메뉴 건너뛰기




Volumn 73, Issue 7, 2010, Pages 1391-1403

A comparison of the accuracy of iTRAQ quantification by nLC-ESI MSMS and nLC-MALDI MSMS methods

Author keywords

iTRAQ quantification; Mascot; nLC ESI MSMS; nLC MALDI MSMS; ProteinPilot

Indexed keywords

ION; PROTEIN;

EID: 77951022016     PISSN: 18743919     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jprot.2010.03.003     Document Type: Article
Times cited : (53)

References (26)
  • 1
    • 34250657012 scopus 로고    scopus 로고
    • Quantitative proteome analysis using isotope-coded affinity tags and mass spectrometry
    • Shiio Y., and Aebersold R. Quantitative proteome analysis using isotope-coded affinity tags and mass spectrometry. Nat Protoc 1 (2006) 139-145
    • (2006) Nat Protoc , vol.1 , pp. 139-145
    • Shiio, Y.1    Aebersold, R.2
  • 2
    • 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., Parker K., Hattan S., et al. Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol Cell Proteomics 3 (2004) 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    Parker, K.5    Hattan, S.6
  • 3
    • 33745782714 scopus 로고    scopus 로고
    • Downregulation of ClpR2 leads to reduced accumulation of the ClpPRS protease complex and defects in chloroplast biogenensis in Arabidopsis
    • Rudella A., Friso G., Alonso J.M., Ecker J.R., and van Wijk K.J. Downregulation of ClpR2 leads to reduced accumulation of the ClpPRS protease complex and defects in chloroplast biogenensis in Arabidopsis. Plant Cell 18 (2006) 1704-1721
    • (2006) Plant Cell , vol.18 , pp. 1704-1721
    • Rudella, A.1    Friso, G.2    Alonso, J.M.3    Ecker, J.R.4    van Wijk, K.J.5
  • 4
    • 44449152171 scopus 로고    scopus 로고
    • iTRAQ-facilitated proteomic analysis of human prostate cancer cells identifies proteins associated with progression
    • Glen A., Gan C.S., Hamdy F.C., Eaton C.L., Cross S.C., Catto J.W.F., et al. iTRAQ-facilitated proteomic analysis of human prostate cancer cells identifies proteins associated with progression. J Proteome Res 7 (2008) 897-907
    • (2008) J Proteome Res , vol.7 , pp. 897-907
    • Glen, A.1    Gan, C.S.2    Hamdy, F.C.3    Eaton, C.L.4    Cross, S.C.5    Catto, J.W.F.6
  • 5
    • 33846582052 scopus 로고    scopus 로고
    • Proteome and differential analysis of membrane cytosolic proteins from mycobacterium avium subsp. paratuberculosis
    • Radosevich T.J., Reinhardt T.A., Lippolis J.D., Bannantine J.P., and Stabel J.R. Proteome and differential analysis of membrane cytosolic proteins from mycobacterium avium subsp. paratuberculosis. J Bacteriol 189 (2007) 1109-1117
    • (2007) J Bacteriol , vol.189 , pp. 1109-1117
    • Radosevich, T.J.1    Reinhardt, T.A.2    Lippolis, J.D.3    Bannantine, J.P.4    Stabel, J.R.5
  • 6
    • 36049014914 scopus 로고    scopus 로고
    • 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., Moser F., Irwin D., et al. 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 18 (2007) 226-230
    • (2007) J Biomol Tech , vol.18 , pp. 226-230
    • Yang, Y.1    Zhang, S.2    Howe, K.3    Wilson, D.B.4    Moser, F.5    Irwin, D.6
  • 7
    • 67650753646 scopus 로고    scopus 로고
    • A comparison of MS/MS-based, stable isotope labelled, quantitation performance on ESI-quadrupole TOF and MALDI-TOF/TOF mass spectrometers
    • Kuzyk M.A., Ohlund L.B., Elliot M.H., Smith D., Qian H., Delany A., et al. A comparison of MS/MS-based, stable isotope labelled, quantitation performance on ESI-quadrupole TOF and MALDI-TOF/TOF mass spectrometers. Proteomics 9 (2009) 3328-3340
    • (2009) Proteomics , vol.9 , pp. 3328-3340
    • Kuzyk, M.A.1    Ohlund, L.B.2    Elliot, M.H.3    Smith, D.4    Qian, H.5    Delany, A.6
  • 8
    • 16544380308 scopus 로고    scopus 로고
    • Proteomic Analysis of Novel Marine Bacteria Using MALDI and ESI Mass Spectrometry
    • Stabels M.D., Cho J.-C., Giovannoni S.J., and Barofsky D.F. Proteomic Analysis of Novel Marine Bacteria Using MALDI and ESI Mass Spectrometry. J Biomol Tech 15 (2004) 191-198
    • (2004) J Biomol Tech , vol.15 , pp. 191-198
    • Stabels, M.D.1    Cho, J.-C.2    Giovannoni, S.J.3    Barofsky, D.F.4
  • 9
    • 0042386232 scopus 로고    scopus 로고
    • Exploiting the complementary nature of LC/MALDI/MS/MS and LC/ESI/MS/MS for increased proteome coverage
    • Bodnar W.M., Blackburn R.K., Krise J.M., and Moseley M.A. Exploiting the complementary nature of LC/MALDI/MS/MS and LC/ESI/MS/MS for increased proteome coverage. J Am Soc Mass Spectrom 14 (2003) 971-979
    • (2003) J Am Soc Mass Spectrom , vol.14 , pp. 971-979
    • Bodnar, W.M.1    Blackburn, R.K.2    Krise, J.M.3    Moseley, M.A.4
  • 10
    • 58149189418 scopus 로고    scopus 로고
    • comparison of relative quantification with isobaric tags on a subset of the murine hepatic proteome using electrospray ionisation quadrupole time of flight and matrix assisted laser desorption ionisation tandem time of flight
    • Scheri R.C., Lee J., Curtis L.R., and Barofsky D.F.A. comparison of relative quantification with isobaric tags on a subset of the murine hepatic proteome using electrospray ionisation quadrupole time of flight and matrix assisted laser desorption ionisation tandem time of flight. Rapid Commum Mass Spectrom 22 (2008) 3137-3146
    • (2008) Rapid Commum Mass Spectrom , vol.22 , pp. 3137-3146
    • Scheri, R.C.1    Lee, J.2    Curtis, L.R.3    Barofsky, D.F.A.4
  • 11
    • 33847174067 scopus 로고    scopus 로고
    • Protein labelling by iTRAQ: A new tool for quantitative mass spectrometry in proteome research
    • Wiese S., Reidergeld K.A., Meyer H.E., and Warscheid B. Protein labelling by iTRAQ: A new tool for quantitative mass spectrometry in proteome research. Proteomics 7 (2007) 340-350
    • (2007) Proteomics , vol.7 , pp. 340-350
    • Wiese, S.1    Reidergeld, K.A.2    Meyer, H.E.3    Warscheid, B.4
  • 12
    • 77951024232 scopus 로고    scopus 로고
    • http://www.abrf.org/ResearchGroups/Proteomics/Studies/ABRF-PRG07Presenta tion.ppt.
  • 13
    • 53049096977 scopus 로고    scopus 로고
    • 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., Romaschin A.D., Colgan T.J., et al. Absolute Quantification of endogenous levels of a potential cancer marker in cancerous and normal endometrial tissues. J Proteome Res 7 (2008) 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    Romaschin, A.D.5    Colgan, T.J.6
  • 14
    • 33645721632 scopus 로고    scopus 로고
    • Quantitive mass spectrometric multiple reaction monitoring assays for major plasma proteins
    • Anderson L., and Hunter C.L. Quantitive mass spectrometric multiple reaction monitoring assays for major plasma proteins. Mol Cell Proteomics 5 (2006) 573-588
    • (2006) Mol Cell Proteomics , vol.5 , pp. 573-588
    • Anderson, L.1    Hunter, C.L.2
  • 15
  • 16
    • 43849113605 scopus 로고    scopus 로고
    • Eight-channel iTRAQ enables comparison of the activity of six leukemogenic tyrosine kinases
    • Pierce A., Unwin R.D., Evans C.A., Griffith S., Carney L., Zhang L., et al. Eight-channel iTRAQ enables comparison of the activity of six leukemogenic tyrosine kinases. Mol Cell Proteomics 7 (2008) 853-863
    • (2008) Mol Cell Proteomics , vol.7 , pp. 853-863
    • Pierce, A.1    Unwin, R.D.2    Evans, C.A.3    Griffith, S.4    Carney, L.5    Zhang, L.6
  • 17
    • 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., Rehman I., and Wright P.C. iTRAQ underestimation in simple and complex mixtures: the good, the bad and the ugly. J Proteome Res 8 (2009) 5347-5355
    • (2009) J Proteome Res , vol.8 , pp. 5347-5355
    • Ow, S.Y.1    Salim, M.2    Noirel, J.3    Evans, C.4    Rehman, I.5    Wright, P.C.6
  • 18
    • 60849087975 scopus 로고    scopus 로고
    • Temporal quantitative proteomics by iTRAQ 2D-LC-MS/MS and corresponding mRNA expression analysis identify post-transcriptional modulation of actin-cytoskeleton regulators during TGF-β-Induced Epithelial-Mesenchymal transition
    • Farinazzo A., Restuccia U., Bachi A., Guerrier L., Fortis F., Boschetti E., et al. Temporal quantitative proteomics by iTRAQ 2D-LC-MS/MS and corresponding mRNA expression analysis identify post-transcriptional modulation of actin-cytoskeleton regulators during TGF-β-Induced Epithelial-Mesenchymal transition. J Proteome Res 8 (2009) 35-47
    • (2009) J Proteome Res , vol.8 , pp. 35-47
    • Farinazzo, A.1    Restuccia, U.2    Bachi, A.3    Guerrier, L.4    Fortis, F.5    Boschetti, E.6
  • 19
    • 44349164578 scopus 로고    scopus 로고
    • Analysis of iTRAQ data using Mascot and Peaks quantification algorithms. Brief Func Genomics
    • Lacerda C.M.R., Xin L., Rogers I., Reardon K.F., Analysis of iTRAQ data using Mascot and Peaks quantification algorithms. Brief Func Genomics Proteomics 2008;7:119-126.
    • (2008) Proteomics , vol.7 , pp. 119-126
    • Lacerda, C.M.R.1    Xin, L.2    Rogers, I.3    Reardon, K.F.4
  • 20
    • 34848889259 scopus 로고    scopus 로고
    • The Paragon Algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra
    • Shilov I.V., Seymour S.L., Patel A.A., Loboda A., Tang W.H., Keating S.P., et al. The Paragon Algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra. Mol Cell Proteomics 6 (2007) 1638-1655
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1638-1655
    • Shilov, I.V.1    Seymour, S.L.2    Patel, A.A.3    Loboda, A.4    Tang, W.H.5    Keating, S.P.6
  • 21
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin D.J.C., Creasy D.M., and Cotrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20 (1999) 3551-3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cotrell, J.S.4
  • 22
    • 33747791792 scopus 로고    scopus 로고
    • Optimized oroteomic analysis of a mouse model of cerebellar dysfunction using amine-specific isobaric tags
    • Hu J., Qian J., Borisov O., Pan S., Li Y., Liu T., et al. Optimized oroteomic analysis of a mouse model of cerebellar dysfunction using amine-specific isobaric tags. Proteomics 6 (2006) 4321-4334
    • (2006) Proteomics , vol.6 , pp. 4321-4334
    • Hu, J.1    Qian, J.2    Borisov, O.3    Pan, S.4    Li, Y.5    Liu, T.6
  • 23
    • 33749046638 scopus 로고    scopus 로고
    • Robust estimation of peptide abundance ratios and rigorous scoring of their variability and bias in quantitative shotgun proteomics
    • Pan C., Kora G., Pelletier D.A., McDonald W.H., Hurst G.B., Hettish R.L., et al. Robust estimation of peptide abundance ratios and rigorous scoring of their variability and bias in quantitative shotgun proteomics. Anal Chem 78 (2006) 7110-7120
    • (2006) Anal Chem , vol.78 , pp. 7110-7120
    • Pan, C.1    Kora, G.2    Pelletier, D.A.3    McDonald, W.H.4    Hurst, G.B.5    Hettish, R.L.6
  • 24
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labelling by amino aicds in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong S.E., Blagoev B., Kratchmarova I., Kristensen D.B., Steen H., Pandy A., et al. Stable isotope labelling by amino aicds in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 1 (2002) 376-386
    • (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    Pandy, A.6
  • 25
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi S.P., Rist B., Gerber S.A., Turecek F., Gelb M.H., and Aebersold R. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat Biotechnol 17 (1999) 994-999
    • (1999) Nat Biotechnol , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 26
    • 0346122950 scopus 로고    scopus 로고
    • A correlation algorithm for the automated analysis of quantitative 'shotgun' proteomics data
    • MacCoss M.J., Wu C.C., Liu H., Sadygov R., and Yates J.R. A correlation algorithm for the automated analysis of quantitative 'shotgun' proteomics data. Anal Chem 75 (2003) 6912-6921
    • (2003) Anal Chem , vol.75 , pp. 6912-6921
    • MacCoss, M.J.1    Wu, C.C.2    Liu, H.3    Sadygov, R.4    Yates, J.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.