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Volumn , Issue 85, 2014, Pages

A new approach for the comparative analysis of multiprotein complexes based on 15N metabolic labeling and quantitative mass spectrometry

Author keywords

Chlamydomonas; Issue 85; Microbiology; Multiprotein complexes; Sucrose density gradients; Thylakoids

Indexed keywords


EID: 84897409989     PISSN: 1940087X     EISSN: None     Source Type: Journal    
DOI: 10.3791/51103     Document Type: Article
Times cited : (3)

References (51)
  • 1
    • 33745604530 scopus 로고    scopus 로고
    • Cyclic electron flow in C3 plants
    • doi:10.1016/j.bbabio.2006.02.018
    • Joliot, P., & Joliot, A. Cyclic electron flow in C3 plants. Biochim. Biophys. Acta. 1757 (5/6), 362-368, (2006). doi:10.1016/j.bbabio.2006.02.018
    • (2006) Biochim. Biophys. Acta , vol.1757 , Issue.5-6 , pp. 362-368
    • Joliot, P.1    Joliot, A.2
  • 2
    • 34250847628 scopus 로고    scopus 로고
    • Cyclic electron transport around photosystem I: Genetic approaches
    • doi:10.1146/annurev.arplant.58.091406.110525
    • Shikanai, T. Cyclic electron transport around photosystem I: genetic approaches. Annu. Rev. Plant Biol. 58, 199-217, (2007). doi:10.1146/annurev.arplant.58.091406.110525
    • (2007) Annu. Rev. Plant Biol , vol.58 , pp. 199-217
    • Shikanai, T.1
  • 3
    • 0032754899 scopus 로고    scopus 로고
    • State transitions, cyclic and linear electron transport and photophosphorylation in Chlamydomonas reinhardtii
    • doi: 10.1016/S0005-2728(99)00089-4
    • Finazzi, G., Furia, A., Barbagallo, R. P., & Forti, G. State transitions, cyclic and linear electron transport and photophosphorylation in Chlamydomonas reinhardtii. Biochim. Biophys. Acta. 1413 (3), 117-129, (1999). doi: 10.1016/S0005-2728(99)00089-4
    • (1999) Biochim. Biophys. Acta , vol.1413 , Issue.3 , pp. 117-129
    • Finazzi, G.1    Furia, A.2    Barbagallo, R.P.3    Forti, G.4
  • 4
    • 80051938286 scopus 로고    scopus 로고
    • Control of hydrogen photoproduction by the proton gradient generated by cyclic electron flow in Chlamydomonas reinhardtii
    • doi: 10.1105/tpc.111.086876
    • Tolleter, D., et al. Control of hydrogen photoproduction by the proton gradient generated by cyclic electron flow in Chlamydomonas reinhardtii. Plant Cell. 23 (7), 2619-2630, (2011). doi: 10.1105/tpc.111.086876
    • (2011) Plant Cell , vol.23 , Issue.7 , pp. 2619-2630
    • Tolleter, D.1
  • 5
    • 84873442819 scopus 로고    scopus 로고
    • PGRL1 Is the Elusive Ferredoxin-Plastoquinone Reductase in Photosynthetic Cyclic Electron Flow
    • doi: 10.1016/j.molcel.2012.11.030
    • Hertle, A. P., et al. PGRL1 Is the Elusive Ferredoxin-Plastoquinone Reductase in Photosynthetic Cyclic Electron Flow. Mol. Cell. 49 (3), 511-523, (2013). doi: 10.1016/j.molcel.2012.11.030
    • (2013) Mol. Cell , vol.49 , Issue.3 , pp. 511-523
    • Hertle, A.P.1
  • 6
    • 84867914796 scopus 로고    scopus 로고
    • Calcium-dependent regulation of cyclic photosynthetic electron transfer by a CAS, ANR1, and PGRL1 complex
    • doi: 10.1073/pnas.1207118109
    • Terashima, M., et al. Calcium-dependent regulation of cyclic photosynthetic electron transfer by a CAS, ANR1, and PGRL1 complex. PNAS. 109 (43), 17717-17722, (2012). doi: 10.1073/pnas.1207118109
    • (2012) PNAS , vol.109 , Issue.43 , pp. 17717-17722
    • Terashima, M.1
  • 7
    • 77951622488 scopus 로고    scopus 로고
    • Isolation of the elusive supercomplex that drives cyclic electron flow in photosynthesis
    • doi: 10.1038/nature08885
    • Iwai, M., Takizawa, K., Tokutsu, R., Okamuro, A., Takahashi, Y., & Minagawa, J. Isolation of the elusive supercomplex that drives cyclic electron flow in photosynthesis. Nature. 464 (7292), 1210-1213, (2010). doi: 10.1038/nature08885
    • (2010) Nature , vol.464 , Issue.7292 , pp. 1210-1213
    • Iwai, M.1    Takizawa, K.2    Tokutsu, R.3    Okamuro, A.4    Takahashi, Y.5    Minagawa, J.6
  • 8
    • 0001347379 scopus 로고
    • Thylakoid Membrane Polypeptides of Chlamydomonas reinhardtii: Wild-Type and Mutant Strains Deficient in Photosystem II Reaction Center
    • doi: 10.1073/pnas.72.6.2175
    • Chua, N. H. & Bennoun, P. Thylakoid Membrane Polypeptides of Chlamydomonas reinhardtii: Wild-Type and Mutant Strains Deficient in Photosystem II Reaction Center. PNAS. 72 (6), 2175-2179, (1975). doi: 10.1073/pnas.72.6.2175
    • (1975) PNAS , vol.72 , Issue.6 , pp. 2175-2179
    • Chua, N.H.1    Bennoun, P.2
  • 9
    • 31044439022 scopus 로고    scopus 로고
    • Identification of the mobile light-harvesting complex II polypeptides for state transitions in Chlamydomonas reinhardtii
    • doi: 10.1073/pnas.0509952103
    • Takahashi, H., Iwai, M., Takahashi, Y. & Minagawa, J. Identification of the mobile light-harvesting complex II polypeptides for state transitions in Chlamydomonas reinhardtii. PNAS. 103 (2), 477-482, (2006). doi: 10.1073/pnas.0509952103
    • (2006) PNAS , vol.103 , Issue.2 , pp. 477-482
    • Takahashi, H.1    Iwai, M.2    Takahashi, Y.3    Minagawa, J.4
  • 10
    • 0000621830 scopus 로고
    • Phosphorylation of Photosystem II Components, CP43 Apoprotein, D1, D2, and 10 to 11 Kilodalton Protein in Chloroplast Thylakoids of Higher Plants
    • doi: 10.1104/pp.85.3.638
    • Ikeuchi, M., Plumley, F. G., Inoue, Y. & Schmidt, G. W. Phosphorylation of Photosystem II Components, CP43 Apoprotein, D1, D2, and 10 to 11 Kilodalton Protein in Chloroplast Thylakoids of Higher Plants. Plant Physiol. 85 (3), 638-642, (1987). doi: 10.1104/pp.85.3.638
    • (1987) Plant Physiol , vol.85 , Issue.3 , pp. 638-642
    • Ikeuchi, M.1    Plumley, F.G.2    Inoue, Y.3    Schmidt, G.W.4
  • 11
    • 0033537961 scopus 로고    scopus 로고
    • Determination of the Stoichiometry and Strength of Binding of Xanthophylls to the Photosystem II Light Harvesting Complexes
    • doi: 10.1074/jbc.274.15.10458
    • Ruban, A. V., Lee, P. J., Wentworth, M., Young, A. J. & Horton, P. Determination of the Stoichiometry and Strength of Binding of Xanthophylls to the Photosystem II Light Harvesting Complexes. J. Biol. Chem. 274 (15), 10458-10465, (1999). doi: 10.1074/jbc.274.15.10458
    • (1999) J. Biol. Chem , vol.274 , Issue.15 , pp. 10458-10465
    • Ruban, A.V.1    Lee, P.J.2    Wentworth, M.3    Young, A.J.4    Horton, P.5
  • 12
    • 84869219071 scopus 로고    scopus 로고
    • Characterization of PSII-LHCII supercomplexes isolated from pea thylakoid membrane by one-step treatment with α- and β-dodecyl-D-maltoside
    • doi: 10.1098/rstb.2012.0056
    • Barera, S., Pagliano, C., Pape, T., Saracco, G. & Barber, J. Characterization of PSII-LHCII supercomplexes isolated from pea thylakoid membrane by one-step treatment with α- and β-dodecyl-D-maltoside. Phil. Trans. R. Soc. B. 367 (1608), 3389-3399, (2012). doi: 10.1098/rstb.2012.0056
    • (2012) Phil. Trans. R. Soc. B , vol.367 , Issue.1608 , pp. 3389-3399
    • Barera, S.1    Pagliano, C.2    Pape, T.3    Saracco, G.4    Barber, J.5
  • 13
    • 34548595687 scopus 로고    scopus 로고
    • A comparative approach towards thylakoid membrane proteome analysis of unicellular green alga Scenedesmus obliquus
    • doi: 10.1016/j.bbamem.2007.04.028
    • Kantzilakis, K. et al. A comparative approach towards thylakoid membrane proteome analysis of unicellular green alga Scenedesmus obliquus. Biochim. Biophys. Acta. 1768 (9), 2271-2279, (2007). doi: 10.1016/j.bbamem.2007.04.028
    • (2007) Biochim. Biophys. Acta , vol.1768 , Issue.9 , pp. 2271-2279
    • Kantzilakis, K.1
  • 14
    • 2942750314 scopus 로고    scopus 로고
    • Comparison of the subunit compositions of the PSI-LHCI supercomplex and the LHCI in the green alga Chlamydomonas reinhardtii
    • doi: 10.1021/bi035988z
    • Takahashi, Y., Yasui, T., Stauber, E. J. & Hippler, M. Comparison of the subunit compositions of the PSI-LHCI supercomplex and the LHCI in the green alga Chlamydomonas reinhardtii. Biochemistry. 43 (24), 7816-7823, (2004). doi: 10.1021/bi035988z
    • (2004) Biochemistry , vol.43 , Issue.24 , pp. 7816-7823
    • Takahashi, Y.1    Yasui, T.2    Stauber, E.J.3    Hippler, M.4
  • 15
    • 37849025862 scopus 로고    scopus 로고
    • Quantitative proteomics in plants: Choices in abundance
    • doi: 10.1105/tpc.107.053991
    • Thelen, J. J. & Peck, S. C. Quantitative proteomics in plants: choices in abundance. Plant Cell. 19 (11), 3339-3346, (2007). doi: 10.1105/tpc.107.053991
    • (2007) Plant Cell , vol.19 , Issue.11 , pp. 3339-3346
    • Thelen, J.J.1    Peck, S.C.2
  • 16
    • 84871873478 scopus 로고    scopus 로고
    • The Proteome of Copper, Iron, Zinc, and Manganese Micronutrient Deficiency in Chlamydomonas reinhardtii
    • doi: 10.1074/mcp.M112.021840
    • Hsieh, S. et al. The Proteome of Copper, Iron, Zinc, and Manganese Micronutrient Deficiency in Chlamydomonas reinhardtii. Mol. Cell. Proteom. 12 (1), 65-86, (2013). doi: 10.1074/mcp.M112.021840
    • (2013) Mol. Cell. Proteom , vol.12 , Issue.1 , pp. 65-86
    • Hsieh, S.1
  • 17
    • 84870893631 scopus 로고    scopus 로고
    • HILIC- and SCX-based quantitative proteomics of Chlamydomonas reinhardtii during nitrogen starvation induced lipid and carbohydrate accumulation
    • doi: 10.1021/pr300692t
    • Longworth, J., Noirel, J., Pandhal, J., Wright, P. C. & Vaidyanathan, S. HILIC- and SCX-based quantitative proteomics of Chlamydomonas reinhardtii during nitrogen starvation induced lipid and carbohydrate accumulation. J. Proteome Res. 11 (12), 5959-5971, (2012). doi: 10.1021/pr300692t
    • (2012) J. Proteome Res , vol.11 , Issue.12 , pp. 5959-5971
    • Longworth, J.1    Noirel, J.2    Pandhal, J.3    Wright, P.C.4    Vaidyanathan, S.5
  • 18
    • 84876213081 scopus 로고    scopus 로고
    • Zinc deficiency impacts CO2 assimilation and disrupts copper homeostasis in Chlamydomonas reinhardtii
    • doi: 10.1074/jbc.M113.455105
    • Malasarn, D. et al. Zinc deficiency impacts CO2 assimilation and disrupts copper homeostasis in Chlamydomonas reinhardtii. J. Biol. Chem. 288 (15), 10672-10683, (2013). doi: 10.1074/jbc.M113.455105
    • (2013) J. Biol. Chem , vol.288 , Issue.15 , pp. 10672-10683
    • Malasarn, D.1
  • 19
    • 84885107729 scopus 로고    scopus 로고
    • The metabolic status drives acclimation of iron deficieny responses in Chlamydomonas reinhardtii as revealed by proteomics based hierarchical clustering and reverse genetics
    • doi: 10.1074/mcp.M113.029991mcp.M113.029991, epub ahead of print
    • Höhner, R. et al. The metabolic status drives acclimation of iron deficieny responses in Chlamydomonas reinhardtii as revealed by proteomics based hierarchical clustering and reverse genetics. Mol. Cell. Proteomics (2013). doi: 10.1074/mcp.M113.029991mcp.M113.029991, epub ahead of print
    • (2013) Mol. Cell. Proteomics
    • Höhner, R.1
  • 20
    • 84857628792 scopus 로고    scopus 로고
    • Proteomic analysis of a model unicellular green alga, Chlamydomonas reinhardtii, during short-term exposure to irradiance stress reveals significant down regulation of several heat-shock proteins
    • doi: 10.1007/s00425-011-1521-x
    • Mahong, B., Roytrakul, S., Phaonaklop, N., Wongratana, J. & Yokthongwattana, K. Proteomic analysis of a model unicellular green alga, Chlamydomonas reinhardtii, during short-term exposure to irradiance stress reveals significant down regulation of several heat-shock proteins. Planta. 235 (3), 499-511, (2012). doi: 10.1007/s00425-011-1521-x
    • (2012) Planta , vol.235 , Issue.3 , pp. 499-511
    • Mahong, B.1    Roytrakul, S.2    Phaonaklop, N.3    Wongratana, J.4    Yokthongwattana, K.5
  • 21
    • 33747780498 scopus 로고    scopus 로고
    • Comparative proteomics of high light stress in the model alga Chlamydomonas reinhardtii
    • doi: 10.1002/pmic.200500907
    • Förster, B., Mathesius, U. & Pogson, B. J. Comparative proteomics of high light stress in the model alga Chlamydomonas reinhardtii. Proteomics. 6 (15), 4309-4320, (2006). doi: 10.1002/pmic.200500907
    • (2006) Proteomics , vol.6 , Issue.15 , pp. 4309-4320
    • Förster, B.1    Mathesius, U.2    Pogson, B.J.3
  • 22
    • 80053200706 scopus 로고    scopus 로고
    • The chloroplast calcium sensor CAS is required for photoacclimation in Chlamydomonas reinhardtii
    • doi: 10.1105/tpc.111.087973
    • Petroutsos, D., et al. The chloroplast calcium sensor CAS is required for photoacclimation in Chlamydomonas reinhardtii. Plant Cell. 23 (8), 2950-2963, (2011). doi: 10.1105/tpc.111.087973
    • (2011) Plant Cell , vol.23 , Issue.8 , pp. 2950-2963
    • Petroutsos, D.1
  • 23
    • 77952530584 scopus 로고    scopus 로고
    • The language of calcium signaling
    • doi: 10.1146/annurev-arplant-070109-104628
    • Dodd, A. N., Kudla, J., & Sanders, D. The language of calcium signaling. Annu. Rev. Plant Biol. 61, 593-620, (2010). doi: 10.1146/annurev-arplant-070109-104628
    • (2010) Annu. Rev. Plant Biol , vol.61 , pp. 593-620
    • Dodd, A.N.1    Kudla, J.2    Sanders, D.3
  • 24
    • 40549107148 scopus 로고    scopus 로고
    • Evidence for chloroplast control of external Ca2+-induced cytosolic Ca2+ transients and stomatal closure
    • doi: 10.1111/j.1365-313X.2007.03390.x
    • Nomura, H., Komori, T., Kobori, M., Nakahira, Y. & Shiina, T. Evidence for chloroplast control of external Ca2+-induced cytosolic Ca2+ transients and stomatal closure. Plant J. 53 (6), 988-998, (2008). doi: 10.1111/j.1365-313X.2007.03390.x
    • (2008) Plant J , vol.53 , Issue.6 , pp. 988-998
    • Nomura, H.1    Komori, T.2    Kobori, M.3    Nakahira, Y.4    Shiina, T.5
  • 25
    • 48249155356 scopus 로고    scopus 로고
    • A plastid protein crucial for Ca2+-regulated stomatal responses
    • doi: 10.1111/j.1469-8137.2008.02492.x
    • Weinl, S., et al. A plastid protein crucial for Ca2+-regulated stomatal responses. New Phytol. 179 (3), 675-686, (2008). doi: 10.1111/j.1469-8137.2008.02492.x
    • (2008) New Phytol , vol.179 , Issue.3 , pp. 675-686
    • Weinl, S.1
  • 26
    • 77952825427 scopus 로고    scopus 로고
    • Characterizing the anaerobic response of Chlamydomonas reinhardtii by quantitative proteomics
    • doi: 10.1074/mcp.M900421-MCP200
    • Terashima, M., Specht, M., Naumann, B., & Hippler, M. Characterizing the anaerobic response of Chlamydomonas reinhardtii by quantitative proteomics. Mol. Cell. Proteomics.9 (7), 1514-1532, (2010). doi: 10.1074/mcp.M900421-MCP200
    • (2010) Mol. Cell. Proteomics , vol.9 , Issue.7 , pp. 1514-1532
    • Terashima, M.1    Specht, M.2    Naumann, B.3    Hippler, M.4
  • 27
    • 70450227314 scopus 로고    scopus 로고
    • PGRL1 participates in iron-induced remodeling of the photosynthetic apparatus and in energy metabolism in Chlamydomonas reinhardtii
    • doi: 10.1074/jbc.M109.050468
    • Petroutsos, D., et al. PGRL1 participates in iron-induced remodeling of the photosynthetic apparatus and in energy metabolism in Chlamydomonas reinhardtii. J. Biol. Chem. 284 (47), 32770-32781, (2009). doi: 10.1074/jbc.M109.050468
    • (2009) J. Biol. Chem , vol.284 , Issue.47 , pp. 32770-32781
    • Petroutsos, D.1
  • 28
    • 38749133045 scopus 로고    scopus 로고
    • A complex containing PGRL1 and PGR5 is involved in the switch between linear and cyclic electron flow in Arabidopsis
    • doi: 10.1016/j.cell.2007.12.028
    • DalCorso, G., et al. A complex containing PGRL1 and PGR5 is involved in the switch between linear and cyclic electron flow in Arabidopsis. Cell. 132 (2), 273-285, (2008). doi: 10.1016/j.cell.2007.12.028
    • (2008) Cell , vol.132 , Issue.2 , pp. 273-285
    • Dalcorso, G.1
  • 29
    • 0032472375 scopus 로고    scopus 로고
    • A systematic survey of conserved histidines in the core subunits of Photosystem I by site-directed mutagenesis reveals the likely axial ligands of P700
    • doi: 10.1093/emboj/17.1.50
    • Redding, K., et al. A systematic survey of conserved histidines in the core subunits of Photosystem I by site-directed mutagenesis reveals the likely axial ligands of P700. EMBO J. 17 (1), 50-60, (1998). doi: 10.1093/emboj/17.1.50
    • (1998) EMBO J , vol.17 , Issue.1 , pp. 50-60
    • Redding, K.1
  • 31
    • 26044440113 scopus 로고
    • Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophylls a and b extracted with four different solvents: Verification of the concentration of chlorophyll standards by atomic absorption spectroscopy
    • doi: 10.1016/S0005-2728(89)80347-0
    • Porra, R. J., Thompson, W. A. & Kriedemann, P. E. Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophylls a and b extracted with four different solvents: verification of the concentration of chlorophyll standards by atomic absorption spectroscopy. Biochim. Biophys. Acta. 975 (3), 384-394, (1989). doi: 10.1016/S0005-2728(89)80347-0
    • (1989) Biochim. Biophys. Acta , vol.975 , Issue.3 , pp. 384-394
    • Porra, R.J.1    Thompson, W.A.2    Kriedemann, P.E.3
  • 32
    • 20144382680 scopus 로고    scopus 로고
    • N-terminal processing of Lhca3 Is a key step in remodeling of the photosystem I-light-harvesting complex under iron deficiency in Chlamydomonas reinhardtii
    • doi: 10.1074/jbc.M414486200
    • Naumann, B., Stauber, E. J., Busch, A., Sommer, F., & Hippler, M. N-terminal processing of Lhca3 Is a key step in remodeling of the photosystem I-light-harvesting complex under iron deficiency in Chlamydomonas reinhardtii. J. Biol. Chem. 280 (21), 20431-20441, (2005). doi: 10.1074/jbc.M414486200
    • (2005) J. Biol. Chem , vol.280 , Issue.21 , pp. 20431-20441
    • Naumann, B.1    Stauber, E.J.2    Busch, A.3    Sommer, F.4    Hippler, M.5
  • 33
    • 0035543903 scopus 로고    scopus 로고
    • Towards functional proteomics of membrane protein complexes: Analysis of thylakoid membranes from Chlamydomonas reinhardtii
    • doi: 10.1046/j.1365-313X.2001.01175.x
    • Hippler, M., Klein, J., Fink, A, Allinger, T. & Hoerth, P. Towards functional proteomics of membrane protein complexes: analysis of thylakoid membranes from Chlamydomonas reinhardtii. Plant J. 28 (5), 595-606, (2001). doi: 10.1046/j.1365-313X.2001.01175.x
    • (2001) Plant J , vol.28 , Issue.5 , pp. 595-606
    • Hippler, M.1    Klein, J.2    Fink, A.3    Allinger, T.4    Hoerth, P.5
  • 34
    • 36048942406 scopus 로고    scopus 로고
    • Comparative quantitative proteomics to investigate the remodeling of bioenergetic pathways under iron deficiency in Chlamydomonas reinhardtii
    • doi: 10.1002/pmic.200700407
    • Naumann, B., et al. Comparative quantitative proteomics to investigate the remodeling of bioenergetic pathways under iron deficiency in Chlamydomonas reinhardtii. Proteomics. 7 (21), 3964-3979, (2007). doi: 10.1002/pmic.200700407
    • (2007) Proteomics , vol.7 , Issue.21 , pp. 3964-3979
    • Naumann, B.1
  • 35
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • doi: 10.1038/nprot.2006.468
    • Shevchenko, A., Tomas, H., Havlis, J., Olsen, J. V & Mann, M. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Prot. 1 (6), 2856-2860, (2006). doi: 10.1038/nprot.2006.468
    • (2006) Nat. Prot , vol.1 , Issue.6 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 36
    • 79954562400 scopus 로고    scopus 로고
    • Proteomics to go: Proteomatic enables the user-friendly creation of versatile MS/MS data evaluation workflows
    • doi: 10.1093/bioinformatics/btr081
    • Specht, M., Kuhlgert, S., Fufezan, C., & Hippler, M. Proteomics to go: Proteomatic enables the user-friendly creation of versatile MS/MS data evaluation workflows. Bioinformatics. 27 (8), 1183-1184, (2011). doi: 10.1093/bioinformatics/btr081
    • (2011) Bioinformatics , vol.27 , Issue.8 , pp. 1183-1184
    • Specht, M.1    Kuhlgert, S.2    Fufezan, C.3    Hippler, M.4
  • 37
    • 7044246160 scopus 로고    scopus 로고
    • Open mass spectrometry search algorithm
    • doi: 10.1021/pr0499491
    • Geer, L. Y., et al. Open mass spectrometry search algorithm. J. Proteome Res. 3 (5), 958-964, (2004). doi: 10.1021/pr0499491
    • (2004) J. Proteome Res , vol.3 , Issue.5 , pp. 958-964
    • Geer, L.Y.1
  • 38
    • 3142702204 scopus 로고    scopus 로고
    • TANDEM: Matching proteins with tandem mass spectra
    • doi: 10.1093/bioinformatics/bth092
    • Craig, R. & Beavis, R. C. TANDEM: matching proteins with tandem mass spectra. Bioinformatics. 20 (9), 1466-1467, (2004). doi: 10.1093/bioinformatics/bth092
    • (2004) Bioinformatics , vol.20 , Issue.9 , pp. 1466-1467
    • Craig, R.1    Beavis, R.C.2
  • 39
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • doi: 10.1038/NMETH1019
    • Elias, J. E. & Gygi, S. P. Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat. Methods. 4 (3), 207-214, (2007). doi: 10.1038/NMETH1019
    • (2007) Nat. Methods , vol.4 , Issue.3 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 40
    • 63549095080 scopus 로고    scopus 로고
    • QVALITY: Non-parametric estimation of q-values and posterior error probabilities
    • doi: 10.1093/bioinformatics/btp021
    • Käll, L., Storey, J. D. & Noble, W. S. QVALITY: non-parametric estimation of q-values and posterior error probabilities. Bioinformatics. 25 (7), 964-966, (2009). doi: 10.1093/bioinformatics/btp021
    • (2009) Bioinformatics , vol.25 , Issue.7 , pp. 964-966
    • Käll, L.1    Storey, J.D.2    Noble, W.S.3
  • 41
    • 0019996218 scopus 로고
    • A new chlorophyll-protein complex related to photosystem I in Chlamydomonas reinhardtii
    • Wollman, F. A. & Bennoun, P. A new chlorophyll-protein complex related to photosystem I in Chlamydomonas reinhardtii. Biochim. Biophys. Acta. 680, 352-360 (1982).
    • (1982) Biochim. Biophys. Acta , vol.680 , pp. 352-360
    • Wollman, F.A.1    Bennoun, P.2
  • 42
    • 0037127195 scopus 로고    scopus 로고
    • A critical role for the Var2 FtsH homologue of Arabidopsis thaliana in the photosystem II repair cycle in vivo
    • doi: 10.1074/jbc.M105878200
    • Bailey, S. et al. A critical role for the Var2 FtsH homologue of Arabidopsis thaliana in the photosystem II repair cycle in vivo. J. Biol. Chem. 277 (3), 2006-2011, (2002). doi: 10.1074/jbc.M105878200
    • (2002) J. Biol. Chem , vol.277 , Issue.3 , pp. 2006-2011
    • Bailey, S.1
  • 43
    • 70350051346 scopus 로고    scopus 로고
    • Protein quality control in chloroplasts: A current model of D1 protein degradation in the photosystem II repair cycle
    • doi: 10.1093/jb/mvp073
    • Kato, Y. & Sakamoto, W. Protein quality control in chloroplasts: a current model of D1 protein degradation in the photosystem II repair cycle. J. Biochem. 146 (4), 463-469, (2009). doi: 10.1093/jb/mvp073
    • (2009) J. Biochem , vol.146 , Issue.4 , pp. 463-469
    • Kato, Y.1    Sakamoto, W.2
  • 44
    • 0344404400 scopus 로고    scopus 로고
    • A nuclear-encoded protein of prokaryotic origin is essential for the stability of photosystem II in Arabidopsis thaliana
    • doi: 10.1093/emboj/17.18.5286
    • Meurer, J., Plücken, H., Kowallik, K. V & Westhoff, P. A nuclear-encoded protein of prokaryotic origin is essential for the stability of photosystem II in Arabidopsis thaliana. EMBO J. 17 (18), 5286-5297, (1998). doi: 10.1093/emboj/17.18.5286
    • (1998) EMBO J , vol.17 , Issue.18 , pp. 5286-5297
    • Meurer, J.1    Plücken, H.2    Kowallik, K.V.3    Westhoff, P.4
  • 45
    • 0028178516 scopus 로고
    • The assembly of cytochrome b6/f complexes: An approach using genetic transformation of the green alga Chlamydomonas reinhardtii
    • Kuras, R. & Wollman, F. A. The assembly of cytochrome b6/f complexes: an approach using genetic transformation of the green alga Chlamydomonas reinhardtii. EMBO J. 13 (5), 1019-1027 (1994).
    • (1994) EMBO J , vol.13 , Issue.5 , pp. 1019-1027
    • Kuras, R.1    Wollman, F.A.2
  • 46
    • 0033213399 scopus 로고    scopus 로고
    • Analysis of the nucleus-encoded and chloroplast-targeted rieske protein by classic and site-directed mutagenesis of Chlamydomonas
    • doi: 10.1105/tpc.11.10.2031
    • de Vitry, C., Finazzi, G., Baymann, F. & Kallas, T. Analysis of the nucleus-encoded and chloroplast-targeted rieske protein by classic and site-directed mutagenesis of Chlamydomonas. Plant Cell. 11 (10), 2031-2044, (1999). doi: 10.1105/tpc.11.10.2031
    • (1999) Plant Cell , vol.11 , Issue.10 , pp. 2031-2044
    • de Vitry, C.1    Finazzi, G.2    Baymann, F.3    Kallas, T.4
  • 47
    • 0034595810 scopus 로고    scopus 로고
    • A new subunit of cytochrome b6f complex undergoes reversible phosphorylation upon state transition
    • doi: 10.1074/jbc.M001468200
    • Hamel, P., Olive, J., Pierre, Y., Wollman, F. A. & de Vitry, C. A new subunit of cytochrome b6f complex undergoes reversible phosphorylation upon state transition. J. Biol. Chem. 275 (22), 17072-17079, (2000). doi: 10.1074/jbc.M001468200
    • (2000) J. Biol. Chem , vol.275 , Issue.22 , pp. 17072-17079
    • Hamel, P.1    Olive, J.2    Pierre, Y.3    Wollman, F.A.4    de Vitry, C.5
  • 48
    • 71049185887 scopus 로고    scopus 로고
    • Quantitative proteomics reveals a dynamic association of proteins to detergent-resistant membranes upon elicitor signaling in tobacco
    • doi: 10.1074/mcp.M900090-MCP200
    • Stanislas, T., et al. Quantitative proteomics reveals a dynamic association of proteins to detergent-resistant membranes upon elicitor signaling in tobacco. Mol. Cell. Proteomics. 8 (9), 2186-2198, (2009). doi: 10.1074/mcp.M900090-MCP200
    • (2009) Mol. Cell. Proteomics , vol.8 , Issue.9 , pp. 2186-2198
    • Stanislas, T.1
  • 49
    • 66749108480 scopus 로고    scopus 로고
    • A proteomic survey of Chlamydomonas reinhardtii mitochondria sheds new light on the metabolic plasticity of the organelle and on the nature of the alpha-proteobacterial mitochondrial ancestor
    • doi: 10.1093/molbev/msp068
    • Atteia, A., et al. A proteomic survey of Chlamydomonas reinhardtii mitochondria sheds new light on the metabolic plasticity of the organelle and on the nature of the alpha-proteobacterial mitochondrial ancestor. Mol. Biol. Evol. 26 (7), 1533-1548, (2009). doi: 10.1093/molbev/msp068
    • (2009) Mol. Biol. Evol , vol.26 , Issue.7 , pp. 1533-1548
    • Atteia, A.1
  • 50
    • 84862221877 scopus 로고    scopus 로고
    • Comparison of the α and β isomeric forms of the detergent n-dodecyl-D-maltoside for solubilizing photosynthetic complexes from pea thylakoid membranes
    • doi: 10.1016/j.bbabio.2011.11.001
    • Pagliano, C., Barera, S., Chimirri, F., Saracco, G., & Barber, J. Comparison of the α and β isomeric forms of the detergent n-dodecyl-D-maltoside for solubilizing photosynthetic complexes from pea thylakoid membranes. Biochim. Biophys. Acta. 1817 (8), 1506-1515, (2012). doi: 10.1016/j.bbabio.2011.11.001
    • (2012) Biochim. Biophys. Acta , vol.1817 , Issue.8 , pp. 1506-1515
    • Pagliano, C.1    Barera, S.2    Chimirri, F.3    Saracco, G.4    Barber, J.5
  • 51
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • doi: 10.1038/NMETH.1322
    • Wisniewski, J. R., Zougman, A., Nagaraj, N., & Mann, M. Universal sample preparation method for proteome analysis. Nat. Methods. 6 (5), 3-7, (2009). doi: 10.1038/NMETH.1322
    • (2009) Nat. Methods , vol.6 , Issue.5 , pp. 3-7
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4


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