메뉴 건너뛰기




Volumn 6, Issue APR, 2015, Pages

Two-dimensional phos-tag zymograms for tracing phosphoproteins by activity in-gel staining

Author keywords

High resolution clear native electrophoresis; IEF; In gel activity staining; NEPHGE; Phos tag; Phosphorylation

Indexed keywords

PHOS;

EID: 84928107334     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2015.00230     Document Type: Article
Times cited : (3)

References (50)
  • 1
    • 84855544323 scopus 로고    scopus 로고
    • Identification of phos-phoproteins in Arabidopsis thaliana leaves using polyethylene glycol fraction-ation, immobilized metal-ion affinity chromatography, two-dimensional gel electrophoresis and mass spectrometry
    • Aryal, U. K., Krochko, J. E., and Ross, A. R. (2012). Identification of phos-phoproteins in Arabidopsis thaliana leaves using polyethylene glycol fraction-ation, immobilized metal-ion affinity chromatography, two-dimensional gel electrophoresis and mass spectrometry. J. Proteome Res. 11, 425–437. doi: 10.1021/pr200917t
    • (2012) J. Proteome Res , vol.11 , pp. 425-437
    • Aryal, U.K.1    Krochko, J.E.2    Ross, A.R.3
  • 2
    • 66749150525 scopus 로고    scopus 로고
    • Phosphoryla-tion regulates the ferritoid-ferritin interaction and nuclear transport
    • Beazley, K. E., Nurminskaya, M., and Linsenmayer, T. F. (2009). Phosphoryla-tion regulates the ferritoid-ferritin interaction and nuclear transport. J. Cell Biochem. 107, 528–536. doi: 10.1002/jcb.22154
    • (2009) J. Cell Biochem , vol.107 , pp. 528-536
    • Beazley, K.E.1    Nurminskaya, M.2    Linsenmayer, T.F.3
  • 3
    • 84867168886 scopus 로고    scopus 로고
    • Phosphoproteome dynamics upon changes in plant water status reveal early events associated with rapid growth adjustment in maize leaves
    • Bonhomme, L., Valot, B., Tardieu, F., and Zivy, M. (2012). Phosphoproteome dynamics upon changes in plant water status reveal early events associated with rapid growth adjustment in maize leaves. Mol. Cell Proteomics 11, 957–972. doi: 10.1074/mcp.M111.015867
    • (2012) Mol. Cell Proteomics , vol.11 , pp. 957-972
    • Bonhomme, L.1    Valot, B.2    Tardieu, F.3    Zivy, M.4
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248–254. doi: 10.1016/0003-2697(76)90527-3
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 70349771207 scopus 로고    scopus 로고
    • Non-classical 2-D electrophoresis
    • Burré, J., Wittig, I., and Schägger, H. (2009). Non-classical 2-D electrophoresis. Methods Mol. Biol. 564, 33–57. doi: 10.1007/978-1-60761-157-8_3
    • (2009) Methods Mol. Biol , vol.564 , pp. 33-57
    • Burré, J.1    Wittig, I.2    Schägger, H.3
  • 6
    • 3142783406 scopus 로고    scopus 로고
    • Nano-scale proteomics approach using two-dimensional fibrin zymography combined with fluorescent SYPRO ruby dye
    • Choi, N. S., Yoo, K. H., Yoon, K. S., Maeng, P. J., and Kim, S. H. (2004). Nano-scale proteomics approach using two-dimensional fibrin zymography combined with fluorescent SYPRO ruby dye. J. Biochem. Mol. Biol. 37, 298–303. doi: 10.5483/BMBRep.2004.37.3.298
    • (2004) J. Biochem. Mol. Biol , vol.37 , pp. 298-303
    • Choi, N.S.1    Yoo, K.H.2    Yoon, K.S.3    Maeng, P.J.4    Kim, S.H.5
  • 7
    • 84881372065 scopus 로고    scopus 로고
    • Protein-serine/threonine/tyrosine kinases in bacterial signaling and regulation
    • Cousin, C., Derouiche, A., Shi, L., Pagot, Y., Poncet, S., and Mijakovic, I. (2013). Protein-serine/threonine/tyrosine kinases in bacterial signaling and regulation. FEMS Microbiol. Lett. 346, 11–19. doi: 10.1111/1574-6968.12189
    • (2013) FEMS Microbiol. Lett , vol.346 , pp. 11-19
    • Cousin, C.1    Derouiche, A.2    Shi, L.3    Pagot, Y.4    Poncet, S.5    Mijakovic, I.6
  • 8
    • 77950957988 scopus 로고    scopus 로고
    • Detection of phosphorylated T and B cell antigen receptor species by Phos-tag SDS- and Blue Native-PAGE
    • Deswal, S., Beck-García, K., Blumenthal, B., Dopfer, E. P., and Schamel, W. W. (2010). Detection of phosphorylated T and B cell antigen receptor species by Phos-tag SDS- and Blue Native-PAGE. Immun. Lett. 130, 51–56. doi: 10.1016/j.imlet.2009.12.012
    • (2010) Immun. Lett , vol.130 , pp. 51-56
    • Deswal, S.1    Beck-García, K.2    Blumenthal, B.3    Dopfer, E.P.4    Schamel, W.W.5
  • 9
    • 73849110528 scopus 로고    scopus 로고
    • Techniques for phosphopep-tide enrichment prior to analysis by mass spectrometry
    • Dunn, J. D., Reid, G. E., and Bruening, M. L. (2010). Techniques for phosphopep-tide enrichment prior to analysis by mass spectrometry. Mass Spectrom. Rev. 29, 29–54. doi: 10.1002/mas.20219
    • (2010) Mass Spectrom. Rev , vol.29 , pp. 29-54
    • Dunn, J.D.1    Reid, G.E.2    Bruening, M.L.3
  • 10
    • 84862201492 scopus 로고    scopus 로고
    • A phosphoproteomic approach towards the understanding of the role of TGF-β in Trypanosoma cruzi biology
    • Ferrão, P. M., de Oliveira, F. L., Degrave, W. M., Araujo-Jorge, T. C., Mendonça-Lima, L., and Waghabi, M. C. (2012). A phosphoproteomic approach towards the understanding of the role of TGF-β in Trypanosoma cruzi biology. PLoS ONE 7:e38736. doi: 10.1371/journal.pone.0038736
    • (2012) Plos ONE , pp. 7
    • Ferrão, P.M.1    De Oliveira, F.L.2    Degrave, W.M.3    Araujo-Jorge, T.C.4    Mendonça-Lima, L.5    Waghabi, M.C.6
  • 11
    • 77953826242 scopus 로고    scopus 로고
    • Physiological and proteomic characterization of manganese sensitivity and tolerance in rice (Oryzasativa) in comparison with barley (Hordeumvul-gare)
    • Führs, H., Behrens, C., Gallien, S., Heintz, D., Van Dorsselaer, A., Braun, H. P., et al. (2010).Physiological and proteomic characterization of manganese sensitivity and tolerance in rice (Oryzasativa) in comparison with barley (Hordeumvul-gare). Ann. Bot. 105, 1129–1110. doi: 10.1093/aob/mcq046
    • (2010) Ann. Bot , vol.105 , pp. 1110-1129
    • Führs, H.1    Behrens, C.2    Gallien, S.3    Heintz, D.4    Van Dorsselaer, A.5    Braun, H.P.6
  • 12
    • 65349092907 scopus 로고    scopus 로고
    • Characterization of leaf apoplastic peroxidases and metabolites in Vignaunguiculata in response to toxic manganese supply and silicon
    • Führs, H., Götze, S., Specht, A., Erban, A., Gallien, S., Heintz, D., et al. (2009). Characterization of leaf apoplastic peroxidases and metabolites in Vignaunguiculata in response to toxic manganese supply and silicon. J. Exp. Bot. 60, 1663–1678. doi: 10.1093/jxb/erp034
    • (2009) J. Exp. Bot , vol.60 , pp. 1663-1678
    • Führs, H.1    Götze, S.2    Specht, A.3    Erban, A.4    Gallien, S.5    Heintz, D.6
  • 13
    • 84866129426 scopus 로고    scopus 로고
    • Gel Electrophoresis of Proteins
    • eds J. Davey and M. Lord (Oxford, UK: Oxford University Press
    • Garfin, D. E. (2003). “Gel Electrophoresis of Proteins,”in Essential Cell Biology, Vol. 1: Cell Structure, A Practical Approach, eds J. Davey and M. Lord (Oxford, UK: Oxford University Press), 197–268.
    • (2003) Essential Cell Biology, Vol. 1: Cell Structure, a Practical Approach , pp. 197-268
    • Garfin, D.E.1
  • 14
    • 84885217184 scopus 로고    scopus 로고
    • From inventory to functional mechanisms
    • Gerbeth, C., Mikropoulou, D., and Meisinger, C. (2013). From inventory to functional mechanisms. FEBS J. 280, 4933–4942. doi: 10.1111/febs.12445
    • (2013) FEBS J , vol.280 , pp. 4933-4942
    • Gerbeth, C.1    Mikropoulou, D.2    Meisinger, C.3
  • 15
    • 12044258919 scopus 로고
    • Fe-Chelate reductase activity of plasma membranes isolated from tomato (Lycopersicon esculentum Mill.) roots: Comparison of enzymes from fe-deficient and fe-sufficient roots
    • Holden, M. J., Luster, D. G., Chaney, R. L., Buckhout, T. J., and Robinson, C. (1991). Fe-Chelate reductase activity of plasma membranes isolated from tomato (Lycopersicon esculentum Mill.) roots: comparison of enzymes from fe-deficient and fe-sufficient roots. Plant Physiol. 97, 537–544. doi: 10.1104/pp.97.2.537
    • (1991) Plant Physiol , vol.97 , pp. 537-544
    • Holden, M.J.1    Luster, D.G.2    Chaney, R.L.3    Buckhout, T.J.4    Robinson, C.5
  • 16
    • 0027375522 scopus 로고
    • Protein internal flexibility and global stability: Effect of urea on hydrogen exchange rates of bovine pancreatic trypsin inhibitor
    • Kim, K. S., and Woodward, C. (1993). Protein internal flexibility and global stability: effect of urea on hydrogen exchange rates of bovine pancreatic trypsin inhibitor. Biochemistry 32, 9609–9613. doi: 10.1021/bi00088a013
    • (1993) Biochemistry , vol.32 , pp. 9609-9613
    • Kim, K.S.1    Woodward, C.2
  • 17
    • 84855963980 scopus 로고    scopus 로고
    • Phos-tag SDS-PAGE systems for phosphorylation profiling of proteins with a wide range of molecular masses under neutral pH conditions
    • Kinoshita, E., and Kinoshita-Kikuta, E. (2012). Phos-tag SDS-PAGE systems for phosphorylation profiling of proteins with a wide range of molecular masses under neutral pH conditions. Proteomics 12, 192–202. doi: 10.1002/pmic.201100524
    • (2012) Proteomics , vol.12 , pp. 192-202
    • Kinoshita, E.1    Kinoshita-Kikuta, E.2
  • 18
    • 33645714857 scopus 로고    scopus 로고
    • Phosphate-binding tag, a new tool to visualize phosphorylated proteins. Mol
    • Kinoshita, E., Kinoshita-Kikuta, E., Takiyama, K., and Koike, T. (2006). Phosphate-binding tag, a new tool to visualize phosphorylated proteins. Mol. Cell. 5, 749–757. doi: 10.1074/mcp.T500024-MCP200
    • (2006) Cell , vol.5 , pp. 749-757
    • Kinoshita, E.1    Kinoshita-Kikuta, E.2    Takiyama, K.3    Koike, T.4
  • 19
    • 33847688584 scopus 로고    scopus 로고
    • Label-free kinase profiling using phosphate affinity polyacrylamide gel electrophoresis
    • Kinoshita-Kikuta, E., Aoki, Y, Kinoshita, E, Koike T. (2007). Label-free kinase profiling using phosphate affinity polyacrylamide gel electrophoresis. MCP 6, 356–366. doi: 10.1074/mcp.T600044-MCP200
    • (2007) MCP , vol.6 , pp. 356-366
    • Kinoshita-Kikuta, E.1    Aoki, Y.2    Kinoshita, E.3    Koike, T.4
  • 20
    • 84866706005 scopus 로고    scopus 로고
    • Cell wall-bound cationic and anionic class III isoperoxidases of pea root: Biochemical characterization and function in root growth
    • Kukavica, B. M., Veljovic-Jovanovic, S. D., Menckhoff, L., and Lüthje, S. (2012). Cell wall-bound cationic and anionic class III isoperoxidases of pea root: biochemical characterization and function in root growth. J. Exp. Bot. 63, 4631–4645. doi: 10.1093/jxb/ers139
    • (2012) J. Exp. Bot , vol.63 , pp. 4631-4645
    • Kukavica, B.M.1    Veljovic-Jovanovic, S.D.2    Menckhoff, L.3    Lüthje, S.4
  • 21
    • 0035258294 scopus 로고    scopus 로고
    • Phospho-proteomics: Evaluation of the use of enzymatic de-phosphorylation and differential mass spectrometric peptide mass mapping for site specific phosphorylation assignment in proteins separated by gel electrophore-sis
    • Larsen, M. R., Sørensen, G. L., Fey, S. J., Larsen, P. M., and Roepstorff, P. (2001). Phospho-proteomics: evaluation of the use of enzymatic de-phosphorylation and differential mass spectrometric peptide mass mapping for site specific phosphorylation assignment in proteins separated by gel electrophore-sis. Proteomics 1, 223–238. doi: 10.1002/1615-9861(200102)1:2<223::AID-PROT223>3.0.CO;2-B
    • (2001) Proteomics , vol.1 , pp. 223-238
    • Larsen, M.R.1    Sørensen, G.L.2    Fey, S.J.3    Larsen, P.M.4    Roepstorff, P.5
  • 22
    • 63049138916 scopus 로고    scopus 로고
    • Database searching and accounting of multiplexed precursor and product ion spectra from the data independent analysis of simple and complex peptide mixtures
    • Li, G. Z., Vissers, J. P., Silva, J. C., Golick, D., Gorenstein, M. V., and Gero-manos, S. J. (2009). Database searching and accounting of multiplexed precursor and product ion spectra from the data independent analysis of simple and complex peptide mixtures. Proteomics 9, 1696–1719. doi: 10.1002/pmic.200800564
    • Proteomics , vol.9 , pp. 1696-1719
    • Li, G.Z.1    Vissers, J.P.2    Silva, J.C.3    Golick, D.4    Gorenstein, M.V.5    Gero-Manos, S.J.6
  • 23
    • 84903441921 scopus 로고    scopus 로고
    • Nonequilibrium pH Gel Electrophoresis (NEPHGE)
    • ed J. M. Walker (Totowa, NJ: Human Press Inc.)
    • Lopez, F. (2002). “Nonequilibrium pH Gel Electrophoresis (NEPHGE),” in The Protein Protocols Handbook 2nd Edn. ed J. M. Walker (Totowa, NJ: Human Press Inc.), 181–183.
    • (2002) The Protein Protocols Handbook 2Nd Edn , pp. 181-183
    • Lopez, F.1
  • 24
    • 84934438395 scopus 로고    scopus 로고
    • Class III peroxidases
    • J. V. Jorrín Novo, S. Komatsu, W. Weckwerth, S. Wienkoop (New York, NY: Humana Press Inc
    • Lüthje, S., Meisrimler, C. N., Hopff, D., Schütze, T., Köppe, J., and Heino, K. (2014). “Class III peroxidases,” in Plant Proteomics, ed J. V. Jorrín Novo, S. Komatsu, W. Weckwerth, S. Wienkoop (New York, NY: Humana Press Inc), 687–706.
    • (2014) Plant Proteomics , pp. 687-706
    • Lüthje, S.1    Meisrimler, C.N.2    Hopff, D.3    Schütze, T.4    Köppe, J.5    Heino, K.6
  • 25
    • 33847409736 scopus 로고    scopus 로고
    • Purification of phosphoproteins by immobilized metal affinity chromatography and its application to phosphoproteome analysis
    • Machida, M., Kosako, H., Shirakabe, K., Kobayashi, M., Ushiyama, M., Inagawa, J., et al. (2007). Purification of phosphoproteins by immobilized metal affinity chromatography and its application to phosphoproteome analysis. FEBS J. 274, 1576–1587. doi: 10.1111/j.1742-4658.2007.05705.x
    • (2007) FEBS J , vol.274 , pp. 1576-1587
    • Machida, M.1    Kosako, H.2    Shirakabe, K.3    Kobayashi, M.4    Ushiyama, M.5    Inagawa, J.6
  • 26
    • 85057488290 scopus 로고    scopus 로고
    • Handbook ofDetectionof Enzymes on Electrophoretic Gels
    • (Florida: CRC Press LLC)
    • Manchenko, G. P. (2002). Handbook ofDetectionof Enzymes on Electrophoretic Gels, 2nd Edn. (Florida: CRC Press LLC).
    • (2002) 2Nd Edn
    • Manchenko, G.P.1
  • 27
    • 84928122288 scopus 로고    scopus 로고
    • Alterations in soluble Class III peroxidases of maize shoots by flooding stress
    • Meisrimler, C. N., Buck, F., and Lüthje, S. (2014). Alterations in soluble Class III peroxidases of maize shoots by flooding stress. Proteomes 2, 303–322. doi: 10.3390/proteomes2030303
    • (2014) Proteomes , vol.2 , pp. 303-322
    • Meisrimler, C.N.1    Buck, F.2    Lüthje, S.3
  • 28
    • 84860453728 scopus 로고    scopus 로고
    • IPG-strips versus off-gel fractionation: Advantages and limits of two-dimensional PAGE in separation of microsomal fractions of frequently used plant species and tissues
    • Meisrimler, C. N., and Lüthje, S. (2012). IPG-strips versus off-gel fractionation: advantages and limits of two-dimensional PAGE in separation of microsomal fractions of frequently used plant species and tissues. J. Proteomics 75, 2550–2562. doi: 10.1016/j.jprot.2012.02.026
    • (2012) J. Proteomics , vol.75 , pp. 2550-2562
    • Meisrimler, C.N.1    Lüthje, S.2
  • 29
    • 79960996033 scopus 로고    scopus 로고
    • Alteration of plasma membrane-bound redox systems of iron deficient pea roots by chitosan
    • Meisrimler, C. N., Planchon, S., Renaut, J., Sergeant, K., and Lüthje, S. (2011). Alteration of plasma membrane-bound redox systems of iron deficient pea roots by chitosan. J. Proteomics 74, 1437–1449. doi: 10.1016/j.jprot.2011.01.012
    • (2011) J. Proteomics , vol.74 , pp. 1437-1449
    • Meisrimler, C.N.1    Planchon, S.2    Renaut, J.3    Sergeant, K.4    Lüthje, S.5
  • 30
    • 76549129262 scopus 로고    scopus 로고
    • Membrane-bound guaiacol peroxidases from maize (Zea mays L.) roots are regulated by methyl jasmonate, salicylic acid, and pathogen elicitors
    • Mika, A., Boenisch, M. J., Hopff, D., and Lüthje, S. (2010). Membrane-bound guaiacol peroxidases from maize (Zea mays L.) roots are regulated by methyl jasmonate, salicylic acid, and pathogen elicitors. J. Exp. Bot. 61, 831–841. doi: 10.1093/jxb/erp353
    • (2010) J. Exp. Bot , vol.61 , pp. 831-841
    • Mika, A.1    Boenisch, M.J.2    Hopff, D.3    Lüthje, S.4
  • 31
    • 33750575732 scopus 로고    scopus 로고
    • Protein stains for pro-teomic applications: Which, when, why?
    • Miller, I., Crawford, J., and Gianazza, E. (2006). Protein stains for pro-teomic applications: which, when, why? Proteomics 6, 5385–5408. doi: 10.1002/pmic.200600323
    • (2006) Proteomics , vol.6 , pp. 5385-5408
    • Miller, I.1    Crawford, J.2    Gianazza, E.3
  • 32
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • Neuhoff, V., Arold, N., Taube, D., and Ehrhardt, W. (1988). Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis 9, 6255–6262. doi: 10.1002/elps.1150090603
    • (1988) Electrophoresis , vol.9 , pp. 6255-6262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 33
    • 70350442773 scopus 로고    scopus 로고
    • 2-D Difference in gel electrophoresis combined with Pro-Q Diamond staining: A successful approach for the identification of kinase/phosphatase targets
    • Orsatti, L., Forte, E, Tomei, L, Caterino, M, Pessi, A, and Talamo, F. (2009). 2-D Difference in gel electrophoresis combined with Pro-Q Diamond staining: a successful approach for the identification of kinase/phosphatase targets. Electrophoresis 30, 2469–2476. doi: 10.1002/elps.200800780
    • (2009) Electrophoresis , vol.30 , pp. 2469-2476
    • Orsatti, L.1    Forte, E.2    Tomei, L.3    Caterino, M.4    Pessi, A.5    Talamo, F.6
  • 34
    • 0000433426 scopus 로고
    • Competitive inhibition of enzyme activity by urea
    • Rajagopalan, K. V., Fridovich, I., and Handler, P. (1961). Competitive inhibition of enzyme activity by urea. J. Biol. Chem. 236, 1059–1065.
    • (1961) J. Biol. Chem , vol.236 , pp. 1059-1065
    • Rajagopalan, K.V.1    Fridovich, I.2    Handler, P.3
  • 35
    • 80053050275 scopus 로고    scopus 로고
    • Egg yolk phosvitin and functional phosphopeptides–review
    • Samaraweera, H., Zhang, W. G., Lee, E. J., and Ahn, D. U. (2011). Egg yolk phosvitin and functional phosphopeptides–review. J. Food Sci. 76, 143–150. doi: 10.1111/j.1750-3841.2011.02291.x
    • (2011) J. Food Sci , vol.76 , pp. 143-150
    • Samaraweera, H.1    Zhang, W.G.2    Lee, E.J.3    Ahn, D.U.4
  • 36
    • 20144388265 scopus 로고    scopus 로고
    • Quantitative proteomic analysis by accurate mass retention time pairs
    • Silva, J. C., Denny, R., Dorschel, C. A., Gorenstein, M., Kass, I. J., Li, G. Z., et al. (2005). Quantitative proteomic analysis by accurate mass retention time pairs. Anal. Chem. 77, 2187–2200. doi: 10.1021/ac048455k
    • (2005) Anal. Chem , vol.77 , pp. 2187-2200
    • Silva, J.C.1    Denny, R.2    Dorschel, C.A.3    Gorenstein, M.4    Kass, I.J.5    Li, G.Z.6
  • 37
    • 42649116833 scopus 로고    scopus 로고
    • Proteomics studies of brassinosteroid signal transduction using prefrac-tionation and two-dimensional DIGE
    • Tang, W., Deng, Z., Oses-Prieto, J. A., Suzuki, N., Zhu, S., Zhang, X., et al. (2008). Proteomics studies of brassinosteroid signal transduction using prefrac-tionation and two-dimensional DIGE. Mol. Cell. Proteomics? 7, 728–738. doi: 10.1074/mcp.M700358-MCP200
    • (2008) Mol. Cell. Proteomics? , vol.7 , pp. 728-738
    • Tang, W.1    Deng, Z.2    Oses-Prieto, J.A.3    Suzuki, N.4    Zhu, S.5    Zhang, X.6
  • 38
    • 69949134806 scopus 로고    scopus 로고
    • Phosphorylated intrinsically disordered region of FACT masks its nucleosomal DNA binding elements
    • Tsunaka, Y., Toga, J., Yamaguchi, H., Tate, S., Hirose, S., and Morikawa, K. (2009). Phosphorylated intrinsically disordered region of FACT masks its nucleosomal DNA binding elements. J. Biol. Chem. 284, 24610–24621. doi: 10.1074/jbc.M109.001958
    • (2009) J. Biol. Chem , vol.284 , pp. 24610-24621
    • Tsunaka, Y.1    Toga, J.2    Yamaguchi, H.3    Tate, S.4    Hirose, S.5    Morikawa, K.6
  • 39
    • 84883262226 scopus 로고    scopus 로고
    • Arabidop-sis PPP family of serine/threonine protein phosphatases: Many targets but few engines
    • Uhrig, R. G., Labandera, A. M., and Moorhead, G. B. (2013). Arabidop-sis PPP family of serine/threonine protein phosphatases: many targets but few engines. Trends Plant Sci. 18, 505–513. doi: 10.1016/j.tplants.2013.05.004
    • (2013) Trends Plant Sci , vol.18 , pp. 505-513
    • Uhrig, R.G.1    Labandera, A.M.2    Moorhead, G.B.3
  • 41
    • 0034085064 scopus 로고    scopus 로고
    • The ferrozine method revisited: Fe (II)/Fe (III) determination in natural waters
    • Viollier, E., Inglett, P. W., Hunter, K., Roychoudhury, A. N., and Van Cap-pellen, P. (2000). The ferrozine method revisited: Fe (II)/Fe (III) determination in natural waters. Appl. Geochem. 15, 785–790. doi: 10.1016/S0883-2927(99) 00097-9
    • (2000) Appl. Geochem , vol.15 , pp. 785-790
    • Viollier, E.1    Inglett, P.W.2    Hunter, K.3    Roychoudhury, A.N.4    Van Cap-Pellen, P.5
  • 42
    • 84907241903 scopus 로고    scopus 로고
    • Simple detection of phosphoproteins in SDS-PAGE by quercetin
    • Wang, X., Ni, M., Niu, C., Zhu, X., Zhao, T., Zhu, Z., et al. (2014). Simple detection of phosphoproteins in SDS-PAGE by quercetin. EuPA Open Proteomics 4, 156–164. doi: 10.1016/j.euprot.2014.07.002
    • (2014) Eupa Open Proteomics , vol.4 , pp. 156-164
    • Wang, X.1    Ni, M.2    Niu, C.3    Zhu, X.4    Zhao, T.5    Zhu, Z.6
  • 43
    • 75149164344 scopus 로고    scopus 로고
    • Measurement of superoxide dismutase, catalase and glutathione peroxidase in cultured cells and tissue
    • Weydert, C. J., and Cullen, J. J. (2010). Measurement of superoxide dismutase, catalase and glutathione peroxidase in cultured cells and tissue. Nat. Protoc. 5, 51–66. doi: 10.1038/nprot.2009.197
    • (2010) Nat. Protoc , vol.5 , pp. 51-66
    • Weydert, C.J.1    Cullen, J.J.2
  • 44
    • 33750378958 scopus 로고    scopus 로고
    • Blue native PAGE
    • Wittig, I., Braun, H. P., and Schägger, H. (2006). Blue native PAGE. Nat. Protoc. 1, 418–428. doi: 10.1038/nprot.2006.62
    • (2006) Nat. Protoc , vol.1 , pp. 418-428
    • Wittig, I.1    Braun, H.P.2    Schägger, H.3
  • 45
    • 34547138661 scopus 로고    scopus 로고
    • High resolution clear native elec-trophoresis for in-gel functional assays and fluorescence studies of membrane protein complexes
    • Wittig, I., Karas, M., and Schägger, H. (2007). High resolution clear native elec-trophoresis for in-gel functional assays and fluorescence studies of membrane protein complexes. Mol. Cell. 6, 1215–1225. doi: 10.1074/mcp.M700076-MCP200
    • (2007) Mol. Cell , vol.6 , pp. 1215-1225
    • Wittig, I.1    Karas, M.2    Schägger, H.3
  • 46
    • 28444497467 scopus 로고    scopus 로고
    • Advantages and limitations of clear-native PAGE
    • Wittig, I., and Schägger, H. (2005). Advantages and limitations of clear-native PAGE. Proteomics 5, 4338–4346. doi: 10.1002/pmic.200500081
    • (2005) Proteomics , vol.5 , pp. 4338-4346
    • Wittig, I.1    Schägger, H.2
  • 47
    • 55749085411 scopus 로고    scopus 로고
    • Features and applications of blue-native and clear-native electrophoresis
    • Wittig, I., and Schägger, H. (2008). Features and applications of blue-native and clear-native electrophoresis. Proteomics 8, 3974–3990. doi: 10.1002/pmic.200800017
    • (2008) Proteomics , vol.8 , pp. 3974-3990
    • Wittig, I.1    Schägger, H.2
  • 48
    • 67349219973 scopus 로고    scopus 로고
    • Resolving mitochondrial protein complexes using non-gradient blue native polyacrylamide gel electrophoresis
    • Yan, L. J., and Forster, J. M. (2009). Resolving mitochondrial protein complexes using non-gradient blue native polyacrylamide gel electrophoresis. Anal. Biochem. 389, 143–149. doi: 10.1016/j.ab.2009.03.043
    • (2009) Anal. Biochem , vol.389 , pp. 143-149
    • Yan, L.J.1    Forster, J.M.2
  • 49
    • 18144420373 scopus 로고    scopus 로고
    • Protein pI shifts due to posttranslational modifications in the separation and characterization of proteins
    • Zhu, K., Zhao, J., Lubman, D. M., Miller, F. R., and Barder, T. J. (2005). Protein pI shifts due to posttranslational modifications in the separation and characterization of proteins. Anal. Chem. 77, 2745–2755. doi: 10.1021/ac048494w
    • (2005) Anal. Chem , vol.77 , pp. 2745-2755
    • Zhu, K.1    Zhao, J.2    Lubman, D.M.3    Miller, F.R.4    Barder, T.J.5
  • 50
    • 0032080534 scopus 로고    scopus 로고
    • Urea effects on protein stability: Hydrogen bonding and the hydrophobic effect
    • Zou, Q., Habermann-Rottinghaus, S. M., and Murphy, K. P. (1998). Urea effects on protein stability: hydrogen bonding and the hydrophobic effect. Proteins 31, 107–115.
    • (1998) Proteins , vol.31 , pp. 107-115
    • Zou, Q.1    Habermann-Rottinghaus, S.M.2    Murphy, K.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.