메뉴 건너뛰기




Volumn 11, Issue 10, 2012, Pages 5081-5089

Combination of gas-phase fractionation and MS3 acquisition modes for relative protein quantification with isobaric tagging

Author keywords

gas phase fractionation; isobaric tag; quantitative proteomics; tandem mass tag; third stage MS

Indexed keywords

ARTICLE; FRACTIONATION; FRAGMENTATION REACTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEOMICS;

EID: 84867460245     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr300519c     Document Type: Article
Times cited : (31)

References (24)
  • 3
    • 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 (8) 1895-1904
    • (2003) Anal. Chem. , vol.75 , Issue.8 , 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
  • 5
    • 39449111536 scopus 로고    scopus 로고
    • Genome-specific gas-phase fractionation strategy for improved shotgun proteomic profiling of proteotypic peptides
    • Scherl, A.; Shaffer, S. A.; Taylor, G. K.; Kulasekara, H. D.; Miller, S. I.; Goodlett, D. R. Genome-specific gas-phase fractionation strategy for improved shotgun proteomic profiling of proteotypic peptides Anal. Chem. 2008, 80 (4) 1182-1191
    • (2008) Anal. Chem. , vol.80 , Issue.4 , pp. 1182-1191
    • Scherl, A.1    Shaffer, S.A.2    Taylor, G.K.3    Kulasekara, H.D.4    Miller, S.I.5    Goodlett, D.R.6
  • 6
    • 14744293536 scopus 로고    scopus 로고
    • Automated approach for quantitative analysis of complex peptide mixtures from tandem mass spectra
    • Venable, J. D.; Dong, M. Q.; Wohlschlegel, J.; Dillin, A.; Yates, J. R. Automated approach for quantitative analysis of complex peptide mixtures from tandem mass spectra Nat. Methods 2004, 1 (1) 39-45
    • (2004) Nat. Methods , vol.1 , Issue.1 , pp. 39-45
    • Venable, J.D.1    Dong, M.Q.2    Wohlschlegel, J.3    Dillin, A.4    Yates, J.R.5
  • 8
    • 84861860481 scopus 로고    scopus 로고
    • Targeted data extraction of the MS/MS spectra generated by data independent acquisition: A new concept for consistent and accurate proteome analysis
    • 10.1074/mcp.O111.016717
    • Gillet, L. C.; Navarro, P.; Tate, S.; Roest, H.; Selevsek, N.; Reiter, L.; Bonner, R.; Aebersold, R. Targeted data extraction of the MS/MS spectra generated by data independent acquisition: a new concept for consistent and accurate proteome analysis Mol. Cell. Proteomics 2012, 10.1074/mcp.O111.016717
    • (2012) Mol. Cell. Proteomics
    • Gillet, L.C.1    Navarro, P.2    Tate, S.3    Roest, H.4    Selevsek, N.5    Reiter, L.6    Bonner, R.7    Aebersold, R.8
  • 9
    • 79954569537 scopus 로고    scopus 로고
    • Faster, quantitative, and accurate precursor acquisition independent from ion count
    • Panchaud, A.; Jung, S.; Shaffer, S. A.; Aitchison, J. D.; Goodlett, D. R. Faster, quantitative, and accurate precursor acquisition independent from ion count Anal. Chem. 2011, 83 (6) 2250-2257
    • (2011) Anal. Chem. , vol.83 , Issue.6 , pp. 2250-2257
    • Panchaud, A.1    Jung, S.2    Shaffer, S.A.3    Aitchison, J.D.4    Goodlett, D.R.5
  • 10
    • 82555185589 scopus 로고    scopus 로고
    • Delayed fragmentation and optimized isolation width settings for improvement of protein identification and accuracy of isobaric mass tag quantification on Orbitrap-type mass spectrometers
    • Savitski, M. M.; Sweetman, G.; Askenazi, M.; Marto, J. A.; Lang, M.; Zinn, N.; Bantscheff, M. Delayed fragmentation and optimized isolation width settings for improvement of protein identification and accuracy of isobaric mass tag quantification on Orbitrap-type mass spectrometers Anal. Chem. 2011, 83 (23) 8959-8967
    • (2011) Anal. Chem. , vol.83 , Issue.23 , pp. 8959-8967
    • Savitski, M.M.1    Sweetman, G.2    Askenazi, M.3    Marto, J.A.4    Lang, M.5    Zinn, N.6    Bantscheff, M.7
  • 11
  • 12
    • 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 (11) 937-940
    • (2011) Nat. Methods , vol.8 , Issue.11 , pp. 937-940
    • Ting, L.1    Rad, R.2    Gygi, S.P.3    Haas, W.4
  • 13
    • 74849138649 scopus 로고    scopus 로고
    • Combining low- and high-energy tandem mass spectra for optimized peptide quantification with isobaric tags
    • Dayon, L.; Pasquarello, C.; Hoogland, C.; Sanchez, J.-C.; Scherl, A. Combining low- and high-energy tandem mass spectra for optimized peptide quantification with isobaric tags J. Proteomics 2010, 73 (4) 769-777
    • (2010) J. Proteomics , vol.73 , Issue.4 , pp. 769-777
    • Dayon, L.1    Pasquarello, C.2    Hoogland, C.3    Sanchez, J.-C.4    Scherl, A.5
  • 14
    • 70349974261 scopus 로고    scopus 로고
    • High precision quantitative proteomics using iTRAQ on an LTQ Orbitrap: A new mass spectrometric method combining the benefits of all
    • Koecher, T.; Pichler, P.; Schutzbier, M.; Stingl, C.; Kaul, A.; Teucher, N.; Hasenfuss, G.; Penninger, J. M.; Mechtler, K. High precision quantitative proteomics using iTRAQ on an LTQ Orbitrap: a new mass spectrometric method combining the benefits of all J. Proteome Res. 2009, 8 (10) 4743-4752
    • (2009) J. Proteome Res. , vol.8 , Issue.10 , pp. 4743-4752
    • Koecher, T.1    Pichler, P.2    Schutzbier, M.3    Stingl, C.4    Kaul, A.5    Teucher, N.6    Hasenfuss, G.7    Penninger, J.M.8    Mechtler, K.9
  • 15
    • 67651027832 scopus 로고    scopus 로고
    • Optimized Orbitrap HCD for quantitative analysis of phosphopeptides
    • Zhang, Y.; Ficarro, S. B.; Li, S.; Marto, J. A. Optimized Orbitrap HCD for quantitative analysis of phosphopeptides J. Am. Soc. Mass Spectrom. 2009, 20 (8) 1425-1434
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , Issue.8 , pp. 1425-1434
    • Zhang, Y.1    Ficarro, S.B.2    Li, S.3    Marto, J.A.4
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 1976, 72, 248-54
    • (1976) Anal. Biochem. , vol.72 , pp. 248-54
    • Bradford, M.M.1
  • 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 (11) 923-925
    • (2007) Nat. Methods , vol.4 , Issue.11 , pp. 923-925
    • Kall, L.1    Canterbury, J.D.2    Weston, J.3    Noble, W.S.4    Maccoss, M.J.5
  • 18
    • 24044513966 scopus 로고    scopus 로고
    • Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations
    • Elias, J. E.; Haas, W.; Faherty, B. K.; Gygi, S. P. Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations Nat. Methods 2005, 2 (9) 667-675
    • (2005) Nat. Methods , vol.2 , Issue.9 , pp. 667-675
    • Elias, J.E.1    Haas, W.2    Faherty, B.K.3    Gygi, S.P.4
  • 19
    • 30344451098 scopus 로고    scopus 로고
    • Two-dimensional separation of peptides using RP-RP-HPLC system with different pH in first and second separation dimensions
    • Gilar, M.; Olivova, P.; Daly, A. E.; Gebler, J. C. Two-dimensional separation of peptides using RP-RP-HPLC system with different pH in first and second separation dimensions J. Sep. Sci. 2005, 28 (14) 1694-703
    • (2005) J. Sep. Sci. , vol.28 , Issue.14 , pp. 1694-703
    • Gilar, M.1    Olivova, P.2    Daly, A.E.3    Gebler, J.C.4
  • 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 (8) 4045-52
    • (2010) J. Proteome Res. , vol.9 , Issue.8 , pp. 4045-52
    • Thingholm, T.E.1    Palmisano, G.2    Kjeldsen, F.3    Larsen, M.R.4
  • 22
    • 76149118094 scopus 로고    scopus 로고
    • Isobaric tagging-based selection and quantitation of cerebrospinal fluid tryptic peptides with reporter calibration curves
    • Dayon, L.; Turck, N.; Kienle, S.; Schulz-Knappe, P.; Hochstrasser, D. F.; Scherl, A.; Sanchez, J.-C. Isobaric tagging-based selection and quantitation of cerebrospinal fluid tryptic peptides with reporter calibration curves Anal. Chem. 2010, 82 (3) 848-858
    • (2010) Anal. Chem. , vol.82 , Issue.3 , pp. 848-858
    • Dayon, L.1    Turck, N.2    Kienle, S.3    Schulz-Knappe, P.4    Hochstrasser, D.F.5    Scherl, A.6    Sanchez, J.-C.7
  • 23
    • 77951533012 scopus 로고    scopus 로고
    • From relative to absolute quantification of tryptic peptides with tandem mass tags: Application to cerebrospinal fluid
    • Dayon, L.; Turck, N.; Scherl, A.; Hochstrasser, D. F.; Burkhard, P. R.; Sanchez, J.-C. From relative to absolute quantification of tryptic peptides with tandem mass tags: application to cerebrospinal fluid Chimia 2010, 64 (3) 132-135
    • (2010) Chimia , vol.64 , Issue.3 , pp. 132-135
    • Dayon, L.1    Turck, N.2    Scherl, A.3    Hochstrasser, D.F.4    Burkhard, P.R.5    Sanchez, J.-C.6
  • 24
    • 84863387252 scopus 로고    scopus 로고
    • Subsecond absolute quantitation of amine metabolites using isobaric tags for discovery of pathway activation in mammalian cells
    • Yuan, W.; Anderson, K. W.; Li, S.; Edwards, J. L. Subsecond absolute quantitation of amine metabolites using isobaric tags for discovery of pathway activation in mammalian cells Anal. Chem. 2012, 84 (6) 2892-2899
    • (2012) Anal. Chem. , vol.84 , Issue.6 , pp. 2892-2899
    • Yuan, W.1    Anderson, K.W.2    Li, S.3    Edwards, J.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.