메뉴 건너뛰기




Volumn 88, Issue , 2013, Pages 109-119

Performance evaluation of a dual linear ion trap-Fourier transform ion cyclotron resonance mass spectrometer for proteomics research

Author keywords

Dual cell fragmentation; Duty cycle; Dynamic range; Instrumentation; Velos FT; Yeast

Indexed keywords

ACCURACY; ARTICLE; FOURIER TRANSFORM MASS SPECTROMETRY; ION CYCLOTRON RESONANCE MASS SPECTROMETRY; ION TRAP MASS SPECTROMETRY; LIQUID CHROMATOGRAPHY; MASS SPECTROMETER; NONHUMAN; PRIORITY JOURNAL; PROTEOMICS; SACCHAROMYCES CEREVISIAE; CHEMISTRY; CYCLOTRON; FOURIER ANALYSIS; MASS SPECTROMETRY; PROCEDURES; DUAL CELL FRAGMENTATION; DUTY CYCLE; DYNAMIC RANGE; EQUIPMENT; METHODOLOGY; VELOS-FT; YEAST;

EID: 84893404193     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2013.04.009     Document Type: Article
Times cited : (24)

References (34)
  • 2
    • 3042789073 scopus 로고    scopus 로고
    • Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
    • Syka J.E., Coon J.J., Schroeder M.J., Shabanowitz J., Hunt D.F. Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc Natl Acad Sci U S A 2004, 101:9528-9533.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 9528-9533
    • Syka, J.E.1    Coon, J.J.2    Schroeder, M.J.3    Shabanowitz, J.4    Hunt, D.F.5
  • 5
    • 70349157281 scopus 로고    scopus 로고
    • Dual-pressure linear ion trap mass spectrometer improving the analysis of complex protein mixtures
    • Second T.P., Blethrow J.D., Schwartz J.C., Merrihew G.E., MacCoss M.J., Swaney D.L., et al. Dual-pressure linear ion trap mass spectrometer improving the analysis of complex protein mixtures. Anal Chem 2009, 81:7757-7765.
    • (2009) Anal Chem , vol.81 , pp. 7757-7765
    • Second, T.P.1    Blethrow, J.D.2    Schwartz, J.C.3    Merrihew, G.E.4    MacCoss, M.J.5    Swaney, D.L.6
  • 6
    • 0001268221 scopus 로고
    • Fourier transform ion cyclotron resonance spectroscopy
    • Comisarow M.B., Marshall A.G. Fourier transform ion cyclotron resonance spectroscopy. Chem Phys Lett 1974, 25:282-283.
    • (1974) Chem Phys Lett , vol.25 , pp. 282-283
    • Comisarow, M.B.1    Marshall, A.G.2
  • 7
    • 0030033198 scopus 로고    scopus 로고
    • Parent ion scans of unseparated peptide mixtures
    • Wilm M., Neubauer G., Mann M. Parent ion scans of unseparated peptide mixtures. Anal Chem 1996, 68:527-533.
    • (1996) Anal Chem , vol.68 , pp. 527-533
    • Wilm, M.1    Neubauer, G.2    Mann, M.3
  • 8
    • 0033621537 scopus 로고    scopus 로고
    • Mass spectrometry. From genomics to proteomics
    • Yates J.R. Mass spectrometry. From genomics to proteomics. Trends Genet 2000, 16:5-8.
    • (2000) Trends Genet , vol.16 , pp. 5-8
    • Yates, J.R.1
  • 9
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn M.P., Wolters D., Yates J.R. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol 2001, 19:242-247.
    • (2001) Nat Biotechnol , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 10
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold R., Mann M. Mass spectrometry-based proteomics. Nature 2003, 422:198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 11
    • 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, 20:3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 12
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng J.K., McCormack A.L., Yates J.R. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J Am Soc Mass Spectrom 1994, 5:976-989.
    • (1994) J Am Soc Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 14
    • 68749094119 scopus 로고    scopus 로고
    • Full dynamic range proteome analysis of S. cerevisiae by targeted proteomics
    • Picotti P., Bodenmiller B., Mueller L.N., Domon B., Aebersold R. Full dynamic range proteome analysis of S. cerevisiae by targeted proteomics. Cell 2009, 138:795-806.
    • (2009) Cell , vol.138 , pp. 795-806
    • Picotti, P.1    Bodenmiller, B.2    Mueller, L.N.3    Domon, B.4    Aebersold, R.5
  • 15
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • Mann M., Jensen O.N. Proteomic analysis of post-translational modifications. Nat Biotechnol 2003, 21:255-261.
    • (2003) Nat Biotechnol , vol.21 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 16
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • Domon B., Aebersold R. Mass spectrometry and protein analysis. Science (New York, N.Y.) 2006, 312:212-217.
    • (2006) Science (New York, N.Y.) , vol.312 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 18
    • 84990643459 scopus 로고
    • Selected-ion accumulation from an external electrospray ionization source with a Fourier-transform ion cyclotron resonance mass spectrometer
    • Bruce J.E., Anderson G.A., Hofstadler S.A., Van Orden S.L., Sherman M.S., Rockwood A.L., et al. Selected-ion accumulation from an external electrospray ionization source with a Fourier-transform ion cyclotron resonance mass spectrometer. Rapid Commun Mass Spectrom 1993, 7:914-919.
    • (1993) Rapid Commun Mass Spectrom , vol.7 , pp. 914-919
    • Bruce, J.E.1    Anderson, G.A.2    Hofstadler, S.A.3    Van Orden, S.L.4    Sherman, M.S.5    Rockwood, A.L.6
  • 19
    • 0029679968 scopus 로고    scopus 로고
    • Prediction of a space charge induced upper molecular mass limit towards achieving unit mass resolution in Fourier transform ion cyclotron resonance mass spectrometry
    • Mitchell D.W., Smith R.D. Prediction of a space charge induced upper molecular mass limit towards achieving unit mass resolution in Fourier transform ion cyclotron resonance mass spectrometry. J Mass Spectrom 1996, 31:771-790.
    • (1996) J Mass Spectrom , vol.31 , pp. 771-790
    • Mitchell, D.W.1    Smith, R.D.2
  • 20
    • 0030200025 scopus 로고    scopus 로고
    • Collision induced decomposition of peptides. Choice of collision parameters
    • Haller I., Mirza U.A., Chait B.T. Collision induced decomposition of peptides. Choice of collision parameters. J Am Soc Mass Spectrom 1996, 7:677-681.
    • (1996) J Am Soc Mass Spectrom , vol.7 , pp. 677-681
    • Haller, I.1    Mirza, U.A.2    Chait, B.T.3
  • 21
    • 0023627313 scopus 로고
    • Rapid lysis technique for mycobacterial species
    • Hurley S.S., Splitter G.A., Welch R.A. Rapid lysis technique for mycobacterial species. J Clin Microbiol 1987, 25:2227-2229.
    • (1987) J Clin Microbiol , vol.25 , pp. 2227-2229
    • Hurley, S.S.1    Splitter, G.A.2    Welch, R.A.3
  • 22
    • 34547727671 scopus 로고    scopus 로고
    • High-speed data reduction, feature detection, and MS/MS spectrum quality assessment of shotgun proteomics data sets using high-resolution mass spectrometry
    • Hoopmann M.R., Finney G.L., MacCoss M.J. High-speed data reduction, feature detection, and MS/MS spectrum quality assessment of shotgun proteomics data sets using high-resolution mass spectrometry. Anal Chem 2007, 79:5620-5632.
    • (2007) Anal Chem , vol.79 , pp. 5620-5632
    • Hoopmann, M.R.1    Finney, G.L.2    MacCoss, M.J.3
  • 23
    • 33746285299 scopus 로고    scopus 로고
    • Label-free quantitative proteomics using large peptide data sets generated by nanoflow liquid chromatography and mass spectrometry
    • Ono M., Shitashige M., Honda K., Isobe T., Kuwabara H., Matsuzuki H., et al. Label-free quantitative proteomics using large peptide data sets generated by nanoflow liquid chromatography and mass spectrometry. Mol Cell Proteomics 2006, 5:1338-1347.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 1338-1347
    • Ono, M.1    Shitashige, M.2    Honda, K.3    Isobe, T.4    Kuwabara, H.5    Matsuzuki, H.6
  • 26
    • 33749606981 scopus 로고    scopus 로고
    • Extending top-down mass spectrometry to proteins with masses greater than 200kilodaltons
    • Han X., Jin M., Breuker K., McLafferty F.W. Extending top-down mass spectrometry to proteins with masses greater than 200kilodaltons. Science (New York, N.Y.) 2006, 314:109-112.
    • (2006) Science (New York, N.Y.) , vol.314 , pp. 109-112
    • Han, X.1    Jin, M.2    Breuker, K.3    McLafferty, F.W.4
  • 27
    • 36749004371 scopus 로고    scopus 로고
    • Top-down MS, a powerful complement to the high capabilities of proteolysis proteomics
    • McLafferty F.W., Breuker K., Jin M., Han X., Infusini G., Jiang H., et al. Top-down MS, a powerful complement to the high capabilities of proteolysis proteomics. FEBS J 2007, 274:6256-6268.
    • (2007) FEBS J , vol.274 , pp. 6256-6268
    • McLafferty, F.W.1    Breuker, K.2    Jin, M.3    Han, X.4    Infusini, G.5    Jiang, H.6
  • 28
    • 2642578319 scopus 로고    scopus 로고
    • A new approach for plant proteomics: characterization of chloroplast proteins of Arabidopsis thaliana by top-down mass spectrometry
    • Zabrouskov V., Giacomelli L., van Wijk K.J., McLafferty F.W. A new approach for plant proteomics: characterization of chloroplast proteins of Arabidopsis thaliana by top-down mass spectrometry. Mol Cell Proteomics 2003, 2:1253-1260.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 1253-1260
    • Zabrouskov, V.1    Giacomelli, L.2    van Wijk, K.J.3    McLafferty, F.W.4
  • 29
    • 2642520417 scopus 로고    scopus 로고
    • Top-down proteomics
    • Kelleher N.L. Top-down proteomics. Anal Chem 2004, 76:197A-203A.
    • (2004) Anal Chem , vol.76 , pp. 197A-203A
    • Kelleher, N.L.1
  • 30
    • 3242717090 scopus 로고    scopus 로고
    • Construction of a hybrid quadrupole/Fourier transform ion cyclotron resonance mass spectrometer for versatile MS/MS above 10kDa
    • Patrie S.M., Charlebois J.P., Whipple D., Kelleher N.L., Hendrickson C.L., Quinn J.P., et al. Construction of a hybrid quadrupole/Fourier transform ion cyclotron resonance mass spectrometer for versatile MS/MS above 10kDa. J Am Soc Mass Spectrom 2004, 15:1099-1108.
    • (2004) J Am Soc Mass Spectrom , vol.15 , pp. 1099-1108
    • Patrie, S.M.1    Charlebois, J.P.2    Whipple, D.3    Kelleher, N.L.4    Hendrickson, C.L.5    Quinn, J.P.6
  • 31
    • 79955755606 scopus 로고    scopus 로고
    • Higher-energy collision-activated dissociation without a dedicated collision cell
    • O111.009456
    • McAlister G.C., Phanstiel D.H., Westphall M.S., Coon J.J. Higher-energy collision-activated dissociation without a dedicated collision cell. Mol Cell Proteomics 2011, 10(5). O111.009456.
    • (2011) Mol Cell Proteomics , vol.10 , Issue.5
    • McAlister, G.C.1    Phanstiel, D.H.2    Westphall, M.S.3    Coon, J.J.4
  • 32
    • 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 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    Parker, K.5    Hattan, S.6
  • 33
    • 84877623973 scopus 로고    scopus 로고
    • Protein interactions, posttranslational modifications and topologies in human cells
    • Chavez J.D., Weisbrod C.R., Zheng C., Eng J.K., Bruce J.E. Protein interactions, posttranslational modifications and topologies in human cells. Mol Cell Proteomics 2013, 12(5):1451-1467.
    • (2013) Mol Cell Proteomics , vol.12 , Issue.5 , pp. 1451-1467
    • Chavez, J.D.1    Weisbrod, C.R.2    Zheng, C.3    Eng, J.K.4    Bruce, J.E.5
  • 34
    • 84875913034 scopus 로고    scopus 로고
    • In vivo protein interaction network identified with a novel real-time cross-linked peptide identification strategy
    • Weisbrod C.R., Chavez J.D., Eng J.K., Yang L., Zheng C., Bruce J.E. In vivo protein interaction network identified with a novel real-time cross-linked peptide identification strategy. J Proteome Res 2013, 12(4):1569-1579.
    • (2013) J Proteome Res , vol.12 , Issue.4 , pp. 1569-1579
    • Weisbrod, C.R.1    Chavez, J.D.2    Eng, J.K.3    Yang, L.4    Zheng, C.5    Bruce, J.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.