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Volumn 38, Issue 7, 2011, Pages 652-660

Expression profiling of chloroplast-encoded proteins in rice leaves at different growth stages

Author keywords

Antibody based rice proteomics; Chloroplast; Protein profiling; Rice

Indexed keywords


EID: 80054004887     PISSN: 10003282     EISSN: None     Source Type: Journal    
DOI: 10.3724/SP.J.1206.2011.00028     Document Type: Article
Times cited : (3)

References (31)
  • 1
    • 0033781930 scopus 로고    scopus 로고
    • Proteomics of the chloroplast: Experimentation and prediction
    • Van Wijk K. Proteomics of the chloroplast: Experimentation and prediction. Trends Plant Sci, 2000, 5(10): 420-425
    • (2000) Trends Plant Sci , vol.5 , Issue.10 , pp. 420-425
    • Van Wijk, K.1
  • 2
    • 84968989005 scopus 로고
    • The complete nucleotide sequence of the tobacco chloroplast genome: Its gene organization and expression
    • Shinozaki K, Ohme M, Tanaka M, et al. The complete nucleotide sequence of the tobacco chloroplast genome: its gene organization and expression. EMBO J, 1986, 5(9): 2043-2049
    • (1986) EMBO J , vol.5 , Issue.9 , pp. 2043-2049
    • Shinozaki, K.1    Ohme, M.2    Tanaka, M.3
  • 3
    • 33644873175 scopus 로고    scopus 로고
    • ChloroplastDB: The chloroplast genome database
    • Database Issue
    • Cui L, Veeraraghavan N, Richter A, et al. ChloroplastDB: The chloroplast genome database. Nucleic Acids Res, 2006, 34(Database Issue): 692-696
    • (2006) Nucleic Acids Res , vol.34 , pp. 692-696
    • Cui, L.1    Veeraraghavan, N.2    Richter, A.3
  • 4
    • 1042291445 scopus 로고    scopus 로고
    • The function of chloroplastic NAD(P)H dehydrogenase in tobacco during chilling stress under low irradiance
    • Li X, Duan W, Meng Q, et al. The function of chloroplastic NAD(P)H dehydrogenase in tobacco during chilling stress under low irradiance. Plant Cell Physiol, 2004, 45(1): 103-108
    • (2004) Plant Cell Physiol , vol.45 , Issue.1 , pp. 103-108
    • Li, X.1    Duan, W.2    Meng, Q.3
  • 5
    • 33644917172 scopus 로고    scopus 로고
    • In vivo fragmentation of the large subunit of ribulose-1, 5-bisphosphate carboxylase by reactive oxygen species in an intact leaf of cucumber under chilling-light conditions
    • Nakano R, Ishida H, Makino A, et al. In vivo fragmentation of the large subunit of ribulose-1, 5-bisphosphate carboxylase by reactive oxygen species in an intact leaf of cucumber under chilling-light conditions. Plant Cell Physiol, 2006, 47(2): 270-276
    • (2006) Plant Cell Physiol , vol.47 , Issue.2 , pp. 270-276
    • Nakano, R.1    Ishida, H.2    Makino, A.3
  • 6
    • 77955721526 scopus 로고    scopus 로고
    • Heat stress results in loss of chloroplast Cu/Zn superoxide dismutase and increased damage to Photosystem II in combined drought-heat stressed Lotus japonicus
    • Sainz M, Diaz P, Monza J, et al. Heat stress results in loss of chloroplast Cu/Zn superoxide dismutase and increased damage to Photosystem II in combined drought-heat stressed Lotus japonicus. Physiol Plant, 2010, 140(1): 46-56
    • (2010) Physiol Plant , vol.140 , Issue.1 , pp. 46-56
    • Sainz, M.1    Diaz, P.2    Monza, J.3
  • 7
    • 77954711265 scopus 로고    scopus 로고
    • Ozone stress-induced proteomic changes in leaf total soluble and chloroplast proteins of soybean reveal that carbon allocation is involved in adaptation in the early developmental stage
    • Ahsan N, Nanjo Y, Sawada H, et al. Ozone stress-induced proteomic changes in leaf total soluble and chloroplast proteins of soybean reveal that carbon allocation is involved in adaptation in the early developmental stage. Proteomics, 2010, 10(14): 2605-2619
    • (2010) Proteomics , vol.10 , Issue.14 , pp. 2605-2619
    • Ahsan, N.1    Nanjo, Y.2    Sawada, H.3
  • 8
    • 21344474571 scopus 로고    scopus 로고
    • Chloroplast genetic engineering: Recent advances and future perspectives
    • DOI 10.1080/07352680590935387
    • Grevicht J, Daniell H. Chloroplast genetic engineering: Recent advances and future perspectives. Critical Reviews in Plant Sciences, 2005, 24(2): 83-107 (Pubitemid 40902349)
    • (2005) Critical Reviews in Plant Sciences , vol.24 , Issue.2 , pp. 83-107
    • Grevich, J.J.1    Daniell, H.2
  • 9
    • 33748751205 scopus 로고    scopus 로고
    • Chloroplast genetic engineering
    • Daniell H. Henry Daniell: chloroplast genetic engineering. Biotechnol J, 2006, 1(1): 31-33
    • (2006) Biotechnol J , vol.1 , Issue.1 , pp. 31-33
    • Daniell, H.1    Daniell, H.2
  • 10
    • 0034858234 scopus 로고    scopus 로고
    • High-resolution two-dimensional electrophoresis separation of proteins from metal-stressed rice (Oryza sativa L.) leaves: Drastic reductions/ fragmentation of ribulose-1,5-bisphosphate carboxylase/oxygenase and induction of stress-related proteins
    • DOI 10.1002/1522-2683(200108)22:13<2824::AID-ELPS2824>3.0.CO;2-C
    • Hajduch M, Rakwal R, Agrawal G K, et al. High-resolution twodimensional electrophoresis separation ofproteins from metalstressed rice (Oryza sativa L.) leaves: drastic reductions/ fragmentation of ribulose-1, 5-bisphosphate carboxylase/oxygenase and induction of stress-related proteins. Electrophoresis, 2001, 22(13): 2824-2831 (Pubitemid 32798953)
    • (2001) Electrophoresis , vol.22 , Issue.13 , pp. 2824-2831
    • Hajduch, M.1    Rakwal, R.2    Agrawal, G.K.3    Yonekura, M.4    Pretova, A.5
  • 11
    • 23844548576 scopus 로고    scopus 로고
    • A proteomic analysis of cold stress responses in rice seedlings
    • DOI 10.1002/pmic.200401148
    • Cui S, Huang F, Wang J, et al. A proteomic analysis of cold stress responses in rice seedlings. Proteomics, 2005, 5(12): 3162-3172 (Pubitemid 41176484)
    • (2005) Proteomics , vol.5 , Issue.12 , pp. 3162-3172
    • Cui, S.1    Huang, F.2    Wang, J.3    Ma, X.4    Cheng, Y.5    Liu, J.6
  • 13
    • 50249184711 scopus 로고    scopus 로고
    • Comparative proteomics analysis reveals an intimate protein network provoked by hydrogen peroxide stress in rice seedling leaves
    • Wan X Y, Liu J Y. Comparative proteomics analysis reveals an intimate protein network provoked by hydrogen peroxide stress in rice seedling leaves. Mol Cell Proteomics, 2008, 7(8): 1469-1488
    • (2008) Mol Cell Proteomics , vol.7 , Issue.8 , pp. 1469-1488
    • Wan, X.Y.1    Liu, J.Y.2
  • 14
    • 77952161465 scopus 로고    scopus 로고
    • ZEBRA-NECROSIS, a thylakoidbound protein, is critical for thephotoprotection of developing chloroplasts during early leaf development
    • Li J, Pandeya D, Nath K, et al. ZEBRA-NECROSIS, a thylakoidbound protein, is critical for thephotoprotection of developing chloroplasts during early leaf development. Plant J, 2010, 62(4): 713-725
    • (2010) Plant J , vol.62 , Issue.4 , pp. 713-725
    • Li, J.1    Pandeya, D.2    Nath, K.3
  • 16
    • 17844396912 scopus 로고    scopus 로고
    • Antibody-based proteomics for human tissue profiling
    • DOI 10.1074/mcp.R500009-MCP200
    • Uhlen M, Ponten F. Antibody-based proteomics for human tissue profiling. Mol Cell Proteomics, 2005, 4(4): 384-393 (Pubitemid 40590558)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.4 , pp. 384-393
    • Uhlen, M.1    Ponten, F.2
  • 19
    • 33644876658 scopus 로고    scopus 로고
    • Plant MPSS databases: Signature-based transcriptional resources for analyses of mRNA and small RNA
    • Database issue
    • Nakano M, Nobuta K, Vemaraju K, et al. Plant MPSS databases: Signature-based transcriptional resources for analyses of mRNA and small RNA. Nucleic Acids Res, 2006, 34 (Database issue): D731-735
    • (2006) Nucleic Acids Res , vol.34
    • Nakano, M.1    Nobuta, K.2    Vemaraju, K.3
  • 21
    • 33745936562 scopus 로고    scopus 로고
    • Structure and function of photosystems I and II
    • DOI 10.1146/annurev.arplant.57.032905.105350
    • Nelson N, Yocum C F. Structure and function of photosystems I and II. Annu Rev Plant Biol, 2006, 57: 521-565 (Pubitemid 44061036)
    • (2006) Annual Review of Plant Biology , vol.57 , pp. 521-565
    • Nelson, N.1    Yocum, C.F.2
  • 22
    • 38849125471 scopus 로고    scopus 로고
    • C-Terminal mutations in the chloroplast ATP synthase gamma subunit impair ATP synthesis and stimulate ATP hydrolysis
    • He F, Samra H S, Johnson E A, et al. C-Terminal mutations in the chloroplast ATP synthase gamma subunit impair ATP synthesis and stimulate ATP hydrolysis. Biochemistry, 2008, 47(2): 836-844
    • (2008) Biochemistry , vol.47 , Issue.2 , pp. 836-844
    • He, F.1    Samra, H.S.2    Johnson, E.A.3
  • 24
    • 44649118756 scopus 로고    scopus 로고
    • Rubiscolytics: Fate of rubisco after its enzymatic function in a cell is terminated
    • DOI 10.1093/jxb/erm242
    • Feller U, Anders I, Mae T. Rubiscolytics: fate of Rubisco after its enzymatic function in a cell is terminated. J Exp Bot, 2008, 59(7): 1615-1624 (Pubitemid 351786558)
    • (2008) Journal of Experimental Botany , vol.59 , Issue.7 , pp. 1615-1624
    • Feller, U.1    Anders, I.2    Mae, T.3
  • 26
    • 33751113885 scopus 로고    scopus 로고
    • Building up of the plastid transcriptional machinery during germination and early plant development
    • Demarsy E, Courtois F, Azevedo J, et al. Building up of the plastid transcriptional machinery during germination and early plant development. Plant Physiol, 2006, 142(3): 993-1003
    • (2006) Plant Physiol , vol.142 , Issue.3 , pp. 993-1003
    • Demarsy, E.1    Courtois, F.2    Azevedo, J.3
  • 27
    • 24644475674 scopus 로고    scopus 로고
    • Plastid RNA polymerases, promoters, and transcription regulators in higher plants
    • Shiina T, Tsunoyama Y, Nakahira Y, et al. Plastid RNA polymerases, promoters, and transcription regulators in higher plants. Int Rev Cytol, 2005, 244: 1-68
    • (2005) Int Rev Cytol , vol.244 , pp. 1-68
    • Shiina, T.1    Tsunoyama, Y.2    Nakahira, Y.3
  • 28
    • 79958082745 scopus 로고    scopus 로고
    • Structure and biogenesis of the chloroplast NAD(P)H dehydrogenase complex
    • doi:10.1016/j.bbabio.2010.10.015
    • Peng L, Yamamoto H, Shikanai T. Structure and biogenesis of the chloroplast NAD(P)H dehydrogenase complex. Biochim Biophys Acta, 2010, doi:10.1016/j.bbabio.2010.10.015
    • (2010) Biochim Biophys Acta
    • Peng, L.1    Yamamoto, H.2    Shikanai, T.3
  • 29
    • 0033978632 scopus 로고    scopus 로고
    • Chlororespiration and poising of cyclic electron transport. Plastoquinone as electron transporter between thylakoid NADH dehydrogenase and peroxidase
    • DOI 10.1074/jbc.275.2.942
    • Casano L M, Zapata J M, Martin M, et al. Chlororespiration and poising of cyclic electron transport. Plastoquinone as electron transporter between thylakoid NADH dehydrogenase and peroxidase. J Biol Chem, 2000, 275(2): 942-948 (Pubitemid 30051139)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.2 , pp. 942-948
    • Casano, L.M.1    Zapata, J.M.2    Martin, M.3    Sabater, B.4
  • 30
    • 0035099626 scopus 로고    scopus 로고
    • Hydrogen peroxide mediates the induction of chloroplastic Ndh complex under photooxidative stress in Barley
    • DOI 10.1104/pp.125.3.1450
    • Casano L M, Martin M, Sabater B. Hydrogen peroxide mediates the induction of chloroplastic Ndh complex under photooxidative stress in barley. Plant Physiol, 2001, 125(3): 1450-1458 (Pubitemid 32224633)
    • (2001) Plant Physiology , vol.125 , Issue.3 , pp. 1450-1458
    • Casano, L.M.1    Martin, M.2    Sabater, B.3
  • 31
    • 33745668217 scopus 로고    scopus 로고
    • Chloroplastic NAD(P)H dehydrogenase in tobacco leaves functions in alleviation of oxidative damage caused by temperature stress
    • DOI 10.1104/pp.105.070490
    • Wang P, Duan W, Takabayashi A, et al. Chloroplastic NAD(P)H dehydrogenase in tobacco leaves functions in alleviation of oxidative damage caused by temperature stress. Plant Physiol, 2006, 141(2): 465-474 (Pubitemid 43974541)
    • (2006) Plant Physiology , vol.141 , Issue.2 , pp. 465-474
    • Wang, P.1    Duan, W.2    Takabayashi, A.3    Endo, T.4    Shikanai, T.5    Ye, J.-Y.6    Mi, H.7


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