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Volumn 6, Issue 5, 2007, Pages 2019-2026

Preparative peptide isoelectric focusing as a tool for improving the identification of lysine-acetylated peptides from complex mixtures

Author keywords

Acetylation; False positive sequence match; Free flow electrophoresis; Peptide isoelectric focusing; Post translational modification; Proteomic; Tandem mass spectrometry

Indexed keywords

FUNGAL PROTEIN; LYSINE;

EID: 34249275640     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr060691j     Document Type: Article
Times cited : (29)

References (36)
  • 1
    • 34249342349 scopus 로고    scopus 로고
    • Verification of single-peptide protein identifications by the application of complementary database search algorithms
    • Rohrbough, J. G.; et al. Verification of single-peptide protein identifications by the application of complementary database search algorithms. J. Biomol. Tech. 2006, 17 (5), 327-32.
    • (2006) J. Biomol. Tech , vol.17 , Issue.5 , pp. 327-332
    • Rohrbough, J.G.1
  • 2
    • 33750728385 scopus 로고    scopus 로고
    • Advances and challenges in liquid chromatography-mass spectrometry-based proteomics profiling for clinical applications
    • Qian, W. J.; et al. Advances and challenges in liquid chromatography-mass spectrometry-based proteomics profiling for clinical applications. Mol. Cell. Proteomics 2006, 5 (10), 1727-44.
    • (2006) Mol. Cell. Proteomics , vol.5 , Issue.10 , pp. 1727-1744
    • Qian, W.J.1
  • 3
    • 20544459308 scopus 로고    scopus 로고
    • High-throughput proteomics using Fourier transform ion cyclotron resonance mass spectrometry
    • Qian, W. J.; Camp, D. G., II; Smith, R. D. High-throughput proteomics using Fourier transform ion cyclotron resonance mass spectrometry. Expert Rev. Proteomics 2004, 1 (1), 87-95.
    • (2004) Expert Rev. Proteomics , vol.1 , Issue.1 , pp. 87-95
    • Qian, W.J.1    Camp II, D.G.2    Smith, R.D.3
  • 4
    • 4544370533 scopus 로고    scopus 로고
    • Improved peptide identification in proteomics by two consecutive stages of mass spectrometric fragmentation
    • Olsen, J. V.; and Mann, M. Improved peptide identification in proteomics by two consecutive stages of mass spectrometric fragmentation. Proc. Natl. Acad. Sci. U.S.A. 2004, 101 (37), 13417-22.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , Issue.37 , pp. 13417-13422
    • Olsen, J.V.1    Mann, M.2
  • 5
    • 27644489325 scopus 로고    scopus 로고
    • Characterization of mouse spleen cells by subtractive proteomics
    • Dieguez-Acuna, F. J.; et al. Characterization of mouse spleen cells by subtractive proteomics. Mol. Cell. Proteomics 2005, 4 (10), 1459-70.
    • (2005) Mol. Cell. Proteomics , vol.4 , Issue.10 , pp. 1459-1470
    • Dieguez-Acuna, F.J.1
  • 6
    • 12444272753 scopus 로고    scopus 로고
    • Use of artificial neural networks for the accurate prediction of peptide liquid chromatography elution times in proteome analyses
    • Petritis, K.; et al. Use of artificial neural networks for the accurate prediction of peptide liquid chromatography elution times in proteome analyses. Anal. Chem. 2003, 75 (5), 1039-48.
    • (2003) Anal. Chem , vol.75 , Issue.5 , pp. 1039-1048
    • Petritis, K.1
  • 7
    • 0037112383 scopus 로고    scopus 로고
    • Prediction of chromatographic retention and protein identification in liquid chromatography/mass spectrometry
    • Palmblad, M.; et al. Prediction of chromatographic retention and protein identification in liquid chromatography/mass spectrometry. Anal. Chem. 2002, 74 (22), 5826-30.
    • (2002) Anal. Chem , vol.74 , Issue.22 , pp. 5826-5830
    • Palmblad, M.1
  • 8
    • 0035870175 scopus 로고    scopus 로고
    • Packed capillary reversed-phase liquid chromatography with high-performance electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry for proteomics
    • Shen, Y.; et al. Packed capillary reversed-phase liquid chromatography with high-performance electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry for proteomics. Anal. Chem. 2001, 73 (8), 1766-75.
    • (2001) Anal. Chem , vol.73 , Issue.8 , pp. 1766-1775
    • Shen, Y.1
  • 9
    • 20544437625 scopus 로고    scopus 로고
    • Quantitative proteome analysis of human plasma following in vivo lipopolysaccharide administration using 160/180 labeling and the accurate mass and time tag approach
    • Qian, W. J.; et al. Quantitative proteome analysis of human plasma following in vivo lipopolysaccharide administration using 160/180 labeling and the accurate mass and time tag approach. Mol. Cell. Proteomics 2005, 4 (5), 700-9.
    • (2005) Mol. Cell. Proteomics , vol.4 , Issue.5 , pp. 700-709
    • Qian, W.J.1
  • 10
    • 33646264529 scopus 로고    scopus 로고
    • Advances in proteomics data analysis and display using an accurate mass and time tag approach
    • Zimmer, J. S.; et al. Advances in proteomics data analysis and display using an accurate mass and time tag approach. Mass Spectrom. Rev. 2006, 25 (3), 450-82.
    • (2006) Mass Spectrom. Rev , vol.25 , Issue.3 , pp. 450-482
    • Zimmer, J.S.1
  • 11
    • 7044272787 scopus 로고    scopus 로고
    • Potential for false positive identifications from large databases through tandem mass spectrometry
    • Cargile, B. J.; Bundy, J. L.; Stephenson, J. L., Jr. Potential for false positive identifications from large databases through tandem mass spectrometry. J. Proteome Res. 2004, 3 (5), 1082-5.
    • (2004) J. Proteome Res , vol.3 , Issue.5 , pp. 1082-1085
    • Cargile, B.J.1    Bundy, J.L.2    Stephenson Jr., J.L.3
  • 12
    • 1642485152 scopus 로고    scopus 로고
    • Immobilized pH gradients as a first dimension in shotgun proteomics and analysis of the accuracy of pI predictability of peptides
    • Cargile, B. J.; Talley, D. L.; Stephenson, J. L., Jr. Immobilized pH gradients as a first dimension in shotgun proteomics and analysis of the accuracy of pI predictability of peptides. Electrophoresis 2004, 25 (6), 936-45.
    • (2004) Electrophoresis , vol.25 , Issue.6 , pp. 936-945
    • Cargile, B.J.1    Talley, D.L.2    Stephenson Jr., J.L.3
  • 13
    • 1242329500 scopus 로고    scopus 로고
    • Gel based isoelectric focusing of peptides and the utility of isoelectric point in protein identification
    • Cargile, B. J.; et al. Gel based isoelectric focusing of peptides and the utility of isoelectric point in protein identification. J. Proteome Res. 2004, 3 (1), 112-9.
    • (2004) J. Proteome Res , vol.3 , Issue.1 , pp. 112-119
    • Cargile, B.J.1
  • 14
    • 33745857712 scopus 로고    scopus 로고
    • In-gel isoelectric focusing of peptides as a tool for improved protein identification
    • Krijgsveld, J.; et al. In-gel isoelectric focusing of peptides as a tool for improved protein identification. J. Proteome Res. 2006, 5 (7), 1721-30.
    • (2006) J. Proteome Res , vol.5 , Issue.7 , pp. 1721-1730
    • Krijgsveld, J.1
  • 15
    • 28644452554 scopus 로고    scopus 로고
    • A catalogue of human saliva proteins identified by free flow electrophoresis-based peptide separation and tandem mass spectrometry
    • Xie, H.; et al. A catalogue of human saliva proteins identified by free flow electrophoresis-based peptide separation and tandem mass spectrometry. Mol. Cell. Proteomics 2005, 4 (11), 1826-30.
    • (2005) Mol. Cell. Proteomics , vol.4 , Issue.11 , pp. 1826-1830
    • Xie, H.1
  • 16
    • 18844404358 scopus 로고    scopus 로고
    • Evaluating preparative isoelectric focusing of complex peptide mixtures for tandem mass spectrometry-based proteomics: A case study in profiling chromatin-enriched subcellular fractions in Saccharomyces cerevisiae
    • Xie, H.; Bandhakavi, S.; Griffin, T. J. Evaluating preparative isoelectric focusing of complex peptide mixtures for tandem mass spectrometry-based proteomics: a case study in profiling chromatin-enriched subcellular fractions in Saccharomyces cerevisiae. Anal. Chem. 2005, 77 (10), 3198-207.
    • (2005) Anal. Chem , vol.77 , Issue.10 , pp. 3198-3207
    • Xie, H.1    Bandhakavi, S.2    Griffin, T.J.3
  • 17
    • 33645790020 scopus 로고    scopus 로고
    • Trade-off between high sensitivity and increased potential for false positive peptide sequence matches using a two-dimensional linear ion trap for tandem mass spectrometry-based proteomics
    • Xie, H.; Griffin, T. J. Trade-off between high sensitivity and increased potential for false positive peptide sequence matches using a two-dimensional linear ion trap for tandem mass spectrometry-based proteomics. J. Proteome Res. 2006, 5 (4), 1003-9.
    • (2006) J. Proteome Res , vol.5 , Issue.4 , pp. 1003-1009
    • Xie, H.1    Griffin, T.J.2
  • 18
    • 29144449247 scopus 로고    scopus 로고
    • Solution isoelectric focusing for peptide analysis: Comparative investigation of an insoluble nuclear protein fraction
    • An, Y.; et al. Solution isoelectric focusing for peptide analysis: comparative investigation of an insoluble nuclear protein fraction. J. Proteome Res. 2005, 4 (6), 2126-32.
    • (2005) J. Proteome Res , vol.4 , Issue.6 , pp. 2126-2132
    • An, Y.1
  • 19
    • 29144480261 scopus 로고    scopus 로고
    • Added value for tandem mass spectrometry shotgun proteomics data validation through isoelectric focusing of peptides
    • Heller, M.; et al. Added value for tandem mass spectrometry shotgun proteomics data validation through isoelectric focusing of peptides. J. Proteome Res. 2005, 4 (6), 2273-82.
    • (2005) J. Proteome Res , vol.4 , Issue.6 , pp. 2273-2282
    • Heller, M.1
  • 20
    • 33750631580 scopus 로고    scopus 로고
    • Efficient fractionation and improved protein identification by peptide OFFGEL electrophoresis
    • Horth, P.; et al. Efficient fractionation and improved protein identification by peptide OFFGEL electrophoresis. Mol. Cell. Proteomics 2006, 5 (10), 1968-74.
    • (2006) Mol. Cell. Proteomics , vol.5 , Issue.10 , pp. 1968-1974
    • Horth, P.1
  • 21
    • 33646903914 scopus 로고    scopus 로고
    • Savitski, M. M.; Nielsen, M. L.; Zubarev, R. A. ModifiComb, a new proteomic tool for mapping substoichiometric post-translational modifications, finding novel types of modifications, and finger-printing complex protein mixtures. Mol. Cell. Proteomics 2006, 5 (5), 935-48.
    • Savitski, M. M.; Nielsen, M. L.; Zubarev, R. A. ModifiComb, a new proteomic tool for mapping substoichiometric post-translational modifications, finding novel types of modifications, and finger-printing complex protein mixtures. Mol. Cell. Proteomics 2006, 5 (5), 935-48.
  • 22
    • 1042275615 scopus 로고    scopus 로고
    • Modification-specific proteomics: Characterization of post-translational modifications by mass spectrometry
    • Jensen, O. N. Modification-specific proteomics: characterization of post-translational modifications by mass spectrometry. Curr. Opin. Chem. Biol. 2004, 8 (1), 33-41.
    • (2004) Curr. Opin. Chem. Biol , vol.8 , Issue.1 , pp. 33-41
    • Jensen, O.N.1
  • 23
    • 18444391517 scopus 로고    scopus 로고
    • Shotgun identification of protein modifications from protein complexes and lens tissue
    • MacCoss, M. J.; et al. Shotgun identification of protein modifications from protein complexes and lens tissue. Proc. Natl. Acad. Sci. USA. 2002, 99 (12), 7900-5.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.12 , pp. 7900-7905
    • MacCoss, M.J.1
  • 24
    • 0036829396 scopus 로고    scopus 로고
    • Probing lysine acetylation with a modification- specific marker ion using high-performance liquid chromatography/electrospray- mass spectrometry with collision-induced dissociation
    • Kim, J. Y.; et al. Probing lysine acetylation with a modification- specific marker ion using high-performance liquid chromatography/electrospray- mass spectrometry with collision-induced dissociation. Anal. Chem. 2002, 74 (21), 5443-9.
    • (2002) Anal. Chem , vol.74 , Issue.21 , pp. 5443-5449
    • Kim, J.Y.1
  • 25
    • 4344574540 scopus 로고    scopus 로고
    • Large-scale characterization of HeLa cell nuclear phosphoproteins
    • Beausoleil, S. A.; et al. Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc. Natl. Acad. Sci. U.S.A. 2004, 101 (33), 12130-5.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , Issue.33 , pp. 12130-12135
    • Beausoleil, S.A.1
  • 26
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: A regulatory modification to rival phosphorylation?
    • Kouzarides, T. Acetylation: a regulatory modification to rival phosphorylation? EMBO J. 2000, 19 (6), 1176-9.
    • (2000) EMBO J , vol.19 , Issue.6 , pp. 1176-1179
    • Kouzarides, T.1
  • 27
    • 0026425260 scopus 로고
    • Nanoscale packed-capillary liquid chromatography coupled with mass spectrometry using a coaxial continuous-flow fast atom bombardment interface
    • Moseley, M. A.; et al. Nanoscale packed-capillary liquid chromatography coupled with mass spectrometry using a coaxial continuous-flow fast atom bombardment interface. Anal. Chem. 1991, 63 (14), 1467-73.
    • (1991) Anal. Chem , vol.63 , Issue.14 , pp. 1467-1473
    • Moseley, M.A.1
  • 28
    • 0032190378 scopus 로고    scopus 로고
    • Protein identification at the low femtomole level from silver-stained gels using a new fritless electrospray interface for liquid chromatography-microspray and nanospray mass spectrometry
    • Gatlin, C. L.; et al. Protein identification at the low femtomole level from silver-stained gels using a new fritless electrospray interface for liquid chromatography-microspray and nanospray mass spectrometry. Anal. Biochem. 1998, 263 (1), 93-101.
    • (1998) Anal. Biochem , vol.263 , Issue.1 , pp. 93-101
    • Gatlin, C.L.1
  • 29
    • 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., III. 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 (11), 976-89.
    • (1994) J. Am. Soc. Mass Spectrom , vol.5 , Issue.11 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 30
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome
    • Peng, J.; et al. Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: the yeast proteome. J. Proteome Res. 2003, 2 (1), 43-50.
    • (2003) J. Proteome Res , vol.2 , Issue.1 , pp. 43-50
    • Peng, J.1
  • 31
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller, A.; et al. Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal. Chem. 2002, 74 (20), 5383-92.
    • (2002) Anal. Chem , vol.74 , Issue.20 , pp. 5383-5392
    • Keller, A.1
  • 32
    • 0034789979 scopus 로고    scopus 로고
    • Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry
    • Han, D. K.; et al. Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry. Nat. Biotechnol. 2001, 19 (10), 946-51.
    • (2001) Nat. Biotechnol , vol.19 , Issue.10 , pp. 946-951
    • Han, D.K.1
  • 33
    • 0036500203 scopus 로고    scopus 로고
    • Fluorescence-labeled peptide pI markers for capillary isoelectric focusing
    • Shimura, K.; et al. Fluorescence-labeled peptide pI markers for capillary isoelectric focusing. Anal. Chem. 2002, 74 (5), 1046-53.
    • (2002) Anal. Chem , vol.74 , Issue.5 , pp. 1046-1053
    • Shimura, K.1
  • 34
    • 33748320788 scopus 로고    scopus 로고
    • Optimized peptide separation and identification for mass spectrometry based proteomics via free-flow electrophoresis
    • Malmstrom, J.; et al. Optimized peptide separation and identification for mass spectrometry based proteomics via free-flow electrophoresis. J. Proteome Res. 2006, 5 (9), 2241-9.
    • (2006) J. Proteome Res , vol.5 , Issue.9 , pp. 2241-2249
    • Malmstrom, J.1
  • 35
    • 18744375196 scopus 로고    scopus 로고
    • Identifying and quantifying in vivo methylation sites by heavy methyl SILAC
    • Ong, S. E.; Mittler, G.; Mann, M. Identifying and quantifying in vivo methylation sites by heavy methyl SILAC. Nat. Methods 2004, 1 (2), 119-26.
    • (2004) Nat. Methods , vol.1 , Issue.2 , pp. 119-126
    • Ong, S.E.1    Mittler, G.2    Mann, M.3
  • 36
    • 33746992118 scopus 로고    scopus 로고
    • Substrate and functional diversity of lysine acetylation revealed by a proteomics survey
    • Kim, S. C.; et al. Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol. Cell 2006, 23 (4), 607-18.
    • (2006) Mol. Cell , vol.23 , Issue.4 , pp. 607-618
    • Kim, S.C.1


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