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Volumn 8, Issue 23-24, 2008, Pages 4886-4897

Difference gel electrophoresis

Author keywords

2 DE; DIGE; Mass spectrometry; Quantitation

Indexed keywords

DIGE; GEL ELECTROPHORESIS; HUMAN; INTERMETHOD COMPARISON; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEOMICS; QUANTITATIVE ANALYSIS; REVIEW; SEPARATION TECHNIQUE; TWO DIMENSIONAL GEL ELECTROPHORESIS;

EID: 57649153125     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200800298     Document Type: Review
Times cited : (203)

References (117)
  • 1
    • 0034921817 scopus 로고    scopus 로고
    • Differential stable isotope labeling of peptides for quantitation and de novo sequence derivation
    • Goodlett, D. R., Keller, A., Watts, J. D., Newitt, R. et al., Differential stable isotope labeling of peptides for quantitation and de novo sequence derivation. Rapid Commun. Mass Spectrom. 2001, 15, 1214-1221.
    • (2001) Rapid Commun. Mass Spectrom , vol.15 , pp. 1214-1221
    • Goodlett, D.R.1    Keller, A.2    Watts, J.D.3    Newitt, R.4
  • 2
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi, S. P., Rist, B., Gerber, S. A., Turecek, F. et al., Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 1999, 17, 994-999.
    • (1999) Nat. Biotechnol , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4
  • 3
    • 34250657012 scopus 로고    scopus 로고
    • Quantitative proteome analysis using isotope-coded affinity tags and mass spectrometry
    • Shiio, Y., Aebersold, R., Quantitative proteome analysis using isotope-coded affinity tags and mass spectrometry. Nat. Protoc. 2006, 1, 139-145.
    • (2006) Nat. Protoc , vol.1 , pp. 139-145
    • Shiio, Y.1    Aebersold, R.2
  • 4
    • 35648942133 scopus 로고    scopus 로고
    • 8-plex quantitation of changes in cerebrospinal fluid protein expression in subjects undergoing intravenous immunoglobulin treatment for Alzheimer's disease
    • Choe, L., D'Ascenzo, M., Relkin, N. R., Pappin, D. et al., 8-plex quantitation of changes in cerebrospinal fluid protein expression in subjects undergoing intravenous immunoglobulin treatment for Alzheimer's disease. Proteomics 2007, 7, 3651-3660.
    • (2007) Proteomics , vol.7 , pp. 3651-3660
    • Choe, L.1    D'Ascenzo, M.2    Relkin, N.R.3    Pappin, D.4
  • 5
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross, P. L., Huang, Y. N., Marchese, J. N., Williamson, B. et al., Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol. Cell. Proteomics 2004, 3, 1154-1169.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 1154-1169
    • Ross, P.L.1    Huang, Y.N.2    Marchese, J.N.3    Williamson, B.4
  • 6
    • 33845329203 scopus 로고    scopus 로고
    • Functional and quantitative proteomics using SILAC
    • Mann, M., Functional and quantitative proteomics using SILAC. Nat. Rev. Mol. Cell Biol. 2006, 7, 952-958.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 952-958
    • Mann, M.1
  • 7
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B. et al., Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 2002, 1, 376-386.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4
  • 8
    • 34250372908 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture for quantitative proteomics
    • Ong, S. E., Mann, M., Stable isotope labeling by amino acids in cell culture for quantitative proteomics. Methods Mol. Biol. 2007, 359, 37-52.
    • (2007) Methods Mol. Biol , vol.359 , pp. 37-52
    • Ong, S.E.1    Mann, M.2
  • 9
    • 13244260803 scopus 로고    scopus 로고
    • A novel strategy for quantitative proteomics using isotope-coded protein labels
    • Schmidt, A., Kellermann, J., Lottspeich, F., A novel strategy for quantitative proteomics using isotope-coded protein labels. Proteomics 2005, 5, 4-15.
    • (2005) Proteomics , vol.5 , pp. 4-15
    • Schmidt, A.1    Kellermann, J.2    Lottspeich, F.3
  • 10
    • 42649132889 scopus 로고    scopus 로고
    • SILAC-labeling and proteome quantitation of mouse embryonic stem cells to a depth of 5111 proteins
    • Graumann, J., Hubner, N. C., Kim, J. B., Ko, K. et al., SILAC-labeling and proteome quantitation of mouse embryonic stem cells to a depth of 5111 proteins. Mol. Cell. Proteomics 2008, 7, 672-683.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 672-683
    • Graumann, J.1    Hubner, N.C.2    Kim, J.B.3    Ko, K.4
  • 11
    • 36048956962 scopus 로고    scopus 로고
    • Multidimensional liquid phase protein separations in conjunction with stable isotope labelling for quantitative proteomics
    • Assiddiq, B. F., Williamson, J. C., Snijders, A. P., Cook, K., Dickman, M. J., Multidimensional liquid phase protein separations in conjunction with stable isotope labelling for quantitative proteomics. Proteomics 2007, 7, 3826-3834.
    • (2007) Proteomics , vol.7 , pp. 3826-3834
    • Assiddiq, B.F.1    Williamson, J.C.2    Snijders, A.P.3    Cook, K.4    Dickman, M.J.5
  • 12
    • 35348939574 scopus 로고    scopus 로고
    • Quantitative proteomics using uniform (15)N-labeling, MASCOT, and the trans-proteomic pipeline
    • Palmblad, M., Bindschedler, L. V., Cramer, R., Quantitative proteomics using uniform (15)N-labeling, MASCOT, and the trans-proteomic pipeline. Proteomics 2007, 7, 3462-3469.
    • (2007) Proteomics , vol.7 , pp. 3462-3469
    • Palmblad, M.1    Bindschedler, L.V.2    Cramer, R.3
  • 13
    • 13844317869 scopus 로고    scopus 로고
    • Proteome dynamics in complex organisms: Using stable isotopes to monitor individual protein turnover rates
    • Doherty, M. K., Whitehead, C., McCormack, H., Gaskell, S. J., Beynon, R. J., Proteome dynamics in complex organisms: using stable isotopes to monitor individual protein turnover rates. Proteomics 2005, 5, 522-533.
    • (2005) Proteomics , vol.5 , pp. 522-533
    • Doherty, M.K.1    Whitehead, C.2    McCormack, H.3    Gaskell, S.J.4    Beynon, R.J.5
  • 14
    • 0001644020 scopus 로고    scopus 로고
    • The human plasma proteome: History, character, and diagnostic prospects
    • Anderson, N. L., Anderson, N. G., The human plasma proteome: history, character, and diagnostic prospects. Mol. Cell. Proteomics 2002, 1, 845-867.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 845-867
    • Anderson, N.L.1    Anderson, N.G.2
  • 15
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlu, M., Morgan, M. E., Minden, J. S., Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis 1997, 18, 2071-2077.
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 16
    • 34248180415 scopus 로고    scopus 로고
    • Two-dimensional difference gel electrophoresis
    • Viswanathan, S., Unlu, M., Minden, J. S., Two-dimensional difference gel electrophoresis. Nat. Protoc 2006, 1, 1351-1358.
    • (2006) Nat. Protoc , vol.1 , pp. 1351-1358
    • Viswanathan, S.1    Unlu, M.2    Minden, J.S.3
  • 17
    • 0036468595 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis: Recent advances in sample preparation, detection and quantitation
    • Lilley, K. S., Razzaq, A., Dupree, P., Two-dimensional gel electrophoresis: recent advances in sample preparation, detection and quantitation. Curr. Opin. Chem. Biol. 2002, 6, 46-50.
    • (2002) Curr. Opin. Chem. Biol , vol.6 , pp. 46-50
    • Lilley, K.S.1    Razzaq, A.2    Dupree, P.3
  • 18
    • 0035491770 scopus 로고    scopus 로고
    • Fluorescent dual colour 2D-protein gel electrophoresis for rapid detection of differences in protein pattern with standard image analysis software
    • Von Eggeling, F., Gawriljuk, A., Fiedler, W., Ernst, G. et al., Fluorescent dual colour 2D-protein gel electrophoresis for rapid detection of differences in protein pattern with standard image analysis software. Int. J. Mol. Med. 2001, 8, 373-377.
    • (2001) Int. J. Mol. Med , vol.8 , pp. 373-377
    • Von Eggeling, F.1    Gawriljuk, A.2    Fiedler, W.3    Ernst, G.4
  • 19
    • 0037253267 scopus 로고    scopus 로고
    • A novel experimental design for comparative two-dimensional gel analysis: Two-dimensional difference gel electrophoresis incorporating a pooled internal standard
    • Alban, A., David, S. O., Bjorkesten, L., Andersson, C. et al., A novel experimental design for comparative two-dimensional gel analysis: Two-dimensional difference gel electrophoresis incorporating a pooled internal standard. Proteomics 2003, 3, 36-44.
    • (2003) Proteomics , vol.3 , pp. 36-44
    • Alban, A.1    David, S.O.2    Bjorkesten, L.3    Andersson, C.4
  • 20
    • 0036463947 scopus 로고    scopus 로고
    • Evaluation of two-dimensional differential gel electrophoresis for proteomic expression analysis of a model breast cancer cell system
    • Gharbi, S., Gaffney, P., Yang, A., Zvelebil, M. J. et al., Evaluation of two-dimensional differential gel electrophoresis for proteomic expression analysis of a model breast cancer cell system. Mol. Cell. Proteomics 2002, 1, 91-98.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 91-98
    • Gharbi, S.1    Gaffney, P.2    Yang, A.3    Zvelebil, M.J.4
  • 21
    • 0034111635 scopus 로고    scopus 로고
    • A thousand points of light: The application of fluorescence detection technologies to two-dimensional gel electrophoresis and proteomics
    • Patton, W. F., A thousand points of light: the application of fluorescence detection technologies to two-dimensional gel electrophoresis and proteomics. Electrophoresis 2000, 21, 1123-1144.
    • (2000) Electrophoresis , vol.21 , pp. 1123-1144
    • Patton, W.F.1
  • 22
    • 0032959478 scopus 로고    scopus 로고
    • Proteomics and automation
    • Quadroni, M., James, P., Proteomics and automation. Electrophoresis 1999, 20, 664-677.
    • (1999) Electrophoresis , vol.20 , pp. 664-677
    • Quadroni, M.1    James, P.2
  • 23
    • 0035289178 scopus 로고    scopus 로고
    • Validation and development of fluorescence two-dimensional differential gel electrophoresis proteomics technology
    • Tonge, R., Shaw, J., Middleton, B., Rowlinson, R. et al., Validation and development of fluorescence two-dimensional differential gel electrophoresis proteomics technology. Proteomics 2001, 1, 377-396.
    • (2001) Proteomics , vol.1 , pp. 377-396
    • Tonge, R.1    Shaw, J.2    Middleton, B.3    Rowlinson, R.4
  • 24
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlu, M., Morgan, M. E., Minden, J. S., Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis 1997, 18, 2071-2077.
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 25
    • 0043166918 scopus 로고    scopus 로고
    • Evaluation of saturation labelling two-dimensional difference gel electrophoresis fluorescent dyes
    • Shaw, J., Rowlinson, R., Nickson, J., Stone, T. et al., Evaluation of saturation labelling two-dimensional difference gel electrophoresis fluorescent dyes. Proteomics 2003, 3, 1181-1195.
    • (2003) Proteomics , vol.3 , pp. 1181-1195
    • Shaw, J.1    Rowlinson, R.2    Nickson, J.3    Stone, T.4
  • 26
    • 18844447205 scopus 로고    scopus 로고
    • Saturation labeling with cysteine-reactive cyanine fluorescent dyes provides increased sensitivity for protein expression profiling of laser-microdissected clinical specimens
    • Greengauz-Roberts, O., Stoppler, H., Nomura, S., Yamaguchi, H. et al., Saturation labeling with cysteine-reactive cyanine fluorescent dyes provides increased sensitivity for protein expression profiling of laser-microdissected clinical specimens. Proteomics 2005, 5, 1746-1757.
    • (2005) Proteomics , vol.5 , pp. 1746-1757
    • Greengauz-Roberts, O.1    Stoppler, H.2    Nomura, S.3    Yamaguchi, H.4
  • 27
    • 23044516594 scopus 로고    scopus 로고
    • Proteomic analysis of redox- and ErbB2-dependent changes in mammary luminal epithelial cells using cysteine- and lysine-labelling two-dimensional difference gel electrophoresis
    • Chan, H. L., Gharbi, S., Gaffney, P. R., Cramer, R. et al., Proteomic analysis of redox- and ErbB2-dependent changes in mammary luminal epithelial cells using cysteine- and lysine-labelling two-dimensional difference gel electrophoresis. Proteomics 2005, 5, 2908-2926.
    • (2005) Proteomics , vol.5 , pp. 2908-2926
    • Chan, H.L.1    Gharbi, S.2    Gaffney, P.R.3    Cramer, R.4
  • 28
    • 33746084916 scopus 로고    scopus 로고
    • Serum amyloid P component as a major target of photolysis
    • Proteomic analysis of UVC irradiation-induced damage of plasma proteins
    • Chan, H. L., Gaffney, P. R., Waterfield, M. D., Anderle, H. et al., Proteomic analysis of UVC irradiation-induced damage of plasma proteins: Serum amyloid P component as a major target of photolysis. FEBS Lett. 2006, 580, 3229-3236.
    • (2006) FEBS Lett , vol.580 , pp. 3229-3236
    • Chan, H.L.1    Gaffney, P.R.2    Waterfield, M.D.3    Anderle, H.4
  • 29
    • 34547592709 scopus 로고    scopus 로고
    • Detection of reactive oxygen species-sensitive thiol proteins by redox difference gel electrophoresis: Implications for mitochondrial redox signaling
    • Hurd, T. R., Prime, T. A., Harbour, M. E., Lilley, K. S., Murphy, M. P., Detection of reactive oxygen species-sensitive thiol proteins by redox difference gel electrophoresis: implications for mitochondrial redox signaling. J. Biol. Chem. 2007, 282, 22040-22051.
    • (2007) J. Biol. Chem , vol.282 , pp. 22040-22051
    • Hurd, T.R.1    Prime, T.A.2    Harbour, M.E.3    Lilley, K.S.4    Murphy, M.P.5
  • 30
    • 0347134635 scopus 로고    scopus 로고
    • Thiol-reactive dyes for fluorescence labeling of proteomic samples
    • Tyagarajan, K., Pretzer, E., Wiktorowicz, J. E., Thiol-reactive dyes for fluorescence labeling of proteomic samples. Electrophoresis 2003, 24, 2348-2358.
    • (2003) Electrophoresis , vol.24 , pp. 2348-2358
    • Tyagarajan, K.1    Pretzer, E.2    Wiktorowicz, J.E.3
  • 31
    • 0034931861 scopus 로고    scopus 로고
    • Protein alkylation in the presence/absence of thiourea in proteome analysis: A matrix assisted laser desorption/ionization-time of flight-mass spectrometry investigation
    • Galvani, M., Rovatti, L., Hamdan, M., Herbert, B., Righetti, P. G., Protein alkylation in the presence/absence of thiourea in proteome analysis: a matrix assisted laser desorption/ionization-time of flight-mass spectrometry investigation. Electrophoresis 2001, 22, 2066-2074.
    • (2001) Electrophoresis , vol.22 , pp. 2066-2074
    • Galvani, M.1    Rovatti, L.2    Hamdan, M.3    Herbert, B.4    Righetti, P.G.5
  • 32
    • 17844407935 scopus 로고    scopus 로고
    • Stress-induced changes in the Schizosaccharomyces pombe proteome using two-dimensional difference gel electrophoresis, mass spectrometry and a novel integrated robotics platform
    • Weeks, M. E., Sinclair, J., Jacob, R. J., Saxton, M. J. et al., Stress-induced changes in the Schizosaccharomyces pombe proteome using two-dimensional difference gel electrophoresis, mass spectrometry and a novel integrated robotics platform. Proteomics 2005, 5, 1669-1685.
    • (2005) Proteomics , vol.5 , pp. 1669-1685
    • Weeks, M.E.1    Sinclair, J.2    Jacob, R.J.3    Saxton, M.J.4
  • 33
    • 37049039722 scopus 로고    scopus 로고
    • Analysis of DIGE data using a linear mixed model allowing for protein-specific dye effects
    • Krogh, M., Liu, Y., Waldemarson, S., Valastro, B., James, P., Analysis of DIGE data using a linear mixed model allowing for protein-specific dye effects. Proteomics 2007, 7, 4235-4244.
    • (2007) Proteomics , vol.7 , pp. 4235-4244
    • Krogh, M.1    Liu, Y.2    Waldemarson, S.3    Valastro, B.4    James, P.5
  • 34
    • 4544270574 scopus 로고    scopus 로고
    • DNA microarray normalization methods can remove bias from differential protein expression analysis of 2D difference gel electrophoresis results
    • Kreil, D. P., Karp, N. A., Lilley, K. S., DNA microarray normalization methods can remove bias from differential protein expression analysis of 2D difference gel electrophoresis results. Bioinformatics 2004, 20, 2026-2034.
    • (2004) Bioinformatics , vol.20 , pp. 2026-2034
    • Kreil, D.P.1    Karp, N.A.2    Lilley, K.S.3
  • 35
    • 2442453377 scopus 로고    scopus 로고
    • Determining a significant change in protein expression with DeCyder during a pair-wise comparison using two-dimensional difference gel electrophoresis
    • Karp, N. A., Kreil, D. P., Lilley, K. S., Determining a significant change in protein expression with DeCyder during a pair-wise comparison using two-dimensional difference gel electrophoresis. Proteomics 2004, 4, 1421-1432.
    • (2004) Proteomics , vol.4 , pp. 1421-1432
    • Karp, N.A.1    Kreil, D.P.2    Lilley, K.S.3
  • 36
    • 23844491490 scopus 로고    scopus 로고
    • Maximising sensitivity for detecting changes in protein expression: Experimental design using minimal CyDyes
    • Karp, N. A., Lilley, K. S., Maximising sensitivity for detecting changes in protein expression: experimental design using minimal CyDyes. Proteomics 2005, 5, 3105-3115.
    • (2005) Proteomics , vol.5 , pp. 3105-3115
    • Karp, N.A.1    Lilley, K.S.2
  • 37
    • 34548409217 scopus 로고    scopus 로고
    • Experimental and statistical considerations to avoid false conclusions in proteomics studies using differential in-gel electrophoresis
    • Karp, N. A., McCormick, P. S., Russell, M. R., Lilley, K. S., Experimental and statistical considerations to avoid false conclusions in proteomics studies using differential in-gel electrophoresis. Mol. Cell. Proteomics 2007, 6, 1354-1364.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1354-1364
    • Karp, N.A.1    McCormick, P.S.2    Russell, M.R.3    Lilley, K.S.4
  • 38
    • 13244258397 scopus 로고    scopus 로고
    • Application of partial least squares discriminant analysis to two-dimensional difference gel studies in expression proteomics
    • Karp, N. A., Griffin, J. L., Lilley, K. S., Application of partial least squares discriminant analysis to two-dimensional difference gel studies in expression proteomics. Proteomics 2005, 5, 81-90.
    • (2005) Proteomics , vol.5 , pp. 81-90
    • Karp, N.A.1    Griffin, J.L.2    Lilley, K.S.3
  • 39
    • 1542720668 scopus 로고    scopus 로고
    • Mechanisms of hydrazine toxicity in rat liver investigated by proteomics and multivariate data analysis
    • Kleno, T. G., Leonardsen, L. R., Kjeldal, H. O., Laursen, S. M. et al., Mechanisms of hydrazine toxicity in rat liver investigated by proteomics and multivariate data analysis. Proteomics 2004, 4, 868-880.
    • (2004) Proteomics , vol.4 , pp. 868-880
    • Kleno, T.G.1    Leonardsen, L.R.2    Kjeldal, H.O.3    Laursen, S.M.4
  • 40
    • 17444386712 scopus 로고    scopus 로고
    • Data analysis methods for detection of differential protein expression in two-dimensional gel electrophoresis
    • Meunier, B., Bouley, J., Piec, I., Bernard, C. et al., Data analysis methods for detection of differential protein expression in two-dimensional gel electrophoresis. Anal. Biochem. 2005, 340, 226-230.
    • (2005) Anal. Biochem , vol.340 , pp. 226-230
    • Meunier, B.1    Bouley, J.2    Piec, I.3    Bernard, C.4
  • 41
    • 34548428842 scopus 로고    scopus 로고
    • Turck, C. W., Falick, A. M., Kowalak, J. A., Lane, W. S. et al., The Association of Biomolecular Resource Facilities Proteomics Research Group 2006 study: relative protein quantitation. Mol. Cell. Proteomics 2007, 6, 1291-1298.
    • Turck, C. W., Falick, A. M., Kowalak, J. A., Lane, W. S. et al., The Association of Biomolecular Resource Facilities Proteomics Research Group 2006 study: relative protein quantitation. Mol. Cell. Proteomics 2007, 6, 1291-1298.
  • 42
    • 33644845960 scopus 로고    scopus 로고
    • Comparative study of three proteomic quantitative methods, DIGE, cICAT, and iTRAQ, using 2D gel- or LC-MALDI TOF/TOF
    • Wu, W. W., Wang, G., Baek, S. J., Shen, R. F., Comparative study of three proteomic quantitative methods, DIGE, cICAT, and iTRAQ, using 2D gel- or LC-MALDI TOF/TOF. J. Proteome Res. 2006, 5, 651-658.
    • (2006) J. Proteome Res , vol.5 , pp. 651-658
    • Wu, W.W.1    Wang, G.2    Baek, S.J.3    Shen, R.F.4
  • 43
    • 15944422816 scopus 로고    scopus 로고
    • Double standards in quantitative proteomics: Direct comparative assessment of difference in gel electrophoresis and metabolic stable isotope labeling
    • Kolkman, A., Dirksen, E. H., Slijper, M., Heck, A. J., Double standards in quantitative proteomics: direct comparative assessment of difference in gel electrophoresis and metabolic stable isotope labeling. Mol. Cell. Proteomics 2005, 4, 255-266.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 255-266
    • Kolkman, A.1    Dirksen, E.H.2    Slijper, M.3    Heck, A.J.4
  • 44
    • 43849099076 scopus 로고    scopus 로고
    • Relative protein quantification by isobaric SILAC with immonium ion splitting (ISIS)
    • Colzani, M., Schutz, F., Potts, A., Waridel, P., Quadroni, M., Relative protein quantification by isobaric SILAC with immonium ion splitting (ISIS). Mol. Cell. Proteomics 2008, 7, 927-937.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 927-937
    • Colzani, M.1    Schutz, F.2    Potts, A.3    Waridel, P.4    Quadroni, M.5
  • 45
    • 39049154321 scopus 로고    scopus 로고
    • Study of early leaf senescence in Arabidopsis thaliana by quantitative proteomics using reciprocal 14N/15N labeling and difference gel electrophoresis
    • Hebeler, R., Oeljeklaus, S., Reidegeld, K. A., Eisenacher, M. et al., Study of early leaf senescence in Arabidopsis thaliana by quantitative proteomics using reciprocal 14N/15N labeling and difference gel electrophoresis. Mol. Cell. Proteomics 2008, 7, 108-120.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 108-120
    • Hebeler, R.1    Oeljeklaus, S.2    Reidegeld, K.A.3    Eisenacher, M.4
  • 46
    • 45649083365 scopus 로고    scopus 로고
    • Hydroponic isotope labelling of entire plants (HILEP) for quantitative plant proteomics
    • Bindschedler, L. V., Palmblad, M., Cramer, R., Hydroponic isotope labelling of entire plants (HILEP) for quantitative plant proteomics. Phytochemistry 2008, 69, 1962-1972.
    • (2008) Phytochemistry , vol.69 , pp. 1962-1972
    • Bindschedler, L.V.1    Palmblad, M.2    Cramer, R.3
  • 47
    • 39749164419 scopus 로고    scopus 로고
    • Chakravarti, B., Gallagher, S. R., Chakravarti, D. N., Difference gel electrophoresis (DIGE) using CyDye DIGE fluor minimal dyes. Curr. Protoc. Mol. Biol. 2005, Chapter 10, Unit 10 23.
    • Chakravarti, B., Gallagher, S. R., Chakravarti, D. N., Difference gel electrophoresis (DIGE) using CyDye DIGE fluor minimal dyes. Curr. Protoc. Mol. Biol. 2005, Chapter 10, Unit 10 23.
  • 48
    • 39449112983 scopus 로고    scopus 로고
    • Microscale solution IEF combined with 2-D DIGE substantially enhances analysis depth of complex proteomes such as mammalian cell and tissue extracts
    • Han, M. J., Herlyn, M., Fisher, A. B., Speicher, D. W., Microscale solution IEF combined with 2-D DIGE substantially enhances analysis depth of complex proteomes such as mammalian cell and tissue extracts. Electrophoresis 2008, 29, 695-705.
    • (2008) Electrophoresis , vol.29 , pp. 695-705
    • Han, M.J.1    Herlyn, M.2    Fisher, A.B.3    Speicher, D.W.4
  • 49
    • 42649116833 scopus 로고    scopus 로고
    • Proteomic studies of brassinosteroid signal transduction using prefractionation and 2-D DIGE
    • Tang, W., Deng, Z., Oses-Prieto, J. A., Suzuki, N. et al., Proteomic studies of brassinosteroid signal transduction using prefractionation and 2-D DIGE. Mol. Cell. Proteomics 2008, 7, 728-738.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 728-738
    • Tang, W.1    Deng, Z.2    Oses-Prieto, J.A.3    Suzuki, N.4
  • 50
    • 57649170599 scopus 로고    scopus 로고
    • Differential protein expression analysis using two-dimensional difference gel electrophoresis
    • 2nd Edition, Wiley-VCH
    • Timms, J. F., Differential protein expression analysis using two-dimensional difference gel electrophoresis. In: Encyclopedia of Molecular Cell Biology and Molecular Medicine, 2nd Edition, Wiley-VCH 2004, 5, 33-51.
    • (2004) Encyclopedia of Molecular Cell Biology and Molecular Medicine , vol.5 , pp. 33-51
    • Timms, J.F.1
  • 51
    • 34247627759 scopus 로고    scopus 로고
    • Two-dimensional fluorescence difference gel electrophoresis for comparative proteomics profiling
    • Tannu, N. S., Hemby, S. E., Two-dimensional fluorescence difference gel electrophoresis for comparative proteomics profiling. Nat. Protoc. 2006, 1, 1732-1742.
    • (2006) Nat. Protoc , vol.1 , pp. 1732-1742
    • Tannu, N.S.1    Hemby, S.E.2
  • 52
    • 34147161968 scopus 로고    scopus 로고
    • Application of highly sensitive fluorescent dyes (CyDye DIGE Fluor saturation dyes) to laser microdissection and two-dimensional difference gel electrophoresis (2D-DIGE) for cancer proteomics
    • Kondo, T., Hirohashi, S., Application of highly sensitive fluorescent dyes (CyDye DIGE Fluor saturation dyes) to laser microdissection and two-dimensional difference gel electrophoresis (2D-DIGE) for cancer proteomics. Nat. Protoc. 2006, 1, 2940-2956.
    • (2006) Nat. Protoc , vol.1 , pp. 2940-2956
    • Kondo, T.1    Hirohashi, S.2
  • 53
    • 15944413138 scopus 로고    scopus 로고
    • Identification of dynamic proteome changes upon ligand activation of Trk-receptors using two-dimensional fluorescence difference gel electrophoresis and mass spectrometry
    • Sitek, B., Apostolov, O., Stuhler, K., Pfeiffer, K. et al., Identification of dynamic proteome changes upon ligand activation of Trk-receptors using two-dimensional fluorescence difference gel electrophoresis and mass spectrometry. Mol. Cell. Proteomics 2005, 4, 291-299.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 291-299
    • Sitek, B.1    Apostolov, O.2    Stuhler, K.3    Pfeiffer, K.4
  • 54
    • 34248335169 scopus 로고    scopus 로고
    • Proteomic analysis of p38alpha mitogen-activated protein kinase-regulated changes in membrane fractions of RAS-transformed fibroblasts
    • Alfonso, P., Dolado, I., Swat, A., Nunez, A. et al., Proteomic analysis of p38alpha mitogen-activated protein kinase-regulated changes in membrane fractions of RAS-transformed fibroblasts. Proteomics 2006, 6 Suppl 1, S262-S271.
    • (2006) Proteomics , vol.6 , Issue.SUPPL. 1
    • Alfonso, P.1    Dolado, I.2    Swat, A.3    Nunez, A.4
  • 55
    • 33646743554 scopus 로고    scopus 로고
    • A parallel proteomic and metabolomic analysis of the hydrogen peroxide- and Sty1p-dependent stress response in Schizosaccharomyces pombe
    • Weeks, M. E., Sinclair, J., Butt, A., Chung, Y. L. et al., A parallel proteomic and metabolomic analysis of the hydrogen peroxide- and Sty1p-dependent stress response in Schizosaccharomyces pombe. Proteomics 2006, 6, 2772-2796.
    • (2006) Proteomics , vol.6 , pp. 2772-2796
    • Weeks, M.E.1    Sinclair, J.2    Butt, A.3    Chung, Y.L.4
  • 56
    • 34447263077 scopus 로고    scopus 로고
    • Analysis of Ras-induced oncogenic transformation of NIH-3T3 cells using differential-display 2-DE proteomics
    • Ji, H., Moritz, R. L., Kim, Y. S., Zhu, H. J., Simpson, R. J., Analysis of Ras-induced oncogenic transformation of NIH-3T3 cells using differential-display 2-DE proteomics. Electrophoresis 2007, 28, 1997-2008.
    • (2007) Electrophoresis , vol.28 , pp. 1997-2008
    • Ji, H.1    Moritz, R.L.2    Kim, Y.S.3    Zhu, H.J.4    Simpson, R.J.5
  • 57
    • 33846609097 scopus 로고    scopus 로고
    • 2-D DIGE analysis of liver and red blood cells provides further evidence for oxidative stress in schizophrenia
    • Prabakaran, S., Wengenroth, M., Lockstone, H. E., Lilley, K. et al., 2-D DIGE analysis of liver and red blood cells provides further evidence for oxidative stress in schizophrenia. J. Proteome Res. 2007, 6, 141-149.
    • (2007) J. Proteome Res , vol.6 , pp. 141-149
    • Prabakaran, S.1    Wengenroth, M.2    Lockstone, H.E.3    Lilley, K.4
  • 58
    • 34249706373 scopus 로고    scopus 로고
    • Identification of endosomal epidermal growth factor receptor signaling targets by functional organelle proteomics
    • Stasyk, T., Schiefermeier, N., Skvortsov, S., Zwierzina, H. et al., Identification of endosomal epidermal growth factor receptor signaling targets by functional organelle proteomics. Mol. Cell. Proteomics 2007, 6, 908-922.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 908-922
    • Stasyk, T.1    Schiefermeier, N.2    Skvortsov, S.3    Zwierzina, H.4
  • 59
    • 1242285130 scopus 로고    scopus 로고
    • Drosophila ventral furrow morphogenesis: A proteomic analysis
    • Gong, L., Puri, M., Unlu, M., Young, M. et al., Drosophila ventral furrow morphogenesis: a proteomic analysis. Development 2004, 131, 643-656.
    • (2004) Development , vol.131 , pp. 643-656
    • Gong, L.1    Puri, M.2    Unlu, M.3    Young, M.4
  • 60
    • 43849087678 scopus 로고    scopus 로고
    • Analysis of the zebrafish proteome during embryonic development
    • Lucitt, M. B., Price, T. S., Pizarro, A., Wu, W. et al., Analysis of the zebrafish proteome during embryonic development. Mol. Cell. Proteomics 2008, 7, 981-994.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 981-994
    • Lucitt, M.B.1    Price, T.S.2    Pizarro, A.3    Wu, W.4
  • 61
    • 0347134696 scopus 로고    scopus 로고
    • Reversed-phase high-performance liquid chromatography prefractionation prior to two-dimensional difference gel electrophoresis and mass spectrometry identifies new differentially expressed proteins between striate cortex of kitten and adult cat
    • Van den Bergh, G., Clerens, S., Vandesande, F., Arckens, L., Reversed-phase high-performance liquid chromatography prefractionation prior to two-dimensional difference gel electrophoresis and mass spectrometry identifies new differentially expressed proteins between striate cortex of kitten and adult cat. Electrophoresis 2003, 24, 1471-1481.
    • (2003) Electrophoresis , vol.24 , pp. 1471-1481
    • Van den Bergh, G.1    Clerens, S.2    Vandesande, F.3    Arckens, L.4
  • 62
    • 31044449729 scopus 로고    scopus 로고
    • Proteomic profiling and neurodegeneration in west-nile-virus-infected neurons
    • Dhingra, V., Li, Q., Allison, A. B., Stallknecht, D. E., Fu, Z. F., Proteomic profiling and neurodegeneration in west-nile-virus-infected neurons. J. Biomed. Biotechnol. 2005, 2005, 271-279.
    • (2005) J. Biomed. Biotechnol , vol.2005 , pp. 271-279
    • Dhingra, V.1    Li, Q.2    Allison, A.B.3    Stallknecht, D.E.4    Fu, Z.F.5
  • 63
    • 33749246403 scopus 로고    scopus 로고
    • 2-D DIGE as a quantitative tool for investigating the HUPO Brain Proteome Project mouse series
    • Focking, M., Boersema, P. J., O'Donoghue, N., Lubec, G. et al., 2-D DIGE as a quantitative tool for investigating the HUPO Brain Proteome Project mouse series. Proteomics 2006, 6, 4914-4931.
    • (2006) Proteomics , vol.6 , pp. 4914-4931
    • Focking, M.1    Boersema, P.J.2    O'Donoghue, N.3    Lubec, G.4
  • 64
    • 33749249918 scopus 로고    scopus 로고
    • Analysis of the HUPO Brain Proteome reference samples using 2-D DIGE and 2-D LC-MS/MS
    • Frohlich, T., Helmstetter, D., Zobawa, M., Crecelius, A. C. et al., Analysis of the HUPO Brain Proteome reference samples using 2-D DIGE and 2-D LC-MS/MS. Proteomics 2006, 6, 4950-4966.
    • (2006) Proteomics , vol.6 , pp. 4950-4966
    • Frohlich, T.1    Helmstetter, D.2    Zobawa, M.3    Crecelius, A.C.4
  • 65
    • 32944461534 scopus 로고    scopus 로고
    • Detection of phosphorylation patterns in rat cortical neurons by combining phosphatase treatment and DIGE technology
    • Raggiaschi, R., Lorenzetto, C., Diodato, E., Caricasole, A. et al., Detection of phosphorylation patterns in rat cortical neurons by combining phosphatase treatment and DIGE technology. Proteomics 2006, 6, 748-756.
    • (2006) Proteomics , vol.6 , pp. 748-756
    • Raggiaschi, R.1    Lorenzetto, C.2    Diodato, E.3    Caricasole, A.4
  • 66
    • 56449084674 scopus 로고    scopus 로고
    • Independent protein-profiling studies show a decrease in apolipoprotein A1 levels in schizophrenia CSF, brain and peripheral tissues
    • in press
    • Huang, J. T., Wang, L., Prabakaran, S., Wengenroth, M. et al., Independent protein-profiling studies show a decrease in apolipoprotein A1 levels in schizophrenia CSF, brain and peripheral tissues. Mol. Psychiatry 2007, in press.
    • (2007) Mol. Psychiatry
    • Huang, J.T.1    Wang, L.2    Prabakaran, S.3    Wengenroth, M.4
  • 67
    • 41149176492 scopus 로고    scopus 로고
    • Sequential detergent fractionation of primary neurons for proteomics studies
    • Bernocco, S., Fondelli, C., Matteoni, S., Magnoni, L. et al., Sequential detergent fractionation of primary neurons for proteomics studies. Proteomics 2008, 8, 930-938.
    • (2008) Proteomics , vol.8 , pp. 930-938
    • Bernocco, S.1    Fondelli, C.2    Matteoni, S.3    Magnoni, L.4
  • 68
    • 22044440445 scopus 로고    scopus 로고
    • Two-dimensional fluorescence difference gel electrophoresis analysis of the urine proteome in human diabetic nephropathy
    • Sharma, K., Lee, S., Han, S., Francos, B. et al., Two-dimensional fluorescence difference gel electrophoresis analysis of the urine proteome in human diabetic nephropathy. Proteomics 2005, 5, 2648-2655.
    • (2005) Proteomics , vol.5 , pp. 2648-2655
    • Sharma, K.1    Lee, S.2    Han, S.3    Francos, B.4
  • 69
    • 33746537718 scopus 로고    scopus 로고
    • Biomarker and drug-target discovery using proteomics in a new rat model of sepsis-induced acute renal failure
    • Holly, M. K., Dear, J. W., Hu, X., Schechter, A. N. et al., Biomarker and drug-target discovery using proteomics in a new rat model of sepsis-induced acute renal failure. Kidney Int. 2006, 70, 496-506.
    • (2006) Kidney Int , vol.70 , pp. 496-506
    • Holly, M.K.1    Dear, J.W.2    Hu, X.3    Schechter, A.N.4
  • 70
    • 33747252210 scopus 로고    scopus 로고
    • The application of DIGE-based proteomics to renal physiology
    • Hoorn, E. J., Hoffert, J. D., Knepper, M. A., The application of DIGE-based proteomics to renal physiology. Nephron. Physiol. 2006, 104, 61-72.
    • (2006) Nephron. Physiol , vol.104 , pp. 61-72
    • Hoorn, E.J.1    Hoffert, J.D.2    Knepper, M.A.3
  • 71
    • 33747792789 scopus 로고    scopus 로고
    • Novel approaches to analyse glomerular proteins from smallest scale murine and human samples using DIGE saturation labelling
    • Sitek, B., Potthoff, S., Schulenborg, T., Stegbauer, J. et al., Novel approaches to analyse glomerular proteins from smallest scale murine and human samples using DIGE saturation labelling. Proteomics 2006, 6, 4337-4345.
    • (2006) Proteomics , vol.6 , pp. 4337-4345
    • Sitek, B.1    Potthoff, S.2    Schulenborg, T.3    Stegbauer, J.4
  • 72
    • 33846248808 scopus 로고    scopus 로고
    • Proteomic analysis of the adaptive response of rat renal proximal tubules to metabolic acidosis
    • Curthoys, N. P., Taylor, L., Hoffert, J. D., Knepper, M. A., Proteomic analysis of the adaptive response of rat renal proximal tubules to metabolic acidosis. Am. J. Physiol. Renal. Physiol. 2007, 292, F140-147.
    • (2007) Am. J. Physiol. Renal. Physiol , vol.292
    • Curthoys, N.P.1    Taylor, L.2    Hoffert, J.D.3    Knepper, M.A.4
  • 73
    • 33847691204 scopus 로고    scopus 로고
    • Proteomic identification of urinary biomarkers of diabetic nephropathy
    • Rao, P. V., Lu, X., Standley, M., Pattee, P. et al., Proteomic identification of urinary biomarkers of diabetic nephropathy. Diabetes Care 2007, 30, 629-637.
    • (2007) Diabetes Care , vol.30 , pp. 629-637
    • Rao, P.V.1    Lu, X.2    Standley, M.3    Pattee, P.4
  • 74
    • 33947367874 scopus 로고    scopus 로고
    • A proteomic investigation of glomerular podocytes from a Denys-Drash syndrome patient with a mutation in the Wilms tumour suppressor gene WT1
    • Viney, R. L., Morrison, A. A., van den Heuvel, L. P., Ni, L. et al., A proteomic investigation of glomerular podocytes from a Denys-Drash syndrome patient with a mutation in the Wilms tumour suppressor gene WT1. Proteomics 2007, 7, 804-815.
    • (2007) Proteomics , vol.7 , pp. 804-815
    • Viney, R.L.1    Morrison, A.A.2    van den Heuvel, L.P.3    Ni, L.4
  • 75
    • 33646263838 scopus 로고    scopus 로고
    • Proteome analysis of cold stress response in Arabidopsis thaliana using DIGE-technology
    • Amme, S., Matros, A., Schlesier, B., Mock, H. P., Proteome analysis of cold stress response in Arabidopsis thaliana using DIGE-technology. J. Exp. Bot. 2006, 57, 1537-1546.
    • (2006) J. Exp. Bot , vol.57 , pp. 1537-1546
    • Amme, S.1    Matros, A.2    Schlesier, B.3    Mock, H.P.4
  • 76
    • 33846474477 scopus 로고    scopus 로고
    • Proteomic analysis of quorum sensing in Rhizobium leguminosarum biovar viciae UPM791
    • Cantero, L., Palacios, J. M., Ruiz-Argueso, T., Imperial, J., Proteomic analysis of quorum sensing in Rhizobium leguminosarum biovar viciae UPM791. Proteomics 2006, 6 Suppl 1, S97-S106.
    • (2006) Proteomics , vol.6 , Issue.SUPPL. 1
    • Cantero, L.1    Palacios, J.M.2    Ruiz-Argueso, T.3    Imperial, J.4
  • 77
    • 33645065565 scopus 로고    scopus 로고
    • Down-regulation of the strawberry Bet v 1-homologous allergen in concert with the flavonoid biosynthesis pathway in colorless strawberry mutant
    • Hjerno, K., Alm, R., Canback, B., Matthiesen, R. et al., Down-regulation of the strawberry Bet v 1-homologous allergen in concert with the flavonoid biosynthesis pathway in colorless strawberry mutant. Proteomics 2006, 6, 1574-1587.
    • (2006) Proteomics , vol.6 , pp. 1574-1587
    • Hjerno, K.1    Alm, R.2    Canback, B.3    Matthiesen, R.4
  • 78
    • 32344434974 scopus 로고    scopus 로고
    • Comparison of two proteomics techniques used to identify proteins regulated by gibberellin in rice
    • Komatsu, S., Zang, X., Tanaka, N., Comparison of two proteomics techniques used to identify proteins regulated by gibberellin in rice. J. Proteome Res. 2006, 5, 270-276.
    • (2006) J. Proteome Res , vol.5 , pp. 270-276
    • Komatsu, S.1    Zang, X.2    Tanaka, N.3
  • 79
    • 34548162709 scopus 로고    scopus 로고
    • Proteomic variation is as large within as between strawberry varieties
    • Alm, R., Ekefjard, A., Krogh, M., Hakkinen, J., Emanuelsson, C., Proteomic variation is as large within as between strawberry varieties. J. Proteome Res. 2007, 6, 3011-3020.
    • (2007) J. Proteome Res , vol.6 , pp. 3011-3020
    • Alm, R.1    Ekefjard, A.2    Krogh, M.3    Hakkinen, J.4    Emanuelsson, C.5
  • 80
    • 34249725560 scopus 로고    scopus 로고
    • A DIGE analysis of developing poplar leaves subjected to ozone reveals major changes in carbon metabolism
    • Bohler, S., Bagard, M., Oufir, M., Planchon, S. et al., A DIGE analysis of developing poplar leaves subjected to ozone reveals major changes in carbon metabolism. Proteomics 2007, 7, 1584-1599.
    • (2007) Proteomics , vol.7 , pp. 1584-1599
    • Bohler, S.1    Bagard, M.2    Oufir, M.3    Planchon, S.4
  • 81
    • 38349052346 scopus 로고    scopus 로고
    • A proteomics study of brassinosteroid response in Arabidopsis
    • Deng, Z., Zhang, X., Tang, W., Oses-Prieto, J. A. et al., A proteomics study of brassinosteroid response in Arabidopsis. Mol. Cell. Proteomics 2007, 6, 2058-2071.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 2058-2071
    • Deng, Z.1    Zhang, X.2    Tang, W.3    Oses-Prieto, J.A.4
  • 82
    • 37848999134 scopus 로고    scopus 로고
    • Two-dimensional differential in-gel electrophoresis (DIGE) of leaf and roots of Lycopersicon esculentum
    • Keeler, M., Letarte, J., Hattrup, E., Hickman, F., Haynes, P. A., Two-dimensional differential in-gel electrophoresis (DIGE) of leaf and roots of Lycopersicon esculentum. Methods Mol. Biol. 2007, 355, 157-174.
    • (2007) Methods Mol. Biol , vol.355 , pp. 157-174
    • Keeler, M.1    Letarte, J.2    Hattrup, E.3    Hickman, F.4    Haynes, P.A.5
  • 83
    • 34248642605 scopus 로고    scopus 로고
    • Differential proteomic analysis of the endoplasmic reticulum from developing and germinating seeds of castor (Ricinus communis) identifies seed protein precursors as significant components of the endoplasmic reticulum
    • Maltman, D. J., Gadd, S. M., Simon, W. J., Slabas, A. R., Differential proteomic analysis of the endoplasmic reticulum from developing and germinating seeds of castor (Ricinus communis) identifies seed protein precursors as significant components of the endoplasmic reticulum. Proteomics 2007, 7, 1513-1528.
    • (2007) Proteomics , vol.7 , pp. 1513-1528
    • Maltman, D.J.1    Gadd, S.M.2    Simon, W.J.3    Slabas, A.R.4
  • 84
    • 0036463563 scopus 로고    scopus 로고
    • 2D differential in-gel electrophoresis for the identification of esophageal scans cell cancer-specific protein markers
    • Zhou, G., Li, H., DeCamp, D., Chen, S. et al., 2D differential in-gel electrophoresis for the identification of esophageal scans cell cancer-specific protein markers. Mol. Cell. Proteomics 2002, 1, 117-124.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 117-124
    • Zhou, G.1    Li, H.2    DeCamp, D.3    Chen, S.4
  • 85
    • 1542406246 scopus 로고    scopus 로고
    • Proteome analysis of human colon cancer by two-dimensional difference gel electrophoresis and mass spectrometry
    • Friedman, D. B., Hill, S., Keller, J. W., Merchant, N. B. et al., Proteome analysis of human colon cancer by two-dimensional difference gel electrophoresis and mass spectrometry. Proteomics 2004, 4, 793-811.
    • (2004) Proteomics , vol.4 , pp. 793-811
    • Friedman, D.B.1    Hill, S.2    Keller, J.W.3    Merchant, N.B.4
  • 86
    • 22044449347 scopus 로고    scopus 로고
    • Proteomic expression analysis of colorectal cancer by two-dimensional differential gel electrophoresis
    • Alfonso, P., Nunez, A., Madoz-Gurpide, J., Lombardia, L. et al., Proteomic expression analysis of colorectal cancer by two-dimensional differential gel electrophoresis. Proteomics 2005, 5, 2602-2611.
    • (2005) Proteomics , vol.5 , pp. 2602-2611
    • Alfonso, P.1    Nunez, A.2    Madoz-Gurpide, J.3    Lombardia, L.4
  • 87
    • 29144525537 scopus 로고    scopus 로고
    • Identification of human hepatocellular carcinoma-related biomarkers by two-dimensional difference gel electrophoresis and mass spectrometry
    • Lee, I. N., Chen, C. H., Sheu, J. C., Lee, H. S. et al., Identification of human hepatocellular carcinoma-related biomarkers by two-dimensional difference gel electrophoresis and mass spectrometry. J. Proteome Res. 2005, 4, 2062-2069.
    • (2005) J. Proteome Res , vol.4 , pp. 2062-2069
    • Lee, I.N.1    Chen, C.H.2    Sheu, J.C.3    Lee, H.S.4
  • 88
    • 23044457353 scopus 로고    scopus 로고
    • Proteomic signatures for histological types of lung cancer
    • Seike, M., Kondo, T., Fujii, K., Okano, T. et al., Proteomic signatures for histological types of lung cancer. Proteomics 2005, 5, 2939-2948.
    • (2005) Proteomics , vol.5 , pp. 2939-2948
    • Seike, M.1    Kondo, T.2    Fujii, K.3    Okano, T.4
  • 89
    • 26844512938 scopus 로고    scopus 로고
    • Characterization of proteins in human pancreatic cancer serum using differential gel electrophoresis and tandem mass spectrometry
    • Yu, K. H., Rustgi, A. K., Blair, I. A., Characterization of proteins in human pancreatic cancer serum using differential gel electrophoresis and tandem mass spectrometry. J. Proteome Res. 2005, 4, 1742-1751.
    • (2005) J. Proteome Res , vol.4 , pp. 1742-1751
    • Yu, K.H.1    Rustgi, A.K.2    Blair, I.A.3
  • 90
    • 33745623631 scopus 로고    scopus 로고
    • Proteomic analysis of colorectal cancer reveals alterations in metabolic pathways: Mechanism of tumorigenesis
    • Bi, X., Lin, Q., Foo, T. W., Joshi, S. et al., Proteomic analysis of colorectal cancer reveals alterations in metabolic pathways: mechanism of tumorigenesis. Mol. Cell. Proteomics 2006, 5, 1119-1130.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1119-1130
    • Bi, X.1    Lin, Q.2    Foo, T.W.3    Joshi, S.4
  • 91
    • 33747011106 scopus 로고    scopus 로고
    • Quantitative and qualitative differences in protein expression between papillary thyroid carcinoma and normal thyroid tissue
    • Brown, L. M., Helmke, S. M., Hunsucker, S. W., Netea-Maier, R. T. et al., Quantitative and qualitative differences in protein expression between papillary thyroid carcinoma and normal thyroid tissue. Mol. Carcinog. 2006, 45, 613-626.
    • (2006) Mol. Carcinog , vol.45 , pp. 613-626
    • Brown, L.M.1    Helmke, S.M.2    Hunsucker, S.W.3    Netea-Maier, R.T.4
  • 92
    • 33646250180 scopus 로고    scopus 로고
    • Biomarker discovery in breast cancer serum using 2-D differential gel electrophoresis/ MALDI-TOF/TOF and data validation by routine clinical assays
    • Huang, H. L., Stasyk, T., Morandell, S., Dieplinger, H. et al., Biomarker discovery in breast cancer serum using 2-D differential gel electrophoresis/ MALDI-TOF/TOF and data validation by routine clinical assays. Electrophoresis 2006, 27, 1641-1650.
    • (2006) Electrophoresis , vol.27 , pp. 1641-1650
    • Huang, H.L.1    Stasyk, T.2    Morandell, S.3    Dieplinger, H.4
  • 93
    • 33751402104 scopus 로고    scopus 로고
    • Protein pattern difference in the colon cancer cell lines examined by two-dimensional differential in-gel electrophoresis and mass spectrometry
    • Katayama, M., Nakano, H., Ishiuchi, A., Wu, W. et al., Protein pattern difference in the colon cancer cell lines examined by two-dimensional differential in-gel electrophoresis and mass spectrometry. Surg. Today 2006, 36, 1085-1093.
    • (2006) Surg. Today , vol.36 , pp. 1085-1093
    • Katayama, M.1    Nakano, H.2    Ishiuchi, A.3    Wu, W.4
  • 94
    • 33751090322 scopus 로고    scopus 로고
    • Proteomic search for potential diagnostic markers and therapeutic targets for ovarian clear cell adenocarcinoma
    • Morita, A., Miyagi, E., Yasumitsu, H., Kawasaki, H. et al., Proteomic search for potential diagnostic markers and therapeutic targets for ovarian clear cell adenocarcinoma. Proteomics 2006, 6, 5880-5890.
    • (2006) Proteomics , vol.6 , pp. 5880-5890
    • Morita, A.1    Miyagi, E.2    Yasumitsu, H.3    Kawasaki, H.4
  • 95
    • 30444435729 scopus 로고    scopus 로고
    • Protein expression profiling identifies maspin and stathmin as potential biomarkers of adenoid cystic carcinoma of the salivary glands
    • Nakashima, D., Uzawa, K., Kasamatsu, A., Koike, H. et al., Protein expression profiling identifies maspin and stathmin as potential biomarkers of adenoid cystic carcinoma of the salivary glands. Int. J. Cancer 2006, 118, 704-713.
    • (2006) Int. J. Cancer , vol.118 , pp. 704-713
    • Nakashima, D.1    Uzawa, K.2    Kasamatsu, A.3    Koike, H.4
  • 96
    • 33846012211 scopus 로고    scopus 로고
    • Proteomic analysis of isolated membrane fractions from super-invasive cancer cells
    • Dowling, P., Meleady, P., Dowd, A., Henry, M. et al., Proteomic analysis of isolated membrane fractions from super-invasive cancer cells. Biochim. Biophys. Acta 2007, 1774, 93-101.
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 93-101
    • Dowling, P.1    Meleady, P.2    Dowd, A.3    Henry, M.4
  • 97
    • 37149043429 scopus 로고    scopus 로고
    • 2-D difference gel electrophoresis of the lung squamous cell carcinoma versus normal sera demonstrates consistent alterations in the levels of ten specific proteins
    • Dowling, P., O'Driscoll, L., Meleady, P., Henry, M. et al., 2-D difference gel electrophoresis of the lung squamous cell carcinoma versus normal sera demonstrates consistent alterations in the levels of ten specific proteins. Electrophoresis 2007, 28, 4302-4310.
    • (2007) Electrophoresis , vol.28 , pp. 4302-4310
    • Dowling, P.1    O'Driscoll, L.2    Meleady, P.3    Henry, M.4
  • 98
    • 36049038546 scopus 로고    scopus 로고
    • Hoagland, L. F. t., Campa, M. J., Gottlin, E. B., Herndon, J. E., 2nd, Patz, E. F., Jr., Haptoglobin and posttranslational glycan-modified derivatives as serum biomarkers for the diagnosis of nonsmall cell lung cancer. Cancer 2007, 110, 2260-2268.
    • Hoagland, L. F. t., Campa, M. J., Gottlin, E. B., Herndon, J. E., 2nd, Patz, E. F., Jr., Haptoglobin and posttranslational glycan-modified derivatives as serum biomarkers for the diagnosis of nonsmall cell lung cancer. Cancer 2007, 110, 2260-2268.
  • 99
    • 34249320200 scopus 로고    scopus 로고
    • Proteomic analysis to dissect mitoxantrone resistance-associated proteins in a squamous lung carcinoma
    • Murphy, L., Clynes, M., Keenan, J., Proteomic analysis to dissect mitoxantrone resistance-associated proteins in a squamous lung carcinoma. Anticancer Res. 2007, 27, 1277-1284.
    • (2007) Anticancer Res , vol.27 , pp. 1277-1284
    • Murphy, L.1    Clynes, M.2    Keenan, J.3
  • 100
    • 36348936819 scopus 로고    scopus 로고
    • Searching urinary tumor markers for bladder cancer using a two-dimensional differential gel electrophoresis (2D-DIGE) approach
    • Orenes-Pinero, E., Corton, M., Gonzalez-Peramato, P., Algaba, F. et al., Searching urinary tumor markers for bladder cancer using a two-dimensional differential gel electrophoresis (2D-DIGE) approach. J. Proteome Res. 2007, 6, 4440-4448.
    • (2007) J. Proteome Res , vol.6 , pp. 4440-4448
    • Orenes-Pinero, E.1    Corton, M.2    Gonzalez-Peramato, P.3    Algaba, F.4
  • 101
    • 35648989121 scopus 로고    scopus 로고
    • Proteomics-based strategy to delineate the molecular mechanisms of the metastasis suppressor gene BRMS1
    • Rivera, J., Megias, D., Bravo, J., Proteomics-based strategy to delineate the molecular mechanisms of the metastasis suppressor gene BRMS1. J. Proteome Res. 2007, 6, 4006-4018.
    • (2007) J. Proteome Res , vol.6 , pp. 4006-4018
    • Rivera, J.1    Megias, D.2    Bravo, J.3
  • 102
    • 35648963627 scopus 로고    scopus 로고
    • Proteome analysis of hepatocellular carcinoma by two-dimensional difference gel electrophoresis: Novel protein markers in hepatocellular carcinoma tissues
    • Sun, W., Xing, B., Sun, Y., Du, X. et al., Proteome analysis of hepatocellular carcinoma by two-dimensional difference gel electrophoresis: novel protein markers in hepatocellular carcinoma tissues. Mol. Cell. Proteomics 2007, 6, 1798-1808.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1798-1808
    • Sun, W.1    Xing, B.2    Sun, Y.3    Du, X.4
  • 103
    • 44449164077 scopus 로고    scopus 로고
    • Biological pathways contributing to organ-specific phenotype of brain metastatic cells
    • Martin, B., Aragues, R., Sanz, R., Oliva, B. et al., Biological pathways contributing to organ-specific phenotype of brain metastatic cells. J. Proteome Res. 2008, 7, 908-920.
    • (2008) J. Proteome Res , vol.7 , pp. 908-920
    • Martin, B.1    Aragues, R.2    Sanz, R.3    Oliva, B.4
  • 104
    • 34047111193 scopus 로고    scopus 로고
    • Alterations in the diabetic myocardial proteome coupled with increased myocardial oxidative stress underlies diabetic cardiomyopathy
    • Hamblin, M., Friedman, D. B., Hill, S., Caprioli, R. M. et al., Alterations in the diabetic myocardial proteome coupled with increased myocardial oxidative stress underlies diabetic cardiomyopathy. J. Mol. Cell. Cardiol. 2007, 42, 884-895.
    • (2007) J. Mol. Cell. Cardiol , vol.42 , pp. 884-895
    • Hamblin, M.1    Friedman, D.B.2    Hill, S.3    Caprioli, R.M.4
  • 105
    • 38649105460 scopus 로고    scopus 로고
    • Application of 2-dimensional difference gel electrophoresis (2D-DIGE) to the study of thrombin-activated human platelet secretome
    • Della Corte, A., Maugeri, N., Pampuch, A., Cerletti, C. et al., Application of 2-dimensional difference gel electrophoresis (2D-DIGE) to the study of thrombin-activated human platelet secretome. Platelets 2008, 19, 43-50.
    • (2008) Platelets , vol.19 , pp. 43-50
    • Della Corte, A.1    Maugeri, N.2    Pampuch, A.3    Cerletti, C.4
  • 106
    • 45849093739 scopus 로고    scopus 로고
    • Plasma biomarkers in pediatric patients undergoing cardiopulmonary bypass
    • Lull, M. E., Carkaci-Salli, N., Freeman, W. M., Myers, J. L. et al., Plasma biomarkers in pediatric patients undergoing cardiopulmonary bypass. Pediatr. Res. 2008, 63, 638-644.
    • (2008) Pediatr. Res , vol.63 , pp. 638-644
    • Lull, M.E.1    Carkaci-Salli, N.2    Freeman, W.M.3    Myers, J.L.4
  • 107
    • 38149014016 scopus 로고    scopus 로고
    • Use of 2-D DIGE analysis reveals altered phosphorylation in a tropomyosin mutant (Glu54Lys) linked to dilated cardiomyopathy
    • Warren, C. M., Arteaga, G. M., Rajan, S., Ahmed, R. P. et al., Use of 2-D DIGE analysis reveals altered phosphorylation in a tropomyosin mutant (Glu54Lys) linked to dilated cardiomyopathy. Proteomics 2008, 8, 100-105.
    • (2008) Proteomics , vol.8 , pp. 100-105
    • Warren, C.M.1    Arteaga, G.M.2    Rajan, S.3    Ahmed, R.P.4
  • 108
    • 0036907867 scopus 로고    scopus 로고
    • Fluorescence two-dimensional difference gel electrophoresis and mass spectrometry based proteomic analysis of Escherichia coli
    • Yan, J. X., Devenish, A. T., Wait, R., Stone, T. et al., Fluorescence two-dimensional difference gel electrophoresis and mass spectrometry based proteomic analysis of Escherichia coli. Proteomics 2002, 2, 1682-1698.
    • (2002) Proteomics , vol.2 , pp. 1682-1698
    • Yan, J.X.1    Devenish, A.T.2    Wait, R.3    Stone, T.4
  • 109
    • 39049097692 scopus 로고    scopus 로고
    • Biological variation of the platelet proteome in the elderly population and its implication for biomarker research
    • Winkler, W., Zellner, M., Diestinger, M., Babeluk, R. et al., Biological variation of the platelet proteome in the elderly population and its implication for biomarker research. Mol. Cell. Proteomics 2008, 7, 193-203.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 193-203
    • Winkler, W.1    Zellner, M.2    Diestinger, M.3    Babeluk, R.4
  • 110
    • 1542344981 scopus 로고    scopus 로고
    • Protein profiling of human postmortem brain using 2-dimensional fluorescence difference gel electrophoresis (2-D DIGE)
    • Swatton, J. E., Prabakaran, S., Karp, N. A., Lilley, K. S., Bahn, S., Protein profiling of human postmortem brain using 2-dimensional fluorescence difference gel electrophoresis (2-D DIGE). Mol. Psychiatry 2004, 9, 128-143.
    • (2004) Mol. Psychiatry , vol.9 , pp. 128-143
    • Swatton, J.E.1    Prabakaran, S.2    Karp, N.A.3    Lilley, K.S.4    Bahn, S.5
  • 111
    • 0036463563 scopus 로고    scopus 로고
    • 2D differential in-gel electrophoresis for the identification of esophageal scans cell cancer-specific protein markers
    • Zhou, G., Li, H., DeCamp, D., Chen, S. et al., 2D differential in-gel electrophoresis for the identification of esophageal scans cell cancer-specific protein markers. Mol. Cell. Proteomics 2002, 1, 117-124.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 117-124
    • Zhou, G.1    Li, H.2    DeCamp, D.3    Chen, S.4
  • 112
    • 33646730688 scopus 로고    scopus 로고
    • Inflammation inhibitors were remarkably up-regulated in plasma of severe acute respiratory syndrome patients at progressive phase
    • Wan, J., Sun, W., Li, X., Ying, W. et al., Inflammation inhibitors were remarkably up-regulated in plasma of severe acute respiratory syndrome patients at progressive phase. Proteomics 2006, 6, 2886-2894.
    • (2006) Proteomics , vol.6 , pp. 2886-2894
    • Wan, J.1    Sun, W.2    Li, X.3    Ying, W.4
  • 113
    • 85047696233 scopus 로고    scopus 로고
    • Absence of increased alpha1-microglobulin in IgA nephropathy proteinuria
    • Yokota, H., Hiramoto, M., Okada, H., Kanno, Y. et al., Absence of increased alpha1-microglobulin in IgA nephropathy proteinuria. Mol. Cell. Proteomics 2007, 6, 738-744.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 738-744
    • Yokota, H.1    Hiramoto, M.2    Okada, H.3    Kanno, Y.4
  • 114
    • 0842308382 scopus 로고    scopus 로고
    • Cellular responses to ErbB-2 overexpression in human mammary luminal epithelial cells: Comparison of mRNA and protein expression
    • White, S. L., Gharbi, S., Bertani, M. F., Chan, H. L. et al., Cellular responses to ErbB-2 overexpression in human mammary luminal epithelial cells: comparison of mRNA and protein expression. Br. J. Cancer 2004, 90, 173-181.
    • (2004) Br. J. Cancer , vol.90 , pp. 173-181
    • White, S.L.1    Gharbi, S.2    Bertani, M.F.3    Chan, H.L.4
  • 115
    • 33846003491 scopus 로고    scopus 로고
    • CyDye immunoblotting for proteomics: Co-detection of specific immunoreactive and total protein profiles
    • Donoghue, P. M., McManus, C. A., O'Donoghue, N. M., Pennington, S. R., Dunn, M. J., CyDye immunoblotting for proteomics: co-detection of specific immunoreactive and total protein profiles. Proteomics 2006, 6, 6400-6404.
    • (2006) Proteomics , vol.6 , pp. 6400-6404
    • Donoghue, P.M.1    McManus, C.A.2    O'Donoghue, N.M.3    Pennington, S.R.4    Dunn, M.J.5
  • 116
    • 35648996442 scopus 로고    scopus 로고
    • Integrated membrane protein analysis of mature and embryonic stem cell-derived smooth muscle cells using a novel combination of CyDye/biotin labeling
    • Sidibe, A., Yin, X., Tarelli, E., Xiao, Q. et al., Integrated membrane protein analysis of mature and embryonic stem cell-derived smooth muscle cells using a novel combination of CyDye/biotin labeling. Mol. Cell. Proteomics 2007, 6, 1788-1797.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1788-1797
    • Sidibe, A.1    Yin, X.2    Tarelli, E.3    Xiao, Q.4
  • 117
    • 34250792155 scopus 로고    scopus 로고
    • Dynamic cofilin phosphorylation in the control of lamellipodial actin homeostasis
    • Jovceva, E., Larsen, M. R., Waterfield, M. D., Baum, B., Timms, J. F., Dynamic cofilin phosphorylation in the control of lamellipodial actin homeostasis. J. Cell Sci. 2007, 120, 1888-1897.
    • (2007) J. Cell Sci , vol.120 , pp. 1888-1897
    • Jovceva, E.1    Larsen, M.R.2    Waterfield, M.D.3    Baum, B.4    Timms, J.F.5


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