D.S.1    Hause, B.2    Lange, P.R.3    Küster, H.4
  • 108
    • 57749117122 scopus 로고    scopus 로고
    • RNA interference-mediated repression of MtCCD1 in mycorrhizal roots of Medicago truncatula causes accumulation of C27 apocarotenoids, shedding light on the functional role of CCD1
    • Floß, D. S., Schliemann, W., Schmidt, J., Strack, D. et al., RNA interference-mediated repression of MtCCD1 in mycorrhizal roots of Medicago truncatula causes accumulation of C27 apocarotenoids, shedding light on the functional role of CCD1. Plant Physiol. 2008, 48, 1267-1282.
    • (2008) Plant Physiol. , vol.48 , pp. 1267-1282
    • Floß, D.S.1    Schliemann, W.2    Schmidt, J.3    Strack, D.4


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