메뉴 건너뛰기




Volumn 10, Issue 2, 2011, Pages

Overcoming key technological challenges in using mass spectrometry for mapping cell surfaces in tissues

Author keywords

[No Author keywords available]

Indexed keywords

LIPID; MEMBRANE PROTEIN; TRYPSIN;

EID: 79953192195     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.R110.000935     Document Type: Review
Times cited : (40)

References (134)
  • 1
    • 34248583886 scopus 로고    scopus 로고
    • MAP kinase signalling pathways in cancer
    • DOI 10.1038/sj.onc.1210421, PII 1210421
    • Dhillon, A. S., Hagan, S., Rath, O., and Kolch, W. (2007) MAP kinase signalling pathways in cancer. Oncogene 26, 3279-3290 (Pubitemid 46763021)
    • (2007) Oncogene , vol.26 , Issue.22 , pp. 3279-3290
    • Dhillon, A.S.1    Hagan, S.2    Rath, O.3    Kolch, W.4
  • 3
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin, E., and von Heijne, G. (1998) Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci. 7, 1029-1038 (Pubitemid 28216544)
    • (1998) Protein Science , vol.7 , Issue.4 , pp. 1029-1038
    • Wallin, E.1    Von Heijne, G.2
  • 4
    • 0037657949 scopus 로고    scopus 로고
    • Membrane proteins ride shotgun
    • Rabilloud, T. (2003) Membrane proteins ride shotgun. Nat. Biotechnol. 21, 508-510
    • (2003) Nat. Biotechnol. , vol.21 , pp. 508-510
    • Rabilloud, T.1
  • 5
    • 0020630407 scopus 로고
    • Capillary endothelial cell cultures: Phenotypic modulation by matrix components
    • Madri, J. A., and Williams, S. K. (1983) Capillary endothelial cell cultures: phenotypic modulation by matrix components. J. Cell Biol. 97, 153-165
    • (1983) J. Cell Biol. , vol.97 , pp. 153-165
    • Madri, J.A.1    Williams, S.K.2
  • 6
    • 3543023287 scopus 로고    scopus 로고
    • Direct proteomic mapping of the lung microvascular endothelial cell surface in vivo and in cell culture
    • Durr, E., Yu, J., Krasinska, K. M., Carver, L. A., Yates, J. R., Testa, J. E., Oh, P., and Schnitzer, J. E. (2004) Direct proteomic mapping of the lung microvascular endothelial cell surface in vivo and in cell culture. Nat. Biotechnol. 22, 985-992
    • (2004) Nat. Biotechnol. , vol.22 , pp. 985-992
    • Durr, E.1    Yu, J.2    Krasinska, K.M.3    Carver, L.A.4    Yates, J.R.5    Testa, J.E.6    Oh, P.7    Schnitzer, J.E.8
  • 7
    • 34250315638 scopus 로고    scopus 로고
    • The antibody-mediated targeted delivery of interleukin-15 and GM-CSF to the tumor neovasculature inhibits tumor growth and metastasis
    • DOI 10.1158/0008-5472.CAN-07-0283
    • Kaspar, M., Trachsel, E., and Neri, D. (2007) The antibody-mediated targeted delivery of interleukin-15 and GM-CSF to the tumor neovasculature inhibits tumor growth and metastasis. Cancer Res. 67, 4940-4948 (Pubitemid 46910202)
    • (2007) Cancer Research , vol.67 , Issue.10 , pp. 4940-4948
    • Kaspar, M.1    Trachsel, E.2    Neri, D.3
  • 8
    • 2942529235 scopus 로고    scopus 로고
    • Subtractive proteomic mapping of the endothelial surface in lung and solid tumours for tissue-specific therapy
    • Oh, P., Li, Y., Yu, J., Durr, E., Krasinska, K. M., Carver, L. A., Testa, J. E., and Schnitzer, J. E. (2004) Subtractive proteomic mapping of the endothelial surface in lung and solid tumours for tissue-specific therapy. Nature 429, 629-635
    • (2004) Nature , vol.429 , pp. 629-635
    • Oh, P.1    Li, Y.2    Yu, J.3    Durr, E.4    Krasinska, K.M.5    Carver, L.A.6    Testa, J.E.7    Schnitzer, J.E.8
  • 10
    • 0042386124 scopus 로고    scopus 로고
    • Caveolae: Mining little caves for new cancer targets
    • Carver, L. A., and Schnitzer, J. E. (2003) Caveolae: mining little caves for new cancer targets. Nat. Rev. Cancer 3, 571-581
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 571-581
    • Carver, L.A.1    Schnitzer, J.E.2
  • 11
    • 20344367537 scopus 로고    scopus 로고
    • Tumour vascular targeting
    • Neri, D., and Bicknell, R. (2005) Tumour vascular targeting. Nat. Rev. Cancer 5, 436-446
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 436-446
    • Neri, D.1    Bicknell, R.2
  • 12
    • 33745946236 scopus 로고    scopus 로고
    • Use of magnetic beads with immobilized monoclonal antibodies for isolation of highly pure plasma membranes
    • DOI 10.1002/elps.200600059
    • Lawson, E. L., Clifton, J. G., Huang, F., Li, X., Hixson, D. C., and Josic, D. (2006) Use of magnetic beads with immobilized monoclonal antibodies for isolation of highly pure plasma membranes. Electrophoresis 27, 2747-2758 (Pubitemid 44057524)
    • (2006) Electrophoresis , vol.27 , Issue.13 , pp. 2747-2758
    • Lawson, E.L.1    Clifton, J.G.2    Huang, F.3    Li, X.4    Hixson, D.C.5    Josic, D.6
  • 13
    • 10644268451 scopus 로고    scopus 로고
    • Zooming in: Fractionation strategies in proteomics
    • Stasyk, T., and Huber, L. A. (2004) Zooming in: fractionation strategies in proteomics. Proteomics 4, 3704-3716
    • (2004) Proteomics , vol.4 , pp. 3704-3716
    • Stasyk, T.1    Huber, L.A.2
  • 14
    • 33645795446 scopus 로고    scopus 로고
    • Modification-specific proteomics of plasma membrane proteins: Identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment
    • Elortza, F., Mohammed, S., Bunkenborg, J., Foster, L. J., Nühse, T. S., Brodbeck, U., Peck, S. C., and Jensen, O. N. (2006) Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment. J. Proteome Res. 5, 935-943
    • (2006) J. Proteome Res. , vol.5 , pp. 935-943
    • Elortza, F.1    Mohammed, S.2    Bunkenborg, J.3    Foster, L.J.4    Nühse, T.S.5    Brodbeck, U.6    Peck, S.C.7    Jensen, O.N.8
  • 16
    • 34347234182 scopus 로고    scopus 로고
    • Shotgun analysis of integral membrane proteins facilitated by elevated temperature
    • Speers, A. E., Blackler, A. R., and Wu, C. C. (2007) Shotgun analysis of integral membrane proteins facilitated by elevated temperature. Anal. Chem. 79, 4613-4620
    • (2007) Anal. Chem. , vol.79 , pp. 4613-4620
    • Speers, A.E.1    Blackler, A.R.2    Wu, C.C.3
  • 17
    • 42049098165 scopus 로고    scopus 로고
    • Shedding & shaving: Disclosure of proteomic expressions on a bacterial face
    • Tjalsma, H., Lambooy, L., Hermans, P. W., and Swinkels, D. W. (2008) Shedding & shaving: disclosure of proteomic expressions on a bacterial face. Proteomics 8, 1415-1428
    • (2008) Proteomics , vol.8 , pp. 1415-1428
    • Tjalsma, H.1    Lambooy, L.2    Hermans, P.W.3    Swinkels, D.W.4
  • 18
    • 34547182806 scopus 로고    scopus 로고
    • Isolation of signal transduction complexes using biotin and crosslinking methodologies
    • DOI 10.1002/pmic.200700219
    • Freed, J. K., Smith, J. R., Li, P., and Greene, A. S. (2007) Isolation of signal transduction complexes using biotin and crosslinking methodologies. Proteomics 7, 2371-2374 (Pubitemid 47121529)
    • (2007) Proteomics , vol.7 , Issue.14 , pp. 2371-2374
    • Freed, J.K.1    Smith, J.R.2    Li, P.3    Greene, A.S.4
  • 19
    • 58549118993 scopus 로고    scopus 로고
    • Photocrosslinking and click chemistry enable the specific detection of proteins interacting with phospholipids at the membrane interface
    • Gubbens, J., Ruijter, E., de Fays, L. E., Damen, J. M., de Kruijff, B., Slijper, M., Rijkers, D. T., Liskamp, R. M., and de Kroon, A. I. (2009) Photocrosslinking and click chemistry enable the specific detection of proteins interacting with phospholipids at the membrane interface. Chem. Biol. 16, 3-14
    • (2009) Chem. Biol. , vol.16 , pp. 3-14
    • Gubbens, J.1    Ruijter, E.2    De Fays, L.E.3    Damen, J.M.4    De Kruijff, B.5    Slijper, M.6    Rijkers, D.T.7    Liskamp, R.M.8    De Kroon, A.I.9
  • 20
    • 0016835175 scopus 로고
    • Basolateral plasma membranes of intestinal epithelial cells. Identification by lactoperoxidase-catalysed iodination and isolation after density perturbation with digitonin
    • Lewis, B. A., Elkin, A., Michell, R. H., and Coleman, R. (1975) Basolateral plasma membranes of intestinal epithelial cells. Identification by lactoperoxidase-catalysed iodination and isolation after density perturbation with digitonin. Biochem. J. 152, 71-84
    • (1975) Biochem. J. , vol.152 , pp. 71-84
    • Lewis, B.A.1    Elkin, A.2    Michell, R.H.3    Coleman, R.4
  • 21
    • 0018665129 scopus 로고
    • Isolation of radio-iodinated apical and basal-lateral plasma membranes of toad bladder epithelium
    • Rodriguez, H. J., and Edelman, I. S. (1979) Isolation of radio-iodinated apical and basal-lateral plasma membranes of toad bladder epithelium. J. Membr. Biol. 45, 215-232
    • (1979) J. Membr. Biol. , vol.45 , pp. 215-232
    • Rodriguez, H.J.1    Edelman, I.S.2
  • 22
    • 0002820899 scopus 로고
    • Albumin interacts specifically with a 60-kDa microvascular endothelial glycoprotein
    • Schnitzer, J. E., Carley, W. W., and Palade, G. E. (1988) Albumin interacts specifically with a 60-kDa microvascular endothelial glycoprotein. Proc. Natl. Acad. Sci. U.S.A. 85, 6773-6777
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 6773-6777
    • Schnitzer, J.E.1    Carley, W.W.2    Palade, G.E.3
  • 23
    • 0026608797 scopus 로고
    • gp60 is an albumin-binding glycoprotein expressed by continuous endothelium involved in albumin transcytosis
    • Schnitzer, J. E. (1992) gp60 is an albumin-binding glycoprotein expressed by continuous endothelium involved in albumin transcytosis. Am. J. Physiol. Heart Circ. Physiol. 262, H246-H254
    • (1992) Am. J. Physiol. Heart Circ. Physiol. , vol.262
    • Schnitzer, J.E.1
  • 24
    • 0024989722 scopus 로고
    • Lectin analysis of common glycoproteins detected on the surface of continuous microvascular endothelium in situ and in culture: Identification of sialoglycoproteins
    • Schnitzer, J. E., Shen, C. P., and Palade, G. E. (1990) Lectin analysis of common glycoproteins detected on the surface of continuous microvascular endothelium in situ and in culture: identification of sialoglycoproteins. Eur. J. Cell Biol. 52, 241-251
    • (1990) Eur. J. Cell Biol. , vol.52 , pp. 241-251
    • Schnitzer, J.E.1    Shen, C.P.2    Palade, G.E.3
  • 25
    • 0025204771 scopus 로고
    • Molecular mapping of pulmonary endothelial membrane glycoproteins of the intact rabbit lung
    • Merker, M. P., Carley, W. W., and Gillis, C. N. (1990) Molecular mapping of pulmonary endothelial membrane glycoproteins of the intact rabbit lung. FASEB J. 4, 3040-3048
    • (1990) FASEB J. , vol.4 , pp. 3040-3048
    • Merker, M.P.1    Carley, W.W.2    Gillis, C.N.3
  • 26
    • 45549091555 scopus 로고    scopus 로고
    • The identification and characterization of membranome components
    • Ghosh, D., Beavis, R. C., and Wilkins, J. A. (2008) The identification and characterization of membranome components. J. Proteome Res. 7, 1572-1583
    • (2008) J. Proteome Res. , vol.7 , pp. 1572-1583
    • Ghosh, D.1    Beavis, R.C.2    Wilkins, J.A.3
  • 27
    • 51049087078 scopus 로고    scopus 로고
    • Preparation of a high-performance multi-lectin affinity chromatography (HP-M-LAC) adsorbent for the analysis of human plasma glycoproteins
    • Kullolli, M., Hancock, W. S., and Hincapie, M. (2008) Preparation of a high-performance multi-lectin affinity chromatography (HP-M-LAC) adsorbent for the analysis of human plasma glycoproteins. J. Sep. Sci. 31, 2733-2739
    • (2008) J. Sep. Sci. , vol.31 , pp. 2733-2739
    • Kullolli, M.1    Hancock, W.S.2    Hincapie, M.3
  • 28
    • 50449090546 scopus 로고    scopus 로고
    • Glycoproteomics and glycomics investigation of membrane N-glycosylproteins from human colon carcinoma cells
    • Vercoutter-Edouart, A. S., Slomianny, M. C., Dekeyzer-Beseme, O., Haeuw, J. F., and Michalski, J. C. (2008) Glycoproteomics and glycomics investigation of membrane N-glycosylproteins from human colon carcinoma cells. Proteomics 8, 3236-3256
    • (2008) Proteomics , vol.8 , pp. 3236-3256
    • Vercoutter-Edouart, A.S.1    Slomianny, M.C.2    Dekeyzer-Beseme, O.3    Haeuw, J.F.4    Michalski, J.C.5
  • 29
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • Zhang, H., Li, X. J., Martin, D. B., and Aebersold, R. (2003) Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat. Biotechnol. 21, 660-666
    • (2003) Nat. Biotechnol. , vol.21 , pp. 660-666
    • Zhang, H.1    Li, X.J.2    Martin, D.B.3    Aebersold, R.4
  • 31
    • 34547767471 scopus 로고    scopus 로고
    • Tags for the stable isotopic labeling of carbohydrates and quantitative analysis by mass spectrometry
    • Bowman, M. J., and Zaia, J. (2007) Tags for the stable isotopic labeling of carbohydrates and quantitative analysis by mass spectrometry. Anal. Chem. 79, 5777-5784
    • (2007) Anal. Chem. , vol.79 , pp. 5777-5784
    • Bowman, M.J.1    Zaia, J.2
  • 32
    • 4444368182 scopus 로고    scopus 로고
    • Method for the comparative glycomic analyses of O-linked, mucin-type oligosaccharides
    • Xie, Y., Liu, J., Zhang, J., Hedrick, J. L., and Lebrilla, C. B. (2004) Method for the comparative glycomic analyses of O-linked, mucin-type oligosaccharides. Anal. Chem. 76, 5186-5197
    • (2004) Anal. Chem. , vol.76 , pp. 5186-5197
    • Xie, Y.1    Liu, J.2    Zhang, J.3    Hedrick, J.L.4    Lebrilla, C.B.5
  • 34
    • 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., Steen, H., Pandey, A., and Mann, M. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 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    Steen, H.5    Pandey, A.6    Mann, M.7
  • 35
    • 0019892169 scopus 로고
    • Growth of human malaria parasites in biotinylated erythrocytes
    • Simpson, G. L., Born, J. L., and Cain, G. (1981) Growth of human malaria parasites in biotinylated erythrocytes. Mol. Biochem. Parasitol. 4, 243-253
    • (1981) Mol. Biochem. Parasitol. , vol.4 , pp. 243-253
    • Simpson, G.L.1    Born, J.L.2    Cain, G.3
  • 36
    • 0039485212 scopus 로고
    • Plant plasma membrane proteins: II. biotinylation of Daucus carota protoplasts and detection of plasma membrane polypeptides after SDS-PAGE
    • Grimes, H. D., Slay, R. M., and Hodges, T. K. (1988) Plant plasma membrane proteins: II. biotinylation of Daucus carota protoplasts and detection of plasma membrane polypeptides after SDS-PAGE. Plant Physiol. 88, 444-449
    • (1988) Plant Physiol. , vol.88 , pp. 444-449
    • Grimes, H.D.1    Slay, R.M.2    Hodges, T.K.3
  • 37
    • 0024520841 scopus 로고
    • Integral and peripheral protein composition of the apical and basolateral membrane domains in MDCK cells
    • Sargiacomo, M., Lisanti, M., Graeve, L., Le Bivic, A., and Rodriguez-Boulan, E. (1989) Integral and peripheral protein composition of the apical and basolateral membrane domains in MDCK cells. J. Membr. Biol. 107, 277-286
    • (1989) J. Membr. Biol. , vol.107 , pp. 277-286
    • Sargiacomo, M.1    Lisanti, M.2    Graeve, L.3    Le Bivic, A.4    Rodriguez-Boulan, E.5
  • 38
    • 0347134596 scopus 로고    scopus 로고
    • Affinity enrichment of plasma membrane for proteomics analysis
    • DOI 10.1002/elps.200305569
    • Zhang, W., Zhou, G., Zhao, Y., White, M. A., and Zhao, Y. (2003) Affinity enrichment of plasma membrane for proteomics analysis. Electrophoresis 24, 2855-2863 (Pubitemid 38089077)
    • (2003) Electrophoresis , vol.24 , Issue.16 , pp. 2855-2863
    • Zhang, W.1    Zhou, G.2    Zhao, Y.3    White, M.A.4    Zhao, Y.5
  • 39
    • 1842529218 scopus 로고    scopus 로고
    • Proteomic analysis of integral plasma membrane proteins
    • Zhao, Y., Zhang, W., Kho, Y., and Zhao, Y. (2004) Proteomic analysis of integral plasma membrane proteins. Anal. Chem. 76, 1817-1823
    • (2004) Anal. Chem. , vol.76 , pp. 1817-1823
    • Zhao, Y.1    Zhang, W.2    Kho, Y.3    Zhao, Y.4
  • 40
    • 55749099458 scopus 로고    scopus 로고
    • Biotinylation reagents for the study of cell surface proteins
    • Elia, G. (2008) Biotinylation reagents for the study of cell surface proteins. Proteomics 8, 4012-4024
    • (2008) Proteomics , vol.8 , pp. 4012-4024
    • Elia, G.1
  • 42
    • 0032567415 scopus 로고    scopus 로고
    • In situ flow activates endothelial nitric oxide synthase in luminal caveolae of endothelium with rapid caveolin dissociation and calmodulin association
    • Rizzo, V., McIntosh, D. P., Oh, P., and Schnitzer, J. E. (1998) In situ flow activates endothelial nitric oxide synthase in luminal caveolae of endothelium with rapid caveolin dissociation and calmodulin association. J. Biol. Chem. 273, 34724-34729
    • (1998) J. Biol. Chem. , vol.273 , pp. 34724-34729
    • Rizzo, V.1    McIntosh, D.P.2    Oh, P.3    Schnitzer, J.E.4
  • 44
    • 18744399322 scopus 로고    scopus 로고
    • In vivo protein biotinylation for identification of organ-specific antigens accessible from the vasculature
    • Rybak, J. N., Ettorre, A., Kaissling, B., Giavazzi, R., Neri, D., and Elia, G. (2005) In vivo protein biotinylation for identification of organ-specific antigens accessible from the vasculature. Nat. Methods 2, 291-298
    • (2005) Nat. Methods , vol.2 , pp. 291-298
    • Rybak, J.N.1    Ettorre, A.2    Kaissling, B.3    Giavazzi, R.4    Neri, D.5    Elia, G.6
  • 45
    • 0026707750 scopus 로고
    • Isolation and partial characterization of the luminal plasmalemma of microvascular endothelium from rat lungs
    • Jacobson, B. S., Schnitzer, J. E., McCaffery, M., and Palade, G. E. (1992) Isolation and partial characterization of the luminal plasmalemma of microvascular endothelium from rat lungs. Eur. J. Cell Biol. 58, 296-306
    • (1992) Eur. J. Cell Biol. , vol.58 , pp. 296-306
    • Jacobson, B.S.1    Schnitzer, J.E.2    McCaffery, M.3    Palade, G.E.4
  • 46
    • 0030115683 scopus 로고    scopus 로고
    • Identification of endothelial cell-surface proteins as targets for diagnosis and treatment of disease
    • Jacobson, B. S., Stolz, D. B., and Schnitzer, J. E. (1996) Identification of endothelial cell-surface proteins as targets for diagnosis and treatment of disease. Nat. Med. 2, 482-484
    • (1996) Nat. Med. , vol.2 , pp. 482-484
    • Jacobson, B.S.1    Stolz, D.B.2    Schnitzer, J.E.3
  • 47
    • 67650567049 scopus 로고    scopus 로고
    • Enhancing identifications of lipid-embedded proteins by mass spectrometry for improved mapping of endothelial plasma membranes in vivo
    • Li, Y., Yu, J., Wang, Y., Griffin, N. M., Long, F., Shore, S., Oh, P., and Schnitzer, J. E. (2009) Enhancing identifications of lipid-embedded proteins by mass spectrometry for improved mapping of endothelial plasma membranes in vivo. Mol. Cell. Proteomics 8, 1219-1235
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 1219-1235
    • Li, Y.1    Yu, J.2    Wang, Y.3    Griffin, N.M.4    Long, F.5    Shore, S.6    Oh, P.7    Schnitzer, J.E.8
  • 48
    • 0037133155 scopus 로고    scopus 로고
    • Targeting endothelium and its dynamic caveolae for tissue-specific transcytosis in vivo: A pathway to overcome cell barriers to drug and gene delivery
    • McIntosh, D. P., Tan, X. Y., Oh, P., and Schnitzer, J. E. (2002) Targeting endothelium and its dynamic caveolae for tissue-specific transcytosis in vivo: a pathway to overcome cell barriers to drug and gene delivery. Proc. Natl. Acad. Sci. U.S.A. 99, 1996-2001
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 1996-2001
    • McIntosh, D.P.1    Tan, X.Y.2    Oh, P.3    Schnitzer, J.E.4
  • 51
    • 0029082412 scopus 로고
    • Separation of caveolae from associated microdomains of GPI-anchored proteins
    • Schnitzer, J. E., McIntosh, D. P., Dvorak, A. M., Liu, J., and Oh, P. (1995) Separation of caveolae from associated microdomains of GPI-anchored proteins. Science 269, 1435-1439
    • (1995) Science , vol.269 , pp. 1435-1439
    • Schnitzer, J.E.1    McIntosh, D.P.2    Dvorak, A.M.3    Liu, J.4    Oh, P.5
  • 52
    • 0025129829 scopus 로고
    • A major endothelial plasmalemmal sialoglycoprotein, gp60, is immunologically related to glycophorin
    • Schnitzer, J. E., Ulmer, J. B., and Palade, G. E. (1990) A major endothelial plasmalemmal sialoglycoprotein, gp60, is immunologically related to glycophorin. Proc. Natl. Acad. Sci. U.S.A. 87, 6843-6847
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 6843-6847
    • Schnitzer, J.E.1    Ulmer, J.B.2    Palade, G.E.3
  • 53
    • 58149360475 scopus 로고    scopus 로고
    • Ubiquitous yet distinct expression of podocalyxin on vascular surfaces in normal and tumor tissues in the rat
    • Testa, J. E., Chrastina, A., Li, Y., Oh, P., and Schnitzer, J. E. (2009) Ubiquitous yet distinct expression of podocalyxin on vascular surfaces in normal and tumor tissues in the rat. J. Vasc. Res. 46, 311-324
    • (2009) J. Vasc. Res. , vol.46 , pp. 311-324
    • Testa, J.E.1    Chrastina, A.2    Li, Y.3    Oh, P.4    Schnitzer, J.E.5
  • 56
    • 0021112527 scopus 로고
    • Coating cells with colloidal silica for high yield isolation of plasma membrane sheets and identification of transmembrane proteins
    • Chaney, L. K., and Jacobson, B. S. (1983) Coating cells with colloidal silica for high yield isolation of plasma membrane sheets and identification of transmembrane proteins. J. Biol. Chem. 258, 10062-10072
    • (1983) J. Biol. Chem. , vol.258 , pp. 10062-10072
    • Chaney, L.K.1    Jacobson, B.S.2
  • 57
    • 0029809310 scopus 로고    scopus 로고
    • Role of GTP hydrolysis in fission of caveolae directly from plasma membranes
    • DOI 10.1126/science.274.5285.239
    • Schnitzer, J. E., Oh, P., and McIntosh, D. P. (1996) Role of GTP hydrolysis in fission of caveolae directly from plasma membranes. Science 274, 239-242 (Pubitemid 26353199)
    • (1996) Science , vol.274 , Issue.5285 , pp. 239-242
    • Schnitzer, J.E.1    Oh, P.2    McIntosh, D.P.3
  • 59
    • 0021289319 scopus 로고
    • Purification of (Ca2+-Mg2+)-ATPase from rat liver plasma membranes
    • Lin, S. H., and Fain, J. N. (1984) Purification of (Ca2+-Mg2+)-ATPase from rat liver plasma membranes. J. Biol. Chem. 259, 3016-3020
    • (1984) J. Biol. Chem. , vol.259 , pp. 3016-3020
    • Lin, S.H.1    Fain, J.N.2
  • 61
    • 0021808682 scopus 로고
    • Purification of liver and hepatoma membrane proteins by high-performance liquid chromatography
    • DOI 10.1016/0014-5793(85)80766-3
    • Josiæ, D., Schuett, W., Neumeier, R., and Reutter, W. (1985) Purification of liver and hepatoma membrane proteins by high-performance liquid chromatography. FEBS Lett. 185, 182-186 (Pubitemid 15058212)
    • (1985) FEBS Letters , vol.185 , Issue.1 , pp. 182-186
    • Josic, D.1    Schuett, W.2    Neumeier, R.3    Reutter, W.4
  • 62
    • 23144449385 scopus 로고    scopus 로고
    • Use of selective extraction and fast chromatographic separation combined with electrophoretic methods for mapping of membrane proteins
    • Josic, D., Brown, M. K., Huang, F., Callanan, H., Ruceviæ, M., Nicoletti, A., Clifton, J., and Hixson, D. C. (2005) Use of selective extraction and fast chromatographic separation combined with electrophoretic methods for mapping of membrane proteins. Electrophoresis 26, 2809-2822
    • (2005) Electrophoresis , vol.26 , pp. 2809-2822
    • Josic, D.1    Brown, M.K.2    Huang, F.3    Callanan, H.4    Ruceviæ, M.5    Nicoletti, A.6    Clifton, J.7    Hixson, D.C.8
  • 63
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki, Y., Hubbard, A. L., Fowler, S., and Lazarow, P. B. (1982) Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J. Cell Biol. 93, 97-102
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 64
    • 33746704413 scopus 로고    scopus 로고
    • Identification of members of the annexin family in the detergent-insoluble fraction of rat Morris hepatoma plasma membranes
    • DOI 10.1016/j.chroma.2006.02.020, PII S0021967306003670
    • Clifton, J. G., Brown, M. K., Huang, F., Li, X., Reutter, W., Hofmann, W., Hixson, D. C., and Josic, D. (2006) Identification of members of the annexin family in the detergent-insoluble fraction of rat Morris hepatoma plasma membranes. J. Chromatogr. A 1123, 205-211 (Pubitemid 44160514)
    • (2006) Journal of Chromatography A , vol.1123 , Issue.2 , pp. 205-211
    • Clifton, J.G.1    Brown, M.K.2    Huang, F.3    Li, X.4    Reutter, W.5    Hofmann, W.6    Hixson, D.C.7    Josic, D.8
  • 65
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier, C. (1981) Phase separation of integral membrane proteins in Triton X-114 solution. J. Biol. Chem. 256, 1604-1607
    • (1981) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 68
    • 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
  • 69
    • 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., and Rabilloud, T. (2000) 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) Electrophoresis , vol.21 , pp. 3329-3344
    • Santoni, V.1    Kieffer, S.2    Desclaux, D.3    Masson, F.4    Rabilloud, T.5
  • 70
    • 0031807109 scopus 로고    scopus 로고
    • Use of thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis
    • Rabilloud, T. (1998) Use of thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis. Electrophoresis 19, 758-760
    • (1998) Electrophoresis , vol.19 , pp. 758-760
    • Rabilloud, T.1
  • 72
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M. P., Wolters, D., and Yates, J. R., 3rd (2001) Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 19, 242-247
    • (2001) Nat. Biotechnol. , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates III, J.R.3
  • 74
    • 33845585903 scopus 로고    scopus 로고
    • Analysis of the synaptic vesicle proteome using three gel-based protein separation techniques
    • DOI 10.1002/pmic.200600357
    • Burré, J., Beckhaus, T., Schägger, H., Corvey, C., Hofmann, S., Karas, M., Zimmermann, H., and Volknandt, W. (2006) Analysis of the synaptic vesicle proteome using three gel-based protein separation techniques. Proteomics 6, 6250-6262 (Pubitemid 44935512)
    • (2006) Proteomics , vol.6 , Issue.23 , pp. 6250-6262
    • Burre, J.1    Beckhaus, T.2    Schagger, H.3    Corvey, C.4    Hofmann, S.5    Karas, M.6    Zimmermann, H.7    Volknandt, W.8
  • 75
    • 1642398957 scopus 로고    scopus 로고
    • Proteomic analysis of the synaptic plasma membrane fraction isolated from rat forebrain
    • Stevens, S. M., Jr., Zharikova, A. D., and Prokai, L. (2003) Proteomic analysis of the synaptic plasma membrane fraction isolated from rat forebrain. Brain Res. Mol. Brain Res. 117, 116-128
    • (2003) Brain Res. Mol. Brain Res. , vol.117 , pp. 116-128
    • Stevens Jr., S.M.1    Zharikova, A.D.2    Prokai, L.3
  • 77
    • 23044494298 scopus 로고    scopus 로고
    • Identification and relative quantification of membrane proteins by surface biotinylation and two-dimensional peptide mapping
    • DOI 10.1002/pmic.200401163
    • Scheurer, S. B., Rybak, J. N., Roesli, C., Brunisholz, R. A., Potthast, F., Schlapbach, R., Neri, D., and Elia, G. (2005) Identification and relative quantification of membrane proteins by surface biotinylation and two-dimensional peptide mapping. Proteomics 5, 2718-2728 (Pubitemid 41059751)
    • (2005) Proteomics , vol.5 , Issue.11 , pp. 2718-2728
    • Scheurer, S.B.1    Rybak, J.-N.2    Roesli, C.3    Brunisholz, R.A.4    Potthast, F.5    Schlapbach, R.6    Neri, D.7    Elia, G.8
  • 78
    • 0242291099 scopus 로고    scopus 로고
    • Enzyme-friendly, mass spectrometry-compatible surfactant for in-solution enzymatic digestion of proteins
    • Yu, Y. Q., Gilar, M., Lee, P. J., Bouvier, E. S., and Gebler, J. C. (2003) Enzyme-friendly, mass spectrometry-compatible surfactant for in-solution enzymatic digestion of proteins. Anal. Chem. 75, 6023-6028
    • (2003) Anal. Chem. , vol.75 , pp. 6023-6028
    • Yu, Y.Q.1    Gilar, M.2    Lee, P.J.3    Bouvier, E.S.4    Gebler, J.C.5
  • 79
    • 34547232157 scopus 로고    scopus 로고
    • Optimization of mass spectrometry-compatible surfactants for shotgun proteomics
    • DOI 10.1021/pr060682a
    • Chen, E. I., Cociorva, D., Norris, J. L., and Yates, J. R., 3rd (2007) Optimization of mass spectrometry-compatible surfactants for shotgun proteomics. J. Proteome Res. 6, 2529-2538 (Pubitemid 47122350)
    • (2007) Journal of Proteome Research , vol.6 , Issue.7 , pp. 2529-2538
    • Chen, E.I.1    Cociorva, D.2    Norris, J.L.3    Yates III, J.R.4
  • 80
    • 0037008238 scopus 로고    scopus 로고
    • Temperature selectivity in reversed-phase high performance liquid chromatography
    • Dolan, J. W. (2002) Temperature selectivity in reversed-phase high performance liquid chromatography. J. Chromatogr. A 965, 195-205
    • (2002) J. Chromatogr. A , vol.965 , pp. 195-205
    • Dolan, J.W.1
  • 81
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 82
    • 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., Doeven, M. K., Canas, B., Veenhoff, L. M., Poolman, B., and Robillard, G. T. (2002) Combined in-gel tryptic digestion and CNBr cleavage for the generation of peptide maps of an integral membrane protein with MALDI-TOF mass spectrometry. Biochim. Biophys. Acta 1555, 111-115
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 111-115
    • Van Montfort, B.A.1    Doeven, M.K.2    Canas, B.3    Veenhoff, L.M.4    Poolman, B.5    Robillard, G.T.6
  • 83
    • 33646557331 scopus 로고    scopus 로고
    • Protein cleavage strategies for an improved analysis of the membrane proteome
    • Fischer, F., and Poetsch, A. (2006) Protein cleavage strategies for an improved analysis of the membrane proteome. Proteome Sci. 4, 2
    • (2006) Proteome Sci. , vol.4 , pp. 2
    • Fischer, F.1    Poetsch, A.2
  • 84
    • 0942276251 scopus 로고    scopus 로고
    • A detergent- and cyanogen bromide-free method for integral membrane proteomics: Application to Halobacterium purple membranes and the human epidermal membrane proteome
    • Blonder, J., Conrads, T. P., Yu, L. R., Terunuma, A., Janini, G. M., Issaq, H. J., Vogel, J. C., and Veenstra, T. D. (2004) A detergent- and cyanogen bromide-free method for integral membrane proteomics: application to Halobacterium purple membranes and the human epidermal membrane proteome. Proteomics 4, 31-45
    • (2004) Proteomics , vol.4 , pp. 31-45
    • Blonder, J.1    Conrads, T.P.2    Yu, L.R.3    Terunuma, A.4    Janini, G.M.5    Issaq, H.J.6    Vogel, J.C.7    Veenstra, T.D.8
  • 86
    • 73149094295 scopus 로고    scopus 로고
    • Membrane protein analysis using an improved peptic in-solution digestion protocol
    • Rietschel, B., Bornemann, S., Arrey, T. N., Baeumlisberger, D., Karas, M., and Meyer, B. (2009) Membrane protein analysis using an improved peptic in-solution digestion protocol. Proteomics 9, 5553-5557
    • (2009) Proteomics , vol.9 , pp. 5553-5557
    • Rietschel, B.1    Bornemann, S.2    Arrey, T.N.3    Baeumlisberger, D.4    Karas, M.5    Meyer, B.6
  • 87
    • 0036624537 scopus 로고    scopus 로고
    • Shotgun proteomics: Tools for the analysis of complex biological systems
    • Wu, C. C., and MacCoss, M. J. (2002) Shotgun proteomics: tools for the analysis of complex biological systems. Curr. Opin. Mol. Ther. 4, 242-250
    • (2002) Curr. Opin. Mol. Ther. , vol.4 , pp. 242-250
    • Wu, C.C.1    MacCoss, M.J.2
  • 88
    • 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., 3rd (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
  • 89
    • 0034057802 scopus 로고    scopus 로고
    • Membrane topology and insertion of membrane proteins: Search for topogenic signals
    • van Geest, M., and Lolkema, J. S. (2000) Membrane topology and insertion of membrane proteins: search for topogenic signals. Microbiol. Mol. Biol. Rev. 64, 13-33
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 13-33
    • Van Geest, M.1    Lolkema, J.S.2
  • 90
    • 0026716643 scopus 로고
    • Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule
    • von Heijne, G. (1992) Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. J. Mol. Biol. 225, 487-494
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • Von Heijne, G.1
  • 91
    • 0028568176 scopus 로고
    • TopPred II: An improved software for membrane protein structure predictions
    • Claros, M. G., and von Heijne, G. (1994) TopPred II: an improved software for membrane protein structure predictions. Comput. Appl. Biosci. 10, 685-686
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 685-686
    • Claros, M.G.1    Von Heijne, G.2
  • 92
    • 0027478779 scopus 로고
    • The topological analysis of integral cytoplasmic membrane proteins
    • Traxler, B., Boyd, D., and Beckwith, J. (1993) The topological analysis of integral cytoplasmic membrane proteins. J. Membr. Biol. 132, 1-11
    • (1993) J. Membr. Biol. , vol.132 , pp. 1-11
    • Traxler, B.1    Boyd, D.2    Beckwith, J.3
  • 93
    • 0022541790 scopus 로고
    • Isolation of phosphoproteins by immobilized metal (Fe3+) affinity chromatography
    • Andersson, L., and Porath, J. (1986) Isolation of phosphoproteins by immobilized metal (Fe3+) affinity chromatography. Anal. Biochem. 154, 250-254
    • (1986) Anal. Biochem. , vol.154 , pp. 250-254
    • Andersson, L.1    Porath, J.2
  • 94
    • 0030667705 scopus 로고    scopus 로고
    • Evidence for phosphorylation of serine 753 in CFTR using a novel metal-ion affinity resin and matrix-assisted laser desorption mass spectrometry
    • Neville, D. C., Rozanas, C. R., Price, E. M., Gruis, D. B., Verkman, A. S., and Townsend, R. R. (1997) Evidence for phosphorylation of serine 753 in CFTR using a novel metal-ion affinity resin and matrix-assisted laser desorption mass spectrometry. Protein Sci. 6, 2436-2445
    • (1997) Protein Sci. , vol.6 , pp. 2436-2445
    • Neville, D.C.1    Rozanas, C.R.2    Price, E.M.3    Gruis, D.B.4    Verkman, A.S.5    Townsend, R.R.6
  • 95
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns
    • Larsen, M. R., Thingholm, T. E., Jensen, O. N., Roepstorff, P., and Jørgensen, T. J. (2005) Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol. Cell. Proteomics 4, 873-886
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 873-886
    • Larsen, M.R.1    Thingholm, T.E.2    Jensen, O.N.3    Roepstorff, P.4    Jørgensen, T.J.5
  • 96
    • 3242688830 scopus 로고    scopus 로고
    • Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns
    • Pinkse, M. W., Uitto, P. M., Hilhorst, M. J., Ooms, B., and Heck, A. J. (2004) Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns. Anal. Chem. 76, 3935-3943
    • (2004) Anal. Chem. , vol.76 , pp. 3935-3943
    • Pinkse, M.W.1    Uitto, P.M.2    Hilhorst, M.J.3    Ooms, B.4    Heck, A.J.5
  • 97
    • 37249053773 scopus 로고    scopus 로고
    • Peptide sequencing and characterization of post-translational modifications by enhanced ion-charging and liquid chromatography electrontransfer dissociation tandem mass spectrometry
    • Kjeldsen, F., Giessing, A. M., Ingrell, C. R., and Jensen, O. N. (2007) Peptide sequencing and characterization of post-translational modifications by enhanced ion-charging and liquid chromatography electrontransfer dissociation tandem mass spectrometry. Anal. Chem. 79, 9243-9252
    • (2007) Anal. Chem. , vol.79 , pp. 9243-9252
    • Kjeldsen, F.1    Giessing, A.M.2    Ingrell, C.R.3    Jensen, O.N.4
  • 99
    • 65249137629 scopus 로고    scopus 로고
    • Global and site-specific quantitative phosphoproteomics: Principles and applications
    • Macek, B., Mann, M., and Olsen, J. V. (2009) Global and site-specific quantitative phosphoproteomics: principles and applications. Annu. Rev. Pharmacol. Toxicol. 49, 199-221
    • (2009) Annu. Rev. Pharmacol. Toxicol. , vol.49 , pp. 199-221
    • Macek, B.1    Mann, M.2    Olsen, J.V.3
  • 100
    • 55849118087 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics by mass spectrometry: Past, present, and future
    • Nita-Lazar, A., Saito-Benz, H., and White, F. M. (2008) Quantitative phosphoproteomics by mass spectrometry: past, present, and future. Pro- teomics 8, 4433-4443
    • (2008) Proteomics , vol.8 , pp. 4433-4443
    • Nita-Lazar, A.1    Saito-Benz, H.2    White, F.M.3
  • 104
    • 67049117495 scopus 로고    scopus 로고
    • Directed sample interrogation utilizing an accurate mass exclusion-based data-dependent acquisition strategy (AMEx)
    • Rudomin, E. L., Carr, S. A., and Jaffe, J. D. (2009) Directed sample interrogation utilizing an accurate mass exclusion-based data-dependent acquisition strategy (AMEx). J. Proteome Res. 8, 3154-3160
    • (2009) J. Proteome Res. , vol.8 , pp. 3154-3160
    • Rudomin, E.L.1    Carr, S.A.2    Jaffe, J.D.3
  • 106
    • 35848949043 scopus 로고    scopus 로고
    • Decoding protein modifications using top-down mass spectrometry
    • Siuti, N., and Kelleher, N. L. (2007) Decoding protein modifications using top-down mass spectrometry. Nat. Methods 4, 817-821
    • (2007) Nat. Methods , vol.4 , pp. 817-821
    • Siuti, N.1    Kelleher, N.L.2
  • 108
    • 33846926966 scopus 로고    scopus 로고
    • Amino acid-coded tagging approaches in quantitative proteomics
    • DOI 10.1586/14789450.4.1.25
    • Chen, X., Sun, L., Yu, Y., Xue, Y., and Yang, P. (2007) Amino acid-coded tagging approaches in quantitative proteomics. Expert Rev. Proteomics 4, 25-37 (Pubitemid 46239470)
    • (2007) Expert Review of Proteomics , vol.4 , Issue.1 , pp. 25-37
    • Chen, X.1    Sun, L.2    Yu, Y.3    Xue, Y.4    Yang, P.5
  • 111
    • 0346874342 scopus 로고    scopus 로고
    • Proteomic characterization of the human centrosome by protein correlation profiling
    • DOI 10.1038/nature02166
    • Andersen, J. S., Wilkinson, C. J., Mayor, T., Mortensen, P., Nigg, E. A., and Mann, M. (2003) Proteomic characterization of the human centrosome by protein correlation profiling. Nature 426, 570-574 (Pubitemid 37522644)
    • (2003) Nature , vol.426 , Issue.6966 , pp. 570-574
    • Andersen, J.S.1    Wilkinson, C.J.2    Mayor, T.3    Mortensen, P.4    Nigg, E.A.5    Mann, M.6
  • 115
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • Liu, H., Sadygov, R. G., and Yates, J. R., 3rd (2004) A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal. Chem. 76, 4193-4201
    • (2004) Anal. Chem. , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates III, J.R.3
  • 116
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (em-PAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • Ishihama, Y., Oda, Y., Tabata, T., Sato, T., Nagasu, T., Rappsilber, J., and Mann, M. (2005) Exponentially modified protein abundance index (em-PAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein. Mol. Cell. Proteomics 4, 1265-1272
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3    Sato, T.4    Nagasu, T.5    Rappsilber, J.6    Mann, M.7
  • 117
    • 34848822499 scopus 로고    scopus 로고
    • Quantitative profile of five murine core proteomes using label-free functional proteomics
    • Cutillas, P. R., and Vanhaesebroeck, B. (2007) Quantitative profile of five murine core proteomes using label-free functional proteomics. Mol. Cell. Proteomics 6, 1560-1573
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1560-1573
    • Cutillas, P.R.1    Vanhaesebroeck, B.2
  • 118
    • 0037106398 scopus 로고    scopus 로고
    • Identification and relative quantitation of protein mixtures by enzymatic digestion followed by capillary reversed-phase liquid chromatography-tandem mass spectrometry
    • Bondarenko, P. V., Chelius, D., and Shaler, T. A. (2002) Identification and relative quantitation of protein mixtures by enzymatic digestion followed by capillary reversed-phase liquid chromatography-tandem mass spectrometry. Anal. Chem. 74, 4741-4749
    • (2002) Anal. Chem. , vol.74 , pp. 4741-4749
    • Bondarenko, P.V.1    Chelius, D.2    Shaler, T.A.3
  • 121
    • 58149295188 scopus 로고    scopus 로고
    • Label-free quantitative analysis of 1D-PAGE LC/MS/MS proteome: Application on angiotensin II stimulated smooth muscle cells secretome
    • Gao, B. B., Stuart, L., and Feener, E. P. (2008) Label-free quantitative analysis of 1D-PAGE LC/MS/MS proteome: application on angiotensin II stimulated smooth muscle cells secretome. Mol. Cell. Proteomics 7, 2399-2409
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 2399-2409
    • Gao, B.B.1    Stuart, L.2    Feener, E.P.3
  • 122
    • 0036665581 scopus 로고    scopus 로고
    • Quantitative profiling of proteins in complex mixtures using liquid chromatography and mass spectrometry
    • Chelius, D., and Bondarenko, P. V. (2002) Quantitative profiling of proteins in complex mixtures using liquid chromatography and mass spectrometry. J. Proteome Res. 1, 317-323
    • (2002) J. Proteome Res. , vol.1 , pp. 317-323
    • Chelius, D.1    Bondarenko, P.V.2
  • 123
    • 0344737959 scopus 로고    scopus 로고
    • Automated statistical analysis of protein abundance ratios from data generated by stable-isotope dilution and tandem mass spectrometry
    • Li, X. J., Zhang, H., Ranish, J. A., and Aebersold, R. (2003) Automated statistical analysis of protein abundance ratios from data generated by stable-isotope dilution and tandem mass spectrometry. Anal. Chem. 75, 6648-6657
    • (2003) Anal. Chem. , vol.75 , pp. 6648-6657
    • Li, X.J.1    Zhang, H.2    Ranish, J.A.3    Aebersold, R.4
  • 124
    • 0034789979 scopus 로고    scopus 로고
    • Quantitative profiling of differentiation-induced microsomal proteins using isotopecoded affinity tags and mass spectrometry
    • Han, D. K., Eng, J., Zhou, H., and Aebersold, R. (2001) Quantitative profiling of differentiation-induced microsomal proteins using isotopecoded affinity tags and mass spectrometry. Nat. Biotechnol. 19, 946-951
    • (2001) Nat. Biotechnol. , vol.19 , pp. 946-951
    • Han, D.K.1    Eng, J.2    Zhou, H.3    Aebersold, R.4
  • 125
    • 0346122950 scopus 로고    scopus 로고
    • A correlation algorithm for the automated quantitative analysis of shotgun proteomics data
    • MacCoss, M. J., Wu, C. C., Liu, H., Sadygov, R., and Yates, J. R., 3rd (2003) A correlation algorithm for the automated quantitative analysis of shotgun proteomics data. Anal. Chem. 75, 6912-6921
    • (2003) Anal. Chem. , vol.75 , pp. 6912-6921
    • MacCoss, M.J.1    Wu, C.C.2    Liu, H.3    Sadygov, R.4    Yates III, J.R.5
  • 126
    • 33646570853 scopus 로고    scopus 로고
    • Application of capture-recapture models to estimation of protein count in MudPIT experiments
    • Koziol, J. A., Feng, A. C., and Schnitzer, J. E. (2006) Application of capture-recapture models to estimation of protein count in MudPIT experiments. Anal. Chem. 78, 3203-3207
    • (2006) Anal. Chem. , vol.78 , pp. 3203-3207
    • Koziol, J.A.1    Feng, A.C.2    Schnitzer, J.E.3
  • 127
    • 74049132731 scopus 로고    scopus 로고
    • Label-free, normalized quantification of complex mass spectrometry data for proteomic analysis
    • Griffin, N. M., Yu, J., Long, F., Oh, P., Shore, S., Li, Y., Koziol, J. A., and Schnitzer, J. E. (2010) Label-free, normalized quantification of complex mass spectrometry data for proteomic analysis. Nat. Biotechnol. 28, 83-89
    • (2010) Nat. Biotechnol. , vol.28 , pp. 83-89
    • Griffin, N.M.1    Yu, J.2    Long, F.3    Oh, P.4    Shore, S.5    Li, Y.6    Koziol, J.A.7    Schnitzer, J.E.8
  • 128
    • 72449185502 scopus 로고    scopus 로고
    • Range charts for agreement in measurement comparison studies, with application to replicate mass spectrometry experiments
    • Koziol, J. A., Feng, A. C., Yu, J., Griffin, N. M., and Schnitzer, J. E. (2008) Range charts for agreement in measurement comparison studies, with application to replicate mass spectrometry experiments. J. Proteomics Bioinform. 1, 287-292
    • (2008) J. Proteomics Bioinform. , vol.1 , pp. 287-292
    • Koziol, J.A.1    Feng, A.C.2    Yu, J.3    Griffin, N.M.4    Schnitzer, J.E.5
  • 132
    • 2342646842 scopus 로고    scopus 로고
    • LSimpute: Accurate estimation of missing values in microarray data with least squares methods
    • Bø, T. H., Dysvik, B., and Jonassen, I. (2004) LSimpute: accurate estimation of missing values in microarray data with least squares methods. Nucleic Acids Res. 32, e34
    • (2004) Nucleic Acids Res. , vol.32
    • Bø, T.H.1    Dysvik, B.2    Jonassen, I.3
  • 134
    • 0002458517 scopus 로고    scopus 로고
    • Isolation and subfractionation of plasma membranes to purify caveolae separately from glycosyl-phosphatidylinositol-anchored protein microdomain
    • Celis, J. E., ed Academic Press, Orlando, FL
    • Oh, P., and Schnitzer, J. E. (1998) Isolation and subfractionation of plasma membranes to purify caveolae separately from glycosyl- phosphatidylinositol-anchored protein microdomain, in Cell Biology: a Laboratory Handbook (Celis, J. E., ed) pp. 34-36, Academic Press, Orlando, FL
    • (1998) Cell Biology: A Laboratory Handbook , pp. 34-36
    • Oh, P.1    Schnitzer, J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.