메뉴 건너뛰기




Volumn 41, Issue 2, 2011, Pages 223-233

Tools for phospho- and glycoproteomics of plasma membranes

Author keywords

Glycosylation; Mass spectrometry; Phosphorylation; Plasma membrane protein

Indexed keywords

DETERGENT; GLYCAN; GLYCOPROTEIN; MEMBRANE PROTEIN; METHANOL; PHOSPHOPROTEIN; PROTEOME;

EID: 79960026710     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-010-0796-8     Document Type: Review
Times cited : (16)

References (91)
  • 1
    • 71649115832 scopus 로고    scopus 로고
    • CaMKII associates with CaV1.2 L-type calcium channels via selected beta subunits to enhance regulatory phosphorylation
    • 19840220 10.1111/j.1471-4159.2009.06436.x 1:CAS:528: DC%2BC3cXhs1GhtA%3D%3D
    • SA Abiria RJ Colbran 2010 CaMKII associates with CaV1.2 L-type calcium channels via selected beta subunits to enhance regulatory phosphorylation J Neurochem 112 150 161 19840220 10.1111/j.1471-4159.2009.06436.x 1:CAS:528:DC%2BC3cXhs1GhtA%3D%3D
    • (2010) J Neurochem , vol.112 , pp. 150-161
    • Abiria, S.A.1    Colbran, R.J.2
  • 2
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • DOI 10.1038/nature01511
    • R Aebersold M Mann 2003 Mass spectrometry-based proteomics Nature 422 198 207 12634793 10.1038/nature01511 1:CAS:528:DC%2BD3sXhvFKgs7s%3D (Pubitemid 36362757)
    • (2003) Nature , vol.422 , Issue.6928 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 3
    • 33644841035 scopus 로고    scopus 로고
    • Tools for glycoproteomic analysis: Size exclusion chromatography facilitates identification of tryptic glycopeptides with N-linked glycosylation sites
    • DOI 10.1021/pr050275j
    • G Alvarez-Manilla J Atwood 3rd Y Guo NL Warren R Orlando M Pierce 2006 Tools for glycoproteomic analysis: size exclusion chromatography facilitates identification of tryptic glycopeptides with N-linked glycosylation sites J Proteome Res 5 701 708 16512686 10.1021/pr050275j 1:CAS:528:DC%2BD28XhtlSrurc%3D (Pubitemid 43364110)
    • (2006) Journal of Proteome Research , vol.5 , Issue.3 , pp. 701-708
    • Alvarez-Manilla, G.1    Atwood III, J.2    Guo, Y.3    Warren, N.L.4    Orlando, R.5    Pierce, M.6
  • 4
    • 38649139336 scopus 로고    scopus 로고
    • Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain
    • DOI 10.1021/pr0701254
    • BA Ballif GR Carey SR Sunyaev SP Gygi 2008 Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain J Proteome Res 7 311 318 18034455 10.1021/pr0701254 1:CAS:528:DC%2BD2sXhtlCqtLbJ (Pubitemid 351171145)
    • (2008) Journal of Proteome Research , vol.7 , Issue.1 , pp. 311-318
    • Ballif, B.A.1    Carey, G.R.2    Sunyaev, S.R.3    Gygi, S.P.4
  • 5
    • 0036665518 scopus 로고    scopus 로고
    • Enrichment of integral membrane proteins for proteomic analysis using liquid chromatography-tandem mass spectrometry
    • DOI 10.1021/pr0255248
    • J Blonder MB Goshe RJ Moore L Pasa-Tolic CD Masselon MS Lipton RD Smith 2002 Enrichment of integral membrane proteins for proteomic analysis using liquid chromatography-tandem mass spectrometry J Proteome Res 1 351 360 12645891 10.1021/pr0255248 1:CAS:528:DC%2BD38Xjs12gsr8%3D (Pubitemid 36395876)
    • (2002) Journal of Proteome Research , vol.1 , Issue.4 , 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
  • 7
    • 1242339573 scopus 로고    scopus 로고
    • Screening for N-glycosylated proteins by liquid chromatography mass spectrometry
    • DOI 10.1002/pmic.200300556
    • J Bunkenborg BJ Pilch AV Podtelejnikov JR Wisniewski 2004 Screening for N-glycosylated proteins by liquid chromatography mass spectrometry Proteomics 4 454 465 14760718 10.1002/pmic.200300556 1:CAS:528:DC%2BD2cXhs1Ciu78%3D (Pubitemid 38235265)
    • (2004) Proteomics , vol.4 , Issue.2 , pp. 454-465
    • Bunkenborg, J.1    Pilch, B.J.2    Podtelejnikov, A.V.3    Wisniewski, J.R.4
  • 8
    • 33644841214 scopus 로고    scopus 로고
    • Integration of a two-phase partition method into proteomics research on rat liver plasma membrane proteins
    • DOI 10.1021/pr050387a
    • R Cao X Li Z Liu X Peng W Hu X Wang P Chen J Xie S Liang 2006 Integration of a two-phase partition method into proteomics research on rat liver plasma membrane proteins J Proteome Res 5 634 642 16512679 10.1021/pr050387a 1:CAS:528:DC%2BD28XhtlOqsLk%3D (Pubitemid 43364104)
    • (2006) Journal of Proteome Research , vol.5 , Issue.3 , pp. 634-642
    • Cao, R.1    Li, X.2    Liu, Z.3    Peng, X.4    Hu, W.5    Wang, X.6    Chen, P.7    Xie, J.8    Liang, S.9
  • 9
    • 0021112527 scopus 로고
    • Coating cells with colloidal silica for high yield isolation of plasma membrane sheets and identification of transmembrane proteins
    • 6309765 1:CAS:528:DyaL3sXltFyrsbo%3D
    • LK Chaney BS Jacobson 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 6309765 1:CAS:528:DyaL3sXltFyrsbo%3D
    • (1983) J Biol Chem , vol.258 , pp. 10062-10072
    • Chaney, L.K.1    Jacobson, B.S.2
  • 10
    • 34547232157 scopus 로고    scopus 로고
    • Optimization of mass spectrometry-compatible surfactants for shotgun proteomics
    • DOI 10.1021/pr060682a
    • EI Chen D Cociorva JL Norris JR Yates 3rd 2007 Optimization of mass spectrometry-compatible surfactants for shotgun proteomics J Proteome Res 6 2529 2538 17530876 10.1021/pr060682a 1:CAS:528:DC%2BD2sXlvVWju78%3D (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
  • 11
    • 56449114837 scopus 로고    scopus 로고
    • Comparisons of mass spectrometry compatible surfactants for global analysis of the mammalian brain proteome
    • 18937422 10.1021/ac800606w 1:CAS:528:DC%2BD1cXhtlGns7bE
    • EI Chen D McClatchy SK Park JR Yates 3rd 2008 Comparisons of mass spectrometry compatible surfactants for global analysis of the mammalian brain proteome Anal Chem 80 8694 8701 18937422 10.1021/ac800606w 1:CAS:528: DC%2BD1cXhtlGns7bE
    • (2008) Anal Chem , vol.80 , pp. 8694-8701
    • Chen, E.I.1    McClatchy, D.2    Park, S.K.3    Yates III, J.R.4
  • 12
    • 37249014081 scopus 로고    scopus 로고
    • The biological impact of mass-spectrometry-based proteomics
    • DOI 10.1038/nature06525, PII NATURE06525
    • BF Cravatt GM Simon JR Yates 3rd 2007 The biological impact of mass-spectrometry-based proteomics Nature 450 991 1000 18075578 10.1038/nature06525 1:CAS:528:DC%2BD2sXhsVaqtr7E (Pubitemid 350273629)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 991-1000
    • Cravatt, B.F.1    Simon, G.M.2    Yates III, J.R.3
  • 13
    • 72149102185 scopus 로고    scopus 로고
    • Affinity enrichment and characterization of mucin core-1 type glycopeptides from bovine serum
    • 19674964 10.1074/mcp.M900211-MCP200 1:CAS:528:DC%2BD1MXhsVSms77M
    • Z Darula KF Medzihradszky 2009 Affinity enrichment and characterization of mucin core-1 type glycopeptides from bovine serum Mol Cell Proteomics 8 2515 2526 19674964 10.1074/mcp.M900211-MCP200 1:CAS:528:DC%2BD1MXhsVSms77M
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2515-2526
    • Darula, Z.1    Medzihradszky, K.F.2
  • 14
    • 76549117726 scopus 로고    scopus 로고
    • The alpha2delta subunits of voltage-gated calcium channels form GPI-anchored proteins, a posttranslational modification essential for function
    • 20080692 10.1073/pnas.0908735107 1:CAS:528:DC%2BC3cXhslGgurY%3D
    • A Davies I Kadurin A Alvarez-Laviada L Douglas M Nieto-Rostro CS Bauer WS Pratt AC Dolphin 2010 The alpha2delta subunits of voltage-gated calcium channels form GPI-anchored proteins, a posttranslational modification essential for function Proc Natl Acad Sci USA 107 1654 1659 20080692 10.1073/pnas. 0908735107 1:CAS:528:DC%2BC3cXhslGgurY%3D
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 1654-1659
    • Davies, A.1    Kadurin, I.2    Alvarez-Laviada, A.3    Douglas, L.4    Nieto-Rostro, M.5    Bauer, C.S.6    Pratt, W.S.7    Dolphin, A.C.8
  • 15
    • 72249094196 scopus 로고    scopus 로고
    • Metabolism, cell surface organization, and disease
    • 20064370 10.1016/j.cell.2009.12.008
    • JW Dennis IR Nabi M Demetriou 2009 Metabolism, cell surface organization, and disease Cell 139 1229 1241 20064370 10.1016/j.cell.2009.12.008
    • (2009) Cell , vol.139 , pp. 1229-1241
    • Dennis, J.W.1    Nabi, I.R.2    Demetriou, M.3
  • 16
    • 0345185172 scopus 로고    scopus 로고
    • β Subunits of Voltage-Gated Calcium Channels
    • DOI 10.1023/B:JOBB.0000008026.37790.5a
    • AC Dolphin 2003 Beta subunits of voltage-gated calcium channels J Bioenerg Biomembr 35 599 620 15000522 10.1023/B:JOBB.0000008026.37790.5a 1:CAS:528:DC%2BD3sXpvVShs7s%3D (Pubitemid 38124815)
    • (2003) Journal of Bioenergetics and Biomembranes , vol.35 , Issue.6 , pp. 599-620
    • Dolphin, A.C.1
  • 17
    • 68649099001 scopus 로고    scopus 로고
    • Calcium channel diversity: Multiple roles of calcium channel subunits
    • 19559597 10.1016/j.conb.2009.06.006 1:CAS:528:DC%2BD1MXhtVent77F
    • AC Dolphin 2009 Calcium channel diversity: multiple roles of calcium channel subunits Curr Opin Neurobiol 19 237 244 19559597 10.1016/j.conb.2009.06. 006 1:CAS:528:DC%2BD1MXhtVent77F
    • (2009) Curr Opin Neurobiol , vol.19 , pp. 237-244
    • Dolphin, A.C.1
  • 18
    • 33749537286 scopus 로고    scopus 로고
    • Targeted glycoproteomics: Serial lectin affinity chromatography in the selection of O-glycosylation sites on proteins from the human blood proteome
    • DOI 10.1016/j.chroma.2006.07.070, PII S0021967306014671
    • M Durham FE Regnier 2006 Targeted glycoproteomics: serial lectin affinity chromatography in the selection of O-glycosylation sites on proteins from the human blood proteome J Chromatogr A 1132 165 173 16919642 10.1016/j.chroma.2006. 07.070 1:CAS:528:DC%2BD28XhtVyksLfK (Pubitemid 44528498)
    • (2006) Journal of Chromatography A , vol.1132 , Issue.1-2 , pp. 165-173
    • Durham, M.1    Regnier, F.E.2
  • 19
    • 3543023287 scopus 로고    scopus 로고
    • Direct proteomic mapping of the lung microvascular endothelial cell surface in vivo and in cell culture
    • DOI 10.1038/nbt993
    • E Durr J Yu KM Krasinska LA Carver JR Yates JE Testa P Oh JE Schnitzer 2004 Direct proteomic mapping of the lung microvascular endothelial cell surface in vivo and in cell culture Nat Biotechnol 22 985 992 15258593 10.1038/nbt993 1:CAS:528:DC%2BD2cXmtFWrurc%3D (Pubitemid 39014475)
    • (2004) Nature Biotechnology , vol.22 , Issue.8 , pp. 985-992
    • Durr, E.1    Yu, J.2    Krasinska, K.M.3    Carver, L.A.4    Yates III, J.R.5    Testa, J.E.6    Oh, P.7    Schnitzer, J.E.8
  • 20
    • 33645466243 scopus 로고    scopus 로고
    • Toward the complete membrane proteome: High coverage of integral membrane proteins through transmembrane peptide detection
    • 16291997 1:CAS:528:DC%2BD28XivVWltLc%3D
    • F Fischer D Wolters M Rogner A Poetsch 2006 Toward the complete membrane proteome: high coverage of integral membrane proteins through transmembrane peptide detection Mol Cell Proteomics 5 444 453 16291997 1:CAS:528: DC%2BD28XivVWltLc%3D
    • (2006) Mol Cell Proteomics , vol.5 , pp. 444-453
    • Fischer, F.1    Wolters, D.2    Rogner, M.3    Poetsch, A.4
  • 21
    • 0033543140 scopus 로고    scopus 로고
    • 2 subunit of L-type voltage-dependent calcium channels
    • DOI 10.1021/bi990896o
    • BL Gerhardstein TS Puri AJ Chien MM Hosey 1999 Identification of the sites phosphorylated by cyclic AMP-dependent protein kinase on the beta 2 subunit of L-type voltage-dependent calcium channels Biochemistry 38 10361 10370 10441130 10.1021/bi990896o 1:CAS:528:DyaK1MXksVOltLc%3D (Pubitemid 29383406)
    • (1999) Biochemistry , vol.38 , Issue.32 , pp. 10361-10370
    • Gerhardstein, B.L.1    Puri, T.S.2    Chien, A.J.3    Hosey, M.M.4
  • 23
    • 72149120326 scopus 로고    scopus 로고
    • The mouse C2C12 myoblast cell surface N-linked glycoproteome: Identification, glycosite occupancy, and membrane orientation
    • 19656770 10.1074/mcp.M900195-MCP200 1:CAS:528:DC%2BD1MXhsVSms77P
    • RL Gundry K Raginski Y Tarasova I Tchernyshyov D Bausch-Fluck ST Elliott KR Boheler JE Van Eyk B Wollscheid 2009 The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation Mol Cell Proteomics 8 2555 2569 19656770 10.1074/mcp.M900195-MCP200 1:CAS:528:DC%2BD1MXhsVSms77P
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2555-2569
    • Gundry, R.L.1    Raginski, K.2    Tarasova, Y.3    Tchernyshyov, I.4    Bausch-Fluck, D.5    Elliott, S.T.6    Boheler, K.R.7    Van Eyk, J.E.8    Wollscheid, B.9
  • 24
    • 4444269089 scopus 로고    scopus 로고
    • A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation
    • DOI 10.1021/pr034112b
    • P Hagglund J Bunkenborg F Elortza ON Jensen P Roepstorff 2004 A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation J Proteome Res 3 556 566 15253437 10.1021/pr034112b (Pubitemid 39207360)
    • (2004) Journal of Proteome Research , vol.3 , Issue.3 , pp. 556-566
    • Hagglund, P.1    Bunkenborg, J.2    Elortza, F.3    Jensen, O.N.4    Roepstorff, P.5
  • 25
    • 0035282989 scopus 로고    scopus 로고
    • Glycoprotein identification and localization of O-glycosylation sites by mass spectrometric analysis of deglycosylated/alkylaminylated peptide fragments
    • DOI 10.1006/abio.2000.4955
    • FG Hanisch M Jovanovic J Peter-Katalinic 2001 Glycoprotein identification and localization of O-glycosylation sites by mass spectrometric analysis of deglycosylated/alkylaminylated peptide fragments Anal Biochem 290 47 59 11180936 10.1006/abio.2000.4955 1:CAS:528:DC%2BD3MXht1artLY%3D (Pubitemid 32182269)
    • (2001) Analytical Biochemistry , vol.290 , Issue.1 , pp. 47-59
    • Hanisch, F.-G.1    Jovanovic, M.2    Peter-Katalinic, J.3
  • 26
    • 60549115995 scopus 로고    scopus 로고
    • Chemical de-O-glycosylation of glycoproteins for application in LC-based proteomics
    • 19132687 10.1002/pmic.200800492 1:CAS:528:DC%2BD1MXjt1Wht78%3D
    • FG Hanisch S Teitz T Schwientek S Muller 2009 Chemical de-O-glycosylation of glycoproteins for application in LC-based proteomics Proteomics 9 710 719 19132687 10.1002/pmic.200800492 1:CAS:528:DC%2BD1MXjt1Wht78%3D
    • (2009) Proteomics , vol.9 , pp. 710-719
    • Hanisch, F.G.1    Teitz, S.2    Schwientek, T.3    Muller, S.4
  • 28
    • 76749135320 scopus 로고    scopus 로고
    • Helicobacter pylori proteomics by 2-DE/MS, 1-DE-LC/MS and functional data mining
    • 19941309 10.1002/pmic.200900361 1:CAS:528:DC%2BC3cXhtVOmsr0%3D
    • PR Jungblut F Schiele U Zimny-Arndt R Ackermann M Schmid S Lange R Stein KP Pleissner 2010 Helicobacter pylori proteomics by 2-DE/MS, 1-DE-LC/MS and functional data mining Proteomics 10 182 193 19941309 10.1002/pmic.200900361 1:CAS:528:DC%2BC3cXhtVOmsr0%3D
    • (2010) Proteomics , vol.10 , pp. 182-193
    • Jungblut, P.R.1    Schiele, F.2    Zimny-Arndt, U.3    Ackermann, R.4    Schmid, M.5    Lange, S.6    Stein, R.7    Pleissner, K.P.8
  • 29
    • 0037685263 scopus 로고    scopus 로고
    • Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins
    • DOI 10.1038/nbt829
    • H Kaji H Saito Y Yamauchi T Shinkawa M Taoka J Hirabayashi K Kasai N Takahashi T Isobe 2003 Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins Nat Biotechnol 21 667 672 12754521 10.1038/nbt829 1:CAS:528:DC%2BD3sXktFSlu7k%3D (Pubitemid 36638094)
    • (2003) Nature Biotechnology , vol.21 , Issue.6 , pp. 667-672
    • Kaji, H.1    Saito, H.2    Yamauchi, Y.3    Shinkawa, T.4    Taoka, M.5    Hirabayashi, J.6    Kasai, K.-I.7    Takahashi, N.8    Isobe, T.9
  • 30
    • 38349038588 scopus 로고    scopus 로고
    • Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins
    • 17761667 10.1074/mcp.M600392-MCP200 1:CAS:528:DC%2BD1cXksF2isA%3D%3D
    • H Kaji J Kamiie H Kawakami K Kido Y Yamauchi T Shinkawa M Taoka N Takahashi T Isobe 2007 Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins Mol Cell Proteomics 6 2100 2109 17761667 10.1074/mcp.M600392-MCP200 1:CAS:528:DC%2BD1cXksF2isA%3D%3D
    • (2007) Mol Cell Proteomics , vol.6 , pp. 2100-2109
    • Kaji, H.1    Kamiie, J.2    Kawakami, H.3    Kido, K.4    Yamauchi, Y.5    Shinkawa, T.6    Taoka, M.7    Takahashi, N.8    Isobe, T.9
  • 31
    • 5444256180 scopus 로고    scopus 로고
    • Efficient in-gel digestion procedure using 5-cyclohexyl-1-pentyl-β- D- maltoside as an additive for gel-based membrane proteomics
    • DOI 10.1002/rcm.1637
    • H Katayama T Tabata Y Ishihama T Sato Y Oda T Nagasu 2004 Efficient in-gel digestion procedure using 5-cyclohexyl-1-pentyl-beta-d-maltoside as an additive for gel-based membrane proteomics Rapid Commun Mass Spectrom 18 2388 2394 15386632 10.1002/rcm.1637 1:CAS:528:DC%2BD2cXovF2qu7c%3D (Pubitemid 39361778)
    • (2004) Rapid Communications in Mass Spectrometry , vol.18 , Issue.20 , pp. 2388-2394
    • Katayama, H.1    Tabata, T.2    Ishihama, Y.3    Sato, T.4    Oda, Y.5    Nagasu, T.6
  • 32
    • 1642535342 scopus 로고    scopus 로고
    • 2δ Subunits: Differential Expression, Function, and Drug Binding
    • DOI 10.1023/B:JOBB.0000008028.41056.58
    • N Klugbauer E Marais F Hofmann 2003 Calcium channel alpha2delta subunits: differential expression, function, and drug binding J Bioenerg Biomembr 35 639 647 15000524 10.1023/B:JOBB.0000008028.41056.58 1:CAS:528:DC%2BD3sXpvVShs7k%3D (Pubitemid 38124817)
    • (2003) Journal of Bioenergetics and Biomembranes , vol.35 , Issue.6 , pp. 639-647
    • Klugbauer, N.1    Marais, E.2    Hofmann, F.3
  • 33
    • 0033106490 scopus 로고    scopus 로고
    • 18O-labeling of N-glycosylation sites to improve the identification of gel-separated glycoproteins using peptide mass mapping and database searching
    • DOI 10.1021/ac981012u
    • 18O-labeling of N-glycosylation sites to improve the identification of gel-separated glycoproteins using peptide mass mapping and database searching Anal Chem 71 1431 1440 10204042 10.1021/ac981012u 1:STN:280:DyaK1M3itVansQ%3D%3D (Pubitemid 29177305)
    • (1999) Analytical Chemistry , vol.71 , Issue.7 , pp. 1431-1440
    • Kuster, B.1    Mann, M.2
  • 34
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns
    • DOI 10.1074/mcp.T500007-MCP200
    • MR Larsen TE Thingholm ON Jensen P Roepstorff TJ Jorgensen 2005 Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns Mol Cell Proteomics 4 873 886 15858219 10.1074/mcp.T500007-MCP200 1:CAS:528:DC%2BD2MXmtFKktbg%3D (Pubitemid 41309146)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.7 , pp. 873-886
    • Larsen, M.R.1    Thingholm, T.E.2    Jensen, O.N.3    Roepstorff, P.4    Jorgensen, T.J.D.5
  • 36
    • 0242690399 scopus 로고    scopus 로고
    • Susceptibility of the hydroxyl groups in serine and threonine to β-elimination/Michael addition under commonly used moderately high-temperature conditions
    • DOI 10.1016/j.ab.2003.08.015
    • W Li PS Backlund RA Boykins G Wang HC Chen 2003 Susceptibility of the hydroxyl groups in serine and threonine to beta-elimination/Michael addition under commonly used moderately high-temperature conditions Anal Biochem 323 94 102 14622963 10.1016/j.ab.2003.08.015 1:CAS:528:DC%2BD3sXovVWgurk%3D (Pubitemid 37393362)
    • (2003) Analytical Biochemistry , vol.323 , Issue.1 , pp. 94-102
    • Li, W.1    Backlund, P.S.2    Boykins, R.A.3    Wang, G.4    Chen, H.-C.5
  • 37
    • 67650567049 scopus 로고    scopus 로고
    • Enhancing identifications of lipid-embedded proteins by mass spectrometry for improved mapping of endothelial plasma membranes in vivo
    • 19155209 10.1074/mcp.M800215-MCP200 1:CAS:528:DC%2BD1MXhtVegurvL
    • Y Li J Yu Y Wang NM Griffin F Long S Shore P Oh JE Schnitzer 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 19155209 10.1074/mcp.M800215-MCP200 1:CAS:528:DC%2BD1MXhtVegurvL
    • (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
  • 38
    • 0042266719 scopus 로고    scopus 로고
    • A genetic approach to mammalian glycan function
    • DOI 10.1146/annurev.biochem.72.121801.161809
    • JB Lowe JD Marth 2003 A genetic approach to Mammalian glycan function Annu Rev Biochem 72 643 691 12676797 10.1146/annurev.biochem.72.121801.161809 1:CAS:528:DC%2BD3sXntFSgtbs%3D (Pubitemid 36930456)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 643-691
    • Lowe, J.B.1    Marth, J.D.2
  • 39
    • 29244464778 scopus 로고    scopus 로고
    • Tube-gel digestion: A novel proteomic approach for high throughput analysis of membrane proteins
    • DOI 10.1074/mcp.M500138-MCP200
    • X Lu H Zhu 2005 Tube-gel digestion: a novel proteomic approach for high throughput analysis of membrane proteins Mol Cell Proteomics 4 1948 1958 16150870 10.1074/mcp.M500138-MCP200 1:CAS:528:DC%2BD2MXhtlWqsb%2FM (Pubitemid 41830189)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.12 , pp. 1948-1958
    • Lu, X.1    Zhu, H.2
  • 40
    • 66749090994 scopus 로고    scopus 로고
    • Comparative proteomic profiling of membrane proteins in rat cerebellum, spinal cord, and sciatic nerve
    • 19290618 10.1021/pr8010364 1:CAS:528:DC%2BD1MXktVejsbw%3D
    • A Lu JR Wisniewski M Mann 2009 Comparative proteomic profiling of membrane proteins in rat cerebellum, spinal cord, and sciatic nerve J Proteome Res 8 2418 2425 19290618 10.1021/pr8010364 1:CAS:528:DC%2BD1MXktVejsbw%3D
    • (2009) J Proteome Res , vol.8 , pp. 2418-2425
    • Lu, A.1    Wisniewski, J.R.2    Mann, M.3
  • 41
    • 67049098536 scopus 로고    scopus 로고
    • Efficient isolation and quantitative proteomic analysis of cancer cell plasma membrane proteins for identification of metastasis-associated cell surface markers
    • 19341246 10.1021/pr801091k 1:CAS:528:DC%2BD1MXltVKkt7Y%3D
    • R Lund R Leth-Larsen ON Jensen HJ Ditzel 2009 Efficient isolation and quantitative proteomic analysis of cancer cell plasma membrane proteins for identification of metastasis-associated cell surface markers J Proteome Res 8 3078 3090 19341246 10.1021/pr801091k 1:CAS:528:DC%2BD1MXltVKkt7Y%3D
    • (2009) J Proteome Res , vol.8 , pp. 3078-3090
    • Lund, R.1    Leth-Larsen, R.2    Jensen, O.N.3    Ditzel, H.J.4
  • 42
    • 57449099068 scopus 로고    scopus 로고
    • Precision proteomics: The case for high resolution and high mass accuracy
    • 18818311 10.1073/pnas.0800788105 1:CAS:528:DC%2BD1cXhsVOmsb7K
    • M Mann NL Kelleher 2008 Precision proteomics: the case for high resolution and high mass accuracy Proc Natl Acad Sci USA 105 18132 18138 18818311 10.1073/pnas.0800788105 1:CAS:528:DC%2BD1cXhsVOmsb7K
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 18132-18138
    • Mann, M.1    Kelleher, N.L.2
  • 43
    • 0034923505 scopus 로고    scopus 로고
    • Analysis of proteins and proteomes by mass spectrometry
    • DOI 10.1146/annurev.biochem.70.1.437
    • M Mann RC Hendrickson A Pandey 2001 Analysis of proteins and proteomes by mass spectrometry Annu Rev Biochem 70 437 473 11395414 10.1146/annurev.biochem. 70.1.437 1:CAS:528:DC%2BD3MXlsVehtL4%3D (Pubitemid 32662217)
    • (2001) Annual Review of Biochemistry , vol.70 , pp. 437-473
    • Mann, M.1    Hendrickson, R.C.2    Pandey, A.3
  • 44
    • 39749125069 scopus 로고    scopus 로고
    • Phase transfer surfactant-aided trypsin digestion for membrane proteome analysis
    • DOI 10.1021/pr700658q
    • T Masuda M Tomita Y Ishihama 2008 Phase transfer surfactant-aided trypsin digestion for membrane proteome analysis J Proteome Res 7 731 740 18183947 10.1021/pr700658q 1:CAS:528:DC%2BD1cXksVylsw%3D%3D (Pubitemid 351294035)
    • (2008) Journal of Proteome Research , vol.7 , Issue.2 , pp. 731-740
    • Masuda, T.1    Tomita, M.2    Ishihama, Y.3
  • 45
    • 75149180460 scopus 로고    scopus 로고
    • Unbiased quantitation of Escherichia coli membrane proteome using phase transfer surfactants
    • 19767571 10.1074/mcp.M900240-MCP200 1:CAS:528:DC%2BD1MXhsFOgsL7K
    • T Masuda N Saito M Tomita Y Ishihama 2009 Unbiased quantitation of Escherichia coli membrane proteome using phase transfer surfactants Mol Cell Proteomics 8 2770 2777 19767571 10.1074/mcp.M900240-MCP200 1:CAS:528: DC%2BD1MXhsFOgsL7K
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2770-2777
    • Masuda, T.1    Saito, N.2    Tomita, M.3    Ishihama, Y.4
  • 46
    • 61649103556 scopus 로고    scopus 로고
    • Combining results from lectin affinity chromatography and glycocapture approaches substantially improves the coverage of the glycoproteome
    • 18923192 1:CAS:528:DC%2BD1MXitV2ksr4%3D
    • CA McDonald JY Yang V Marathe TY Yen BA Macher 2009 Combining results from lectin affinity chromatography and glycocapture approaches substantially improves the coverage of the glycoproteome Mol Cell Proteomics 8 287 301 18923192 1:CAS:528:DC%2BD1MXitV2ksr4%3D
    • (2009) Mol Cell Proteomics , vol.8 , pp. 287-301
    • McDonald, C.A.1    Yang, J.Y.2    Marathe, V.3    Yen, T.Y.4    MacHer, B.A.5
  • 47
    • 58149383887 scopus 로고    scopus 로고
    • Detergent-based but gel-free method allows identification of several hundred membrane proteins in single LC-MS runs
    • 18839980 10.1021/pr800412j 1:CAS:528:DC%2BD1cXht1Wjsr3K
    • N Nagaraj A Lu M Mann JR Wisniewski 2008 Detergent-based but gel-free method allows identification of several hundred membrane proteins in single LC-MS runs J Proteome Res 7 5028 5032 18839980 10.1021/pr800412j 1:CAS:528:DC%2BD1cXht1Wjsr3K
    • (2008) J Proteome Res , vol.7 , pp. 5028-5032
    • Nagaraj, N.1    Lu, A.2    Mann, M.3    Wisniewski, J.R.4
  • 49
    • 11444263845 scopus 로고    scopus 로고
    • Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry
    • 14506206 10.1074/mcp.T300006-MCP200
    • TS Nuhse A Stensballe ON Jensen SC Peck 2003 Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry Mol Cell Proteomics 2 1234 1243 14506206 10.1074/mcp.T300006-MCP200
    • (2003) Mol Cell Proteomics , vol.2 , pp. 1234-1243
    • Nuhse, T.S.1    Stensballe, A.2    Jensen, O.N.3    Peck, S.C.4
  • 50
    • 4544291080 scopus 로고    scopus 로고
    • Phosphoproteomics of the arabidopsis plasma membrane and a new phosphorylation site database W inside box sign
    • DOI 10.1105/tpc.104.023150
    • TS Nuhse A Stensballe ON Jensen SC Peck 2004 Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database Plant Cell 16 2394 2405 15308754 10.1105/tpc.104.023150 (Pubitemid 39247080)
    • (2004) Plant Cell , vol.16 , Issue.9 , pp. 2394-2405
    • Nuhse, T.S.1    Stensballe, A.2    Jensen, O.N.3    Peck, S.C.4
  • 51
    • 29244447154 scopus 로고    scopus 로고
    • Cell surface labeling and mass spectrometry reveal diversity of cell surface markers and signaling molecules expressed in undifferentiated mouse embryonic stem cells
    • DOI 10.1074/mcp.M500216-MCP200
    • K Nunomura K Nagano C Itagaki M Taoka N Okamura Y Yamauchi S Sugano N Takahashi T Izumi T Isobe 2005 Cell surface labeling and mass spectrometry reveal diversity of cell surface markers and signaling molecules expressed in undifferentiated mouse embryonic stem cells Mol Cell Proteomics 4 1968 1976 16176923 10.1074/mcp.M500216-MCP200 1:CAS:528:DC%2BD2MXhtlWqsb%2FO (Pubitemid 41830191)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.12 , pp. 1968-1976
    • Nunomura, K.1    Nagano, K.2    Itagaki, C.3    Masato, T.4    Okamura, N.5    Yamauchi, Y.6    Sugano, S.7    Takahashi, N.8    Izumi, T.9    Isobe, T.10
  • 52
    • 2942529235 scopus 로고    scopus 로고
    • Subtractive proteomic mapping of the endothelial surface in lung and solid tumours for tissue-specific therapy
    • DOI 10.1038/nature02580
    • P Oh Y Li J Yu E Durr KM Krasinska LA Carver JE Testa JE Schnitzer 2004 Subtractive proteomic mapping of the endothelial surface in lung and solid tumours for tissue-specific therapy Nature 429 629 635 15190345 10.1038/nature02580 1:CAS:528:DC%2BD2cXks1Kls7c%3D (Pubitemid 38812308)
    • (2004) Nature , vol.429 , Issue.6992 , 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
  • 53
    • 2142721825 scopus 로고    scopus 로고
    • HysTag - A novel proteomic quantification tool applied to differential display analysis of membrane proteins from distinct areas of mouse brain
    • DOI 10.1074/mcp.M300103-MCP200
    • JV Olsen JR Andersen PA Nielsen ML Nielsen D Figeys M Mann JR Wisniewski 2004 HysTag-a novel proteomic quantification tool applied to differential display analysis of membrane proteins from distinct areas of mouse brain Mol Cell Proteomics 3 82 92 14610161 1:CAS:528:DC%2BD2cXhtVantLg%3D (Pubitemid 38697107)
    • (2004) Molecular and Cellular Proteomics , vol.3 , Issue.1 , pp. 82-92
    • Olsen, J.V.1    Andersen, J.R.2    Nielsen, P.Aa.3    Nielsen, M.L.4    Figeys, D.5    Mann, M.6    Wisniewski, J.R.7
  • 54
    • 33750456519 scopus 로고    scopus 로고
    • Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks
    • DOI 10.1016/j.cell.2006.09.026, PII S0092867406012748
    • JV Olsen B Blagoev F Gnad B Macek C Kumar P Mortensen M Mann 2006 Global, in vivo, and site-specific phosphorylation dynamics in signaling networks Cell 127 635 648 17081983 10.1016/j.cell.2006.09.026 1:CAS:528:DC%2BD28Xht1WgtbzO (Pubitemid 44647421)
    • (2006) Cell , vol.127 , Issue.3 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 55
    • 33846376260 scopus 로고    scopus 로고
    • Quantitative proteomic profiling of membrane proteins from the mouse brain cortex, hippocampus, and cerebellum using the HysTag reagent: Mapping of neurotransmitter receptors and ion channels
    • DOI 10.1016/j.brainres.2006.11.082, PII S0006899306034731
    • JV Olsen PA Nielsen JR Andersen M Mann JR Wisniewski 2007 Quantitative proteomic profiling of membrane proteins from the mouse brain cortex, hippocampus, and cerebellum using the HysTag reagent: mapping of neurotransmitter receptors and ion channels Brain Res 1134 95 106 17207779 10.1016/j.brainres.2006.11.082 1:CAS:528:DC%2BD2sXpvFSjsQ%3D%3D (Pubitemid 46135536)
    • (2007) Brain Research , vol.1134 , Issue.1 , pp. 95-106
    • Olsen, J.V.1    Nielsen, P.Aa.2    Andersen, J.R.3    Mann, M.4    Wisniewski, J.R.5
  • 56
    • 77954378942 scopus 로고    scopus 로고
    • Proteome, phosphoproteome, and N-glycoproteome are quantitatively preserved in formalin-fixed paraffin-embedded tissue and analyzable by high-resolution mass spectrometry
    • 20469934 10.1021/pr100234w 1:CAS:528:DC%2BC3cXmsFSnsrk%3D
    • P Ostasiewicz DF Zielinska M Mann JR Wisniewski 2010 Proteome, phosphoproteome, and N-glycoproteome are quantitatively preserved in formalin-fixed paraffin-embedded tissue and analyzable by high-resolution mass spectrometry J Proteome Res 9 3688 3700 20469934 10.1021/pr100234w 1:CAS:528:DC%2BC3cXmsFSnsrk%3D
    • (2010) J Proteome Res , vol.9 , pp. 3688-3700
    • Ostasiewicz, P.1    Zielinska, D.F.2    Mann, M.3    Wisniewski, J.R.4
  • 57
    • 11144300133 scopus 로고    scopus 로고
    • Integration of Jacobson's pellicle method into proteomic strategies for plasma membrane proteins
    • DOI 10.1021/pr040004t
    • AM Rahbar C Fenselau 2004 Integration of Jacobson's pellicle method into proteomic strategies for plasma membrane proteins J Proteome Res 3 1267 1277 15595737 10.1021/pr040004t 1:CAS:528:DC%2BD2cXotlalt7o%3D (Pubitemid 40040382)
    • (2004) Journal of Proteome Research , vol.3 , Issue.6 , pp. 1267-1277
    • Rahbar, A.M.1    Fenselau, C.2
  • 58
    • 29144449245 scopus 로고    scopus 로고
    • Unbiased examination of changes in plasma membrane proteins in drug resistant cancer cells
    • DOI 10.1021/pr0502370
    • AM Rahbar C Fenselau 2005 Unbiased examination of changes in plasma membrane proteins in drug resistant cancer cells J Proteome Res 4 2148 2153 16335961 10.1021/pr0502370 1:CAS:528:DC%2BD2MXhtFegs7vE (Pubitemid 41814282)
    • (2005) Journal of Proteome Research , vol.4 , Issue.6 , pp. 2148-2153
    • Rahbar, A.M.1    Fenselau, C.2
  • 59
    • 33644663350 scopus 로고    scopus 로고
    • Proteomic analysis of brain plasma membranes isolated by affinity two-phase partitioning
    • DOI 10.1074/mcp.T500017-MCP200
    • J Schindler U Lewandrowski A Sickmann E Friauf HG Nothwang 2006 Proteomic analysis of brain plasma membranes isolated by affinity two-phase partitioning Mol Cell Proteomics 5 390 400 16249173 1:CAS:528:DC%2BD28XitVeqsLs%3D (Pubitemid 43329316)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.2 , pp. 390-400
    • Schindler, J.1    Lewandrowski, U.2    Sickmann, A.3    Friauf, E.4    Nothwang, H.G.5
  • 60
    • 70350519351 scopus 로고    scopus 로고
    • Finding one's way in proteomics: A protein species nomenclature
    • 19740416 10.1186/1752-153X-3-11
    • H Schluter R Apweiler HG Holzhutter PR Jungblut 2009 Finding one's way in proteomics: a protein species nomenclature Chem Cent J 3 11 19740416 10.1186/1752-153X-3-11
    • (2009) Chem Cent J , vol.3 , pp. 11
    • Schluter, H.1    Apweiler, R.2    Holzhutter, H.G.3    Jungblut, P.R.4
  • 61
    • 61849145815 scopus 로고    scopus 로고
    • Exploiting differential dissociation chemistries of O-linked glycopeptide ions for the localization of mucin-type protein glycosylation
    • 19067536 10.1021/pr8007072 1:CAS:528:DC%2BD1cXhsVOmtrrK
    • RR Seipert ED Dodds CB Lebrilla 2009 Exploiting differential dissociation chemistries of O-linked glycopeptide ions for the localization of mucin-type protein glycosylation J Proteome Res 8 493 501 19067536 10.1021/pr8007072 1:CAS:528:DC%2BD1cXhsVOmtrrK
    • (2009) J Proteome Res , vol.8 , pp. 493-501
    • Seipert, R.R.1    Dodds, E.D.2    Lebrilla, C.B.3
  • 62
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • DOI 10.1021/ac950914h
    • A Shevchenko M Wilm O Vorm M Mann 1996 Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels Anal Chem 68 850 858 8779443 10.1021/ac950914h 1:CAS:528:DyaK28XntlygtA%3D%3D (Pubitemid 26101214)
    • (1996) Analytical Chemistry , vol.68 , Issue.5 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 63
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • 17406544 10.1038/nprot.2006.468 1:CAS:528:DC%2BD2sXhtFGjt7nM
    • A Shevchenko H Tomas J Havlis JV Olsen M Mann 2006 In-gel digestion for mass spectrometric characterization of proteins and proteomes Nat Protoc 1 2856 2860 17406544 10.1038/nprot.2006.468 1:CAS:528:DC%2BD2sXhtFGjt7nM
    • (2006) Nat Protoc , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 64
    • 33751004676 scopus 로고    scopus 로고
    • Global profiling of surface plasma membrane proteome of oviductal epithelial cells
    • DOI 10.1021/pr060366w
    • E Sostaric AS Georgiou CH Wong PF Watson WV Holt A Fazeli 2006 Global profiling of surface plasma membrane proteome of oviductal epithelial cells J Proteome Res 5 3029 3037 17081054 10.1021/pr060366w 1:CAS:528:DC%2BD28XhtVyrsbfN (Pubitemid 44749220)
    • (2006) Journal of Proteome Research , vol.5 , Issue.11 , pp. 3029-3037
    • Sostaric, E.1    Georgiou, A.S.2    Wong, C.H.3    Watson, P.F.4    Holt, W.V.5    Fazeli, A.6
  • 65
    • 33645748520 scopus 로고    scopus 로고
    • Selective isolation of glycoproteins and glycopeptides for MALDI-TOF MS detection supported by magnetic particles
    • 16522863
    • K Sparbier S Koch I Kessler T Wenzel M Kostrzewa 2005 Selective isolation of glycoproteins and glycopeptides for MALDI-TOF MS detection supported by magnetic particles J Biomol Tech 16 407 413 16522863
    • (2005) J Biomol Tech , vol.16 , pp. 407-413
    • Sparbier, K.1    Koch, S.2    Kessler, I.3    Wenzel, T.4    Kostrzewa, M.5
  • 66
    • 34548202704 scopus 로고    scopus 로고
    • Proteomics of integral membrane proteins - Theory and application
    • DOI 10.1021/cr068286z
    • AE Speers CC Wu 2007 Proteomics of integral membrane proteins-theory and application Chem Rev 107 3687 3714 17683161 10.1021/cr068286z 1:CAS:528:DC%2BD2sXos1egs7o%3D (Pubitemid 47322748)
    • (2007) Chemical Reviews , vol.107 , Issue.8 , pp. 3687-3714
    • Speers, A.E.1    Wu, C.C.2
  • 67
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: Nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • RG Spiro 2002 Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds Glycobiology 12 43R 56R 12042244 10.1093/glycob/12.4.43R 1:CAS:528:DC%2BD38XltVyhtrY%3D (Pubitemid 34760066)
    • (2002) Glycobiology , vol.12 , Issue.4
    • Spiro, R.G.1
  • 68
    • 0035258256 scopus 로고    scopus 로고
    • Characterization of phosphoproteins from electrophoretic gels by nanoscale Fe(III) affinity chromatography with off-line mass spectrometry analysis
    • A Stensballe S Andersen ON Jensen 2001 Characterization of phosphoproteins from electrophoretic gels by nanoscale Fe(III) affinity chromatography with off-line mass spectrometry analysis Proteomics 1 207 222 11680868 10.1002/1615-9861(200102)1:2<207::AID-PROT207>3.0.CO;2-3 1:CAS:528:DC%2BD3MXhvVCisrw%3D (Pubitemid 33586717)
    • (2001) Proteomics , vol.1 , Issue.2 , pp. 207-222
    • Stensballe, A.1    Andersen, S.2    Jensen, O.N.3
  • 70
    • 44449123735 scopus 로고    scopus 로고
    • +-immobilized magnetic nanoparticles for phosphoproteome analysis of the plasma membrane of mouse liver
    • 18266315 10.1021/pr700655d 1:CAS:528:DC%2BD1cXhsl2qurk%3D
    • +-immobilized magnetic nanoparticles for phosphoproteome analysis of the plasma membrane of mouse liver J Proteome Res 7 1078 1087 18266315 10.1021/pr700655d 1:CAS:528:DC%2BD1cXhsl2qurk%3D
    • (2008) J Proteome Res , vol.7 , pp. 1078-1087
    • Tan, F.1    Zhang, Y.2    Mi, W.3    Wang, J.4    Wei, J.5    Cai, Y.6    Qian, X.7
  • 71
    • 53049101603 scopus 로고    scopus 로고
    • TiO(2)-based phosphoproteomic analysis of the plasma membrane and the effects of phosphatase inhibitor treatment
    • 18578522 10.1021/pr800099y 1:CAS:528:DC%2BD1cXns1yqtr0%3D
    • TE Thingholm MR Larsen CR Ingrell M Kassem ON Jensen 2008 TiO(2)-based phosphoproteomic analysis of the plasma membrane and the effects of phosphatase inhibitor treatment J Proteome Res 7 3304 3313 18578522 10.1021/pr800099y 1:CAS:528:DC%2BD1cXns1yqtr0%3D
    • (2008) J Proteome Res , vol.7 , pp. 3304-3313
    • Thingholm, T.E.1    Larsen, M.R.2    Ingrell, C.R.3    Kassem, M.4    Jensen, O.N.5
  • 72
    • 65249162283 scopus 로고    scopus 로고
    • N-linked glycoproteomic analysis of formalin-fixed and paraffin-embedded tissues
    • 19714870 10.1021/pr800952h 1:CAS:528:DC%2BD1MXisVCjtL4%3D
    • Y Tian K Gurley DL Meany CJ Kemp H Zhang 2009 N-linked glycoproteomic analysis of formalin-fixed and paraffin-embedded tissues J Proteome Res 8 1657 1662 19714870 10.1021/pr800952h 1:CAS:528:DC%2BD1MXisVCjtL4%3D
    • (2009) J Proteome Res , vol.8 , pp. 1657-1662
    • Tian, Y.1    Gurley, K.2    Meany, D.L.3    Kemp, C.J.4    Zhang, H.5
  • 75
    • 0035937586 scopus 로고    scopus 로고
    • Glycosylation of nucleocytoplasmic proteins: Signal transduction and O-GlcNAc
    • DOI 10.1126/science.1058714
    • L Wells K Vosseller GW Hart 2001 Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc Science 291 2376 2378 11269319 10.1126/science.1058714 1:CAS:528:DC%2BD3MXit1Knsb0%3D (Pubitemid 32231793)
    • (2001) Science , vol.291 , Issue.5512 , pp. 2376-2378
    • Wells, L.1    Vosseller, K.2    Hart, G.W.3
  • 76
    • 54449100126 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics: Principles, perspectives, and challenges
    • 18834211 1:CAS:528:DC%2BD1cXht1OmsbfK
    • JR Wisniewski 2008 Mass spectrometry-based proteomics: principles, perspectives, and challenges Arch Pathol Lab Med 132 1566 1569 18834211 1:CAS:528:DC%2BD1cXht1OmsbfK
    • (2008) Arch Pathol Lab Med , vol.132 , pp. 1566-1569
    • Wisniewski, J.R.1
  • 77
    • 70350728339 scopus 로고    scopus 로고
    • Spin filter-based sample preparation for shotgun proteomics (Reply)
    • 10.1038/nmeth1109-785b 1:CAS:528:DC%2BD1MXhtlaksrvO
    • JR Wisniewski M Mann 2009 Spin filter-based sample preparation for shotgun proteomics (Reply) Nat Methods 6 785 786 10.1038/nmeth1109-785b 1:CAS:528:DC%2BD1MXhtlaksrvO
    • (2009) Nat Methods , vol.6 , pp. 785-786
    • Wisniewski, J.R.1    Mann, M.2
  • 78
    • 71549117585 scopus 로고    scopus 로고
    • Combination of FASP and StageTip-based fractionation allows in-depth analysis of the hippocampal membrane proteome
    • 19848406 10.1021/pr900748n 1:CAS:528:DC%2BD1MXhtl2qu73K
    • JR Wisniewski A Zougman M Mann 2009 Combination of FASP and StageTip-based fractionation allows in-depth analysis of the hippocampal membrane proteome J Proteome Res 8 5674 5678 19848406 10.1021/pr900748n 1:CAS:528:DC%2BD1MXhtl2qu73K
    • (2009) J Proteome Res , vol.8 , pp. 5674-5678
    • Wisniewski, J.R.1    Zougman, A.2    Mann, M.3
  • 79
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • 19377485 10.1038/nmeth.1322 1:CAS:528:DC%2BD1MXks12ksb0%3D
    • JR Wisniewski A Zougman N Nagaraj M Mann 2009 Universal sample preparation method for proteome analysis Nat Methods 6 359 362 19377485 10.1038/nmeth.1322 1:CAS:528:DC%2BD1MXks12ksb0%3D
    • (2009) Nat Methods , vol.6 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 80
    • 77954565509 scopus 로고    scopus 로고
    • Brain phosphoproteome obtained by a FASP-based method reveals plasma membrane protein topology
    • 20415495 10.1021/pr1002214 1:CAS:528:DC%2BC3cXlslygsr4%3D
    • JR Wisniewski N Nagaraj A Zougman F Gnad M Mann 2010 Brain phosphoproteome obtained by a FASP-based method reveals plasma membrane protein topology J Proteome Res 9 3280 3289 20415495 10.1021/pr1002214 1:CAS:528:DC%2BC3cXlslygsr4%3D
    • (2010) J Proteome Res , vol.9 , pp. 3280-3289
    • Wisniewski, J.R.1    Nagaraj, N.2    Zougman, A.3    Gnad, F.4    Mann, M.5
  • 81
    • 64349089985 scopus 로고    scopus 로고
    • Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins
    • 19349973 10.1038/nbt.1532 1:CAS:528:DC%2BD1MXktVKgtro%3D
    • B Wollscheid D Bausch-Fluck C Henderson R O'Brien M Bibel R Schiess R Aebersold JD Watts 2009 Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins Nat Biotechnol 27 378 386 19349973 10.1038/nbt.1532 1:CAS:528:DC%2BD1MXktVKgtro%3D
    • (2009) Nat Biotechnol , vol.27 , pp. 378-386
    • Wollscheid, B.1    Bausch-Fluck, D.2    Henderson, C.3    O'Brien, R.4    Bibel, M.5    Schiess, R.6    Aebersold, R.7    Watts, J.D.8
  • 82
    • 0028490510 scopus 로고
    • Protein surface oligosaccharides and protein function
    • 7664073 10.1038/nsb0894-499 1:CAS:528:DyaK2MXitVGhs7w%3D
    • RJ Woods CJ Edge RA Dwek 1994 Protein surface oligosaccharides and protein function Nat Struct Biol 1 499 501 7664073 10.1038/nsb0894-499 1:CAS:528:DyaK2MXitVGhs7w%3D
    • (1994) Nat Struct Biol , vol.1 , pp. 499-501
    • Woods, R.J.1    Edge, C.J.2    Dwek, R.A.3
  • 83
    • 0037337308 scopus 로고    scopus 로고
    • The application of mass spectrometry to membrane proteomics
    • DOI 10.1038/nbt0303-262
    • CC Wu JR Yates 3rd 2003 The application of mass spectrometry to membrane proteomics Nat Biotechnol 21 262 267 12610573 10.1038/nbt0303-262 1:CAS:528:DC%2BD3sXhsFajsrs%3D (Pubitemid 36314809)
    • (2003) Nature Biotechnology , vol.21 , Issue.3 , pp. 262-267
    • Wu, C.C.1    Yates III, J.R.2
  • 84
    • 0038561131 scopus 로고    scopus 로고
    • A method for the comprehensive proteomic analysis of membrane proteins
    • DOI 10.1038/nbt819
    • CC Wu MJ MacCoss KE Howell JR Yates 3rd 2003 A method for the comprehensive proteomic analysis of membrane proteins Nat Biotechnol 21 532 538 12692561 10.1038/nbt819 1:CAS:528:DC%2BD3sXjt1Onsb4%3D (Pubitemid 36532018)
    • (2003) Nature Biotechnology , vol.21 , Issue.5 , pp. 532-538
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Yates III, J.R.4
  • 85
    • 0348142250 scopus 로고    scopus 로고
    • Comparative Proteomics of Glycoproteins Based on Lectin Selection and Isotope Coding
    • DOI 10.1021/pr0340274
    • L Xiong D Andrews F Regnier 2003 Comparative proteomics of glycoproteins based on lectin selection and isotope coding J Proteome Res 2 618 625 14692455 10.1021/pr0340274 1:CAS:528:DC%2BD3sXmtVShsr4%3D (Pubitemid 38017106)
    • (2003) Journal of Proteome Research , vol.2 , Issue.6 , pp. 618-625
    • Xiong, L.1    Andrews, D.2    Regnier, F.3
  • 86
    • 33749145859 scopus 로고    scopus 로고
    • Multilectin affinity chromatography for characterization of multiple glycoprotein biomarker candidates in serum from breast cancer patients
    • DOI 10.1373/clinchem.2005.065862
    • Z Yang LE Harris DE Palmer-Toy WS Hancock 2006 Multilectin affinity chromatography for characterization of multiple glycoprotein biomarker candidates in serum from breast cancer patients Clin Chem 52 1897 1905 16916992 10.1373/clinchem.2005.065862 1:CAS:528:DC%2BD28XhtVCgtb%2FM (Pubitemid 44470697)
    • (2006) Clinical Chemistry , vol.52 , Issue.10 , pp. 1897-1905
    • Yang, Z.1    Harris, L.E.2    Palmer-Toy, D.E.3    Hancock, W.S.4
  • 87
    • 70349991237 scopus 로고    scopus 로고
    • Optimization of protein solubilization for the analysis of the CD14 human monocyte membrane proteome using LC-MS/MS
    • 19709643 10.1016/j.jprot.2009.08.008 1:CAS:528:DC%2BD1MXhtlWitrjJ
    • X Ye DJ Johann Jr RM Hakami Z Xiao Z Meng RG Ulrich HJ Issaq TD Veenstra J Blonder 2009 Optimization of protein solubilization for the analysis of the CD14 human monocyte membrane proteome using LC-MS/MS J Proteomics 73 112 122 19709643 10.1016/j.jprot.2009.08.008 1:CAS:528:DC%2BD1MXhtlWitrjJ
    • (2009) J Proteomics , vol.73 , pp. 112-122
    • Ye, X.1    Johann Jr., D.J.2    Hakami, R.M.3    Xiao, Z.4    Meng, Z.5    Ulrich, R.G.6    Issaq, H.J.7    Veenstra, T.D.8    Blonder, J.9
  • 88
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • DOI 10.1038/nbt827
    • H Zhang XJ Li DB Martin R Aebersold 2003 Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry Nat Biotechnol 21 660 666 12754519 10.1038/nbt827 1:CAS:528:DC%2BD3sXktFSlu7s%3D (Pubitemid 36638093)
    • (2003) Nature Biotechnology , vol.21 , Issue.6 , pp. 660-666
    • Zhang, H.1    Li, X.-J.2    Martin, D.B.3    Aebersold, R.4
  • 89
    • 28444455281 scopus 로고    scopus 로고
    • Proteomic analysis of mouse liver plasma membrane: Use of differential extraction to enrich Hydrophobic membrane proteins
    • DOI 10.1002/pmic.200401318
    • L Zhang J Xie X Wang X Liu X Tang R Cao W Hu S Nie C Fan S Liang 2005 Proteomic analysis of mouse liver plasma membrane: use of differential extraction to enrich hydrophobic membrane proteins Proteomics 5 4510 4524 16222721 10.1002/pmic.200401318 1:CAS:528:DC%2BD2MXht12nt7rI (Pubitemid 41739929)
    • (2005) Proteomics , vol.5 , Issue.17 , pp. 4510-4524
    • Zhang, L.1    Xie, J.2    Wang, X.3    Liu, X.4    Tang, X.5    Cao, R.6    Hu, W.7    Nie, S.8    Fan, C.9    Liang, S.10
  • 90
    • 1842529218 scopus 로고    scopus 로고
    • Proteomic Analysis of Integral Plasma Membrane Proteins
    • DOI 10.1021/ac0354037
    • Y Zhao W Zhang Y Kho Y Zhao 2004 Proteomic analysis of integral plasma membrane proteins Anal Chem 76 1817 1823 15053638 10.1021/ac0354037 1:CAS:528:DC%2BD2cXhs1WmsbY%3D (Pubitemid 38451494)
    • (2004) Analytical Chemistry , vol.76 , Issue.7 , pp. 1817-1823
    • Zhao, Y.1    Zhang, W.2    Kho, Y.3    Zhao, Y.4
  • 91
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • 20510933 10.1016/j.cell.2010.04.012 1:CAS:528:DC%2BC3cXnsFKmsLc%3D
    • DF Zielinska F Gnad JR Wisniewski M Mann 2010 Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints Cell 141 897 907 20510933 10.1016/j.cell.2010.04.012 1:CAS:528:DC%2BC3cXnsFKmsLc%3D
    • (2010) Cell , vol.141 , pp. 897-907
    • Zielinska, D.F.1    Gnad, F.2    Wisniewski, J.R.3    Mann, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.