메뉴 건너뛰기




Volumn 11, Issue 11, 2011, Pages 2341-2346

Minimising iTRAQ ratio compression through understanding LC-MS elution dependence and high-resolution HILIC fractionation

Author keywords

ITRAQ proteomics; ITRAQ underestimation; MS MS mixing; Quantitative proteomics; Technology

Indexed keywords

ARTICLE; LIQUID CHROMATOGRAPHY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEOMICS; QUANTITATIVE ANALYSIS; TANDEM MASS SPECTROMETRY;

EID: 79956270174     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201000752     Document Type: Article
Times cited : (104)

References (22)
  • 1
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross, P. L., Huang, Y. N., Marchese, J. N., Williamson, B. et al., Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol. Cell. Proteomics 2004, 3, 1154-1169.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 1154-1169
    • Ross, P.L.1    Huang, Y.N.2    Marchese, J.N.3    Williamson, B.4
  • 3
    • 33646269941 scopus 로고    scopus 로고
    • A perspective on the use of iTRAQ reagent technology for protein complex and profiling studies
    • Zieske, L. R., A perspective on the use of iTRAQ reagent technology for protein complex and profiling studies. J. Exp. Bot. 2006, 57, 1501-1508.
    • (2006) J. Exp. Bot. , vol.57 , pp. 1501-1508
    • Zieske, L.R.1
  • 4
    • 79952774780 scopus 로고    scopus 로고
    • Methods in quantitative proteomics: setting iTRAQ on the right track
    • Noirel, J., Evans, C., Salim, M., Mukherjee, J. et al., Methods in quantitative proteomics: setting iTRAQ on the right track. Curr. Proteomics 2011, 8, 17-30.
    • (2011) Curr. Proteomics , vol.8 , pp. 17-30
    • Noirel, J.1    Evans, C.2    Salim, M.3    Mukherjee, J.4
  • 5
    • 36049014914 scopus 로고    scopus 로고
    • A comparison of nLC-ESI-MS/MS and nLC-MALDI-MS/MS for GeLC-based protein identification and iTRAQ-based shotgun quantitative proteomics
    • Yang, Y., Zhang, S., Howe, K., Wilson, D. B. et al., A comparison of nLC-ESI-MS/MS and nLC-MALDI-MS/MS for GeLC-based protein identification and iTRAQ-based shotgun quantitative proteomics. J. Biomol. Tech. 2007, 18, 226-237.
    • (2007) J. Biomol. Tech. , vol.18 , pp. 226-237
    • Yang, Y.1    Zhang, S.2    Howe, K.3    Wilson, D.B.4
  • 6
    • 36348987990 scopus 로고    scopus 로고
    • iTRAQ reagent-based quantitative proteomic analysis on a linear ion trap mass spectrometer
    • Griffin, T. J., Xie, H., Bandhakavi, S., Popko, J. et al., iTRAQ reagent-based quantitative proteomic analysis on a linear ion trap mass spectrometer. J. Proteome Res. 2007, 6, 4200-4209.
    • (2007) J. Proteome Res. , vol.6 , pp. 4200-4209
    • Griffin, T.J.1    Xie, H.2    Bandhakavi, S.3    Popko, J.4
  • 7
    • 52649098504 scopus 로고    scopus 로고
    • Robust and sensitive iTRAQ quantification on an LTQ Orbitrap mass spectrometer
    • Bantscheff, M., Boesche, M., Eberhard, D., Matthieson, T. et al., Robust and sensitive iTRAQ quantification on an LTQ Orbitrap mass spectrometer. Mol. Cell. Proteomics 2008, 7, 1702-1713.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1702-1713
    • Bantscheff, M.1    Boesche, M.2    Eberhard, D.3    Matthieson, T.4
  • 8
    • 77955462279 scopus 로고    scopus 로고
    • Addressing accuracy and precision issues in iTRAQ quantitation
    • Karp, N. A., Huber, W., Sadowski, P. G., Charles, P. D. et al., Addressing accuracy and precision issues in iTRAQ quantitation. Mol. Cell. Proteomics 2010, 9, 1885-1897.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1885-1897
    • Karp, N.A.1    Huber, W.2    Sadowski, P.G.3    Charles, P.D.4
  • 9
    • 70449412362 scopus 로고    scopus 로고
    • iTRAQ underestimation in simple and complex mixtures: the good, the bad and the ugly
    • Ow, S. Y., Salim, M., Noirel, J., Evans, C. et al., iTRAQ underestimation in simple and complex mixtures: the good, the bad and the ugly. J. Proteome Res. 2009, 8, 5347-5355.
    • (2009) J. Proteome Res. , vol.8 , pp. 5347-5355
    • Ow, S.Y.1    Salim, M.2    Noirel, J.3    Evans, C.4
  • 10
    • 77956836941 scopus 로고    scopus 로고
    • Targeted data acquisition for improved reproducibility and robustness of proteomic mass spectrometry assays
    • Savitski, M. M., Fischer, F., Mathieson, T., Sweetman, G. et al., Targeted data acquisition for improved reproducibility and robustness of proteomic mass spectrometry assays. J. Am. Soc. Mass Spectrom. 2010, 21, 1668-1679.
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 1668-1679
    • Savitski, M.M.1    Fischer, F.2    Mathieson, T.3    Sweetman, G.4
  • 11
    • 53049096977 scopus 로고    scopus 로고
    • Multiple reaction monitoring of mTRAQ-labeled peptides enables absolute quantification of endogenous levels of a potential cancer marker in cancerous and normal endometrial tissues
    • DeSouza, L. V., Taylor, A. M., Li, W., Minkoff, M. S. et al., Multiple reaction monitoring of mTRAQ-labeled peptides enables absolute quantification of endogenous levels of a potential cancer marker in cancerous and normal endometrial tissues. J. Proteome Res. 2008, 7, 3525-3534.
    • (2008) J. Proteome Res. , vol.7 , pp. 3525-3534
    • DeSouza, L.V.1    Taylor, A.M.2    Li, W.3    Minkoff, M.S.4
  • 12
    • 77952979841 scopus 로고    scopus 로고
    • Balancing robust quantification and identification for iTRAQ: application of UHR-ToF MS
    • Ow, S. Y., Noirel, J., Salim, M., Evans, C. et al., Balancing robust quantification and identification for iTRAQ: application of UHR-ToF MS. Proteomics 2010, 10, 2205-2213.
    • (2010) Proteomics , vol.10 , pp. 2205-2213
    • Ow, S.Y.1    Noirel, J.2    Salim, M.3    Evans, C.4
  • 13
    • 36348936820 scopus 로고    scopus 로고
    • Two-dimensional reversed-phase x ion-pair reversed-phase HPLC: an alternative approach to high-resolution peptide separation for shotgun proteome analysis
    • Delmotte, N., Lasaosa, M., Tholey, A., Heinzle, E., Huber, C. G., Two-dimensional reversed-phase x ion-pair reversed-phase HPLC: an alternative approach to high-resolution peptide separation for shotgun proteome analysis. J. Proteome Res. 2007, 6, 4363-4373.
    • (2007) J. Proteome Res. , vol.6 , pp. 4363-4373
    • Delmotte, N.1    Lasaosa, M.2    Tholey, A.3    Heinzle, E.4    Huber, C.G.5
  • 14
    • 51549102028 scopus 로고    scopus 로고
    • Comparison of two-dimensional fractionation techniques for shotgun proteomics
    • Dowell, J. A., Frost, D. C., Zhang, J., Li, L., Comparison of two-dimensional fractionation techniques for shotgun proteomics. Anal. Chem. 2008, 80, 6715-6723.
    • (2008) Anal. Chem. , vol.80 , pp. 6715-6723
    • Dowell, J.A.1    Frost, D.C.2    Zhang, J.3    Li, L.4
  • 15
    • 77955602986 scopus 로고    scopus 로고
    • Shotgun proteome analysis utilising mixed mode (reversed phase-anion exchange chromatography) in conjunction with reversed phase liquid chromatography mass spectrometry analysis
    • Phillips, H. L., Williamson, J. C., van Elburg, K. A., Snijders, A. P. et al., Shotgun proteome analysis utilising mixed mode (reversed phase-anion exchange chromatography) in conjunction with reversed phase liquid chromatography mass spectrometry analysis. Proteomics 2010, 10, 2950-2960.
    • (2010) Proteomics , vol.10 , pp. 2950-2960
    • Phillips, H.L.1    Williamson, J.C.2    van Elburg, K.A.3    Snijders, A.P.4
  • 16
    • 79956265630 scopus 로고    scopus 로고
    • 58th Annual American Society for Mass Spectrometry Meeting, Matrix Science, Salt Lake City
    • Pappin, D., Emery, P., 58th Annual American Society for Mass Spectrometry Meeting, Matrix Science, Salt Lake City 2010.
    • (2010)
    • Pappin, D.1    Emery, P.2
  • 17
    • 43849091451 scopus 로고    scopus 로고
    • Hydrophilic interaction chromatography reduces the complexity of the phosphoproteome and improves global phosphopeptide isolation and detection
    • McNulty, D. E., Annan, R. S., Hydrophilic interaction chromatography reduces the complexity of the phosphoproteome and improves global phosphopeptide isolation and detection. Mol. Cell. Proteomics 2008, 7, 971-980.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 971-980
    • McNulty, D.E.1    Annan, R.S.2
  • 18
    • 47849125967 scopus 로고    scopus 로고
    • A multidimensional chromatography technology for in-depth phosphoproteome analysis
    • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V. et al., A multidimensional chromatography technology for in-depth phosphoproteome analysis. Mol. Cell. Proteomics 2008, 7, 1389-1396.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1389-1396
    • Albuquerque, C.P.1    Smolka, M.B.2    Payne, S.H.3    Bafna, V.4
  • 19
    • 20544442274 scopus 로고    scopus 로고
    • Comparison of protein and peptide prefractionation methods for the shotgun proteomic analysis of Synechocystis sp. PCC 6803
    • Gan, C. S., Reardon, K. F., Wright, P. C., Comparison of protein and peptide prefractionation methods for the shotgun proteomic analysis of Synechocystis sp. PCC 6803. Proteomics 2005, 5, 2468-2478.
    • (2005) Proteomics , vol.5 , pp. 2468-2478
    • Gan, C.S.1    Reardon, K.F.2    Wright, P.C.3
  • 21
    • 79956264740 scopus 로고    scopus 로고
    • 58th Annual American Society for Mass Spectrometry Meeting, American Society for Mass Spectrometry, Salt Lake City.
    • Wenger, C. D., Phanstiel, D., Coon, J. J., 58th Annual American Society for Mass Spectrometry Meeting, American Society for Mass Spectrometry, Salt Lake City 2010.
    • (2010)
    • Wenger, C.D.1    Phanstiel, D.2    Coon, J.J.3
  • 22
    • 70449360870 scopus 로고    scopus 로고
    • iTRAQ gets put to the test
    • Perkel, J. M., iTRAQ gets put to the test. J. Proteome Res. 2009, 8, 4885.
    • (2009) J. Proteome Res. , vol.8 , pp. 4885
    • Perkel, J.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.