메뉴 건너뛰기




Volumn 21, Issue 3, 2003, Pages 262-267

The application of mass spectrometry to membrane proteomics

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CELLS; GELS; MASS SPECTROMETRY;

EID: 0037337308     PISSN: 10870156     EISSN: None     Source Type: Journal    
DOI: 10.1038/nbt0303-262     Document Type: Review
Times cited : (525)

References (39)
  • 1
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin, E. & Von Heijne, G. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci. 7, 1029-1038 (1998).
    • (1998) Protein Sci. , vol.7 , pp. 1029-1038
    • Wallin, E.1    Von Heijne, G.2
  • 2
    • 0034213573 scopus 로고    scopus 로고
    • Do more complex organisms have a greater proportion of membrane proteins in their genomes?
    • Stevens, T.J. & Arkin, I.T. Do more complex organisms have a greater proportion of membrane proteins in their genomes? Proteins 39, 417-420 (2000).
    • (2000) Proteins , vol.39 , pp. 417-420
    • Stevens, T.J.1    Arkin, I.T.2
  • 4
    • 0035987407 scopus 로고    scopus 로고
    • The post-genomic era of interactive proteomics: Facts and perspectives
    • Auerbach, D., Thaminy, S., Hottiger, M.O. & Stagljar, I. The post-genomic era of interactive proteomics: facts and perspectives. Proteomics 2, 611-623 (2002).
    • (2002) Proteomics , vol.2 , pp. 611-623
    • Auerbach, D.1    Thaminy, S.2    Hottiger, M.O.3    Stagljar, I.4
  • 5
    • 0037305948 scopus 로고    scopus 로고
    • Peptide libraries: At the crossroads of proteomics and bioinformatics
    • Turk, B.E. & Cantley. L.C. Peptide libraries: at the crossroads of proteomics and bioinformatics. Curr. Opin. Chem. Biol. 7, 84-90 (2003).
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 84-90
    • Turk, B.E.1    Cantley, L.C.2
  • 6
    • 0036789265 scopus 로고    scopus 로고
    • Analyzing yeast protein-protein interaction data obtained from different sources
    • Bader G.D. & Hogue C.W. Analyzing yeast protein-protein interaction data obtained from different sources. Nat. Biotechnol. 20, 991-997 (2002).
    • (2002) Nat. Biotechnol. , vol.20 , pp. 991-997
    • Bader, G.D.1    Hogue, C.W.2
  • 7
    • 0033778077 scopus 로고    scopus 로고
    • Membrane proteomics: Use of additive main effects with multiplicative interaction model to classify plasma membrane proteins according to their solubility and electrophoretic properties
    • Santoni, V., Kieffer, S., Desclaux, D., Masson, F. & Rabilloud, T. Membrane proteomics: use of additive main effects with multiplicative interaction model to classify plasma membrane proteins according to their solubility and electrophoretic properties. Electrophoresis 21, 3329-3344 (2000).
    • (2000) Electrophoresis , vol.21 , pp. 3329-3344
    • Santoni, V.1    Kieffer, S.2    Desclaux, D.3    Masson, F.4    Rabilloud, T.5
  • 8
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: Un amour impossible?
    • Santoni, V., Malloy, M. & Rabilloud, T. Membrane proteins and proteomics: un amour impossible? Electrophoresis 21, 1054-1070 (2000).
    • (2000) Electrophoresis , vol.21 , pp. 1054-1070
    • Santoni, V.1    Malloy, M.2    Rabilloud, T.3
  • 9
    • 0037143630 scopus 로고    scopus 로고
    • Integral membrane proteins of the chloroplast envelope: Identification and subcellular localization of new transporters
    • Ferro, M. et al. Integral membrane proteins of the chloroplast envelope: identification and subcellular localization of new transporters. Proc. Natl. Acad. Sci. USA 99, 11487-11492 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11487-11492
    • Ferro, M.1
  • 10
    • 0033773868 scopus 로고    scopus 로고
    • Organic solvent extraction as a versatile procedure to identify hydrophobic chloroplast membrane proteins
    • Ferro, M. et al. Organic solvent extraction as a versatile procedure to identify hydrophobic chloroplast membrane proteins. Electrophoresis 21, 3517-3526 (2002).
    • (2002) Electrophoresis , vol.21 , pp. 3517-3526
    • Ferro, M.1
  • 11
    • 12244289683 scopus 로고    scopus 로고
    • Proteomic analysis of rat brain tissue: Comparison of protocols for two-dimensional gel electrophoresis analysis based on different solubilizing agents
    • Carboni, L., Piubelli, C., Righetti, P.G., Jansson, B. & Domenici, E. Proteomic analysis of rat brain tissue: comparison of protocols for two-dimensional gel electrophoresis analysis based on different solubilizing agents. Electrophoresis 23, 4132-4141 (2002).
    • (2002) Electrophoresis , vol.23 , pp. 4132-4141
    • Carboni, L.1    Piubelli, C.2    Righetti, P.G.3    Jansson, B.4    Domenici, E.5
  • 12
    • 0036857488 scopus 로고    scopus 로고
    • Application of zwitterionic detergents to the solubilization of integral membrane proteins for two-dimensional gel electrophoresis and mass spectrometry
    • Henningsen, R., Gale, B.L., Straub, K.M. & DeNagel, D.C. Application of zwitterionic detergents to the solubilization of integral membrane proteins for two-dimensional gel electrophoresis and mass spectrometry. Proteomics 2, 1479-1488 (2002).
    • (2002) Proteomics , vol.2 , pp. 1479-1488
    • Henningsen, R.1    Gale, B.L.2    Straub, K.M.3    DeNagel, D.C.4
  • 13
    • 0035987523 scopus 로고    scopus 로고
    • Comparison of one-dimensional and two-dimensional gel electrophoresis as a separation tool for proteomic analysis of rat liver microsomes: Cytochromes P450 and other membrane proteins
    • Galeva, N. & Altermann, M. Comparison of one-dimensional and two-dimensional gel electrophoresis as a separation tool for proteomic analysis of rat liver microsomes: cytochromes P450 and other membrane proteins. Proteomics 2, 713-722 (2002).
    • (2002) Proteomics , vol.2 , pp. 713-722
    • Galeva, N.1    Altermann, M.2
  • 14
    • 0034120122 scopus 로고    scopus 로고
    • Proteomic analysis of the human colon carcinoma cell line (LIM 1215): Development of a membrane protein database
    • Simpson, R.J. et al. Proteomic analysis of the human colon carcinoma cell line (LIM 1215): Development of a membrane protein database. Electrophoresis 21, 1707-1732 (2000).
    • (2000) Electrophoresis , vol.21 , pp. 1707-1732
    • Simpson, R.J.1
  • 15
    • 0036668515 scopus 로고    scopus 로고
    • High throughput two-dimensional blue-native electrophoresis: A tool for functional proteomics of mitochondria and signaling complexes
    • Brookes, P.S. et al. High throughput two-dimensional blue-native electrophoresis: a tool for functional proteomics of mitochondria and signaling complexes. Proteomics 2, 969-977 (2002).
    • (2002) Proteomics , vol.2 , pp. 969-977
    • Brookes, P.S.1
  • 16
    • 0036668062 scopus 로고    scopus 로고
    • Mass spectrometric identification of mitochondrial oxidative phosphorylation subunits separated by two-dimensional blue-native polyacrylamide gel electrophoresis
    • Devreese, B., Vanrobaeys, F., Smet, J., Van Beeumen, J. & Van Coster, R. Mass spectrometric identification of mitochondrial oxidative phosphorylation subunits separated by two-dimensional blue-native polyacrylamide gel electrophoresis. Electrophoresis 23, 2525-2533 (2002).
    • (2002) Electrophoresis , vol.23 , pp. 2525-2533
    • Devreese, B.1    Vanrobaeys, F.2    Smet, J.3    Van Beeumen, J.4    Van Coster, R.5
  • 17
    • 0033662185 scopus 로고    scopus 로고
    • Postelectrophoretic staining of proteins separated by two-dimensional gel electrophoresis using SYPRO dyes
    • Yan, J.X., Harry, R.A., Spibey, C. & Dunn, M.J. Postelectrophoretic staining of proteins separated by two-dimensional gel electrophoresis using SYPRO dyes. Electrophoresis 21, 3657-3665 (2000).
    • (2000) Electrophoresis , vol.21 , pp. 3657-3665
    • Yan, J.X.1    Harry, R.A.2    Spibey, C.3    Dunn, M.J.4
  • 18
    • 0035403371 scopus 로고    scopus 로고
    • A new silver staining apparatus and procedure for matrix-assisted laser desorption/ionization-time of flight analysis of proteins after two-dimensional electrophoresis
    • Sinha, R, Poland, J., Schnolzer, M. & Rabilloud, T. A new silver staining apparatus and procedure for matrix-assisted laser desorption/ionization-time of flight analysis of proteins after two-dimensional electrophoresis. Proteomics 1, 835-840 (2001).
    • (2001) Proteomics , vol.1 , pp. 835-840
    • Sinha, R.1    Poland, J.2    Schnolzer, M.3    Rabilloud, T.4
  • 19
    • 0036127937 scopus 로고    scopus 로고
    • Improved in-gel approaches to generate peptide maps of integral membrane proteins with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • van Montfort, B.A., Canas, B., Duurkens, R., Godovac-Zimmermann, J. & Robillard, G.T. Improved in-gel approaches to generate peptide maps of integral membrane proteins with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. J. Mass Spectrom. 37, 322-330 (2002).
    • (2002) J. Mass Spectrom. , vol.37 , pp. 322-330
    • Van Montfort, B.A.1    Canas, B.2    Duurkens, R.3    Godovac-Zimmermann, J.4    Robillard, G.T.5
  • 20
    • 0037056021 scopus 로고    scopus 로고
    • Combined in-gel tryptic digestion and CNBr cleavage for the generation of peptide maps of an integral membrane protein with MALDI-TOF mass spectrometry
    • van Montfort, B.A. et al. Combined in-gel tryptic digestion and CNBr cleavage for the generation of peptide maps of an integral membrane protein with MALDI-TOF mass spectrometry. Biochem. Biophys. Acta 1555, 111-115 (2002).
    • (2002) Biochem. Biophys. Acta , vol.1555 , pp. 111-115
    • Van Montfort, B.A.1
  • 21
    • 0034789979 scopus 로고    scopus 로고
    • Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry
    • Han, D.K., Eng, J., Zhou, H., & Aebersold, R. Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry. Nat. Biotechnol. 19, 946-951 (2002).
    • (2002) Nat. Biotechnol. , vol.19 , pp. 946-951
    • Han, D.K.1    Eng, J.2    Zhou, H.3    Aebersold, R.4
  • 22
    • 0036665518 scopus 로고    scopus 로고
    • Enrichment of integral membrane proteins for proteomic analysis using liquid chromatography-tandem mass spectrometry
    • Blonder, J., Goshe, M.B., Moore, R.J., Pasa-Tolic, L., Masselon, C.D., Lipton, M.S. & Smith, R.D. Enrichment of integral membrane proteins for proteomic analysis using liquid chromatography-tandem mass spectrometry. J. Prot. Res. 1, 351-360 (2002).
    • (2002) J. Prot. Res. , vol.1 , pp. 351-360
    • Blonder, J.1    Goshe, M.B.2    Moore, R.J.3    Pasa-Tolic, L.4    Masselon, C.D.5    Lipton, M.S.6    Smith, R.D.7
  • 23
    • 0012253253 scopus 로고    scopus 로고
    • Affinity labeling of highly hydrophobic integral membrane proteins for proteome-wide analysis
    • in press
    • Goshe, M.B., Blonder, J., & Smith, R.D. Affinity labeling of highly hydrophobic integral membrane proteins for proteome-wide analysis. J. Prot. Res., in press (2003).
    • (2003) J. Prot. Res.
    • Goshe, M.B.1    Blonder, J.2    Smith, R.D.3
  • 24
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M.P., Wolters,D. & Yates III, J.R. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 19, 242-247 (2001).
    • (2001) Nat. Biotechnol. , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates J.R. III3
  • 25
    • 0036246088 scopus 로고    scopus 로고
    • Quantitative proteome analysis by solid-phase isotope tagging and mass spectrometry
    • Zhou, H., Ranish, J.A., Watts, J.D., & Aebersold, R. Quantitative proteome analysis by solid-phase isotope tagging and mass spectrometry. Nat. Biotechnol. 20, 512-515 (2002).
    • (2002) Nat. Biotechnol. , vol.20 , pp. 512-515
    • Zhou, H.1    Ranish, J.A.2    Watts, J.D.3    Aebersold, R.4
  • 26
    • 0038561131 scopus 로고    scopus 로고
    • A method for the comprehensive proteomicanalysis of membrane proteins: Identification, modifications, and topology
    • in press
    • Wu, C.C., MacCoss, M.J., Howell, K.E. & Yates III, J.R. A method for the comprehensive proteomic analysis of membrane proteins: identification, modifications, and topology. Nat. Biotechnol., in press (2003).
    • (2003) Nat. Biotechnol.
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Yates J.R. III4
  • 27
    • 0020071663 scopus 로고
    • Hepatic Golgi fractions resolved into membrane and content subfractions
    • Howell, K.E. & Palade, G.E. Hepatic Golgi fractions resolved into membrane and content subfractions. J. Cell Biol. 92, 822-832 (1982).
    • (1982) J. Cell Biol. , vol.92 , pp. 822-832
    • Howell, K.E.1    Palade, G.E.2
  • 28
    • 0002739166 scopus 로고    scopus 로고
    • Posttranslational modifications
    • Angeletti, R.H. (ed.). Academic Press, San Diego, CA
    • Gudepu, R.G. & Wold, F. Posttranslational modifications. in Proteins: Analysis and Design. Angeletti, R.H. (ed.). 121-207 (Academic Press, San Diego, CA; 1998).
    • (1998) Proteins: Analysis and Design , pp. 121-207
    • Gudepu, R.G.1    Wold, F.2
  • 29
    • 0034681905 scopus 로고    scopus 로고
    • Proteomics on full-length membrane proteins using mass spectrometry
    • le Coutre, J. et al. Proteomics on full-length membrane proteins using mass spectrometry. Biochemistry 39, 4237-4242 (2000).
    • (2000) Biochemistry , vol.39 , pp. 4237-4242
    • Le Coutre, J.1
  • 30
    • 0012252011 scopus 로고    scopus 로고
    • Full subunit converage liquid chromatography electrospray ionization mass spectrometry (LCMS+) of an oligomeric membrane protein
    • Whitelegge, J.P., Zhang, H., Aguilera, R., Taylor, R.M. & Cramer, W.A. Full subunit converage liquid chromatography electrospray ionization mass spectrometry (LCMS+) of an oligomeric membrane protein. Mol. Cell. Proteomics 1, 816-827 (2002).
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 816-827
    • Whitelegge, J.P.1    Zhang, H.2    Aguilera, R.3    Taylor, R.M.4    Cramer, W.A.5
  • 31
    • 0036051481 scopus 로고    scopus 로고
    • The chloroplast grana defined by intact mass measurements from liquid chromatography mass spectrometry
    • Gómez, S.M., Nishio, J.N., Faull, K.F. & Whitelegge, J.P. The chloroplast grana defined by intact mass measurements from liquid chromatography mass spectrometry. Mol. Cell. Proteomics 1, 46-59 (2002).
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 46-59
    • Gómez, S.M.1    Nishio, J.N.2    Faull, K.F.3    Whitelegge, J.P.4
  • 32
    • 0034669677 scopus 로고    scopus 로고
    • A robust, detergent-friendly method for mass spectrophometric analysis of integral membrane proteins
    • Cadene, M. & Chait, B.T. A robust, detergent-friendly method for mass spectrophometric analysis of integral membrane proteins. Anal. Chem. 72, 5655-5658 (2000).
    • (2000) Anal. Chem. , vol.72 , pp. 5655-5658
    • Cadene, M.1    Chait, B.T.2
  • 33
    • 0036645727 scopus 로고    scopus 로고
    • Processing complex mixtures of intact proteins for direct analysis by mass spectrometry
    • Meng, F., Cargile, B.J., Patri, S.M., Johnson, J.R., McLoughlin, S.M. & Kelleher, N.L. Processing complex mixtures of intact proteins for direct analysis by mass spectrometry. Anal. Chem. 74, 2923-2929 (2002).
    • (2002) Anal. Chem. , vol.74 , pp. 2923-2929
    • Meng, F.1    Cargile, B.J.2    Patri, S.M.3    Johnson, J.R.4    McLoughlin, S.M.5    Kelleher, N.L.6
  • 34
    • 0035067251 scopus 로고    scopus 로고
    • Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome
    • Oda, Y., Nagasu, T. & Chait, B.D. Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome. Nat. Biotechnol. 19, 379-382 (2001).
    • (2001) Nat. Biotechnol. , vol.19 , pp. 379-382
    • Oda, Y.1    Nagasu, T.2    Chait, B.D.3
  • 35
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • Zhou, H., Watts, J.D. & Aebersold, R. A systematic approach to the analysis of protein phosphorylation. Nat. Biotechnol. 19, 375-378 (2001).
    • (2001) Nat. Biotechnol. , vol.19 , pp. 375-378
    • Zhou, H.1    Watts, J.D.2    Aebersold, R.3
  • 36
    • 0035356565 scopus 로고    scopus 로고
    • Phosphoprotein isotope-coded affinity tag approach for isolating and quantitating phosphopeptides in proteome-wide analysis
    • Goshe, M.B. et al. Phosphoprotein isotope-coded affinity tag approach for isolating and quantitating phosphopeptides in proteome-wide analysis. Anal. Chem. 73, 2578-2586 (2001).
    • (2001) Anal. Chem. , vol.73 , pp. 2578-2586
    • Goshe, M.B.1
  • 37
    • 0036198435 scopus 로고    scopus 로고
    • Phosphoproteome analysis by mass spectrometry and its application to Saccaromyces cerevisiae
    • Ficarro, S.B. et al. Phosphoproteome analysis by mass spectrometry and its application to Saccaromyces cerevisiae. Nat. Biotechnol. 20, 301-305 (2002).
    • (2002) Nat. Biotechnol. , vol.20 , pp. 301-305
    • Ficarro, S.B.1
  • 38
    • 18444391517 scopus 로고    scopus 로고
    • Shotgun identification of protein modifications from protein complexes and lens tissue
    • MacCoss, M.J. et al. Shotgun identification of protein modifications from protein complexes and lens tissue. Proc. Natl. Acad. Sci. USA 99, 7900-7905 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7900-7905
    • MacCoss, M.J.1
  • 39
    • 0035843079 scopus 로고    scopus 로고
    • Projection structure of a CICtype chloride channel at 6.5 Å resolution
    • Mindell, J.A., Maduke, M., Miller, C. & Grigorieff, N. Projection structure of a CICtype chloride channel at 6.5 Å resolution. Nature 409, 219-223 (2002).
    • (2002) Nature , vol.409 , pp. 219-223
    • Mindell, J.A.1    Maduke, M.2    Miller, C.3    Grigorieff, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.