메뉴 건너뛰기




Volumn 31, Issue 6, 2004, Pages 563-571

Location, location, location: Surveying the intracellular real estate through proteomics in plants

Author keywords

Mass spectrometry; Membranes; Organelles; Plants; Proteomics; Subcellular fractionation

Indexed keywords

BIOLOGICAL MEMBRANES; CELLS; GENETIC ENGINEERING; PROTEINS;

EID: 3342890632     PISSN: 14454408     EISSN: None     Source Type: Journal    
DOI: 10.1071/FP04034     Document Type: Review
Times cited : (18)

References (66)
  • 1
    • 0036746523 scopus 로고    scopus 로고
    • Proteomic characterisation of wheat amyloplasts using identification of proteins by tandem mass spectrometry
    • doi:10.1002/1615-9861(200209)2:9 〈1156::AID-PROT1156〉3.0.CO;2-4
    • Andon NL, Hollingworth S, Koller A, Greenland AJ, Yates JR III, Haynes PA (2002) Proteomic characterisation of wheat amyloplasts using identification of proteins by tandem mass spectrometry. Proteomics 2, 1156-1168. doi: 10.1002/1615-9861(200209)2:9 〈1156::AID-PROT1156〉3.0.CO;2-4
    • (2002) Proteomics , vol.2 , pp. 1156-1168
    • Andon, N.L.1    Hollingworth, S.2    Koller, A.3    Greenland, A.J.4    Yates III, J.R.5    Haynes, P.A.6
  • 2
    • 0344668825 scopus 로고    scopus 로고
    • Analysis of the Arabidopsis nuclear proteome and its response to cold stress
    • doi:10.1046/J.1365-313X.2003.01907.X
    • Bae MS, Cho EJ, Choi EY, Park OK (2003) Analysis of the Arabidopsis nuclear proteome and its response to cold stress. The Plant Journal 36, 652-663. doi: 10.1046/J.1365-313X.2003.01907.X
    • (2003) The Plant Journal , vol.36 , pp. 652-663
    • Bae, M.S.1    Cho, E.J.2    Choi, E.Y.3    Park, O.K.4
  • 3
    • 0035997274 scopus 로고    scopus 로고
    • A survey of the plant mitochondrial proteome in relation to development
    • doi:10.1002/1615-9861(200207)2:7〈880:: AID-PROT880〉3.0.CO;2-0
    • Bardel J, Louwagie M, Jaquinod M, Jourdain A, Luche S, Rabilloud T, Macherel D, Garin J, Bourguignon J (2002) A survey of the plant mitochondrial proteome in relation to development. Proteomics 2, 880-898. doi: 10.1002/1615-9861(200207)2:7〈880:: AID-PROT880〉3.0.CO;2-0
    • (2002) Proteomics , vol.2 , pp. 880-898
    • Bardel, J.1    Louwagie, M.2    Jaquinod, M.3    Jourdain, A.4    Luche, S.5    Rabilloud, T.6    Macherel, D.7    Garin, J.8    Bourguignon, J.9
  • 4
    • 0031836080 scopus 로고    scopus 로고
    • Free-flow electrophoresis for fractionation of Arabidopsis thaliana membranes
    • Bardy N, Carrasco A, Galaud JP, Pont-Lezica R, Canut H (1998) Free-flow electrophoresis for fractionation of Arabidopsis thaliana membranes. Electrophoresis 19, 1145-1153.
    • (1998) Electrophoresis , vol.19 , pp. 1145-1153
    • Bardy, N.1    Carrasco, A.2    Galaud, J.P.3    Pont-Lezica, R.4    Canut, H.5
  • 5
    • 0037783246 scopus 로고    scopus 로고
    • Identification of glycosylphosphatidylinositol-anchored proteins in Arabidopsis. A proteomic and genomic analysis
    • doi:10.1104/PP.103.021170
    • Borner GH, Lilley KS, Stevens TJ, Dupree P (2003) Identification of glycosylphosphatidylinositol-anchored proteins in Arabidopsis. A proteomic and genomic analysis. Plant Physiology 132, 568-577. doi: 10.1104/PP.103.021170
    • (2003) Plant Physiology , vol.132 , pp. 568-577
    • Borner, G.H.1    Lilley, K.S.2    Stevens, T.J.3    Dupree, P.4
  • 6
    • 0036669677 scopus 로고    scopus 로고
    • Advances in gentle immunoaffinity chromatography
    • doi:10.1016/S0958-1669(02)00340-3
    • Burgess RR, Thompson NE (2002) Advances in gentle immunoaffinity chromatography. Current Opinion in Biotechnology 13, 304-308. doi: 10.1016/S0958-1669(02)00340-3
    • (2002) Current Opinion in Biotechnology , vol.13 , pp. 304-308
    • Burgess, R.R.1    Thompson, N.E.2
  • 7
    • 0141529726 scopus 로고    scopus 로고
    • A proteomic study of the Arabidopsis nuclear matrix
    • doi:10.1002/JCB.10624
    • Calikowski TT, Meulia T, Meier I (2003) A proteomic study of the Arabidopsis nuclear matrix. Journal of Cellular Biochemistry 90, 361-378. doi: 10.1002/JCB.10624
    • (2003) Journal of Cellular Biochemistry , vol.90 , pp. 361-378
    • Calikowski, T.T.1    Meulia, T.2    Meier, I.3
  • 8
    • 0344875538 scopus 로고    scopus 로고
    • Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants
    • doi:10.1074/JBC. M307525200
    • Chew O, Whelan J, Millar AH (2003) Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants. Journal of Biological Chemistry 278, 46869-46877. doi: 10.1074/JBC. M307525200
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 46869-46877
    • Chew, O.1    Whelan, J.2    Millar, A.H.3
  • 9
    • 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 JL, Soll J, Schleiff E, Millar AH, Whelan J (2004) A plant outer mitochondrial membrane protein with high amino acid sequence identity to a chloroplast protein import receptor. FEBS Letters 557, 109-114. doi: 10.1016/S0014-5793(03)01457-1
    • (2004) FEBS Letters , vol.557 , pp. 109-114
    • Chew, O.1    Lister, R.2    Qbadou, S.3    Heazlewood, J.L.4    Soll, J.5    Schleiff, E.6    Millar, A.H.7    Whelan, J.8
  • 10
    • 0036303255 scopus 로고    scopus 로고
    • Proteomic analysis of the Arabidopsis thaliana cell wall
    • doi:10.1002/1522-2683(200206)23:11〈1754::AID-ELPS1754 〉3.0.CO;2-E
    • Chivasa S, Ndimba BK, Simon WJ, Robertson D, Yu XL, Knox JP, Bolwell P, Slabas AR (2002) Proteomic analysis of the Arabidopsis thaliana cell wall. Electrophoresis 23, 1754-1765. doi: 10.1002/1522-2683(200206)23:11〈1754:: AID-ELPS1754 〉3.0.CO;2-E
    • (2002) Electrophoresis , vol.23 , pp. 1754-1765
    • Chivasa, S.1    Ndimba, B.K.2    Simon, W.J.3    Robertson, D.4    Yu, X.L.5    Knox, J.P.6    Bolwell, P.7    Slabas, A.R.8
  • 11
    • 0034724178 scopus 로고    scopus 로고
    • Random GFP::cDNA fusions enable visualisation of subcellular structures in cells of Arabidopsis at a high frequency
    • doi:10.1073/PNAS. 97.7.3718
    • Cutler SR, Ehrhardt DW, Griffitts JS, Somerville CR (2000) Random GFP::cDNA fusions enable visualisation of subcellular structures in cells of Arabidopsis at a high frequency. Proceedings of the National Academy of Sciences USA 97, 3718-3723. doi: 10.1073/PNAS. 97.7.3718
    • (2000) Proceedings of the National Academy of Sciences USA , vol.97 , pp. 3718-3723
    • Cutler, S.R.1    Ehrhardt, D.W.2    Griffitts, J.S.3    Somerville, C.R.4
  • 12
    • 0037934549 scopus 로고    scopus 로고
    • Subcellular proteomics
    • doi:10.1002/MAS.10047
    • Dreger M (2003) Subcellular proteomics. Mass Spectrometry Reviews 22, 27-56. doi: 10.1002/MAS.10047
    • (2003) Mass Spectrometry Reviews , vol.22 , pp. 27-56
    • Dreger, M.1
  • 14
    • 0141872898 scopus 로고    scopus 로고
    • Predicting protein subcellular localisation from amino acid sequence information
    • Emanuelsson O (2002) Predicting protein subcellular localisation from amino acid sequence information. Briefing in Bioinformatics 3, 361-376.
    • (2002) Briefing in Bioinformatics , vol.3 , pp. 361-376
    • Emanuelsson, O.1
  • 15
    • 0035852328 scopus 로고    scopus 로고
    • Prediction of organellar targeting signals
    • doi:10.1016/S0167-4889(01)00145-8
    • Emanuelsson O, von Heijne G (2001) Prediction of organellar targeting signals. Biochimica et Biophysica Acta 1541, 114-119. doi: 10.1016/S0167- 4889(01)00145-8
    • (2001) Biochimica et Biophysica Acta , vol.1541 , pp. 114-119
    • Emanuelsson, O.1    Von Heijne, G.2
  • 16
    • 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 NM, Haupt S, Thow G, Boevink P, Chapman S, 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. The Plant Cell 15, 1507-1523. doi: 10.1105/TPC.013284
    • (2003) The 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
  • 17
    • 0141786914 scopus 로고    scopus 로고
    • New insights into the respiratory chain of plant mitochondria, supercomplexes and a unique composition of complex II
    • doi:10.1104/PP.103.024620
    • Eubel H, Jansch L, Braun HP (2003) New insights into the respiratory chain of plant mitochondria, supercomplexes and a unique composition of complex II. Plant Physiology 133, 274-286. doi: 10.1104/PP.103.024620
    • (2003) Plant Physiology , vol.133 , pp. 274-286
    • Eubel, H.1    Jansch, L.2    Braun, H.P.3
  • 18
    • 0030112537 scopus 로고    scopus 로고
    • Plasma membrane isolation from freshwater and salt-tolerant species of Chara: Antibody cross-reactions and phosphohydrolase activities
    • Faraday CD, Spanswick RM, Bisson MA (1996) Plasma membrane isolation from freshwater and salt-tolerant species of Chara: antibody cross-reactions and phosphohydrolase activities. Journal of Experimental Botany 47, 589-594.
    • (1996) Journal of Experimental Botany , vol.47 , pp. 589-594
    • Faraday, C.D.1    Spanswick, R.M.2    Bisson, M.A.3
  • 21
    • 1042279117 scopus 로고    scopus 로고
    • In-depth analysis of the thylakoid membrane proteome of Arabidopsis thaliana chloroplasts; new proteins, functions and a plastid proteome database
    • doi:10.1105/TPC.017814
    • Friso G, Ytterberg AJ, Giacomelli L, Peltier JB, Rudella A, Sun Q, van Wijk KJ (2004) In-depth analysis of the thylakoid membrane proteome of Arabidopsis thaliana chloroplasts; new proteins, functions and a plastid proteome database. The Plant Cell 16, 478-499. doi: 10.1105/TPC.017814
    • (2004) The Plant Cell , vol.16 , pp. 478-499
    • Friso, G.1    Ytterberg, A.J.2    Giacomelli, L.3    Peltier, J.B.4    Rudella, A.5    Sun, Q.6    Van Wijk, K.J.7
  • 22
    • 0041733229 scopus 로고    scopus 로고
    • Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilising alternatives to traditional two-dimensional electrophoresis
    • doi:10.1021/ PR034025J
    • Froehlich JE, Wilkerson CG, Ray K, McAndrew RS, Osteryoung KW, Gage DA, Phinney BS (2003) Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilising alternatives to traditional two-dimensional electrophoresis. Journal of Proteome Research 2, 413-425. doi: 10.1021/ PR034025J
    • (2003) Journal of Proteome Research , vol.2 , pp. 413-425
    • Froehlich, J.E.1    Wilkerson, C.G.2    Ray, K.3    McAndrew, R.S.4    Osteryoung, K.W.5    Gage, D.A.6    Phinney, B.S.7
  • 23
    • 0036346730 scopus 로고    scopus 로고
    • Proteomic analysis of leaf peroxisomal proteins in greening cotyledons of Arabidopsis thalima
    • doi:10.1093/PCP/ PCF101
    • Fukao Y, Hayashi M, Nishimura M (2002) Proteomic analysis of leaf peroxisomal proteins in greening cotyledons of Arabidopsis thalima. Plant and Cell Physiology 43, 689-696. doi: 10.1093/PCP/ PCF101
    • (2002) Plant and Cell Physiology , vol.43 , pp. 689-696
    • Fukao, Y.1    Hayashi, M.2    Nishimura, M.3
  • 24
    • 0242403025 scopus 로고    scopus 로고
    • Novel glyoxysomal protein kinase, GPK1, identified by proteomic analysis of glyoxysomes in etiolated cotyledons of Arabidopsis thaliana
    • doi:10.1093/ PCP/PCG145
    • Fukao Y, Hayashi M, Hara-Nishimura I, Nishimura M (2003) Novel glyoxysomal protein kinase, GPK1, identified by proteomic analysis of glyoxysomes in etiolated cotyledons of Arabidopsis thaliana. Plant and Cell Physiology 44, 1002-1012. doi: 10.1093/ PCP/PCG145
    • (2003) Plant and Cell Physiology , vol.44 , pp. 1002-1012
    • Fukao, Y.1    Hayashi, M.2    Hara-Nishimura, I.3    Nishimura, M.4
  • 25
    • 0037023349 scopus 로고    scopus 로고
    • A draft sequence of the rice genome (Oryza sativa L. ssp. japonica)
    • doi:10.1126/SCIENCE.1068275
    • Goff SA, Ricke D, Lan T-H, Presting G, Wang R, et al. (2002) A draft sequence of the rice genome (Oryza sativa L. ssp. japonica). Science 296, 92-100. doi: 10.1126/SCIENCE.1068275
    • (2002) Science , vol.296 , pp. 92-100
    • Goff, S.A.1    Ricke, D.2    Lan, T.-H.3    Presting, G.4    Wang, R.5
  • 26
    • 0345864026 scopus 로고    scopus 로고
    • DBSubLoc: Database of protein subcellular localisation
    • doi:10.1093/NAR/GKH109
    • Guo T, Hua S, Ji X, Sun Z (2004) DBSubLoc: database of protein subcellular localisation. Nucleic Acids Research 32, D122-D124. doi: 10.1093/NAR/GKH109
    • (2004) Nucleic Acids Research , vol.32
    • Guo, T.1    Hua, S.2    Ji, X.3    Sun, Z.4
  • 27
    • 0036629573 scopus 로고    scopus 로고
    • Modern strategies for protein quantification in proteome analysis: Advantages and limitations
    • doi:10.1002/MAS.10032
    • Hamdan M, Righetti PG (2002) Modern strategies for protein quantification in proteome analysis: advantages and limitations. Mass Spectrometry Reviews 21, 287-302. doi: 10.1002/MAS.10032
    • (2002) Mass Spectrometry Reviews , vol.21 , pp. 287-302
    • Hamdan, M.1    Righetti, P.G.2
  • 29
    • 0037626984 scopus 로고    scopus 로고
    • Integrated plant proteomics: Putting the green genomes to work
    • doi:10.1071/FP03036
    • Heazlewood JL, Millar AH (2003) Integrated plant proteomics: putting the green genomes to work. Functional Plant Biology 30, 471-482. doi: 10.1071/FP03036
    • (2003) Functional Plant Biology , vol.30 , pp. 471-482
    • Heazlewood, J.L.1    Millar, A.H.2
  • 30
    • 0038433229 scopus 로고    scopus 로고
    • Mitochondrial complex I form Arabidopsis and rice: Orthologs of mammalian and funal components coupled with plant-specific subunits
    • doi:10.1016/80005-2728(03) 00045-8
    • Heazlewood JL, Howell KA, Millar AH (2003a) Mitochondrial complex I form Arabidopsis and rice: orthologs of mammalian and funal components coupled with plant-specific subunits. Biochimica et Biophysica Acta 1604, 159-169. doi: 10.1016/80005-2728(03) 00045-8
    • (2003) Biochimica et Biophysica Acta , vol.1604 , pp. 159-169
    • Heazlewood, J.L.1    Howell, K.A.2    Millar, A.H.3
  • 31
    • 0037509843 scopus 로고    scopus 로고
    • Towards an analysis of the rice mitochondrial proteome
    • doi:10.1104/PP.102.018986
    • Heazlewood JL, Howell KA, Whelan J, Millar AH (2003b) Towards an analysis of the rice mitochondrial proteome. Plant Physiology 132, 230-242. doi: 10.1104/PP.102.018986
    • (2003) Plant Physiology , vol.132 , pp. 230-242
    • Heazlewood, J.L.1    Howell, K.A.2    Whelan, J.3    Millar, A.H.4
  • 33
    • 0842270043 scopus 로고    scopus 로고
    • Experimental analysis of the Arabidopsis mitochondrial proteome highlights signalling and regulatory components, provides assessment of targeting prediction programs and points to plant specific mitochondrial proteins
    • doi:10.1105/TPC.016055
    • Heazlewood JL, Tonti-Filippini JS, Gout AM, Day DA, Whelan J, Millar AH (2004) Experimental analysis of the Arabidopsis mitochondrial proteome highlights signalling and regulatory components, provides assessment of targeting prediction programs and points to plant specific mitochondrial proteins. The Plant Cell 16, 241-256. doi: 10.1105/TPC.016055
    • (2004) The Plant Cell , vol.16 , pp. 241-256
    • Heazlewood, J.L.1    Tonti-Filippini, J.S.2    Gout, A.M.3    Day, D.A.4    Whelan, J.5    Millar, A.H.6
  • 34
    • 0037468460 scopus 로고    scopus 로고
    • Proteomic identification of divalent metal cation binding proteins in plant mitochondria
    • doi:10.1016/S0014-5793(03)00101-7
    • Herald VL, Heazlewood JL, Day DA, Millar AH (2003) Proteomic identification of divalent metal cation binding proteins in plant mitochondria. FEBS Letters 537, 96-100. doi: 10.1016/S0014-5793(03)00101-7
    • (2003) FEBS Letters , vol.537 , pp. 96-100
    • Herald, V.L.1    Heazlewood, J.L.2    Day, D.A.3    Millar, A.H.4
  • 35
    • 1642564541 scopus 로고    scopus 로고
    • Cytoplasmic regulation of the accumulation of nuclear-encoded proteins in the mitochondrial proteome of maize
    • Hochholdinger F, Guo L, Schnable PS (2004) Cytoplasmic regulation of the accumulation of nuclear-encoded proteins in the mitochondrial proteome of maize. The Plant Journal 37, 199-208.
    • (2004) The Plant Journal , vol.37 , pp. 199-208
    • Hochholdinger, F.1    Guo, L.2    Schnable, P.S.3
  • 36
    • 0036834966 scopus 로고    scopus 로고
    • Comparison of peptides in the phloem sap of flowering and non-flowering Perilla and lupine plants using microbore HPLC followed by matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry
    • doi:10.1007/S00425-002-0916-0
    • Hoffmann-Benning S, McIntosh DA, Gage L, Kende H, Zeevaart JAD (2002) Comparison of peptides in the phloem sap of flowering and non-flowering Perilla and lupine plants using microbore HPLC followed by matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry. Planta 216, 140-147. doi: 10.1007/S00425-002-0916-0
    • (2002) Planta , vol.216 , pp. 140-147
    • Hoffmann-Benning, S.1    McIntosh, D.A.2    Gage, L.3    Kende, H.4    Zeevaart, J.A.D.5
  • 37
    • 0038364020 scopus 로고    scopus 로고
    • Organelle proteomics: Implications for subcellular fractionation in proteomics
    • doi:10.1161/01.RES.0000071748.48338.25
    • Huber LA, Pfaller K, Vietor I (2003) Organelle proteomics: implications for subcellular fractionation in proteomics. Circulation Research 92, 962-968. doi: 10.1161/01.RES.0000071748.48338.25
    • (2003) Circulation Research , vol.92 , pp. 962-968
    • Huber, L.A.1    Pfaller, K.2    Vietor, I.3
  • 39
    • 0034947503 scopus 로고    scopus 로고
    • Mass spectrometry for protein and peptide characterisation
    • Jonsson AP (2001) Mass spectrometry for protein and peptide characterisation. Cellular and Molecular Life Sciences 58, 868-884.
    • (2001) Cellular and Molecular Life Sciences , vol.58 , pp. 868-884
    • Jonsson, A.P.1
  • 40
    • 0033773392 scopus 로고    scopus 로고
    • Proteomics meets cell biology: The establishment of subcellular proteomes
    • doi:10.1002/1522-2683(20001001)21:16〈3369::AID-ELPS3369〉3.0. CO;2-7
    • Jung E, Heller M, Sanchez JC, Hochstrasser DF (2000) Proteomics meets cell biology: the establishment of subcellular proteomes. Electrophoresis 21, 3369-3377. doi: 10.1002/1522-2683(20001001)21:16〈3369::AID-ELPS3369〉3. 0.CO;2-7
    • (2000) Electrophoresis , vol.21 , pp. 3369-3377
    • Jung, E.1    Heller, M.2    Sanchez, J.C.3    Hochstrasser, D.F.4
  • 41
    • 0347755545 scopus 로고    scopus 로고
    • Rice proteome database based on two-dimensional polyacrylamide gel electrophoresis: Its status in 2003
    • doi:10.1093/NAR/GKH020
    • Komatsu S, Kojima K, Suzuki K, Ozaki K, Higo K (2004) Rice proteome database based on two-dimensional polyacrylamide gel electrophoresis: its status in 2003. Nucleic Acids Research 32, D388-D392. doi: 10.1093/NAR/GKH020
    • (2004) Nucleic Acids Research , vol.32
    • Komatsu, S.1    Kojima, K.2    Suzuki, K.3    Ozaki, K.4    Higo, K.5
  • 42
    • 85047683107 scopus 로고    scopus 로고
    • Proteomic approach to identify novel mitochondrial proteins in Arabidopsis
    • doi:10.1104/PP.127. 4.1694
    • Kruft V, Eubel H, Jansch L, Werhahn W, Braun HP (2001) Proteomic approach to identify novel mitochondrial proteins in Arabidopsis. Plant Physiology 127, 1694-1710. doi: 10.1104/PP.127. 4.1694
    • (2001) Plant Physiology , vol.127 , pp. 1694-1710
    • Kruft, V.1    Eubel, H.2    Jansch, L.3    Werhahn, W.4    Braun, H.P.5
  • 43
    • 0036120467 scopus 로고    scopus 로고
    • Proteomic analysis of the endoplasmic reticulum from developing and germinating seed of castor (Ricinus communis)
    • doi:10.1002/1522-2683(200202)23:4〈626::AID-ELPS626〉3.0.CO;2-#
    • Maltman DJ, Simon WJ, Wheeler CH, Dunn MJ, Wait R, Slabas AR (2002) Proteomic analysis of the endoplasmic reticulum from developing and germinating seed of castor (Ricinus communis). Electrophoresis 23, 626-639. doi: 10.1002/1522-2683(200202)23:4〈626::AID-ELPS626〉3.0.CO;2-#
    • (2002) Electrophoresis , vol.23 , pp. 626-639
    • Maltman, D.J.1    Simon, W.J.2    Wheeler, C.H.3    Dunn, M.J.4    Wait, R.5    Slabas, A.R.6
  • 44
    • 0037321898 scopus 로고    scopus 로고
    • Genomic and proteomic analysis of mitochondrial carrier proteins in Arabidopsis
    • doi:10.1104/PP.009985
    • Millar AH, Heazlewood JL (2003) Genomic and proteomic analysis of mitochondrial carrier proteins in Arabidopsis. Plant Physiology 131, 443-453. doi: 10.1104/PP.009985
    • (2003) Plant Physiology , vol.131 , pp. 443-453
    • Millar, A.H.1    Heazlewood, J.L.2
  • 45
    • 67651108027 scopus 로고    scopus 로고
    • Analysis of the Arabidopsis mitochondrial proteome
    • doi:10.1104/PP127.4.1711
    • Millar AH, Sweetlove LJ, Giege P, Leaver CJ (2001) Analysis of the Arabidopsis mitochondrial proteome. Plant Physiology 127, 1711-1727. doi: 10.1104/PP127.4.1711
    • (2001) Plant Physiology , vol.127 , pp. 1711-1727
    • Millar, A.H.1    Sweetlove, L.J.2    Giege, P.3    Leaver, C.J.4
  • 46
    • 0036107468 scopus 로고    scopus 로고
    • Identification of defence-related cell wall proteins in Phytophthorasojae-infected soybean roots by ESI-MS/MS
    • doi:10.1046/J.1364-3703.2002.00109.X
    • Mithoefer A, Mueller B, Wanner G, Eichacker LA (2002) Identification of defence-related cell wall proteins in Phytophthorasojae-infected soybean roots by ESI-MS/MS. Molecular Plant Pathology 3, 163-166. doi: 10.1046/J.1364-3703. 2002.00109.X
    • (2002) Molecular Plant Pathology , vol.3 , pp. 163-166
    • Mithoefer, A.1    Mueller, B.2    Wanner, G.3    Eichacker, L.A.4
  • 47
    • 11444263845 scopus 로고    scopus 로고
    • Large-scale analysis of in vivo phosphorylated membrane proteins by immobilised metal ion affinity chromatography and mass spectrometry
    • doi:10.1074/MCP.T300006-MCP200
    • Nuhse TS, Stensballe A, Jensen ON, Peck SC (2003) Large-scale analysis of in vivo phosphorylated membrane proteins by immobilised metal ion affinity chromatography and mass spectrometry. Molecular and Cellular Proteomics 2, 1234-1243. doi: 10.1074/MCP.T300006-MCP200
    • (2003) Molecular and Cellular Proteomics , vol.2 , pp. 1234-1243
    • Nuhse, T.S.1    Stensballe, A.2    Jensen, O.N.3    Peck, S.C.4
  • 48
    • 0035852247 scopus 로고    scopus 로고
    • Dual targeting to mitochondria and chloroplasts
    • doi:10.1016/S0167-4889(01)00146-X
    • Peeters N, Small I (2001) Dual targeting to mitochondria and chloroplasts. Biochimica et Biophysica Acta 1541, 54-63. doi: 10.1016/S0167-4889(01)00146-X
    • (2001) Biochimica et Biophysica Acta , vol.1541 , pp. 54-63
    • Peeters, N.1    Small, I.2
  • 49
    • 0034026047 scopus 로고    scopus 로고
    • Proteomics of the chloroplast: Systematic identification and largeting analysis of lumenal and peripheral thylakoid proteins
    • doi:10.1105/ TPC.12.3.319
    • Peltier JB, Friso G, Kalume DE, Roepstorff P, Nilsson F, Adamska I, van Wijk KJ (2000) Proteomics of the chloroplast: systematic identification and largeting analysis of lumenal and peripheral thylakoid proteins. The Plant Cell 12, 319-341. doi: 10.1105/ TPC.12.3.319
    • (2000) The Plant Cell , vol.12 , pp. 319-341
    • Peltier, J.B.1    Friso, G.2    Kalume, D.E.3    Roepstorff, P.4    Nilsson, F.5    Adamska, I.6    Van Wijk, K.J.7
  • 50
    • 0036007922 scopus 로고    scopus 로고
    • Central functions of the lumenal and peripheral thylakoid proteome of Arabidopsis determined by experimentation and genome-wide prediction
    • doi:10.1105/TPC.010304
    • Peltier J-B, Emanuelsson O, Kalume DE, Ytterberg J, Friso G, et al. (2002) Central functions of the lumenal and peripheral thylakoid proteome of Arabidopsis determined by experimentation and genome-wide prediction. The Plant Cell 14, 211-236. doi: 10.1105/TPC.010304
    • (2002) The Plant Cell , vol.14 , pp. 211-236
    • Peltier, J.-B.1    Emanuelsson, O.2    Kalume, D.E.3    Ytterberg, J.4    Friso, G.5
  • 51
    • 0033769445 scopus 로고    scopus 로고
    • A proteomic analysis of organelles from Arabidopsis thaliana
    • doi:10.1002/1522-2683(20001001)21:16〈3488::AID-ELPS3488〉3.0. CO;2-3
    • Prime TA, Sherrier DJ, Mahon P, Packman LC, Dupree P (2000) A proteomic analysis of organelles from Arabidopsis thaliana. Electrophoresis 21, 3488-3499. doi: 10.1002/1522-2683(20001001)21:16〈3488::AID-ELPS3488〉3.0.CO;2-3
    • (2000) Electrophoresis , vol.21 , pp. 3488-3499
    • Prime, T.A.1    Sherrier, D.J.2    Mahon, P.3    Packman, L.C.4    Dupree, P.5
  • 52
    • 0036438898 scopus 로고    scopus 로고
    • The import of ferredoxin-NADP+ reductase precursor into chloroplasts is modulated by the region between the transit peptide and the mature core of the protein
    • doi:10.1046/J.1432-1033.2002.03233.X
    • Rial DV, Lombardo VA, Ceccarelli EA, Ottado J (2002) The import of ferredoxin-NADP+ reductase precursor into chloroplasts is modulated by the region between the transit peptide and the mature core of the protein. European Journal of Biochemistry 269, 5431-5439. doi: 10.1046/J.1432-1033.2002.03233.X
    • (2002) European Journal of Biochemistry , vol.269 , pp. 5431-5439
    • Rial, D.V.1    Lombardo, V.A.2    Ceccarelli, E.A.3    Ottado, J.4
  • 53
    • 0038015611 scopus 로고    scopus 로고
    • Evolutionary diversification of mitochondrial proteomes: Implications for human disease
    • doi:10.1016/S0168-9525(03)00137-9
    • Richly E, Chinnery PF, Leister D (2003) Evolutionary diversification of mitochondrial proteomes: implications for human disease. Trends in Genetics 19, 356-362. doi: 10.1016/S0168-9525(03)00137-9
    • (2003) Trends in Genetics , vol.19 , pp. 356-362
    • Richly, E.1    Chinnery, P.F.2    Leister, D.3
  • 54
    • 0023354237 scopus 로고
    • Lipid composition of plasma membranes isolated from light-grown barley (Hordeum vulgare) leaves: Identification of cerebroside as a major component
    • Rochester CP, Kjellbom P, Andersson B, Larsson C (1987) Lipid composition of plasma membranes isolated from light-grown barley (Hordeum vulgare) leaves: identification of cerebroside as a major component. Archives of Biochemistry and Biophysics 255, 385-391.
    • (1987) Archives of Biochemistry and Biophysics , vol.255 , pp. 385-391
    • Rochester, C.P.1    Kjellbom, P.2    Andersson, B.3    Larsson, C.4
  • 55
    • 0036211102 scopus 로고    scopus 로고
    • Characterisation by proteomics of peribacteroid space and peribacteroid membrane preparations from pea (Pisum sativum) symbiosomes
    • doi:10.1002/1615-9861(200203)2:3〈325::AID-PROT325〉3.0. CO;2-W
    • Saalbach G, Erik P, Wienkoop S (2002) Characterisation by proteomics of peribacteroid space and peribacteroid membrane preparations from pea (Pisum sativum) symbiosomes. Proteomics 2, 325-337. doi: 10.1002/1615-9861(200203)2: 3〈325::AID-PROT325〉3.0. CO;2-W
    • (2002) Proteomics , vol.2 , pp. 325-337
    • Saalbach, G.1    Erik, P.2    Wienkoop, S.3
  • 56
    • 0032746655 scopus 로고    scopus 로고
    • Large scale characterisation of plant plasma membrane proteins
    • doi:10.1016/S0300-9084 (99)80122-9
    • Santoni V, Doumas P, Rouquie D, Mansion M, Rabilloud T, Rossignol M (1999) Large scale characterisation of plant plasma membrane proteins. Biochimie 81, 655-661. doi: 10.1016/S0300-9084 (99)80122-9
    • (1999) Biochimie , vol.81 , pp. 655-661
    • Santoni, V.1    Doumas, P.2    Rouquie, D.3    Mansion, M.4    Rabilloud, T.5    Rossignol, M.6
  • 57
    • 0037667409 scopus 로고    scopus 로고
    • A proteomic study reveals novel insights into the diversity of aquaporin forms expressed in the plasma membrane of plant roots
    • doi:10.1042/ BJ20030159
    • Santoni V, Vinh J, Pflieger D, Sommerer N, Maurel C (2003) A proteomic study reveals novel insights into the diversity of aquaporin forms expressed in the plasma membrane of plant roots. The Biochemical Journal 373, 289-296. doi: 10.1042/ BJ20030159
    • (2003) The Biochemical Journal , vol.373 , pp. 289-296
    • Santoni, V.1    Vinh, J.2    Pflieger, D.3    Sommerer, N.4    Maurel, C.5
  • 60
    • 0345865040 scopus 로고    scopus 로고
    • Localising the proteome
    • doi:10.1186/GB-2003-4-12-240
    • Simpson JC, Pepperkok R (2003) Localising the proteome. Genome Biology 4, 240. doi: 10.1186/GB-2003-4-12-240
    • (2003) Genome Biology , vol.4 , pp. 240
    • Simpson, J.C.1    Pepperkok, R.2
  • 62
    • 3142671423 scopus 로고    scopus 로고
    • Proteomics of the rice cell: Systematic identification of the protein population in subcellular compartments
    • In press. doi:10.1007/S00438-004-1002-Z
    • Tanaka N, Fujita M, Handa H, Murayama S, Uemura M, et al. (2004) Proteomics of the rice cell: systematic identification of the protein population in subcellular compartments. Molecular Genetics and Genomics. In press. doi: 10.1007/S00438-004-1002-Z
    • (2004) Molecular Genetics and Genomics
    • Tanaka, N.1    Fujita, M.2    Handa, H.3    Murayama, S.4    Uemura, M.5
  • 63
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • doi:10.1038/35048692
    • The Arabidopsis genome initiative (2000) Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 408, 796-815. doi: 10.1038/35048692
    • (2000) Nature , vol.408 , pp. 796-815
  • 64
    • 0036119404 scopus 로고    scopus 로고
    • Biochemical dissection of the mitochondrial proteome from Arabidopsis thaliana by three-dimensional gel electrophoresis
    • doi:10.1002/1522-2683(200202)23:4〈640::AID-ELPS640〉3.0. CO;2-F
    • Werhahn W, Braun HP (2002) Biochemical dissection of the mitochondrial proteome from Arabidopsis thaliana by three-dimensional gel electrophoresis. Electrophoresis 23, 640-646. doi: 10.1002/1522-2683(200202)23:4〈640::AID- ELPS640〉3.0. CO;2-F
    • (2002) Electrophoresis , vol.23 , pp. 640-646
    • Werhahn, W.1    Braun, H.P.2
  • 65
    • 0037353653 scopus 로고    scopus 로고
    • Proteome analysis. Novel proteins identified at the peribacteroid membrane from Lotus japonicus root nodules
    • doi:10.1104/PP.102. 015362
    • Wienkoop S, Saalbach G (2003) Proteome analysis. Novel proteins identified at the peribacteroid membrane from Lotus japonicus root nodules. Plant Physiology 131, 1080-1090. doi: 10.1104/PP.102. 015362
    • (2003) Plant Physiology , vol.131 , pp. 1080-1090
    • Wienkoop, S.1    Saalbach, G.2
  • 66
    • 0034927421 scopus 로고    scopus 로고
    • The N-terminal portion of mature aldehyde dehydrogenase affects protein folding and assembly
    • doi:10.1110/PS.5301
    • Zhou J, Weiner H (2001) The N-terminal portion of mature aldehyde dehydrogenase affects protein folding and assembly. Protein Science 10, 1490-1497. doi: 10.1110/PS.5301
    • (2001) Protein Science , vol.10 , pp. 1490-1497
    • Zhou, J.1    Weiner, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.