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Volumn 14, Issue 6, 2015, Pages 2500-2510

Low-pH solid-phase amino labeling of complex peptide digests with TMTs improves peptide identification rates for multiplexed global phosphopeptide analysis

Author keywords

chemical labeling; isobaric tags; Mass spectrometry; phosphorylation; proteomics; TMT

Indexed keywords

AMINO ACID; HISTIDINE; PHOSPHOPEPTIDE; THREONINE; TYROSINE; AMINE;

EID: 84930583084     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/acs.jproteome.5b00072     Document Type: Article
Times cited : (31)

References (27)
  • 2
    • 0033565503 scopus 로고    scopus 로고
    • Immobilized gallium(III) affinity chromatography of phosphopeptides
    • Posewitz, M. C.; Tempst, P. Immobilized gallium(III) affinity chromatography of phosphopeptides Anal. Chem. 1999, 71, 2883-92
    • (1999) Anal. Chem. , vol.71 , pp. 2883-2892
    • Posewitz, M.C.1    Tempst, P.2
  • 3
    • 84875208164 scopus 로고    scopus 로고
    • Robust phosphoproteome enrichment using monodisperse microsphere-based immobilized titanium (IV) ion affinity chromatography
    • Zhou, H.; Ye, M.; Dong, J.; Corradini, E.; Cristobal, A.; Heck, A. J.; Zou, H.; Mohammed, S. Robust phosphoproteome enrichment using monodisperse microsphere-based immobilized titanium (IV) ion affinity chromatography Nat. Protoc. 2013, 8, 461-80
    • (2013) Nat. Protoc. , vol.8 , pp. 461-480
    • Zhou, H.1    Ye, M.2    Dong, J.3    Corradini, E.4    Cristobal, A.5    Heck, A.J.6    Zou, H.7    Mohammed, S.8
  • 4
    • 3242688830 scopus 로고    scopus 로고
    • Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns
    • Pinkse, M. W.; Uitto, P. M.; Hilhorst, M. J.; Ooms, B.; Heck, A. J. Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns Anal. Chem. 2004, 76, 3935-43
    • (2004) Anal. Chem. , vol.76 , pp. 3935-3943
    • Pinkse, M.W.1    Uitto, P.M.2    Hilhorst, M.J.3    Ooms, B.4    Heck, A.J.5
  • 5
    • 84984933087 scopus 로고    scopus 로고
    • The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry
    • Villén, J.; Gygi, S. P. The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry Nat. Protoc. 2008, 3, 1630-8
    • (2008) Nat. Protoc. , vol.3 , pp. 1630-1638
    • Villén, J.1    Gygi, S.P.2
  • 6
    • 12444345515 scopus 로고    scopus 로고
    • Tandem mass tags: A novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS
    • Thompson, A.; Schafer, J.; Kuhn, K.; Kienle, S.; Schwarz, J.; Schmidt, G.; Neumann, T.; Hamon, C. Tandem mass tags: a novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS Anal. Chem. 2003, 75, 1895-904
    • (2003) Anal. Chem. , vol.75 , pp. 1895-1904
    • Thompson, A.1    Schafer, J.2    Kuhn, K.3    Kienle, S.4    Schwarz, J.5    Schmidt, G.6    Neumann, T.7    Hamon, C.8
  • 9
    • 84922216168 scopus 로고    scopus 로고
    • Evaluating multiplexed quantitative phosphopeptide analysis on a hybrid quadrupole mass filter/linear ion trap/orbitrap mass spectrometer
    • Erickson, B. K.; Jedrychowski, M. P.; McAlister, G. C.; Everley, R. A.; Kunz, R.; Gygi, S. P. Evaluating multiplexed quantitative phosphopeptide analysis on a hybrid quadrupole mass filter/linear ion trap/orbitrap mass spectrometer Anal. Chem. 2015, 87, 1241-9
    • (2015) Anal. Chem. , vol.87 , pp. 1241-1249
    • Erickson, B.K.1    Jedrychowski, M.P.2    McAlister, G.C.3    Everley, R.A.4    Kunz, R.5    Gygi, S.P.6
  • 11
    • 32544447058 scopus 로고    scopus 로고
    • Accelerated on-column lysine derivatization and cysteine methylation by imidazole reaction in a deuterated environment for enhanced product ion analysis
    • Cindric, M.; Cepo, T.; Skrlin, A.; Vuletic, M.; Bindila, L. Accelerated on-column lysine derivatization and cysteine methylation by imidazole reaction in a deuterated environment for enhanced product ion analysis Rapid Commun. Mass Spectrom. 2006, 20, 694-702
    • (2006) Rapid Commun. Mass Spectrom. , vol.20 , pp. 694-702
    • Cindric, M.1    Cepo, T.2    Skrlin, A.3    Vuletic, M.4    Bindila, L.5
  • 12
    • 33645734804 scopus 로고    scopus 로고
    • Sulfonation chemistry as a powerful tool for MALDI TOF/TOF de novo sequencing and post-translational modification analysis
    • Conrotto, P.; Hellman, U. Sulfonation chemistry as a powerful tool for MALDI TOF/TOF de novo sequencing and post-translational modification analysis J. Biomol. Tech. 2005, 16, 441-52
    • (2005) J. Biomol. Tech. , vol.16 , pp. 441-452
    • Conrotto, P.1    Hellman, U.2
  • 13
    • 64749108158 scopus 로고    scopus 로고
    • Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics
    • Boersema, P. J.; Raijmakers, R.; Lemeer, S.; Mohammed, S.; Heck, A. J. Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics Nat. Protoc. 2009, 4, 484-94
    • (2009) Nat. Protoc. , vol.4 , pp. 484-494
    • Boersema, P.J.1    Raijmakers, R.2    Lemeer, S.3    Mohammed, S.4    Heck, A.J.5
  • 14
    • 84865773882 scopus 로고    scopus 로고
    • Phosphopeptide characterization by mass spectrometry using reversed-phase supports for solid-phase beta-elimination/Michael addition
    • Nika, H.; Lee, J.; Willis, I. M.; Angeletti, R. H.; Hawke, D. H. Phosphopeptide characterization by mass spectrometry using reversed-phase supports for solid-phase beta-elimination/Michael addition J. Biomol. Tech. 2012, 23, 51-68
    • (2012) J. Biomol. Tech. , vol.23 , pp. 51-68
    • Nika, H.1    Lee, J.2    Willis, I.M.3    Angeletti, R.H.4    Hawke, D.H.5
  • 15
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N.; Pappin, D. J.; Creasy, D. M.; Cottrell, J. S. Probability-based protein identification by searching sequence databases using mass spectrometry data Electrophoresis 1999, 20, 3551-67
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 16
    • 0029644596 scopus 로고
    • Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database
    • Yates, J. R.; Eng, J. K.; McCormack, A. L.; Schieltz, D. Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database Anal. Chem. 1995, 67, 1426-36
    • (1995) Anal. Chem. , vol.67 , pp. 1426-1436
    • Yates, J.R.1    Eng, J.K.2    McCormack, A.L.3    Schieltz, D.4
  • 17
    • 35748972060 scopus 로고    scopus 로고
    • Semi-supervised learning for peptide identification from shotgun proteomics datasets
    • Kall, L.; Canterbury, J. D.; Weston, J.; Noble, W. S.; MacCoss, M. J. Semi-supervised learning for peptide identification from shotgun proteomics datasets Nat. Methods 2007, 4, 923-5
    • (2007) Nat. Methods , vol.4 , pp. 923-925
    • Kall, L.1    Canterbury, J.D.2    Weston, J.3    Noble, W.S.4    Maccoss, M.J.5
  • 19
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias, J. E.; Gygi, S. P. Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry Nat. Methods 2007, 4, 207-14
    • (2007) Nat. Methods , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 20
    • 77953595441 scopus 로고    scopus 로고
    • Undesirable charge-enhancement of isobaric tagged phosphopeptides leads to reduced identification efficiency
    • Thingholm, T. E.; Palmisano, G.; Kjeldsen, F.; Larsen, M. R. Undesirable charge-enhancement of isobaric tagged phosphopeptides leads to reduced identification efficiency J. Proteome Res. 2010, 9, 4045-52
    • (2010) J. Proteome Res. , vol.9 , pp. 4045-4052
    • Thingholm, T.E.1    Palmisano, G.2    Kjeldsen, F.3    Larsen, M.R.4
  • 21
    • 77955159809 scopus 로고    scopus 로고
    • Peptide labeling with isobaric tags yields higher identification rates using iTRAQ 4-plex compared to TMT 6-plex and iTRAQ 8-plex on LTQ Orbitrap
    • Pichler, P.; Kocher, T.; Holzmann, J.; Mazanek, M.; Taus, T.; Ammerer, G.; Mechtler, K. Peptide labeling with isobaric tags yields higher identification rates using iTRAQ 4-plex compared to TMT 6-plex and iTRAQ 8-plex on LTQ Orbitrap Anal. Chem. 2010, 82, 6549-58
    • (2010) Anal. Chem. , vol.82 , pp. 6549-6558
    • Pichler, P.1    Kocher, T.2    Holzmann, J.3    Mazanek, M.4    Taus, T.5    Ammerer, G.6    Mechtler, K.7
  • 23
    • 84857995363 scopus 로고    scopus 로고
    • Identification of consistent alkylation of cysteine-less peptides in a proteomics experiment
    • Woods, A. G.; Sokolowska, I.; Darie, C. C. Identification of consistent alkylation of cysteine-less peptides in a proteomics experiment Biochem. Biophys. Res. Commun. 2012, 419, 305-8
    • (2012) Biochem. Biophys. Res. Commun. , vol.419 , pp. 305-308
    • Woods, A.G.1    Sokolowska, I.2    Darie, C.C.3
  • 24
    • 84874967213 scopus 로고    scopus 로고
    • Protein carbamylation: In vivo modification or in vitro artefact?
    • Kollipara, L.; Zahedi, R. P. Protein carbamylation: in vivo modification or in vitro artefact? Proteomics 2013, 13, 941-4
    • (2013) Proteomics , vol.13 , pp. 941-944
    • Kollipara, L.1    Zahedi, R.P.2
  • 25
    • 80155124832 scopus 로고    scopus 로고
    • MS3 eliminates ratio distortion in isobaric multiplexed quantitative proteomics
    • Ting, L.; Rad, R.; Gygi, S. P.; Haas, W. MS3 eliminates ratio distortion in isobaric multiplexed quantitative proteomics Nat. Methods 2011, 8, 937-40
    • (2011) Nat. Methods , vol.8 , pp. 937-940
    • Ting, L.1    Rad, R.2    Gygi, S.P.3    Haas, W.4
  • 26
    • 84895538371 scopus 로고    scopus 로고
    • Minimal, encapsulated proteomic-sample processing applied to copy-number estimation in eukaryotic cells
    • Kulak, N. A.; Pichler, G.; Paron, I.; Nagaraj, N.; Mann, M. Minimal, encapsulated proteomic-sample processing applied to copy-number estimation in eukaryotic cells Nat. Methods 2014, 11, 319-24
    • (2014) Nat. Methods , vol.11 , pp. 319-324
    • Kulak, N.A.1    Pichler, G.2    Paron, I.3    Nagaraj, N.4    Mann, M.5
  • 27
    • 71549117585 scopus 로고    scopus 로고
    • Combination of FASP and StageTip-based fractionation allows in-depth analysis of the hippocampal membrane proteome
    • Wisniewski, J. R.; Zougman, A.; Mann, M. Combination of FASP and StageTip-based fractionation allows in-depth analysis of the hippocampal membrane proteome J. Proteome Res. 2009, 8, 5674-8
    • (2009) J. Proteome Res. , vol.8 , pp. 5674-5678
    • Wisniewski, J.R.1    Zougman, A.2    Mann, M.3


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