메뉴 건너뛰기




Volumn 28, Issue 1, 2004, Pages 63-76

Recent advances in gel-based proteome profiling techniques

Author keywords

DIGE; Fluorescence; ICAT; Isotope labeling; Proteomics; SDS PAGE; Two dimensional

Indexed keywords

ACRYLICS; ELECTROPHORESIS; GELS; MOLECULAR BIOLOGY; POLYAMIDES; PROBES; RADIOISOTOPES;

EID: 13844270303     PISSN: 10736085     EISSN: None     Source Type: Journal    
DOI: 10.1385/MB:28:1:63     Document Type: Review
Times cited : (29)

References (58)
  • 2
    • 0034659898 scopus 로고    scopus 로고
    • Genomics, gene expression and DNA arrays
    • Lockhart, D. J. and Winzeler, E. A. (2000) Genomics, gene expression and DNA arrays. Nature. 405, 827-836.
    • (2000) Nature , vol.405 , pp. 827-836
    • Lockhart, D.J.1    Winzeler, E.A.2
  • 3
    • 0033016717 scopus 로고    scopus 로고
    • Correlation between protein and mRNA abundance in yeast
    • Gygi, S. P., Rochon, Y., Franza, B. R., and Aebersold, R. (1999) Correlation between protein and mRNA abundance in yeast. Mol. Cell Biol. 19, 1720-1730.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 1720-1730
    • Gygi, S.P.1    Rochon, Y.2    Franza, B.R.3    Aebersold, R.4
  • 5
    • 0348129535 scopus 로고    scopus 로고
    • Proteome analysis of Saccharomyces cerevisiae under metal stress by two-dimensional differential gel electrophoresis
    • Hu, Y., Wang, G., Chen, G. Y. J., Fu, X., and Yao, S. Q. (2003) Proteome analysis of Saccharomyces cerevisiae under metal stress by two-dimensional differential gel electrophoresis. Electrophoresis 24, 1458-1470.
    • (2003) Electrophoresis , vol.24 , pp. 1458-1470
    • Hu, Y.1    Wang, G.2    Chen, G.Y.J.3    Fu, X.4    Yao, S.Q.5
  • 6
    • 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. (2000) A thousand points of light: the application of fluorescence detection technologies to two-dimensional gel electrophoresis and proteomics. Electrophoresis 21, 1123-1144.
    • (2000) Electrophoresis , vol.21 , pp. 1123-1144
    • Patton, W.F.1
  • 7
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R. and Mann, M. (2003) Mass spectrometry-based proteomics. Nature 422, 198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 9
    • 0035464862 scopus 로고    scopus 로고
    • Proteomics comes to the surface
    • MacBeath, G. (2001) Proteomics comes to the surface. Nat. Biotechnol. 19, 828-829.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 828-829
    • MacBeath, G.1
  • 10
    • 0035860499 scopus 로고    scopus 로고
    • Global analysis of protein activities using proteome chips
    • Zhu, H., Bilgin, M., Bangham, R., et al. (2001) Global analysis of protein activities using proteome chips. Science 293, 2101-2105.
    • (2001) Science , vol.293 , pp. 2101-2105
    • Zhu, H.1    Bilgin, M.2    Bangham, R.3
  • 11
    • 0037205866 scopus 로고    scopus 로고
    • Intein-mediated biotinylation of proteins and its application in a protein microarray
    • Lesaicherre, M. L., Lue, Y. P. R., Chen, G. Y. J., Zhu, Q., and Yao, S. Q. (2002) Intein-mediated biotinylation of proteins and its application in a protein microarray, J. Am. Chem. Soc. 124, 8768-8769.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 8768-8769
    • Lesaicherre, M.L.1    Lue, Y.P.R.2    Chen, G.Y.J.3    Zhu, Q.4    Yao, S.Q.5
  • 12
    • 0242432396 scopus 로고    scopus 로고
    • Developing a strategy for activity-based detection of enzymes in a protein microarray
    • Chen, G. Y. J., Uttamchandani, M., Zhu, Q., Wang, G., and Yao, S. Q. (2003) Developing a strategy for activity-based detection of enzymes in a protein microarray. Chembiochem. 4, 336-339.
    • (2003) Chembiochem. , vol.4 , pp. 336-339
    • Chen, G.Y.J.1    Uttamchandani, M.2    Zhu, Q.3    Wang, G.4    Yao, S.Q.5
  • 13
    • 0037135998 scopus 로고    scopus 로고
    • Developing site-specific immobilization strategies of peptides in a microarray
    • Lesaicherre, M. L., Uttamchandani, M., Chen, G. Y. J., and Yao, S. Q. (2002) Developing site-specific immobilization strategies of peptides in a microarray. Bioorg. Med. Chem. Lett. 12, 2079-2083.
    • (2002) Bioorg. Med. Chem. Lett. , vol.12 , pp. 2079-2083
    • Lesaicherre, M.L.1    Uttamchandani, M.2    Chen, G.Y.J.3    Yao, S.Q.4
  • 14
  • 15
    • 0038601676 scopus 로고    scopus 로고
    • An enzymatic profiling system in a small-molecule microarray
    • Zhu, Q., Uttamchandani, M., Li, D.B., Lesaicherre, M. L., and Yao, S. Q. (2003) An enzymatic profiling system in a small-molecule microarray. Org. Lett. 5, 1257-1260.
    • (2003) Org. Lett. , vol.5 , pp. 1257-1260
    • Zhu, Q.1    Uttamchandani, M.2    Li, D.B.3    Lesaicherre, M.L.4    Yao, S.Q.5
  • 16
    • 0043022188 scopus 로고    scopus 로고
    • Combinatorial peptide microarrays for the rapid determination of kinase specificity
    • Uttamchandani, M., Chan, E. W. S., Chen, G. Y. J., and Yao, S. Q. (2003) Combinatorial peptide microarrays for the rapid determination of kinase specificity. Bioorg. Med. Chem. Lett. 13, 2997-3000.
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 2997-3000
    • Uttamchandani, M.1    Chan, E.W.S.2    Chen, G.Y.J.3    Yao, S.Q.4
  • 17
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlu, M., Morgan, M. E., and Minden, J. S. (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
  • 18
    • 0035289178 scopus 로고    scopus 로고
    • Validation and development of fluorescence two-dimensional differential gel electrophoresis proteomics technology
    • Tonge, R., Shaw, J., Middleton, B., et al. (2001) Validation and development of fluorescence two-dimensional differential gel electrophoresis proteomics technology. Proteomics 1, 377-396.
    • (2001) Proteomics , vol.1 , pp. 377-396
    • Tonge, R.1    Shaw, J.2    Middleton, B.3
  • 19
    • 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., et al. (2002) Evaluation of two-dimensional differential gel electrophoresis for proteomic expression analysis of a model breast cancer cell system. Mol. Cell. Proteomics 1, 91-98.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 91-98
    • Gharbi, S.1    Gaffney, P.2    Yang, A.3
  • 20
    • 0041871026 scopus 로고    scopus 로고
    • Evaluation of two-dimensional difference gel electrophoresis for protein profiling: Soluble proteins of the marine bacterium Pirellula sp. strain 1
    • Gade, D., Thiermann, J., Markowsky, D., and Rabus, R. (2003) Evaluation of two-dimensional difference gel electrophoresis for protein profiling: soluble proteins of the marine bacterium Pirellula sp. strain 1. J. Mol. Microbiol. Biotechnol. 5, 240-251.
    • (2003) J. Mol. Microbiol. Biotechnol. , vol.5 , pp. 240-251
    • Gade, D.1    Thiermann, J.2    Markowsky, D.3    Rabus, R.4
  • 21
    • 0037898953 scopus 로고    scopus 로고
    • Differential protein analysis of spasmolytic polypeptide expressing metaplasia using laser capture microdissection and two-dimensional difference gel electrophoresis
    • Lee, J. R., Baxter, T. M., Yamaguchi, H., Wang, T. C., Goldenring, J. R., and Anderson, M. G. (2003) Differential protein analysis of spasmolytic polypeptide expressing metaplasia using laser capture microdissection and two-dimensional difference gel electrophoresis. Appl. Immunohistochem. Mol. Morphol. 11, 188-193.
    • (2003) Appl. Immunohistochem. Mol. Morphol. , vol.11 , pp. 188-193
    • Lee, J.R.1    Baxter, T.M.2    Yamaguchi, H.3    Wang, T.C.4    Goldenring, J.R.5    Anderson, M.G.6
  • 22
    • 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., et al. (2002) 2D differential in-gel electrophoresis for the identification of esophageal scans cell cancer-specific protein markers. Mol. Cell. Proteomics 1, 117-124.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 117-124
    • Zhou, G.1    Li, H.2    DeCamp, D.3
  • 23
    • 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., and Arckens, L. (2003) 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 24, 1471-1481.
    • (2003) Electrophoresis , vol.24 , pp. 1471-1481
    • Van Den Bergh, G.1    Clerens, S.2    Vandesande, F.3    Arckens, L.4
  • 24
    • 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., Lewis, S., and Fowler, S. (2002) Fluorescence two-dimensional difference gel electrophoresis and mass spectrometry based proteomic analysis of Escherichia coli. Proteomics 2, 1682-1698.
    • (2002) Proteomics , vol.2 , pp. 1682-1698
    • Yan, J.X.1    Devenish, A.T.2    Wait, R.3    Stone, T.4    Lewis, S.5    Fowler, S.6
  • 25
    • 0043166918 scopus 로고    scopus 로고
    • Evaluation of saturation labelling two-dimensional difference gel electrophoresis fluorescent dyes
    • Shaw, J., Rowlinson, R., Nickson, J., et al. (2003) Evaluation of saturation labelling two-dimensional difference gel electrophoresis fluorescent dyes. Proteomics 3, 1181-1195.
    • (2003) Proteomics , vol.3 , pp. 1181-1195
    • Shaw, J.1    Rowlinson, R.2    Nickson, J.3
  • 26
    • 0035408680 scopus 로고    scopus 로고
    • Rapid and simple single nanogram detection of glycoproteins in polyacrylamide gels and on electroblots
    • Steinberg, T. H., Pretty On Top, K., Berggren, K. N., et al. (2001) Rapid and simple single nanogram detection of glycoproteins in polyacrylamide gels and on electroblots. Proteomics 1, 841-855.
    • (2001) Proteomics , vol.1 , pp. 841-855
    • Steinberg, T.H.1    Pretty On Top, K.2    Berggren, K.N.3
  • 27
    • 12444315072 scopus 로고    scopus 로고
    • Global quantitative phosphoprotein analysis using multiplexed proteomics technology
    • Steinberg, T. H., Agnew, B. J., Gee, K. R., et al. (2003) Global quantitative phosphoprotein analysis using multiplexed proteomics technology. Proteomics 3, 1128-1144.
    • (2003) Proteomics , vol.3 , pp. 1128-1144
    • Steinberg, T.H.1    Agnew, B.J.2    Gee, K.R.3
  • 29
    • 0038445766 scopus 로고    scopus 로고
    • Mapping glycosylation changes related to cancer using the multiplexed proteomics technology: A protein differential display approach
    • Schulenberg, B., Beechem, J. M., and Patton, W. F. (2003) Mapping glycosylation changes related to cancer using the multiplexed proteomics technology: a protein differential display approach. J Chromatogr. B Analyt. Technol. Biomed. Life Sci. 793, 127-139.
    • (2003) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.793 , pp. 127-139
    • Schulenberg, B.1    Beechem, J.M.2    Patton, W.F.3
  • 30
    • 0036208704 scopus 로고    scopus 로고
    • Differential gel exposure: A new methodology for the two-dimensional comparison of protein samples
    • Monribot-Espagne, C. and Boucherie, H. (2002) Differential gel exposure: a new methodology for the two-dimensional comparison of protein samples. Proteomics 2, 229-240.
    • (2002) Proteomics , vol.2 , pp. 229-240
    • Monribot-Espagne, C.1    Boucherie, H.2
  • 31
    • 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., Gelb, M. H., and Aebersold, R. (1999) Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 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    Gelb, M.H.5    Aebersold, R.6
  • 32
    • 0036161596 scopus 로고    scopus 로고
    • Mass spectrometry in coupling with affinity capture-release and isotope-coded affinity tags for quantitative protein analysis
    • Turecek, F. (2002) Mass spectrometry in coupling with affinity capture-release and isotope-coded affinity tags for quantitative protein analysis. J. Mass Spectrom. 37, 1-14.
    • (2002) J. Mass Spectrom. , vol.37 , pp. 1-14
    • Turecek, F.1
  • 33
    • 0036049889 scopus 로고    scopus 로고
    • Quantitative protein profiling using two-dimensional gel electrophoresis, isotope-coded affinity tag labeling, and mass spectrometry
    • Smolka, M., Zhou, H., and Aebersold, R. (2002) Quantitative protein profiling using two-dimensional gel electrophoresis, isotope-coded affinity tag labeling, and mass spectrometry. Mol. Cell Proteomics 1, 19-29.
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 19-29
    • Smolka, M.1    Zhou, H.2    Aebersold, R.3
  • 34
    • 0035896609 scopus 로고    scopus 로고
    • A proteome analysis of the cadmium response in Saccharomyces cerevisiae
    • Vido, K., Spector, D., Lagniel, G., Lopez, S., Toledano, M. B., and Labarre, J. (2001) A proteome analysis of the cadmium response in Saccharomyces cerevisiae. J. Biol. Chem. 276, 8469-8474.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8469-8474
    • Vido, K.1    Spector, D.2    Lagniel, G.3    Lopez, S.4    Toledano, M.B.5    Labarre, J.6
  • 35
    • 0030010479 scopus 로고    scopus 로고
    • Rapid identification of yeast proteins on two-dimensional gels
    • Maillet, I., Lagniel, G., Perrot, M., Boucherie, H., and Labarre, J. (1996) Rapid identification of yeast proteins on two-dimensional gels. J. Biol. Chem. 271, 10263-10270.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10263-10270
    • Maillet, I.1    Lagniel, G.2    Perrot, M.3    Boucherie, H.4    Labarre, J.5
  • 36
    • 0042357079 scopus 로고    scopus 로고
    • Transcriptional, proteomic, and metabolic responses to lithium in galactose-grown yeast cells
    • Bro, C., Regenberg, B., Lagniel, G., Labarre, J., Montero-Lomeli, M., and Nielsen, J. (2003) Transcriptional, proteomic, and metabolic responses to lithium in galactose-grown yeast cells. J. Biol. Chem. 278, 32141-32149.
    • (2003) J. Biol. Chem. , vol.278 , pp. 32141-32149
    • Bro, C.1    Regenberg, B.2    Lagniel, G.3    Labarre, J.4    Montero-Lomeli, M.5    Nielsen, J.6
  • 37
    • 0036665484 scopus 로고    scopus 로고
    • Quantitative analysis of the yeast proteome by incorporation of isotopically labeled leucine
    • Jiang, H. and English, A. M. (2002) Quantitative analysis of the yeast proteome by incorporation of isotopically labeled leucine. J. Proteome Res. 1, 345-350.
    • (2002) J. Proteome Res. , vol.1 , pp. 345-350
    • Jiang, H.1    English, A.M.2
  • 38
    • 0041706161 scopus 로고    scopus 로고
    • Metabolic labeling of C. elegans and D. melanogaster for quantitative proteomics
    • Krijgsveld, J., Ketting, R. F., Mahmoudi, T., et al. (2003) Metabolic labeling of C. elegans and D. melanogaster for quantitative proteomics. Nat. Biotechnol. 21, 927-931.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 927-931
    • Krijgsveld, J.1    Ketting, R.F.2    Mahmoudi, T.3
  • 39
    • 0029278864 scopus 로고
    • Elevated levels of wild-type p53 induced by radiolabeling of cells leads to apoptosis or sustained growth arrest
    • Yeargin, J. and Haas, M. (1995) Elevated levels of wild-type p53 induced by radiolabeling of cells leads to apoptosis or sustained growth arrest. Curr. Biol. 5, 423-431.
    • (1995) Curr. Biol. , vol.5 , pp. 423-431
    • Yeargin, J.1    Haas, M.2
  • 40
    • 0037307787 scopus 로고    scopus 로고
    • Chemical proteomics and its application to drug discovery
    • Jeffery, D. A. and Boygo, M. (2003) Chemical proteomics and its application to drug discovery. Curr. Opin. Biotechnol. 14, 87-95.
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 87-95
    • Jeffery, D.A.1    Boygo, M.2
  • 42
    • 0013177603 scopus 로고    scopus 로고
    • Solid-phase synthesis of peptide vinyl sulfones and their uses in large-scale proteomic experiments
    • Wang, G., Uttamchandani, M., Chen, G. Y. J., and Yao, S. Q. (2003) Solid-phase synthesis of peptide vinyl sulfones and their uses in large-scale proteomic experiments. Org. Lett. 5, 737-740.
    • (2003) Org. Lett. , vol.5 , pp. 737-740
    • Wang, G.1    Uttamchandani, M.2    Chen, G.Y.J.3    Yao, S.Q.4
  • 43
    • 0037463732 scopus 로고    scopus 로고
    • Activity-based fluorescent probes that targets phosphatases
    • Zhu, Q., Huang, X., Chen, G. Y. J., and Yao, S. Q. (2003) Activity-based fluorescent probes that targets phosphatases. Tetrahedron Lett. 44, 2669-2672.
    • (2003) Tetrahedron Lett. , vol.44 , pp. 2669-2672
    • Zhu, Q.1    Huang, X.2    Chen, G.Y.J.3    Yao, S.Q.4
  • 44
    • 0037467853 scopus 로고    scopus 로고
    • Design and synthesis of an affinity probe that targets caspases in proteomic experiments
    • Liau, M. L., Panicker, R. C., and Yao, S. Q. (2003) Design and synthesis of an affinity probe that targets caspases in proteomic experiments. Tetrahedron Lett. 44, 1043-1046.
    • (2003) Tetrahedron Lett. , vol.44 , pp. 1043-1046
    • Liau, M.L.1    Panicker, R.C.2    Yao, S.Q.3
  • 45
    • 0037462106 scopus 로고    scopus 로고
    • Activity-based protein profiling in vivo using a copper(i)-catalyzed azide-alkyne [3 + 2] cycloaddition
    • Speers, A. E., Adam, G. C., and Cravatt, B. F. (2003) Activity-based protein profiling in vivo using a copper(i)-catalyzed azide-alkyne [3 + 2] cycloaddition. J. Am. Chem. Soc. 125, 4686-4687.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 4686-4687
    • Speers, A.E.1    Adam, G.C.2    Cravatt, B.F.3
  • 46
    • 0038157152 scopus 로고    scopus 로고
    • Dosage sensitivity and the evolution of gene families in yeast
    • Papp, B., Pal, C., and Hurst, L. D. (2003) Dosage sensitivity and the evolution of gene families in yeast. Nature 424, 194-197.
    • (2003) Nature , vol.424 , pp. 194-197
    • Papp, B.1    Pal, C.2    Hurst, L.D.3
  • 47
    • 0036817905 scopus 로고    scopus 로고
    • Proteomic technologies in modern biomedical science
    • Govorun, V. M. and Archakov, A. I. (2002) Proteomic technologies in modern biomedical science. Biochemistry (Mosc) 67, 1109-1123.
    • (2002) Biochemistry (Mosc) , vol.67 , pp. 1109-1123
    • Govorun, V.M.1    Archakov, A.I.2
  • 48
    • 0035987407 scopus 로고    scopus 로고
    • The post-genomic era of interactive proteomics: Facts and perspectives
    • Auerbach, D., Thaminy, S., Hottiger, M. O., and Stagljar, I. (2002) The post-genomic era of interactive proteomics: facts and perspectives. Proteomics 2, 611-623.
    • (2002) Proteomics , vol.2 , pp. 611-623
    • Auerbach, D.1    Thaminy, S.2    Hottiger, M.O.3    Stagljar, I.4
  • 49
    • 0030963019 scopus 로고    scopus 로고
    • Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens
    • Fromont-Racine, M., Rain, J. C., and Legrain, P. (1997) Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens. Nat. Genet. 16, 277-282.
    • (1997) Nat. Genet. , vol.16 , pp. 277-282
    • Fromont-Racine, M.1    Rain, J.C.2    Legrain, P.3
  • 50
    • 0032574840 scopus 로고    scopus 로고
    • A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo
    • Stagljar, I., Korostensky, C., Johnsson, N., and te Heesen, S. (1998) A genetic system based on split-ubiquitin for the analysis of interactions between membrane proteins in vivo. Proc. Natl. Acad. Sci. USA 95, 5187-5192.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5187-5192
    • Stagljar, I.1    Korostensky, C.2    Johnsson, N.3    Te Heesen, S.4
  • 51
    • 0034628508 scopus 로고    scopus 로고
    • A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae
    • Uetz, P., Giot, L., Cagney, G., et al. (2000) A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 403, 623-627.
    • (2000) Nature , vol.403 , pp. 623-627
    • Uetz, P.1    Giot, L.2    Cagney, G.3
  • 52
    • 0034841844 scopus 로고    scopus 로고
    • The tandem affinity purification (TAP) method: A general procedure of protein complex purification
    • Puig, O., Caspary, F., Rigaut, G., et al. (2001) The tandem affinity purification (TAP) method: a general procedure of protein complex purification. Methods 24, 218-229.
    • (2001) Methods , vol.24 , pp. 218-229
    • Puig, O.1    Caspary, F.2    Rigaut, G.3
  • 53
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • Gavin, A. C., Bosche, M., Krause, R., et al. (2002) Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415, 141-147.
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.C.1    Bosche, M.2    Krause, R.3
  • 54
    • 0036491512 scopus 로고    scopus 로고
    • Isolation of protein subpopulations undergoing protein-protein interactions
    • Nelson, T. J., Backlund, P. S.. Jr., Yergey, A. L., and Alkon, D. L. (2002) Isolation of protein subpopulations undergoing protein-protein interactions. Mol. Cell. Proteomics 1, 253-259.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 253-259
    • Nelson, T.J.1    Backlund Jr., P.S.2    Yergey, A.L.3    Alkon, D.L.4
  • 55
    • 0037337310 scopus 로고    scopus 로고
    • A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling
    • Blagoev, B., Kratchmarova, I., Ong, S. E., Nielsen, M., Foster, L. J., and Mann, M. (2003) A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. Nat. Biotechnol. 21, 315-318.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 315-318
    • Blagoev, B.1    Kratchmarova, I.2    Ong, S.E.3    Nielsen, M.4    Foster, L.J.5    Mann, M.6
  • 56
    • 0037337308 scopus 로고    scopus 로고
    • The application of mass spectrometry to membrane proteomics
    • Wu, C. C. and Yates, J. R., III. (2003) The application of mass spectrometry to membrane proteomics. Nat. Biotechnol. 21, 262-267.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 262-267
    • Wu, C.C.1    Yates III, J.R.2
  • 57
    • 0038561131 scopus 로고    scopus 로고
    • A method for the comprehensive proteomic analysis of membrane proteins
    • Wu, C. C., MacCoss, M. J., Howell, K. E., and Yates, J. R., III. (2003) A method for the comprehensive proteomic analysis of membrane proteins. Nat. Biotechnol. 21, 532-538.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 532-538
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Yates III, J.R.4
  • 58
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • Mann, M., Jensen, O. N. (2003) Proteomic analysis of post-translational modifications. Nat. Biotechnol. 21, 255-261.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.