메뉴 건너뛰기




Volumn 33, Issue 1, 2008, Pages 3-11

Methods and approaches for the comprehensive characterization and quantification of cellular proteomes using mass spectrometry

Author keywords

Isotopic labeling; Phosphoproteomics; Quantitative proteomics

Indexed keywords

CELL PROTEIN; PROTEOME;

EID: 41349089337     PISSN: 10948341     EISSN: 15312267     Source Type: Journal    
DOI: 10.1152/physiolgenomics.00292.2007     Document Type: Review
Times cited : (41)

References (130)
  • 1
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold R, Mann M. Mass spectrometry-based proteomics. Nature 422: 198-207, 2003.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 3
    • 5444230640 scopus 로고    scopus 로고
    • Dynamic identification of phosphopeptides using immobilized metal ion affinity chromatography enrichment, subsequent partial beta-elimination/ chemical tagging and matrix-assisted laser desorption/ionization mass spectrometric analysis
    • Ahn YH, Park EJ, Cho K, Kim JY, Ha SH, Ryu SH, Yoo JS. Dynamic identification of phosphopeptides using immobilized metal ion affinity chromatography enrichment, subsequent partial beta-elimination/ chemical tagging and matrix-assisted laser desorption/ionization mass spectrometric analysis. Rapid Commun Mass Spectrom 18: 2495-2501, 2004.
    • (2004) Rapid Commun Mass Spectrom , vol.18 , pp. 2495-2501
    • Ahn, Y.H.1    Park, E.J.2    Cho, K.3    Kim, J.Y.4    Ha, S.H.5    Ryu, S.H.6    Yoo, J.S.7
  • 4
    • 0026069069 scopus 로고
    • Recognition of phosphate groups by immobilized aluminium( III) ions
    • Andersson L. Recognition of phosphate groups by immobilized aluminium( III) ions. J Chromatogr A 539: 327-334, 1991.
    • (1991) J Chromatogr A , vol.539 , pp. 327-334
    • Andersson, L.1
  • 7
    • 0032990126 scopus 로고    scopus 로고
    • Electron capture dissociation of substance P using a commercially available Fourier transform ion cyclotron resonance mass spectrometer
    • Axelsson J, Palmblad M, Hakansson K, Hakansson P. Electron capture dissociation of substance P using a commercially available Fourier transform ion cyclotron resonance mass spectrometer. Rapid Commun Mass Spectrom 13: 474-477, 1999.
    • (1999) Rapid Commun Mass Spectrom , vol.13 , pp. 474-477
    • Axelsson, J.1    Palmblad, M.2    Hakansson, K.3    Hakansson, P.4
  • 10
    • 0036177656 scopus 로고    scopus 로고
    • Phosphopeptide detection and sequencing by matrix-assisted laser desorption/ionization quadrupole time-of-flight tandem mass spectrometry
    • Bennett KL, Stensballe A, Podtelejnikov AV, Moniatte M, Jensen ON. Phosphopeptide detection and sequencing by matrix-assisted laser desorption/ionization quadrupole time-of-flight tandem mass spectrometry. J Mass Spectrom 37: 179-190, 2002.
    • (2002) J Mass Spectrom , vol.37 , pp. 179-190
    • Bennett, K.L.1    Stensballe, A.2    Podtelejnikov, A.V.3    Moniatte, M.4    Jensen, O.N.5
  • 11
    • 0025670535 scopus 로고
    • Sequencing of peptides by tandem mass spectrometry and high-energy collision-induced dissociation
    • Biemann K. Sequencing of peptides by tandem mass spectrometry and high-energy collision-induced dissociation. Methods Enzymol 193: 455-479, 1990.
    • (1990) Methods Enzymol , vol.193 , pp. 455-479
    • Biemann, K.1
  • 12
    • 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 PV, Chelius D, Shaler TA. 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.
    • (2002) Anal Chem , vol.74 , pp. 4741-4749
    • Bondarenko, P.V.1    Chelius, D.2    Shaler, T.A.3
  • 13
    • 0037417791 scopus 로고    scopus 로고
    • Quantitation of changes in protein phosphorylation: A simple method based on stable isotope labeling and mass spectrometry
    • Bonenfant D, Schmelzle T, Jacinto E, Crespo JL, Mini T, Hall MN, Jenoe P. Quantitation of changes in protein phosphorylation: a simple method based on stable isotope labeling and mass spectrometry. Proc Natl Acad Sci USA 100: 880-885, 2003.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 880-885
    • Bonenfant, D.1    Schmelzle, T.2    Jacinto, E.3    Crespo, J.L.4    Mini, T.5    Hall, M.N.6    Jenoe, P.7
  • 14
    • 3042662113 scopus 로고    scopus 로고
    • In silico proteome analysis to facilitate proteomics experiments using mass spectrometry
    • Cagney G, Amiri S, Premawaradena T, Lindo M, Emili A. In silico proteome analysis to facilitate proteomics experiments using mass spectrometry. Proteome Sci 1: 5, 2003.
    • (2003) Proteome Sci , vol.1 , pp. 5
    • Cagney, G.1    Amiri, S.2    Premawaradena, T.3    Lindo, M.4    Emili, A.5
  • 15
    • 0035975882 scopus 로고    scopus 로고
    • Twenty-five years of immobilized metal ion affinity chromatography: Past, present and future
    • Chaga GS. Twenty-five years of immobilized metal ion affinity chromatography: past, present and future. J Biochem Biophys Methods 49: 313-334, 2001.
    • (2001) J Biochem Biophys Methods , vol.49 , pp. 313-334
    • Chaga, G.S.1
  • 16
    • 0036665581 scopus 로고    scopus 로고
    • Quantitative profiling of proteins in complex mixtures using liquid chromatography and mass spectrometry
    • Chelius D, Bondarenko PV. Quantitative profiling of proteins in complex mixtures using liquid chromatography and mass spectrometry. J Proteome Res 1: 317-323, 2002.
    • (2002) J Proteome Res , vol.1 , pp. 317-323
    • Chelius, D.1    Bondarenko, P.V.2
  • 17
    • 33646570847 scopus 로고    scopus 로고
    • Isobaric tags for relative and absolute quantitation (iTRAQ) reproducibility: Implication of multiple injections
    • Chong PK, Gan CS, Pham TK, Wright PC. Isobaric tags for relative and absolute quantitation (iTRAQ) reproducibility: implication of multiple injections. J Proteome Res 5: 1232-1240, 2006.
    • (2006) J Proteome Res , vol.5 , pp. 1232-1240
    • Chong, P.K.1    Gan, C.S.2    Pham, T.K.3    Wright, P.C.4
  • 19
    • 0031148680 scopus 로고    scopus 로고
    • Mass spectrometry of whole proteins eluted from sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels
    • Cohen SL, Chait BT. Mass spectrometry of whole proteins eluted from sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels. Anal Biochem 247: 257-267, 1997.
    • (1997) Anal Biochem , vol.247 , pp. 257-267
    • Cohen, S.L.1    Chait, B.T.2
  • 20
    • 34547163411 scopus 로고    scopus 로고
    • Dynamic collision-induced dissociation of peptides in a quadrupole ion trap mass spectrometer
    • Collin OL, Beier M, Jackson GP. Dynamic collision-induced dissociation of peptides in a quadrupole ion trap mass spectrometer. Anal Chem 79: 5468-5473, 2007.
    • (2007) Anal Chem , vol.79 , pp. 5468-5473
    • Collin, O.L.1    Beier, M.2    Jackson, G.P.3
  • 21
  • 24
    • 37249014081 scopus 로고    scopus 로고
    • The biological impact of mass-spectrometry-based proteomics
    • Cravatt BF, Simon GM, Yates JR 3rd. The biological impact of mass-spectrometry-based proteomics. Nature 450: 991-1000, 2007.
    • (2007) Nature , vol.450 , pp. 991-1000
    • Cravatt, B.F.1    Simon, G.M.2    Yates 3rd, J.R.3
  • 25
    • 0024502683 scopus 로고
    • Determination of changes in the phosphorylation state of the neuron-specific protein kinase C substrate B-50 (GAP43) by quantitative immunoprecipitation
    • De Graan PN, Dekker LV, Oestreicher AB, Van der Voorn L, Gispen WH. Determination of changes in the phosphorylation state of the neuron-specific protein kinase C substrate B-50 (GAP43) by quantitative immunoprecipitation. J Neurochem 52: 17-23, 1989.
    • (1989) J Neurochem , vol.52 , pp. 17-23
    • De Graan, P.N.1    Dekker, L.V.2    Oestreicher, A.B.3    Van der Voorn, L.4    Gispen, W.H.5
  • 26
    • 0037294431 scopus 로고    scopus 로고
    • Emerging strategies in mass-spectrometry based proteomics
    • Dreger M. Emerging strategies in mass-spectrometry based proteomics. Eur J Biochem 270: 569, 2003.
    • (2003) Eur J Biochem , vol.270 , pp. 569
    • Dreger, M.1
  • 27
    • 32444436985 scopus 로고    scopus 로고
    • Top-down approaches for measuring expression ratios of intact yeast proteins using Fourier transform mass spectrometry
    • Du Y, Parks BA, Sohn S, Kwast KE, Kelleher NL. Top-down approaches for measuring expression ratios of intact yeast proteins using Fourier transform mass spectrometry. Anal Chem 78: 686-694, 2006.
    • (2006) Anal Chem , vol.78 , pp. 686-694
    • Du, Y.1    Parks, B.A.2    Sohn, S.3    Kwast, K.E.4    Kelleher, N.L.5
  • 28
    • 0033934709 scopus 로고    scopus 로고
    • A general method for the rapid characterization of tyrosine-phosphorylated proteins by mini two-dimensional gel electrophoresis
    • Ducret A, Desponts C, Desmarais S, Gresser MJ, Ramachandran C. A general method for the rapid characterization of tyrosine-phosphorylated proteins by mini two-dimensional gel electrophoresis. Electrophoresis 21: 2196-2208, 2000.
    • (2000) Electrophoresis , vol.21 , pp. 2196-2208
    • Ducret, A.1    Desponts, C.2    Desmarais, S.3    Gresser, M.J.4    Ramachandran, C.5
  • 29
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng JK, McCormack AL, Yates JR. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J Am Soc Mass Spectrom 5: 976-989, 1994.
    • (1994) J Am Soc Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 30
    • 34848886063 scopus 로고    scopus 로고
    • Immobilized zirconium ion affinity chromatography for specific enrichment of phosphopeptides in phosphoproteome analysis
    • Feng S, Ye M, Zhou H, Jiang X, Jiang X, Zou H, Gong B. Immobilized zirconium ion affinity chromatography for specific enrichment of phosphopeptides in phosphoproteome analysis. Mol Cell Proteomics 6: 1656-1665, 2007.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1656-1665
    • Feng, S.1    Ye, M.2    Zhou, H.3    Jiang, X.4    Jiang, X.5    Zou, H.6    Gong, B.7
  • 31
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn JB, Mann M, Meng CK, Wong SF, Whitehouse CM. Electrospray ionization for mass spectrometry of large biomolecules. Science 246: 64-71, 1989.
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 32
    • 0025871647 scopus 로고
    • Antiphosphotyrosine immunoprecipitation of an insulin-stimulated receptor phosphatase activity from FRTL5 cells
    • Formisano P, Condorelli G, Condorelli G, Beguinot F. Antiphosphotyrosine immunoprecipitation of an insulin-stimulated receptor phosphatase activity from FRTL5 cells. Endocrinology 128: 2949-2957, 1991.
    • (1991) Endocrinology , vol.128 , pp. 2949-2957
    • Formisano, P.1    Condorelli, G.2    Condorelli, G.3    Beguinot, F.4
  • 34
    • 0035356565 scopus 로고    scopus 로고
    • Phosphoprotein isotope-coded affinity tag approach for isolating and quantitating phosphopeptides in proteome-wide analyses
    • Goshe MB, Conrads TP, Panisko EA, Angell NH, Veenstra TD, Smith RD. Phosphoprotein isotope-coded affinity tag approach for isolating and quantitating phosphopeptides in proteome-wide analyses. Anal Chem 73: 2578-2586, 2001.
    • (2001) Anal Chem , vol.73 , pp. 2578-2586
    • Goshe, M.B.1    Conrads, T.P.2    Panisko, E.A.3    Angell, N.H.4    Veenstra, T.D.5    Smith, R.D.6
  • 35
    • 0036652968 scopus 로고    scopus 로고
    • A mass spectrometry-based proteomic approach for identification of serine/threonine-phosphorylated proteins by enrichment with phospho-specific antibodies: Identification of a novel protein, Frigg, as a protein kinase A substrate
    • Gronborg M, Kristiansen TZ, Stensballe A, Andersen JS, Ohara O, Mann M, Jensen ON, Pandey A. A mass spectrometry-based proteomic approach for identification of serine/threonine-phosphorylated proteins by enrichment with phospho-specific antibodies: identification of a novel protein, Frigg, as a protein kinase A substrate. Mol Cell Proteomics 1: 517-527, 2002.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 517-527
    • Gronborg, M.1    Kristiansen, T.Z.2    Stensballe, A.3    Andersen, J.S.4    Ohara, O.5    Mann, M.6    Jensen, O.N.7    Pandey, A.8
  • 36
    • 29244443641 scopus 로고    scopus 로고
    • Efficient analysis and extraction of MS/MS result data from Mascot result files
    • Grosse-Coosmann F, Boehm AM, Sickmann A. Efficient analysis and extraction of MS/MS result data from Mascot result files. BMC Bioinformatics 6: 290, 2005.
    • (2005) BMC Bioinformatics , vol.6 , pp. 290
    • Grosse-Coosmann, F.1    Boehm, A.M.2    Sickmann, A.3
  • 38
    • 33744901953 scopus 로고    scopus 로고
    • Phosphopeptide anion characterization via sequential charge inversion and electron-transfer dissociation
    • Gunawardena HP, Emory JF, McLuckey SA. Phosphopeptide anion characterization via sequential charge inversion and electron-transfer dissociation. Anal Chem 78: 3788-3793, 2006.
    • (2006) Anal Chem , vol.78 , pp. 3788-3793
    • Gunawardena, H.P.1    Emory, J.F.2    McLuckey, S.A.3
  • 39
    • 0028232354 scopus 로고
    • Analysis of cellular phosphoproteins by two-dimensional gel electrophoresis: Applications for cell signaling in normal and cancer cells
    • Guy GR, Philip R, Tan YH. Analysis of cellular phosphoproteins by two-dimensional gel electrophoresis: applications for cell signaling in normal and cancer cells. Electrophoresis 15: 417-440, 1994.
    • (1994) Electrophoresis , vol.15 , pp. 417-440
    • Guy, G.R.1    Philip, R.2    Tan, Y.H.3
  • 40
    • 0035884155 scopus 로고    scopus 로고
    • Electron capture dissociation and infrared multiphoton dissociation MS/MS of an N-glycosylated tryptic peptic to yield complementary sequence information
    • Hakansson K, Cooper HJ, Emmett MR, Costello CE, Marshall AG, Nilsson CL. Electron capture dissociation and infrared multiphoton dissociation MS/MS of an N-glycosylated tryptic peptic to yield complementary sequence information. Anal Chem 73: 4530-4536, 2001.
    • (2001) Anal Chem , vol.73 , pp. 4530-4536
    • Hakansson, K.1    Cooper, H.J.2    Emmett, M.R.3    Costello, C.E.4    Marshall, A.G.5    Nilsson, C.L.6
  • 42
    • 0842299091 scopus 로고    scopus 로고
    • Identification of novel phosphorylation sites on Xenopus laevis Aurora A and analysis of phosphopeptide enrichment by immobilized metal-affinity chromatography
    • Haydon CE, Eyers PA, Aveline-Wolf LD, Resing KA, Maller JL, Ahn NG. Identification of novel phosphorylation sites on Xenopus laevis Aurora A and analysis of phosphopeptide enrichment by immobilized metal-affinity chromatography. Mol Cell Proteomics 2: 1055-1067, 2003.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 1055-1067
    • Haydon, C.E.1    Eyers, P.A.2    Aveline-Wolf, L.D.3    Resing, K.A.4    Maller, J.L.5    Ahn, N.G.6
  • 43
    • 19444367322 scopus 로고    scopus 로고
    • 18O labeling with an ion trap mass spectrometer and the analysis software application ZoomQuant. J Am Soc Mass Spectrom 16: 916-925, 2005.
    • 18O labeling with an ion trap mass spectrometer and the analysis software application "ZoomQuant." J Am Soc Mass Spectrom 16: 916-925, 2005.
  • 44
    • 0027286502 scopus 로고
    • MASCOT: Multiple alignment system for protein sequences based on three-way dynamic programming
    • Hirosawa M, Hoshida M, Ishikawa M, Toya T. MASCOT: multiple alignment system for protein sequences based on three-way dynamic programming. Comput Appl Biosci 9: 161-167, 1993.
    • (1993) Comput Appl Biosci , vol.9 , pp. 161-167
    • Hirosawa, M.1    Hoshida, M.2    Ishikawa, M.3    Toya, T.4
  • 46
    • 33646485094 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics of vasopressin-sensitive renal cells: Regulation of aquaporin-2 phosphorylation at two sites
    • Hoffert JD, Pisitkun T, Wang G, Shen RF, Knepper MA. Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites. Proc Natl Acad Sci USA 103: 7159-7164, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7159-7164
    • Hoffert, J.D.1    Pisitkun, T.2    Wang, G.3    Shen, R.F.4    Knepper, M.A.5
  • 47
    • 0035234035 scopus 로고    scopus 로고
    • Immunoprecipitation and western blotting of phosphotyrosine-containing proteins
    • Ignatoski KM. Immunoprecipitation and western blotting of phosphotyrosine-containing proteins. Methods Mol Biol 124: 39-48, 2001.
    • (2001) Methods Mol Biol , vol.124 , pp. 39-48
    • Ignatoski, K.M.1
  • 48
    • 0023877295 scopus 로고
    • Detection of phosphorylated forms of Moloney murine leukemia virus major capsid protein p30 by immunoprecipitation and two-dimensional gel electrophoresis
    • Ikuta K, Luftig RB. Detection of phosphorylated forms of Moloney murine leukemia virus major capsid protein p30 by immunoprecipitation and two-dimensional gel electrophoresis. J Virol 62: 40-46, 1988.
    • (1988) J Virol , vol.62 , pp. 40-46
    • Ikuta, K.1    Luftig, R.B.2
  • 49
    • 29244432748 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis maps of the proteome and phosphoproteome of primitively cultured rat mesangial cells
    • Jiang XS, Tang LY, Cao XJ, Zhou H, Xia QC, Wu JR, Zeng R. Two-dimensional gel electrophoresis maps of the proteome and phosphoproteome of primitively cultured rat mesangial cells. Electrophoresis 26: 4540-4562, 2005.
    • (2005) Electrophoresis , vol.26 , pp. 4540-4562
    • Jiang, X.S.1    Tang, L.Y.2    Cao, X.J.3    Zhou, H.4    Xia, Q.C.5    Wu, J.R.6    Zeng, R.7
  • 50
    • 29244482282 scopus 로고    scopus 로고
    • Quantitative analysis of protein phosphorylation in mouse brain by hypothesis-driven multistage mass spectrometry
    • Jin M, Bateup H, Padovan JC, Greengard P, Nairn AC, Chait BT. Quantitative analysis of protein phosphorylation in mouse brain by hypothesis-driven multistage mass spectrometry. Anal Chem 77: 7845-7851, 2005.
    • (2005) Anal Chem , vol.77 , pp. 7845-7851
    • Jin, M.1    Bateup, H.2    Padovan, J.C.3    Greengard, P.4    Nairn, A.C.5    Chait, B.T.6
  • 51
    • 0032759676 scopus 로고    scopus 로고
    • Capillary electrophoresis/tandem mass spectrometry for analysis of proteins from two-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis
    • Jin X, Chen Y, Lubman DM, Misek D, Hanash SM. Capillary electrophoresis/tandem mass spectrometry for analysis of proteins from two-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis. Rapid Commun Mass Spectrom 13: 2327-2334, 1999.
    • (1999) Rapid Commun Mass Spectrom , vol.13 , pp. 2327-2334
    • Jin, X.1    Chen, Y.2    Lubman, D.M.3    Misek, D.4    Hanash, S.M.5
  • 52
    • 4444367197 scopus 로고    scopus 로고
    • Phosphoproteomics finds its timing
    • Johnson SA, Hunter T. Phosphoproteomics finds its timing. Nat Biotechnol 22: 1093-1094, 2004.
    • (2004) Nat Biotechnol , vol.22 , pp. 1093-1094
    • Johnson, S.A.1    Hunter, T.2
  • 54
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons
    • Karas M, Hillenkamp F. Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Anal Chem 60: 2299-2301, 1988.
    • (1988) Anal Chem , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 56
    • 33750619876 scopus 로고    scopus 로고
    • Posttranslational protein modifications: Current implications for cancer detection, prevention, and therapeutics
    • Krueger KE, Srivastava S. Posttranslational protein modifications: current implications for cancer detection, prevention, and therapeutics. Mol Cell Proteomics 5: 1799-1810, 2006.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 1799-1810
    • Krueger, K.E.1    Srivastava, S.2
  • 57
    • 5644259649 scopus 로고    scopus 로고
    • Phosphopeptide-selective column-switching RP-HPLC with a titania precolumn
    • Kuroda I, Shintani Y, Motokawa M, Abe S, Furuno M. Phosphopeptide-selective column-switching RP-HPLC with a titania precolumn. Anal Sci 20: 1313-1319, 2004.
    • (2004) Anal Sci , vol.20 , pp. 1313-1319
    • Kuroda, I.1    Shintani, Y.2    Motokawa, M.3    Abe, S.4    Furuno, M.5
  • 58
    • 33645217942 scopus 로고    scopus 로고
    • Selective zirconium dioxide-based enrichment of phosphorylated peptides for mass spectrometric analysis
    • Kweon HK, Hakansson K. Selective zirconium dioxide-based enrichment of phosphorylated peptides for mass spectrometric analysis. Anal Chem 78: 1743-1749, 2006.
    • (2006) Anal Chem , vol.78 , pp. 1743-1749
    • Kweon, H.K.1    Hakansson, K.2
  • 59
    • 33746570234 scopus 로고    scopus 로고
    • Analysis of posttranslational modifications of proteins by tandem mass spectrometry
    • Larsen MR, Trelle MB, Thingholm TE, Jensen ON. Analysis of posttranslational modifications of proteins by tandem mass spectrometry. Biotechniques 40: 790-798, 2006.
    • (2006) Biotechniques , vol.40 , pp. 790-798
    • Larsen, M.R.1    Trelle, M.B.2    Thingholm, T.E.3    Jensen, O.N.4
  • 60
    • 0038636984 scopus 로고    scopus 로고
    • Electron capture dissociation initiates a free radical reaction cascade
    • Leymarie N, Costello CE, O'Connor PB. Electron capture dissociation initiates a free radical reaction cascade. J Am Chem Soc 125: 8949-8958, 2003.
    • (2003) J Am Chem Soc , vol.125 , pp. 8949-8958
    • Leymarie, N.1    Costello, C.E.2    O'Connor, P.B.3
  • 61
    • 34548228858 scopus 로고    scopus 로고
    • CILAT - a new reagent for quantitative proteomics
    • Li S, Zeng D. CILAT - a new reagent for quantitative proteomics. Chem Commun (Camb) 2181-2183, 2007.
    • (2007) Chem Commun (Camb) , vol.2181-2183
    • Li, S.1    Zeng, D.2
  • 62
    • 26244434578 scopus 로고    scopus 로고
    • Evaluation of several two-dimensional gel electrophoresis techniques in cardiac proteomics
    • Li ZB, Flint PW, Boluyt MO. Evaluation of several two-dimensional gel electrophoresis techniques in cardiac proteomics. Electrophoresis 26: 3572-3585, 2005.
    • (2005) Electrophoresis , vol.26 , pp. 3572-3585
    • Li, Z.B.1    Flint, P.W.2    Boluyt, M.O.3
  • 63
    • 13844255828 scopus 로고    scopus 로고
    • Quantitative proteomics
    • Linscheid MW. Quantitative proteomics. Anal Bioanal Chem 381: 64-66, 2005.
    • (2005) Anal Bioanal Chem , vol.381 , pp. 64-66
    • Linscheid, M.W.1
  • 64
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • Liu H, Sadygov RG, Yates JR 3rd. A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal Chem 76: 4193-4201, 2004.
    • (2004) Anal Chem , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates 3rd, J.R.3
  • 65
    • 0036828724 scopus 로고    scopus 로고
    • Probability-based validation of protein identifications using a modified SEQUEST algorithm
    • MacCoss MJ, Wu CC, Yates JR 3rd. Probability-based validation of protein identifications using a modified SEQUEST algorithm. Anal Chem 74: 5593-5599, 2002.
    • (2002) Anal Chem , vol.74 , pp. 5593-5599
    • MacCoss, M.J.1    Wu, C.C.2    Yates 3rd, J.R.3
  • 66
    • 33646899550 scopus 로고    scopus 로고
    • Top-down protein sequencing and MS3 on a hybrid linear quadrupole ion trap-orbitrap mass spectrometer
    • Macek B, Waanders LF, Olsen JV, Mann M. Top-down protein sequencing and MS3 on a hybrid linear quadrupole ion trap-orbitrap mass spectrometer. Mol Cell Proteomics 5: 949-958, 2006.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 949-958
    • Macek, B.1    Waanders, L.F.2    Olsen, J.V.3    Mann, M.4
  • 67
  • 68
    • 0032846162 scopus 로고    scopus 로고
    • Quantitative proteomics?
    • Mann M. Quantitative proteomics? Nat Biotechnol 17: 954-955, 1999.
    • (1999) Nat Biotechnol , vol.17 , pp. 954-955
    • Mann, M.1
  • 69
    • 0033930599 scopus 로고    scopus 로고
    • Identification of proteins from one-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis using electrospray quadrupole-time-of-flight tandem mass spectrometry
    • Marvin L, Millar A, Saulot V, Machour N, Charlionet R, Tron F, Lange C. Identification of proteins from one-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis using electrospray quadrupole-time-of-flight tandem mass spectrometry. Rapid Commun Mass Spectrom 14: 1287-1292, 2000.
    • (2000) Rapid Commun Mass Spectrom , vol.14 , pp. 1287-1292
    • Marvin, L.1    Millar, A.2    Saulot, V.3    Machour, N.4    Charlionet, R.5    Tron, F.6    Lange, C.7
  • 70
    • 41349111699 scopus 로고    scopus 로고
    • Biomarker discovery: Proteome fractionation and separation in biological samples
    • December 27, doi:10.1152/physiolgenomics.00282
    • Matt P, Fu Z, Fu Q, Van Eyk J. Biomarker discovery: proteome fractionation and separation in biological samples. Physiol Genomics December 27, 2007; doi:10.1152/physiolgenomics.00282.2007.
    • (2007) Physiol Genomics
    • Matt, P.1    Fu, Z.2    Fu, Q.3    Van Eyk, J.4
  • 71
    • 34249022000 scopus 로고    scopus 로고
    • Implementation of electron-transfer dissociation on a hybrid linear ion trap-orbitrap mass spectrometer
    • McAlister GC, Phanstiel D, Good DM, Berggren WT, Coon JJ. Implementation of electron-transfer dissociation on a hybrid linear ion trap-orbitrap mass spectrometer. Anal Chem 79: 3525-3534, 2007.
    • (2007) Anal Chem , vol.79 , pp. 3525-3534
    • McAlister, G.C.1    Phanstiel, D.2    Good, D.M.3    Berggren, W.T.4    Coon, J.J.5
  • 72
    • 34548391374 scopus 로고    scopus 로고
    • Quantification of the synaptosomal proteome of the rat cerebellum during post-natal development
    • McClatchy DB, Liao L, Park SK, Venable JD, Yates JR. Quantification of the synaptosomal proteome of the rat cerebellum during post-natal development. Genome Res 17: 1378-1388, 2007.
    • (2007) Genome Res , vol.17 , pp. 1378-1388
    • McClatchy, D.B.1    Liao, L.2    Park, S.K.3    Venable, J.D.4    Yates, J.R.5
  • 73
    • 0034795584 scopus 로고    scopus 로고
    • Proteomics: Posttranslational modifications, immune responses and current analytical tools
    • Meri S, Baumann M. Proteomics: posttranslational modifications, immune responses and current analytical tools. Biomol Eng 18: 213-220, 2001.
    • (2001) Biomol Eng , vol.18 , pp. 213-220
    • Meri, S.1    Baumann, M.2
  • 74
    • 0023046921 scopus 로고
    • Sequence analysis of phosphoserine-containing peptides. Modification for picomolar sensitivity
    • Meyer HE, Hoffmann-Posorske E, Korte H, Heilmeyer LM Jr. Sequence analysis of phosphoserine-containing peptides. Modification for picomolar sensitivity. FEBS Lett 204: 61-66, 1986.
    • (1986) FEBS Lett , vol.204 , pp. 61-66
    • Meyer, H.E.1    Hoffmann-Posorske, E.2    Korte, H.3    Heilmeyer Jr., L.M.4
  • 75
    • 33846105280 scopus 로고    scopus 로고
    • 18O-labeling strategies for quantitative proteomics
    • 18O-labeling strategies for quantitative proteomics. Mass Spectrom Rev 26: 121-136, 2007.
    • (2007) Mass Spectrom Rev , vol.26 , pp. 121-136
    • Miyagi, M.1    Rao, K.C.2
  • 76
    • 33847782587 scopus 로고    scopus 로고
    • Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry
    • Molina H, Horn DM, Tang N, Mathivanan S, Pandey A. Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci USA 104: 2199-2204, 2007.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2199-2204
    • Molina, H.1    Horn, D.M.2    Tang, N.3    Mathivanan, S.4    Pandey, A.5
  • 77
    • 0036112145 scopus 로고    scopus 로고
    • Fragmentation of phosphopeptides by atmospheric pressure MALDI and ESI/ion trap mass spectrometry
    • Moyer SC, Cotter RJ, Woods AS. Fragmentation of phosphopeptides by atmospheric pressure MALDI and ESI/ion trap mass spectrometry. J Am Soc Mass Spectrom 13: 274-283, 2002.
    • (2002) J Am Soc Mass Spectrom , vol.13 , pp. 274-283
    • Moyer, S.C.1    Cotter, R.J.2    Woods, A.S.3
  • 78
    • 14644443603 scopus 로고    scopus 로고
    • In silico evaluation of two mass spectrometry-based approaches for the identification of novel human leukocyte cell-surface proteins
    • Nicholson IC, Ayhan M, Hoogenraad NJ, Zola H. In silico evaluation of two mass spectrometry-based approaches for the identification of novel human leukocyte cell-surface proteins. J Leukoc Biol 77: 190-198, 2005.
    • (2005) J Leukoc Biol , vol.77 , pp. 190-198
    • Nicholson, I.C.1    Ayhan, M.2    Hoogenraad, N.J.3    Zola, H.4
  • 79
    • 0034855587 scopus 로고    scopus 로고
    • Large-gel two-dimensional electrophoresis-matrix assisted laser desorption/ionization-time of flight-mass spectrometry: An analytical challenge for studying complex protein mixtures
    • Nordhoff E, Egelhofer V, Giavalisco P, Eickhoff H, Horn M, Przewieslik T, Theiss D, Schneider U, Lehrach H, Gobom J. Large-gel two-dimensional electrophoresis-matrix assisted laser desorption/ionization-time of flight-mass spectrometry: an analytical challenge for studying complex protein mixtures. Electrophoresis 22: 2844-2855, 2001.
    • (2001) Electrophoresis , vol.22 , pp. 2844-2855
    • Nordhoff, E.1    Egelhofer, V.2    Giavalisco, P.3    Eickhoff, H.4    Horn, M.5    Przewieslik, T.6    Theiss, D.7    Schneider, U.8    Lehrach, H.9    Gobom, J.10
  • 80
    • 0035067251 scopus 로고    scopus 로고
    • Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome
    • Oda Y, Nagasu T, Chait BT. Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome. Nat Biotechnol 19: 379-382, 2001.
    • (2001) Nat Biotechnol , vol.19 , pp. 379-382
    • Oda, Y.1    Nagasu, T.2    Chait, B.T.3
  • 82
    • 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 SE, Blagoev B, Kratchmarova I, Kristensen DB, Steen H, Pandey A, Mann M. 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.
    • (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
  • 83
    • 0037326081 scopus 로고    scopus 로고
    • Mass spectrometric-based approaches in quantitative proteomics
    • Ong SE, Foster LJ, Mann M. Mass spectrometric-based approaches in quantitative proteomics. Methods 29: 124-130, 2003.
    • (2003) Methods , vol.29 , pp. 124-130
    • Ong, S.E.1    Foster, L.J.2    Mann, M.3
  • 85
    • 0034602654 scopus 로고    scopus 로고
    • Analysis of receptor signaling pathways by mass spectrometry: Identification of vav-2 as a substrate of the epidermal and platelet-derived growth factor receptors
    • Pandey A, Podtelejnikov AV, Blagoev B, Bustelo XR, Mann M, Lodish HF. Analysis of receptor signaling pathways by mass spectrometry: identification of vav-2 as a substrate of the epidermal and platelet-derived growth factor receptors. Proc Natl Acad Sci USA 97: 179-184, 2000.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 179-184
    • Pandey, A.1    Podtelejnikov, A.V.2    Blagoev, B.3    Bustelo, X.R.4    Mann, M.5    Lodish, H.F.6
  • 87
    • 23144463202 scopus 로고    scopus 로고
    • Separation techniques hyphenated to electrospray-tandem mass spectrometry in proteomics: Capillary electrophoresis versus nanoliquid chromatography
    • Pelzing M, Neususs C. Separation techniques hyphenated to electrospray-tandem mass spectrometry in proteomics: capillary electrophoresis versus nanoliquid chromatography. Electrophoresis 26: 2717-2728, 2005.
    • (2005) Electrophoresis , vol.26 , pp. 2717-2728
    • Pelzing, M.1    Neususs, C.2
  • 88
    • 0016717761 scopus 로고
    • Metal chelate affinity chromatography, a new approach to protein fractionation
    • Porath J, Carlsson J, Olsson I, Belfrage G. Metal chelate affinity chromatography, a new approach to protein fractionation. Nature 258: 598-599, 1975.
    • (1975) Nature , vol.258 , pp. 598-599
    • Porath, J.1    Carlsson, J.2    Olsson, I.3    Belfrage, G.4
  • 89
    • 0033565503 scopus 로고    scopus 로고
    • Immobilized gallium(III) affinity chromatography of phosphopeptides
    • Posewitz MC, Tempst P. Immobilized gallium(III) affinity chromatography of phosphopeptides. Anal Chem 71: 2883-2892, 1999.
    • (1999) Anal Chem , vol.71 , pp. 2883-2892
    • Posewitz, M.C.1    Tempst, P.2
  • 90
    • 0142040631 scopus 로고    scopus 로고
    • Phosphoprotein isotope-coded solid-phase tag approach for enrichment and quantitative analysis of phosphopeptides from complex mixtures
    • Qian WJ, Goshe MB, Camp DG 2nd, Yu LR, Tang K, Smith RD. Phosphoprotein isotope-coded solid-phase tag approach for enrichment and quantitative analysis of phosphopeptides from complex mixtures. Anal Chem 75: 5441-5450, 2003.
    • (2003) Anal Chem , vol.75 , pp. 5441-5450
    • Qian, W.J.1    Goshe, M.B.2    Camp 2nd, D.G.3    Yu, L.R.4    Tang, K.5    Smith, R.D.6
  • 92
    • 27744563093 scopus 로고    scopus 로고
    • State-of-the-art in phosphoproteomics
    • Reinders J, Sickmann A. State-of-the-art in phosphoproteomics. Proteomics 5: 4052-4061, 2005.
    • (2005) Proteomics , vol.5 , pp. 4052-4061
    • Reinders, J.1    Sickmann, A.2
  • 93
    • 0029156626 scopus 로고
    • Mass spectrometric analysis of 21 phosphorylation sites in the internal repeat of rat profilaggrin, precursor of an intermediate filament associated protein
    • Resing KA, Johnson RS, Walsh KA. Mass spectrometric analysis of 21 phosphorylation sites in the internal repeat of rat profilaggrin, precursor of an intermediate filament associated protein. Biochemistry 34: 9477-9487, 1995.
    • (1995) Biochemistry , vol.34 , pp. 9477-9487
    • Resing, K.A.1    Johnson, R.S.2    Walsh, K.A.3
  • 94
    • 36148954308 scopus 로고    scopus 로고
    • High-throughput cellular assays for regulated posttranslational modifications
    • Robers MB, Horton RA, Bercher MR, Vogel KW, Machleidt T. High-throughput cellular assays for regulated posttranslational modifications. Anal Biochem 372: 189-197, 2008.
    • (2008) Anal Biochem , vol.372 , pp. 189-197
    • Robers, M.B.1    Horton, R.A.2    Bercher, M.R.3    Vogel, K.W.4    Machleidt, T.5
  • 96
    • 27844600289 scopus 로고    scopus 로고
    • Phosphoproteomics by mass spectrometry and classical protein chemistry approaches
    • Salih E. Phosphoproteomics by mass spectrometry and classical protein chemistry approaches. Mass Spectrom Rev 24: 828-846, 2005.
    • (2005) Mass Spectrom Rev , vol.24 , pp. 828-846
    • Salih, E.1
  • 97
    • 3042575877 scopus 로고    scopus 로고
    • Titania as a chemo-affinity support for the column-switching HPLC analysis of phosphopeptides: Application to the characterization of phosphorylation sites in proteins by combination with protease digestion and electrospray ionization mass spectrometry
    • Sano A, Nakamura H. Titania as a chemo-affinity support for the column-switching HPLC analysis of phosphopeptides: application to the characterization of phosphorylation sites in proteins by combination with protease digestion and electrospray ionization mass spectrometry. Anal Sci 20: 861-864, 2004.
    • (2004) Anal Sci , vol.20 , pp. 861-864
    • Sano, A.1    Nakamura, H.2
  • 98
    • 0037087029 scopus 로고    scopus 로고
    • Liquid chromatography-mass spectrometry and capillary electrophoresis combined approach for separation and characterization of multicomponent peptide mixtures. Application to crude products of leuprolide synthesis
    • Sanz-Nebot V, Benavente F, Barbosa J. Liquid chromatography-mass spectrometry and capillary electrophoresis combined approach for separation and characterization of multicomponent peptide mixtures. Application to crude products of leuprolide synthesis. J Chromatogr A 950: 99-111, 2002.
    • (2002) J Chromatogr A , vol.950 , pp. 99-111
    • Sanz-Nebot, V.1    Benavente, F.2    Barbosa, J.3
  • 99
    • 33646252021 scopus 로고    scopus 로고
    • Sarioglu H, Brandner S, Jacobsen C, Meindl T, Schmidt A, Kellermann J, Lottspeich F, Andrae U. Quantitative analysis of 2,3,7,8- tetrachlorodibenzo-p-dioxin-induced proteome alterations in 5L rat hepatoma cells using isotope-coded protein labels. Proteomics 6: 2407-2421, 2006.
    • Sarioglu H, Brandner S, Jacobsen C, Meindl T, Schmidt A, Kellermann J, Lottspeich F, Andrae U. Quantitative analysis of 2,3,7,8- tetrachlorodibenzo-p-dioxin-induced proteome alterations in 5L rat hepatoma cells using isotope-coded protein labels. Proteomics 6: 2407-2421, 2006.
  • 100
    • 13244260803 scopus 로고    scopus 로고
    • A novel strategy for quantitative proteomics using isotope-coded protein labels
    • Schmidt A, Kellermann J, Lottspeich F. A novel strategy for quantitative proteomics using isotope-coded protein labels. Proteomics 5: 4-15, 2005.
    • (2005) Proteomics , vol.5 , pp. 4-15
    • Schmidt, A.1    Kellermann, J.2    Lottspeich, F.3
  • 101
    • 0037304325 scopus 로고    scopus 로고
    • Quantitative proteomics using mass spectrometry
    • Sechi S, Oda Y. Quantitative proteomics using mass spectrometry. Curr Opin Chem Biol 7: 70-77, 2003.
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 70-77
    • Sechi, S.1    Oda, Y.2
  • 102
    • 2642576571 scopus 로고    scopus 로고
    • Isotope-coded affinity tag approach to identify and quantify oxidant-sensitive protein thiols
    • Sethuraman M, McComb ME, Heibeck T, Costello CE, Cohen RA. Isotope-coded affinity tag approach to identify and quantify oxidant-sensitive protein thiols. Mol Cell Proteomics 3: 273-278, 2004.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 273-278
    • Sethuraman, M.1    McComb, M.E.2    Heibeck, T.3    Costello, C.E.4    Cohen, R.A.5
  • 105
    • 0035477025 scopus 로고    scopus 로고
    • Optimization of the isotope-coded affinity tag-labeling procedure for quantitative proteome analysis
    • Smolka MB, Zhou H, Purkayastha S, Aebersold R. Optimization of the isotope-coded affinity tag-labeling procedure for quantitative proteome analysis. Anal Biochem 297: 25-31, 2001.
    • (2001) Anal Biochem , vol.297 , pp. 25-31
    • Smolka, M.B.1    Zhou, H.2    Purkayastha, S.3    Aebersold, R.4
  • 107
    • 0029806666 scopus 로고    scopus 로고
    • Ion/ion proton transfer reactions for protein mixture analysis
    • Stephenson JL Jr, McLuckey SA. Ion/ion proton transfer reactions for protein mixture analysis. Anal Chem 68: 4026-4032, 1996.
    • (1996) Anal Chem , vol.68 , pp. 4026-4032
    • Stephenson Jr, J.L.1    McLuckey, S.A.2
  • 111
    • 34247147568 scopus 로고    scopus 로고
    • Electron capture dissociation in the analysis of protein phosphorylation
    • Sweet SM, Cooper HJ. Electron capture dissociation in the analysis of protein phosphorylation. Expert Rev Proteomics 4: 149-159, 2007.
    • (2007) Expert Rev Proteomics , vol.4 , pp. 149-159
    • Sweet, S.M.1    Cooper, H.J.2
  • 112
    • 3042789073 scopus 로고    scopus 로고
    • Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
    • Syka JE, Coon JJ, Schroeder MJ, Shabanowitz J, Hunt DF. Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc Natl Acad Sci USA 101: 9528-9533, 2004.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9528-9533
    • Syka, J.E.1    Coon, J.J.2    Schroeder, M.J.3    Shabanowitz, J.4    Hunt, D.F.5
  • 115
    • 0042922612 scopus 로고    scopus 로고
    • Proteome analysis of posttranslational modifications
    • Veenstra TD. Proteome analysis of posttranslational modifications. Adv Protein Chem 65: 161-194, 2003.
    • (2003) Adv Protein Chem , vol.65 , pp. 161-194
    • Veenstra, T.D.1
  • 116
    • 33746432742 scopus 로고    scopus 로고
    • The application of new software tools to quantitative protein profiling via isotope-coded affinity tag (ICAT) and tandem mass spectrometry. I. Statistically annotated datasets for peptide sequences and proteins identified via the application of ICAT and tandem mass spectrometry to proteins copurifying with T cell lipid rafts
    • von Haller PD, Yi E, Donohoe S, Vaughn K, Keller A, Nesvizhskii AI, Eng J, Li XJ, Goodlett DR, Aebersold R, Watts JD. The application of new software tools to quantitative protein profiling via isotope-coded affinity tag (ICAT) and tandem mass spectrometry. I. Statistically annotated datasets for peptide sequences and proteins identified via the application of ICAT and tandem mass spectrometry to proteins copurifying with T cell lipid rafts. Mol Cell Proteomics 2: 426-427, 2003.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 426-427
    • von Haller, P.D.1    Yi, E.2    Donohoe, S.3    Vaughn, K.4    Keller, A.5    Nesvizhskii, A.I.6    Eng, J.7    Li, X.J.8    Goodlett, D.R.9    Aebersold, R.10    Watts, J.D.11
  • 117
    • 33646564676 scopus 로고    scopus 로고
    • Label-free protein quantification using LC-coupled ion trap or FT mass spectrometry: Reproducibility, linearity, and application with complex proteomes
    • Wang G, Wu WW, Zeng W, Chou CL, Shen RF. Label-free protein quantification using LC-coupled ion trap or FT mass spectrometry: reproducibility, linearity, and application with complex proteomes. J Proteome Res 5: 1214-1223, 2006.
    • (2006) J Proteome Res , vol.5 , pp. 1214-1223
    • Wang, G.1    Wu, W.W.2    Zeng, W.3    Chou, C.L.4    Shen, R.F.5
  • 119
    • 30144438909 scopus 로고    scopus 로고
    • Collision-induced dissociation (CID) of peptides and proteins
    • Wells JM, McLuckey SA. Collision-induced dissociation (CID) of peptides and proteins. Methods Enzymol 402: 148-185, 2005.
    • (2005) Methods Enzymol , vol.402 , pp. 148-185
    • Wells, J.M.1    McLuckey, S.A.2
  • 120
    • 0030637275 scopus 로고    scopus 로고
    • Two-dimensional polyacrylamide gel electrophoresis of cancer-associated proteins
    • Wirth PJ, Luo LD, Hoang T, Benjamin T. Two-dimensional polyacrylamide gel electrophoresis of cancer-associated proteins. Recent Results Cancer Res 143: 145-160, 1997.
    • (1997) Recent Results Cancer Res , vol.143 , pp. 145-160
    • Wirth, P.J.1    Luo, L.D.2    Hoang, T.3    Benjamin, T.4
  • 121
    • 0018391857 scopus 로고
    • Two-dimensional gel electrophoresis of cytosol phosphoproteins of Novikoff hepatoma and regenerating liver
    • Wu BC, Spohn WH, Busch H. Two-dimensional gel electrophoresis of cytosol phosphoproteins of Novikoff hepatoma and regenerating liver. Cancer Res 39: 116-122, 1979.
    • (1979) Cancer Res , vol.39 , pp. 116-122
    • Wu, B.C.1    Spohn, W.H.2    Busch, H.3
  • 122
    • 38049035341 scopus 로고    scopus 로고
    • Global profiling of phosphopeptides by Titania affinity enrichment
    • Wu J, Shakey Q, Liu W, Schuller A, Follettie MT. Global profiling of phosphopeptides by Titania affinity enrichment. J Proteome Res 6: 4684-4689, 2007.
    • (2007) J Proteome Res , vol.6 , pp. 4684-4689
    • Wu, J.1    Shakey, Q.2    Liu, W.3    Schuller, A.4    Follettie, M.T.5
  • 123
    • 19444363756 scopus 로고    scopus 로고
    • Mass spectrometry-based quantitative proteomic profiling
    • Yan W, Chen SS. Mass spectrometry-based quantitative proteomic profiling. Brief Funct Genomic Proteomic 4: 27-38, 2005.
    • (2005) Brief Funct Genomic Proteomic , vol.4 , pp. 27-38
    • Yan, W.1    Chen, S.S.2
  • 124
    • 12244300698 scopus 로고    scopus 로고
    • A dataset of human liver proteins identified by protein profiling via isotope-coded affinity tag (ICAT) and tandem mass spectrometry
    • Yan W, Lee H, Deutsch EW, Lazaro CA, Tang W, Chen E, Fausto N, Katze MG, Aebersold R. A dataset of human liver proteins identified by protein profiling via isotope-coded affinity tag (ICAT) and tandem mass spectrometry. Mol Cell Proteomics 3: 1039-1041, 2004.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 1039-1041
    • Yan, W.1    Lee, H.2    Deutsch, E.W.3    Lazaro, C.A.4    Tang, W.5    Chen, E.6    Fausto, N.7    Katze, M.G.8    Aebersold, R.9
  • 126
    • 0028330012 scopus 로고
    • Matrix-assisted laser desorption mass spectrometric peptide mapping of proteins separated by two-dimensional gel electrophoresis: Determination of phosphorylation in synapsin I
    • Zhang W, Czernik AJ, Yungwirth T, Aebersold R, Chait BT. Matrix-assisted laser desorption mass spectrometric peptide mapping of proteins separated by two-dimensional gel electrophoresis: determination of phosphorylation in synapsin I. Protein Sci 3: 677-686, 1994.
    • (1994) Protein Sci , vol.3 , pp. 677-686
    • Zhang, W.1    Czernik, A.J.2    Yungwirth, T.3    Aebersold, R.4    Chait, B.T.5
  • 127
    • 26844576371 scopus 로고    scopus 로고
    • Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules
    • Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM. Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol Cell Proteomics 4: 1240-1250, 2005.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1240-1250
    • Zhang, Y.1    Wolf-Yadlin, A.2    Ross, P.L.3    Pappin, D.J.4    Rush, J.5    Lauffenburger, D.A.6    White, F.M.7
  • 128
    • 0035347440 scopus 로고    scopus 로고
    • Quantitative proteomics goes global
    • Ziegler Z. Quantitative proteomics goes global. Anal Chem 73: 251A, 2001.
    • (2001) Anal Chem , vol.73
    • Ziegler, Z.1
  • 129
    • 33646269941 scopus 로고    scopus 로고
    • A perspective on the use of iTRAQ reagent technology for protein complex and profiling studies
    • Zieske LR. A perspective on the use of iTRAQ reagent technology for protein complex and profiling studies. J Exp Bot 57: 1501-1508, 2006.
    • (2006) J Exp Bot , vol.57 , pp. 1501-1508
    • Zieske, L.R.1
  • 130
    • 0035815472 scopus 로고    scopus 로고
    • High-performance liquid chromatography coupled on-line with electrospray ionization mass spectrometry for the simultaneous separation and identification of the Synechocystis PCC 6803 phycobilisome proteins
    • Zolla L, Bianchetti M. High-performance liquid chromatography coupled on-line with electrospray ionization mass spectrometry for the simultaneous separation and identification of the Synechocystis PCC 6803 phycobilisome proteins. J Chromatogr A 912: 269-279, 2001.
    • (2001) J Chromatogr A , vol.912 , pp. 269-279
    • Zolla, L.1    Bianchetti, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.