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Volumn 144, Issue 3, 2010, Pages 703-714

Mass spectrometry in plant proteomic analysis

Author keywords

Complex mixtures; LC MS MS; Plant sample preparation; Protein tagging; TAP tag

Indexed keywords


EID: 77957764188     PISSN: 11263504     EISSN: 17245575     Source Type: Journal    
DOI: 10.1080/11263501003764392     Document Type: Article
Times cited : (7)

References (80)
  • 1
    • 0344668825 scopus 로고    scopus 로고
    • Analysis of the Arabidopsis nuclear proteome and its response to cold stress
    • Bae MS, Cho EJ, Choi EY, Park OK. 2003. Analysis of the Arabidopsis nuclear proteome and its response to cold stress. Plant J 36(5): 652-663.
    • (2003) Plant J , vol.36 , Issue.5 , pp. 652-663
    • Bae, M.S.1    Cho, E.J.2    Choi, E.Y.3    Park, O.K.4
  • 2
    • 44249091879 scopus 로고    scopus 로고
    • Genome-scale proteomics reveals Arabidopsis thaliana gene models and proteome dynamics
    • Baerenfaller K, Grossmann J, Grobei MA, Hull R, Hirsch-Hoffmann M, Yalovsky S, et al. 2008. Genome-scale proteomics reveals Arabidopsis thaliana gene models and proteome dynamics. Science 320(5878): 938-941.
    • (2008) Science , vol.320 , Issue.5878 , pp. 938-941
    • Baerenfaller, K.1    Grossmann, J.2    Grobei, M.A.3    Hull, R.4    Hirsch-Hoffmann, M.5    Yalovsky, S.6
  • 4
    • 45649083365 scopus 로고    scopus 로고
    • Hydroponic isotope labelling of entire plants (HILEP) for quantitative plant proteomics: An oxidative stress case study
    • Bindschedler LV, Palmblad M, Cramer R. 2008. Hydroponic isotope labelling of entire plants (HILEP) for quantitative plant proteomics: An oxidative stress case study. Phytochemistry 69(10): 1962-1972.
    • (2008) Phytochemistry , vol.69 , Issue.10 , pp. 1962-1972
    • Bindschedler, L.V.1    Palmblad, M.2    Cramer, R.3
  • 5
    • 0034852208 scopus 로고    scopus 로고
    • An introduction to quadrupole-time-of-flight mass spectrometry
    • Chernushevich IV, Loboda AV, Thomson BA. 2001. An introduction to quadrupole-time-of-flight mass spectrometry. J Mass Spectrom 36(8): 849-865.
    • (2001) J Mass Spectrom , vol.36 , Issue.8 , pp. 849-865
    • Chernushevich, I.V.1    Loboda, A.V.2    Thomson, B.A.3
  • 7
    • 12244270638 scopus 로고    scopus 로고
    • Differential proteomics via probabilistic peptide identification scores
    • Colinge J, Chiappe D, Lagache S, Moniatte M, Bougueleret L. 2005. Differential proteomics via probabilistic peptide identification scores. Anal Chem 77(2): 596-606.
    • (2005) Anal Chem , vol.77 , Issue.2 , pp. 596-606
    • Colinge, J.1    Chiappe, D.2    Lagache, S.3    Moniatte, M.4    Bougueleret, L.5
  • 9
    • 11144320641 scopus 로고    scopus 로고
    • Open source system for analyzing, validating, and storing protein identification data
    • Craig R, Cortens JP, Beavis RC. 2004. Open source system for analyzing, validating, and storing protein identification data. J Proteome Res 3(6): 1234-1242.
    • (2004) J Proteome Res , vol.3 , Issue.6 , pp. 1234-1242
    • Craig, R.1    Cortens, J.P.2    Beavis, R.C.3
  • 10
    • 20544468239 scopus 로고    scopus 로고
    • High-throughput proteomics using matrix-assisted laser desorption/ionization mass spectrometry
    • Cramer R, Gobom J, Nordhoff E. 2005. High-throughput proteomics using matrix-assisted laser desorption/ionization mass spectrometry. Expert Rev Proteomics 2(3): 407-420.
    • (2005) Expert Rev Proteomics , vol.2 , Issue.3 , pp. 407-420
    • Cramer, R.1    Gobom, J.2    Nordhoff, E.3
  • 11
    • 33745533636 scopus 로고    scopus 로고
    • Microplate-based, label-free detection of biomolecular interactions: Applications in proteomics
    • Cunningham BT, Laing L. 2006. Microplate-based, label-free detection of biomolecular interactions: Applications in proteomics. Expert Rev Proteomics 3(3): 271-281.
    • (2006) Expert Rev Proteomics , vol.3 , Issue.3 , pp. 271-281
    • Cunningham, B.T.1    Laing, L.2
  • 13
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • Domon B, Aebersold R. 2006. Mass spectrometry and protein analysis. Science 312(5771): 212-217.
    • (2006) Science , vol.312 , Issue.5771 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 14
  • 15
    • 3042660176 scopus 로고    scopus 로고
    • The use of isotope-coded affinity tags (ICAT) to study organelle proteomes in Arabidopsis thaliana
    • Dunkley TP, Dupree P, Watson RB, Lilley KS. 2004. The use of isotope-coded affinity tags (ICAT) to study organelle proteomes in Arabidopsis thaliana. Biochem Soc Trans 32(Pt3): 520-523.
    • (2004) Biochem Soc Trans , vol.32 , Issue.Pt3 , pp. 520-523
    • Dunkley, T.P.1    Dupree, P.2    Watson, R.B.3    Lilley, K.S.4
  • 17
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng JK, McCormack AL, Yates JRI. 1994. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J Am Soc Mass Spectrom 5: 976-989.
    • (1994) J Am Soc Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.I.3
  • 18
    • 0141662946 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry: How it all began
    • Fenn JB. 2002. Electrospray ionization mass spectrometry: How it all began. J Biomol Tech 13(3): 101-118.
    • (2002) J Biomol Tech , vol.13 , Issue.3 , pp. 101-118
    • Fenn, J.B.1
  • 19
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn JB, Mann M, Meng CK, Wong SF, Whitehouse CM. 1989. Electrospray ionization for mass spectrometry of large biomolecules. Science 246(4926): 64-71.
    • (1989) Science , vol.246 , Issue.4926 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 21
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi SP, Rist B, Gerber SA, Turecek F, Gelb MH, Aebersold R. 1999. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat Biotechnol 17(10): 994-999.
    • (1999) Nat Biotechnol , vol.17 , Issue.10 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 22
    • 0037398266 scopus 로고    scopus 로고
    • Interfacing the orbitrap mass analyzer to an electrospray ion source
    • Hardman M, Makarov AA. 2003. Interfacing the orbitrap mass analyzer to an electrospray ion source. Anal Chem 75(7): 1699-1705.
    • (2003) Anal Chem , vol.75 , Issue.7 , pp. 1699-1705
    • Hardman, M.1    Makarov, A.A.2
  • 23
    • 0036493224 scopus 로고    scopus 로고
    • A question of size: The eukaryotic proteome and the problems in defining it
    • Harrison PM, Kumar A, Lang N, Snyder M, Gerstein M. 2002. A question of size: The eukaryotic proteome and the problems in defining it. Nucleic Acids Res 30(5): 1083-1090.
    • (2002) Nucleic Acids Res , vol.30 , Issue.5 , pp. 1083-1090
    • Harrison, P.M.1    Kumar, A.2    Lang, N.3    Snyder, M.4    Gerstein, M.5
  • 24
    • 39049154321 scopus 로고    scopus 로고
    • Study of early leaf senescence in Arabidopsis thaliana by quantitative proteomics using reciprocal 14N/15N labeling and difference gel electrophoresis
    • Hebeler R, Oeljeklaus S, Reidegeld KA, Eisenacher M, Stephan C, Sitek B, et al. 2008. Study of early leaf senescence in Arabidopsis thaliana by quantitative proteomics using reciprocal 14N/15N labeling and difference gel electrophoresis. Mol Cell Proteomics 7(1): 108-120.
    • (2008) Mol Cell Proteomics , vol.7 , Issue.1 , pp. 108-120
    • Hebeler, R.1    Oeljeklaus, S.2    Reidegeld, K.A.3    Eisenacher, M.4    Stephan, C.5    Sitek, B.6
  • 25
    • 4344702777 scopus 로고    scopus 로고
    • A mini-review of mass spectrometry using high-performance FTICR-MS methods
    • Heeren RM, Kleinnijenhuis AJ, McDonnell LA, Mize TH. 2004. A mini-review of mass spectrometry using high-performance FTICR-MS methods. Anal Bioanal Chem 378(4): 1048-1058.
    • (2004) Anal Bioanal Chem , vol.378 , Issue.4 , pp. 1048-1058
    • Heeren, R.M.1    Kleinnijenhuis, A.J.2    McDonnell, L.A.3    Mize, T.H.4
  • 27
    • 0942265386 scopus 로고    scopus 로고
    • In vivo uniform (15)N-isotope labelling of plants: Using the greenhouse for structural proteomics
    • Ippel JH, Pouvreau L, Kroef T, Gruppen H, Versteeg G, van den Putten P, et al. 2004. In vivo uniform (15)N-isotope labelling of plants: Using the greenhouse for structural proteomics. Proteomics 4(1): 226-234.
    • (2004) Proteomics , vol.4 , Issue.1 , pp. 226-234
    • Ippel, J.H.1    Pouvreau, L.2    Kroef, T.3    Gruppen, H.4    Versteeg, G.5    van den Putten, P.6
  • 28
    • 33750117539 scopus 로고    scopus 로고
    • Analysis of the defence phosphoproteome of Arabidopsis thaliana using differential mass tagging
    • Jones AM, Bennett MH, Mansfield JW, Grant M. 2006. Analysis of the defence phosphoproteome of Arabidopsis thaliana using differential mass tagging. Proteomics 6(14): 4155-4165.
    • (2006) Proteomics , vol.6 , Issue.14 , pp. 4155-4165
    • Jones, A.M.1    Bennett, M.H.2    Mansfield, J.W.3    Grant, M.4
  • 29
    • 0037329401 scopus 로고    scopus 로고
    • Ion formation in MALDI: The cluster ionization mechanism
    • Karas M, Kruger R. 2003. Ion formation in MALDI: The cluster ionization mechanism. Chem Rev 103(2): 427-440.
    • (2003) Chem Rev , vol.103 , Issue.2 , pp. 427-440
    • Karas, M.1    Kruger, R.2
  • 30
    • 3142669357 scopus 로고    scopus 로고
    • Addition of a peptide tag at the C terminus of AtHKT1 inhibits its Na+ transport
    • Kato Y, Hazama A, Yamagami M, Uozumi N. 2003. Addition of a peptide tag at the C terminus of AtHKT1 inhibits its Na+ transport. Biosci Biotechnol Biochem 67(10): 2291-2293.
    • (2003) Biosci Biotechnol Biochem , vol.67 , Issue.10 , pp. 2291-2293
    • Kato, Y.1    Hazama, A.2    Yamagami, M.3    Uozumi, N.4
  • 31
    • 44049088958 scopus 로고    scopus 로고
    • ICPL - Isotope-coded protein label
    • Kellermann J. 2008. ICPL - Isotope-coded protein label. Methods Mol Biol 424: 113-123.
    • (2008) Methods Mol Biol , vol.424 , pp. 113-123
    • Kellermann, J.1
  • 33
    • 67651122830 scopus 로고    scopus 로고
    • Dynamic behavior of Arabidopsis eIF4A-III, putative core protein of exon junction complex: Fast relocation to nucleolus and splicing speckles under hypoxia
    • Koroleva OA, Calder G, Pendle AF, Kim SH, Lewandowska D, Simpson CG, et al. 2009. Dynamic behavior of Arabidopsis eIF4A-III, putative core protein of exon junction complex: Fast relocation to nucleolus and splicing speckles under hypoxia. Plant Cell 21(5): 1592-1606.
    • (2009) Plant Cell , vol.21 , Issue.5 , pp. 1592-1606
    • Koroleva, O.A.1    Calder, G.2    Pendle, A.F.3    Kim, S.H.4    Lewandowska, D.5    Simpson, C.G.6
  • 34
    • 4544265606 scopus 로고    scopus 로고
    • CycD1, a putative G1 cyclin from Antirrhinum majus, accelerates the cell cycle in cultured tobacco BY-2 cells by enhancing both G1/S entry and progression through S and G2 phases
    • Koroleva OA, Tomlinson M, Parinyapong P, Sakvarelidze L, Leader D, Shaw P, et al. 2004. CycD1, a putative G1 cyclin from Antirrhinum majus, accelerates the cell cycle in cultured tobacco BY-2 cells by enhancing both G1/S entry and progression through S and G2 phases. Plant Cell 16(9): 2364-2379.
    • (2004) Plant Cell , vol.16 , Issue.9 , pp. 2364-2379
    • Koroleva, O.A.1    Tomlinson, M.2    Parinyapong, P.3    Sakvarelidze, L.4    Leader, D.5    Shaw, P.6
  • 35
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • Liu H, Sadygov RG, Yates JR, III. 2004. A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal Chem 76(14): 4193-4201.
    • (2004) Anal Chem , vol.76 , Issue.14 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates, J.R.3
  • 36
    • 0141989734 scopus 로고    scopus 로고
    • PEAKS: Powerful software for peptide de novo sequencing by tandem mass spectrometry
    • Ma B, Zhang K, Hendrie C, Liang C, Li M, Doherty-Kirby A, et al. 2003. PEAKS: Powerful software for peptide de novo sequencing by tandem mass spectrometry. Rapid Commun Mass Spectrom 17(20): 2337-2342.
    • (2003) Rapid Commun Mass Spectrom , vol.17 , Issue.20 , pp. 2337-2342
    • Ma, B.1    Zhang, K.2    Hendrie, C.3    Liang, C.4    Li, M.5    Doherty-Kirby, A.6
  • 38
    • 0032846162 scopus 로고    scopus 로고
    • Quantitative proteomics?
    • Mann M. 1999. Quantitative proteomics? Nat Biotechnol 17(10): 954-955.
    • (1999) Nat Biotechnol , vol.17 , Issue.10 , pp. 954-955
    • Mann, M.1
  • 39
    • 0034923505 scopus 로고    scopus 로고
    • Analysis of proteins and proteomes by mass spectrometry
    • Mann M, Hendrickson RC, Pandey A. 2001. Analysis of proteins and proteomes by mass spectrometry. Annu Rev Biochem 70: 437-473.
    • (2001) Annu Rev Biochem , vol.70 , pp. 437-473
    • Mann, M.1    Hendrickson, R.C.2    Pandey, A.3
  • 40
    • 0031623267 scopus 로고    scopus 로고
    • Fourier transform ion cyclotron resonance mass spectrometry: A primer
    • Marshall AG, Hendrickson CL, Jackson GS. 1998. Fourier transform ion cyclotron resonance mass spectrometry: A primer. Mass Spectrom Rev 17(1): 1-35.
    • (1998) Mass Spectrom Rev , vol.17 , Issue.1 , pp. 1-35
    • Marshall, A.G.1    Hendrickson, C.L.2    Jackson, G.S.3
  • 42
    • 0036671611 scopus 로고    scopus 로고
    • Phosphorylation of retinoblastoma-related protein by the cyclin D/cyclin-dependent kinase complex is activated at the G1/S-phase transition in tobacco
    • Nakagami H, Kawamura K, Sugisaka K, Sekine M, Shinmyo A. 2002. Phosphorylation of retinoblastoma-related protein by the cyclin D/cyclin-dependent kinase complex is activated at the G1/S-phase transition in tobacco. Plant Cell 14(8): 1847-1857.
    • (2002) Plant Cell , vol.14 , Issue.8 , pp. 1847-1857
    • Nakagami, H.1    Kawamura, K.2    Sugisaka, K.3    Sekine, M.4    Shinmyo, A.5
  • 44
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong SE, Blagoev B, Kratchmarova I, Kristensen DB, Steen H, Pandey A, et al. 2002. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 1(5): 376-386.
    • (2002) Mol Cell Proteomics , vol.1 , Issue.5 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6
  • 45
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong SE, Mann M. 2005. Mass spectrometry-based proteomics turns quantitative. Nat Chem Biol 1(5): 252-262.
    • (2005) Nat Chem Biol , vol.1 , Issue.5 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 46
    • 33746285299 scopus 로고    scopus 로고
    • Label-free quantitative proteomics using large peptide data sets generated by nanoflow liquid chromatography and mass spectrometry
    • Ono M, Shitashige M, Honda K, Isobe T, Kuwabara H, Matsuzuki H, et al. 2006. Label-free quantitative proteomics using large peptide data sets generated by nanoflow liquid chromatography and mass spectrometry. Mol Cell Proteomics 5(7): 1338-1347.
    • (2006) Mol Cell Proteomics , vol.5 , Issue.7 , pp. 1338-1347
    • Ono, M.1    Shitashige, M.2    Honda, K.3    Isobe, T.4    Kuwabara, H.5    Matsuzuki, H.6
  • 47
    • 35348939574 scopus 로고    scopus 로고
    • Quantitative proteomics using uniform (15)N-labeling, MASCOT, and the trans-proteomic pipeline
    • Palmblad M, Bindschedler LV, Cramer R. 2007. Quantitative proteomics using uniform (15)N-labeling, MASCOT, and the trans-proteomic pipeline. Proteomics 7(19): 3462-3469.
    • (2007) Proteomics , vol.7 , Issue.19 , pp. 3462-3469
    • Palmblad, M.1    Bindschedler, L.V.2    Cramer, R.3
  • 48
    • 0034659815 scopus 로고    scopus 로고
    • Proteomics to study genes and genomes
    • Pandey A, Mann M. 2000. Proteomics to study genes and genomes. Nature 405(6788): 837-846.
    • (2000) Nature , vol.405 , Issue.6788 , pp. 837-846
    • Pandey, A.1    Mann, M.2
  • 49
    • 30344453385 scopus 로고    scopus 로고
    • Tandem mass spectrometry in quadrupole ion trap and ion cyclotron resonance mass spectrometers
    • Payne AH, Glish GL. 2005. Tandem mass spectrometry in quadrupole ion trap and ion cyclotron resonance mass spectrometers. Methods Enzymol 402: 109-148.
    • (2005) Methods Enzymol , vol.402 , pp. 109-148
    • Payne, A.H.1    Glish, G.L.2
  • 50
    • 33748853882 scopus 로고    scopus 로고
    • Purification of GFP fusion proteins from transgenic plant cell cultures
    • Peckham GD, Bugos RC, Su WW. 2006. Purification of GFP fusion proteins from transgenic plant cell cultures. Protein Expr Purif 49(2): 183-189.
    • (2006) Protein Expr Purif , vol.49 , Issue.2 , pp. 183-189
    • Peckham, G.D.1    Bugos, R.C.2    Su, W.W.3
  • 51
    • 19944400417 scopus 로고    scopus 로고
    • Proteomic analysis of the Arabidopsis nucleolus suggests novel nucleolar functions
    • Pendle AF, Clark GP, Boon R, Lewandowska D, Lam YW, Andersen J, et al. 2005. Proteomic analysis of the Arabidopsis nucleolus suggests novel nucleolar functions. Mol Biol Cell 16(1): 260-269.
    • (2005) Mol Biol Cell , vol.16 , Issue.1 , pp. 260-269
    • Pendle, A.F.1    Clark, G.P.2    Boon, R.3    Lewandowska, D.4    Lam, Y.W.5    Andersen, J.6
  • 52
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJ, Creasy DM, Cottrell JS. 1999. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20(18): 3551-3567.
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 53
    • 61349113308 scopus 로고    scopus 로고
    • Purification of low-abundance Arabidopsis plasma-membrane protein complexes and identification of candidate components
    • Qi Y, Katagiri F. 2009. Purification of low-abundance Arabidopsis plasma-membrane protein complexes and identification of candidate components. Plant J 57(5): 932-944.
    • (2009) Plant J , vol.57 , Issue.5 , pp. 932-944
    • Qi, Y.1    Katagiri, F.2
  • 54
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut G, Shevchenko A, Rutz B, Wilm M, Mann M, Seraphin B. 1999. A generic protein purification method for protein complex characterization and proteome exploration. Nat Biotechnol 17(10): 1030-1032.
    • (1999) Nat Biotechnol , vol.17 , Issue.10 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Seraphin, B.6
  • 55
    • 0036221525 scopus 로고    scopus 로고
    • The Cf-9 disease resistance protein is present in an approximately 420-kilodalton heteromultimeric membrane-associated complex at one molecule per complex
    • Rivas S, Romeis T, Jones JD. 2002. The Cf-9 disease resistance protein is present in an approximately 420-kilodalton heteromultimeric membrane-associated complex at one molecule per complex. Plant Cell 14(3): 689-702.
    • (2002) Plant Cell , vol.14 , Issue.3 , pp. 689-702
    • Rivas, S.1    Romeis, T.2    Jones, J.D.3
  • 56
    • 1842430185 scopus 로고    scopus 로고
    • Improved tandem affinity purification tag and methods for isolation of protein heterocomplexes from plants
    • Rohila JS, Chen M, Cerny R, Fromm ME. 2004. Improved tandem affinity purification tag and methods for isolation of protein heterocomplexes from plants. Plant J 38(1): 172-181.
    • (2004) Plant J , vol.38 , Issue.1 , pp. 172-181
    • Rohila, J.S.1    Chen, M.2    Cerny, R.3    Fromm, M.E.4
  • 57
    • 33646831324 scopus 로고    scopus 로고
    • Protein-protein interactions of tandem affinity purification-tagged protein kinases in rice
    • Rohila JS, Chen M, Chen S, Chen J, Cerny R, Dardick C, et al. 2006. Protein-protein interactions of tandem affinity purification-tagged protein kinases in rice. Plant J 46(1): 1-13.
    • (2006) Plant J , vol.46 , Issue.1 , pp. 1-13
    • Rohila, J.S.1    Chen, M.2    Chen, S.3    Chen, J.4    Cerny, R.5    Dardick, C.6
  • 58
    • 0026694947 scopus 로고
    • In-gel digestion of proteins for internal sequence analysis after oneor two-dimensional gel electrophoresis
    • Rosenfeld J, Capdevielle J, Guillemot JC, Ferrara P. 1992. In-gel digestion of proteins for internal sequence analysis after oneor two-dimensional gel electrophoresis. Anal Biochem 203(1): 173-179.
    • (1992) Anal Biochem , vol.203 , Issue.1 , pp. 173-179
    • Rosenfeld, J.1    Capdevielle, J.2    Guillemot, J.C.3    Ferrara, P.4
  • 59
    • 14844310253 scopus 로고    scopus 로고
    • An alternative tandem affinity purification strategy applied to Arabidopsis protein complex isolation
    • Rubio V, Shen Y, Saijo Y, Liu Y, Gusmaroli G, Dinesh-Kumar SP, et al. 2005. An alternative tandem affinity purification strategy applied to Arabidopsis protein complex isolation. Plant J 41(5): 767-778.
    • (2005) Plant J , vol.41 , Issue.5 , pp. 767-778
    • Rubio, V.1    Shen, Y.2    Saijo, Y.3    Liu, Y.4    Gusmaroli, G.5    Dinesh-Kumar, S.P.6
  • 60
    • 57649093858 scopus 로고    scopus 로고
    • SILIP: A novel stable isotope labeling method for in planta quantitative proteomic analysis
    • Schaff JE, Mbeunkui F, Blackburn K, Bird DM, Goshe MB. 2008. SILIP: A novel stable isotope labeling method for in planta quantitative proteomic analysis. Plant J 56(5): 840-854.
    • (2008) Plant J , vol.56 , Issue.5 , pp. 840-854
    • Schaff, J.E.1    Mbeunkui, F.2    Blackburn, K.3    Bird, D.M.4    Goshe, M.B.5
  • 61
    • 3843094797 scopus 로고    scopus 로고
    • Transcriptional repression of target genes by LEUNIG and SEUSS, two interacting regulatory proteins for Arabidopsis flower development
    • Sridhar VV, Surendrarao A, Gonzalez D, Conlan RS, Liu Z. 2004. Transcriptional repression of target genes by LEUNIG and SEUSS, two interacting regulatory proteins for Arabidopsis flower development. Proc Natl Acad Sci USA 101(31): 11494-11499.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.31 , pp. 11494-11499
    • Sridhar, V.V.1    Surendrarao, A.2    Gonzalez, D.3    Conlan, R.S.4    Liu, Z.5
  • 62
    • 33748795801 scopus 로고    scopus 로고
    • APETALA1 and SEPALLATA3 interact with SEUSS to mediate transcription repression during flower development
    • Sridhar VV, Surendrarao A, Liu Z. 2006. APETALA1 and SEPALLATA3 interact with SEUSS to mediate transcription repression during flower development. Development 133(16): 3159-3166.
    • (2006) Development , vol.133 , Issue.16 , pp. 3159-3166
    • Sridhar, V.V.1    Surendrarao, A.2    Liu, Z.3
  • 63
    • 4444335470 scopus 로고    scopus 로고
    • The ABC's (and XYZ's) of peptide sequencing
    • Steen H, Mann M. 2004. The ABC's (and XYZ's) of peptide sequencing. Nat Rev Mol Cell Biol 5(9): 699-711.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , Issue.9 , pp. 699-711
    • Steen, H.1    Mann, M.2
  • 64
    • 46949090817 scopus 로고    scopus 로고
    • The DNA replication checkpoint aids survival of plants deficient in the novel replisome factor ETG1
    • Takahashi N, Lammens T, Boudolf V, Maes S, Yoshizumi T, De Jaeger G, et al. 2008. The DNA replication checkpoint aids survival of plants deficient in the novel replisome factor ETG1. EMBO J 27(13): 1840-1851.
    • (2008) EMBO J , vol.27 , Issue.13 , pp. 1840-1851
    • Takahashi, N.1    Lammens, T.2    Boudolf, V.3    Maes, S.4    Yoshizumi, T.5    de Jaeger, G.6
  • 65
    • 84984042980 scopus 로고
    • Protein and polymer analyses up to m/z 100 000 by laser ionization time-of flight mass spectrometry
    • Tanaka KW, Waki H, Ido Y, Akita S, Yoshida Y, Yoshida T. 1988. Protein and polymer analyses up to m/z 100 000 by laser ionization time-of flight mass spectrometry. Rapid Commun Mass Spectrom 2(20): 151-153.
    • (1988) Rapid Commun Mass Spectrom , vol.2 , Issue.20 , pp. 151-153
    • Tanaka, K.W.1    Waki, H.2    Ido, Y.3    Akita, S.4    Yoshida, Y.5    Yoshida, T.6
  • 66
    • 36349019368 scopus 로고    scopus 로고
    • Mitochondrial type-I prohibitins of Arabidopsis thaliana are required for supporting proficient meristem development
    • Van Aken O, Pecenkova T, van de Cotte B, De Rycke R, Eeckhout D, Fromm H, et al. 2007. Mitochondrial type-I prohibitins of Arabidopsis thaliana are required for supporting proficient meristem development. Plant J 52(5): 850-864.
    • (2007) Plant J , vol.52 , Issue.5 , pp. 850-864
    • van Aken, O.1    Pecenkova, T.2    van de Cotte, B.3    de Rycke, R.4    Eeckhout, D.5    Fromm, H.6
  • 67
    • 34547137389 scopus 로고    scopus 로고
    • A tandem affinity purificationbased technology platform to study the cell cycle interactome in Arabidopsis thaliana
    • Van Leene J, Stals H, Eeckhout D, Persiau G, Van De Slijke E, Van Isterdael G, et al. 2007. A tandem affinity purificationbased technology platform to study the cell cycle interactome in Arabidopsis thaliana. Mol Cell Proteomics 6(7): 1226-1238.
    • (2007) Mol Cell Proteomics , vol.6 , Issue.7 , pp. 1226-1238
    • van Leene, J.1    Stals, H.2    Eeckhout, D.3    Persiau, G.4    van de Slijke, E.5    van Isterdael, G.6
  • 68
    • 53149142072 scopus 로고    scopus 로고
    • Boosting tandem affinity purification of plant protein complexes
    • Van Leene J, Witters E, Inze D, De Jaeger G. 2008. Boosting tandem affinity purification of plant protein complexes. Trends Plant Sci 13(10): 517-520.
    • (2008) Trends Plant Sci , vol.13 , Issue.10 , pp. 517-520
    • van Leene, J.1    Witters, E.2    Inze, D.3    de Jaeger, G.4
  • 69
    • 33646564676 scopus 로고    scopus 로고
    • Label free protein quantification using LC-coupled ion trap or FT mass spectrometry: Reproducibility, linearity, and application with complex proteomes
    • Wang G, Wu WW, Zeng W, Chou CL, Shen RF. 2006. Label free protein quantification using LC-coupled ion trap or FT mass spectrometry: Reproducibility, linearity, and application with complex proteomes. J Proteome Res 5(5): 1214-1223.
    • (2006) J Proteome Res , vol.5 , Issue.5 , pp. 1214-1223
    • Wang, G.1    Wu, W.W.2    Zeng, W.3    Chou, C.L.4    Shen, R.F.5
  • 70
    • 10744233766 scopus 로고    scopus 로고
    • Quantification of proteins and metabolites by mass spectrometry without isotopic labeling or spiked standards
    • Wang W, Zhou H, Lin H, Roy S, Shaler TA, Hill LR, et al. 2003. Quantification of proteins and metabolites by mass spectrometry without isotopic labeling or spiked standards. Anal Chem 75(18): 4818-4826.
    • (2003) Anal Chem , vol.75 , Issue.18 , pp. 4818-4826
    • Wang, W.1    Zhou, H.2    Lin, H.3    Roy, S.4    Shaler, T.A.5    Hill, L.R.6
  • 71
    • 0028200813 scopus 로고
    • Molecular cloning of cDNAs and genes coding for betamethylcrotonyl-CoA carboxylase of tomato
    • Wang X, Wurtele ES, Keller G, McKean AL, Nikolau BJ. 1994. Molecular cloning of cDNAs and genes coding for betamethylcrotonyl-CoA carboxylase of tomato. J Biol Chem 269(16): 11760-11768.
    • (1994) J Biol Chem , vol.269 , Issue.16 , pp. 11760-11768
    • Wang, X.1    Wurtele, E.S.2    Keller, G.3    McKean, A.L.4    Nikolau, B.J.5
  • 72
    • 6044226889 scopus 로고    scopus 로고
    • Differential mass spectrometry: A label-free LC-MS method for finding significant differences in complex peptide and protein mixtures
    • Wiener MC, Sachs JR, Deyanova EG, Yates NA. 2004. Differential mass spectrometry: A label-free LC-MS method for finding significant differences in complex peptide and protein mixtures. Anal Chem 76(20): 6085-6096.
    • (2004) Anal Chem , vol.76 , Issue.20 , pp. 6085-6096
    • Wiener, M.C.1    Sachs, J.R.2    Deyanova, E.G.3    Yates, N.A.4
  • 73
    • 0025281379 scopus 로고
    • Introduction to avidin-biotin technology
    • Wilchek M, Bayer EA. 1990. Introduction to avidin-biotin technology. Methods Enzymol 184: 5-13.
    • (1990) Methods Enzymol , vol.184 , pp. 5-13
    • Wilchek, M.1    Bayer, E.A.2
  • 75
    • 7044279162 scopus 로고    scopus 로고
    • Rapid one-step protein purification from plant material using the eight-amino acid Strep II epitope
    • Witte CP, Noel LD, Gielbert J, Parker JE, Romeis T. 2004. Rapid one-step protein purification from plant material using the eight-amino acid Strep II epitope. Plant Mol Biol 55(1): 135-147.
    • (2004) Plant Mol Biol , vol.55 , Issue.1 , pp. 135-147
    • Witte, C.P.1    Noel, L.D.2    Gielbert, J.3    Parker, J.E.4    Romeis, T.5
  • 76
    • 22244489044 scopus 로고    scopus 로고
    • A hybrid LC-Gel-MS method for proteomics research and its application to protease functional pathway mapping
    • Wu S, Tang XT, Siems WF, Bruce JE. 2005. A hybrid LC-Gel-MS method for proteomics research and its application to protease functional pathway mapping. J Chromatogr B Analyt Technol Biomed Life Sci 822(1-2): 98-111.
    • (2005) J Chromatogr B Analyt Technol Biomed Life Sci , vol.822 , Issue.2 , pp. 98-111
    • Wu, S.1    Tang, X.T.2    Siems, W.F.3    Bruce, J.E.4
  • 77
    • 0035384687 scopus 로고    scopus 로고
    • Proteolytic 18O labeling for comparative proteomics: Model studies with two serotypes of adenovirus
    • Yao X, Freas A, Ramirez J, Demirev PA, Fenselau C. 2001. Proteolytic 18O labeling for comparative proteomics: Model studies with two serotypes of adenovirus. Anal Chem 73(13): 2836-2842.
    • (2001) Anal Chem , vol.73 , Issue.13 , pp. 2836-2842
    • Yao, X.1    Freas, A.2    Ramirez, J.3    Demirev, P.A.4    Fenselau, C.5
  • 78
    • 26944438704 scopus 로고    scopus 로고
    • Immunopurification of polyribosomal complexes of Arabidopsis for global analysis of gene expression
    • Zanetti ME, Chang IF, Gong F, Galbraith DW, Bailey-Serres J. 2005. Immunopurification of polyribosomal complexes of Arabidopsis for global analysis of gene expression. Plant Physiol 138(2): 624-635.
    • (2005) Plant Physiol , vol.138 , Issue.2 , pp. 624-635
    • Zanetti, M.E.1    Chang, I.F.2    Gong, F.3    Galbraith, D.W.4    Bailey-Serres, J.5
  • 79
    • 53149083819 scopus 로고    scopus 로고
    • Two distinct interacting classes of nuclear envelope-associated coiled-coil proteins are required for the tissue-specific nuclear envelope targeting of Arabidopsis RanGAP
    • Zhao Q, Brkljacic J, Meier I. 2008. Two distinct interacting classes of nuclear envelope-associated coiled-coil proteins are required for the tissue-specific nuclear envelope targeting of Arabidopsis RanGAP. Plant Cell 20(6): 1639-1651.
    • (2008) Plant Cell , vol.20 , Issue.6 , pp. 1639-1651
    • Zhao, Q.1    Brkljacic, J.2    Meier, I.3
  • 80
    • 0242653772 scopus 로고    scopus 로고
    • Development of a system for the study of protein-protein interactions in planta: Characterization of a TATA-box binding protein complex in Oryza sativa
    • Zhong J, Haynes PA, Zhang S, Yang X, Andon NL, Eckert D, et al. 2003. Development of a system for the study of protein-protein interactions in planta: Characterization of a TATA-box binding protein complex in Oryza sativa. J Proteome Res 2(5): 514-522.
    • (2003) J Proteome Res , vol.2 , Issue.5 , pp. 514-522
    • Zhong, J.1    Haynes, P.A.2    Zhang, S.3    Yang, X.4    Andon, N.L.5    Eckert, D.6


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