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Volumn 20, Issue 9, 2009, Pages 1652-1659

Comparison of CID Versus ETD Based MS/MS Fragmentation for the Analysis of Protein Ubiquitination

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL METHODS; DERIVED DATA; DNA POLYMERASE; ELECTRON-TRANSFER DISSOCIATION; FRAGMENT IONS; FRAGMENTATION PATTERNS; ISOPEPTIDE BOND; LC-MS/MS; LIQUID CHROMATOGRAPHY-TANDEM MASS SPECTROMETRY; MS/MS FRAGMENTATION; POST-TRANSLATIONAL MODIFICATIONS; PRECURSOR IONS; PROTEIN FUNCTIONS; SIDE CHAINS; UBIQUITINATED PROTEINS; UBIQUITINATION;

EID: 69749124866     PISSN: 10440305     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jasms.2009.04.023     Document Type: Article
Times cited : (68)

References (48)
  • 2
    • 50149086108 scopus 로고    scopus 로고
    • Diversity of degradation signals in the ubiquitin-proteasome system
    • Ravid T., and Hochstrasser M. Diversity of degradation signals in the ubiquitin-proteasome system. Nat. Rev. Mol. Cell. Biol. 9 9 (2008) 679-690
    • (2008) Nat. Rev. Mol. Cell. Biol. , vol.9 , Issue.9 , pp. 679-690
    • Ravid, T.1    Hochstrasser, M.2
  • 3
    • 39049187931 scopus 로고    scopus 로고
    • From loops to chains: Unraveling the mysteries of polyubiquitin chain specificity and processivity
    • Sowa M.E., and Harper J.W. From loops to chains: Unraveling the mysteries of polyubiquitin chain specificity and processivity. ACS Chem. Biol. 1 1 (2006) 20-24
    • (2006) ACS Chem. Biol. , vol.1 , Issue.1 , pp. 20-24
    • Sowa, M.E.1    Harper, J.W.2
  • 5
    • 13444254137 scopus 로고    scopus 로고
    • Proteomic insights into ubiquitin and ubiquitin-like proteins
    • Denison C., Kirkpatrick D.S., and Gygi S.P. Proteomic insights into ubiquitin and ubiquitin-like proteins. Curr. Opin. Chem. Biol. 9 1 (2005) 69-75
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , Issue.1 , pp. 69-75
    • Denison, C.1    Kirkpatrick, D.S.2    Gygi, S.P.3
  • 6
    • 23144452492 scopus 로고    scopus 로고
    • Weighing in on ubiquitin: The expanding role of mass-spectrometry-based proteomics
    • Kirkpatrick D.S., Denison C., and Gygi S.P. Weighing in on ubiquitin: The expanding role of mass-spectrometry-based proteomics. Nat. Cell. Biol. 7 8 (2005) 750-757
    • (2005) Nat. Cell. Biol. , vol.7 , Issue.8 , pp. 750-757
    • Kirkpatrick, D.S.1    Denison, C.2    Gygi, S.P.3
  • 8
    • 42049091467 scopus 로고    scopus 로고
    • Evaluation of proteomic strategies for analyzing ubiquitinated proteins
    • Peng J. Evaluation of proteomic strategies for analyzing ubiquitinated proteins. BMB Rep. 41 3 (2008) 177-183
    • (2008) BMB Rep. , vol.41 , Issue.3 , pp. 177-183
    • Peng, J.1
  • 12
    • 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., and Hunt D.F. Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 101 26 (2004) 9528-9533
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , Issue.26 , pp. 9528-9533
    • Syka, J.E.1    Coon, J.J.2    Schroeder, M.J.3    Shabanowitz, J.4    Hunt, D.F.5
  • 13
    • 58749083921 scopus 로고    scopus 로고
    • Methods for analyzing peptides and proteins on a chromatographic timescale by electron-transfer dissociation mass spectrometry
    • Udeshi N.D., Compton P.D., Shabanowitz J., Hunt D.F., and Rose K.L. Methods for analyzing peptides and proteins on a chromatographic timescale by electron-transfer dissociation mass spectrometry. Nat. Protoc. 3 11 (2008) 1709-1717
    • (2008) Nat. Protoc. , vol.3 , Issue.11 , pp. 1709-1717
    • Udeshi, N.D.1    Compton, P.D.2    Shabanowitz, J.3    Hunt, D.F.4    Rose, K.L.5
  • 14
    • 36749094051 scopus 로고    scopus 로고
    • Analysis of proteins and peptides on a chromatographic timescale by electron-transfer dissociation MS
    • Udeshi N.D., Shabanowitz J., Hunt D.F., and Rose K.L. Analysis of proteins and peptides on a chromatographic timescale by electron-transfer dissociation MS. FEBS J. 274 24 (2007) 6269-6276
    • (2007) FEBS J. , vol.274 , Issue.24 , pp. 6269-6276
    • Udeshi, N.D.1    Shabanowitz, J.2    Hunt, D.F.3    Rose, K.L.4
  • 15
    • 36349016738 scopus 로고    scopus 로고
    • On-line LC-MS approach combining collision-induced dissociation (CID), electron-transfer dissociation (ETD), and CID of an isolated charge-reduced species for the trace-level characterization of proteins with post-translational modifications
    • Wu S.L., Huhmer A.F., Hao Z., and Karger B.L. On-line LC-MS approach combining collision-induced dissociation (CID), electron-transfer dissociation (ETD), and CID of an isolated charge-reduced species for the trace-level characterization of proteins with post-translational modifications. J. Proteome Res. 6 11 (2007) 4230-4244
    • (2007) J. Proteome Res. , vol.6 , Issue.11 , pp. 4230-4244
    • Wu, S.L.1    Huhmer, A.F.2    Hao, Z.3    Karger, B.L.4
  • 16
    • 36749068401 scopus 로고    scopus 로고
    • Performance characteristics of electron transfer dissociation mass spectrometry
    • Good D.M., Wirtala M., McAlister G.C., and Coon J.J. Performance characteristics of electron transfer dissociation mass spectrometry. Mol. Cell. Proteom. 6 11 (2007) 1942-1951
    • (2007) Mol. Cell. Proteom. , vol.6 , Issue.11 , pp. 1942-1951
    • Good, D.M.1    Wirtala, M.2    McAlister, G.C.3    Coon, J.J.4
  • 17
    • 4444335470 scopus 로고    scopus 로고
    • The ABC's (and XYZ's) of peptide sequencing
    • Steen H., and Mann M. The ABC's (and XYZ's) of peptide sequencing. Nat. Rev. Mol. Cell. Biol. 5 9 (2004) 699-711
    • (2004) Nat. Rev. Mol. Cell. Biol. , vol.5 , Issue.9 , pp. 699-711
    • Steen, H.1    Mann, M.2
  • 18
    • 0000944563 scopus 로고    scopus 로고
    • Electron capture dissociation of multiply charged protein cations. A nonergodic process
    • Zubarev R.A., Kelleher N.L., and McLafferty F.W. Electron capture dissociation of multiply charged protein cations. A nonergodic process. J. Am. Chem. Soc. 120 (1998) 3265-3266
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 3265-3266
    • Zubarev, R.A.1    Kelleher, N.L.2    McLafferty, F.W.3
  • 19
    • 53149153136 scopus 로고    scopus 로고
    • The effect of fixed charge modifications on electron capture dissociation
    • Li X., Cournoyer J.J., Lin C., and O'Connor P.B. The effect of fixed charge modifications on electron capture dissociation. J Am. Soc. Mass Spectrom. 19 10 (2008) 1514-1526
    • (2008) J Am. Soc. Mass Spectrom. , vol.19 , Issue.10 , pp. 1514-1526
    • Li, X.1    Cournoyer, J.J.2    Lin, C.3    O'Connor, P.B.4
  • 20
    • 50849120714 scopus 로고    scopus 로고
    • Multiple ion/ion reactions in the 3D ion trap: Selective reagent anion production for ETD and PTR from a single compound
    • Hartmer R., Kaplan D.A., Gebhardt C.R., Ledertheil T., and Brekenfeld A. Multiple ion/ion reactions in the 3D ion trap: Selective reagent anion production for ETD and PTR from a single compound. Int. J. Mass Spectrom. 276 (2008) 82-90
    • (2008) Int. J. Mass Spectrom. , vol.276 , pp. 82-90
    • Hartmer, R.1    Kaplan, D.A.2    Gebhardt, C.R.3    Ledertheil, T.4    Brekenfeld, A.5
  • 22
    • 39549106043 scopus 로고    scopus 로고
    • CHIP-mediated degradation and DNA damage-dependent stabilization regulate base excision repair proteins
    • Parsons J.L., Tait P.S., Finch D., Dianova I.I., Allinson S.L., and Dianov G.L. CHIP-mediated degradation and DNA damage-dependent stabilization regulate base excision repair proteins. Mol. Cell. 29 4 (2008) 477-487
    • (2008) Mol. Cell. , vol.29 , Issue.4 , pp. 477-487
    • Parsons, J.L.1    Tait, P.S.2    Finch, D.3    Dianova, I.I.4    Allinson, S.L.5    Dianov, G.L.6
  • 23
    • 33745914259 scopus 로고    scopus 로고
    • Ultra-fast tandem mass spectrometry scanning combined with monolithic column liquid chromatography increases throughput in proteomic analysis
    • Batycka M., Inglis N.F., Cook K., Adam A., Fraser-Pitt D., Smith D.G., Main L., Lubben A., and Kessler B.M. Ultra-fast tandem mass spectrometry scanning combined with monolithic column liquid chromatography increases throughput in proteomic analysis. Rapid Commun. Mass Spectrom. 20 14 (2006) 2074-2080
    • (2006) Rapid Commun. Mass Spectrom. , vol.20 , Issue.14 , pp. 2074-2080
    • Batycka, M.1    Inglis, N.F.2    Cook, K.3    Adam, A.4    Fraser-Pitt, D.5    Smith, D.G.6    Main, L.7    Lubben, A.8    Kessler, B.M.9
  • 24
    • 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. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20 18 (1999) 3551-3567
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 25
    • 28044461531 scopus 로고    scopus 로고
    • Rules governing protein identification by mass spectrometry
    • Taylor G.K., and Goodlett D.R. Rules governing protein identification by mass spectrometry. Rapid Commun. Mass Spectrom. 19 23 (2005) 3420
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , Issue.23 , pp. 3420
    • Taylor, G.K.1    Goodlett, D.R.2
  • 26
    • 0030863993 scopus 로고    scopus 로고
    • Inhibition of the 26 S proteasome by polyubiquitin chains synthesized to have defined lengths
    • Piotrowski J., Beal R., Hoffman L., Wilkinson K.D., Cohen R.E., and Pickart C.M. Inhibition of the 26 S proteasome by polyubiquitin chains synthesized to have defined lengths. J Biol. Chem. 272 38 (1997) 23712-23721
    • (1997) J Biol. Chem. , vol.272 , Issue.38 , pp. 23712-23721
    • Piotrowski, J.1    Beal, R.2    Hoffman, L.3    Wilkinson, K.D.4    Cohen, R.E.5    Pickart, C.M.6
  • 27
    • 0025617140 scopus 로고
    • Appendix 5. Nomenclature for peptide fragment ions (positive ions)
    • Biemann K. Appendix 5. Nomenclature for peptide fragment ions (positive ions). Methods Enzymol 193 (1990) 886-887
    • (1990) Methods Enzymol , vol.193 , pp. 886-887
    • Biemann, K.1
  • 28
    • 55849104839 scopus 로고    scopus 로고
    • Application of electron transfer dissociation (ETD) for the analysis of posttranslational modifications
    • Wiesner J., Premsler T., and Sickmann A. Application of electron transfer dissociation (ETD) for the analysis of posttranslational modifications. Proteomics 8 21 (2008) 4466-4483
    • (2008) Proteomics , vol.8 , Issue.21 , pp. 4466-4483
    • Wiesner, J.1    Premsler, T.2    Sickmann, A.3
  • 29
    • 0038631820 scopus 로고    scopus 로고
    • Electrospray ionization Fourier transform ion cyclotron resonance mass spectrometric analysis of metal-ion selected dynamic protein libraries
    • Cooper H.J., Case M.A., McLendon G.L., and Marshall A.G. Electrospray ionization Fourier transform ion cyclotron resonance mass spectrometric analysis of metal-ion selected dynamic protein libraries. J. Am. Chem. Soc. 125 18 (2003) 5331-5339
    • (2003) J. Am. Chem. Soc. , vol.125 , Issue.18 , pp. 5331-5339
    • Cooper, H.J.1    Case, M.A.2    McLendon, G.L.3    Marshall, A.G.4
  • 30
    • 69749101222 scopus 로고    scopus 로고
    • Electron capture dissociation in a radio-frequency linear ion trap
    • Baba T., Satake H., Manri N., and Hasegawa H. Electron capture dissociation in a radio-frequency linear ion trap. NanoFrontier NF/TN(E)002 (2009) 1-4
    • (2009) NanoFrontier , vol.NF-TNE002 , pp. 1-4
    • Baba, T.1    Satake, H.2    Manri, N.3    Hasegawa, H.4
  • 31
    • 15444375314 scopus 로고    scopus 로고
    • Electron transfer ion/ion reactions in a three-dimensional quadrupole ion trap: Reactions of doubly and triply protonated peptides with SO2*
    • Pitteri S.J., Chrisman P.A., Hogan J.M., and McLuckey S.A. Electron transfer ion/ion reactions in a three-dimensional quadrupole ion trap: Reactions of doubly and triply protonated peptides with SO2*. Anal. Chem. 77 6 (2005) 1831-1839
    • (2005) Anal. Chem. , vol.77 , Issue.6 , pp. 1831-1839
    • Pitteri, S.J.1    Chrisman, P.A.2    Hogan, J.M.3    McLuckey, S.A.4
  • 36
    • 10044289273 scopus 로고    scopus 로고
    • Identification of sites of ubiquitination in proteins: A Fourier transform ion cyclotron resonance mass spectrometry approach
    • Cooper H.J., Health J.K., Jaffray E., Hay R.T., Lam T.T., and Marshall A.G. Identification of sites of ubiquitination in proteins: A Fourier transform ion cyclotron resonance mass spectrometry approach. Anal. Chem. 76 23 (2004) 6982-6988
    • (2004) Anal. Chem. , vol.76 , Issue.23 , pp. 6982-6988
    • Cooper, H.J.1    Health, J.K.2    Jaffray, E.3    Hay, R.T.4    Lam, T.T.5    Marshall, A.G.6
  • 37
    • 44449108277 scopus 로고    scopus 로고
    • Iodoacetamide-induced artifact mimics ubiquitination in mass spectrometry
    • Nielsen M.L., Vermeulen M., Bonaldi T., Cox J., Moroder L., and Mann M. Iodoacetamide-induced artifact mimics ubiquitination in mass spectrometry. Nat. Methods 5 6 (2008) 459-460
    • (2008) Nat. 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
  • 38
    • 33846269339 scopus 로고    scopus 로고
    • A supplemental activation method for high efficiency electron transfer dissociation of doubly protonated peptide precursors
    • Coon J.J. A supplemental activation method for high efficiency electron transfer dissociation of doubly protonated peptide precursors. Anal. Chem. 79 2 (2007) 477-485
    • (2007) Anal. Chem. , vol.79 , Issue.2 , pp. 477-485
    • Coon, J.J.1
  • 39
    • 0041358793 scopus 로고    scopus 로고
    • OLAV: Towards high-throughput tandem mass spectrometry data identification
    • Colinge J., Masselot A., Giron M., Dessingy T., and Magnin J. OLAV: Towards high-throughput tandem mass spectrometry data identification. Proteomics 3 8 (2003) 1454-1463
    • (2003) Proteomics , vol.3 , Issue.8 , pp. 1454-1463
    • Colinge, J.1    Masselot, A.2    Giron, M.3    Dessingy, T.4    Magnin, J.5
  • 44
    • 42949113985 scopus 로고    scopus 로고
    • Straightforward ladder sequencing of peptides using a Lys-N metalloendopeptidase
    • Taouatas N., Drugan M.M., Heck A.J., and Mohammed S. Straightforward ladder sequencing of peptides using a Lys-N metalloendopeptidase. Nat. Methods 5 5 (2008) 405-407
    • (2008) Nat. Methods , vol.5 , Issue.5 , pp. 405-407
    • Taouatas, N.1    Drugan, M.M.2    Heck, A.J.3    Mohammed, S.4
  • 45
  • 46
    • 42049105662 scopus 로고    scopus 로고
    • Characterization of polyubiquitin chain structure by middle-down mass spectrometry
    • Xu P., and Peng J. Characterization of polyubiquitin chain structure by middle-down mass spectrometry. Anal. Chem. 80 9 (2008) 3438-4344
    • (2008) Anal. Chem. , vol.80 , Issue.9 , pp. 3438-4344
    • Xu, P.1    Peng, J.2
  • 47
    • 33746211620 scopus 로고    scopus 로고
    • Impact of the N-terminal amino acid on targeted protein degradation
    • Meinnel T., Serero A., and Giglione C. Impact of the N-terminal amino acid on targeted protein degradation. Biol. Chem. 387 7 (2006) 839-851
    • (2006) Biol. Chem. , vol.387 , Issue.7 , pp. 839-851
    • Meinnel, T.1    Serero, A.2    Giglione, C.3
  • 48
    • 33947539481 scopus 로고    scopus 로고
    • Autoregulation of an E2 enzyme by ubiquitin-chain assembly on its catalytic residue
    • Ravid T., and Hochstrasser M. Autoregulation of an E2 enzyme by ubiquitin-chain assembly on its catalytic residue. Nat. Cell. Biol. 9 4 (2007) 422-427
    • (2007) Nat. Cell. Biol. , vol.9 , Issue.4 , pp. 422-427
    • Ravid, T.1    Hochstrasser, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.