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Volumn 28, Issue 5, 2009, Pages 816-843

Power and limitations of electrophoretic separations in proteomics strategies

Author keywords

Electrophoresis; Immobilized ph gradients; Isoelectric focusing; Peptides; Proteins; Proteomics; Two dimensional electrophoresis

Indexed keywords

CHROMATOGRAPHY; MASS SPECTROMETRY; MOLECULAR BIOLOGY; PEPTIDES; PROTEINS; SEPARATION;

EID: 69849103563     PISSN: 02777037     EISSN: None     Source Type: Journal    
DOI: 10.1002/mas.20204     Document Type: Review
Times cited : (81)

References (227)
  • 1
    • 0023430927 scopus 로고
    • Internal amino acid sequence analysis of proteins separated by one-or twodimensional gel electrophoresis after in situ protease digestion on nitrocellulose
    • Aebersold RH, Leavitt J, Saavedra RA, Hood LE, Kent SB. 1987. Internal amino acid sequence analysis of proteins separated by one-or twodimensional gel electrophoresis after in situ protease digestion on nitrocellulose. Proc Natl Acad Sci USA 84: 6970-6974.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6970-6974
    • Aebersold, R.H.1    Leavitt, J.2    Saavedra, R.A.3    Hood, L.E.4    Kent, S.B.5
  • 2
    • 29144449247 scopus 로고    scopus 로고
    • Solution isoelectric focusing for peptide analysis: Comparative investigation of an insoluble nuclear protein fraction
    • An Y, Fu Z, Gutierrez P, Fenselau C. 2005. Solution isoelectric focusing for peptide analysis: Comparative investigation of an insoluble nuclear protein fraction. J Proteome Res 4: 2126-2132.
    • (2005) J. Proteome Res. , vol.4 , pp. 2126-2132
    • An, Y.1    Fu, Z.2    Gutierrez, P.3    Fenselau, C.4
  • 4
    • 0017721398 scopus 로고
    • High resolution two-dimensional electrophoresis of human plasma proteins
    • Anderson L, Anderson NG. 1977. High resolution two-dimensional electrophoresis of human plasma proteins. Proc Natl Acad Sci USA 74: 5421-5425.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 5421-5425
    • Anderson, L.1    Anderson, N.G.2
  • 5
    • 0018084288 scopus 로고
    • Analytical techniques for cell fractions. XXI. Two-dimensional analysis of serum and tissue proteins: Multiple isoelectric focusing
    • Anderson NG, Anderson NL. 1978a. Analytical techniques for cell fractions. XXI. Two-dimensional analysis of serum and tissue proteins: Multiple isoelectric focusing. Anal Biochem 85: 331-340.
    • (1978) Anal Biochem. , vol.85 , pp. 331-340
    • Anderson, N.G.1    Anderson, N.L.2
  • 6
    • 0018167339 scopus 로고
    • Analytical techniques for cell fractions. XXII. Two-dimensional analysis of serum and tissue proteins: Multiple gradient-slab gel electrophoresis
    • Anderson NL, Anderson NG. 1978b. Analytical techniques for cell fractions. XXII. Two-dimensional analysis of serum and tissue proteins: Multiple gradient-slab gel electrophoresis. Anal Biochem 85: 341-354.
    • (1978) Anal Biochem. , vol.85 , pp. 341-354
    • Anderson, N.L.1    Anderson, N.G.2
  • 7
    • 0001644020 scopus 로고    scopus 로고
    • The human plasma proteome: History, character, and diagnostic prospects
    • Anderson NL, Anderson NG. 2002. The human plasma proteome: History, character, and diagnostic prospects. Mol Cell Proteomics 1: 845-867.
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 845-867
    • Anderson, N.L.1    Anderson, N.G.2
  • 8
    • 0019808432 scopus 로고
    • The TYCHO system for computer analysis of two-dimensional gel electrophoresis patterns
    • Anderson NL, Taylor J, Scandora AE, Coulter BP, Anderson NG. 1981. The TYCHO system for computer analysis of two-dimensional gel electrophoresis patterns. Clin Chem 27: 1807-1820.
    • (1981) Clin Chem. , vol.27 , pp. 1807-1820
    • Anderson, N.L.1    Taylor, J.2    Scandora, A.E.3    Coulter, B.P.4    Anderson, N.G.5
  • 9
    • 0023856847 scopus 로고
    • Automatic classification of two-dimensional gel electrophoresis pictures by heuristic clustering analysis: A step toward machine learning
    • Appel R, Hochstrasser D, Roch C, Funk M, Muller AF, Pellegrini C. 1988. Automatic classification of two-dimensional gel electrophoresis pictures by heuristic clustering analysis: A step toward machine learning. Electrophoresis 9: 136-142.
    • (1988) Electrophoresis , vol.9 , pp. 136-142
    • Appel, R.1    Hochstrasser, D.2    Roch, C.3    Funk, M.4    Muller, A.F.5    Pellegrini, C.6
  • 10
    • 0021402057 scopus 로고
    • Fractionation techniques in a hydro-organic environment. 2. Acryloyl-morpholine polymers as a matrix for electrophoresis in hydro-organic solvents
    • Artoni G, Gianazza E, Zanoni M, Gelfi C, Tanzi MC, Barozzi C, Ferruti P, Righetti PG. 1984. Fractionation techniques in a hydro-organic environment. 2. Acryloyl-morpholine polymers as a matrix for electrophoresis in hydro-organic solvents. Anal Biochem 137: 420-428.
    • (1984) Anal Biochem. , vol.137 , pp. 420-428
    • Artoni, G.1    Gianazza, E.2    Zanoni, M.3    Gelfi, C.4    Tanzi, M.C.5    Barozzi, C.6    Ferruti, P.7    Righetti, P.G.8
  • 11
    • 2942547734 scopus 로고    scopus 로고
    • Fractionation of peptides and identification of proteins from Saccharomyces cerevisiae in proteomics with the use of reversed-phase capillary liquid chromatography and pI-based approach
    • Baczek T. 2004a. Fractionation of peptides and identification of proteins from Saccharomyces cerevisiae in proteomics with the use of reversed-phase capillary liquid chromatography and pI-based approach. J Pharm Biomed Anal 35: 895-904.
    • (2004) J. Pharm Biomed Anal , vol.35 , pp. 895-904
    • Baczek, T.1
  • 12
    • 1542302553 scopus 로고    scopus 로고
    • Fractionation of peptides in proteomics with the use of pI-based approach and ZipTip pipette tips
    • Baczek T. 2004b. Fractionation of peptides in proteomics with the use of pI-based approach and ZipTip pipette tips. J Pharm Biomed Anal 34: 851-860.
    • (2004) J. Pharm Biomed Anal , vol.34 , pp. 851-860
    • Baczek, T.1
  • 14
    • 0033915670 scopus 로고    scopus 로고
    • Background-free, high sensitivity staining of proteins in one-and two-dimensional sodium dodecyl sulfate-polyacrylamide gels using a luminescent ruthenium complex
    • Berggren K, Chernokalskaya E, Steinberg TH, Kemper C, Lopez MF, Diwu Z, Haugland RP, Patton WF. 2000. Background-free, high sensitivity staining of proteins in one-and two-dimensional sodium dodecyl sulfate-polyacrylamide gels using a luminescent ruthenium complex. Electrophoresis 21: 2509-2521.
    • (2000) Electrophoresis , vol.21 , pp. 2509-2521
    • Berggren, K.1    Chernokalskaya, E.2    Steinberg, T.H.3    Kemper, C.4    Lopez, M.F.5    Diwu, Z.6    Haugland, R.P.7    Patton, W.F.8
  • 17
    • 0016203040 scopus 로고
    • A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels
    • Bonner WM, Laskey RA. 1974. A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem 46: 83-88.
    • (1974) Eur J. Biochem. , vol.46 , pp. 83-88
    • Bonner, W.M.1    Laskey, R.A.2
  • 18
  • 19
    • 0018849930 scopus 로고
    • A search for differential polypeptide synthesis throughout the cell cycle of HeLa cells
    • Bravo R, Celis JE. 1980. A search for differential polypeptide synthesis throughout the cell cycle of HeLa cells. J Cell Biol 84: 795-802.
    • (1980) J. Cell Biol. , vol.84 , pp. 795-802
    • Bravo, R.1    Celis, J.E.2
  • 20
    • 0020072810 scopus 로고
    • Human proteins sensitive to neoplastic transformation in cultured epithelial and fibroblast cells
    • Bravo R, Celis JE. 1982. Human proteins sensitive to neoplastic transformation in cultured epithelial and fibroblast cells. Clin Chem 28: 949-954.
    • (1982) Clin Chem. , vol.28 , pp. 949-954
    • Bravo, R.1    Celis, J.E.2
  • 21
    • 0019838350 scopus 로고
    • Identification of a nuclear and of a cytoplasmic polypeptide whose relative proportions are sensitive to changes in the rate of cell proliferation
    • Bravo R, Fey SJ, Bellatin J, Larsen PM, Arevalo J, Celis JE. 1981. Identification of a nuclear and of a cytoplasmic polypeptide whose relative proportions are sensitive to changes in the rate of cell proliferation. Exp Cell Res 136: 311-319.
    • (1981) Exp Cell Res. , vol.136 , pp. 311-319
    • Bravo, R.1    Fey, S.J.2    Bellatin, J.3    Larsen, P.M.4    Arevalo, J.5    Celis, J.E.6
  • 22
    • 0023091627 scopus 로고
    • Cyclin/PCNA is the auxiliary protein of DNA polymerase-delta
    • Bravo R, Frank R, Blundell PA, Macdonald-Bravo H. 1987. Cyclin/PCNA is the auxiliary protein of DNA polymerase-delta. Nature 326: 515-517.
    • (1987) Nature , vol.326 , pp. 515-517
    • Bravo, R.1    Frank, R.2    Blundell, P.A.3    Macdonald-Bravo, H.4
  • 23
    • 0023775410 scopus 로고
    • Mixed anionic detergent/aliphatic alcohol-polyacrylamide gel electrophoresis alters the separation of proteins relative to conventional sodium dodecyl sulfate-polyacrylamidegel electrophoresis
    • Brown EG. 1988. Mixed anionic detergent/aliphatic alcohol-polyacrylamide gel electrophoresis alters the separation of proteins relative to conventional sodium dodecyl sulfate-polyacrylamidegel electrophoresis. Anal Biochem 174: 337-348.
    • (1988) Anal Biochem. , vol.174 , pp. 337-348
    • Brown, E.G.1
  • 24
    • 0141855260 scopus 로고    scopus 로고
    • Proteomic analysis of acrylamide gel separated proteins immobilized on polyvinylidene difluoride membranes followingproteolytic digestion in the presenceof80%acetonitrile
    • Bunai K, Nozaki M, Hamano M, Ogane S, Inoue T, Nemoto T, Nakanishi H, Yamane K. 2003. Proteomic analysis of acrylamide gel separated proteins immobilized on polyvinylidene difluoride membranes followingproteolytic digestion in the presenceof80%acetonitrile. Proteomics 3: 1738-1749.
    • (2003) Proteomics , vol.3 , pp. 1738-1749
    • Bunai, K.1    Nozaki, M.2    Hamano, M.3    Ogane, S.4    Inoue, T.5    Nemoto, T.6    Nakanishi, H.7    Yamane, K.8
  • 27
    • 0019792891 scopus 로고
    • Analysis of protein and peptide mixtures-Evaluation of 3 sodium dodecyl sulfate-polyacrylamide gel-electrophoresis buffer systems
    • Bury AF. 1981. Analysis of protein and peptide mixtures-Evaluation of 3 sodium dodecyl sulfate-polyacrylamide gel-electrophoresis buffer systems. J Chromatogr 213: 491-500.
    • (1981) J. Chromatogr. , vol.213 , pp. 491-500
    • Bury, A.F.1
  • 28
    • 0027369199 scopus 로고
    • On the efficiency of methylene blue versus persulfate catalysis of polyacrylamide gels, as investigated by capillary zone electrophoresis
    • Caglio S, Righetti PG. 1993. On the efficiency of methylene-blue versus persulfate catalysis of polyacrylamide gels, as investigated by capillary zone electrophoresis. Electrophoresis 14: 997-1003. (Pubitemid 23359585)
    • (1993) Electrophoresis , vol.14 , Issue.10 , pp. 997-1003
    • Caglio, S.1    Righetti, P.G.2
  • 29
    • 0028258079 scopus 로고
    • Get polymerization in detergents-Conversion efficiency of methylene-blue vs persulfate catalysis, as investigated by capillary zone electrophoresis
    • Caglio S, Chiari M, Righetti PG. 1994. Get polymerization in detergents-Conversion efficiency of methylene-blue vs persulfate catalysis, as investigated by capillary zone electrophoresis. Electrophoresis 15: 209-214.
    • (1994) Electrophoresis , vol.15 , pp. 209-214
    • Caglio, S.1    Chiari, M.2    Righetti, P.G.3
  • 30
    • 2642529334 scopus 로고    scopus 로고
    • Two-dimensional blue native/SDS gel electrophoresis of multi-protein complexes from whole cellular lysates-A proteomics approach
    • Camacho-Carvajal MM, Wollscheid B, Aebersold R, Steimle V, Schamel WWA. 2004. Two-dimensional blue native/SDS gel electrophoresis of multi-protein complexes from whole cellular lysates-A proteomics approach. Mol Cell Proteomics 3: 176-182.
    • (2004) Mol. Cell Proteomics , vol.3 , pp. 176-182
    • Camacho-Carvajal, M.M.1    Wollscheid, B.2    Aebersold, R.3    Steimle, V.4    Schamel, W.W.A.5
  • 31
    • 30744432140 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of the tumor necrosis factor pathway
    • Cantin GT, Venable JD, Cociorva D, Yates JR III. 2006. Quantitative phosphoproteomic analysis of the tumor necrosis factor pathway. J Proteome Res 5: 127-134.
    • (2006) J. Proteome Res. , vol.5 , pp. 127-134
    • Cantin, G.T.1    Venable, J.D.2    Cociorva, D.3    Yates III, J.R.4
  • 32
    • 0347758353 scopus 로고    scopus 로고
    • An alternative to tandem mass spectrometry: Isoelectric point and accurate mass for the identification of peptides
    • Cargile BJ, Stephenson JL Jr. 2004. An alternative to tandem mass spectrometry: Isoelectric point and accurate mass for the identification of peptides. Anal Chem 76: 267-275.
    • (2004) Anal Chem. , vol.76 , pp. 267-275
    • Cargile, B.J.1    Stephenson, Jr.J.L.2
  • 33
    • 1642485152 scopus 로고    scopus 로고
    • Immobilized pH gradients as a first dimensionin shotgun proteomics and analysis of the accuracy of pI predictability of peptides
    • Cargile BJ, Talley DL, Stephenson JL Jr. 2004. Immobilized pH gradients as a first dimensionin shotgun proteomics and analysis of the accuracy of pI predictability of peptides. Electrophoresis 25: 936-945.
    • (2004) Electrophoresis , vol.25 , pp. 936-945
    • Cargile, B.J.1    Talley, D.L.2    Stephenson, Jr.J.L.3
  • 34
    • 47549117421 scopus 로고    scopus 로고
    • Calculation of the isoelectric point of tryptic peptides in the pH 3.5-4.5 range based on adjacent amino acid effects
    • Cargile BJ, Sevinsky JR, Essader AS, Eu JP, Stephenson JL Jr. 2008. Calculation of the isoelectric point of tryptic peptides in the pH 3.5-4.5 range based on adjacent amino acid effects. Electrophoresis 29: 2768-2778.
    • (2008) Electrophoresis , vol.29 , pp. 2768-2778
    • Cargile, B.J.1    Sevinsky, J.R.2    Essader, A.S.3    Eu, J.P.4    Stephenson, Jr.J.L.5
  • 35
    • 0032924359 scopus 로고    scopus 로고
    • Proteome analysis of polyacrylamide gel-separated proteins visualized by reversible negative staining using imidazole-zinc salts
    • Castellanos-Serra L, Proenza W, Huerta V, Moritz RL, Simpson RJ. 1999. Proteome analysis of polyacrylamide gel-separated proteins visualized by reversible negative staining using imidazole-zinc salts. Electrophoresis 20: 732-737.
    • (1999) Electrophoresis , vol.20 , pp. 732-737
    • Castellanos-Serra, L.1    Proenza, W.2    Huerta, V.3    Moritz, R.L.4    Simpson, R.J.5
  • 36
    • 0014407525 scopus 로고
    • Carbamylation of globin in electrophoresis and chromatography in the presence of urea
    • Cejka J, Vodrazka Z, Salak J. 1968. Carbamylation of globin in electrophoresis and chromatography in the presence of urea. Biochim Biophys Acta 154: 589-591.
    • (1968) Biochim Biophys Acta , vol.154 , pp. 589-591
    • Cejka, J.1    Vodrazka, Z.2    Salak, J.3
  • 38
    • 0041376854 scopus 로고    scopus 로고
    • Dynamic enhancements of sample loading and analyte concentration in capillary isoelectric focusing for proteome studies
    • Chen J, Gao J, Lee CS. 2003. Dynamic enhancements of sample loading and analyte concentration in capillary isoelectric focusing for proteome studies. J Proteome Res 2: 249-254.
    • (2003) J. Proteome Res. , vol.2 , pp. 249-254
    • Chen, J.1    Gao, J.2    Lee, C.S.3
  • 40
    • 0026618996 scopus 로고
    • Preincubation with cysteine prevents modification of sulfhydryl-groups in proteins by unreacted acrylamide in a gel
    • Chiari M, Righetti PG, Negri A, Ceciliani F, Ronchi S. 1992. Preincubation with cysteine prevents modification of sulfhydryl-groups in proteins by unreacted acrylamide in a gel. Electrophoresis 13: 882-884.
    • (1992) Electrophoresis , vol.13 , pp. 882-884
    • Chiari, M.1    Righetti, P.G.2    Negri, A.3    Ceciliani, F.4    Ronchi, S.5
  • 41
    • 0028210269 scopus 로고
    • Towards new formulations for polyacrylamide matrices-N- Acryloylaminoethoxyethanol, a novel monomer combining high hydrophilicity with extreme hydrolytic stability
    • Chiari M, Micheletti C, Nesi M, Fazio M, Righetti PG. 1994. Towards new formulations for polyacrylamide matrices-N-Acryloylaminoethoxyethanol, a novel monomer combining high hydrophilicity with extreme hydrolytic stability. Electrophoresis 15: 177-186.
    • (1994) Electrophoresis , vol.15 , pp. 177-186
    • Chiari, M.1    Micheletti, C.2    Nesi, M.3    Fazio, M.4    Righetti, P.G.5
  • 42
    • 44449112824 scopus 로고    scopus 로고
    • Characterization of the rat liver membrane proteome using peptide immobilized pH gradient isoelectric focusing
    • Chick JM, Haynes PA, Molloy MP, Bjellqvist B, Baker MS, Len AC. 2008. Characterization of the rat liver membrane proteome using peptide immobilized pH gradient isoelectric focusing. J Proteome Res 7: 1036-1045.
    • (2008) J. Proteome Res. , vol.7 , pp. 1036-1045
    • Chick, J.M.1    Haynes, P.A.2    Molloy, M.P.3    Bjellqvist, B.4    Baker, M.S.5    Len, A.C.6
  • 43
    • 5644302445 scopus 로고    scopus 로고
    • Characterization of protein variants and post-translational modifications: ESI-MSn analyses of intact proteins eluted from polyacrylamide gels
    • Claverol S, Burlet-Schiltz O, Gairin JE, Monsarrat B. 2003. Characterization of protein variants and post-translational modifications: ESI-MSn analyses of intact proteins eluted from polyacrylamide gels. Mol Cell Proteomics 2: 483-493.
    • (2003) Mol. Cell Proteomics , vol.2 , pp. 483-493
    • Claverol, S.1    Burlet-Schiltz, O.2    Gairin, J.E.3    Monsarrat, B.4
  • 44
    • 0017613305 scopus 로고
    • Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis
    • Cleveland DW, Fischer SG, Kirschner MW, Laemmli UK. 1977. Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J Biol Chem 252: 1102-1106.
    • (1977) J. Biol. Chem. , vol.252 , pp. 1102-1106
    • Cleveland, D.W.1    Fischer, S.G.2    Kirschner, M.W.3    Laemmli, U.K.4
  • 45
    • 0031148680 scopus 로고    scopus 로고
    • Mass spectrometry of whole proteins eluted from sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels
    • Cohen SL, Chait BT. 1997. Mass spectrometry of whole proteins eluted from sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels. Anal Biochem 247: 257-267.
    • (1997) Anal Biochem. , vol.247 , pp. 257-267
    • Cohen, S.L.1    Chait, B.T.2
  • 46
    • 0041358793 scopus 로고    scopus 로고
    • OLAV: Towards high-throughput tandem mass spectrometry data identification
    • Colinge J, Masselot A, Giron M, Dessingy T, Magnin J. 2003. OLAV: Towards high-throughput tandem mass spectrometry data identification. Proteomics 3: 1454-1463.
    • (2003) Proteomics , vol.3 , pp. 1454-1463
    • Colinge, J.1    Masselot, A.2    Giron, M.3    Dessingy, T.4    Magnin, J.5
  • 47
    • 0027992574 scopus 로고
    • Positional reproducibility of protein spots in two-dimensional polyacrylamide gel electrophoresis using immobilised pH gradient isoelectric focusing in the first dimension: An interlaboratory comparison
    • Corbett JM, Dunn MJ, Posch A, Gorg A. 1994. Positional reproducibility of protein spots in two-dimensional polyacrylamide gel electrophoresis using immobilised pH gradient isoelectric focusing in the first dimension: An interlaboratory comparison. Electrophoresis 15: 1205-1211.
    • (1994) Electrophoresis , vol.15 , pp. 1205-1211
    • Corbett, J.M.1    Dunn, M.J.2    Posch, A.3    Gorg, A.4
  • 48
    • 5644302164 scopus 로고    scopus 로고
    • The synaptic vesicle proteome: A comparative study in membrane protein identification
    • Coughenour HD, Spaulding RS, Thompson CM. 2004. The synaptic vesicle proteome: A comparative study in membrane protein identification. Proteomics 4: 3141-3155.
    • (2004) Proteomics , vol.4 , pp. 3141-3155
    • Coughenour, H.D.1    Spaulding, R.S.2    Thompson, C.M.3
  • 49
    • 0030905461 scopus 로고    scopus 로고
    • Comparison of in-gel and onmembrane digestion methods at low to sub-pmol level for subsequent peptide and fragment-ion mass analysis using matrix-assisted laserdesorption/ionization mass spectrometry
    • Courchesne PL, Luethy R, Patterson SD. 1997. Comparison of in-gel and onmembrane digestion methods at low to sub-pmol level for subsequent peptide and fragment-ion mass analysis using matrix-assisted laserdesorption/ionization mass spectrometry. Electrophoresis 18: 369-381.
    • (1997) Electrophoresis , vol.18 , pp. 369-381
    • Courchesne, P.L.1    Luethy, R.2    Patterson, S.D.3
  • 50
    • 34547572949 scopus 로고    scopus 로고
    • Is proteomics the new genomics?
    • Cox J, Mann M. 2007. Is proteomics the new genomics? Cell 130: 395-398.
    • (2007) Cell , vol.130 , pp. 395-398
    • Cox, J.1    Mann, M.2
  • 51
    • 0021417615 scopus 로고
    • Rapid fluorescent staining of histones in sodium dodecyl sulfate-polyacrylamide gels
    • Daban JR, Aragay AM. 1984. Rapid fluorescent staining of histones in sodium dodecyl sulfate-polyacrylamide gels. Anal Biochem 138: 223-228.
    • (1984) Anal Biochem. , vol.138 , pp. 223-228
    • Daban, J.R.1    Aragay, A.M.2
  • 52
    • 0026409394 scopus 로고
    • Use of the hydrophobic probe Nile red for the fluorescent staining of protein bands in sodium dodecyl sulfate-polyacrylamide gels
    • Daban JR, Bartolome S, Samso M. 1991. Use of the hydrophobic probe Nile red for the fluorescent staining of protein bands in sodium dodecyl sulfate-polyacrylamide gels. Anal Biochem 199: 169-174.
    • (1991) Anal Biochem. , vol.199 , pp. 169-174
    • Daban, J.R.1    Bartolome, S.2    Samso, M.3
  • 53
    • 78651153791 scopus 로고
    • Disc electrophoresis. II. Method and application to human serum proteins
    • Davis BJ. 1964. Disc electrophoresis. II. Method and application to human serum proteins. Ann NYAcad Sci 121: 404-427.
    • (1964) Ann NYAcad. Sci. , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 54
    • 33750622611 scopus 로고    scopus 로고
    • Challenges and opportunities in proteomics data analysis
    • Domon B, Aebersold R. 2006. Challenges and opportunities in proteomics data analysis. Mol Cell Proteomics 5: 1921-1926.
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 1921-1926
    • Domon, B.1    Aebersold, R.2
  • 55
    • 0032531568 scopus 로고    scopus 로고
    • Coupling 2D SDS-PAGE with CNBr cleavage and MALDI-TOFMS: A strategy applied to the identification of proteins induced by a hypochlorous acid stress in Escherichia coli
    • Dukan S, Turlin E, Biville F, Bolbach G, Touati D, Tabet JC, Blais JC. 1998. Coupling 2D SDS-PAGE with CNBr cleavage and MALDI-TOFMS: A strategy applied to the identification of proteins induced by a hypochlorous acid stress in Escherichia coli. Anal Chem 70: 4433-4440.
    • (1998) Anal Chem. , vol.70 , pp. 4433-4440
    • Dukan, S.1    Turlin, E.2    Biville, F.3    Bolbach, G.4    Touati, D.5    Tabet, J.C.6    Blais, J.C.7
  • 56
    • 0020085946 scopus 로고
    • How many proteins are there in a typical mammalian cell?
    • Duncan R, McConkey EH. 1982. How many proteins are there in a typical mammalian cell? Clin Chem 28: 749-755.
    • (1982) Clin Chem. , vol.28 , pp. 749-755
    • Duncan, R.1    McConkey, E.H.2
  • 57
    • 0023749584 scopus 로고
    • Isolation of monoclonal antibodies to phencyclidine from ascites fluid by preparative isoelectric focusing in the Rotofor
    • Egen NB, Bliss M, Mayersohn M, Owens SM, Arnold L, Bier M. 1988. Isolation of monoclonal antibodies to phencyclidine from ascites fluid by preparative isoelectric focusing in the Rotofor. Anal Biochem 172: 488-494.
    • (1988) Anal Biochem. , vol.172 , pp. 488-494
    • Egen, N.B.1    Bliss, M.2    Mayersohn, M.3    Owens, S.M.4    Arnold, L.5    Bier, M.6
  • 58
    • 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 JR. 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.3
  • 60
    • 13244271374 scopus 로고    scopus 로고
    • A comparison of immobilized pH gradient isoelectric focusing and strong-cationexchange chromatography as a first dimension in shotgun proteomics
    • Essader AS, Cargile BJ, Bundy JL, Stephenson JL Jr. 2005. A comparison of immobilized pH gradient isoelectric focusing and strong-cationexchange chromatography as a first dimension in shotgun proteomics. Proteomics 5: 24-34.
    • (2005) Proteomics , vol.5 , pp. 24-34
    • Essader, A.S.1    Cargile, B.J.2    Bundy, J.L.3    Stephenson, Jr.J.L.4
  • 61
    • 0026599977 scopus 로고
    • Reverse staining of sodium dodecyl sulfate polyacrylamide gels by imidazolezinc salts: Sensitive detection of unmodified proteins
    • Fernandez-Patron C, Castellanos-Serra L, Rodriguez P. 1992. Reverse staining of sodium dodecyl sulfate polyacrylamide gels by imidazolezinc salts: Sensitive detection of unmodified proteins. Biotechniques 12: 564-573.
    • (1992) Biotechniques , vol.12 , pp. 564-573
    • Fernandez-Patron, C.1    Castellanos-Serra, L.2    Rodriguez, P.3
  • 62
    • 0031722252 scopus 로고    scopus 로고
    • Optimization of solid phase microextraction-Capillary zone electrophoresis-Mass spectrometry for high sensitivity protein identification
    • Figeys D, Zhang Y, Aebersold R. 1998. Optimization of solid phase microextraction-Capillary zone electrophoresis-Mass spectrometry for high sensitivity protein identification. Electrophoresis 19: 2338-2347.
    • (1998) Electrophoresis , vol.19 , pp. 2338-2347
    • Figeys, D.1    Zhang, Y.2    Aebersold, R.3
  • 63
    • 0024402489 scopus 로고
    • Factors affecting polyacrylamide gel electrophoresis and electroblotting of high-molecular-weight myofibrillar proteins
    • Fritz JD, Swartz DR, Greaser ML. 1989. Factors affecting polyacrylamide gel electrophoresis and electroblotting of high-molecular-weight myofibrillar proteins. Anal Biochem 180: 205-210.
    • (1989) Anal Biochem. , vol.180 , pp. 205-210
    • Fritz, J.D.1    Swartz, D.R.2    Greaser, M.L.3
  • 64
    • 0018575918 scopus 로고
    • Changes in protein synthesis during myogenesis in a clonal cell line
    • Garrels JI. 1979a. Changes in protein synthesis during myogenesis in a clonal cell line. Dev Biol 73: 134-152.
    • (1979) Dev Biol. , vol.73 , pp. 134-152
    • Garrels, J.I.1
  • 65
    • 0018675951 scopus 로고
    • Two dimensional gel electrophoresis and computer analysis of proteins synthesized by clonal cell lines
    • Garrels JI. 1979b. Two dimensional gel electrophoresis and computer analysis of proteins synthesized by clonal cell lines. J Biol Chem 254: 7961-7977.
    • (1979) J. Biol. Chem. , vol.254 , pp. 7961-7977
    • Garrels, J.I.1
  • 66
    • 84988099177 scopus 로고
    • Polymerization kinetics of polyacrylamide gels. 2. Effect of Temperature
    • Gelfi C, Righetti PG. 1981a. Polymerization kinetics of polyacrylamide gels. 2. Effect of Temperature. Electrophoresis 2: 220-228.
    • (1981) Electrophoresis , vol.2 , pp. 220-228
    • Gelfi, C.1    Righetti, P.G.2
  • 67
    • 84988058867 scopus 로고
    • Polymerization kinetics of polyacrylamide gels. 1. Effect of different cross-linkers
    • Gelfi C, Righetti PG. 1981b. Polymerization kinetics of polyacrylamide gels. 1. Effect of different cross-linkers. Electrophoresis 2: 213-219.
    • (1981) Electrophoresis , vol.2 , pp. 213-219
    • Gelfi, C.1    Righetti, P.G.2
  • 68
    • 0018836434 scopus 로고
    • Muscle protein analysis. II. Two-dimensional electrophoresis of normal and diseased human skelet al. muscle
    • Giometti CS, Barany M, Danon MJ, Anderson NG. 1980. Muscle protein analysis. II. Two-dimensional electrophoresis of normal and diseased human skelet al. muscle. Clin Chem 26: 1152-1155.
    • (1980) Clin Chem. , vol.26 , pp. 1152-1155
    • Giometti, C.S.1    Barany, M.2    Danon, M.J.3    Anderson, N.G.4
  • 69
    • 0002365131 scopus 로고
    • The relationship of structure to the effectiveness of denaturing agents for proteins
    • Gordon JA, Jencks WP. 1963. The relationship of structure to the effectiveness of denaturing agents for proteins. Biochemistry 2: 47-57.
    • (1963) Biochemistry , vol.2 , pp. 47-57
    • Gordon, J.A.1    Jencks, W.P.2
  • 71
    • 0023768475 scopus 로고
    • The current state of two-dimensional electrophoresis with immobilized pH gradients
    • Gorg A, Postel W, Gunther S. 1988. The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis 9: 531-546.
    • (1988) Electrophoresis , vol.9 , pp. 531-546
    • Gorg, A.1    Postel, W.2    Gunther, S.3
  • 73
    • 0036917339 scopus 로고    scopus 로고
    • Sample prefractionation with Sephadex isoelectric focusing prior to narrow pH range two-dimensional gels
    • Gorg A, Boguth G, Kopf A, Reil G, Parlar H, Weiss W. 2002. Sample prefractionation with Sephadex isoelectric focusing prior to narrow pH range two-dimensional gels. Proteomics 2: 1652-1657.
    • (2002) Proteomics , vol.2 , pp. 1652-1657
    • Gorg, A.1    Boguth, G.2    Kopf, A.3    Reil, G.4    Parlar, H.5    Weiss, W.6
  • 74
    • 0037196139 scopus 로고    scopus 로고
    • Fractionation of beta-lactoglobulin tryptic peptides by ampholyte-free isoelectric focusing
    • Groleau PE, Jimenez-Flores R, Gauthier SF, Pouliot Y. 2002. Fractionation of beta-lactoglobulin tryptic peptides by ampholyte-free isoelectric focusing. J Agric Food Chem 50: 578-583.
    • (2002) J. Agric Food Chem. , vol.50 , pp. 578-583
    • Groleau, P.E.1    Jimenez-Flores, R.2    Gauthier, S.F.3    Pouliot, Y.4
  • 75
    • 12444281868 scopus 로고
    • Rapid isolation and separation of the nonhistone proteins of rat liver nuclei
    • Gronow M, Griffiths G. 1971. Rapid isolation and separation of the nonhistone proteins of rat liver nuclei. FEBS Lett 15: 340-344.
    • (1971) FEBS Lett. , vol.15 , pp. 340-344
    • Gronow, M.1    Griffiths, G.2
  • 76
    • 55049129918 scopus 로고    scopus 로고
    • A multiplexed quantitative strategy for membrane proteomics: Opportunities for mining therapeutic targets for autosomal-dominant polycystic kidney disease
    • Han CL, Chien CW, Chen WC, Chen YR, Wu CP, Li H, Chen YJ. 2008. A multiplexed quantitative strategy for membrane proteomics: Opportunities for mining therapeutic targets for autosomal-dominant polycystic kidney disease. Mol Cell Proteomics 7: 1983-1997.
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 1983-1997
    • Han, C.L.1    Chien, C.W.2    Chen, W.C.3    Chen, Y.R.4    Wu, C.P.5    Li, H.6    Chen, Y.J.7
  • 77
    • 0017831747 scopus 로고
    • Polyacrylamide gel electrophoretic fractionation of histones
    • Hardison R, Chalkley R. 1978. Polyacrylamide gel electrophoretic fractionation of histones. Methods Cell Biol 17: 235-251.
    • (1978) Methods Cell Biol. , vol.17 , pp. 235-251
    • Hardison, R.1    Chalkley, R.2
  • 78
    • 0030586426 scopus 로고    scopus 로고
    • 16-BAC/SDS-PAGE: A two-dimensional gel electrophoresis system suitable for the separation of integral membrane proteins
    • Hartinger J, Stenius K, Hogemann D, Jahn R. 1996. 16-BAC/SDS-PAGE: A two-dimensional gel electrophoresis system suitable for the separation of integral membrane proteins. Anal Biochem 240: 126-133.
    • (1996) Anal Biochem. , vol.240 , pp. 126-133
    • Hartinger, J.1    Stenius, K.2    Hogemann, D.3    Jahn, R.4
  • 81
    • 0027198862 scopus 로고
    • Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases
    • Henzel WJ, Billeci TM, Stults JT, Wong SC, Grimley C, Watanabe C. 1993. Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases. Proc Natl Acad Sci USA 90: 5011-5015.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5011-5015
    • Henzel, W.J.1    Billeci, T.M.2    Stults, J.T.3    Wong, S.C.4    Grimley, C.5    Watanabe, C.6
  • 82
    • 0026021350 scopus 로고
    • Twodimensional gel electrophoresis of the membrane-bound protein complexes, including photosystem I, of thylakoid membranes in the presence of sodium oligooxyethylene alkyl ether sulfate/dimethyl dodecylamine oxide and sodium dodecyl sulfate
    • Hisabori T, Inoue K, Akabane Y, Iwakami S, Manabe K. 1991. Twodimensional gel electrophoresis of the membrane-bound protein complexes, including photosystem I, of thylakoid membranes in the presence of sodium oligooxyethylene alkyl ether sulfate/dimethyl dodecylamine oxide and sodium dodecyl sulfate. J Biochem Biophys Methods 22: 253-260.
    • (1991) J. Biochem. Biophys Methods , vol.22 , pp. 253-260
    • Hisabori, T.1    Inoue, K.2    Akabane, Y.3    Iwakami, S.4    Manabe, K.5
  • 83
    • 39749091667 scopus 로고    scopus 로고
    • Taking aim at shotgun phosphoproteomics
    • Hoffert JD, Knepper MA. 2008. Taking aim at shotgun phosphoproteomics. Anal Biochem 375: 1-10.
    • (2008) Anal Biochem. , vol.375 , pp. 1-10
    • Hoffert, J.D.1    Knepper, M.A.2
  • 84
    • 0035404418 scopus 로고    scopus 로고
    • Continuous free-flow electrophoresis separation of cytosolic proteins from the human colon carcinoma cell line LIM1215: A non two-dimensional gel electrophoresis-based proteome analysis strategy
    • Hoffmann P, Ji H, Moritz RL, Connolly LM, Frecklington DF, Layton MJ, Eddes JS, Simpson RJ. 2001. Continuous free-flow electrophoresis separation of cytosolic proteins from the human colon carcinoma cell line LIM1215: A non two-dimensional gel electrophoresis-based proteome analysis strategy. Proteomics 1: 807-818.
    • (2001) Proteomics , vol.1 , pp. 807-818
    • Hoffmann, P.1    Ji, H.2    Moritz, R.L.3    Connolly, L.M.4    Frecklington, D.F.5    Layton, M.J.6    Eddes, J.S.7    Simpson, R.J.8
  • 85
    • 0023403593 scopus 로고
    • Ion-enhanced fluorescence staining of sodium dodecyl sulfate- polyacrylamide gels using bis (8-p-toluidino-1-naphthalenesulfonate)
    • Horowitz PM, Bowman S. 1987. Ion-enhanced fluorescence staining of sodium dodecyl sulfate-polyacrylamide gels using bis (8-p-toluidino-1- naphthalenesulfonate). Anal Biochem 165: 430-434.
    • (1987) Anal Biochem. , vol.165 , pp. 430-434
    • Horowitz, P.M.1    Bowman, S.2
  • 86
    • 33750631580 scopus 로고    scopus 로고
    • Efficient fractionation and improved protein identification by peptide OFFGEL electrophoresis
    • Horth P, Miller CA, Preckel T, Wenz C. 2006. Efficient fractionation and improved protein identification by peptide OFFGEL electrophoresis. Mol Cell Proteomics 5: 1968-1974.
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 1968-1974
    • Horth, P.1    Miller, C.A.2    Preckel, T.3    Wenz, C.4
  • 89
    • 0020405648 scopus 로고
    • Enhanced resolution in two-dimensional electrophoresis of low-molecular-weight proteins while utilizing enlarged gels
    • Johnson BF. 1982. Enhanced resolution in two-dimensional electrophoresis of low-molecular-weight proteins while utilizing enlarged gels. Anal Biochem 127: 235-246.
    • (1982) Anal Biochem. , vol.127 , pp. 235-246
    • Johnson, B.F.1
  • 91
    • 2942576336 scopus 로고    scopus 로고
    • Efficacy and compatibility with mass spectrometry of methods for elution of proteins from sodium dodecyl sulfate-polyacrylamide gels and polyvinyldifluoride membranes
    • Jorgensen CS, Jagd M, Sorensen BK, McGuire J, Barkholt V, Hojrup P, Houen G. 2004. Efficacy and compatibility with mass spectrometry of methods for elution of proteins from sodium dodecyl sulfate-polyacrylamide gels and polyvinyldifluoride membranes. Anal Biochem 330: 87-97.
    • (2004) Anal Biochem. , vol.330 , pp. 87-97
    • Jorgensen, C.S.1    Jagd, M.2    Sorensen, B.K.3    McGuire, J.4    Barkholt, V.5    Hojrup, P.6    Houen, G.7
  • 92
    • 0015937156 scopus 로고
    • Multiphasic zone electrophoresis. I. Steady-state movingboundary systems formed by different electrolyte combinations
    • Jovin TM. 1973a. Multiphasic zone electrophoresis. I. Steady-state movingboundary systems formed by different electrolyte combinations. Biochemistry 12: 871-879.
    • (1973) Biochemistry , vol.12 , pp. 871-879
    • Jovin, T.M.1
  • 93
    • 0015937106 scopus 로고
    • Multiphasic zone electrophoresis. II. Design of integrated discontinuous buffer systems for analytical and preparative fractionation
    • Jovin TM. 1973b. Multiphasic zone electrophoresis. II. Design of integrated discontinuous buffer systems for analytical and preparative fractionation. Biochemistry 12: 879-890.
    • (1973) Biochemistry , vol.12 , pp. 879-890
    • Jovin, T.M.1
  • 94
    • 38349053169 scopus 로고    scopus 로고
    • Recent developments in CE and CEC of peptides
    • Kasicka V. 2008. Recent developments in CE and CEC of peptides. Electrophoresis 29: 179-206.
    • (2008) Electrophoresis , vol.29 , pp. 179-206
    • Kasicka, V.1
  • 95
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller A, Nesvizhskii AI, Kolker E, Aebersold R. 2002. Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal Chem 74: 5383-5392.
    • (2002) Anal Chem. , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 96
    • 4344691276 scopus 로고    scopus 로고
    • Recent progress of free-flow electrophoresis method and its application for proteomics
    • Kobayashi N. 2004. Recent progress of free-flow electrophoresis method and its application for proteomics. Tanpakushitsu Kakusan Koso 49: 1333-1340.
    • (2004) Tanpakushitsu Kakusan Koso , vol.49 , pp. 1333-1340
    • Kobayashi, N.1
  • 97
    • 33745857712 scopus 로고    scopus 로고
    • In-gel isoelectric focusing of peptides as a tool for improved protein identification
    • Krijgsveld J, Gauci S, Dormeyer W, Heck AJ. 2006. In-gel isoelectric focusing of peptides as a tool for improved protein identification. J Proteome Res 5: 1721-1730.
    • (2006) J. Proteome Res. , vol.5 , pp. 1721-1730
    • Krijgsveld, J.1    Gauci, S.2    Dormeyer, W.3    Heck, A.J.4
  • 98
    • 33751208935 scopus 로고    scopus 로고
    • Sequence-specific retention calculator. Algorithm for peptide retention prediction in ion-pair RP-HPLC: Application to 300-and 100-A pore size C18 sorbents
    • Krokhin OV. 2006. Sequence-specific retention calculator. Algorithm for peptide retention prediction in ion-pair RP-HPLC: Application to 300-and 100-A pore size C18 sorbents. Anal Chem 78: 7785-7795.
    • (2006) Anal Chem. , vol.78 , pp. 7785-7795
    • Krokhin, O.V.1
  • 101
    • 0020826112 scopus 로고
    • A discontinuous electrophoretic system for separating peptides on polyacrylamide gels
    • Kyte J, Rodriguez H. 1983. A discontinuous electrophoretic system for separating peptides on polyacrylamide gels. Anal Biochem 133: 515-522.
    • (1983) Anal Biochem. , vol.133 , pp. 515-522
    • Kyte, J.1    Rodriguez, H.2
  • 102
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 106
    • 34250349206 scopus 로고    scopus 로고
    • ITRAQ compatibility of peptide immobilized pH gradient isoelectric focusing
    • Lengqvist J, Uhlen K, Lehtio J. 2007. iTRAQ compatibility of peptide immobilized pH gradient isoelectric focusing. Proteomics 7: 1746-1752.
    • (2007) Proteomics , vol.7 , pp. 1746-1752
    • Lengqvist, J.1    Uhlen, K.2    Lehtio, J.3
  • 107
    • 0030584491 scopus 로고    scopus 로고
    • Characterization of SDS-PAGE-separated proteins by matrix-assisted laser desorption/ionization mass spectrometry
    • Liang X, Bai J, Liu YH, Lubman DM. 1996. Characterization of SDS-PAGE-separated proteins by matrix-assisted laser desorption/ionization mass spectrometry. Anal Chem 68: 1012-1018.
    • (1996) Anal Chem. , vol.68 , pp. 1012-1018
    • Liang, X.1    Bai, J.2    Liu, Y.H.3    Lubman, D.M.4
  • 109
    • 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: 4193-4201.
    • (2004) Anal Chem. , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates III, J.R.3
  • 110
    • 0034234689 scopus 로고    scopus 로고
    • Techniques for the optimization of proteomic strategies based on head column stacking capillary electrophoresis
    • Locke S, Figeys D. 2000. Techniques for the optimization of proteomic strategies based on head column stacking capillary electrophoresis. Anal Chem 72: 2684-2689.
    • (2000) Anal Chem. , vol.72 , pp. 2684-2689
    • Locke, S.1    Figeys, D.2
  • 113
    • 29244464778 scopus 로고    scopus 로고
    • Tube-gel digestion: A novel proteomic approach for high throughput analysis of membrane proteins
    • Lu X, Zhu H. 2005. Tube-gel digestion: A novel proteomic approach for high throughput analysis of membrane proteins. Mol Cell Proteomics 4: 1948-1958.
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 1948-1958
    • Lu, X.1    Zhu, H.2
  • 114
    • 41449095461 scopus 로고    scopus 로고
    • Improving protein identification sensitivity by combining MS and MS/MS information for shotgun proteomics using LTQ-Orbitrap high mass accuracy data
    • Lu B, Motoyama A, Ruse C, Venable J, Yates JR III. 2008. Improving protein identification sensitivity by combining MS and MS/MS information for shotgun proteomics using LTQ-Orbitrap high mass accuracy data. Anal Chem 80: 2018-2025.
    • (2008) Anal Chem. , vol.80 , pp. 2018-2025
    • Lu, B.1    Motoyama, A.2    Ruse, C.3    Venable, J.4    Yates III, J.R.5
  • 115
    • 33846165487 scopus 로고    scopus 로고
    • Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation
    • Lu P, Vogel C, Wang R, Yao X, Marcotte EM. 2007. Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation. Nat Biotechnol 25: 117-124.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 117-124
    • Lu, P.1    Vogel, C.2    Wang, R.3    Yao, X.4    Marcotte, E.M.5
  • 116
    • 34948856551 scopus 로고    scopus 로고
    • Ultrafast coelectrophoretic fluorescent staining of proteins with carbocyanines
    • Luche S, Lelong C, Diemer H, Van Dorsselaer A, Rabilloud T. 2007. Ultrafast coelectrophoretic fluorescent staining of proteins with carbocyanines. Proteomics 7: 3234-3244.
    • (2007) Proteomics , vol.7 , pp. 3234-3244
    • Luche, S.1    Lelong, C.2    Diemer, H.3    Van Dorsselaer, A.4    Rabilloud, T.5
  • 117
    • 0030588172 scopus 로고    scopus 로고
    • Methodical analysis of protein-nitrocellulose interactions to design a refined digestion protocol
    • Lui M, Tempst P, Erdjument-Bromage H. 1996. Methodical analysis of protein-nitrocellulose interactions to design a refined digestion protocol. Anal Biochem 241: 156-166.
    • (1996) Anal Biochem. , vol.241 , pp. 156-166
    • Lui, M.1    Tempst, P.2    Erdjument-Bromage, H.3
  • 118
    • 33644670810 scopus 로고    scopus 로고
    • Quantitation of protein on gels and blots by infrared fluorescence of Coomassie blue and Fast Green
    • Luo S, Wehr NB, Levine RL. 2006. Quantitation of protein on gels and blots by infrared fluorescence of Coomassie blue and Fast Green. Anal Biochem 350: 233-238.
    • (2006) Anal Biochem. , vol.350 , pp. 233-238
    • Luo, S.1    Wehr, N.B.2    Levine, R.L.3
  • 119
    • 33746263851 scopus 로고    scopus 로고
    • Use of nitrocellulose membranes for protein characterization by matrix-assisted laser desorption/ionization mass spectrometry
    • Luque-Garcia JL, Zhou G, Sun TT, Neubert TA. 2006. Use of nitrocellulose membranes for protein characterization by matrix-assisted laser desorption/ionization mass spectrometry. Anal Chem 78: 5102-5108.
    • (2006) Anal Chem. , vol.78 , pp. 5102-5108
    • Luque-Garcia, J.L.1    Zhou, G.2    Sun, T.T.3    Neubert, T.A.4
  • 121
    • 0021104416 scopus 로고
    • Use of benzyldimethyl-n-hexadecylammonium chloride ("16-BAC"), a cationic detergent, in an acidic polyacrylamide gel electrophoresis system to detect base labile protein methylation in intact cells
    • Macfarlane DE. 1983. Use of benzyldimethyl-n-hexadecylammonium chloride ("16-BAC"), a cationic detergent, in an acidic polyacrylamide gel electrophoresis system to detect base labile protein methylation in intact cells. Anal Biochem 132: 231-235.
    • (1983) Anal Biochem. , vol.132 , pp. 231-235
    • Macfarlane, D.E.1
  • 122
    • 0024545833 scopus 로고
    • Two dimensional benzyldimethyl-n-hexadecylammonium chloride-Sodium dodecyl sulfate preparative polyacrylamide gel electrophoresis: A high capacity high resolution technique for the purification of proteins from complex mixtures
    • Macfarlane DE. 1989. Two dimensional benzyldimethyl-n-hexadecylammonium chloride-Sodium dodecyl sulfate preparative polyacrylamide gel electrophoresis: A high capacity high resolution technique for the purification of proteins from complex mixtures. Anal Biochem 176:457-463.
    • (1989) Anal Biochem. , vol.176 , pp. 457-463
    • Macfarlane, D.E.1
  • 123
    • 0015968532 scopus 로고
    • The heterogeneity of mouse-chromatin nonhistone proteins as evidenced by two-dimensional polyacrylamidegel electrophoresis and ion-exchange chromatography
    • MacGillivray AJ, Rickwood D. 1974. The heterogeneity of mouse-chromatin nonhistone proteins as evidenced by two-dimensional polyacrylamidegel electrophoresis and ion-exchange chromatography. Eur J Biochem 41: 181-190.
    • (1974) Eur J. Biochem. , vol.41 , pp. 181-190
    • MacGillivray, A.J.1    Rickwood, D.2
  • 127
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira P. 1987. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J Biol Chem 262: 10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 128
    • 0027468021 scopus 로고
    • Peptide mapping using EOF-driven capillary isoelectric focusing
    • Mazzeo JR, Martineau JA, Krull IS. 1993. Peptide mapping using EOF-driven capillary isoelectric focusing. Anal Biochem 208: 323-329.
    • (1993) Anal Biochem. , vol.208 , pp. 323-329
    • Mazzeo, J.R.1    Martineau, J.A.2    Krull, I.S.3
  • 129
    • 0015948565 scopus 로고
    • Two-dimensional polyacrylamide gel electrophoresis: An improved method for ribosomal proteins
    • Mets LJ, Bogorad L. 1974. Two-dimensional polyacrylamide gel electrophoresis: An improved method for ribosomal proteins. Anal Biochem 57: 200-210.
    • (1974) Anal Biochem. , vol.57 , pp. 200-210
    • Mets, L.J.1    Bogorad, L.2
  • 130
    • 4043074774 scopus 로고    scopus 로고
    • A proteome strategy for fractionating proteins and peptides using continuous free-flow electrophoresis coupled off-line to reversed-phase high-performance liquid chromatography
    • Moritz RL, Ji H, Schutz F, Connolly LM, Kapp EA, Speed TP, Simpson RJ. 2004. A proteome strategy for fractionating proteins and peptides using continuous free-flow electrophoresis coupled off-line to reversed-phase high-performance liquid chromatography. Anal Chem 76: 4811-4824.
    • (2004) Anal Chem. , vol.76 , pp. 4811-4824
    • Moritz, R.L.1    Ji, H.2    Schutz, F.3    Connolly, L.M.4    Kapp, E.A.5    Speed, T.P.6    Simpson, R.J.7
  • 131
    • 0026777966 scopus 로고
    • Analysis of tubulin isoforms by two-dimensional gel electrophoresis using SDS-polyacrylamide gel electrophoresis in the first dimension
    • Nakamura K, Okuya Y, Katahira M, Yoshida S, Wada S, Okuno M. 1992. Analysis of tubulin isoforms by two-dimensional gel electrophoresis using SDS-polyacrylamide gel electrophoresis in the first dimension. J Biochem Biophys Methods 24: 195-203.
    • (1992) J. Biochem. Biophys. Methods , vol.24 , pp. 195-203
    • Nakamura, K.1    Okuya, Y.2    Katahira, M.3    Yoshida, S.4    Wada, S.5    Okuno, M.6
  • 132
    • 0036908432 scopus 로고    scopus 로고
    • Subproteomics: Identification of plasma membrane proteins from the yeast Saccharomyces cerevisiae
    • Navarre C, Degand H, Bennett KL, Crawford JS, Mortz E, Boutry M. 2002. Subproteomics: Identification of plasma membrane proteins from the yeast Saccharomyces cerevisiae. Proteomics 2: 1706-1714.
    • (2002) Proteomics , vol.2 , pp. 1706-1714
    • Navarre, C.1    Degand, H.2    Bennett, K.L.3    Crawford, J.S.4    Mortz, E.5    Boutry, M.6
  • 133
    • 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, 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: 255-262.
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 134
    • 33846010726 scopus 로고    scopus 로고
    • Extent of modifications in human proteome samples and their effect on dynamic range of analysis in shotgun proteomics
    • Nielsen ML, Savitski MM, Zubarev RA. 2006. Extent of modifications in human proteome samples and their effect on dynamic range of analysis in shotgun proteomics. Mol Cell Proteomics 5: 2384-2391.
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 2384-2391
    • Nielsen, M.L.1    Savitski, M.M.2    Zubarev, R.A.3
  • 135
    • 33645829296 scopus 로고    scopus 로고
    • Separation of nuclear protein complexes by blue native polyacrylamide gel electrophoresis
    • Novakova Z, Man P, Novak P, Hozak P, Hodny Z. 2006. Separation of nuclear protein complexes by blue native polyacrylamide gel electrophoresis. Electrophoresis 27: 1277-1287.
    • (2006) Electrophoresis , vol.27 , pp. 1277-1287
    • Novakova, Z.1    Man, P.2    Novak, P.3    Hozak, P.4    Hodny, Z.5
  • 136
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell PH. 1975. High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250: 4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 137
    • 0017696571 scopus 로고
    • High resolution twodimensional electrophoresis of basic as well as acidic proteins
    • O'Farrell PZ, Goodman HM, O'Farrell PH. 1977. High resolution twodimensional electrophoresis of basic as well as acidic proteins. Cell 12: 1133-1141.
    • (1977) Cell , vol.12 , pp. 1133-1141
    • O'Farrell, P.Z.1    Goodman, H.M.2    O'Farrell, P.H.3
  • 139
    • 0015906758 scopus 로고
    • Comparison of nucleolar proteins of normal rat liver and Novikoff hepatoma ascites cells by twodimensional polyacrylamide gel electrophoresis
    • Orrick LR, Olson MO, Busch H. 1973. Comparison of nucleolar proteins of normal rat liver and Novikoff hepatoma ascites cells by twodimensional polyacrylamide gel electrophoresis. Proc Natl Acad Sci USA 70: 1316-1320.
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 1316-1320
    • Orrick, L.R.1    Olson, M.O.2    Busch, H.3
  • 140
    • 0026601551 scopus 로고
    • Imidazole-SDS-Zn reverse staining of proteins in gels containing or not SDS and microsequence of individual unmodified electroblotted proteins
    • Ortiz ML, Calero M, Fernandez Patron C, Patron CF, Castellanos L, Mendez E. 1992. Imidazole-SDS-Zn reverse staining of proteins in gels containing or not SDS and microsequence of individual unmodified electroblotted proteins. FEBS Lett 296: 300-304.
    • (1992) FEBS Lett. , vol.296 , pp. 300-304
    • Ortiz, M.L.1    Calero, M.2    Fernandez C. Patron3    Patron, C.F.4    Castellanos, L.5    Mendez, E.6
  • 141
    • 33847648535 scopus 로고    scopus 로고
    • Formation of epsilonformyllysine on silver-stained proteins: Implications for assignment of isobaric dimethylation sites by tandem mass spectrometry
    • Oses-Prieto JA, Zhang X, Burlingame AL. 2007. Formation of epsilonformyllysine on silver-stained proteins: Implications for assignment of isobaric dimethylation sites by tandem mass spectrometry. Mol Cell Proteomics 6: 181-192.
    • (2007) Mol. Cell Proteomics , vol.6 , pp. 181-192
    • Oses-Prieto, J.A.1    Zhang, X.2    Burlingame, A.L.3
  • 142
    • 12944269065 scopus 로고
    • Rapid identification of proteins by peptide-mass fingerprinting
    • Pappin DJ, Hojrup P, Bleasby AJ. 1993. Rapid identification of proteins by peptide-mass fingerprinting. Curr Biol 3: 327-332.
    • (1993) Curr. Biol. , vol.3 , pp. 327-332
    • Pappin, D.J.1    Hojrup, P.2    Bleasby, A.J.3
  • 143
    • 0025899047 scopus 로고
    • Tris-tricine and Tris-borate buffer systems provide better estimates of human mesothelial cell intermediate filament protein molecular weights than the standard Tris-glycine system
    • Patton WF, Chung-Welch N, Lopez MF, Cambria RP, Utterback BL, Skea WM. 1991. Tris-tricine and Tris-borate buffer systems provide better estimates of human mesothelial cell intermediate filament protein molecular weights than the standard Tris-glycine system. Anal Biochem 197: 25-33.
    • (1991) Anal Biochem. , vol.197 , pp. 25-33
    • Patton, W.F.1    Chung-Welch, N.2    Lopez, M.F.3    Cambria, R.P.4    Utterback, B.L.5    Skea, W.M.6
  • 144
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome
    • Peng J, Elias JE, Thoreen CC, Licklider LJ, Gygi SP. 2003. Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome. J Proteome Res 2: 43-50.
    • (2003) J. Proteome Res. , vol.2 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 145
    • 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: 3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 147
    • 0021484814 scopus 로고
    • Electrophoretic transfer of proteins from fixed and stained gels
    • Phelps DS. 1984. Electrophoretic transfer of proteins from fixed and stained gels. Anal Biochem 141: 409-412.
    • (1984) Anal Biochem. , vol.141 , pp. 409-412
    • Phelps, D.S.1
  • 148
    • 0025053763 scopus 로고
    • Mechanisms of protein silver staining in polyacrylamide gels: A 10-year synthesis
    • Rabilloud T. 1990. Mechanisms of protein silver staining in polyacrylamide gels: A 10-year synthesis. Electrophoresis 11: 785-794.
    • (1990) Electrophoresis , vol.11 , pp. 785-794
    • Rabilloud, T.1
  • 149
    • 0031807109 scopus 로고    scopus 로고
    • Use of thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis
    • DOI 10.1002/elps.1150190526
    • Rabilloud T. 1998. Use of thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis. Electrophoresis 19: 758-760. (Pubitemid 28236679)
    • (1998) Electrophoresis , vol.19 , Issue.5 , pp. 758-760
    • Rabilloud, T.1
  • 150
    • 0035346790 scopus 로고    scopus 로고
    • Comparison between Sypro Ruby and ruthenium II tris (bathophenanthroline disulfonate) as fluorescent stains for protein detection in gels
    • Rabilloud T, Strub JM, Luche S, van Dorsselaer A, Lunardi J. 2001. Comparison between Sypro Ruby and ruthenium II tris (bathophenanthroline disulfonate) as fluorescent stains for protein detection in gels. Proteomics 1: 699-704.
    • (2001) Proteomics , vol.1 , pp. 699-704
    • Rabilloud, T.1    Strub, J.M.2    Luche, S.3    Van Dorsselaer, A.4    Lunardi, J.5
  • 151
    • 0037205455 scopus 로고    scopus 로고
    • Proteomics analysis of cellular response to oxidative stress-Evidence for in vivo overoxidation of peroxiredoxins at their active site
    • Rabilloud T, Heller M, Gasnier F, Luche S, Rey C, Aebersold R, Benahmed M, Louisot P, Lunardi J. 2002. Proteomics analysis of cellular response to oxidative stress-Evidence for in vivo overoxidation of peroxiredoxins at their active site. J Biol Chem 277: 19396-19401.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19396-19401
    • Rabilloud, T.1    Heller, M.2    Gasnier, F.3    Luche, S.4    Rey, C.5    Aebersold, R.6    Benahmed, M.7    Louisot, P.8    Lunardi, J.9
  • 152
    • 0015931522 scopus 로고
    • Isoelectric focusing in layers of granulated gels. I. Thinlayer isoelectric focusing of proteins
    • Radola BJ. 1973. Isoelectric focusing in layers of granulated gels. I. Thinlayer isoelectric focusing of proteins. Biochim Biophys Acta 295: 412-428.
    • (1973) Biochim Biophys. Acta , vol.295 , pp. 412-428
    • Radola, B.J.1
  • 153
    • 0016637313 scopus 로고
    • Isoelectric focusing in layers of granulated gels. II. Preparative isoelectric focusing
    • Radola BJ. 1975. Isoelectric focusing in layers of granulated gels. II. Preparative isoelectric focusing. Biochim Biophys Acta 386: 181-195.
    • (1975) Biochim. Biophys. Acta , vol.386 , pp. 181-195
    • Radola, B.J.1
  • 154
    • 3543043510 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis for the isolation of integral membrane proteins and mass spectrometric identification
    • Rais I, Karas M, Schagger H. 2004. Two-dimensional electrophoresis for the isolation of integral membrane proteins and mass spectrometric identification. Proteomics 4: 2567-2571.
    • (2004) Proteomics , vol.4 , pp. 2567-2571
    • Rais, I.1    Karas, M.2    Schagger, H.3
  • 155
    • 0029098053 scopus 로고
    • Nonreducing twodimensional polyacrylamide gel electrophoretic analysis of human colonic proteins
    • Reid GE, Ji H, Eddes JS, Moritz RL, Simpson RJ. 1995. Nonreducing twodimensional polyacrylamide gel electrophoretic analysis of human colonic proteins. Electrophoresis 16: 1120-1130.
    • (1995) Electrophoresis , vol.16 , pp. 1120-1130
    • Reid, G.E.1    Ji, H.2    Eddes, J.S.3    Moritz, R.L.4    Simpson, R.J.5
  • 156
    • 0014816360 scopus 로고
    • Binding of dodecyl sulfate to proteins at high binding ratios. Possible implications for the state of proteins in biological membranes
    • Reynolds JA, Tanford C. 1970. Binding of dodecyl sulfate to proteins at high binding ratios. Possible implications for the state of proteins in biological membranes. Proc Natl Acad Sci USA 66: 1002-1007.
    • (1970) Proc. Natl. Acad. Sci. USA , vol.66 , pp. 1002-1007
    • Reynolds, J.A.1    Tanford, C.2
  • 158
    • 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: 1030-1032.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Seraphin, B.6
  • 160
    • 0027281603 scopus 로고
    • On the kinetics of monomer incorporation into polyacrylamide gels, as investigated by capillary zone electrophoresis
    • Righetti PG, Caglio S. 1993. On the kinetics of monomer incorporation into polyacrylamide gels, as investigated by capillary zone electrophoresis. Electrophoresis 14: 573-582. (Pubitemid 23257933)
    • (1993) Electrophoresis , vol.14 , Issue.7 , pp. 573-582
    • Righetti, P.G.1    Caglio, S.2
  • 161
    • 0023083636 scopus 로고
    • Isoelectric focusing in immobilized pH gradients: Theory and newer methodology
    • Righetti PG, Gianazza E. 1987. Isoelectric focusing in immobilized pH gradients: Theory and newer methodology. Methods Biochem Anal 32: 215-278.
    • (1987) Methods Biochem. Anal , vol.32 , pp. 215-278
    • Righetti, P.G.1    Gianazza, E.2
  • 163
    • 26444475952 scopus 로고    scopus 로고
    • How to bring the "unseen" proteome to the limelight via electrophoretic pre-fractionation techniques
    • Righetti PG, Castagna A, Herbert B, Candiano G. 2005. How to bring the "unseen" proteome to the limelight via electrophoretic pre-fractionation techniques. Biosci Rep 25: 3-17.
    • (2005) Biosci. Rep. , vol.25 , pp. 3-17
    • Righetti, P.G.1    Castagna, A.2    Herbert, B.3    Candiano, G.4
  • 166
    • 0026694947 scopus 로고
    • In-gel digestion of proteins for internal sequence analysis after one-or two-dimensional gel electrophoresis
    • Rosenfeld J, Capdevielle J, Guillemot JC, Ferrara P. 1992. In-gel digestion of proteins for internal sequence analysis after one-or two-dimensional gel electrophoresis. Anal Biochem 203: 173-179.
    • (1992) Anal Biochem. , vol.203 , pp. 173-179
    • Rosenfeld, J.1    Capdevielle, J.2    Guillemot, J.C.3    Ferrara, P.4
  • 168
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: Un amour impossible
    • Santoni V, Molloy M, Rabilloud T. 2000. Membrane proteins and proteomics: Un amour impossible? Electrophoresis 21: 1054-1070.
    • (2000) Electrophoresis , vol.21 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 169
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H, von Jagow G. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166: 368-379.
    • (1987) Anal Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 170
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger H, von Jagow G. 1991. Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal Biochem 199: 223-231.
    • (1991) Anal Biochem. , vol.199 , pp. 223-231
    • Schagger, H.1    Von Jagow, G.2
  • 172
    • 1842499791 scopus 로고    scopus 로고
    • Profiling core proteomes of human cell lines by one-dimensional PAGE and liquid chromatographytandem mass spectrometry
    • Schirle M, Heurtier MA, Kuster B. 2003. Profiling core proteomes of human cell lines by one-dimensional PAGE and liquid chromatographytandem mass spectrometry. Mol Cell Proteomics 2: 1297-1305.
    • (2003) Mol. Cell Proteomics , vol.2 , pp. 1297-1305
    • Schirle, M.1    Heurtier, M.A.2    Kuster, B.3
  • 173
    • 34748891107 scopus 로고    scopus 로고
    • Evaluation of two proteomics technologies used to screen the membrane proteomes of wild-type Corynebacterium glutamicum and an L-lysine-producing strain
    • Schluesener D, Rogner M, Poetsch A. 2007. Evaluation of two proteomics technologies used to screen the membrane proteomes of wild-type Corynebacterium glutamicum and an L-lysine-producing strain. Anal Bioanal Chem 389: 1055-1064.
    • (2007) Anal Bioanal Chem. , vol.389 , pp. 1055-1064
    • Schluesener, D.1    Rogner, M.2    Poetsch, A.3
  • 174
    • 0034914489 scopus 로고    scopus 로고
    • Theory of genetic algorithms
    • Schmitt LM. 2001. Theory of genetic algorithms. Theor Comput Sci 259: 1-61.
    • (2001) Theor Comput. Sci. , vol.259 , pp. 1-61
    • Schmitt, L.M.1
  • 175
    • 33847651332 scopus 로고    scopus 로고
    • Minimizing back exchange in 18O/16O quantitative proteomics experiments by incorporation of immobilized trypsin into the initial digestion step
    • Sevinsky JR, Brown KJ, Cargile BJ, Bundy JL, Stephenson JL Jr. 2007. Minimizing back exchange in 18O/16O quantitative proteomics experiments by incorporation of immobilized trypsin into the initial digestion step. Anal Chem 79: 2158-2162.
    • (2007) Anal Chem. , vol.79 , pp. 2158-2162
    • Sevinsky, J.R.1    Brown, K.J.2    Cargile, B.J.3    Bundy, J.L.4    Stephenson, Jr.J.L.5
  • 177
    • 0346504157 scopus 로고    scopus 로고
    • Carrier ampholyte-free solution isoelectric focusing as a prefractionation method for the proteomic analysis of complex protein mixtures
    • Shang TQ, Ginter JM, Johnston MV, Larsen BS, McEwen CN. 2003. Carrier ampholyte-free solution isoelectric focusing as a prefractionation method for the proteomic analysis of complex protein mixtures. Electrophoresis 24: 2359-2368.
    • (2003) Electrophoresis , vol.24 , pp. 2359-2368
    • Shang, T.Q.1    Ginter, J.M.2    Johnston, M.V.3    Larsen, B.S.4    McEwen, C.N.5
  • 178
    • 0014195281 scopus 로고
    • Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels
    • Shapiro AL, Vinuela E, Maizel JV Jr. 1967. Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem Biophys Res Commun 28: 815-820.
    • (1967) Biochem Biophys. Res. Commun. , vol.28 , pp. 815-820
    • Shapiro, A.L.1    Vinuela, E.2    Maizel, Jr.J.V.3
  • 179
    • 0034193643 scopus 로고    scopus 로고
    • High-efficiency capillary isoelectric focusing of peptides
    • DOI 10.1021/ac991367t
    • Shen Y, Berger SJ, Anderson GA, Smith RD. 2000. High-efficiency capillary isoelectric focusing of peptides. Anal Chem 72: 2154-2159. (Pubitemid 30316595)
    • (2000) Analytical Chemistry , vol.72 , Issue.9 , pp. 2154-2159
    • Shen, Y.1    Berger, S.J.2    Anderson, G.A.3    Smith, R.D.4
  • 180
    • 0034307281 scopus 로고    scopus 로고
    • Accuracy in the determination of isoelectric points of some proteins and a peptide by capillary isoelectric focusing: Utility of synthetic peptides as isoelectric point markers
    • Shimura K, Zhi W, Matsumoto H, Kasai K. 2000. Accuracy in the determination of isoelectric points of some proteins and a peptide by capillary isoelectric focusing: Utility of synthetic peptides as isoelectric point markers. Anal Chem 72: 4747-4757.
    • (2000) Anal Chem. , vol.72 , pp. 4747-4757
    • Shimura, K.1    Zhi, W.2    Matsumoto, H.3    Kasai, K.4
  • 181
    • 0036500203 scopus 로고    scopus 로고
    • Fluorescence-labeled peptide pI markers for capillary isoelectric focusing
    • DOI 10.1021/ac0108010
    • Shimura K, Kamiya K, Matsumoto H, Kasai K. 2002. Fluorescence-labeled peptide pI markers for capillary isoelectric focusing. Anal Chem 74: 1046-1053. (Pubitemid 34203026)
    • (2002) Analytical Chemistry , vol.74 , Issue.5 , pp. 1046-1053
    • Shimura, K.1    Kamiya, K.-I.2    Matsumoto, H.3    Kasai, K.-I.4
  • 182
    • 0018213778 scopus 로고
    • A new analytical procedure for two-dimensional electrophoresis of cellular proteins: Comparison of protein compositions of parent strain and a K+-accumulation mutant of E
    • Siemankowski RF, Giambalvo A, Dreizen P. 1978. A new analytical procedure for two-dimensional electrophoresis of cellular proteins: Comparison of protein compositions of parent strain and a K+-accumulation mutant of E. coli. Physiol Chem Phys 10: 415-434.
    • (1978) Coli. Physiol Chem. Phys , vol.10 , pp. 415-434
    • Siemankowski, R.F.1    Giambalvo, A.2    Dreizen, P.3
  • 183
    • 0029658953 scopus 로고    scopus 로고
    • Novel acrylamido monomers with higher hydrophilicity and improved hydrolytic stability. 2. Properties of N-acryloylaminopropanol
    • SimoAlfonso E, Gelfi C, Sebastiano R, Citterio A, Righetti PG. 1996. Novel acrylamido monomers with higher hydrophilicity and improved hydrolytic stability. 2. Properties of N-acryloylaminopropanol. Electrophoresis 17: 732-737.
    • (1996) Electrophoresis , vol.17 , pp. 732-737
    • SimoAlfonso, E.1    Gelfi, C.2    Sebastiano, R.3    Citterio, A.4    Righetti, P.G.5
  • 184
    • 18444393438 scopus 로고    scopus 로고
    • Combining capillary electrophoresis with mass spectrometry for applications in proteomics
    • Simpson DC, Smith RD. 2005. Combining capillary electrophoresis with mass spectrometry for applications in proteomics. Electrophoresis 26: 1291-1305.
    • (2005) Electrophoresis , vol.26 , pp. 1291-1305
    • Simpson, D.C.1    Smith, R.D.2
  • 185
    • 0030219531 scopus 로고    scopus 로고
    • Applications of SYPRO Orange and SYPRO Red protein gel stains
    • Steinberg TH, Haugland RP, Singer VL. 1996. Applications of SYPRO Orange and SYPRO Red protein gel stains. Anal Biochem 239: 238-245.
    • (1996) Anal Biochem. , vol.239 , pp. 238-245
    • Steinberg, T.H.1    Haugland, R.P.2    Singer, V.L.3
  • 186
    • 0034002993 scopus 로고    scopus 로고
    • Fluorescence detection of proteins in sodium dodecyl sulfatepolyacrylamide gels using environmentally benign, nonfixative, saline solution
    • Steinberg TH, Lauber WM, Berggren K, Kemper C, Yue S, Patton WF. 2000. Fluorescence detection of proteins in sodium dodecyl sulfatepolyacrylamide gels using environmentally benign, nonfixative, saline solution. Electrophoresis 21: 497-508.
    • (2000) Electrophoresis , vol.21 , pp. 497-508
    • Steinberg, T.H.1    Lauber, W.M.2    Berggren, K.3    Kemper, C.4    Yue, S.5    Patton, W.F.6
  • 187
    • 0018720271 scopus 로고
    • A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide gels
    • Switzer RC III, Merril CR, Shifrin S. 1979. A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide gels. Anal Biochem 98: 231-237.
    • (1979) Anal Biochem. , vol.98 , pp. 231-237
    • Switzer III, R.C.1    Merril, C.R.2    Shifrin, S.3
  • 188
    • 1242294379 scopus 로고    scopus 로고
    • Largescale characterization of integral proteins from Arabidopsis vacuolar membrane by two-dimensional liquid chromatography
    • Szponarski W, Sommerer N, Boyer JC, Rossignol M, Gibrat R. 2004. Largescale characterization of integral proteins from Arabidopsis vacuolar membrane by two-dimensional liquid chromatography. Proteomics 4: 397-406.
    • (2004) Proteomics , vol.4 , pp. 397-406
    • Szponarski, W.1    Sommerer, N.2    Boyer, J.C.3    Rossignol, M.4    Gibrat, R.5
  • 189
    • 37849052010 scopus 로고    scopus 로고
    • Separation, identification, and profiling of membrane proteins by GFC/IEC/SDS-PAGE and MALDI TOF MS
    • Szponarski W, Delom F, Sommerer N, Rossignol M, Gibrat R. 2007. Separation, identification, and profiling of membrane proteins by GFC/IEC/SDS-PAGE and MALDI TOF MS. Methods Mol Biol 355: 267-278.
    • (2007) Methods Mol. Biol. , vol.355 , pp. 267-278
    • Szponarski, W.1    Delom, F.2    Sommerer, N.3    Rossignol, M.4    Gibrat, R.5
  • 190
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and Contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb DL, McDonald WH, Yates JR III. 2002. DTASelect and Contrast: Tools for assembling and comparing protein identifications from shotgun proteomics. J Proteome Res 1: 21-26.
    • (2002) J. Proteome Res. , vol.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates III, J.R.3
  • 191
    • 0036812037 scopus 로고    scopus 로고
    • A miniaturized multichamber solution isoelectric focusing device for separation of protein digests
    • Tan A, Pashkova A, Zang L, Foret F, Karger BL. 2002. A miniaturized multichamber solution isoelectric focusing device for separation of protein digests. Electrophoresis 23: 3599-3607.
    • (2002) Electrophoresis , vol.23 , pp. 3599-3607
    • Tan, A.1    Pashkova, A.2    Zang, L.3    Foret, F.4    Karger, B.L.5
  • 192
    • 84988122225 scopus 로고
    • Hermes-A 2nd generation approach to the automatic-analysis of two-dimensional electrophoresis gels. 5. Data-analysis
    • Tarroux P, Vincens P, Rabilloud T. 1987. Hermes-A 2nd generation approach to the automatic-analysis of two-dimensional electrophoresis gels. 5. Data-analysis. Electrophoresis 8: 187-199.
    • (1987) Electrophoresis , vol.8 , pp. 187-199
    • Tarroux, P.1    Vincens, P.2    Rabilloud, T.3
  • 193
  • 194
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc Natl Acad Sci USA 76: 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 195
    • 0035468229 scopus 로고    scopus 로고
    • Application of chemical selective cleavage methods to analyze posttranslational modification in proteins
    • Tsugita A, Miyazaki K, Nabetani T, Nozawa T, Kamo M, Kawakami T. 2001. Application of chemical selective cleavage methods to analyze posttranslational modification in proteins. Proteomics 1: 1082-1091.
    • (2001) Proteomics , vol.1 , pp. 1082-1091
    • Tsugita, A.1    Miyazaki, K.2    Nabetani, T.3    Nozawa, T.4    Kamo, M.5    Kawakami, T.6
  • 196
    • 0018390530 scopus 로고
    • A two-dimensional polyacrylamide gel electrophoresis (PAGE) system using sodium dodecyl sulfate-PAGE in the first dimension
    • Tuszynski GP, Buck CA, Warren L.1979. A two-dimensional polyacrylamide gel electrophoresis (PAGE) system using sodium dodecyl sulfate-PAGE in the first dimension. Anal Biochem 93: 329-338.
    • (1979) Anal Biochem. , vol.93 , pp. 329-338
    • Tuszynski, G.P.1    Buck, C.A.2    Warren, L.3
  • 197
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlu M, Morgan ME, Minden JS. 1997. Difference gel electrophoresis: A single gel method for detecting changes in protein extracts. Electrophoresis 18: 2071-2077.
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 198
    • 0031149870 scopus 로고    scopus 로고
    • Colloidal silver staining of electroblotted proteins for high sensitivity peptide mapping by liquid chromatography-electrospray ionization tandem mass spectrometry
    • van Oostveen I, Ducret A, Aebersold R. 1997. Colloidal silver staining of electroblotted proteins for high sensitivity peptide mapping by liquid chromatography-electrospray ionization tandem mass spectrometry. Anal Biochem 247: 310-318.
    • (1997) Anal Biochem. , vol.247 , pp. 310-318
    • Van Oostveen, I.1    Ducret, A.2    Aebersold, R.3
  • 199
    • 0028070397 scopus 로고
    • Peptide mapping of bovine and chicken cytochrome c by capillary isoelectric focusing with universal concentration gradient imaging
    • Vonguyen L, Wu J, Pawliszyn J. 1994. Peptide mapping of bovine and chicken cytochrome c by capillary isoelectric focusing with universal concentration gradient imaging. J Chromatogr B Biomed Appl 657: 333-338.
    • (1994) J. Chromatogr. B Biomed Appl. , vol.657 , pp. 333-338
    • Vonguyen, L.1    Wu, J.2    Pawliszyn, J.3
  • 200
    • 0019311086 scopus 로고
    • Very-high-resolution two-dimensional gel electrophoresis of proteins using giant gels
    • Voris BP, Young DA. 1980. Very-high-resolution two-dimensional gel electrophoresis of proteins using giant gels. Anal Biochem 104: 478-484.
    • (1980) Anal Biochem. , vol.104 , pp. 478-484
    • Voris, B.P.1    Young, D.A.2
  • 201
    • 5644240979 scopus 로고    scopus 로고
    • Free flow electrophoresis coupled with liquid chromatography-mass spectrometry for a proteomic study of the human cell line (K562/CR3)
    • Wang Y, Hancock WS, Weber G, Eckerskorn C, Palmer-Toy D. 2004. Free flow electrophoresis coupled with liquid chromatography-mass spectrometry for a proteomic study of the human cell line (K562/CR3). J Chromatogr A 1053: 269-278.
    • (2004) J. Chromatogr. A , vol.1053 , pp. 269-278
    • Wang, Y.1    Hancock, W.S.2    Weber, G.3    Eckerskorn, C.4    Palmer-Toy, D.5
  • 202
    • 33847006270 scopus 로고    scopus 로고
    • Membrane proteome analysis of microdissected ovarian tumor tissues using capillary isoelectric focusing/reversed-phase liquid chromatography-tandem MS
    • Wang W, Guo T, Rudnick PA, Song T, Li J, Zhuang Z, Zheng W, Devoe DL, Lee CS, Balgley BM. 2007. Membrane proteome analysis of microdissected ovarian tumor tissues using capillary isoelectric focusing/reversed-phase liquid chromatography-tandem MS. Anal Chem 79: 1002-1009.
    • (2007) Anal Chem. , vol.79 , pp. 1002-1009
    • Wang, W.1    Guo, T.2    Rudnick, P.A.3    Song, T.4    Li, J.5    Zhuang, Z.6    Zheng, W.7    Devoe, D.L.8    Lee, C.S.9    Balgley, B.M.10
  • 203
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • DOI 10.1038/85686
    • Washburn MP, Wolters D, Yates JR. 2001. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol 19: 242-247. (Pubitemid 32220565)
    • (2001) Nature Biotechnology , vol.19 , Issue.3 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 204
    • 0015239825 scopus 로고
    • Reversible denaturation of enzymes by sodium dodecyl sulfate
    • Weber K, Kuter DJ. 1971. Reversible denaturation of enzymes by sodium dodecyl sulfate. J Biol Chem 246: 4504-4509.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4504-4509
    • Weber, K.1    Kuter, D.J.2
  • 205
    • 0021104541 scopus 로고
    • Ionic interactions between proteins in nonequilibrium pH gradient electrophoresis: Histones affect the migration of high mobility group nonhistone chromatin proteins
    • Wen L, Tweten RK, Isackson PJ, Iandolo JJ, Reeck GR. 1983. Ionic interactions between proteins in nonequilibrium pH gradient electrophoresis: Histones affect the migration of high mobility group nonhistone chromatin proteins. Anal Biochem 132: 294-304.
    • (1983) Anal Biochem. , vol.132 , pp. 294-304
    • Wen, L.1    Tweten, R.K.2    Isackson, P.J.3    Iandolo, J.J.4    Reeck, G.R.5
  • 206
    • 84988073798 scopus 로고
    • Polyacrylamide-gel electrophoresis of small peptides
    • West MHP, Wu RS, Bonner WM. 1984. Polyacrylamide-gel electrophoresis of small peptides. Electrophoresis 5: 133-138.
    • (1984) Electrophoresis , vol.5 , pp. 133-138
    • West, M.H.P.1    Wu, R.S.2    Bonner, W.M.3
  • 208
    • 0031861758 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis for proteome projects: The effects of protein hydrophobicity and copy number
    • Wilkins MR, Gasteiger E, Sanchez JC, Bairoch A, Hochstrasser DF. 1998. Two-dimensional gel electrophoresis for proteome projects: The effects of protein hydrophobicity and copy number. Electrophoresis 19: 1501-1505.
    • (1998) Electrophoresis , vol.19 , pp. 1501-1505
    • Wilkins, M.R.1    Gasteiger, E.2    Sanchez, J.C.3    Bairoch, A.4    Hochstrasser, D.F.5
  • 209
    • 33746702583 scopus 로고    scopus 로고
    • A novel Bicine running buffer system for doubled sodium dodecyl sulfate-Polyacrylamide gel electrophoresis of membrane proteins
    • Williams TI, Combs JC, Thakur AP, Strobel HJ, Lynn BC. 2006. A novel Bicine running buffer system for doubled sodium dodecyl sulfate-Polyacrylamide gel electrophoresis of membrane proteins. Electrophoresis 27: 2984-2995.
    • (2006) Electrophoresis , vol.27 , pp. 2984-2995
    • Williams, T.I.1    Combs, J.C.2    Thakur, A.P.3    Strobel, H.J.4    Lynn, B.C.5
  • 210
    • 0025782516 scopus 로고
    • A new multiphasic buffer system for sodium dodecyl sulfate-polyacrylamide gel electrophoresis of proteins and peptides with molecular masses 100, 000-1000, and their detection with picomolar sensitivity
    • Wiltfang J, Arold N, Neuhoff V. 1991. A new multiphasic buffer system for sodium dodecyl sulfate-polyacrylamide gel electrophoresis of proteins and peptides with molecular masses 100, 000-1000, and their detection with picomolar sensitivity. Electrophoresis 12: 352-366.
    • (1991) Electrophoresis , vol.12 , pp. 352-366
    • Wiltfang, J.1    Arold, N.2    Neuhoff, V.3
  • 211
    • 34447290244 scopus 로고    scopus 로고
    • Silver-and Coomassie-staining protocols: Detection limits and compatibility with ESI MS
    • Winkler C, Denker K, Wortelkamp S, Sickmann A. 2007. Silver-and Coomassie-staining protocols: Detection limits and compatibility with ESI MS. Electrophoresis 28: 2095-2099.
    • (2007) Electrophoresis , vol.28 , pp. 2095-2099
    • Winkler, C.1    Denker, K.2    Wortelkamp, S.3    Sickmann, A.4
  • 212
    • 0026062398 scopus 로고
    • Transfer of silver-stained proteins from polyacrylamide gels to polyvinylidene difluoride membranes
    • Wise GE, Lin F. 1991. Transfer of silver-stained proteins from polyacrylamide gels to polyvinylidene difluoride membranes. J Biochem Biophys Methods 22: 223-231.
    • (1991) J. Biochem. Biophys. Methods , vol.22 , pp. 223-231
    • Wise, G.E.1    Lin, F.2
  • 213
    • 35848970747 scopus 로고    scopus 로고
    • Mapping protein posttranslational modifications with mass spectrometry
    • Witze ES, Old WM, Resing KA, Ahn NG. 2007. Mapping protein posttranslational modifications with mass spectrometry. Nature Methods 4: 798-806.
    • (2007) Nature Methods , vol.4 , pp. 798-806
    • Witze, E.S.1    Old, W.M.2    Resing, K.A.3    Ahn, N.G.4
  • 215
    • 18844404358 scopus 로고    scopus 로고
    • Evaluating preparative isoelectric focusing of complex peptide mixtures for tandem mass spectrometrybased proteomics: A case study in profiling chromatin-enriched subcellular fractions in Saccharomyces cerevisiae
    • Xie H, Bandhakavi S, Griffin TJ. 2005. Evaluating preparative isoelectric focusing of complex peptide mixtures for tandem mass spectrometrybased proteomics: A case study in profiling chromatin-enriched subcellular fractions in Saccharomyces cerevisiae. Anal Chem 77: 3198-3207.
    • (2005) Anal Chem. , vol.77 , pp. 3198-3207
    • Xie, H.1    Bandhakavi, S.2    Griffin, T.J.3
  • 216
    • 34249275640 scopus 로고    scopus 로고
    • Preparative peptide isoelectric focusing as a tool for improving the identification of lysineacetylated peptides from complex mixtures
    • Xie H, Bandhakavi S, Roe MR, Griffin TJ. 2007. Preparative peptide isoelectric focusing as a tool for improving the identification of lysineacetylated peptides from complex mixtures. J Proteome Res 6: 2019-2026.
    • (2007) J. Proteome Res. , vol.6 , pp. 2019-2026
    • Xie, H.1    Bandhakavi, S.2    Roe, M.R.3    Griffin, T.J.4
  • 217
    • 40549131927 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis with cationic detergents, a powerful tool for the proteomic analysis of myelin proteins. Part 1: Technical aspects of electrophoresis
    • DOI 10.1002/jnr.21547
    • Yamaguchi Y, Miyagi Y, Baba H. 2008a. Two-dimensional electrophoresis with cationic detergents: A powerful tool for the proteomic analysis of myelin proteins. Part 1: Technical aspects of electrophoresis. J Neurosci Res 86: 755-765. (Pubitemid 351357757)
    • (2008) Journal of Neuroscience Research , vol.86 , Issue.4 , pp. 755-765
    • Yamaguchi, Y.1    Miyagi, Y.2    Baba, H.3
  • 218
    • 40549122720 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis with cationic detergents: A powerful tool for the proteomic analysis of myelin proteins. Part 2: Analytical aspects
    • DOI 10.1002/jnr.21549
    • Yamaguchi Y, Miyagi Y, Baba H. 2008b. Two-dimensional electrophoresis with cationic detergents: A powerful tool for the proteomic analysis of myelin proteins. Part2:Analytical aspects. J Neurosci Res 86: 766-775. (Pubitemid 351357758)
    • (2008) Journal of Neuroscience Research , vol.86 , Issue.4 , pp. 766-775
    • Yamaguchi, Y.1    Miyagi, Y.2    Baba, H.3
  • 219
    • 0008006733 scopus 로고    scopus 로고
    • Fractionation of peptides in protease digests of proteins by preparative isoelectric focusing in the absence of added ampholyte: A biocompatible and low-cost approach referred to as autofocusing
    • Yata M, Sato K, Ohtsuki K, Kawabata M. 1996. Fractionation of peptides in protease digests of proteins by preparative isoelectric focusing in the absence of added ampholyte: A biocompatible and low-cost approach referred to as autofocusing. J Agric Food Chem 44: 76-79.
    • (1996) J. Agric Food Chem. , vol.44 , pp. 76-79
    • Yata, M.1    Sato, K.2    Ohtsuki, K.3    Kawabata, M.4
  • 220
    • 0027375364 scopus 로고
    • Peptide mass maps: A highly informative approach to protein identification
    • Yates JR III, Speicher S, Griffin PR, Hunkapiller T. 1993. Peptide mass maps: A highly informative approach to protein identification. Anal Biochem 214: 397-408.
    • (1993) Anal Biochem. , vol.214 , pp. 397-408
    • Yates III, J.R.1    Speicher, S.2    Griffin, P.R.3    Hunkapiller, T.4
  • 221
    • 0021591436 scopus 로고
    • Advantages of separations on "giant" two-dimensional gels for detection of physiologically relevant changes in the expression of protein gene-products
    • Young DA. 1984. Advantages of separations on "giant" two-dimensional gels for detection of physiologically relevant changes in the expression of protein gene-products. Clin Chem 30: 2104-2108.
    • (1984) Clin Chem. , vol.30 , pp. 2104-2108
    • Young, D.A.1
  • 222
    • 33745360841 scopus 로고    scopus 로고
    • Comprehensive two-dimensional separation in coupling of reversed-phase chromatography with capillary isoelectric focusing followed by MALDI-MS identification using on-target digestion for intact protein analysis
    • Yu W, Li Y, Deng C, Zhang X. 2006. Comprehensive two-dimensional separation in coupling of reversed-phase chromatography with capillary isoelectric focusing followed by MALDI-MS identification using on-target digestion for intact protein analysis. Electrophoresis 27: 2100-2110.
    • (2006) Electrophoresis , vol.27 , pp. 2100-2110
    • Li, W.Y.Y.1    Deng, C.2    Zhang, X.3
  • 224
    • 25844494397 scopus 로고    scopus 로고
    • Two-dimensional benzyldimethyl-n-hexadecylammonium chloride/SDS-PAGE for membrane proteomics
    • Zahedi RP, Meisinger C, Sickmann A. 2005. Two-dimensional benzyldimethyl-n-hexadecylammonium chloride/SDS-PAGE for membrane proteomics. Proteomics 5: 3581-3588.
    • (2005) Proteomics , vol.5 , pp. 3581-3588
    • Zahedi, R.P.1    Meisinger, C.2    Sickmann, A.3
  • 225
    • 0026679750 scopus 로고
    • Polyethyleneglycol methacrylate 200 as an electrophoresis matrix in hydroorganic solvents
    • Zewert T, Harrington M. 1992. Polyethyleneglycol methacrylate 200 as an electrophoresis matrix in hydroorganic solvents. Electrophoresis 13: 824-831.
    • (1992) Electrophoresis , vol.13 , pp. 824-831
    • Zewert, T.1    Harrington, M.2
  • 227
    • 0034633273 scopus 로고    scopus 로고
    • A method for global analysis of complex proteomes using sample prefractionation by solution isoelectrofocusing prior to two-dimensional electrophoresis
    • Zuo X, Speicher DW. 2000. A method for global analysis of complex proteomes using sample prefractionation by solution isoelectrofocusing prior to two-dimensional electrophoresis. Anal Biochem 284: 266-278.
    • (2000) Anal Biochem. , vol.284 , pp. 266-278
    • Zuo, X.1    Speicher, D.W.2


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