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Volumn 7, Issue C, 2005, Pages 247-264

Isoelectric focusing and proteomics

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EID: 79959603794     PISSN: 18771718     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0149-6395(05)80012-5     Document Type: Book
Times cited : (1)

References (84)
  • 3
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M. P., Wolters, D. and Yates, J. R. III. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 19: 242-247, 2001.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates III, J.R.3
  • 4
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi, S. E, Rist, B., Gerber, S. A., Turecek, E, Gelb, M. H. and Aebersold, R. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 17:994-999, 1999.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.E.1    Rist, B.2    Gerber, S.A.3    Turecek, E.4    Gelb, M.H.5    Aebersold, R.6
  • 6
    • 0036208433 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis in proteomics: old, old fashioned, but it still climbs up the mountains
    • Rabilloud, T. Two-dimensional gel electrophoresis in proteomics: old, old fashioned, but it still climbs up the mountains. Proteomics 2:3-10, 2002.
    • (2002) Proteomics , vol.2 , pp. 3-10
    • Rabilloud, T.1
  • 8
    • 0034013175 scopus 로고    scopus 로고
    • Subproteomics based upon protein cellular location and relative solubilities in conjunction with composite two-dimensional electrophoresis gels
    • Cordwell, S. J., Nouwens, A. S., Verrills, N. M., Basseal, D. J. and Walsh, B. J. Subproteomics based upon protein cellular location and relative solubilities in conjunction with composite two-dimensional electrophoresis gels. Electrophoresis 21:1094-1103, 2000.
    • (2000) Electrophoresis , vol.21 , pp. 1094-1103
    • Cordwell, S.J.1    Nouwens, A.S.2    Verrills, N.M.3    Basseal, D.J.4    Walsh, B.J.5
  • 9
    • 0033849339 scopus 로고    scopus 로고
    • Towards higher resolution: two-dimensional electrophoresis of Saccharomyces cerevisiae proteins using overlapping narrow immobilized pH gradients
    • Wildgruber, R., Harder, A., Obermaier, C., Boguth, G., Weiss, W., Fey, S. J., Larsen, P. M. and Görg, A. Towards higher resolution: two-dimensional electrophoresis of Saccharomyces cerevisiae proteins using overlapping narrow immobilized pH gradients. Electrophoresis 21:2610-2616, 2000.
    • (2000) Electrophoresis , vol.21 , pp. 2610-2616
    • Wildgruber, R.1    Harder, A.2    Obermaier, C.3    Boguth, G.4    Weiss, W.5    Fey, S.J.6    Larsen, P.M.7    Görg, A.8
  • 10
    • 0034848343 scopus 로고    scopus 로고
    • Zooming-in on the proteome: very narrow-range immobilised pH gradients reveal more protein species and isoforms
    • Westbrook, J. A., Yan, J. X., Wait, R., Welson, S. Y. and Dunn, M. J. Zooming-in on the proteome: very narrow-range immobilised pH gradients reveal more protein species and isoforms. Electrophoresis 22:2865-2871, 2001.
    • (2001) Electrophoresis , vol.22 , pp. 2865-2871
    • Westbrook, J.A.1    Yan, J.X.2    Wait, R.3    Welson, S.Y.4    Dunn, M.J.5
  • 11
    • 0037023859 scopus 로고    scopus 로고
    • Detection technologies in proteome analysis
    • Patton, W. F. Detection technologies in proteome analysis. J. Chromatogr. B. 771:3-31, 2002.
    • (2002) J. Chromatogr. B. , vol.771 , pp. 3-31
    • Patton, W.F.1
  • 14
    • 0037294859 scopus 로고    scopus 로고
    • Proteome analysis at the level of subcellular structures
    • Dreger, M. Proteome analysis at the level of subcellular structures. Eur. J. Biochem. 270:589-599, 2003.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 589-599
    • Dreger, M.1
  • 16
    • 0032720603 scopus 로고    scopus 로고
    • Enrichment of human brain proteins by heparin chromatography
    • Karlsson, K., Cairns, N., Lubec, G. and Fountoulakis, M. Enrichment of human brain proteins by heparin chromatography. Electrophoresis 20:2970-2976, 1999.
    • (1999) Electrophoresis , vol.20 , pp. 2970-2976
    • Karlsson, K.1    Cairns, N.2    Lubec, G.3    Fountoulakis, M.4
  • 17
    • 0344898564 scopus 로고    scopus 로고
    • Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography
    • Fountoulakis, M., Takacs, M. E, Berndt, E, Langen, H. and Takacs, B. Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography. Electrophoresis 20:2181-2195, 1999.
    • (1999) Electrophoresis , vol.20 , pp. 2181-2195
    • Fountoulakis, M.1    Takacs, M.2    Berndt, E.3    Langen, E.4    Takacs, H.B.5
  • 19
    • 0036224270 scopus 로고    scopus 로고
    • Organellar proteomics: the prizes and pitfalls of opening the nuclear envelope
    • Schirmer, E. C. and Gerace, L. Organellar proteomics: the prizes and pitfalls of opening the nuclear envelope. Genome Biol. 3:1008.1-1008.4, 2002.
    • (2002) Genome Biol , vol.3
    • Schirmer, E.C.1    Gerace, L.2
  • 20
    • 0038637237 scopus 로고    scopus 로고
    • Mitochondrial proteomicsmundercover in the lipid bilayer
    • McDonald, T. G. and Van Eyk, J. E. Mitochondrial proteomicsmundercover in the lipid bilayer. Basic Res. Cardiol. 98:219-227, 2003.
    • (2003) Basic Res. Cardiol. , vol.98 , pp. 219-227
    • McDonald, T.G.1    Van Eyk, J.E.2
  • 21
    • 0037269174 scopus 로고    scopus 로고
    • The mitochondrial proteins of the neuroblastoma cell line IMR-32
    • Fountoulakis, M. and Schlaeger, E. J. The mitochondrial proteins of the neuroblastoma cell line IMR-32. Electrophoresis 24: 260-275, 2003.
    • (2003) Electrophoresis , vol.24 , pp. 260-275
    • Fountoulakis, M.1    Schlaeger, E.J.2
  • 23
    • 0034630358 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis of membrane proteins using immobilized pH gradients
    • Molloy, M. P. Two-dimensional electrophoresis of membrane proteins using immobilized pH gradients. Anal. Biochem. 280:1-10, 2000.
    • (2000) Anal. Biochem. , vol.280 , pp. 1-10
    • Molloy, M.P.1
  • 26
    • 0036908432 scopus 로고    scopus 로고
    • Subproteomics: identification of plasma membrane proteins from the yeast Saccharomyces cerevisiae
    • Navarre, C., Degand, H., Bennett, K. L., Crawford, J. S., Mortz, E. and Boutry, M. Subproteomics: identification of plasma membrane proteins from the yeast Saccharomyces cerevisiae. Proteomics 2:1706-1714, 2002.
    • (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
  • 27
    • 0344494027 scopus 로고    scopus 로고
    • Applications of affinity chromatography in proteomics
    • Lee, W.-C. and Lee, K. H. Applications of affinity chromatography in proteomics. Anal. Biochem. 324:1-10, 2004.
    • (2004) Anal. Biochem. , vol.324 , pp. 1-10
    • Lee, W.-C.1    Lee, K.H.2
  • 28
    • 0037387175 scopus 로고    scopus 로고
    • Multicomponent immunoaffinity subtraction chromatography: an innovative step towards a comprehensive survey of the human plasma proteome
    • Pieper, R., Su, Q., Gatlin, C. L., Huang, S. T., Anderson, N. L. and Steiner, S. Multicomponent immunoaffinity subtraction chromatography: an innovative step towards a comprehensive survey of the human plasma proteome. Proteomics 3:422-432, 2003.
    • (2003) Proteomics , vol.3 , pp. 422-432
    • Pieper, R.1    Su, Q.2    Gatlin, C.L.3    Huang, S.T.4    Anderson, N.L.5    Steiner, S.6
  • 30
    • 0033944610 scopus 로고    scopus 로고
    • Identification of two-dimensionally separated human cerebrospinal fluid proteins by N-terminal sequencing, matrix-assisted laser desorption/ionization - mass spectrometry, nanoliquid chromatography - electrospray ionization -time of flight mass spectrometry, and tandem mass spectrometry
    • Raymackers, J., Daniels, A., De Brabandere, V., Missiaen, C., Dauwe, M., Verhaert, R, Vanmechelen, E. and Meheus, L. Identification of two-dimensionally separated human cerebrospinal fluid proteins by N-terminal sequencing, matrix-assisted laser desorption/ionization - mass spectrometry, nanoliquid chromatography - electrospray ionization -time of flight mass spectrometry, and tandem mass spectrometry. Electrophoresis 21:2266-2283, 2000.
    • (2000) Electrophoresis , vol.21 , pp. 2266-2283
    • Raymackers, J.1    Daniels, A.2    De Brabandere, V.3    Missiaen, C.4    Dauwe, M.5    Verhaert, R.6    Vanmechelen, E.7    Meheus, L.8
  • 31
    • 0027284485 scopus 로고    scopus 로고
    • Classification of mouse liver proteins by immobilized metal affinity chromatography and two-dimensional electrophoresis
    • Jungblut, P., Baumeister, H. and Klose, J. Classification of mouse liver proteins by immobilized metal affinity chromatography and two-dimensional electrophoresis. Electrophoresis 14:638-643, 1996.
    • (1996) Electrophoresis , vol.14 , pp. 638-643
    • Jungblut, P.1    Baumeister, H.2    Klose, J.3
  • 34
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R. and Mann, M. Mass spectrometry-based proteomics. Nature 422:198-207, 2003.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 36
    • 0038034950 scopus 로고    scopus 로고
    • Analysis of steady-state protein phosphorylation in mitochondria using a novel fluorescent phosphosensor dye
    • Schulenberg, B., Aggeler, R., Beechem, J. M., Capaldi, R. A. and Patton, W. F. Analysis of steady-state protein phosphorylation in mitochondria using a novel fluorescent phosphosensor dye. J. Biol. Chem. 278:27251-27255, 2003.
    • (2003) J. Biol. Chem. , vol.278 , pp. 27251-27255
    • Schulenberg, B.1    Aggeler, R.2    Beechem, J.M.3    Capaldi, R.A.4    Patton, W.F.5
  • 37
    • 0037296893 scopus 로고    scopus 로고
    • Detection of glycoproteins in polyacrylamide gels and on electroblots using Pro-Q Emerald 488 dye, a fluorescent periodate Schiff-base stain
    • Hart, C., Schulenberg, B., Steinberg, T. H., Leung, W. Y. and Patton, W. F. Detection of glycoproteins in polyacrylamide gels and on electroblots using Pro-Q Emerald 488 dye, a fluorescent periodate Schiff-base stain. Electrophoresis 24:588-598, 2003.
    • (2003) Electrophoresis , vol.24 , pp. 588-598
    • Hart, C.1    Schulenberg, B.2    Steinberg, T.H.3    Leung, W.Y.4    Patton, W.F.5
  • 39
    • 0026043017 scopus 로고
    • Preparative isoelectric focusing and high resolution 2-dimensional gel electrophoresis for concentration and purification of proteins
    • Hochstrasser, A. C., James, R. W., Pometta, D. and Hochstrasser, D. F. Preparative isoelectric focusing and high resolution 2-dimensional gel electrophoresis for concentration and purification of proteins. Appl. Theor. Electrophoresis 1:333-337, 1991.
    • (1991) Appl. Theor. Electrophoresis , vol.1 , pp. 333-337
    • Hochstrasser, A.C.1    James, R.W.2    Pometta, D.3    Hochstrasser, D.F.4
  • 40
    • 0032787029 scopus 로고    scopus 로고
    • Analysis of intact proteins from cerebrospinal fluid by matrix-assisted laser desorption/ionization mass spectrometry after two-dimensional liquid-phase electrophoresis
    • Puchades, M., Westman, A., Blennow, K. and Davidsson, P. Analysis of intact proteins from cerebrospinal fluid by matrix-assisted laser desorption/ionization mass spectrometry after two-dimensional liquid-phase electrophoresis. Rapid Commun. Mass Spectrom. 13:2450-2455, 1999.
    • (1999) Rapid Commun. Mass Spectrom. , vol.13 , pp. 2450-2455
    • Puchades, M.1    Westman, A.2    Blennow, K.3    Davidsson, P.4
  • 41
    • 0032713887 scopus 로고    scopus 로고
    • Peptide mapping of proteins in cerebrospinal fluid utilizing a rapid preparative two-dimensional electrophoretic procedure and matrixassisted laser desorption/ionization mass spectrometry
    • Davidsson, P. and Nilsson, C. L. Peptide mapping of proteins in cerebrospinal fluid utilizing a rapid preparative two-dimensional electrophoretic procedure and matrixassisted laser desorption/ionization mass spectrometry. Biochim. Biophys. Acta 1473:391-399,1999.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 391-399
    • Davidsson, P.1    Nilsson, C.L.2
  • 42
    • 0036748267 scopus 로고    scopus 로고
    • A protein molecular weight map of ES2 clear cell ovarian carcinoma cells using a two-dimensional liquid separations/mass mapping technique
    • Wang, H., Kachman, M. T., Schwartz, D. R., Cho, K. R. and Lubman, D. M. A protein molecular weight map of ES2 clear cell ovarian carcinoma cells using a two-dimensional liquid separations/mass mapping technique. Electrophoresis 23:3168-3181, 2002.
    • (2002) Electrophoresis , vol.23 , pp. 3168-3181
    • Wang, H.1    Kachman, M.T.2    Schwartz, D.R.3    Cho, K.R.4    Lubman, D.M.5
  • 43
    • 0346504157 scopus 로고    scopus 로고
    • Carrier ampholyte-free solution isoelectric focusing as a prefractionation method for the proteomic analysis of complex protein mixtures
    • Shang, T. Q., Ginter, J. M., Johnston, M. V., Larsen, B. S. and McEwen, C. N. Carrier ampholyte-free solution isoelectric focusing as a prefractionation method for the proteomic analysis of complex protein mixtures. Electrophoresis 24:2359-2368, 2003.
    • (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
  • 45
    • 0037345830 scopus 로고    scopus 로고
    • Depletion of the highly abundant protein albumin from human plasma using the Gradiflow
    • Rothemund, D. L., Locke, V. L., Liew, A., Thomas, T. M., Wasinger, V. and Rylatt, D. B. Depletion of the highly abundant protein albumin from human plasma using the Gradiflow. Proteomics 3:279-287, 2003.
    • (2003) Proteomics , vol.3 , pp. 279-287
    • Rothemund, D.L.1    Locke, V.L.2    Liew, A.3    Thomas, T.M.4    Wasinger, V.5    Rylatt, D.B.6
  • 46
    • 0036744355 scopus 로고    scopus 로고
    • Gradiflow as a prefractionation tool for two-dimensional electrophoresis
    • Locke, V. L., Gibson, T. S., Thomas, T. M., Corthals, G. L. and Rylatt, D. B. Gradiflow as a prefractionation tool for two-dimensional electrophoresis. Proteomics 2:1254-1260, 2002.
    • (2002) Proteomics , vol.2 , pp. 1254-1260
    • Locke, V.L.1    Gibson, T.S.2    Thomas, T.M.3    Corthals, G.L.4    Rylatt, D.B.5
  • 47
    • 0347134482 scopus 로고    scopus 로고
    • Impact of prefractionation using Gradiflow™ on two-dimensional gel electrophoresis and protein identification by matrix assisted laser desorption/ionization-time of flightmass spectrometry
    • Pang, L., Fryksdale, B. G., Chow, N., Wong, D. L., Gaertner, A. L. and Miller, B. S. Impact of prefractionation using Gradiflow™ on two-dimensional gel electrophoresis and protein identification by matrix assisted laser desorption/ionization-time of flightmass spectrometry. Electrophoresis 24:3484-3492, 2003.
    • (2003) Electrophoresis , vol.24 , pp. 3484-3492
    • Pang, L.1    Fryksdale, B.G.2    Chow, N.3    Wong, D.L.4    Gaertner, A.L.5    Miller, B.S.6
  • 49
    • 0025189519 scopus 로고
    • Preparative purification of human monoclonal antibody isoforms in a multi-compartment electrolyser with immobiline membranes
    • Righetti, P. G., Wenisch, E., Jungbauer, A., Katinger, H. and Faupel, M. Preparative purification of human monoclonal antibody isoforms in a multi-compartment electrolyser with immobiline membranes. J. Chromatogr. 500:681-696, 1990.
    • (1990) J. Chromatogr. , vol.500 , pp. 681-696
    • Righetti, P.G.1    Wenisch, E.2    Jungbauer, A.3    Katinger, H.4    Faupel, M.5
  • 50
    • 0030783605 scopus 로고    scopus 로고
    • Protein purification in multicompartment electrolyzers with isoelectric membranes
    • Righetti, P. G., Bossi, A., Wenisch, E. and Orsini, G. Protein purification in multicompartment electrolyzers with isoelectric membranes. J. Chromatogr. B. 699:105-115, 1997.
    • (1997) J. Chromatogr. B. , vol.699 , pp. 105-115
    • Righetti, P.G.1    Bossi, A.2    Wenisch, E.3    Orsini, G.4
  • 51
    • 0033672478 scopus 로고    scopus 로고
    • A turning point in proteome analysis: sample prefractionation via multicompartment electrolyzers with isoelectric membranes
    • Herbert, B. and Righetti, P. G. A turning point in proteome analysis: sample prefractionation via multicompartment electrolyzers with isoelectric membranes. Electrophoresis 21:3639-3648, 2000.
    • (2000) Electrophoresis , vol.21 , pp. 3639-3648
    • Herbert, B.1    Righetti, P.G.2
  • 52
    • 0034633273 scopus 로고    scopus 로고
    • A method for global analysis of complex proteomes using sample prefractionation by solution isoelectricfocusing prior to two-dimensional electrophoresis
    • Zuo, X. and Speicher, D. W. A method for global analysis of complex proteomes using sample prefractionation by solution isoelectricfocusing prior to two-dimensional electrophoresis. Anal. Biochem. 284:266-278, 2000.
    • (2000) Anal. Biochem. , vol.284 , pp. 266-278
    • Zuo, X.1    Speicher, D.W.2
  • 53
    • 0036206101 scopus 로고    scopus 로고
    • Comprehensive analysis of complex proteomes using microscale solution isolectricfocusing prior to narrow pH range two-dimensional electrophoresis
    • Zuo, X. and Speicher, D. W. Comprehensive analysis of complex proteomes using microscale solution isolectricfocusing prior to narrow pH range two-dimensional electrophoresis. Proteomics 2:58-68, 2002.
    • (2002) Proteomics , vol.2 , pp. 58-68
    • Zuo, X.1    Speicher, D.W.2
  • 54
    • 0037176218 scopus 로고    scopus 로고
    • Enhanced analysis of human breast cancer proteomes using micro-scale solution isoelectricfocusing combined with high resolution 1-D and 2-D gels
    • Zuo, X., Hembach, P., Echan, L. and Speicher, D. W. Enhanced analysis of human breast cancer proteomes using micro-scale solution isoelectricfocusing combined with high resolution 1-D and 2-D gels. J. Chromatogr. B 782:253-265, 2002.
    • (2002) J. Chromatogr. B , vol.782 , pp. 253-265
    • Zuo, X.1    Hembach, P.2    Echan, L.3    Speicher, D.W.4
  • 55
    • 73649124287 scopus 로고    scopus 로고
    • Towards global analysis of mammalian proteomes using sample prefractionation prior to narrow pH range two-dimensional gels and using one-dimensional gels for insoluble and large proteins
    • Zuo, X., Echan, L., Hembach, P., Tang, H. Y., Speicher, K. D., Santoli, D. and Speicher, D. W. Towards global analysis of mammalian proteomes using sample prefractionation prior to narrow pH range two-dimensional gels and using one-dimensional gels for insoluble and large proteins. Electrophoresis 22:1603-1615, 2001.
    • (2001) Electrophoresis , vol.22 , pp. 1603-1615
    • Zuo, X.1    Echan, L.2    Hembach, P.3    Tang, H.Y.4    Speicher, K.D.5    Santoli, D.6    Speicher, D.W.7
  • 56
    • 0036917339 scopus 로고    scopus 로고
    • Sample prefractionation with Sephadex isoelectric focusing prior to narrow pH range two-dimensional gels
    • Görg, A., Boguth, G., Kopf, A., Reil, G., Parlar, H. and Weiss, W. Sample prefractionation with Sephadex isoelectric focusing prior to narrow pH range two-dimensional gels. Proteomics 2:1652-1657, 2002.
    • (2002) Proteomics , vol.2 , pp. 1652-1657
    • Görg, A.1    Boguth, G.2    Kopf, A.3    Reil, G.4    Parlar, H.5    Weiss, W.6
  • 57
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P. H. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250:4007-4021, 1975.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 58
    • 0032617061 scopus 로고    scopus 로고
    • E 2-D electrophoresis using carrier ampholytes in the first dimension (IEF)
    • Lopez, M. E 2-D electrophoresis using carrier ampholytes in the first dimension (IEF). Methods Mol. Biol. 112:111-127, 1999.
    • (1999) Methods Mol. Biol. , vol.112 , pp. 111-127
    • Lopez, M.1
  • 59
    • 0033947571 scopus 로고    scopus 로고
    • Bladder squamous cell carcinoma biomarkers derived from proteomics
    • Celis, J. E., Wolf, H. and Ostergaard, M. Bladder squamous cell carcinoma biomarkers derived from proteomics. Electrophoresis 21:2115-2121, 2000.
    • (2000) Electrophoresis , vol.21 , pp. 2115-2121
    • Celis, J.E.1    Wolf, H.2    Ostergaard, M.3
  • 60
    • 0032948126 scopus 로고    scopus 로고
    • 2-D protein electrophoresis: can it be perfected? Curr
    • Celis, J. E. and Gromov, P. 2-D protein electrophoresis: can it be perfected? Curr. Opin. Biotechnol. 10:16-21, 1999.
    • (1999) Opin. Biotechnol. , vol.10 , pp. 16-21
    • Celis, J.E.1    Gromov, P.2
  • 62
    • 0141497111 scopus 로고    scopus 로고
    • Probing the molecular physiology of the microbial organism, Escherichia coli using proteomics
    • VanBogelen, R. A. Probing the molecular physiology of the microbial organism, Escherichia coli using proteomics. Adv. Biochem. Eng. Biotechnol. 83:27-55 (2003).
    • (2003) Adv. Biochem. Eng. Biotechnol. , vol.83 , pp. 27-55
    • VanBogelen, R.A.1
  • 63
    • 0029418629 scopus 로고
    • Application of two-dimensional protein gels in biotechnology
    • VanBogelen, R. A. and Olson, E. R. Application of two-dimensional protein gels in biotechnology. Biotechnol. Annu. Rev. 1:69-103, 1995.
    • (1995) Biotechnol. Annu. Rev. , vol.1 , pp. 69-103
    • VanBogelen, R.A.1    Olson, E.R.2
  • 64
    • 0141831778 scopus 로고    scopus 로고
    • A proteomic view of cell physiology of Bacillus subtilis--bringing the genome sequence to life
    • Hecker, M. A proteomic view of cell physiology of Bacillus subtilis--bringing the genome sequence to life. Adv. Biochem. Eng. Biotechnol. 83:57-92, 2003.
    • (2003) Adv. Biochem. Eng. Biotechnol. , vol.83 , pp. 57-92
    • Hecker, M.1
  • 65
    • 0034118606 scopus 로고    scopus 로고
    • Proteomics, DNA arrays and the analysis of still unknown regulons and unknown proteins of Bacillus subtilis and pathogenic grampositive bacteria
    • Hecker, M. and Engelmann, S. Proteomics, DNA arrays and the analysis of still unknown regulons and unknown proteins of Bacillus subtilis and pathogenic grampositive bacteria. Int. J. Med. Microbiol. 290:123-134, 2000.
    • (2000) Int. J. Med. Microbiol. , vol.290 , pp. 123-134
    • Hecker, M.1    Engelmann, S.2
  • 66
    • 0346504006 scopus 로고    scopus 로고
    • Quantitative and qualitative measure of interlaboratory two-dimensional protein gel reproducibility and the effects of sample preparation, sample load, and image analysis
    • Choe, L. H. and Lee, K. H. Quantitative and qualitative measure of interlaboratory two-dimensional protein gel reproducibility and the effects of sample preparation, sample load, and image analysis. Electrophoresis 24:3500-3507, 2003.
    • (2003) Electrophoresis , vol.24 , pp. 3500-3507
    • Choe, L.H.1    Lee, K.H.2
  • 67
    • 0036638067 scopus 로고    scopus 로고
    • Quantitative evaluation of proteins in one- and twodimensional polyacrylamide gels using a fluorescent stain
    • Nishihara, J. C. and Champion, K. M. Quantitative evaluation of proteins in one- and twodimensional polyacrylamide gels using a fluorescent stain. Electrophoresis 23:2203-2215, 2002.
    • (2002) Electrophoresis , vol.23 , pp. 2203-2215
    • Nishihara, J.C.1    Champion, K.M.2
  • 68
    • 0037563355 scopus 로고    scopus 로고
    • Very alkaline immobilized pH gradients for two-dimensional electrophoresis of ribosomal and nuclear proteins
    • Görg, A., Obermaier, C., Boguth, G., Csordas, A., Diaz, J. J. and Madjar, J. J. Very alkaline immobilized pH gradients for two-dimensional electrophoresis of ribosomal and nuclear proteins. Electrophoresis 18:328-337, 1997.
    • (1997) Electrophoresis , vol.18 , pp. 328-337
    • Görg, A.1    Obermaier, C.2    Boguth, G.3    Csordas, A.4    Diaz, J.J.5    Madjar, J.J.6
  • 69
    • 0017696571 scopus 로고
    • High resolution two-dimensional electrophoresis of basic as well as acidic proteins
    • O'Farrell, P. Z., Goodman, H. M. and O'Farrell, P. H. High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell 12:1133-1141, 1977.
    • (1977) Cell , vol.12 , pp. 1133-1141
    • O'Farrell, P.Z.1    Goodman, H.M.2    O'Farrell, P.H.3
  • 70
    • 0030852415 scopus 로고    scopus 로고
    • Characterisation of basic proteins from Spiroplasma melliferum using novel immobilised pH gradients
    • Cordwell, S. J., Basseal, D. J., Bjellqvist, B., Shaw, D. C. and Humphery-Smith, I. Characterisation of basic proteins from Spiroplasma melliferum using novel immobilised pH gradients. Electrophoresis 18:1393-1398, 1997.
    • (1997) Electrophoresis , vol.18 , pp. 1393-1398
    • Cordwell, S.J.1    Basseal, D.J.2    Bjellqvist, B.3    Shaw, D.C.4    Humphery-Smith, I.5
  • 71
    • 0036858458 scopus 로고    scopus 로고
    • Organic disulfides as a means to generate streak-free two-dimensional maps with narrow range basic immobilized pH gradient strips as first dimension
    • Olsson, I., Larrson, K., Palmgren, R. and Bjellqvist, B. Organic disulfides as a means to generate streak-free two-dimensional maps with narrow range basic immobilized pH gradient strips as first dimension. Proteomics 2:1630-1632, 2002.
    • (2002) Proteomics , vol.2 , pp. 1630-1632
    • Olsson, I.1    Larrson, K.2    Palmgren, R.3    Bjellqvist, B.4
  • 72
    • 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. and Righetti, P. G. Towards new formulations for polyacrylamide matrices: N-acryloylaminoethoxyethanol, a novel monomer combining high hydrophilicity with extreme hydrolytic stability. Electrophoresis 15:177-186, 1994.
    • (1994) Electrophoresis , vol.15 , pp. 177-186
    • Chiari, M.1    Micheletti, C.2    Nesi, M.3    Fazio, M.4    Righetti, P.G.5
  • 73
    • 0036204065 scopus 로고    scopus 로고
    • Preparative two-dimensional gel electrophoresis at alkaline pH using narrow range immobilized pH gradients
    • Hoving, S., Gerrits, B., Voshol, H., Müller, D., Roberts, R. C. and van Oostrum, J. M Preparative two-dimensional gel electrophoresis at alkaline pH using narrow range immobilized pH gradients. Proteomics 2:127-134, 2002.
    • (2002) Proteomics , vol.2 , pp. 127-134
    • Hoving, S.1    Gerrits, B.2    Voshol, H.3    Müller, D.4    Roberts, R.C.5    van Oostrum, J.6
  • 74
    • 2642535128 scopus 로고    scopus 로고
    • A high-throughput approach for subcellular proteome: identification of rat liver proteins using subcellular fractionation coupled with twodimensional liquid chromatography tandem mass spectrometry and bioinformatic analysis
    • Jiang, X. S., Zhou, H., Zhang, L., Sheng, Q. H., Li, S. J., Li, L., Hao, P., Li, Y. X., Xia, Q. C., Wu, J. R. and Zeng, R. A high-throughput approach for subcellular proteome: identification of rat liver proteins using subcellular fractionation coupled with twodimensional liquid chromatography tandem mass spectrometry and bioinformatic analysis. Mol. Cell Proteomics 3:441-455, 2004.
    • (2004) Mol. Cell Proteomics , vol.3 , pp. 441-455
    • Jiang, X.S.1    Zhou, H.2    Zhang, L.3    Sheng, Q.H.4    Li, S.J.5    Li, L.6    Hao, P.7    Li, Y.X.8    Xia, Q.C.9    Wu, J.R.10    Zeng, R.11
  • 76
    • 0036178646 scopus 로고    scopus 로고
    • Two-dimensional maps in soft immobilized pH gradient gels: a new approach to the proteome of the third millennium
    • Candiano, G., Musante, L., Bruschi, M., Ghiggeri, G. M., Herbert, B., Antonucci, E and Righetti, E G. Two-dimensional maps in soft immobilized pH gradient gels: a new approach to the proteome of the third millennium. Electrophoresis 23:292-297, 2002.
    • (2002) Electrophoresis , vol.23 , pp. 292-297
    • Candiano, G.1    Musante, L.2    Bruschi, M.3    Ghiggeri, G.M.4    Herbert, B.5    Antonucci, E.6    Righetti, E.G.7
  • 78
    • 0037023865 scopus 로고    scopus 로고
    • Separation techniques for high-molecular-mass proteins
    • Oh-Ishi, M. and Maeda, T. Separation techniques for high-molecular-mass proteins. J. Chromatogr. B 771:49-66, 2002.
    • (2002) J. Chromatogr. B , vol.771 , pp. 49-66
    • Oh-Ishi, M.1    Maeda, T.2
  • 79
    • 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. and von Jagow, G. 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.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 80
    • 0029983370 scopus 로고    scopus 로고
    • Micropreparative gel electrophoresis of low-molecular-weight peptides: purification of highly insoluble amyloid peptide fragments
    • Baumann, M., Golabek, A., Lalowski, M. and Wisniewski, T. Micropreparative gel electrophoresis of low-molecular-weight peptides: purification of highly insoluble amyloid peptide fragments. Anal. Biochem. 236:191-198, 1996.
    • (1996) Anal. Biochem. , vol.236 , pp. 191-198
    • Baumann, M.1    Golabek, A.2    Lalowski, M.3    Wisniewski, T.4
  • 82
    • 0032449759 scopus 로고    scopus 로고
    • Small genes/gene-products in Escherichia coli K12
    • Wasinger, V. C. and Humphery-Smith, I. Small genes/gene-products in Escherichia coli K12. FEMS Microbiol. Lett. 169:375-382, 1998.
    • (1998) FEMS Microbiol. Lett. , vol.169 , pp. 375-382
    • Wasinger, V.C.1    Humphery-Smith, I.2
  • 83
    • 1442300865 scopus 로고    scopus 로고
    • Fractionation of liver proteins by preparative electrophoresis
    • Fountoulakis, M., Juranville, J. F., Tsangaris, G. and Suter, L. Fractionation of liver proteins by preparative electrophoresis. Amino Acids 26:27-36, 2004.
    • (2004) Amino Acids , vol.26 , pp. 27-36
    • Fountoulakis, M.1    Juranville, J.F.2    Tsangaris, G.3    Suter, L.4
  • 84
    • 0037442466 scopus 로고    scopus 로고
    • Enrichment of low-abundance brain proteins by preparative electrophoresis
    • Fountoulakis, M. and Juranville, J. F. Enrichment of low-abundance brain proteins by preparative electrophoresis. Anal. Biochem. 313:267-282, 2003.
    • (2003) Anal. Biochem. , vol.313 , pp. 267-282
    • Fountoulakis, M.1    Juranville, J.F.2


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