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Volumn 13, Issue 4, 2002, Pages 321-328

Two-dimensional gel electrophoresis; better than a poke in the ICAT?

Author keywords

[No Author keywords available]

Indexed keywords

ANALYTIC METHOD; INTERMETHOD COMPARISON; ISOTOPE CODED AFFINITY TAGGING; LIQUID CHROMATOGRAPHY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEOMICS; REVIEW; TWO DIMENSIONAL GEL ELECTROPHORESIS;

EID: 0036669447     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(02)00333-6     Document Type: Review
Times cited : (96)

References (42)
  • 2
    • 0034517388 scopus 로고    scopus 로고
    • Identification of novel MAP kinase pathway signaling targets by functional proteomics and mass spectrometry
    • Lewis T., Hunt J., Aveline L., Jonscher K., Louie D., Yeh J., Nahreini T., Resing K., Ahn N. Identification of novel MAP kinase pathway signaling targets by functional proteomics and mass spectrometry. Mol Cell. 6:2000;1343-1354. Demonstration of the global capabilities of 2DGE to monitor the activation of signal transduction pathways. In this study, 25 new substrates of the MAP kinase pathway were identified.
    • (2000) Mol Cell , vol.6 , pp. 1343-1354
    • Lewis, T.1    Hunt, J.2    Aveline, L.3    Jonscher, K.4    Louie, D.5    Yeh, J.6    Nahreini, T.7    Resing, K.8    Ahn, N.9
  • 3
    • 0035408680 scopus 로고    scopus 로고
    • Rapid and simple single nanogram detection of glycoproteins in polyacrylamide gels and on electroblots
    • Steinberg T., Pretty On Top K., Berggren K., Kemper C., Jones L., Diwu Z., Haugland R., Patton W. Rapid and simple single nanogram detection of glycoproteins in polyacrylamide gels and on electroblots. Proteomics. 1:2001;841-855. Demonstration of global fluorescence detection at the nanogram level of glycosylation and protein expression levels in complex samples from a single polyacrylamide gel.
    • (2001) Proteomics , vol.1 , pp. 841-855
    • Steinberg, T.1    Pretty On Top, K.2    Berggren, K.3    Kemper, C.4    Jones, L.5    Diwu, Z.6    Haugland, R.7    Patton, W.8
  • 4
    • 0034662907 scopus 로고    scopus 로고
    • Evaluation of two-dimensional gel electrophoresis-based proteome analysis technology
    • Gygi S., Corthals G., Zhang Y., Rochon Y., Aebersold R. Evaluation of two-dimensional gel electrophoresis-based proteome analysis technology. Proc Natl Acad Sci USA. 97:2000;9390-9395.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 9390-9395
    • Gygi, S.1    Corthals, G.2    Zhang, Y.3    Rochon, Y.4    Aebersold, R.5
  • 5
    • 0035252854 scopus 로고    scopus 로고
    • 2D or not 2D. Two-dimensional gel electrophoresis
    • Fey S., Larson P. 2D or not 2D. Two-dimensional gel electrophoresis. Curr Opin Chem Biol. 5:2001;26-33.
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 26-33
    • Fey, S.1    Larson, P.2
  • 6
    • 0005143684 scopus 로고    scopus 로고
    • Why proteomics can't let go of 2D gels
    • Sender A. Why proteomics can't let go of 2D gels. Genome Technol. 12:2001;34-38.
    • (2001) Genome Technol , vol.12 , pp. 34-38
    • Sender, A.1
  • 8
    • 0035207977 scopus 로고    scopus 로고
    • Possibilities to improve automation, speed and precision of proteome analysis: A comparison of two-dimensional electrophoresis and alternatives
    • Hille J., Freed A., Watzig H. Possibilities to improve automation, speed and precision of proteome analysis: a comparison of two-dimensional electrophoresis and alternatives. Electrophoresis. 22:2001;4035-4052.
    • (2001) Electrophoresis , vol.22 , pp. 4035-4052
    • Hille, J.1    Freed, A.2    Watzig, H.3
  • 9
    • 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. 2:2002;3-10.
    • (2002) Proteomics , vol.2 , pp. 3-10
    • Rabilloud, T.1
  • 10
    • 0033027936 scopus 로고    scopus 로고
    • Proteome analysis II. Protein subcellular redistribution; Linking physiology to genomics via the proteome and separation technologies involved
    • Patton W. Proteome analysis II. Protein subcellular redistribution; linking physiology to genomics via the proteome and separation technologies involved. J Chromatogr B. 722:1999;203-223.
    • (1999) J Chromatogr B , vol.722 , pp. 203-223
    • Patton, W.1
  • 11
    • 0033915670 scopus 로고    scopus 로고
    • Background-free, high-sensitivity staining of proteins in one- and two-dimensional sodium dodecyl sulfate-polyacrylamide gels using a luminescent ruthenium complex
    • Berggren K., Chernokalskaya E., Steinberg T., Kemper C., Lopez M., Diwu Z., Haugland R., Patton W. Background-free, high-sensitivity staining of proteins in one- and two-dimensional sodium dodecyl sulfate-polyacrylamide gels using a luminescent ruthenium complex. Electrophoresis. 21:2000;2509-2521.
    • (2000) Electrophoresis , vol.21 , pp. 2509-2521
    • Berggren, K.1    Chernokalskaya, E.2    Steinberg, T.3    Kemper, C.4    Lopez, M.5    Diwu, Z.6    Haugland, R.7    Patton, W.8
  • 12
    • 0033667456 scopus 로고    scopus 로고
    • A comparison of silver stain and SYPRO ruby protein gel stain with respect to protein detection in two-dimensional gels and identification by peptide mass profiling
    • Lopez M., Berggren K., Chernokalskaya E., Lazarev A., Robinson M., Patton W. A comparison of silver stain and SYPRO ruby protein gel stain with respect to protein detection in two-dimensional gels and identification by peptide mass profiling. Electrophoresis. 21:2000;3673-3683.
    • (2000) Electrophoresis , vol.21 , pp. 3673-3683
    • Lopez, M.1    Berggren, K.2    Chernokalskaya, E.3    Lazarev, A.4    Robinson, M.5    Patton, W.6
  • 13
    • 0034075850 scopus 로고    scopus 로고
    • Making blind robots see; The synergy between fluorescent dyes and imaging devices in automated proteomics
    • Patton W. Making blind robots see; the synergy between fluorescent dyes and imaging devices in automated proteomics. Biotechniques. 28:2000;944-957. This paper describes integration of fluorescence detection technologies into the 2DGE-MS proteomics work environment.
    • (2000) Biotechniques , vol.28 , pp. 944-957
    • Patton, W.1
  • 14
    • 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. A thousand points of light; the application of fluorescence detection technologies to two-dimensional gel electrophoresis and proteomics. Electrophoresis. 21:2000;1123-1144. This review article is a comprehensive summary of 50 years worth of fluorescence and colorimetric detection technologies for polyacrylamide gels and electroblot membranes. The paper demonstrates that fluorescence detection technologies offer a 1000-fold linear dynamic range of quantification.
    • (2000) Electrophoresis , vol.21 , pp. 1123-1144
    • Patton, W.1
  • 15
    • 0036468910 scopus 로고    scopus 로고
    • Rainbow's end: The quest for multiplexed fluorescence quantitative analysis in proteomics
    • Patton W., Beechem J. Rainbow's end: the quest for multiplexed fluorescence quantitative analysis in proteomics. Curr Opin Chem Biol. 6:2002;63-69. A comparison of two fluorescence-based multiplexed detection strategies suitable for 2DGE. Difference gel electrophoresis utilizes a gel-based strategy that is analogous to ICAT, whereas MP employs different fluorophores to highlight different functional attributes of proteins.
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 63-69
    • Patton, W.1    Beechem, J.2
  • 16
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi S., Rist B., Gerber S., Turecek F., Gelb M., Aebersold R. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat Biotechnol. 17:1999;994-999.
    • (1999) Nat Biotechnol , vol.17 , pp. 994-999
    • Gygi, S.1    Rist, B.2    Gerber, S.3    Turecek, F.4    Gelb, M.5    Aebersold, R.6
  • 17
    • 0033679078 scopus 로고    scopus 로고
    • Quantitative proteome analysis. Methods and applications
    • Aebersold R., Rist B., Gygi S. Quantitative proteome analysis. Methods and applications. Ann New York Acad Sci. 919:2000;33-47.
    • (2000) Ann New York Acad Sci , vol.919 , pp. 33-47
    • Aebersold, R.1    Rist, B.2    Gygi, S.3
  • 19
    • 0036049889 scopus 로고    scopus 로고
    • Quantitative protein profiling using two-dimensional gel electrophoresis, isotope coded affinity tag labeling and mass spectrometry
    • in press
    • Smolka M, Zhou H, Aebersold R: Quantitative protein profiling using two-dimensional gel electrophoresis, isotope coded affinity tag labeling and mass spectrometry. Mol Cell Proteomics 2002, in press.
    • (2002) Mol Cell Proteomics
    • Smolka, M.1    Zhou, H.2    Aebersold, R.3
  • 20
    • 0035477025 scopus 로고    scopus 로고
    • Optimization of the isotope-coded affinity tag-labeling procedure for quantitative proteome analysis
    • Smolka M., Zhou H., Purkayastha S., Aebersold R. Optimization of the isotope-coded affinity tag-labeling procedure for quantitative proteome analysis. Anal Biochem. 297:2001;25-31.
    • (2001) Anal Biochem , vol.297 , pp. 25-31
    • Smolka, M.1    Zhou, H.2    Purkayastha, S.3    Aebersold, R.4
  • 21
    • 0002532058 scopus 로고    scopus 로고
    • Current trends in differential expression proteomics: Isotopically coded tags
    • Moseley M. Current trends in differential expression proteomics: isotopically coded tags. Trends Biotechnol. 19:2001;S10-S16. Detailed review of the ICAT method for protein quantification. Thiol-reactive biotin tags are utilized to label two samples, which are subsequently combined, proteolyzed, affinity fractionated and evaluated by MS.
    • (2001) Trends Biotechnol , vol.19
    • Moseley, M.1
  • 22
    • 0036161596 scopus 로고    scopus 로고
    • Mass spectrometry in coupling with affinity capture-release and isotope-coded affinity tags for quantitative protein analysis
    • Turecek F. Mass spectrometry in coupling with affinity capture-release and isotope-coded affinity tags for quantitative protein analysis. J Mass Spectrom. 37:2002;1-14.
    • (2002) J Mass Spectrom , vol.37 , pp. 1-14
    • Turecek, F.1
  • 23
    • 0035499083 scopus 로고    scopus 로고
    • Fractionation of isotopically labeled peptides in quantitative proteomics
    • Zhang R., Sioma C., Wang S., Regnier F. Fractionation of isotopically labeled peptides in quantitative proteomics. Anal Chem. 73:2001;5142-5149.
    • (2001) Anal Chem , vol.73 , pp. 5142-5149
    • Zhang, R.1    Sioma, C.2    Wang, S.3    Regnier, F.4
  • 24
    • 2142856295 scopus 로고    scopus 로고
    • Proteome profiling - Pitfalls and progress
    • Haynes P., Yates J. Proteome profiling - Pitfalls and progress. Yeast. 17:2000;81-87.
    • (2000) Yeast , vol.17 , pp. 81-87
    • Haynes, P.1    Yates, J.2
  • 25
    • 0036463388 scopus 로고    scopus 로고
    • Selective detection of membrane proteins without antibodies: A mass spectrometric version of the western blot
    • in press
    • Arnott D, Kishiyama A, Luis E, Ludlum S, Marsters J, Stults J: Selective detection of membrane proteins without antibodies: a mass spectrometric version of the western blot. Mol Cell Proteomics 2002, in press. Description of a technique for the analysis of specific proteins in complex mixtures using ICAT reagents and MS. The paper demonstrates that the dynamic range of ICAT is roughly 10-fold.
    • (2002) Mol Cell Proteomics
    • Arnott, D.1    Kishiyama, A.2    Luis, E.3    Ludlum, S.4    Marsters, J.5    Stults, J.6
  • 28
    • 0035137205 scopus 로고    scopus 로고
    • Role of alternative splicing in generating isoforms diversity among plasma membrane calcium pumps
    • Strehler E., Zacharias D. Role of alternative splicing in generating isoforms diversity among plasma membrane calcium pumps. Physiol Rev. 81:2001;21-50.
    • (2001) Physiol Rev , vol.81 , pp. 21-50
    • Strehler, E.1    Zacharias, D.2
  • 29
    • 0034789979 scopus 로고    scopus 로고
    • Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry
    • Han D., Eng J., Zhou H., Aebersold R. Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry. Nat Biotechnol. 19:2001;946-951. Comprehensive study of microsomal/mitochondrial proteins detected using the ICAT technique. It is particularly useful to compare the proteins identified in this study with proteins identified by 2DGE/MS from microsomal/mitochondrial databases.
    • (2001) Nat Biotechnol , vol.19 , pp. 946-951
    • Han, D.1    Eng, J.2    Zhou, H.3    Aebersold, R.4
  • 30
    • 0035980117 scopus 로고    scopus 로고
    • Proteomic analysis of the mammalian mitochondrial ribosome. Identification of protein components in the 28S small subunit
    • Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A., Watanabe K. Proteomic analysis of the mammalian mitochondrial ribosome. Identification of protein components in the 28S small subunit. J Biol Chem. 276:2001;33181-33195.
    • (2001) J Biol Chem , vol.276 , pp. 33181-33195
    • Suzuki, T.1    Terasaki, M.2    Takemoto-Hori, C.3    Hanada, T.4    Ueda, T.5    Wada, A.6    Watanabe, K.7
  • 31
    • 0035877697 scopus 로고    scopus 로고
    • Structural compensation for the deficit of rRNA with proteins in the mammalian mitochondrial ribosome. Systematic analysis of protein components of the large ribosomal subunit from mammalian mitochondria
    • Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A., Watanabe K. Structural compensation for the deficit of rRNA with proteins in the mammalian mitochondrial ribosome. Systematic analysis of protein components of the large ribosomal subunit from mammalian mitochondria. J Biol Chem. 276:2001;21724-21736.
    • (2001) J Biol Chem , vol.276 , pp. 21724-21736
    • Suzuki, T.1    Terasaki, M.2    Takemoto-Hori, C.3    Hanada, T.4    Ueda, T.5    Wada, A.6    Watanabe, K.7
  • 32
    • 0031813004 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis of human placental mitochondria and protein identification by mass spectrometry: Toward a human mitochondrial proteome
    • Rabilloud T., Kieffer S., Procaccio V., Louwaggie M., Courchesne P., Patterson S., Martinez P., Garin J., Lunardi J. Two-dimensional electrophoresis of human placental mitochondria and protein identification by mass spectrometry: toward a human mitochondrial proteome. Electrophoresis. 19:1998;1006-1014.
    • (1998) Electrophoresis , vol.19 , pp. 1006-1014
    • Rabilloud, T.1    Kieffer, S.2    Procaccio, V.3    Louwaggie, M.4    Courchesne, P.5    Patterson, S.6    Martinez, P.7    Garin, J.8    Lunardi, J.9
  • 34
    • 0000233053 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis and mass spectrometric identification of mitochondrial proteins from a SH-SY5Y neuroblastoma cell line
    • Scheffler N., Miller S., Carroll A., Anderson C., Davis R., Ghosh S., Gibson B. Two-dimensional electrophoresis and mass spectrometric identification of mitochondrial proteins from a SH-SY5Y neuroblastoma cell line. Mitochondrion. 1:2001;161-179.
    • (2001) Mitochondrion , vol.1 , pp. 161-179
    • Scheffler, N.1    Miller, S.2    Carroll, A.3    Anderson, C.4    Davis, R.5    Ghosh, S.6    Gibson, B.7
  • 35
    • 67651108027 scopus 로고    scopus 로고
    • Analysis of the Arabidopsis mitochondrial proteome
    • Millar H., Sweetlove L., Giege P., Leaver C. Analysis of the Arabidopsis mitochondrial proteome. Plant Physiol. 127:2001;1711-1727.
    • (2001) Plant Physiol , vol.127 , pp. 1711-1727
    • Millar, H.1    Sweetlove, L.2    Giege, P.3    Leaver, C.4
  • 36
    • 85047683107 scopus 로고    scopus 로고
    • Proteomic approach to identify novel mitochondrial proteins in Arabidopsis
    • Kruft V., Eubel H., Jansch L., Werhahn W., Braun H. Proteomic approach to identify novel mitochondrial proteins in Arabidopsis. Plant Physiol. 127:2001;1694-1710.
    • (2001) Plant Physiol , vol.127 , pp. 1694-1710
    • Kruft, V.1    Eubel, H.2    Jansch, L.3    Werhahn, W.4    Braun, H.5
  • 37
    • 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., Muller D., Roberts R., van Oostrum J. Preparative two-dimensional gel electrophoresis at alkaline pH using narrow range immobilized pH gradients. Proteomics. 2:2002;127-134.
    • (2002) Proteomics , vol.2 , pp. 127-134
    • Hoving, S.1    Gerrits, B.2    Voshol, H.3    Muller, D.4    Roberts, R.5    Van Oostrum, J.6
  • 38
    • 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., Madjar J. Very alkaline immobilized pH gradients for two-dimensional electrophoresis of ribosomal and nuclear proteins. Electrophoresis. 18:1997;328-337.
    • (1997) Electrophoresis , vol.18 , pp. 328-337
    • Görg, A.1    Obermaier, C.2    Boguth, G.3    Csordas, A.4    Diaz, J.5    Madjar, J.6
  • 39
    • 0033847227 scopus 로고    scopus 로고
    • Improved sensitivity proteomics by post-harvest alkylation and radioactive labeling of proteins
    • Vuong G., Weiss S., Kammer W., Priemer M., Vingron M., Nordheim A., Cahill M. Improved sensitivity proteomics by post-harvest alkylation and radioactive labeling of proteins. Electrophoresis. 21:2000;2594-2605.
    • (2000) Electrophoresis , vol.21 , pp. 2594-2605
    • Vuong, G.1    Weiss, S.2    Kammer, W.3    Priemer, M.4    Vingron, M.5    Nordheim, A.6    Cahill, M.7
  • 40
    • 0035106351 scopus 로고    scopus 로고
    • Large scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn M., Wolters D., Yates J. Large scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol. 19:2001;242-247.
    • (2001) Nat Biotechnol , vol.19 , pp. 242-247
    • Washburn, M.1    Wolters, D.2    Yates, J.3
  • 41
    • 0037040827 scopus 로고    scopus 로고
    • Applied proteomics: Mitochondrial proteins and effect on function
    • Lopez M., Melov S. Applied proteomics: mitochondrial proteins and effect on function. Circ Res. 90:2002;380-389. Useful summary of strategies and accomplishments from a variety of 2DGE/MS studies of the mitochondrial proteome.
    • (2002) Circ Res , vol.90 , pp. 380-389
    • Lopez, M.1    Melov, S.2
  • 42
    • 0036246088 scopus 로고    scopus 로고
    • Quantitative proteome analysis by solid-phase isotope tagging and mass spectrometry
    • Zhou H., Ranish J., Watts J., Aebersold R. Quantitative proteome analysis by solid-phase isotope tagging and mass spectrometry. Nat Biotechnol. 20:2002;512-515.
    • (2002) Nat Biotechnol , vol.20 , pp. 512-515
    • Zhou, H.1    Ranish, J.2    Watts, J.3    Aebersold, R.4


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