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Volumn 13, Issue 8, 2014, Pages 1914-1924

Analytical utility of mass spectral binning in proteomic experiments by SPectral Immonium Ion Detection (SPIID)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLATION; ARTICLE; AUTOANALYSIS; CHEMICAL COMPOSITION; FRAGMENTATION REACTION; HISTOGRAM; MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PROTEOMICS; SPECTRAL IMMONIUM ION DETECTION; SUMOYLATION; TANDEM MASS SPECTROMETRY; UBIQUITINATION; ALGORITHM; CHEMISTRY; COMPUTER PROGRAM; PROCEDURES; PROTEIN DATABASE;

EID: 84905251480     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.O113.035915     Document Type: Article
Times cited : (19)

References (68)
  • 1
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko, A., Tomas, H., Havlis, J., Olsen, J. V., and Mann, M. (2007) In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 1, 2856-2860
    • (2007) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 2
    • 77952956167 scopus 로고    scopus 로고
    • Decoding signalling networks by mass spectrometry-based proteomics
    • Choudhary, C., and Mann, M. (2010) Decoding signalling networks by mass spectrometry-based proteomics. Nat. Rev. Mol. Cell Biol. 11, 427-439
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 427-439
    • Choudhary, C.1    Mann, M.2
  • 3
    • 0022135673 scopus 로고
    • Peptide mixture sequencing by tandem Fourier-transform mass spectrometry
    • Cody, R. B., Amster, I. J., and McLafferty, F. W. (1985) Peptide mixture sequencing by tandem Fourier-transform mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 82, 6367-6370
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 6367-6370
    • Cody, R.B.1    Amster, I.J.2    McLafferty, F.W.3
  • 5
    • 84987419408 scopus 로고
    • Proposal for a common nomenclature for sequence ions in mass spectra of peptides
    • Roepstorff, P., and Fohlman, J. (1984) Proposal for a common nomenclature for sequence ions in mass spectra of peptides. Biomed. Mass Spectrom. 11, 601
    • (1984) Biomed. Mass Spectrom. , vol.11 , pp. 601
    • Roepstorff, P.1    Fohlman, J.2
  • 6
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • DOI 10.1038/nature01511
    • Aebersold, R., and Mann, M. (2003) Mass spectrometry-based proteomics. Nature 422, 198-207 (Pubitemid 36362757)
    • (2003) Nature , vol.422 , Issue.6928 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 7
    • 4444335470 scopus 로고    scopus 로고
    • The ABC's (and XYZ's) of peptide sequencing
    • DOI 10.1038/nrm1468
    • Steen, H., and Mann, M. (2004) The ABC's (and XYZ's) of peptide sequencing. Nat. Rev. Mol. Cell Biol. 5, 699-711 (Pubitemid 39208180)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.9 , pp. 699-711
    • Steen, H.1    Mann, M.2
  • 8
    • 0023386279 scopus 로고
    • INSTRUMENTATION, APPLICATIONS, AND ENERGY DEPOSITION IN QUADRUPOLE ION-TRAP TANDEM MASS SPECTROMETRY
    • Louris, J. N., Cooks, R. G., Syka, J. E. P., Kelley, P. E., Stafford, G. C., and Todd, J. F. J. (1987) Instrumentation, applications, and energy deposition in quadrupole ion-trap tandem mass spectrometry. Anal. Chem. 59, 1677-1685 (Pubitemid 17623527)
    • (1987) Analytical Chemistry , vol.59 , Issue.13 , pp. 1677-1685
    • Todd, J.F.J.1    Stafford Jr., G.C.2    Kelley, P.E.3    Syka, J.E.P.4    Cooks R.Graham5    Louris, J.N.6
  • 9
    • 0023804303 scopus 로고
    • Contributions of mass spectrometry to peptide and protein structure
    • Biemann, K. (1988) Contributions of mass spectrometry to peptide and protein structure. Biomed. Environ. Mass Spectrom. 16, 99-111
    • (1988) Biomed. Environ. Mass Spectrom. , vol.16 , pp. 99-111
    • Biemann, K.1
  • 10
    • 30144438909 scopus 로고    scopus 로고
    • Collision-induced dissociation (CID) of peptides and proteins
    • Wells, J. M., and McLuckey, S. A. (2005) Collision-induced dissociation (CID) of peptides and proteins. Methods Enzymol. 402, 148-185
    • (2005) Methods Enzymol. , vol.402 , pp. 148-185
    • Wells, J.M.1    McLuckey, S.A.2
  • 11
    • 0023449998 scopus 로고
    • Novel fragmentation process of peptides by collision-induced decomposition in a tandem mass spectrometer: Differentiation of leucine and isoleucine
    • Johnson, R. S., Martin, S. A., Biemann, K., Stults, J. T., and Watson, J. T. (1987) Novel fragmentation process of peptides by collision-induced decomposition in a tandem mass spectrometer: differentiation of leucine and isoleucine. Anal. Chem. 59, 2621-2625
    • (1987) Anal. Chem. , vol.59 , pp. 2621-2625
    • Johnson, R.S.1    Martin, S.A.2    Biemann, K.3    Stults, J.T.4    Watson, J.T.5
  • 12
    • 0019796284 scopus 로고
    • Fast-atom-bombardment mass spectra of enkephalins
    • Barber, M., Bordoli, R. S., Garner, G. V., Gordon, D. B., Sedgwick, R. D., Tetler, L. W., and Tyler, A. N. (1981) Fast-atom-bombardment mass spectra of enkephalins. Biochem. J. 197, 401-404 (Pubitemid 11013974)
    • (1981) Biochemical Journal , vol.197 , Issue.2 , pp. 401-404
    • Barber, M.1    Bordoli, R.S.2    Garner, G.V.3
  • 13
    • 84989065211 scopus 로고
    • Fast atom bombardment mass spectrometry of two isomeric tripeptides
    • Barber, M., Bordoli, R. S., Sedgwick, R. D., and Tetler, L. W. (1981) Fast atom bombardment mass spectrometry of two isomeric tripeptides. Organic Mass Spectrom. 16, 256-260
    • (1981) Organic Mass Spectrom. , vol.16 , pp. 256-260
    • Barber, M.1    Bordoli, R.S.2    Sedgwick, R.D.3    Tetler, L.W.4
  • 14
    • 84864592872 scopus 로고    scopus 로고
    • Reduction in database search space by utilization of amino acid composition information from electron transfer dissociation and higher-energy collisional dissociation mass spectra
    • Hansen, T. A., Kryuchkov, F., and Kjeldsen, F. (2012) Reduction in database search space by utilization of amino acid composition information from electron transfer dissociation and higher-energy collisional dissociation mass spectra. Anal. Chem. 84, 6638-6645
    • (2012) Anal. Chem. , vol.84 , pp. 6638-6645
    • Hansen, T.A.1    Kryuchkov, F.2    Kjeldsen, F.3
  • 15
    • 0000183664 scopus 로고
    • Low-mass ions produced from peptides by high-energy collision-induced dissociation in tandem mass spectrometry
    • Falick, A. M., Hines, W. M., Medzihradszky, K. F., Baldwin, M. A., and Gibson, B. W. (1993) Low-mass ions produced from peptides by high-energy collision-induced dissociation in tandem mass spectrometry. J. Am. Soc. Mass Spectrom. 4, 882-893
    • (1993) J. Am. Soc. Mass Spectrom. , vol.4 , pp. 882-893
    • Falick, A.M.1    Hines, W.M.2    Medzihradszky, K.F.3    Baldwin, M.A.4    Gibson, B.W.5
  • 18
    • 0037059770 scopus 로고    scopus 로고
    • Tyrosine phosphorylation mapping of the epidermal growth factor receptor signaling pathway
    • DOI 10.1074/jbc.M109992200
    • Steen, H., Kuster, B., Fernandez, M., Pandey, A., and Mann, M. (2002) Tyrosine phosphorylation mapping of the epidermal growth factor receptor signaling pathway. J. Biol. Chem. 277, 1031-1039 (Pubitemid 34968848)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.2 , pp. 1031-1039
    • Steen, H.1    Kuster, B.2    Fernandez, M.3    Pandey, A.4    Mann, M.5
  • 19
    • 24044553566 scopus 로고    scopus 로고
    • Multiple reaction monitoring to identify sites of protein phosphorylation with high sensitivity
    • DOI 10.1074/mcp.M500113-MCP200
    • Unwin, R. D., Griffiths, J. R., Leverentz, M. K., Grallert, A., Hagan, I. M., and Whetton, A. D. (2005) Multiple reaction monitoring to identify sites of protein phosphorylation with high sensitivity. Mol. Cell. Proteomics 4, 1134-1144 (Pubitemid 41223372)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.8 , pp. 1134-1144
    • Unwin, R.D.1    Griffiths, J.R.2    Leverentz, M.K.3    Grallert, A.4    Hagan, I.M.5    Whetton, A.D.6
  • 23
    • 84861800006 scopus 로고    scopus 로고
    • Optimized fast and sensitive acquisition methods for shotgun proteomics on a quadrupole orbitrap mass spectrometer
    • Kelstrup, C. D., Young, C., Lavallee, R., Nielsen, M. L., and Olsen, J. V. (2012) Optimized fast and sensitive acquisition methods for shotgun proteomics on a quadrupole orbitrap mass spectrometer. J. Proteome Res. 11, 3487-3497
    • (2012) J. Proteome Res. , vol.11 , pp. 3487-3497
    • Kelstrup, C.D.1    Young, C.2    Lavallee, R.3    Nielsen, M.L.4    Olsen, J.V.5
  • 27
    • 34548336772 scopus 로고    scopus 로고
    • Higher-energy C-trap dissociation for peptide modification analysis
    • DOI 10.1038/nmeth1060, PII NMETH1060
    • Olsen, J. V., Macek, B., Lange, O., Makarov, A., Horning, S., and Mann, M. (2007) Higher-energy C-trap dissociation for peptide modification analysis. Nat. Methods 4, 709-712 (Pubitemid 47338163)
    • (2007) Nature Methods , vol.4 , Issue.9 , pp. 709-712
    • Olsen, J.V.1    Macek, B.2    Lange, O.3    Makarov, A.4    Horning, S.5    Mann, M.6
  • 28
    • 0019618203 scopus 로고
    • Sequence analysis of polypeptides by collision activated dissociation on a triple quadrupole mass spectrometer
    • Hunt, D. F., Buko, A. M., Ballard, J. M., Shabanowitz, J., and Giordani, A. B. (1981) Sequence analysis of polypeptides by collision activated dissociation on a triple quadrupole mass spectrometer. Biomed. Mass Spectrom. 8, 397-408
    • (1981) Biomed. Mass Spectrom. , vol.8 , pp. 397-408
    • Hunt, D.F.1    Buko, A.M.2    Ballard, J.M.3    Shabanowitz, J.4    Giordani, A.B.5
  • 30
  • 32
    • 44449108277 scopus 로고    scopus 로고
    • Iodoacetamide-induced artifact mimics ubiquitination in mass spectrometry
    • DOI 10.1038/nmeth0608-459, PII NMETH0608-459
    • Nielsen, M. L., Vermeulen, M., Bonaldi, T., Cox, J., Moroder, L., and Mann, M. (2008) Iodoacetamide-induced artifact mimics ubiquitination in mass spectrometry. Nat. Methods 5, 459-460 (Pubitemid 351761746)
    • (2008) Nature Methods , vol.5 , Issue.6 , pp. 459-460
    • Nielsen, M.L.1    Vermeulen, M.2    Bonaldi, T.3    Cox, J.4    Moroder, L.5    Mann, M.6
  • 33
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • DOI 10.1038/nprot.2007.261, PII NPROT.2007.261
    • Rappsilber, J., Mann, M., and Ishihama, Y. (2007) Protocol for micropurification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat. Protoc. 2, 1896-1906 (Pubitemid 47308128)
    • (2007) Nature Protocols , vol.2 , Issue.8 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 34
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J., and Mann, M. (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367-1372
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 36
    • 3042815334 scopus 로고    scopus 로고
    • Trypsin cleaves exclusively C-terminal to arginine and lysine residues
    • DOI 10.1074/mcp.T400003-MCP200
    • Olsen, J. V., Ong, S. E., and Mann, M. (2004) Trypsin cleaves exclusively C-terminal to arginine and lysine residues. Mol. Cell. Proteomics 3, 608-614 (Pubitemid 38878520)
    • (2004) Molecular and Cellular Proteomics , vol.3 , Issue.6 , pp. 608-614
    • Olsen, J.V.1    Ong, S.-E.2    Mann, M.3
  • 37
    • 67651173106 scopus 로고    scopus 로고
    • Proteomics by mass spectrometry: Approaches, advances, and applications
    • Yates, J. R., Ruse, C. I., and Nakorchevsky, A. (2009) Proteomics by mass spectrometry: approaches, advances, and applications. Annu. Rev. Biomed. Eng. 11, 49-79
    • (2009) Annu. Rev. Biomed. Eng. , vol.11 , pp. 49-79
    • Yates, J.R.1    Ruse, C.I.2    Nakorchevsky, A.3
  • 38
    • 0035298820 scopus 로고    scopus 로고
    • Detection of tyrosine phosphorylated peptides by precursor ion scanning quadrupole TOF mass spectrometry in positive ion mode
    • DOI 10.1021/ac001318c
    • Steen, H., Kuster, B., Fernandez, M., Pandey, A., and Mann, M. (2001) Detection of tyrosine phosphorylated peptides by precursor ion scanning quadrupole TOF mass spectrometry in positive ion mode. Anal. Chem. 73, 1440-1448 (Pubitemid 32896198)
    • (2001) Analytical Chemistry , vol.73 , Issue.7 , pp. 1440-1448
    • Steen, H.1    Kuster, B.2    Fernandez, M.3    Pandey, A.4    Mann, M.5
  • 39
    • 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
    • DOI 10.1021/ac0256080
    • Kim, J. Y., Kim, K. W., Kwon, H. J., Lee, D. W., and Yoo, J. S. (2002) Probing lysine acetylation with a modification-specific marker ion using high-performance liquid chromatography/electrospray-mass spectrometry with collision-induced dissociation. Anal. Chem. 74, 5443-5449 (Pubitemid 35253104)
    • (2002) Analytical Chemistry , vol.74 , Issue.21 , pp. 5443-5449
    • Kim, J.Y.1    Kim, K.W.2    Kwon, H.J.3    Lee, D.W.4    Yoo, J.S.5
  • 40
    • 33846010726 scopus 로고    scopus 로고
    • Extent of modifications in human proteome samples and their effect on dynamic range of analysis in shotgun proteomics
    • DOI 10.1074/mcp.M600248-MCP200
    • Nielsen, M. L., Savitski, M. M., and Zubarev, R. A. (2006) Extent of modifications in human proteome samples and their effect on dynamic range of analysis in shotgun proteomics. Mol. Cell. Proteomics 5, 2384-2391 (Pubitemid 46040642)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.12 , pp. 2384-2391
    • Nielsen, M.L.1    Savitski, M.M.2    Zubarev, R.A.3
  • 41
    • 0942276237 scopus 로고    scopus 로고
    • Differentiation between peptides containing acetylated or tri-methylated lysines by mass spectrometry: An application for determining lysine 9 acetylation and methylation of histone H3
    • DOI 10.1002/pmic.200300503
    • Zhang, K., Yau, P. M., Chandrasekhar, B., New, R., Kondrat, R., Imai, B. S., and Bradbury, M. E. (2004) Differentiation between peptides containing acetylated or tri-methylated lysines by mass spectrometry: an application for determining lysine 9 acetylation and methylation of histone H3. Proteomics 4, 1-10 (Pubitemid 38140869)
    • (2004) Proteomics , vol.4 , Issue.1 , pp. 1-10
    • Zhang, K.1    Yau, P.M.2    Chandrasekhar, B.3    New, R.4    Kondrat, R.5    Imai, B.S.6    Bradbury, M.E.7
  • 42
    • 42949135961 scopus 로고    scopus 로고
    • Utility of immonium ions for assignment of epsilon-N-acetyllysine- containing peptides by tandem mass spectrometry
    • DOI 10.1021/ac800005n
    • Trelle, M. B., and Jensen, O. N. (2008) Utility of immonium ions for assignment of epsilon-N-acetyllysine-containing peptides by tandem mass spectrometry. Anal. Chem. 80, 3422-3430 (Pubitemid 351620730)
    • (2008) Analytical Chemistry , vol.80 , Issue.9 , pp. 3422-3430
    • Trelle, M.B.1    Jensen, O.N.2
  • 43
    • 2342593352 scopus 로고    scopus 로고
    • De novo sequencing, peptide composition analysis, and composition-based sequencing: A new strategy employing accurate mass determination by Fourier transform ion cyclotron resonance mass spectrometry
    • Spengler, B. (2004) De novo sequencing, peptide composition analysis, and composition-based sequencing: a new strategy employing accurate mass determination by Fourier transform ion cyclotron resonance mass spectrometry. J. Am. Soc. Mass Spectrom. 15, 703-714
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 703-714
    • Spengler, B.1
  • 47
    • 80054033461 scopus 로고    scopus 로고
    • A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles
    • M111.013284
    • Wagner, S. A., Beli, P., Weinert, B. T., Nielsen, M. L., Cox, J., Mann, M., and Choudhary, C. (2011) A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Mol. Cell. Proteomics 10, M111.013284
    • (2011) Mol. Cell. Proteomics , vol.10
    • Wagner, S.A.1    Beli, P.2    Weinert, B.T.3    Nielsen, M.L.4    Cox, J.5    Mann, M.6    Choudhary, C.7
  • 48
    • 84875252687 scopus 로고    scopus 로고
    • Advances in characterizing ubiquitylation sites by mass spectrometry
    • Sylvestersen, K. B., Young, C., and Nielsen, M. L. (2013) Advances in characterizing ubiquitylation sites by mass spectrometry. Curr. Opin. Chem. Biol. 17, 49-58
    • (2013) Curr. Opin. Chem. Biol. , vol.17 , pp. 49-58
    • Sylvestersen, K.B.1    Young, C.2    Nielsen, M.L.3
  • 50
    • 39149121854 scopus 로고    scopus 로고
    • epsilon-Formylation of lysine is a widespread post-translational modification of nuclear proteins occurring at residues involved in regulation of chromatin function
    • DOI 10.1093/nar/gkm1057
    • Wisniewski, J. R., Zougman, A., and Mann, M. (2008) Nepsilon-formylation of lysine is a widespread post-translational modification of nuclear proteins occurring at residues involved in regulation of chromatin function. Nucleic Acids Res. 36, 570-577 (Pubitemid 351250448)
    • (2008) Nucleic Acids Research , vol.36 , Issue.2 , pp. 570-577
    • Wisniewski, J.R.1    Zougman, A.2    Mann, M.3
  • 51
    • 79952496201 scopus 로고    scopus 로고
    • Characterization and diagnostic value of amino acid side chain neutral losses following electron-transfer dissociation
    • Xia, Q., Lee, M. V., Rose, C. M., Marsh, A. J., Hubler, S. L., Wenger, C. D., and Coon, J. J. (2011) Characterization and diagnostic value of amino acid side chain neutral losses following electron-transfer dissociation. J. Am. Soc. Mass Spectrom. 22, 255-264
    • (2011) J. Am. Soc. Mass Spectrom. , vol.22 , pp. 255-264
    • Xia, Q.1    Lee, M.V.2    Rose, C.M.3    Marsh, A.J.4    Hubler, S.L.5    Wenger, C.D.6    Coon, J.J.7
  • 52
    • 55549086485 scopus 로고    scopus 로고
    • Analytical utility of small neutral losses from reduced species in electron capture dissociation studied using SwedECD database
    • Falth, M., Savitski, M. M., Nielsen, M. L., Kjeldsen, F., Andren, P. E., and Zubarev, R. A. (2008) Analytical utility of small neutral losses from reduced species in electron capture dissociation studied using SwedECD database. Anal. Chem. 80, 8089-8094
    • (2008) Anal. Chem. , vol.80 , pp. 8089-8094
    • Falth, M.1    Savitski, M.M.2    Nielsen, M.L.3    Kjeldsen, F.4    Andren, P.E.5    Zubarev, R.A.6
  • 53
    • 23044442790 scopus 로고    scopus 로고
    • Investigation of neutral loss during collision-induced dissociation of peptide ions
    • DOI 10.1021/ac050701k
    • Martin, D. B., Eng, J. K., Nesvizhskii, A. I., Gemmill, A., and Aebersold, R. (2005) Investigation of neutral loss during collision-induced dissociation of peptide ions. Anal. Chem. 77, 4870-4882 (Pubitemid 41076678)
    • (2005) Analytical Chemistry , vol.77 , Issue.15 , pp. 4870-4882
    • Martin, D.B.1    Eng, J.K.2    Nesvizhskii, A.I.3    Gemmill, A.4    Aebersold, R.5
  • 54
    • 84868332118 scopus 로고    scopus 로고
    • A systematic investigation into the nature of tryptic HCD spectra
    • Michalski, A., Neuhauser, N., Cox, J., and Mann, M. (2012) A systematic investigation into the nature of tryptic HCD spectra. J. Proteome Res. 11, 5479-5491
    • (2012) J. Proteome Res. , vol.11 , pp. 5479-5491
    • Michalski, A.1    Neuhauser, N.2    Cox, J.3    Mann, M.4
  • 55
    • 33750456519 scopus 로고    scopus 로고
    • Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks
    • DOI 10.1016/j.cell.2006.09.026, PII S0092867406012748
    • Olsen, J. V., Blagoev, B., Gnad, F., Macek, B., Kumar, C., Mortensen, P., and Mann, M. (2006) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127, 635-648 (Pubitemid 44647421)
    • (2006) Cell , vol.127 , Issue.3 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 57
    • 77956326489 scopus 로고    scopus 로고
    • Comprehensive profiling of phosphopeptides based on anion exchange followed by flow-through enrichment with titanium dioxide (AFET)
    • Nie, S., Dai, J., Ning, Z. B., Cao, X. J., Sheng, Q. H., and Zeng, R. (2010) Comprehensive profiling of phosphopeptides based on anion exchange followed by flow-through enrichment with titanium dioxide (AFET). J. Proteome Res. 9, 4585-4594
    • (2010) J. Proteome Res. , vol.9 , pp. 4585-4594
    • Nie, S.1    Dai, J.2    Ning, Z.B.3    Cao, X.J.4    Sheng, Q.H.5    Zeng, R.6
  • 58
    • 79959988139 scopus 로고    scopus 로고
    • Pinpointing phosphorylation sites: Quantitative filtering and a novel site-specific x-ion fragment
    • Kelstrup, C. D., Hekmat, O., Francavilla, C., and Olsen, J. V. (2011) Pinpointing phosphorylation sites: quantitative filtering and a novel site-specific x-ion fragment. J. Proteome Res. 10, 2937-2948
    • (2011) J. Proteome Res. , vol.10 , pp. 2937-2948
    • Kelstrup, C.D.1    Hekmat, O.2    Francavilla, C.3    Olsen, J.V.4
  • 59
    • 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., and Cottrell, J. S. (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567 (Pubitemid 30007252)
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 60
    • 84870721324 scopus 로고    scopus 로고
    • File formats commonly used in mass spectrometry proteomics
    • Deutsch, E. W. (2012) File formats commonly used in mass spectrometry proteomics. Mol. Cell. Proteomics 11, 1612-1621
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 1612-1621
    • Deutsch, E.W.1
  • 61
    • 63049105321 scopus 로고    scopus 로고
    • MassMatrix: A database search program for rapid characterization of proteins and peptides from tandem mass spectrometry data
    • Xu, H., and Freitas, M. A. (2009) MassMatrix: a database search program for rapid characterization of proteins and peptides from tandem mass spectrometry data. Proteomics 9, 1548-1555
    • (2009) Proteomics , vol.9 , pp. 1548-1555
    • Xu, H.1    Freitas, M.A.2
  • 63
    • 84871836266 scopus 로고    scopus 로고
    • Pyteomics - A Python framework for exploratory data analysis and rapid software prototyping in proteomics
    • Goloborodko, A. A., Levitsky, L. I., Ivanov, M. V., and Gorshkov, M. V. (2013) Pyteomics - a Python framework for exploratory data analysis and rapid software prototyping in proteomics. J. Am. Soc. Mass Spectrom. 24, 301-304
    • (2013) J. Am. Soc. Mass Spectrom. , vol.24 , pp. 301-304
    • Goloborodko, A.A.1    Levitsky, L.I.2    Ivanov, M.V.3    Gorshkov, M.V.4
  • 64
    • 54949129419 scopus 로고    scopus 로고
    • ProteoWizard: Open source software for rapid proteomics tools development
    • Kessner, D., Chambers, M., Burke, R., Agus, D., and Mallick, P. (2008) ProteoWizard: open source software for rapid proteomics tools development. Bioinformatics 24, 2534-2536
    • (2008) Bioinformatics , vol.24 , pp. 2534-2536
    • Kessner, D.1    Chambers, M.2    Burke, R.3    Agus, D.4    Mallick, P.5
  • 66
    • 1242339631 scopus 로고    scopus 로고
    • Diagnostic ions for the rapid analysis by nano-electrospray ionization quadrupole time-of-flight mass spectrometry of O-glycans from human mucins
    • Robbe, C., Capon, C., Coddeville, B., and Michalski, J. C. (2004) Diagnostic ions for the rapid analysis by nano-electrospray ionization quadrupole time-of-flight mass spectrometry of O-glycans from human mucins. Rapid Commun. Mass Spectrom. 18, 412-420 (Pubitemid 38235175)
    • (2004) Rapid Communications in Mass Spectrometry , vol.18 , Issue.4 , pp. 412-420
    • Robbe, C.1    Capon, C.2    Coddeville, B.3    Michalski, J.-C.4
  • 67
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • DOI 10.1038/nbt0303-255
    • Mann, M., and Jensen, O. N. (2003) Proteomic analysis of post-translational modifications. Nat. Biotechnol. 21, 255-261 (Pubitemid 36314808)
    • (2003) Nature Biotechnology , vol.21 , Issue.3 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 68
    • 84886246082 scopus 로고    scopus 로고
    • Proteome-wide identification of poly(ADP-ribosyl)ation targets in different genotoxic stress responses
    • Jungmichel, S., Rosenthal, F., Altmeyer, M., Lukas, J., Hottiger, M. O., and Nielsen, M. L. (2013) Proteome-wide identification of poly(ADP-ribosyl)ation targets in different genotoxic stress responses. Mol. Cell 52, 272-285
    • (2013) Mol. Cell , vol.52 , pp. 272-285
    • Jungmichel, S.1    Rosenthal, F.2    Altmeyer, M.3    Lukas, J.4    Hottiger, M.O.5    Nielsen, M.L.6


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