메뉴 건너뛰기




Volumn 9, Issue 3, 2010, Pages 1323-1329

Value of using multiple proteases for large-scale mass spectrometry-based proteomics

Author keywords

Electron transfer dissociation; Mass spectrometry; Model organisms; Proteomics

Indexed keywords

PROTEINASE; TRYPSIN;

EID: 77949786295     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr900863u     Document Type: Article
Times cited : (373)

References (32)
  • 1
    • 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 (3), 242-247.
    • (2001) Nat. Biotechnol. , vol.19 , Issue.3 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 2
    • 55249096894 scopus 로고    scopus 로고
    • Comprehensive massspectrometry-based proteome quantification of haploid versus diploid yeast
    • de Godoy, L. M. F.; Olsen, J. V.; Cox, J.; Nielsen, M. L.; Hubner, N. C.; Frohlich, F.; Walther, T. C.; Mann, M. Comprehensive massspectrometry-based proteome quantification of haploid versus diploid yeast. Nature 2008, 455 (7217), 1251-1254.
    • (2008) Nature , vol.455 , Issue.7217 , pp. 1251-1254
    • De Godoy, L.M.F.1    Olsen, J.V.2    Cox, J.3    Nielsen, M.L.4    Hubner, N.C.5    Frohlich, F.6    Walther, T.C.7    Mann, M.8
  • 3
    • 33745591083 scopus 로고    scopus 로고
    • Status of complete proteome analysis by mass spectrometry: SILAC labeled yeast as a model system
    • de Godoy, L.; Olsen, J.; de Souza, G.; Li, G.; Mortensen, P.; Mann, M. Status of complete proteome analysis by mass spectrometry: SILAC labeled yeast as a model system. Genome Biol. 2006, 7 (6), R50.
    • (2006) Genome Biol. , vol.7 , Issue.6
    • De Godoy, L.1    Olsen, J.2    De Souza, G.3    Li, G.4    Mortensen, P.5    Mann, M.6
  • 4
    • 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. M.; Elias, J. E.; Thoreen, C. C.; Licklider, L. J.; Gygi, S. P. 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.M.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 5
    • 0029810698 scopus 로고    scopus 로고
    • Influence of peptide composition, gas-phase basicity, and chemical modification on fragmentation efficiency: Evidence for the mobile proton model
    • Dongre, A. R.; Jones, J. L.; Somogyi, A.; Wysocki, V. H. Influence of peptide composition, gas-phase basicity, and chemical modification on fragmentation efficiency: Evidence for the mobile proton model. J. Am. Chem. Soc. 1996, 118 (35), 8365-8374.
    • (1996) J. Am. Chem. Soc. , vol.118 , Issue.35 , pp. 8365-8374
    • Dongre, A.R.1    Jones, J.L.2    Somogyi, A.3    Wysocki, V.H.4
  • 6
    • 20444459841 scopus 로고    scopus 로고
    • Statistical characterization of the charge state and residue dependence of low-energy CID peptide dissociation patterns
    • Huang, Y. Y.; Triscari, J. M.; Tseng, G. C.; Pasa-Tolic, L.; Lipton, M. S.; Smith, R. D.; Wysocki, V. H. Statistical characterization of the charge state and residue dependence of low-energy CID peptide dissociation patterns. Anal. Chem. 2005, 77 (18), 5800-5813.
    • (2005) Anal. Chem. , vol.77 , Issue.18 , pp. 5800-5813
    • Huang, Y.Y.1    Triscari, J.M.2    Tseng, G.C.3    Pasa-Tolic, L.4    Lipton, M.S.5    Smith, R.D.6    Wysocki, V.H.7
  • 7
    • 36749068401 scopus 로고    scopus 로고
    • Performance characteristics of electron transfer dissociation mass spectrometry
    • Good, D. M.; Wirtala, M.; McAlister, G. C.; Coon, J. J. Performance Characteristics of Electron Transfer Dissociation Mass Spectrometry. Mol. Cell. Proteomics 2007, 6 (11), 1942-1951.
    • (2007) Mol. Cell. Proteomics , vol.6 , Issue.11 , pp. 1942-1951
    • Good, D.M.1    Wirtala, M.2    McAlister, G.C.3    Coon, J.J.4
  • 8
    • 56149086397 scopus 로고    scopus 로고
    • Decision tree-driven tandem mass spectrometry for shotgun proteomics
    • Swaney, D. L.; McAlister, G. C.; Coon, J. J. Decision tree-driven tandem mass spectrometry for shotgun proteomics. Nat. Methods 2008, 5 (11), 959-964.
    • (2008) Nat. Methods , vol.5 , Issue.11 , pp. 959-964
    • Swaney, D.L.1    McAlister, G.C.2    Coon, J.J.3
  • 9
    • 0023430927 scopus 로고
    • Internal amino-acid sequence-analysis of proteins separated by one-dimensional or two-dimensional gel-electrophoresis after insitu protease digestion on nitrocellulose
    • Aebersold, R. H.; Leavitt, J.; Saavedra, R. A.; Hood, L. E.; Kent, S. B. H. Internal amino-acid sequence-analysis of proteins separated by one-dimensional or two-dimensional gel-electrophoresis after insitu protease digestion on nitrocellulose. Proc. Natl. Acad. Sci. U.S.A. 1987, 84 (20), 6970-6974.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , Issue.20 , pp. 6970-6974
    • Aebersold, R.H.1    Leavitt, J.2    Saavedra, R.A.3    Hood, L.E.4    Kent, S.B.H.5
  • 12
    • 23744504888 scopus 로고    scopus 로고
    • Mapping of Phosphorylation Sites by a Multi-Protease Approach with Specific Phosphopeptide Enrichment and NanoLC-MS/MS Analysis
    • Schlosser, A.; Vanselow, J. T.; Kramer, A. Mapping of Phosphorylation Sites by a Multi-Protease Approach with Specific Phosphopeptide Enrichment and NanoLC-MS/MS Analysis. Anal. Chem. 2005, 77 (16), 5243-5250.
    • (2005) Anal. Chem. , vol.77 , Issue.16 , pp. 5243-5250
    • Schlosser, A.1    Vanselow, J.T.2    Kramer, A.3
  • 13
    • 58149119846 scopus 로고    scopus 로고
    • Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis
    • Wang, B.; Malik, R.; Nigg, E. A.; KoÌr̂ner, R. Evaluation of the Low-Specificity Protease Elastase for Large-Scale Phosphoproteome Analysis. Anal. Chem. 2008, 80 (24), 9526-9533.
    • (2008) Anal. Chem. , vol.80 , Issue.24 , pp. 9526-9533
    • Wang, B.1    Malik, R.2    Nigg, E.A.3    Koìr̂ner, R.4
  • 14
    • 33748573295 scopus 로고    scopus 로고
    • Enhanced sequence coverage of proteins in human cerebrospinal fluid using multiple enzymatic digestion and linear ion trap LC-MS/MS
    • Biringer, R. G.; Amato, H.; Harrington, M. G.; Fonteh, A. N.; Riggins, J. N.; Huhmer, A. F. R. Enhanced sequence coverage of proteins in human cerebrospinal fluid using multiple enzymatic digestion and linear ion trap LC-MS/MS. Brief Funct. Genomic Proteomic 2006, 5 (2), 144-153.
    • (2006) Brief Funct. Genomic Proteomic , vol.5 , Issue.2 , pp. 144-153
    • Biringer, R.G.1    Amato, H.2    Harrington, M.G.3    Fonteh, A.N.4    Riggins, J.N.5    Huhmer, A.F.R.6
  • 15
    • 0037274605 scopus 로고    scopus 로고
    • Multiple enzymatic digestion for enhanced sequence coverage of proteins in complex proteomic mixtures using capillary LC with ion trap MS/MS
    • Choudhary, G.; Wu, S.-L.; Shieh, P.; Hancock, W. S. Multiple Enzymatic Digestion for Enhanced Sequence Coverage of Proteins in Complex Proteomic Mixtures Using Capillary LC with Ion Trap MS/MS. J. Proteome Res. 2003, 2 (1), 59-67.
    • (2003) J. Proteome Res. , vol.2 , Issue.1 , pp. 59-67
    • Choudhary, G.1    Wu, S.-L.2    Shieh, P.3    Hancock, W.S.4
  • 17
    • 0242653718 scopus 로고    scopus 로고
    • Mining a tandem mass spectrometry database to determine the trends and global factors influencing peptide fragmentation
    • Kapp, E. A.; Schutz, F.; Reid, G. E.; Eddes, J. S.; Moritz, R. L.; O'Hair, R. A. J.; Speed, T. P.; Simpson, R. J. Mining a tandem mass spectrometry database to determine the trends and global factors influencing peptide fragmentation. Anal. Chem. 2003, 75 (22), 6251-6264.
    • (2003) Anal. Chem. , vol.75 , Issue.22 , pp. 6251-6264
    • Kapp, E.A.1    Schutz, F.2    Reid, G.E.3    Eddes, J.S.4    Moritz, R.L.5    O'hair, R.A.J.6    Speed, T.P.7    Simpson, R.J.8
  • 18
    • 3042789073 scopus 로고    scopus 로고
    • Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
    • Syka, J. E. P.; 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 (26), 9528-9533.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , Issue.26 , pp. 9528-9533
    • Syka, J.E.P.1    Coon, J.J.2    Schroeder, M.J.3    Shabanowitz, J.4    Hunt, D.F.5
  • 19
    • 0000944563 scopus 로고    scopus 로고
    • Electron capture dissociation of multiply charged protein cations. A nonergodic process
    • Zubarev, R. A.; Kelleher, N. L.; McLafferty, F. W. Electron capture dissociation of multiply charged protein cations. A nonergodic process. J. Am. Chem. Soc. 1998, 120 (13), 3265-3266.
    • (1998) J. Am. Chem. Soc. , vol.120 , Issue.13 , pp. 3265-3266
    • Zubarev, R.A.1    Kelleher, N.L.2    McLafferty, F.W.3
  • 21
    • 66149091950 scopus 로고    scopus 로고
    • Improved electrospray ionization efficiency compensates for diminished chromatographic resolution and enables proteomics analysis of tyrosine signaling in embryonic stem cells
    • Ficarro, S. B.; Zhang, Y.; Lu, Y.; Moghimi, A. R.; Askenazi, M.; Hyatt, E.; Smith, E. D.; Boyer, L.; Schlaeger, T. M.; Luckey, C. J.; Marto, J. A. Improved Electrospray Ionization Efficiency Compensates for Diminished Chromatographic Resolution and Enables Proteomics Analysis of Tyrosine Signaling in Embryonic Stem Cells. Anal. Chem. 2009, 81 (9), 3440-3447.
    • (2009) Anal. Chem. , vol.81 , Issue.9 , pp. 3440-3447
    • Ficarro, S.B.1    Zhang, Y.2    Lu, Y.3    Moghimi, A.R.4    Askenazi, M.5    Hyatt, E.6    Smith, E.D.7    Boyer, L.8    Schlaeger, T.M.9    Luckey, C.J.10    Marto, J.A.11
  • 23
    • 34249022000 scopus 로고    scopus 로고
    • Implementation of electron-transfer dissociation on a hybrid linear ion trap-orbitrap mass spectrometer
    • McAlister, G. C.; Phanstiel, D.; Good, D. M.; Berggren, W. T.; Coon, J. J. Implementation of electron-transfer dissociation on a hybrid linear ion trap-orbitrap mass spectrometer. Anal. Chem. 2007, 79 (10), 3525-3534.
    • (2007) Anal. Chem. , vol.79 , Issue.10 , pp. 3525-3534
    • McAlister, G.C.1    Phanstiel, D.2    Good, D.M.3    Berggren, W.T.4    Coon, J.J.5
  • 25
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias, J. E.; Gygi, S. P. Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat. Methods 2007, 4 (3), 207-214.
    • (2007) Nat. Methods , vol.4 , Issue.3 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 27
    • 27644555055 scopus 로고    scopus 로고
    • Interpretation of shotgun proteomic data: The protein inference problem
    • Nesvizhskii, A. I.; Aebersold, R. Interpretation of Shotgun Proteomic Data: The Protein Inference Problem. Mol. Cell. Proteomics 2005, 4 (10), 1419-1440.
    • (2005) Mol. Cell. Proteomics , vol.4 , Issue.10 , pp. 1419-1440
    • Nesvizhskii, A.I.1    Aebersold, R.2
  • 31
    • 66349106471 scopus 로고    scopus 로고
    • Lys-N and Trypsin Cover Complementary Parts of the Phosphoproteome in a Refined SCX-Based Approach
    • Gauci, S.; Helbig, A. O.; Slijper, M.; Krijgsveld, J.; Heck, A. J. R.; Mohammed, S. Lys-N and Trypsin Cover Complementary Parts of the Phosphoproteome in a Refined SCX-Based Approach. Anal. Chem. 2009, 81 (11), 4493-4501.
    • (2009) Anal. Chem. , vol.81 , Issue.11 , pp. 4493-4501
    • Gauci, S.1    Helbig, A.O.2    Slijper, M.3    Krijgsveld, J.4    Heck, A.J.R.5    Mohammed, S.6
  • 32
    • 33847782587 scopus 로고    scopus 로고
    • Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry
    • Molina, H.; Horn, D. M.; Tang, N.; Mathivanan, S.; Pandey, A. Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 2007, 104 (7), 2199-2204.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , Issue.7 , pp. 2199-2204
    • Molina, H.1    Horn, D.M.2    Tang, N.3    Mathivanan, S.4    Pandey, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.