메뉴 건너뛰기




Volumn 73, Issue 11, 2010, Pages 2092-2123

A survey of computational methods and error rate estimation procedures for peptide and protein identification in shotgun proteomics

Author keywords

Bioinformatics; False discovery rates; Mass spectrometry; Peptide identification; Protein inference; Proteomics; Statistical models

Indexed keywords

PEPTIDE;

EID: 77957221582     PISSN: 18743919     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jprot.2010.08.009     Document Type: Review
Times cited : (442)

References (289)
  • 1
    • 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
  • 2
    • 77957233015 scopus 로고    scopus 로고
    • Yeast Proteomics and Protein Microarrays. J Proteomics
    • Chen R, Snyder M. Yeast Proteomics and Protein Microarrays. J Proteomics 73 (11): 2147-2157.
    • , vol.73 , Issue.11 , pp. 2147-2157
    • Chen, R.1    Snyder, M.2
  • 3
    • 35848970747 scopus 로고    scopus 로고
    • Mapping protein post-translational modifications with mass spectrometry
    • Witze E.S., Old W.M., Resing K.A., Ahn N.G. Mapping protein post-translational modifications with mass spectrometry. Nat Meth 2007, 4:798-806.
    • (2007) Nat Meth , vol.4 , pp. 798-806
    • Witze, E.S.1    Old, W.M.2    Resing, K.A.3    Ahn, N.G.4
  • 4
    • 68949206409 scopus 로고    scopus 로고
    • Applying mass spectrometry-based proteomics to genetics, genomics and network biology
    • Gstaiger M., Aebersold R. Applying mass spectrometry-based proteomics to genetics, genomics and network biology. Nat Rev Genet 2009, 10:617-627.
    • (2009) Nat Rev Genet , vol.10 , pp. 617-627
    • Gstaiger, M.1    Aebersold, R.2
  • 5
    • 55249096894 scopus 로고    scopus 로고
    • Comprehensive mass-spectrometry-based proteome quantification of haploid versus diploid yeast
    • 1251-U60
    • de Godoy L.M.F., Olsen J.V., Cox J., Nielsen M.L., Hubner N.C., Frohlich F., et al. Comprehensive mass-spectrometry-based proteome quantification of haploid versus diploid yeast. Nature 2008, 455. 1251-U60.
    • (2008) Nature , vol.455
    • de Godoy, L.M.F.1    Olsen, J.V.2    Cox, J.3    Nielsen, M.L.4    Hubner, N.C.5    Frohlich, F.6
  • 6
    • 4644335402 scopus 로고    scopus 로고
    • Systems biology, proteomics, and the future of health care: toward predictive, preventative, and personalized medicine
    • Weston A.D., Hood L. Systems biology, proteomics, and the future of health care: toward predictive, preventative, and personalized medicine. J Proteome Res 2004, 3:179-196.
    • (2004) J Proteome Res , vol.3 , pp. 179-196
    • Weston, A.D.1    Hood, L.2
  • 7
    • 70350217754 scopus 로고    scopus 로고
    • Proteomics data repositories
    • Riffle M., Eng J.K. Proteomics data repositories. Proteomics 2009, 9:4653-4663.
    • (2009) Proteomics , vol.9 , pp. 4653-4663
    • Riffle, M.1    Eng, J.K.2
  • 8
    • 1042266254 scopus 로고    scopus 로고
    • Analysis, statistical validation and dissemination of large-scale proteomics datasets generated by tandem MS
    • Nesvizhskii A.I., Aebersold R. Analysis, statistical validation and dissemination of large-scale proteomics datasets generated by tandem MS. Drug Discov Today 2004, 9:173-181.
    • (2004) Drug Discov Today , vol.9 , pp. 173-181
    • Nesvizhskii, A.I.1    Aebersold, R.2
  • 10
    • 2542640024 scopus 로고    scopus 로고
    • Protein identification by mass spectrometry - issues to be considered
    • Baldwin M.A. Protein identification by mass spectrometry - issues to be considered. Mol Cell Proteomics 2004, 3:1-9.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 1-9
    • Baldwin, M.A.1
  • 11
    • 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, 5:1093-1099.
    • (2006) J Proteome Res , vol.5 , pp. 1093-1099
    • Xie, H.1    Griffin, T.J.2
  • 12
    • 33644864034 scopus 로고    scopus 로고
    • Challenges in deriving high-confidence protein identifications from data gathered by a HUPO plasma proteome collaborative study
    • States D.J., Omenn G.S., Blackwell T.W., Fermin D., Eng J., Speicher D.W., et al. Challenges in deriving high-confidence protein identifications from data gathered by a HUPO plasma proteome collaborative study. Nat Biotechnol 2006, 24:333-338.
    • (2006) Nat Biotechnol , vol.24 , pp. 333-338
    • States, D.J.1    Omenn, G.S.2    Blackwell, T.W.3    Fermin, D.4    Eng, J.5    Speicher, D.W.6
  • 13
    • 0037434977 scopus 로고    scopus 로고
    • Biomedical informatics for proteomics
    • Boguski M.S., McIntosh M.W. Biomedical informatics for proteomics. Nature 2003, 422:233-237.
    • (2003) Nature , vol.422 , pp. 233-237
    • Boguski, M.S.1    McIntosh, M.W.2
  • 14
    • 0037338297 scopus 로고    scopus 로고
    • Data analysis - the Achilles heel of proteomics
    • Patterson S.D. Data analysis - the Achilles heel of proteomics. Nat Biotechnol 2003, 21:221-222.
    • (2003) Nat Biotechnol , vol.21 , pp. 221-222
    • Patterson, S.D.1
  • 15
    • 3042735127 scopus 로고    scopus 로고
    • The need for guidelines in publication of peptide and protein identification data: working group on publication guidelines for peptide and protein identification data
    • Carr S., Aebersold R., Baldwin M., Burlingame A., Clauser K., Nesvizhskii A. The need for guidelines in publication of peptide and protein identification data: working group on publication guidelines for peptide and protein identification data. Mol Cell Proteomics 2004, 3:531-533.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 531-533
    • Carr, S.1    Aebersold, R.2    Baldwin, M.3    Burlingame, A.4    Clauser, K.5    Nesvizhskii, A.6
  • 16
    • 4444335470 scopus 로고    scopus 로고
    • The ABC's (and XYZ's) of peptide sequencing
    • Steen H., Mann M. The ABC's (and XYZ's) of peptide sequencing. Nat Rev Mol Cell Biol 2004, 5:699-711.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 699-711
    • Steen, H.1    Mann, M.2
  • 17
    • 34447313945 scopus 로고    scopus 로고
    • How do shotgun proteomics algorithms identify proteins?
    • Marcotte E.M. How do shotgun proteomics algorithms identify proteins?. Nat Biotechnol 2007, 25:755-757.
    • (2007) Nat Biotechnol , vol.25 , pp. 755-757
    • Marcotte, E.M.1
  • 18
    • 67651173106 scopus 로고    scopus 로고
    • Proteomics by mass spectrometry: approaches, advances, and applications
    • Yates J.R., Ruse C.I., Nakorchevsky A. Proteomics by mass spectrometry: approaches, advances, and applications. Annu Rev Biomed Eng 2009, 11:49-79.
    • (2009) Annu Rev Biomed Eng , vol.11 , pp. 49-79
    • Yates, J.R.1    Ruse, C.I.2    Nakorchevsky, A.3
  • 19
    • 33750594230 scopus 로고    scopus 로고
    • Chemistry meets proteomics: the use of chemical tagging reactions for MS-based proteomics
    • Leitner A., Lindner W. Chemistry meets proteomics: the use of chemical tagging reactions for MS-based proteomics. Proteomics 2006, 6:5418-5434.
    • (2006) Proteomics , vol.6 , pp. 5418-5434
    • Leitner, A.1    Lindner, W.2
  • 21
    • 39049175370 scopus 로고    scopus 로고
    • Protein identification by tandem mass spectrometry and sequence database searching
    • Nesvizhskii A.I. Protein identification by tandem mass spectrometry and sequence database searching. Meth Mol Biol 2007, 367:87-119.
    • (2007) Meth Mol Biol , vol.367 , pp. 87-119
    • Nesvizhskii, A.I.1
  • 22
    • 23944451618 scopus 로고    scopus 로고
    • An evaluation, comparison, and accurate benchmarking of several publicly available MS/MS search algorithms: sensitivity and specificity analysis
    • Kapp E.A., Schutz F., Connolly L.M., Chakel J.A., Meza J.E., Miller C.A., et al. An evaluation, comparison, and accurate benchmarking of several publicly available MS/MS search algorithms: sensitivity and specificity analysis. Proteomics 2005, 5:3475-3490.
    • (2005) Proteomics , vol.5 , pp. 3475-3490
    • Kapp, E.A.1    Schutz, F.2    Connolly, L.M.3    Chakel, J.A.4    Meza, J.E.5    Miller, C.A.6
  • 23
    • 24044513966 scopus 로고    scopus 로고
    • Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations
    • Elias J.E., Haas W., Faherty B.K., Gygi S.P. Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations. Nat Meth 2005, 2:667-675.
    • (2005) Nat Meth , vol.2 , pp. 667-675
    • Elias, J.E.1    Haas, W.2    Faherty, B.K.3    Gygi, S.P.4
  • 24
    • 69749114144 scopus 로고    scopus 로고
    • Evaluation of several MS/MS search algorithms for analysis of spectra derived from electron transfer dissociation experiments
    • Kandasamy K., Pandey A., Molina H. Evaluation of several MS/MS search algorithms for analysis of spectra derived from electron transfer dissociation experiments. Anal Chem 2009, 81:7170-7180.
    • (2009) Anal Chem , vol.81 , pp. 7170-7180
    • Kandasamy, K.1    Pandey, A.2    Molina, H.3
  • 25
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller A., Nesvizhskii A.I., Kolker E., Aebersold R. Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal Chem 2002, 74:5383-5392.
    • (2002) Anal Chem , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 26
    • 10044248655 scopus 로고    scopus 로고
    • Statistical model for large-scale peptide identification in databases from tandem mass spectra using SEQUEST
    • Lopez-Ferrer D., Martinez-Bartolome S., Villar M., Campillos M., Martin-Maroto F., Vazquez J. Statistical model for large-scale peptide identification in databases from tandem mass spectra using SEQUEST. Anal Chem 2004, 76:6853-6860.
    • (2004) Anal Chem , vol.76 , pp. 6853-6860
    • Lopez-Ferrer, D.1    Martinez-Bartolome, S.2    Villar, M.3    Campillos, M.4    Martin-Maroto, F.5    Vazquez, J.6
  • 27
    • 0042972838 scopus 로고    scopus 로고
    • A new algorithm for the evaluation of shotgun peptide sequencing in proteomics: support vector machine classification of peptide MS/MS spectra and SEQUEST scores
    • Anderson D.C., Li W.Q., Payan D.G., Noble W.S. A new algorithm for the evaluation of shotgun peptide sequencing in proteomics: support vector machine classification of peptide MS/MS spectra and SEQUEST scores. J Proteome Res 2003, 2:137-146.
    • (2003) J Proteome Res , vol.2 , pp. 137-146
    • Anderson, D.C.1    Li, W.Q.2    Payan, D.G.3    Noble, W.S.4
  • 29
    • 33645467062 scopus 로고    scopus 로고
    • Improved classification of mass spectrometry database search results using newer machine learning approaches
    • Ulintz P.J., Zhu J., Qin Z.H.S., Andrews P.C. Improved classification of mass spectrometry database search results using newer machine learning approaches. Mol Cell Proteomics 2006, 5:497-509.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 497-509
    • Ulintz, P.J.1    Zhu, J.2    Qin, Z.H.S.3    Andrews, P.C.4
  • 30
    • 67149093415 scopus 로고    scopus 로고
    • A new probabilistic database search algorithm for ETD spectra
    • Sadygov R.G., Good D.M., Swaney D.L., Coon J.J. A new probabilistic database search algorithm for ETD spectra. J Proteome Res 2009, 8:3198-3205.
    • (2009) J Proteome Res , vol.8 , pp. 3198-3205
    • Sadygov, R.G.1    Good, D.M.2    Swaney, D.L.3    Coon, J.J.4
  • 31
    • 53049084796 scopus 로고    scopus 로고
    • Phosphorylation-specific MS/MS scoring for rapid and accurate phosphoproteome analysis
    • Payne S.H., Yau M., Smolka M.B., Tanner S., Zhou H.L., Bafna V. Phosphorylation-specific MS/MS scoring for rapid and accurate phosphoproteome analysis. J Proteome Res 2008, 7:3373-3381.
    • (2008) J Proteome Res , vol.7 , pp. 3373-3381
    • Payne, S.H.1    Yau, M.2    Smolka, M.B.3    Tanner, S.4    Zhou, H.L.5    Bafna, V.6
  • 32
    • 77956545752 scopus 로고    scopus 로고
    • Improving software performance for peptide ETD data analysis by implementation of charge-state and sequence-dependent scoring. Mol Cell Proteomics
    • Baker PR, Medzihradszky KF, Chalkley RJ. Improving software performance for peptide ETD data analysis by implementation of charge-state and sequence-dependent scoring. Mol Cell Proteomics 2010;9:1795-803.
    • (2010) , vol.9 , pp. 1795-803
    • Baker, P.R.1    Medzihradszky, K.F.2    Chalkley, R.J.3
  • 33
    • 0742305695 scopus 로고    scopus 로고
    • Intensity-based protein identification by machine learning from a library of tandem mass spectra
    • Elias J.E., Gibbons F.D., King O.D., Roth F.P., Gygi S.P. Intensity-based protein identification by machine learning from a library of tandem mass spectra. Nat Biotechnol 2004, 22:214-219.
    • (2004) Nat Biotechnol , vol.22 , pp. 214-219
    • Elias, J.E.1    Gibbons, F.D.2    King, O.D.3    Roth, F.P.4    Gygi, S.P.5
  • 34
    • 0037317111 scopus 로고    scopus 로고
    • Intensity-based statistical scorer for tandem mass spectrometry
    • Havilio M., Haddad Y., Smilansky Z. Intensity-based statistical scorer for tandem mass spectrometry. Anal Chem 2003, 75:435-444.
    • (2003) Anal Chem , vol.75 , pp. 435-444
    • Havilio, M.1    Haddad, Y.2    Smilansky, Z.3
  • 35
    • 51249111303 scopus 로고    scopus 로고
    • A machine learning approach to explore the spectra intensity pattern of peptides using tandem mass spectrometry data
    • Zhou C., Bowler L.D., Feng J.F. A machine learning approach to explore the spectra intensity pattern of peptides using tandem mass spectrometry data. BMC Bioinform 2008, 9:325.
    • (2008) BMC Bioinform , vol.9 , pp. 325
    • Zhou, C.1    Bowler, L.D.2    Feng, J.F.3
  • 36
    • 66749129629 scopus 로고    scopus 로고
    • A ranking-based scoring function for peptide-spectrum matches
    • Frank A.M. A ranking-based scoring function for peptide-spectrum matches. J Proteome Res 2009, 8:2241-2252.
    • (2009) J Proteome Res , vol.8 , pp. 2241-2252
    • Frank, A.M.1
  • 37
    • 66749169317 scopus 로고    scopus 로고
    • Predicting intensity ranks of peptide fragment ions
    • Frank A.M. Predicting intensity ranks of peptide fragment ions. J Proteome Res 2009, 8:2226-2240.
    • (2009) J Proteome Res , vol.8 , pp. 2226-2240
    • Frank, A.M.1
  • 38
    • 46249088907 scopus 로고    scopus 로고
    • Modeling peptide fragmentation with dynamic Bayesian networks for peptide identification
    • Klammer A.A., Reynolds S.M., Bilmes J.A., MacCoss M.J., Noble W.S. Modeling peptide fragmentation with dynamic Bayesian networks for peptide identification. Bioinformatics 2008, 24:I348-I356.
    • (2008) Bioinformatics , vol.24
    • Klammer, A.A.1    Reynolds, S.M.2    Bilmes, J.A.3    MacCoss, M.J.4    Noble, W.S.5
  • 40
    • 77749305060 scopus 로고    scopus 로고
    • Prediction of electron-transfer/capture dissociation spectra of peptides
    • Zhang Z.Q. Prediction of electron-transfer/capture dissociation spectra of peptides. Anal Chem 2010, 82:1990-2005.
    • (2010) Anal Chem , vol.82 , pp. 1990-2005
    • Zhang, Z.Q.1
  • 41
    • 63049138916 scopus 로고    scopus 로고
    • Database searching and accounting of multiplexed precursor and product ion spectra from the data independent analysis of simple and complex peptide mixtures
    • Li G.Z., Vissers J.P.C., Silva J.C., Golick D., Gorenstein M.V., Geromanos S.J. Database searching and accounting of multiplexed precursor and product ion spectra from the data independent analysis of simple and complex peptide mixtures. Proteomics 2009, 9:1696-1719.
    • (2009) Proteomics , vol.9 , pp. 1696-1719
    • Li, G.Z.1    Vissers, J.P.C.2    Silva, J.C.3    Golick, D.4    Gorenstein, M.V.5    Geromanos, S.J.6
  • 42
    • 77649240336 scopus 로고    scopus 로고
    • Speeding up tandem mass spectrometry based database searching by peptide and spectrum indexing
    • Li Y., Chi H., Wang L.H., Wang H.P., Fu Y., Yuan Z.F., et al. Speeding up tandem mass spectrometry based database searching by peptide and spectrum indexing. Rapid Commun Mass Spectrom 2010, 24:807-814.
    • (2010) Rapid Commun Mass Spectrom , vol.24 , pp. 807-814
    • Li, Y.1    Chi, H.2    Wang, L.H.3    Wang, H.P.4    Fu, Y.5    Yuan, Z.F.6
  • 43
  • 44
    • 33749843580 scopus 로고    scopus 로고
    • IndexToolkit: an open source toolbox to index protein databases for high-throughput proteomics
    • Li D.Q., Gao W., Ling C.X., Wang X.B., Sun R.X., He S.M. IndexToolkit: an open source toolbox to index protein databases for high-throughput proteomics. Bioinformatics 2006, 22:2572-2573.
    • (2006) Bioinformatics , vol.22 , pp. 2572-2573
    • Li, D.Q.1    Gao, W.2    Ling, C.X.3    Wang, X.B.4    Sun, R.X.5    He, S.M.6
  • 46
    • 36448936713 scopus 로고    scopus 로고
    • PepSplice: cache-efficient search algorithms for comprehensive identification of tandem mass spectra
    • Roos F.F., Jacob R., Grossmann J., Fischer B., Buhmann J.M., Gruissem W., et al. PepSplice: cache-efficient search algorithms for comprehensive identification of tandem mass spectra. Bioinformatics 2007, 23:3016-3023.
    • (2007) Bioinformatics , vol.23 , pp. 3016-3023
    • Roos, F.F.1    Jacob, R.2    Grossmann, J.3    Fischer, B.4    Buhmann, J.M.5    Gruissem, W.6
  • 47
    • 34047125445 scopus 로고    scopus 로고
    • Speeding up tandem mass spectrometry database search: metric embeddings and fast near neighbor search
    • Dutta D., Chen T. Speeding up tandem mass spectrometry database search: metric embeddings and fast near neighbor search. Bioinformatics 2007, 23:612-618.
    • (2007) Bioinformatics , vol.23 , pp. 612-618
    • Dutta, D.1    Chen, T.2
  • 48
  • 49
    • 67049134015 scopus 로고    scopus 로고
    • Low cost, scalable proteomics data analysis using Amazon's cloud computing services and open source search algorithms
    • Halligan B.D., Geiger J.F., Vallejos A.K., Greene A.S., Twigger S.N. Low cost, scalable proteomics data analysis using Amazon's cloud computing services and open source search algorithms. J Proteome Res 2009, 8:3148-3153.
    • (2009) J Proteome Res , vol.8 , pp. 3148-3153
    • Halligan, B.D.1    Geiger, J.F.2    Vallejos, A.K.3    Greene, A.S.4    Twigger, S.N.5
  • 50
    • 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, 4:1419-1440.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1419-1440
    • Nesvizhskii, A.I.1    Aebersold, R.2
  • 51
    • 33645708138 scopus 로고    scopus 로고
    • Dynamic spectrum quality assessment and iterative computational analysis of shotgun proteomic data: toward more efficient identification of post-translational modifications, sequence polymorphisms, and novel peptides
    • Nesvizhskii A.I., Roos F.F., Grossmann J., Vogelzang M., Eddes J.S., Gruissem W., et al. Dynamic spectrum quality assessment and iterative computational analysis of shotgun proteomic data: toward more efficient identification of post-translational modifications, sequence polymorphisms, and novel peptides. Mol Cell Proteomics 2006, 5:652-670.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 652-670
    • Nesvizhskii, A.I.1    Roos, F.F.2    Grossmann, J.3    Vogelzang, M.4    Eddes, J.S.5    Gruissem, W.6
  • 52
    • 0035346719 scopus 로고    scopus 로고
    • Interrogating the human genome using uninterpreted mass spectrometry data
    • Choudhary J.S., Blackstock W.P., Creasy D.M., Cottrell J.S. Interrogating the human genome using uninterpreted mass spectrometry data. Proteomics 2001, 1:651-667.
    • (2001) Proteomics , vol.1 , pp. 651-667
    • Choudhary, J.S.1    Blackstock, W.P.2    Creasy, D.M.3    Cottrell, J.S.4
  • 53
    • 14844329057 scopus 로고    scopus 로고
    • Experiments in searching small proteins in unannotated large eukaryotic genomes
    • Colinge J., Cusin I., Reffas S., Mahe E., Niknejad A., Rey P.-A., et al. Experiments in searching small proteins in unannotated large eukaryotic genomes. J Proteome Res 2005, 4:167-174.
    • (2005) J Proteome Res , vol.4 , pp. 167-174
    • Colinge, J.1    Cusin, I.2    Reffas, S.3    Mahe, E.4    Niknejad, A.5    Rey, P.-A.6
  • 54
    • 34247254351 scopus 로고    scopus 로고
    • Novel peptide identification from tandem mass spectra using ESTs and sequence database compression
    • Edwards N.J. Novel peptide identification from tandem mass spectra using ESTs and sequence database compression. Mol Syst Biol 2007, 3:102.
    • (2007) Mol Syst Biol , vol.3 , pp. 102
    • Edwards, N.J.1
  • 55
    • 20144381803 scopus 로고    scopus 로고
    • Integration with the human genome of peptide sequences obtained by high-throughput mass spectrometry
    • Desiere F., Deutsch E.W., Nesvizhskii A.I., Mallick P., King N.L., Eng J.K., et al. Integration with the human genome of peptide sequences obtained by high-throughput mass spectrometry. Genome Biol 2005, 6:R9.
    • (2005) Genome Biol , vol.6
    • Desiere, F.1    Deutsch, E.W.2    Nesvizhskii, A.I.3    Mallick, P.4    King, N.L.5    Eng, J.K.6
  • 56
    • 77749282896 scopus 로고    scopus 로고
    • An integrated mass-spectrometry pipeline identifies novel protein coding-regions in the human genome
    • Bitton D.A., Smith D.L., Connolly Y., Scutt P.J., Miller C.J. An integrated mass-spectrometry pipeline identifies novel protein coding-regions in the human genome. PLoS ONE 2010, 5:e8949.
    • (2010) PLoS ONE , vol.5
    • Bitton, D.A.1    Smith, D.L.2    Connolly, Y.3    Scutt, P.J.4    Miller, C.J.5
  • 57
    • 77949790696 scopus 로고    scopus 로고
    • Detection of alternative splice variants at the proteome level in Aspergillus flavus
    • Chang K.Y., Georgianna D.R., Heber S., Payne G.A., Muddiman D.C. Detection of alternative splice variants at the proteome level in Aspergillus flavus. J Proteome Res 2010, 9:1209-1217.
    • (2010) J Proteome Res , vol.9 , pp. 1209-1217
    • Chang, K.Y.1    Georgianna, D.R.2    Heber, S.3    Payne, G.A.4    Muddiman, D.C.5
  • 58
    • 66049143064 scopus 로고    scopus 로고
    • Proteomic discovery of previously unannotated, rapidly evolving seminal fluid genes in Drosophila
    • Findlay G.D., MacCoss M.J., Swanson W.J. Proteomic discovery of previously unannotated, rapidly evolving seminal fluid genes in Drosophila. Genome Res 2009, 19:886-896.
    • (2009) Genome Res , vol.19 , pp. 886-896
    • Findlay, G.D.1    MacCoss, M.J.2    Swanson, W.J.3
  • 59
    • 61649112956 scopus 로고    scopus 로고
    • The Drosophila melanogaster PeptideAtlas facilitates the use of peptide data for improved fly proteomics and genome annotation
    • Loevenich S.N., Brunner E., King N.L., Deutsch E.W., Stein S.E., Aebersold R., et al. The Drosophila melanogaster PeptideAtlas facilitates the use of peptide data for improved fly proteomics and genome annotation. BMC Bioinform 2009, 10:59.
    • (2009) BMC Bioinform , vol.10 , pp. 59
    • Loevenich, S.N.1    Brunner, E.2    King, N.L.3    Deutsch, E.W.4    Stein, S.E.5    Aebersold, R.6
  • 60
    • 53549100731 scopus 로고    scopus 로고
    • Use of shotgun proteomics for the identification, confirmation, and correction of C. elegans gene annotations
    • Merrihew G.E., Davis C., Ewing B., Williams G., Kall L., Frewen B.E., et al. Use of shotgun proteomics for the identification, confirmation, and correction of C. elegans gene annotations. Genome Res 2008, 18:1660-1669.
    • (2008) Genome Res , vol.18 , pp. 1660-1669
    • Merrihew, G.E.1    Davis, C.2    Ewing, B.3    Williams, G.4    Kall, L.5    Frewen, B.E.6
  • 61
    • 57449088165 scopus 로고    scopus 로고
    • Proteomics studies confirm the presence of alternative protein isoforms on a large scale
    • Tress M.L., Bodenmiller B., Aebersold R., Valencia A. Proteomics studies confirm the presence of alternative protein isoforms on a large scale. Genome Biol 2008, 9:R162.
    • (2008) Genome Biol , vol.9
    • Tress, M.L.1    Bodenmiller, B.2    Aebersold, R.3    Valencia, A.4
  • 63
    • 33745054329 scopus 로고    scopus 로고
    • Novel gene and gene model detection using a whole genome open reading frame analysis in proteomics
    • Fermin D., Allen B.B., Blackwell T.W., Menon R., Adamski M., Xu Y., et al. Novel gene and gene model detection using a whole genome open reading frame analysis in proteomics. Genome Biol 2006, 7:R35.
    • (2006) Genome Biol , vol.7
    • Fermin, D.1    Allen, B.B.2    Blackwell, T.W.3    Menon, R.4    Adamski, M.5    Xu, Y.6
  • 64
    • 25444475024 scopus 로고    scopus 로고
    • Genome annotation of Anopheles gambiae using mass spectrometry-derived data
    • Kalume D., Peri S., Reddy R., Zhong J., Okulate M., Kumar N., et al. Genome annotation of Anopheles gambiae using mass spectrometry-derived data. BMC Genomics 2005, 6:128.
    • (2005) BMC Genomics , vol.6 , pp. 128
    • Kalume, D.1    Peri, S.2    Reddy, R.3    Zhong, J.4    Okulate, M.5    Kumar, N.6
  • 66
    • 0041859530 scopus 로고    scopus 로고
    • Preprocessing of tandem mass spectrometric data to support automatic protein identification
    • Gentzel M., Kocher T., Ponnusamy S., Wilm M. Preprocessing of tandem mass spectrometric data to support automatic protein identification. Proteomics 2003, 3:1597-1610.
    • (2003) Proteomics , vol.3 , pp. 1597-1610
    • Gentzel, M.1    Kocher, T.2    Ponnusamy, S.3    Wilm, M.4
  • 67
    • 33749610164 scopus 로고    scopus 로고
    • Cleaning of raw peptide MS/MS spectra: improved protein identification following deconvolution of multiply charged peaks, isotope clusters, and removal of background noise
    • Mujezinovic N., Raidl G., Hutchins J.R.A., Peters J.M., Mechtler K., Eisenhaber F. Cleaning of raw peptide MS/MS spectra: improved protein identification following deconvolution of multiply charged peaks, isotope clusters, and removal of background noise. Proteomics 2006, 6:5117-5131.
    • (2006) Proteomics , vol.6 , pp. 5117-5131
    • Mujezinovic, N.1    Raidl, G.2    Hutchins, J.R.A.3    Peters, J.M.4    Mechtler, K.5    Eisenhaber, F.6
  • 69
    • 1842580753 scopus 로고    scopus 로고
    • Improving large-scale proteomics by clustering of mass spectrometry data
    • Beer I., Barnea E., Ziv T., Admon A. Improving large-scale proteomics by clustering of mass spectrometry data. Proteomics 2004, 4:950-960.
    • (2004) Proteomics , vol.4 , pp. 950-960
    • Beer, I.1    Barnea, E.2    Ziv, T.3    Admon, A.4
  • 71
    • 77955455399 scopus 로고    scopus 로고
    • Quantifying the impact of chimera MS/MS spectra on peptide identification in large scale proteomics studies. J Proteome Res
    • Houel S, Abernathy R, Renganathan K, Meyer-Arendt K, Ahn N, Old WM. Quantifying the impact of chimera MS/MS spectra on peptide identification in large scale proteomics studies. J Proteome Res 2010;9:4152-60.
    • (2010) , vol.9 , pp. 4152-60
    • Houel, S.1    Abernathy, R.2    Renganathan, K.3    Meyer-Arendt, K.4    Ahn, N.5    Old, W.M.6
  • 73
    • 76149113930 scopus 로고    scopus 로고
    • Deconvolution of mixture spectra from ion-trap data-independent-acquisition tandem mass spectrometry
    • Bern M., Finney G., Hoopmann M.R., Merrihew G., Toth M.J., MacCoss M.J. Deconvolution of mixture spectra from ion-trap data-independent-acquisition tandem mass spectrometry. Anal Chem 2010, 82:833-841.
    • (2010) Anal Chem , vol.82 , pp. 833-841
    • Bern, M.1    Finney, G.2    Hoopmann, M.R.3    Merrihew, G.4    Toth, M.J.5    MacCoss, M.J.6
  • 74
    • 27744469683 scopus 로고    scopus 로고
    • ProblDtree: an automated software program capable of identifying multiple peptides from a single collision-induced dissociation spectrum collected by a tandem mass spectrometer
    • Zhang N., Li X.J., Ye M.L., Pan S., Schwikowski B., Aebersold R. ProblDtree: an automated software program capable of identifying multiple peptides from a single collision-induced dissociation spectrum collected by a tandem mass spectrometer. Proteomics 2005, 5:4096-4106.
    • (2005) Proteomics , vol.5 , pp. 4096-4106
    • Zhang, N.1    Li, X.J.2    Ye, M.L.3    Pan, S.4    Schwikowski, B.5    Aebersold, R.6
  • 75
    • 77954751922 scopus 로고    scopus 로고
    • Peptide identification from mixture tandem mass spectra. Mol Cell Proteomics
    • Wang J, Perez-Santiago J, Katz JE, Mallick P, Bandeira N. Peptide identification from mixture tandem mass spectra. Mol Cell Proteomics 2010;9:1476-85.
    • (2010) , vol.9 , pp. 1476-85
    • Wang, J.1    Perez-Santiago, J.2    Katz, J.E.3    Mallick, P.4    Bandeira, N.5
  • 76
    • 0034484286 scopus 로고    scopus 로고
    • Method for screening peptide fragment ion mass spectra prior to database searching
    • Moore R.E., Young M.K., Lee T.D. Method for screening peptide fragment ion mass spectra prior to database searching. J Am Soc Mass Spectrom 2000, 11:422-426.
    • (2000) J Am Soc Mass Spectrom , vol.11 , pp. 422-426
    • Moore, R.E.1    Young, M.K.2    Lee, T.D.3
  • 77
    • 33847654762 scopus 로고    scopus 로고
    • MsmsEval: tandem mass spectral quality assignment for high-throughput proteomics
    • Wong J.W.H., Sullivan M.J., Cartwright H.M., Cagney G. msmsEval: tandem mass spectral quality assignment for high-throughput proteomics. BMC Bioinform 2007, 8.
    • (2007) BMC Bioinform , vol.8
    • Wong, J.W.H.1    Sullivan, M.J.2    Cartwright, H.M.3    Cagney, G.4
  • 78
    • 33645653958 scopus 로고    scopus 로고
    • Improving the reliability and throughput of mass spectrometry-based proteomics by spectrum quality filtering
    • Flikka K., Martens L., Vandekerckhoe J., Gevaert K., Eidhammer I. Improving the reliability and throughput of mass spectrometry-based proteomics by spectrum quality filtering. Proteomics 2006, 6:2086-2094.
    • (2006) Proteomics , vol.6 , pp. 2086-2094
    • Flikka, K.1    Martens, L.2    Vandekerckhoe, J.3    Gevaert, K.4    Eidhammer, I.5
  • 79
    • 17444423714 scopus 로고    scopus 로고
    • Assessing data quality of peptide mass spectra obtained by quadrupole ion trap mass spectrometry
    • Xu M., Geer L.Y., Bryant S.H., Roth J.S., Kowalak J.A., Maynard D.M., et al. Assessing data quality of peptide mass spectra obtained by quadrupole ion trap mass spectrometry. J Proteome Res 2005, 4:300-305.
    • (2005) J Proteome Res , vol.4 , pp. 300-305
    • Xu, M.1    Geer, L.Y.2    Bryant, S.H.3    Roth, J.S.4    Kowalak, J.A.5    Maynard, D.M.6
  • 80
    • 53049085543 scopus 로고    scopus 로고
    • Separating the wheat from the chaff: unbiased filtering of background tandem mass spectra improves protein identification
    • Junqueira M., Spirin V., Balbuena T.S., Waridel P., Surendranath V., Kryukov G., et al. Separating the wheat from the chaff: unbiased filtering of background tandem mass spectra improves protein identification. J Proteome Res 2008, 7:3382-3395.
    • (2008) J Proteome Res , vol.7 , pp. 3382-3395
    • Junqueira, M.1    Spirin, V.2    Balbuena, T.S.3    Waridel, P.4    Surendranath, V.5    Kryukov, G.6
  • 81
    • 55249083770 scopus 로고    scopus 로고
    • Robust prediction of the MASCOT score for an improved quality assessment in mass spectrometric proteomics
    • Koenig T., Menze B.H., Kirchner M., Monigatti F., Parker K.C., Patterson T., et al. Robust prediction of the MASCOT score for an improved quality assessment in mass spectrometric proteomics. J Proteome Res 2008, 7:3708-3717.
    • (2008) J Proteome Res , vol.7 , pp. 3708-3717
    • Koenig, T.1    Menze, B.H.2    Kirchner, M.3    Monigatti, F.4    Parker, K.C.5    Patterson, T.6
  • 82
    • 41149169225 scopus 로고    scopus 로고
    • CIFTER: automated charge-state determination for peptide tandem mass spectra
    • Na S., Paek E., Lee C. CIFTER: automated charge-state determination for peptide tandem mass spectra. Anal Chem 2008, 80:1520-1528.
    • (2008) Anal Chem , vol.80 , pp. 1520-1528
    • Na, S.1    Paek, E.2    Lee, C.3
  • 84
    • 33745238061 scopus 로고    scopus 로고
    • Determination of peptide and protein ion charge states by Fourier transformation of isotope-resolved mass spectra
    • Tabb D.L., Shah M.B., Strader M.B., Connelly H.M., Hettich R.L., Hurst G.B. Determination of peptide and protein ion charge states by Fourier transformation of isotope-resolved mass spectra. J Am Soc Mass Spectrom 2006, 17:903-915.
    • (2006) J Am Soc Mass Spectrom , vol.17 , pp. 903-915
    • Tabb, D.L.1    Shah, M.B.2    Strader, M.B.3    Connelly, H.M.4    Hettich, R.L.5    Hurst, G.B.6
  • 85
    • 38349104744 scopus 로고    scopus 로고
    • Charger: combination of signal processing and statistical learning algorithms for precursor charge-state determination from electron-transfer dissociation spectra
    • Sadygov R.G., Hao Z., Huhmer A.F.R. Charger: combination of signal processing and statistical learning algorithms for precursor charge-state determination from electron-transfer dissociation spectra. Anal Chem 2008, 80:376-386.
    • (2008) Anal Chem , vol.80 , pp. 376-386
    • Sadygov, R.G.1    Hao, Z.2    Huhmer, A.F.R.3
  • 86
    • 55249111329 scopus 로고    scopus 로고
    • Precursor-ion mass re-estimation improves peptide identification on hybrid instruments
    • Luethy R., Kessner D.E., Katz J.E., McLean B., Grothe R., Kani K., et al. Precursor-ion mass re-estimation improves peptide identification on hybrid instruments. J Proteome Res 2008, 7:4031-4039.
    • (2008) J Proteome Res , vol.7 , pp. 4031-4039
    • Luethy, R.1    Kessner, D.E.2    Katz, J.E.3    McLean, B.4    Grothe, R.5    Kani, K.6
  • 87
    • 41349120246 scopus 로고    scopus 로고
    • DeconMSn: a software tool for accurate parent ion monoisotopic mass determination for tandem mass spectra
    • Mayampurath A.M., Jaitly N., Purvine S.O., Monroe M.E., Auberry K.J., Adkins J.N., et al. DeconMSn: a software tool for accurate parent ion monoisotopic mass determination for tandem mass spectra. Bioinformatics 2008, 24:1021-1023.
    • (2008) Bioinformatics , vol.24 , pp. 1021-1023
    • Mayampurath, A.M.1    Jaitly, N.2    Purvine, S.O.3    Monroe, M.E.4    Auberry, K.J.5    Adkins, J.N.6
  • 88
    • 70449533143 scopus 로고    scopus 로고
    • A software program for more reliable precursor ion assignation from LC-MS analysis using LTQ ultra zoom scan
    • Shinkawa T., Nagano K., Inomata N., Haramura M. A software program for more reliable precursor ion assignation from LC-MS analysis using LTQ ultra zoom scan. J Proteomics 2009, 73:357-360.
    • (2009) J Proteomics , vol.73 , pp. 357-360
    • Shinkawa, T.1    Nagano, K.2    Inomata, N.3    Haramura, M.4
  • 89
    • 0032159387 scopus 로고    scopus 로고
    • Method to compare collision-induced dissociation spectra of peptides: potential for library searching and subtractive analysis
    • Yates J.R., Morgan S.F., Gatlin C.L., Griffin P.R., Eng J.K. Method to compare collision-induced dissociation spectra of peptides: potential for library searching and subtractive analysis. Anal Chem 1998, 70:3557-3565.
    • (1998) Anal Chem , vol.70 , pp. 3557-3565
    • Yates, J.R.1    Morgan, S.F.2    Gatlin, C.L.3    Griffin, P.R.4    Eng, J.K.5
  • 90
    • 33747170146 scopus 로고    scopus 로고
    • Using annotated peptide mass spectrum libraries for protein identification
    • Craig R., Cortens J.C., Fenyo D., Beavis R.C. Using annotated peptide mass spectrum libraries for protein identification. J Proteome Res 2006, 5:1843-1849.
    • (2006) J Proteome Res , vol.5 , pp. 1843-1849
    • Craig, R.1    Cortens, J.C.2    Fenyo, D.3    Beavis, R.C.4
  • 91
    • 33747626954 scopus 로고    scopus 로고
    • Analysis of peptide MS/MS spectra from large-scale proteomics experiments using spectrum libraries
    • Frewen B.E., Merrihew G.E., Wu C.C., Noble W.S., MacCoss M.J. Analysis of peptide MS/MS spectra from large-scale proteomics experiments using spectrum libraries. Anal Chem 2006, 78:5678-5684.
    • (2006) Anal Chem , vol.78 , pp. 5678-5684
    • Frewen, B.E.1    Merrihew, G.E.2    Wu, C.C.3    Noble, W.S.4    MacCoss, M.J.5
  • 92
    • 33947366516 scopus 로고    scopus 로고
    • Development and validation of a spectral library searching method for peptide identification from MS/MS
    • Lam H., Deutsch E.W., Eddes J.S., Eng J.K., King N., Stein S.E., et al. Development and validation of a spectral library searching method for peptide identification from MS/MS. Proteomics 2007, 7:655-667.
    • (2007) Proteomics , vol.7 , pp. 655-667
    • Lam, H.1    Deutsch, E.W.2    Eddes, J.S.3    Eng, J.K.4    King, N.5    Stein, S.E.6
  • 93
    • 0000881748 scopus 로고
    • Optimization and testing of mass-spectral library search algorithms for compound identification
    • Stein S.E., Scott D.R. Optimization and testing of mass-spectral library search algorithms for compound identification. J Am Soc Mass Spectrom 1994, 5:859-866.
    • (1994) J Am Soc Mass Spectrom , vol.5 , pp. 859-866
    • Stein, S.E.1    Scott, D.R.2
  • 94
    • 53249098366 scopus 로고    scopus 로고
    • Building consensus spectral libraries for peptide identification in proteomics
    • Lam H., Deutsch E.W., Eddes J.S., Eng J.K., Stein S.E., Aebersold R. Building consensus spectral libraries for peptide identification in proteomics. Nat Meth 2008, 5:873-875.
    • (2008) Nat Meth , vol.5 , pp. 873-875
    • Lam, H.1    Deutsch, E.W.2    Eddes, J.S.3    Eng, J.K.4    Stein, S.E.5    Aebersold, R.6
  • 95
    • 76749169902 scopus 로고    scopus 로고
    • A ubiquitin and ubiquitin-like protein spectral library
    • Srikumar T., Jeram S.M., Lam H., Raught B. A ubiquitin and ubiquitin-like protein spectral library. Proteomics 2010, 10:337-342.
    • (2010) Proteomics , vol.10 , pp. 337-342
    • Srikumar, T.1    Jeram, S.M.2    Lam, H.3    Raught, B.4
  • 98
    • 34249717879 scopus 로고    scopus 로고
    • A high-quality catalog of the Drosophila melanogaster proteome. Nat Biotechnol
    • Brunner E, Ahrens CH, Mohanty S, Baetschmann H, Loevenich S, Potthast F, et al. A high-quality catalog of the Drosophila melanogaster proteome. Nat Biotechnol 2007;25:576-83.
    • (2007) , vol.25 , pp. 576-83
    • Brunner, E.1    Ahrens, C.H.2    Mohanty, S.3    Baetschmann, H.4    Loevenich, S.5    Potthast, F.6
  • 99
    • 66149152717 scopus 로고    scopus 로고
    • A simulated MS/MS library for spectrum-to-spectrum searching in large scale identification of proteins
    • Yen C.Y., Meyer-Arendt K., Eichelberger B., Sun S.J., Houel S., Old W.M., et al. A simulated MS/MS library for spectrum-to-spectrum searching in large scale identification of proteins. Mol Cell Proteomics 2009, 8:857-869.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 857-869
    • Yen, C.Y.1    Meyer-Arendt, K.2    Eichelberger, B.3    Sun, S.J.4    Houel, S.5    Old, W.M.6
  • 100
    • 77954191980 scopus 로고    scopus 로고
    • Open MS/MS spectral library search to identify unanticipated post-translational modifications and increase spectral identification rate
    • Ye D., Fu Y., Sun R.X., Wang H.P., Yuan Z.F., Chi H., et al. Open MS/MS spectral library search to identify unanticipated post-translational modifications and increase spectral identification rate. Bioinformatics 2010, 26:i399-i406.
    • (2010) Bioinformatics , vol.26
    • Ye, D.1    Fu, Y.2    Sun, R.X.3    Wang, H.P.4    Yuan, Z.F.5    Chi, H.6
  • 101
    • 77957220208 scopus 로고    scopus 로고
    • Proteomics data repositories: Providing a safe haven for your data and acting as a springboard for further research. J Proteomics
    • Vizcaíno JA, Foster JM, Martens L. Proteomics data repositories: Providing a safe haven for your data and acting as a springboard for further research. J Proteomics 77 (11) 2136-2146.
    • , vol.77 , Issue.11 , pp. 2136-2146
    • Vizcaíno, J.A.1    Foster, J.M.2    Martens, L.3
  • 102
    • 43049127826 scopus 로고    scopus 로고
    • PeptideAtlas: a resource for target selection for emerging targeted proteomics workflows
    • Deutsch E.W., Lam H., Aebersold R. PeptideAtlas: a resource for target selection for emerging targeted proteomics workflows. EMBO Rep 2008, 9:429-434.
    • (2008) EMBO Rep , vol.9 , pp. 429-434
    • Deutsch, E.W.1    Lam, H.2    Aebersold, R.3
  • 104
    • 0037253223 scopus 로고    scopus 로고
    • Expanding the organismal scope of proteomics: cross-species protein identification by mass spectrometry and its implications
    • Liska A.J., Shevchenko A. Expanding the organismal scope of proteomics: cross-species protein identification by mass spectrometry and its implications. Proteomics 2003, 3:19-28.
    • (2003) Proteomics , vol.3 , pp. 19-28
    • Liska, A.J.1    Shevchenko, A.2
  • 105
    • 37049006551 scopus 로고    scopus 로고
    • A workflow to increase the detection rate of proteins from unsequenced organisms in high-throughput proteomics experiments
    • Grossmann J., Fischer B., Baerenfaller K., Owiti J., Buhmann J.M., Gruissem W., et al. A workflow to increase the detection rate of proteins from unsequenced organisms in high-throughput proteomics experiments. Proteomics 2007, 7:4245-4254.
    • (2007) Proteomics , vol.7 , pp. 4245-4254
    • Grossmann, J.1    Fischer, B.2    Baerenfaller, K.3    Owiti, J.4    Buhmann, J.M.5    Gruissem, W.6
  • 107
    • 77956404066 scopus 로고    scopus 로고
    • OVNIp: an open source application facilitating the interpretation, the validation and the edition of proteomics data generated by MS analyses and de novo sequencing
    • Tessier D., Yclon P., Jacquemin I., Larre C., Rogniaux H. OVNIp: an open source application facilitating the interpretation, the validation and the edition of proteomics data generated by MS analyses and de novo sequencing. Proteomics 2010, 10:1794-1801.
    • (2010) Proteomics , vol.10 , pp. 1794-1801
    • Tessier, D.1    Yclon, P.2    Jacquemin, I.3    Larre, C.4    Rogniaux, H.5
  • 108
    • 55749111513 scopus 로고    scopus 로고
    • Simplified validation of borderline hits of database searches
    • Thomas H., Shevchenko A. Simplified validation of borderline hits of database searches. Proteomics 2008, 8:4173-4177.
    • (2008) Proteomics , vol.8 , pp. 4173-4177
    • Thomas, H.1    Shevchenko, A.2
  • 110
    • 77950521889 scopus 로고    scopus 로고
    • A high-throughput de novo sequencing approach for shotgun proteomics using high-resolution tandem mass spectrometry
    • Pan C., Park B.H., McDonald W.H., Carey P.A., Banfield J.F., VerBerkmoes N.C., et al. A high-throughput de novo sequencing approach for shotgun proteomics using high-resolution tandem mass spectrometry. BMC Bioinform 2010, 11:18.
    • (2010) BMC Bioinform , vol.11 , pp. 18
    • Pan, C.1    Park, B.H.2    McDonald, W.H.3    Carey, P.A.4    Banfield, J.F.5    VerBerkmoes, N.C.6
  • 111
    • 77952048255 scopus 로고    scopus 로고
    • PNovo: de novo peptide sequencing and identification using HCD spectra
    • Chi H., Sun R.X., Yang B., Song C.Q., Wang L.H., Liu C., et al. pNovo: de novo peptide sequencing and identification using HCD spectra. J Proteome Res 2010, 9:2713-2724.
    • (2010) J Proteome Res , vol.9 , pp. 2713-2724
    • Chi, H.1    Sun, R.X.2    Yang, B.3    Song, C.Q.4    Wang, L.H.5    Liu, C.6
  • 112
    • 77949702383 scopus 로고    scopus 로고
    • LysNDeNovo: an algorithm enabling de novo sequencing of Lys-N generated peptides fragmented by electron transfer dissociation
    • van Breukelen B., Georgiou A., Drugan M.M., Taouatas N., Mohammed S., Heck A.J.R. LysNDeNovo: an algorithm enabling de novo sequencing of Lys-N generated peptides fragmented by electron transfer dissociation. Proteomics 2010, 10:1196-1201.
    • (2010) Proteomics , vol.10 , pp. 1196-1201
    • van Breukelen, B.1    Georgiou, A.2    Drugan, M.M.3    Taouatas, N.4    Mohammed, S.5    Heck, A.J.R.6
  • 113
    • 70349207551 scopus 로고    scopus 로고
    • Spectrum fusion: using multiple mass spectra for de novo peptide sequencing
    • Datta R., Bern M. Spectrum fusion: using multiple mass spectra for de novo peptide sequencing. J Comput Biol 2009, 16:1169-1182.
    • (2009) J Comput Biol , vol.16 , pp. 1169-1182
    • Datta, R.1    Bern, M.2
  • 114
    • 70649108890 scopus 로고    scopus 로고
    • De novo peptide sequencing by tandem MS using complementary CID and electron transfer dissociation
    • Bertsch A., Leinenbach A., Pervukhin A., Lubeck M., Hartmer R., Baessmann C., et al. De novo peptide sequencing by tandem MS using complementary CID and electron transfer dissociation. Electrophoresis 2009, 30:3736-3747.
    • (2009) Electrophoresis , vol.30 , pp. 3736-3747
    • Bertsch, A.1    Leinenbach, A.2    Pervukhin, A.3    Lubeck, M.4    Hartmer, R.5    Baessmann, C.6
  • 115
    • 0028575316 scopus 로고
    • Error tolerant identification of peptides in sequence databases by peptide sequence tags
    • Mann M., Wilm M. Error tolerant identification of peptides in sequence databases by peptide sequence tags. Anal Chem 1994, 66:4390-4399.
    • (1994) Anal Chem , vol.66 , pp. 4390-4399
    • Mann, M.1    Wilm, M.2
  • 116
    • 22544465253 scopus 로고    scopus 로고
    • SPIDER: software for protein identification from sequence tags with de novo sequencing error
    • Han Y., Ma B., Zhang K. SPIDER: software for protein identification from sequence tags with de novo sequencing error. J Bioinform Comput Biol 2005, 3:697-716.
    • (2005) J Bioinform Comput Biol , vol.3 , pp. 697-716
    • Han, Y.1    Ma, B.2    Zhang, K.3
  • 117
    • 17444406699 scopus 로고    scopus 로고
    • Identification of protein modifications using MS/MS de novo sequencing and the OpenSea alignment algorithm
    • Searle B.C., Dasari S., Wilmarth P.A., Turner M., Reddy A.P., David L.L., et al. Identification of protein modifications using MS/MS de novo sequencing and the OpenSea alignment algorithm. J Proteome Res 2005, 4:546-554.
    • (2005) J Proteome Res , vol.4 , pp. 546-554
    • Searle, B.C.1    Dasari, S.2    Wilmarth, P.A.3    Turner, M.4    Reddy, A.P.5    David, L.L.6
  • 118
    • 0037444813 scopus 로고    scopus 로고
    • MultiTag: multiple error-tolerant sequence tag search for the sequence-similarity identification of proteins by mass spectrometry
    • Sunyaev S., Liska A.J., Golod A., Shevchenko A., Shevchenko A. MultiTag: multiple error-tolerant sequence tag search for the sequence-similarity identification of proteins by mass spectrometry. Anal Chem 2003, 75:1307-1315.
    • (2003) Anal Chem , vol.75 , pp. 1307-1315
    • Sunyaev, S.1    Liska, A.J.2    Golod, A.3    Shevchenko, A.4    Shevchenko, A.5
  • 119
    • 0345600791 scopus 로고    scopus 로고
    • GutenTag: high-throughput sequence tagging via an empirically derived fragmentation model
    • Tabb D.L., Saraf A., Yates J.R. GutenTag: high-throughput sequence tagging via an empirically derived fragmentation model. Anal Chem 2003, 75:6415-6421.
    • (2003) Anal Chem , vol.75 , pp. 6415-6421
    • Tabb, D.L.1    Saraf, A.2    Yates, J.R.3
  • 120
    • 27544511899 scopus 로고    scopus 로고
    • InsPecT: identification of posttranslationally modified peptides from tandem mass spectra
    • Tanner S., Shu H., Frank A., Wang L.C., Zandi E., Mumby M., et al. InsPecT: identification of posttranslationally modified peptides from tandem mass spectra. Anal Chem 2005, 77:4626-4639.
    • (2005) Anal Chem , vol.77 , pp. 4626-4639
    • Tanner, S.1    Shu, H.2    Frank, A.3    Wang, L.C.4    Zandi, E.5    Mumby, M.6
  • 121
    • 24044508863 scopus 로고    scopus 로고
    • New data base-independent, sequence tag-based scoring of peptide MS/MS data validates Mowse scores, recovers below threshold data, singles out modified peptides, and assesses the quality of MS/MS techniques
    • Savitski M.M., Nielsen M.L., Zubarev R.A. New data base-independent, sequence tag-based scoring of peptide MS/MS data validates Mowse scores, recovers below threshold data, singles out modified peptides, and assesses the quality of MS/MS techniques. Mol Cell Proteomics 2005, 4:1180-1188.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1180-1188
    • Savitski, M.M.1    Nielsen, M.L.2    Zubarev, R.A.3
  • 122
    • 34848889259 scopus 로고    scopus 로고
    • The paragon algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra
    • Shilov I.V., Seymour S.L., Patel A.A., Loboda A., Tang W.H., Keating S.P., et al. The paragon algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra. Mol Cell Proteomics 2007, 6:1638-1655.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1638-1655
    • Shilov, I.V.1    Seymour, S.L.2    Patel, A.A.3    Loboda, A.4    Tang, W.H.5    Keating, S.P.6
  • 124
    • 23944455372 scopus 로고    scopus 로고
    • Peptide sequence tags for fast database search in mass-spectrometry
    • Frank A., Tanner S., Bafna V., Pevzner P. Peptide sequence tags for fast database search in mass-spectrometry. J Proteome Res 2005, 4:1287-1295.
    • (2005) J Proteome Res , vol.4 , pp. 1287-1295
    • Frank, A.1    Tanner, S.2    Bafna, V.3    Pevzner, P.4
  • 125
    • 55249118638 scopus 로고    scopus 로고
    • DirecTag: accurate sequence tags from peptide MS/MS through statistical scoring
    • Tabb D.L., Ma Z.Q., Martin D.B., Ham A.J.L., Chambers M.C. DirecTag: accurate sequence tags from peptide MS/MS through statistical scoring. J Proteome Res 2008, 7:3838-3846.
    • (2008) J Proteome Res , vol.7 , pp. 3838-3846
    • Tabb, D.L.1    Ma, Z.Q.2    Martin, D.B.3    Ham, A.J.L.4    Chambers, M.C.5
  • 126
    • 55949128226 scopus 로고    scopus 로고
    • Improved sequence tag generation method for peptide identification in tandem mass spectrometry
    • Cao X., Nesvizhskii A.I. Improved sequence tag generation method for peptide identification in tandem mass spectrometry. J Proteome Res 2008, 7:4422-4434.
    • (2008) J Proteome Res , vol.7 , pp. 4422-4434
    • Cao, X.1    Nesvizhskii, A.I.2
  • 127
    • 0036828610 scopus 로고    scopus 로고
    • Searching sequence databases via de novo peptide sequencing by tandem mass spectrometry
    • Johnson R.S., Taylor J.A. Searching sequence databases via de novo peptide sequencing by tandem mass spectrometry. Mol Biotechnol 2002, 22:301-315.
    • (2002) Mol Biotechnol , vol.22 , pp. 301-315
    • Johnson, R.S.1    Taylor, J.A.2
  • 128
    • 59149096107 scopus 로고    scopus 로고
    • Spectral dictionaries: integrating de novo peptide sequencing with database search of tandem mass spectra
    • Kim S., Gupta N., Bandeira N., Pevzner P.A. Spectral dictionaries: integrating de novo peptide sequencing with database search of tandem mass spectra. Mol Cell Proteomics 2009, 8:53-69.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 53-69
    • Kim, S.1    Gupta, N.2    Bandeira, N.3    Pevzner, P.A.4
  • 129
    • 67650535647 scopus 로고    scopus 로고
    • Spectral profiles, a novel representation of tandem mass spectra and their applications for de novo peptide sequencing and identification
    • Kim S., Bandeira N., Pevzner P.A. Spectral profiles, a novel representation of tandem mass spectra and their applications for de novo peptide sequencing and identification. Mol Cell Proteomics 2009, 8:1391-1400.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 1391-1400
    • Kim, S.1    Bandeira, N.2    Pevzner, P.A.3
  • 130
    • 54349083037 scopus 로고    scopus 로고
    • De novo sequencing of unique sequence tags for discovery of post-translational modifications of proteins
    • Shen Y.F., Tolic N., Hixson K.K., Purvine S.O., Anderson G.A., Smith R.D. De novo sequencing of unique sequence tags for discovery of post-translational modifications of proteins. Anal Chem 2008, 80:7742-7754.
    • (2008) Anal Chem , vol.80 , pp. 7742-7754
    • Shen, Y.F.1    Tolic, N.2    Hixson, K.K.3    Purvine, S.O.4    Anderson, G.A.5    Smith, R.D.6
  • 131
    • 41449112363 scopus 로고    scopus 로고
    • Proteome-wide identification of proteins and their modifications with decreased ambiguities and improved false discovery rates using unique sequence tags
    • Shen Y.F., Tolic N., Hixson K.K., Purvine S.O., Pasa-Tolic L., Qian W.J., et al. Proteome-wide identification of proteins and their modifications with decreased ambiguities and improved false discovery rates using unique sequence tags. Anal Chem 2008, 80:1871-1882.
    • (2008) Anal Chem , vol.80 , pp. 1871-1882
    • Shen, Y.F.1    Tolic, N.2    Hixson, K.K.3    Purvine, S.O.4    Pasa-Tolic, L.5    Qian, W.J.6
  • 132
    • 33847234661 scopus 로고    scopus 로고
    • Lookup peaks: a hybrid of de novo sequencing and database search for protein identification by tandem mass spectrometry
    • Bern M., Cai Y.H., Goldberg D. Lookup peaks: a hybrid of de novo sequencing and database search for protein identification by tandem mass spectrometry. Anal Chem 2007, 79:1393-1400.
    • (2007) Anal Chem , vol.79 , pp. 1393-1400
    • Bern, M.1    Cai, Y.H.2    Goldberg, D.3
  • 133
    • 33645708138 scopus 로고    scopus 로고
    • Dynamic spectrum quality assessment and iterative computational analysis of shotgun proteomic data: toward more efficient identification of post-translational modifications, sequence polymorphisms, and novel peptides
    • Nesvizhskii A.I., Roos F.F., Grossmann J., Vogelzang M., Eddes J.S., Gruissem W., et al. Dynamic spectrum quality assessment and iterative computational analysis of shotgun proteomic data: toward more efficient identification of post-translational modifications, sequence polymorphisms, and novel peptides. Mol Cell Proteomics 2006, 5:652-670.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 652-670
    • Nesvizhskii, A.I.1    Roos, F.F.2    Grossmann, J.3    Vogelzang, M.4    Eddes, J.S.5    Gruissem, W.6
  • 134
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii A.I., Keller A., Kolker E., Aebersold R. A statistical model for identifying proteins by tandem mass spectrometry. Anal Chem 2003, 75:4646-4658.
    • (2003) Anal Chem , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 135
    • 24044491542 scopus 로고    scopus 로고
    • Comprehensive analysis of a multidimensional liquid chromatography mass spectrometry dataset acquired on a quadrupole selecting, quadrupole collision cell, time-of-flight mass spectrometer - II. New developments in protein prospector allow for reliable and comprehensive automatic analysis of large datasets.
    • Chalkley R.J., Baker P.R., Huang L., Hansen K.C., Allen N.P., Rexach M., et al. Comprehensive analysis of a multidimensional liquid chromatography mass spectrometry dataset acquired on a quadrupole selecting, quadrupole collision cell, time-of-flight mass spectrometer - II. New developments in protein prospector allow for reliable and comprehensive automatic analysis of large datasets. Mol Cell Proteomics 2005, 4:1194-1204.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1194-1204
    • Chalkley, R.J.1    Baker, P.R.2    Huang, L.3    Hansen, K.C.4    Allen, N.P.5    Rexach, M.6
  • 136
    • 33846010726 scopus 로고    scopus 로고
    • Extent of modifications in human proteome samples and their effect on dynamic range of analysis in shotgun proteomics
    • Nielsen M.L., Savitski M.M., Zubarev R.A. Extent of modifications in human proteome samples and their effect on dynamic range of analysis in shotgun proteomics. Mol Cell Proteomics 2006, 5:2384-2391.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 2384-2391
    • Nielsen, M.L.1    Savitski, M.M.2    Zubarev, R.A.3
  • 137
    • 58149307960 scopus 로고    scopus 로고
    • Unrestrictive identification of multiple post-translational modifications from tandem mass spectrometry using an error-tolerant algorithm based on an extended sequence tag approach
    • Na S., Jeong J., Park H., Lee K.J., Paek E. Unrestrictive identification of multiple post-translational modifications from tandem mass spectrometry using an error-tolerant algorithm based on an extended sequence tag approach. Mol Cell Proteomics 2008, 7:2452-2463.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 2452-2463
    • Na, S.1    Jeong, J.2    Park, H.3    Lee, K.J.4    Paek, E.5
  • 138
    • 33747873469 scopus 로고    scopus 로고
    • Peptide sequence tag-based blind identification of post-translational modifications with point process model
    • Liu C., Yan B., Song Y., Xu Y., Cai L. Peptide sequence tag-based blind identification of post-translational modifications with point process model. Bioinformatics 2006, 22:E307-E313.
    • (2006) Bioinformatics , vol.22
    • Liu, C.1    Yan, B.2    Song, Y.3    Xu, Y.4    Cai, L.5
  • 140
    • 58849092421 scopus 로고    scopus 로고
    • PTMap - a sequence alignment software for unrestricted, accurate, and full-spectrum identification of post-translational modification sites
    • Chen Y., Chen W., Cobb M.H., Zhao Y.M. PTMap - a sequence alignment software for unrestricted, accurate, and full-spectrum identification of post-translational modification sites. Proc Natl Acad Sci USA 2009, 106:761-766.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 761-766
    • Chen, Y.1    Chen, W.2    Cobb, M.H.3    Zhao, Y.M.4
  • 141
    • 38649111957 scopus 로고    scopus 로고
    • Accurate annotation of peptide modifications through unrestrictive database search
    • Tanner S., Payne S.H., Dasari S., Shen Z., Wilmarth P.A., David L.L., et al. Accurate annotation of peptide modifications through unrestrictive database search. J Proteome Res 2008, 7:170-181.
    • (2008) J Proteome Res , vol.7 , pp. 170-181
    • Tanner, S.1    Payne, S.H.2    Dasari, S.3    Shen, Z.4    Wilmarth, P.A.5    David, L.L.6
  • 142
    • 28644447919 scopus 로고    scopus 로고
    • Identification of post-translational modifications by blind search of mass spectra
    • Tsur D., Tanner S., Zandi E., Bafna V., Pevzner P.A. Identification of post-translational modifications by blind search of mass spectra. Nat Biotechnol 2005, 23:1562-1567.
    • (2005) Nat Biotechnol , vol.23 , pp. 1562-1567
    • Tsur, D.1    Tanner, S.2    Zandi, E.3    Bafna, V.4    Pevzner, P.A.5
  • 143
    • 77149158441 scopus 로고    scopus 로고
    • Unrestricted identification of modified proteins using MS/MS
    • Ahrne E., Muller M., Lisacek F. Unrestricted identification of modified proteins using MS/MS. Proteomics 2010, 10:671-686.
    • (2010) Proteomics , vol.10 , pp. 671-686
    • Ahrne, E.1    Muller, M.2    Lisacek, F.3
  • 144
    • 70349135910 scopus 로고    scopus 로고
    • Spectral clustering in peptidomics studies helps to unravel modification profile of biologically active peptides and enhances peptide identification rate
    • Menschaert G., Vandekerckhove T.T.M., Landuyt B., Hayakawa E., Schoofs L., Luyten W., et al. Spectral clustering in peptidomics studies helps to unravel modification profile of biologically active peptides and enhances peptide identification rate. Proteomics 2009, 9:4381-4388.
    • (2009) Proteomics , vol.9 , pp. 4381-4388
    • Menschaert, G.1    Vandekerckhove, T.T.M.2    Landuyt, B.3    Hayakawa, E.4    Schoofs, L.5    Luyten, W.6
  • 145
    • 58149391408 scopus 로고    scopus 로고
    • A spectral clustering approach to MS/MS identification of post-translational modifications
    • Falkner J.A., Falkner J.W., Yocum A.K., Andrews P.C. A spectral clustering approach to MS/MS identification of post-translational modifications. J Proteome Res 2008, 7:4614-4622.
    • (2008) J Proteome Res , vol.7 , pp. 4614-4622
    • Falkner, J.A.1    Falkner, J.W.2    Yocum, A.K.3    Andrews, P.C.4
  • 146
    • 0036138754 scopus 로고    scopus 로고
    • Peptide sequence motif analysis of tandem MS data with the SALSA algorithm
    • Liebler D.C., Hansen B.T., Davey S.W., Tiscareno L., Mason D.E. Peptide sequence motif analysis of tandem MS data with the SALSA algorithm. Anal Chem 2002, 74:203-210.
    • (2002) Anal Chem , vol.74 , pp. 203-210
    • Liebler, D.C.1    Hansen, B.T.2    Davey, S.W.3    Tiscareno, L.4    Mason, D.E.5
  • 147
    • 54349102503 scopus 로고    scopus 로고
    • Sequential interval motif search: unrestricted database surveys of global MS/MS data sets for detection of putative post-translational modifications
    • Erassov J.L.A., Halina P., Canete M., Vo N.D., Chung C., Cagney G., et al. Sequential interval motif search: unrestricted database surveys of global MS/MS data sets for detection of putative post-translational modifications. Anal Chem 2008, 80:7846-7854.
    • (2008) Anal Chem , vol.80 , pp. 7846-7854
    • Erassov, J.L.A.1    Halina, P.2    Canete, M.3    Vo, N.D.4    Chung, C.5    Cagney, G.6
  • 148
    • 55249092493 scopus 로고    scopus 로고
    • SeMoP: a new computational strategy for the unrestricted search for modified peptides using LC-MS/MS data
    • Baumgartner C., Rejtar T., Kullolli M., Akella L.M., Karger B.L. SeMoP: a new computational strategy for the unrestricted search for modified peptides using LC-MS/MS data. J Proteome Res 2008, 7:4199-4208.
    • (2008) J Proteome Res , vol.7 , pp. 4199-4208
    • Baumgartner, C.1    Rejtar, T.2    Kullolli, M.3    Akella, L.M.4    Karger, B.L.5
  • 149
    • 33847242627 scopus 로고    scopus 로고
    • Large-scale unrestricted identification of post-translation modifications using tandem mass spectrometry
    • Havilio M., Wool A. Large-scale unrestricted identification of post-translation modifications using tandem mass spectrometry. Anal Chem 2007, 79:1362-1368.
    • (2007) Anal Chem , vol.79 , pp. 1362-1368
    • Havilio, M.1    Wool, A.2
  • 150
    • 3142702204 scopus 로고    scopus 로고
    • TANDEM: matching proteins with tandem mass spectra
    • Craig R., Beavis R.C. TANDEM: matching proteins with tandem mass spectra. Bioinformatics 2004, 20:1466-1467.
    • (2004) Bioinformatics , vol.20 , pp. 1466-1467
    • Craig, R.1    Beavis, R.C.2
  • 151
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin D.J.C., 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.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 152
    • 77949752005 scopus 로고    scopus 로고
    • Data maximization by multipass analysis of protein mass spectra
    • Tharakan R., Edwards N., Graham D.R.M. Data maximization by multipass analysis of protein mass spectra. Proteomics 2010, 10:1160-1171.
    • (2010) Proteomics , vol.10 , pp. 1160-1171
    • Tharakan, R.1    Edwards, N.2    Graham, D.R.M.3
  • 153
    • 38649114671 scopus 로고    scopus 로고
    • Improving sensitivity by probabilistically combining results from multiple MS/MS search methodologies
    • Searle B.C., Turner M., Nesvizhskii A.I. Improving sensitivity by probabilistically combining results from multiple MS/MS search methodologies. J Proteome Res 2008, 7:245-253.
    • (2008) J Proteome Res , vol.7 , pp. 245-253
    • Searle, B.C.1    Turner, M.2    Nesvizhskii, A.I.3
  • 154
    • 77949768663 scopus 로고    scopus 로고
    • Maximizing the sensitivity and reliability of peptide identification in large-scale proteomic experiments by harnessing multiple search engines
    • Yu W., Taylor J.A., Davis M.T., Bonilla L.E., Lee K.A., Auger P.L., et al. Maximizing the sensitivity and reliability of peptide identification in large-scale proteomic experiments by harnessing multiple search engines. Proteomics 2010, 10:1172-1189.
    • (2010) Proteomics , vol.10 , pp. 1172-1189
    • Yu, W.1    Taylor, J.A.2    Davis, M.T.3    Bonilla, L.E.4    Lee, K.A.5    Auger, P.L.6
  • 155
    • 34147115205 scopus 로고    scopus 로고
    • EBP, a program for protein identification using multiple tandem mass spectrometry datasets
    • Price T.S., Lucitt M.B., Wu W.C., Austin D.J., Pizarro A., Yocum A.K., et al. EBP, a program for protein identification using multiple tandem mass spectrometry datasets. Mol Cell Proteomics 2007, 6:527-536.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 527-536
    • Price, T.S.1    Lucitt, M.B.2    Wu, W.C.3    Austin, D.J.4    Pizarro, A.5    Yocum, A.K.6
  • 156
    • 77954693858 scopus 로고    scopus 로고
    • Computational analysis of unassigned high quality MS/MS spectra in proteomic datasets
    • Ning K., Fermin D., Nesvizhskii A.I. Computational analysis of unassigned high quality MS/MS spectra in proteomic datasets. Proteomics 2010, 10:2712-2718.
    • (2010) Proteomics , vol.10 , pp. 2712-2718
    • Ning, K.1    Fermin, D.2    Nesvizhskii, A.I.3
  • 157
    • 63049121561 scopus 로고    scopus 로고
    • A simple workflow to increase MS2 identification rate by subsequent spectral library search
    • Ahrne E., Masselot A., Binz P.A., Muller M., Lisacek F. A simple workflow to increase MS2 identification rate by subsequent spectral library search. Proteomics 2009, 9:1731-1736.
    • (2009) Proteomics , vol.9 , pp. 1731-1736
    • Ahrne, E.1    Masselot, A.2    Binz, P.A.3    Muller, M.4    Lisacek, F.5
  • 158
    • 67650564834 scopus 로고    scopus 로고
    • Multi-site assessment of the precision and reproducibility of multiple reaction monitoring-based measurements of proteins in plasma
    • Addona T.A., Abbatiello S.E., Schilling B., Skates S.J., Mani D.R., Bunk D.M., et al. Multi-site assessment of the precision and reproducibility of multiple reaction monitoring-based measurements of proteins in plasma. Nat Biotech 2009, 27:633-641.
    • (2009) Nat Biotech , vol.27 , pp. 633-641
    • Addona, T.A.1    Abbatiello, S.E.2    Schilling, B.3    Skates, S.J.4    Mani, D.R.5    Bunk, D.M.6
  • 159
    • 24044487850 scopus 로고    scopus 로고
    • Comprehensive analysis of a multidimensional liquid chromatography mass spectrometry dataset acquired on a quadrupole selecting, quadrupole collision cell, time-of-flight mass spectrometer - I. How much of the data is theoretically interpretable by search engines?
    • Chalkley R.J., Baker P.R., Hansen K.C., Medzihradszky K.F., Allen N.P., Rexach M., et al. Comprehensive analysis of a multidimensional liquid chromatography mass spectrometry dataset acquired on a quadrupole selecting, quadrupole collision cell, time-of-flight mass spectrometer - I. How much of the data is theoretically interpretable by search engines?. Mol Cell Proteomics 2005, 4:1189-1193.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1189-1193
    • Chalkley, R.J.1    Baker, P.R.2    Hansen, K.C.3    Medzihradszky, K.F.4    Allen, N.P.5    Rexach, M.6
  • 160
    • 67049132397 scopus 로고    scopus 로고
    • Mascot-derived false positive peptide identifications revealed by manual analysis of tandem mass spectra
    • Chen Y., Zhang J.M., Xing G., Zhao Y.M. Mascot-derived false positive peptide identifications revealed by manual analysis of tandem mass spectra. J Proteome Res 2009, 8:3141-3147.
    • (2009) J Proteome Res , vol.8 , pp. 3141-3147
    • Chen, Y.1    Zhang, J.M.2    Xing, G.3    Zhao, Y.M.4
  • 161
    • 58149375925 scopus 로고    scopus 로고
    • Adaptive discriminant function analysis and reranking of MS/MS database search results for improved peptide identification in shotgun proteomics
    • Ding Y., Choi H., Nesvizhskii A.I. Adaptive discriminant function analysis and reranking of MS/MS database search results for improved peptide identification in shotgun proteomics. J Proteome Res 2008, 7:4878-4889.
    • (2008) J Proteome Res , vol.7 , pp. 4878-4889
    • Ding, Y.1    Choi, H.2    Nesvizhskii, A.I.3
  • 162
    • 0037442649 scopus 로고    scopus 로고
    • A method for assessing the statistical significance of mass spectrometry-based protein identifications using general scoring schemes
    • Fenyo D., Beavis R.C. A method for assessing the statistical significance of mass spectrometry-based protein identifications using general scoring schemes. Anal Chem 2003, 75:768-774.
    • (2003) Anal Chem , vol.75 , pp. 768-774
    • Fenyo, D.1    Beavis, R.C.2
  • 164
    • 0043064042 scopus 로고    scopus 로고
    • A hypergeometric probability model for protein identification and validation using tandem mass spectral data and protein sequence databases
    • Sadygov R.G., Yates J.R. A hypergeometric probability model for protein identification and validation using tandem mass spectral data and protein sequence databases. Anal Chem 2003, 75:3792-3798.
    • (2003) Anal Chem , vol.75 , pp. 3792-3798
    • Sadygov, R.G.1    Yates, J.R.2
  • 166
    • 38449088855 scopus 로고    scopus 로고
    • RAId_DbS: peptide identification using database searches with realistic statistics
    • Alves G., Ogurtsov A.Y., Yu Y.K. RAId_DbS: peptide identification using database searches with realistic statistics. Biol Direct 2007, 2:25.
    • (2007) Biol Direct , vol.2 , pp. 25
    • Alves, G.1    Ogurtsov, A.Y.2    Yu, Y.K.3
  • 167
    • 65249097774 scopus 로고    scopus 로고
    • Statistical calibration of the SEQUEST XCorr function
    • Klammer A.A., Park C.Y., Noble W.S. Statistical calibration of the SEQUEST XCorr function. J Proteome Res 2009, 8:2106-2113.
    • (2009) J Proteome Res , vol.8 , pp. 2106-2113
    • Klammer, A.A.1    Park, C.Y.2    Noble, W.S.3
  • 168
    • 50149117169 scopus 로고    scopus 로고
    • Spectral probabilities and generating functions of tandem mass spectra: a strike against decoy databases
    • Kim S., Gupta N., Pevzner P.A. Spectral probabilities and generating functions of tandem mass spectra: a strike against decoy databases. J Proteome Res 2008, 7:3354-3363.
    • (2008) J Proteome Res , vol.7 , pp. 3354-3363
    • Kim, S.1    Gupta, N.2    Pevzner, P.A.3
  • 169
    • 0036376993 scopus 로고    scopus 로고
    • Statistical methods for identifying differentially expressed genes in replicated cDNA microarray experiments
    • Dudoit S., Yang Y.H., Callow M.J., Speed T.P. Statistical methods for identifying differentially expressed genes in replicated cDNA microarray experiments. Stat Sin 2002, 12:111-139.
    • (2002) Stat Sin , vol.12 , pp. 111-139
    • Dudoit, S.1    Yang, Y.H.2    Callow, M.J.3    Speed, T.P.4
  • 170
    • 0001677717 scopus 로고
    • Controlling the false discovery rate - a practical and powerful approach to multiple testing
    • Benjamini Y., Hochberg Y. Controlling the false discovery rate - a practical and powerful approach to multiple testing. J R Stat Soc B Methodol 1995, 57:289-300.
    • (1995) J R Stat Soc B Methodol , vol.57 , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2
  • 171
    • 0035942271 scopus 로고    scopus 로고
    • Significance analysis of microarrays applied to the ionizing radiation response
    • Tusher V.G., Tibshirani R., Chu G. Significance analysis of microarrays applied to the ionizing radiation response. Proc Natl Acad Sci USA 2001, 98:5116-5121.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 5116-5121
    • Tusher, V.G.1    Tibshirani, R.2    Chu, G.3
  • 172
    • 0042424602 scopus 로고    scopus 로고
    • Statistical significance for genomewide studies
    • Storey J.D., Tibshirani R. Statistical significance for genomewide studies. Proc Natl Acad Sci USA 2003, 100:9440-9445.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 9440-9445
    • Storey, J.D.1    Tibshirani, R.2
  • 174
    • 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 Meth 2007, 4:207-214.
    • (2007) Nat Meth , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 175
    • 73649110293 scopus 로고    scopus 로고
    • Artificial decoy spectral libraries for false discovery rate estimation in spectral library searching in proteomics
    • Lam H., Deutsch E.W., Aebersold R. Artificial decoy spectral libraries for false discovery rate estimation in spectral library searching in proteomics. J Proteome Res 2010, 9:605-610.
    • (2010) J Proteome Res , vol.9 , pp. 605-610
    • Lam, H.1    Deutsch, E.W.2    Aebersold, R.3
  • 176
    • 38649090064 scopus 로고    scopus 로고
    • False discovery rates and related statistical concepts in mass spectrometry-based proteomics
    • Choi H., Nesvizhskii A.I. False discovery rates and related statistical concepts in mass spectrometry-based proteomics. J Proteome Res 2008, 7:47-50.
    • (2008) J Proteome Res , vol.7 , pp. 47-50
    • Choi, H.1    Nesvizhskii, A.I.2
  • 177
    • 38649136282 scopus 로고    scopus 로고
    • Modes of inference for evaluating the confidence of peptide identifications
    • Fitzgibbon M., Li Q.H., McIntosh M. Modes of inference for evaluating the confidence of peptide identifications. J Proteome Res 2008, 7:35-39.
    • (2008) J Proteome Res , vol.7 , pp. 35-39
    • Fitzgibbon, M.1    Li, Q.H.2    McIntosh, M.3
  • 178
    • 38649129079 scopus 로고    scopus 로고
    • Posterior error probabilities and false discovery rates: two sides of the same coin
    • Kall L., Storey J.D., MacCoss M.J., Noble W.S. Posterior error probabilities and false discovery rates: two sides of the same coin. J Proteome Res 2008, 7:40-44.
    • (2008) J Proteome Res , vol.7 , pp. 40-44
    • Kall, L.1    Storey, J.D.2    MacCoss, M.J.3    Noble, W.S.4
  • 179
    • 38649083118 scopus 로고    scopus 로고
    • Assigning significance to peptides identified by tandem mass spectrometry using decoy databases
    • Kall L., Storey J.D., MacCoss M.J., Noble W.S. Assigning significance to peptides identified by tandem mass spectrometry using decoy databases. J Proteome Res 2008, 7:29-34.
    • (2008) J Proteome Res , vol.7 , pp. 29-34
    • Kall, L.1    Storey, J.D.2    MacCoss, M.J.3    Noble, W.S.4
  • 180
    • 34249316472 scopus 로고    scopus 로고
    • Estimating the statistical significance of peptide identifications from shotgun proteomics experiments
    • Higgs R.E., Knierman M.D., Freeman A.B., Gelbert L.M., Patil S.T., Hale J.E. Estimating the statistical significance of peptide identifications from shotgun proteomics experiments. J Proteome Res 2007, 6:1758-1767.
    • (2007) J Proteome Res , vol.6 , pp. 1758-1767
    • Higgs, R.E.1    Knierman, M.D.2    Freeman, A.B.3    Gelbert, L.M.4    Patil, S.T.5    Hale, J.E.6
  • 181
    • 4544370533 scopus 로고    scopus 로고
    • Improved peptide identification in proteomics by two consecutive stages of mass spectrometric fragmentation
    • Olsen J.V., Mann M. Improved peptide identification in proteomics by two consecutive stages of mass spectrometric fragmentation. Proc Natl Acad Sci USA 2004, 101:13417-13422.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13417-13422
    • Olsen, J.V.1    Mann, M.2
  • 182
    • 21044459357 scopus 로고    scopus 로고
    • A heuristic method for assigning a false-discovery rate for protein identifications from mascot database search results
    • Weatherly D.B., Atwood J.A., Minning T.A., Cavola C., Tarleton R.L., Orlando R. A heuristic method for assigning a false-discovery rate for protein identifications from mascot database search results. Mol Cell Proteomics 2005, 4:762-772.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 762-772
    • Weatherly, D.B.1    Atwood, J.A.2    Minning, T.A.3    Cavola, C.4    Tarleton, R.L.5    Orlando, R.6
  • 183
    • 65249143361 scopus 로고    scopus 로고
    • Comparison of novel decoy database designs for optimizing protein identification searches using ABRF sPRG2006 standard MS/MS data sets
    • Bianco L., Mead J.A., Bessant C. Comparison of novel decoy database designs for optimizing protein identification searches using ABRF sPRG2006 standard MS/MS data sets. J Proteome Res 2009, 8:1782-1791.
    • (2009) J Proteome Res , vol.8 , pp. 1782-1791
    • Bianco, L.1    Mead, J.A.2    Bessant, C.3
  • 184
    • 65249144535 scopus 로고    scopus 로고
    • A refined method to calculate false discovery rates for peptide identification using decoy databases
    • Navarro P., Vazquez J. A refined method to calculate false discovery rates for peptide identification using decoy databases. J Proteome Res 2009, 8:1792-1796.
    • (2009) J Proteome Res , vol.8 , pp. 1792-1796
    • Navarro, P.1    Vazquez, J.2
  • 185
    • 58149465395 scopus 로고    scopus 로고
    • Decoy methods for assessing false positives and false discovery rates in shotgun proteomics
    • Wang G., Wu W.W., Zhang Z., Masilamani S., Shen R.F. Decoy methods for assessing false positives and false discovery rates in shotgun proteomics. Anal Chem 2009, 81:146-159.
    • (2009) Anal Chem , vol.81 , pp. 146-159
    • Wang, G.1    Wu, W.W.2    Zhang, Z.3    Masilamani, S.4    Shen, R.F.5
  • 186
    • 34548802987 scopus 로고    scopus 로고
    • Probability-based pattern recognition and statistical framework for randomization: modeling tandem mass spectrum/peptide sequence false match frequencies
    • Feng J., Naiman D.Q., Cooper B. Probability-based pattern recognition and statistical framework for randomization: modeling tandem mass spectrum/peptide sequence false match frequencies. Bioinformatics 2007, 23:2210-2217.
    • (2007) Bioinformatics , vol.23 , pp. 2210-2217
    • Feng, J.1    Naiman, D.Q.2    Cooper, B.3
  • 187
    • 38649125220 scopus 로고    scopus 로고
    • Semisupervised model-based validation of peptide identifications in mass spectrometry-based proteomics
    • Choi H., Nesvizhskii A.I. Semisupervised model-based validation of peptide identifications in mass spectrometry-based proteomics. J Proteome Res 2008, 7:254-265.
    • (2008) J Proteome Res , vol.7 , pp. 254-265
    • Choi, H.1    Nesvizhskii, A.I.2
  • 188
    • 38649083116 scopus 로고    scopus 로고
    • Statistical validation of peptide identifications in large-scale proteomics using the target-decoy database search strategy and flexible mixture modeling
    • Choi H., Ghosh D., Nesvizhskii A.I. Statistical validation of peptide identifications in large-scale proteomics using the target-decoy database search strategy and flexible mixture modeling. J Proteome Res 2008, 7:286-292.
    • (2008) J Proteome Res , vol.7 , pp. 286-292
    • Choi, H.1    Ghosh, D.2    Nesvizhskii, A.I.3
  • 190
    • 49549099563 scopus 로고    scopus 로고
    • Non-parametric estimation of posterior error probabilities associated with peptides identified by tandem mass spectrometry
    • Kall L., Storey J.D., Noble W.S. Non-parametric estimation of posterior error probabilities associated with peptides identified by tandem mass spectrometry. Bioinformatics 2008, 24:I42-I48.
    • (2008) Bioinformatics , vol.24
    • Kall, L.1    Storey, J.D.2    Noble, W.S.3
  • 191
    • 55249121202 scopus 로고    scopus 로고
    • Nonlinear fitting method for determining local false discovery rates from decoy database searches
    • Tang W.H., Shilov I.V., Seymour S.L. Nonlinear fitting method for determining local false discovery rates from decoy database searches. J Proteome Res 2008, 7:3661-3667.
    • (2008) J Proteome Res , vol.7 , pp. 3661-3667
    • Tang, W.H.1    Shilov, I.V.2    Seymour, S.L.3
  • 192
    • 40749116092 scopus 로고    scopus 로고
    • A nonparametric model for quality control of database search results in shotgun proteomics
    • Zhang J.Y., Li J.Q., Liu X., Xie H.W., Zhu Y.P., He F.C. A nonparametric model for quality control of database search results in shotgun proteomics. BMC Bioinform 2008, 9:29.
    • (2008) BMC Bioinform , vol.9 , pp. 29
    • Zhang, J.Y.1    Li, J.Q.2    Liu, X.3    Xie, H.W.4    Zhu, Y.P.5    He, F.C.6
  • 193
    • 63049091003 scopus 로고    scopus 로고
    • Bayesian nonparametric model for the validation of peptide identification in shotgun proteomics
    • Zhang J.Y., Ma J., Dou L., Wu S.F., Qian X.H., Xie H.W., et al. Bayesian nonparametric model for the validation of peptide identification in shotgun proteomics. Mol Cell Proteomics 2009, 8:547-557.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 547-557
    • Zhang, J.Y.1    Ma, J.2    Dou, L.3    Wu, S.F.4    Qian, X.H.5    Xie, H.W.6
  • 194
  • 196
    • 52649158232 scopus 로고    scopus 로고
    • Generalized method for probability-based peptide and protein identification from tandem mass spectrometry data and sequence database searching
    • Ramos-Fernandez A., Paradela A., Navajas R., Albar J.P. Generalized method for probability-based peptide and protein identification from tandem mass spectrometry data and sequence database searching. Mol Cell Proteomics 2008, 7:1748-1754.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 1748-1754
    • Ramos-Fernandez, A.1    Paradela, A.2    Navajas, R.3    Albar, J.P.4
  • 197
    • 1842423492 scopus 로고    scopus 로고
    • A computational method for assessing peptide-identification reliability in tandem mass spectrometry analysis with SEQUEST
    • Razumovskaya J., Olman V., Xu D., Uberbacher E.C., VerBerkmoes N.C., Hettich R.L., et al. A computational method for assessing peptide-identification reliability in tandem mass spectrometry analysis with SEQUEST. Proteomics 2004, 4:961-969.
    • (2004) Proteomics , vol.4 , pp. 961-969
    • Razumovskaya, J.1    Olman, V.2    Xu, D.3    Uberbacher, E.C.4    VerBerkmoes, N.C.5    Hettich, R.L.6
  • 199
    • 4444350538 scopus 로고    scopus 로고
    • Application of peptide LC retention time information in a discriminant function for peptide identification by tandem mass spectrometry
    • Strittmatter E.F., Kangas L.J., Petritis K., Mottaz H.M., Anderson G.A., Shen Y.F., et al. Application of peptide LC retention time information in a discriminant function for peptide identification by tandem mass spectrometry. J Proteome Res 2004, 3:760-769.
    • (2004) J Proteome Res , vol.3 , pp. 760-769
    • Strittmatter, E.F.1    Kangas, L.J.2    Petritis, K.3    Mottaz, H.M.4    Anderson, G.A.5    Shen, Y.F.6
  • 200
    • 14844360847 scopus 로고    scopus 로고
    • Probability-based evaluation of peptide and protein identifications from tandem mass spectrometry and SEQUEST analysis: the human proteome
    • Qian W.J., Liu T., Monroe M.E., Strittmatter E.F., Jacobs J.M., Kangas L.J., et al. Probability-based evaluation of peptide and protein identifications from tandem mass spectrometry and SEQUEST analysis: the human proteome. J Proteome Res 2005, 4:53-62.
    • (2005) J Proteome Res , vol.4 , pp. 53-62
    • Qian, W.J.1    Liu, T.2    Monroe, M.E.3    Strittmatter, E.F.4    Jacobs, J.M.5    Kangas, L.J.6
  • 201
    • 61349150487 scopus 로고    scopus 로고
    • Predictions of peptides' retention times in reversed-phase liquid chromatography as a new supportive tool to improve protein identification in proteomics
    • Baczek T., Kaliszan R. Predictions of peptides' retention times in reversed-phase liquid chromatography as a new supportive tool to improve protein identification in proteomics. Proteomics 2009, 9:835-847.
    • (2009) Proteomics , vol.9 , pp. 835-847
    • Baczek, T.1    Kaliszan, R.2
  • 202
    • 33748320788 scopus 로고    scopus 로고
    • Optimized peptide separation and identification for mass spectrometry based proteomics via free-flow electrophoresis
    • Malmstrom J., Lee H., Nesvizhskii A.I., Shteynberg D., Mohanty S., Brunner E., et al. Optimized peptide separation and identification for mass spectrometry based proteomics via free-flow electrophoresis. J Proteome Res 2006, 5:2241-2249.
    • (2006) J Proteome Res , vol.5 , pp. 2241-2249
    • Malmstrom, J.1    Lee, H.2    Nesvizhskii, A.I.3    Shteynberg, D.4    Mohanty, S.5    Brunner, E.6
  • 203
    • 1242329500 scopus 로고    scopus 로고
    • Gel based isoelectric focusing of peptides and the utility of isoelectric point in protein identification
    • Cargile B.J., Bundy J.L., Freeman T.W., Stephenson J.L. Gel based isoelectric focusing of peptides and the utility of isoelectric point in protein identification. J Proteome Res 2004, 3:112-119.
    • (2004) J Proteome Res , vol.3 , pp. 112-119
    • Cargile, B.J.1    Bundy, J.L.2    Freeman, T.W.3    Stephenson, J.L.4
  • 204
    • 20144383119 scopus 로고    scopus 로고
    • High throughput quantitative analysis of serum proteins using glycopeptide capture and liquid chromatography mass spectrometry
    • Zhang H., Yi E.C., Li X.J., Mallick P., Kelly-Spratt K.S., Masselon C.D., et al. High throughput quantitative analysis of serum proteins using glycopeptide capture and liquid chromatography mass spectrometry. Mol Cell Proteomics 2005, 4:144-155.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 144-155
    • Zhang, H.1    Yi, E.C.2    Li, X.J.3    Mallick, P.4    Kelly-Spratt, K.S.5    Masselon, C.D.6
  • 205
    • 29144480261 scopus 로고    scopus 로고
    • Added value for tandem mass spectrometry shotgun proteomics data validation through isoelectric focusing of peptides
    • Heller M., Ye M.L., Michel P.E., Morier P., Stalder D., Junger M.A., et al. Added value for tandem mass spectrometry shotgun proteomics data validation through isoelectric focusing of peptides. J Proteome Res 2005, 4:2273-2282.
    • (2005) J Proteome Res , vol.4 , pp. 2273-2282
    • Heller, M.1    Ye, M.L.2    Michel, P.E.3    Morier, P.4    Stalder, D.5    Junger, M.A.6
  • 206
    • 29244448703 scopus 로고    scopus 로고
    • Parts per million mass accuracy on an orbitrap mass spectrometer via lock mass injection into a C-trap
    • Olsen J.V., de Godoy L.M.F., Li G.Q., Macek B., Mortensen P., Pesch R., et al. Parts per million mass accuracy on an orbitrap mass spectrometer via lock mass injection into a C-trap. Mol Cell Proteomics 2005, 4:2010-2021.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 2010-2021
    • Olsen, J.V.1    de Godoy, L.M.F.2    Li, G.Q.3    Macek, B.4    Mortensen, P.5    Pesch, R.6
  • 207
    • 23944477893 scopus 로고    scopus 로고
    • Large scale analysis of MASCOT results using a mass ccuracy-based THreshold (MATH) effectively improves data interpretation
    • Rudnick P.A., Wang Y.J., Evans E., Lee C.S., Balgley B.M. Large scale analysis of MASCOT results using a mass ccuracy-based THreshold (MATH) effectively improves data interpretation. J Proteome Res 2005, 4:1353-1360.
    • (2005) J Proteome Res , vol.4 , pp. 1353-1360
    • Rudnick, P.A.1    Wang, Y.J.2    Evans, E.3    Lee, C.S.4    Balgley, B.M.5
  • 208
    • 76149104250 scopus 로고    scopus 로고
    • Target-decoy with mass binning: a simple and effective validation method for shotgun proteomics using high resolution mass spectrometry
    • Joo J.W.J., Na S., Baek J.H., Lee C., Paek E. Target-decoy with mass binning: a simple and effective validation method for shotgun proteomics using high resolution mass spectrometry. J Proteome Res 2010, 9:1150-1156.
    • (2010) J Proteome Res , vol.9 , pp. 1150-1156
    • Joo, J.W.J.1    Na, S.2    Baek, J.H.3    Lee, C.4    Paek, E.5
  • 209
    • 34547156610 scopus 로고    scopus 로고
    • A platform for accurate mass and time analyses of mass spectrometry data
    • May D., Fitzgibbon M., Liu Y., Holzman T., Eng J., Kemp C.J., et al. A platform for accurate mass and time analyses of mass spectrometry data. J Proteome Res 2007, 6:2685-2694.
    • (2007) J Proteome Res , vol.6 , pp. 2685-2694
    • May, D.1    Fitzgibbon, M.2    Liu, Y.3    Holzman, T.4    Eng, J.5    Kemp, C.J.6
  • 210
    • 77649174058 scopus 로고    scopus 로고
    • DtaRefinery, a software tool for elimination of systematic errors from parent ion mass measurements in tandem mass spectra data sets
    • Petyuk V.A., Mayampurath A.M., Monroe M.E., Polpitiya A.D., Purvine S.O., Anderson G.A., et al. DtaRefinery, a software tool for elimination of systematic errors from parent ion mass measurements in tandem mass spectra data sets. Mol Cell Proteomics 2010, 9:486-496.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 486-496
    • Petyuk, V.A.1    Mayampurath, A.M.2    Monroe, M.E.3    Polpitiya, A.D.4    Purvine, S.O.5    Anderson, G.A.6
  • 211
    • 48949099046 scopus 로고    scopus 로고
    • Increasing information from shotgun proteomic data by accounting for misassigned precursor ion masses
    • Scherl A., Tsai Y.S., Shaffer S.A., Goodlett D.R. Increasing information from shotgun proteomic data by accounting for misassigned precursor ion masses. Proteomics 2008, 8:2791-2797.
    • (2008) Proteomics , vol.8 , pp. 2791-2797
    • Scherl, A.1    Tsai, Y.S.2    Shaffer, S.A.3    Goodlett, D.R.4
  • 212
    • 46749089668 scopus 로고    scopus 로고
    • Postexperiment monoisotopic mass filtering and refinement (PE-MMR) of tandem mass spectrometric data increases accuracy of peptide identification in LC/MS/MS
    • Shin B., Jung H.J., Hyung S.W., Kim H., Lee D., Lee C., et al. Postexperiment monoisotopic mass filtering and refinement (PE-MMR) of tandem mass spectrometric data increases accuracy of peptide identification in LC/MS/MS. Mol Cell Proteomics 2008, 7:1124-1134.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 1124-1134
    • Shin, B.1    Jung, H.J.2    Hyung, S.W.3    Kim, H.4    Lee, D.5    Lee, C.6
  • 213
    • 68549125514 scopus 로고    scopus 로고
    • Improving peptide identification in proteome analysis by a two-dimensional retention time filtering approach
    • Pfeifer N., Leinenbach A., Huber C.G., Kohlbacher O. Improving peptide identification in proteome analysis by a two-dimensional retention time filtering approach. J Proteome Res 2009, 8:4109-4115.
    • (2009) J Proteome Res , vol.8 , pp. 4109-4115
    • Pfeifer, N.1    Leinenbach, A.2    Huber, C.G.3    Kohlbacher, O.4
  • 214
    • 34548041670 scopus 로고    scopus 로고
    • Improving tandem mass spectrum identification using peptide retention time prediction across diverse chromatography conditions
    • Klammer A.A., Yi X.H., MacCoss M.J., Noble W.S. Improving tandem mass spectrum identification using peptide retention time prediction across diverse chromatography conditions. Anal Chem 2007, 79:6111-6118.
    • (2007) Anal Chem , vol.79 , pp. 6111-6118
    • Klammer, A.A.1    Yi, X.H.2    MacCoss, M.J.3    Noble, W.S.4
  • 215
    • 35748972060 scopus 로고    scopus 로고
    • Semi-supervised learning for peptide identification from shotgun proteomics datasets
    • Kall L., Canterbury J.D., Weston J., Noble W.S., MacCoss M.J. Semi-supervised learning for peptide identification from shotgun proteomics datasets. Nat Meth 2007, 4:923-925.
    • (2007) Nat Meth , vol.4 , pp. 923-925
    • Kall, L.1    Canterbury, J.D.2    Weston, J.3    Noble, W.S.4    MacCoss, M.J.5
  • 216
    • 67049118923 scopus 로고    scopus 로고
    • Accurate and sensitive peptide identification with mascot percolator
    • Brosch M., Yu L., Hubbard T., Choudhary J. Accurate and sensitive peptide identification with mascot percolator. J Proteome Res 2009, 8:3176-3181.
    • (2009) J Proteome Res , vol.8 , pp. 3176-3181
    • Brosch, M.1    Yu, L.2    Hubbard, T.3    Choudhary, J.4
  • 217
    • 77952038093 scopus 로고    scopus 로고
    • MUDE: a new approach for optimizing sensitivity in the target-decoy search strategy for large-scale peptide/protein identification
    • Cerqueira F.R., Graber A., Schwikowski B., Baumgartner C. MUDE: a new approach for optimizing sensitivity in the target-decoy search strategy for large-scale peptide/protein identification. J Proteome Res 2010, 9:2265-2277.
    • (2010) J Proteome Res , vol.9 , pp. 2265-2277
    • Cerqueira, F.R.1    Graber, A.2    Schwikowski, B.3    Baumgartner, C.4
  • 218
    • 49849101216 scopus 로고    scopus 로고
    • Linear discriminant analysis-based estimation of the false discovery rate for phosphopeptide identifications
    • Du X., Yang F., Manes N.P., Stenoien D.L., Monroe M.E., Adkins J.N., et al. Linear discriminant analysis-based estimation of the false discovery rate for phosphopeptide identifications. J Proteome Res 2008, 7:2195-2203.
    • (2008) J Proteome Res , vol.7 , pp. 2195-2203
    • Du, X.1    Yang, F.2    Manes, N.P.3    Stenoien, D.L.4    Monroe, M.E.5    Adkins, J.N.6
  • 219
    • 34249316472 scopus 로고    scopus 로고
    • Estimating the statistical significance of peptide identifications from shotgun proteomics experiments
    • Higgs R.E., Knierman M.D., BonnerFreeman A., Gelbert L.M., Patil S.T., Hale J.E. Estimating the statistical significance of peptide identifications from shotgun proteomics experiments. J Proteome Res 2007, 6:1758-1767.
    • (2007) J Proteome Res , vol.6 , pp. 1758-1767
    • Higgs, R.E.1    Knierman, M.D.2    BonnerFreeman, A.3    Gelbert, L.M.4    Patil, S.T.5    Hale, J.E.6
  • 220
    • 33746930864 scopus 로고    scopus 로고
    • A uniform proteomics MS/MS analysis platform utilizing open XML file formats. Mol Syst Biol :msb4100024-E1-msb-E8
    • Keller A, Eng J, Zhang N, Li X-J, Aebersold R. A uniform proteomics MS/MS analysis platform utilizing open XML file formats. Mol Syst Biol 2005;1:msb4100024-E1-msb-E8.
    • (2005) , vol.1
    • Keller, A.1    Eng, J.2    Zhang, N.3    Li, X-J.4    Aebersold, R.5
  • 221
    • 53049093468 scopus 로고    scopus 로고
    • Enhancing peptide identification confidence by combining search methods
    • Alves G., Wu W.W., Wang G.H., Shen R.F., Yu Y.K. Enhancing peptide identification confidence by combining search methods. J Proteome Res 2008, 7:3102-3113.
    • (2008) J Proteome Res , vol.7 , pp. 3102-3113
    • Alves, G.1    Wu, W.W.2    Wang, G.H.3    Shen, R.F.4    Yu, Y.K.5
  • 222
    • 63049120021 scopus 로고    scopus 로고
    • Improving sensitivity in proteome studies by analysis of false discovery rates for multiple search engines
    • Jones A.R., Siepen J.A., Hubbard S.J., Paton N.W. Improving sensitivity in proteome studies by analysis of false discovery rates for multiple search engines. Proteomics 2009, 9:1220-1229.
    • (2009) Proteomics , vol.9 , pp. 1220-1229
    • Jones, A.R.1    Siepen, J.A.2    Hubbard, S.J.3    Paton, N.W.4
  • 224
    • 3042815334 scopus 로고    scopus 로고
    • Trypsin cleaves exclusively C-terminal to arginine and lysine residues
    • Olsen J.V., Ong S.E., Mann M. Trypsin cleaves exclusively C-terminal to arginine and lysine residues. Mol Cell Proteomics 2004, 3:608-614.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 608-614
    • Olsen, J.V.1    Ong, S.E.2    Mann, M.3
  • 225
    • 34848903890 scopus 로고    scopus 로고
    • The implications of proteolytic background for shotgun proteomics
    • Picotti P., Aebersold R., Domon B. The implications of proteolytic background for shotgun proteomics. Mol Cell Proteomics 2007, 6:1589-1598.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1589-1598
    • Picotti, P.1    Aebersold, R.2    Domon, B.3
  • 226
    • 58149299336 scopus 로고    scopus 로고
    • Significance analysis of spectral count data in label-free shotgun proteomics
    • Choi H., Fermin D., Nesvizhskii A.I. Significance analysis of spectral count data in label-free shotgun proteomics. Mol Cell Proteomics 2008, 7:2373-2385.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 2373-2385
    • Choi, H.1    Fermin, D.2    Nesvizhskii, A.I.3
  • 227
    • 0036470450 scopus 로고    scopus 로고
    • What does it mean to identify a protein in proteomics?
    • Rappsilber J., Mann M. What does it mean to identify a protein in proteomics?. Trends Biochem Sci 2002, 27:74-78.
    • (2002) Trends Biochem Sci , vol.27 , pp. 74-78
    • Rappsilber, J.1    Mann, M.2
  • 228
    • 1542617945 scopus 로고    scopus 로고
    • Statistical models for protein validation using tandem mass spectral data and protein amino acid sequence databases
    • Sadygov R.G., Liu H.B., Yates J.R. Statistical models for protein validation using tandem mass spectral data and protein amino acid sequence databases. Anal Chem 2004, 76:1664-1671.
    • (2004) Anal Chem , vol.76 , pp. 1664-1671
    • Sadygov, R.G.1    Liu, H.B.2    Yates, J.R.3
  • 229
    • 77955463487 scopus 로고    scopus 로고
    • Protein and gene model inference based on statistical modeling in k-partite graphs
    • Gerster S., Qeli E., Ahrens C.H., Buhlmann P. Protein and gene model inference based on statistical modeling in k-partite graphs. Proc Natl Acad Sci USA 2010, 107:12101-12106.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 12101-12106
    • Gerster, S.1    Qeli, E.2    Ahrens, C.H.3    Buhlmann, P.4
  • 230
    • 38349166945 scopus 로고    scopus 로고
    • A hierarchical statistical model to assess the confidence of peptides and proteins inferred from tandem mass spectrometry
    • Shen C.Y., Wang Z.P., Shankar G., Zhang X., Li L. A hierarchical statistical model to assess the confidence of peptides and proteins inferred from tandem mass spectrometry. Bioinformatics 2008, 24:202-208.
    • (2008) Bioinformatics , vol.24 , pp. 202-208
    • Shen, C.Y.1    Wang, Z.P.2    Shankar, G.3    Zhang, X.4    Li, L.5
  • 231
    • 77955459838 scopus 로고    scopus 로고
    • A nested mixture model for protein identification using mass spectrometry
    • Li Q., MacCoss M.J., Stephens M. A nested mixture model for protein identification using mass spectrometry. Ann Appl Stat 2010, 4:962-987.
    • (2010) Ann Appl Stat , vol.4 , pp. 962-987
    • Li, Q.1    MacCoss, M.J.2    Stephens, M.3
  • 232
    • 34249047337 scopus 로고    scopus 로고
    • Probability model for assessing proteins assembled from peptide sequences inferred from tandem mass spectrometry data
    • Feng J., Naiman D.Q., Cooper B. Probability model for assessing proteins assembled from peptide sequences inferred from tandem mass spectrometry data. Anal Chem 2007, 79:3901-3911.
    • (2007) Anal Chem , vol.79 , pp. 3901-3911
    • Feng, J.1    Naiman, D.Q.2    Cooper, B.3
  • 233
    • 51349096085 scopus 로고    scopus 로고
    • Improved ranking functions for protein and modification-site identifications
    • Bern M., Goldberg D. Improved ranking functions for protein and modification-site identifications. J Comput Biol 2008, 15:705-719.
    • (2008) J Comput Biol , vol.15 , pp. 705-719
    • Bern, M.1    Goldberg, D.2
  • 234
    • 70349912263 scopus 로고    scopus 로고
    • False discovery rates of protein identifications: a strike against the two-peptide rule
    • Gupta N., Pevzner P.A. False discovery rates of protein identifications: a strike against the two-peptide rule. J Proteome Res 2009, 8:4173-4181.
    • (2009) J Proteome Res , vol.8 , pp. 4173-4181
    • Gupta, N.1    Pevzner, P.A.2
  • 235
    • 33846133955 scopus 로고    scopus 로고
    • EComputational prediction of proteotypic peptides for quantitative proteomics
    • Mallick P., Schirle M., Chen S.S., Flory M.R., Lee H., Martin D., et al. eComputational prediction of proteotypic peptides for quantitative proteomics. Nat Biotechnol 2007, 25:125-131.
    • (2007) Nat Biotechnol , vol.25 , pp. 125-131
    • Mallick, P.1    Schirle, M.2    Chen, S.S.3    Flory, M.R.4    Lee, H.5    Martin, D.6
  • 236
    • 69249122100 scopus 로고    scopus 로고
    • Network-assisted protein identification and data interpretation in shotgun proteomics
    • Li J., Zimmerman L.J., Park B.H., Tabb D.L., Liebler D.C., Zhang B. Network-assisted protein identification and data interpretation in shotgun proteomics. Mol Syst Biol 2009, 5:303.
    • (2009) Mol Syst Biol , vol.5 , pp. 303
    • Li, J.1    Zimmerman, L.J.2    Park, B.H.3    Tabb, D.L.4    Liebler, D.C.5    Zhang, B.6
  • 238
    • 65649152557 scopus 로고    scopus 로고
    • Integrating shotgun proteomics and mRNA expression data to improve protein identification
    • Ramakrishnan S.R., Vogel C., Prince J.T., Li Z.H., Penalva L.O., Myers M., et al. Integrating shotgun proteomics and mRNA expression data to improve protein identification. Bioinformatics 2009, 25:1397-1403.
    • (2009) Bioinformatics , vol.25 , pp. 1397-1403
    • Ramakrishnan, S.R.1    Vogel, C.2    Prince, J.T.3    Li, Z.H.4    Penalva, L.O.5    Myers, M.6
  • 239
    • 54049090766 scopus 로고    scopus 로고
    • Selected reaction monitoring for quantitative proteomics: a tutorial
    • Lange V., Picotti P., Domon B., Aebersold R. Selected reaction monitoring for quantitative proteomics: a tutorial. Mol Syst Biol 2008, 4:422.
    • (2008) Mol Syst Biol , vol.4 , pp. 422
    • Lange, V.1    Picotti, P.2    Domon, B.3    Aebersold, R.4
  • 241
    • 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., Mann M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat Biotechnol 2008, 26:1367-1372.
    • (2008) Nat Biotechnol , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 242
    • 68549092907 scopus 로고    scopus 로고
    • IDPicker 2.0: improved protein assembly with high discrimination peptide identification filtering
    • Ma Z.Q., Dasari S., Chambers M.C., Litton M.D., Sobecki S.M., Zimmerman L.J., et al. IDPicker 2.0: improved protein assembly with high discrimination peptide identification filtering. J Proteome Res 2009, 8:3872-3881.
    • (2009) J Proteome Res , vol.8 , pp. 3872-3881
    • Ma, Z.Q.1    Dasari, S.2    Chambers, M.C.3    Litton, M.D.4    Sobecki, S.M.5    Zimmerman, L.J.6
  • 243
    • 77957223908 scopus 로고    scopus 로고
    • Efficient marginalization to compute protein posterior probabilities from shotgun mass spectrometry data. J Proteome Res in press. [pmid: 20712337].
    • Serang O, MacCoss MJ, Noble WS. Efficient marginalization to compute protein posterior probabilities from shotgun mass spectrometry data. J Proteome Res in press. [pmid: 20712337].
    • Serang, O.1    MacCoss, M.J.2    Noble, W.S.3
  • 244
    • 34249826390 scopus 로고    scopus 로고
    • Protein identification by spectral networks analysis
    • Bandeira N., Tsur D., Frank A., Pevzner P.A. Protein identification by spectral networks analysis. Pnas 2007, 104:6140-6145.
    • (2007) Pnas , vol.104 , pp. 6140-6145
    • Bandeira, N.1    Tsur, D.2    Frank, A.3    Pevzner, P.A.4
  • 245
    • 36048937342 scopus 로고    scopus 로고
    • Tandem mass spectrometry for the detection of plant pathogenic fungi and the effects of database composition on protein inferences
    • Padliya N.D., Garrett W.M., Campbell K.B., Tabb D.L., Cooper B. Tandem mass spectrometry for the detection of plant pathogenic fungi and the effects of database composition on protein inferences. Proteomics 2007, 7:3932-3942.
    • (2007) Proteomics , vol.7 , pp. 3932-3942
    • Padliya, N.D.1    Garrett, W.M.2    Campbell, K.B.3    Tabb, D.L.4    Cooper, B.5
  • 246
    • 70149084269 scopus 로고    scopus 로고
    • Deterministic protein inference for shotgun proteomics data provides new insights into Arabidopsis pollen development and function
    • Grobei M.A., Qeli E., Brunner E., Rehrauer H., Zhang R.X., Roschitzki B., et al. Deterministic protein inference for shotgun proteomics data provides new insights into Arabidopsis pollen development and function. Genome Res 2009, 19:1786-1800.
    • (2009) Genome Res , vol.19 , pp. 1786-1800
    • Grobei, M.A.1    Qeli, E.2    Brunner, E.3    Rehrauer, H.4    Zhang, R.X.5    Roschitzki, B.6
  • 247
    • 44849103670 scopus 로고    scopus 로고
    • Interpretation of large-scale quantitative shotgun proteomic profiles for biomarker discovery
    • Isserlin R., Emili A. Interpretation of large-scale quantitative shotgun proteomic profiles for biomarker discovery. Curr Opin Mol Ther 2008, 10:231-242.
    • (2008) Curr Opin Mol Ther , vol.10 , pp. 231-242
    • Isserlin, R.1    Emili, A.2
  • 250
    • 72149093828 scopus 로고    scopus 로고
    • Protein identification false discovery rates for very large proteomics data sets generated by tandem mass spectrometry
    • Reiter L., Claassen M., Schrimpf S.P., Jovanovic M., Schmidt A., Buhmann J.M., et al. Protein identification false discovery rates for very large proteomics data sets generated by tandem mass spectrometry. Mol Cell Proteomics 2009, 8:2405-2417.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2405-2417
    • Reiter, L.1    Claassen, M.2    Schrimpf, S.P.3    Jovanovic, M.4    Schmidt, A.5    Buhmann, J.M.6
  • 251
    • 76149098839 scopus 로고    scopus 로고
    • Unbiased statistical analysis for multi-stage proteomic search strategies
    • Everett L.J., Bierl C., Master S.R. Unbiased statistical analysis for multi-stage proteomic search strategies. J Proteome Res 2010, 9:700-707.
    • (2010) J Proteome Res , vol.9 , pp. 700-707
    • Everett, L.J.1    Bierl, C.2    Master, S.R.3
  • 252
    • 64849106343 scopus 로고    scopus 로고
    • Phosphoproteomics: miles to go before its routine
    • Piggee C. Phosphoproteomics: miles to go before its routine. Anal Chem 2009, 81:2418-2420.
    • (2009) Anal Chem , vol.81 , pp. 2418-2420
    • Piggee, C.1
  • 253
    • 74049120875 scopus 로고    scopus 로고
    • Phosphoproteomics by mass spectrometry: insights, implications, applications and limitations
    • Mayya V., Han D.K. Phosphoproteomics by mass spectrometry: insights, implications, applications and limitations. Expert Rev Proteomics 2009, 6:605-618.
    • (2009) Expert Rev Proteomics , vol.6 , pp. 605-618
    • Mayya, V.1    Han, D.K.2
  • 254
    • 33847616949 scopus 로고    scopus 로고
    • Reproducible isolation of distinct, overlapping segments of the phosphoproteome. Nat Methods
    • Bodenmiller B, Mueller LN, Mueller M, Domon B, Aebersold R. Reproducible isolation of distinct, overlapping segments of the phosphoproteome. Nat Methods 2007;4:231-7.
    • (2007) , vol.4 , pp. 231-7
    • Bodenmiller, B.1    Mueller, L.N.2    Mueller, M.3    Domon, B.4    Aebersold, R.5
  • 255
    • 31644439146 scopus 로고    scopus 로고
    • Phosphorylation analysis by mass spectrometry: myths, facts, and the consequences for qualitative and quantitative measurements
    • Steen H., Jebanathirajah J.A., Rush J., Morrice N., Kirschner M.W. Phosphorylation analysis by mass spectrometry: myths, facts, and the consequences for qualitative and quantitative measurements. Mol Cell Proteomics 2006, 5:172-181.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 172-181
    • Steen, H.1    Jebanathirajah, J.A.2    Rush, J.3    Morrice, N.4    Kirschner, M.W.5
  • 256
    • 49549116189 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of signaling network dynamics
    • White F.M. Quantitative phosphoproteomic analysis of signaling network dynamics. Curr Opin Biotechnol 2008, 19:404-409.
    • (2008) Curr Opin Biotechnol , vol.19 , pp. 404-409
    • White, F.M.1
  • 257
    • 39049088086 scopus 로고    scopus 로고
    • Investigating MS2/MS3 matching statistics: a model for coupling consecutive stage mass spectrometry data for increased peptide identification confidence
    • Ulintz P.J., Bodenmiller B., Andrews P.C., Aebersold R., Nesvizhskii A.I. Investigating MS2/MS3 matching statistics: a model for coupling consecutive stage mass spectrometry data for increased peptide identification confidence. Mol Cell Proteomics 2008, 7:71-87.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 71-87
    • Ulintz, P.J.1    Bodenmiller, B.2    Andrews, P.C.3    Aebersold, R.4    Nesvizhskii, A.I.5
  • 259
    • 68549104477 scopus 로고    scopus 로고
    • Increased confidence in large-scale phosphoproteomics data by complementary mass spectrometric techniques and matching of phosphopeptide data sets
    • Alcolea M.P., Kleiner O., Cutillas P.R. Increased confidence in large-scale phosphoproteomics data by complementary mass spectrometric techniques and matching of phosphopeptide data sets. J Proteome Res 2009, 8:3808-3815.
    • (2009) J Proteome Res , vol.8 , pp. 3808-3815
    • Alcolea, M.P.1    Kleiner, O.2    Cutillas, P.R.3
  • 262
    • 33749853607 scopus 로고    scopus 로고
    • A probability-based approach for high-throughput protein phosphorylation analysis and site localization
    • Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol 2006, 24:1285-1292.
    • (2006) Nat Biotechnol , vol.24 , pp. 1285-1292
    • Beausoleil, S.A.1    Villen, J.2    Gerber, S.A.3    Rush, J.4    Gygi, S.P.5
  • 263
    • 51649090664 scopus 로고    scopus 로고
    • PhosphoScore: an open-source phosphorylation site assignment tool for MSn data
    • Ruttenberg B.E., Pisitkun T., Knepper M.A., Hoffert J.D. PhosphoScore: an open-source phosphorylation site assignment tool for MSn data. J Proteome Res 2008, 7:3054-3059.
    • (2008) J Proteome Res , vol.7 , pp. 3054-3059
    • Ruttenberg, B.E.1    Pisitkun, T.2    Knepper, M.A.3    Hoffert, J.D.4
  • 264
    • 33646907086 scopus 로고    scopus 로고
    • Reporting protein identification data - the next generation of guidelines
    • Bradshaw R.A., Burlingame A.L., Carr S., Aebersold R. Reporting protein identification data - the next generation of guidelines. Mol Cell Proteomics 2006, 5:787-788.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 787-788
    • Bradshaw, R.A.1    Burlingame, A.L.2    Carr, S.3    Aebersold, R.4
  • 265
    • 33845902530 scopus 로고    scopus 로고
    • Overcoming the dynamic range problem in mass spectrometry-based shotgun proteomics
    • Wu L., Han D.K. Overcoming the dynamic range problem in mass spectrometry-based shotgun proteomics. Expert Rev Proteomics 2006, 3:611-619.
    • (2006) Expert Rev Proteomics , vol.3 , pp. 611-619
    • Wu, L.1    Han, D.K.2
  • 266
    • 14344257790 scopus 로고    scopus 로고
    • Detection and localization of protein modifications by high resolution tandem mass spectrometry
    • Meng F.Y., Forbes A.J., Miller L.M., Kelleher N.L. Detection and localization of protein modifications by high resolution tandem mass spectrometry. Mass Spectrom Rev 2005, 24:126-134.
    • (2005) Mass Spectrom Rev , vol.24 , pp. 126-134
    • Meng, F.Y.1    Forbes, A.J.2    Miller, L.M.3    Kelleher, N.L.4
  • 267
    • 33645453254 scopus 로고    scopus 로고
    • Global landscape of protein complexes in the yeast Saccharomyces cerevisiae
    • Krogan N.J., Cagney G., Yu H., Zhong G., Guo X., Ignatchenko A., et al. Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Nature 2006, 440:637-643.
    • (2006) Nature , vol.440 , pp. 637-643
    • Krogan, N.J.1    Cagney, G.2    Yu, H.3    Zhong, G.4    Guo, X.5    Ignatchenko, A.6
  • 268
    • 33749615256 scopus 로고    scopus 로고
    • CHEMISTRY: mass spectrometry: bottom-up or top-down?
    • Chait B.T. CHEMISTRY: mass spectrometry: bottom-up or top-down?. Science 2006, 314:65-66.
    • (2006) Science , vol.314 , pp. 65-66
    • Chait, B.T.1
  • 269
    • 74249106136 scopus 로고    scopus 로고
    • What Does the Future Hold for Top Down Mass Spectrometry?
    • Garcia B.A. What Does the Future Hold for Top Down Mass Spectrometry?. J Am Soc Mass Spectrom 2010, 21:193-202.
    • (2010) J Am Soc Mass Spectrom , vol.21 , pp. 193-202
    • Garcia, B.A.1
  • 270
    • 13844319908 scopus 로고    scopus 로고
    • PepNovo: de novo peptide sequencing via probabilistic network modeling
    • Frank A., Pevzner P. PepNovo: de novo peptide sequencing via probabilistic network modeling. Anal Chem 2005, 77:964-973.
    • (2005) Anal Chem , vol.77 , pp. 964-973
    • Frank, A.1    Pevzner, P.2
  • 272
    • 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
  • 273
    • 0033565832 scopus 로고    scopus 로고
    • Role of accurate mass measurement (+/-10ppm) in protein identification strategies employing MS or MS MS and database searching
    • Clauser K.R., Baker P., Burlingame A.L. Role of accurate mass measurement (+/-10ppm) in protein identification strategies employing MS or MS MS and database searching. Anal Chem 1999, 71:2871-2882.
    • (1999) Anal Chem , vol.71 , pp. 2871-2882
    • Clauser, K.R.1    Baker, P.2    Burlingame, A.L.3
  • 274
    • 0036808207 scopus 로고    scopus 로고
    • ProbID: a probabilistic algorithm to identify peptides through sequence database searching using tandem mass spectral data
    • Zhang N., Aebersold R., Schwilkowski B. ProbID: a probabilistic algorithm to identify peptides through sequence database searching using tandem mass spectral data. Proteomics 2002, 2:1406-1412.
    • (2002) Proteomics , vol.2 , pp. 1406-1412
    • Zhang, N.1    Aebersold, R.2    Schwilkowski, B.3
  • 275
    • 0041358793 scopus 로고    scopus 로고
    • OLAV: towards high-throughput tandem mass spectrometry data identification
    • Colinge J., Masselot A., Giron M., Dessingy T., Magnin J. OLAV: towards high-throughput tandem mass spectrometry data identification. Proteomics 2003, 3:1454-1463.
    • (2003) Proteomics , vol.3 , pp. 1454-1463
    • Colinge, J.1    Masselot, A.2    Giron, M.3    Dessingy, T.4    Magnin, J.5
  • 276
    • 29144535689 scopus 로고    scopus 로고
    • VEMS 3.0: algorithms and computational tools for tandem mass spectrometry based identification of post-translational modifications in proteins
    • Matthiesen R., Trelle M.B., Hojrup P., Bunkenborg J., Jensen O.N. VEMS 3.0: algorithms and computational tools for tandem mass spectrometry based identification of post-translational modifications in proteins. J Proteome Res 2005, 4:2338-2347.
    • (2005) J Proteome Res , vol.4 , pp. 2338-2347
    • Matthiesen, R.1    Trelle, M.B.2    Hojrup, P.3    Bunkenborg, J.4    Jensen, O.N.5
  • 277
    • 33847401893 scopus 로고    scopus 로고
    • MyriMatch: highly accurate tandem mass spectral peptide identification by multivariate hypergeometric analysis
    • Tabb D.L., Fernando C.G., Chambers M.C. MyriMatch: highly accurate tandem mass spectral peptide identification by multivariate hypergeometric analysis. J Proteome Res 2007, 6:654-661.
    • (2007) J Proteome Res , vol.6 , pp. 654-661
    • Tabb, D.L.1    Fernando, C.G.2    Chambers, M.C.3
  • 278
    • 51649094314 scopus 로고    scopus 로고
    • Monte Carlo simulation-based algorithms for analysis of shotgun proteomic data
    • Xu H., Freitas M.A. Monte Carlo simulation-based algorithms for analysis of shotgun proteomic data. J Proteome Res 2008, 7:2605-2615.
    • (2008) J Proteome Res , vol.7 , pp. 2605-2615
    • Xu, H.1    Freitas, M.A.2
  • 279
    • 27544511899 scopus 로고    scopus 로고
    • InsPecT: identification of posttransiationally modified peptides from tandem mass spectra
    • Tanner S., Shu H.J., Frank A., Wang L.C., Zandi E., Mumby M., et al. InsPecT: identification of posttransiationally modified peptides from tandem mass spectra. Anal Chem 2005, 77:4626-4639.
    • (2005) Anal Chem , vol.77 , pp. 4626-4639
    • Tanner, S.1    Shu, H.J.2    Frank, A.3    Wang, L.C.4    Zandi, E.5    Mumby, M.6
  • 280
    • 0038047148 scopus 로고    scopus 로고
    • Popitam: towards new heuristic strategies to improve protein identification from tandem mass spectrometry data
    • Hernandez P., Gras R., Frey J., Appel R.D. Popitam: towards new heuristic strategies to improve protein identification from tandem mass spectrometry data. Proteomics 2003, 3:870-878.
    • (2003) Proteomics , vol.3 , pp. 870-878
    • Hernandez, P.1    Gras, R.2    Frey, J.3    Appel, R.D.4
  • 281
    • 21244443812 scopus 로고    scopus 로고
    • The use of proteotypic peptide libraries for protein identification
    • Craig R., Cortens J.P., Beavis R.C. The use of proteotypic peptide libraries for protein identification. Rapid Commun Mass Spectrom 2005, 19:1844-1850.
    • (2005) Rapid Commun Mass Spectrom , vol.19 , pp. 1844-1850
    • Craig, R.1    Cortens, J.P.2    Beavis, R.C.3
  • 282
    • 77949695293 scopus 로고    scopus 로고
    • Scaffold: a bioinformatic tool for validating MS/MS-based proteomic studies
    • Searle B.C. Scaffold: a bioinformatic tool for validating MS/MS-based proteomic studies. Proteomics 2010, 10:1265-1269.
    • (2010) Proteomics , vol.10 , pp. 1265-1269
    • Searle, B.C.1
  • 283
    • 77955595309 scopus 로고    scopus 로고
    • MassSieve: panning MS/MS peptide data for proteins
    • Slotta D.J., McFarland M.A., Markey S.P. MassSieve: panning MS/MS peptide data for proteins. Proteomics 2010, 10:3035-3039.
    • (2010) Proteomics , vol.10 , pp. 3035-3039
    • Slotta, D.J.1    McFarland, M.A.2    Markey, S.P.3
  • 284
    • 77954502710 scopus 로고    scopus 로고
    • PeptideClassifier for protein inference and targeted quantitative proteomics
    • Qeli E., Ahrens C.H. PeptideClassifier for protein inference and targeted quantitative proteomics. Nat Biotech 2010, 28:647-650.
    • (2010) Nat Biotech , vol.28 , pp. 647-650
    • Qeli, E.1    Ahrens, C.H.2
  • 285
    • 67049100049 scopus 로고    scopus 로고
    • The Proteios Software Environment: an extensible multiuser platform for management and analysis of proteomics data
    • Hakkinen J., Vincic G., Mansson O., Warell K., Levander F. The Proteios Software Environment: an extensible multiuser platform for management and analysis of proteomics data. J Proteome Res 2009, 8:3037-3043.
    • (2009) J Proteome Res , vol.8 , pp. 3037-3043
    • Hakkinen, J.1    Vincic, G.2    Mansson, O.3    Warell, K.4    Levander, F.5
  • 286
    • 30744438115 scopus 로고    scopus 로고
    • Computational Proteomics Analysis System (CPAS): an extensible, open-source analytic system for evaluating and publishing proteomic data and high throughput biological experiments
    • Rauch A., Bellew M., Eng J., Fitzgibbon M., Holzman T., Hussey P., et al. Computational Proteomics Analysis System (CPAS): an extensible, open-source analytic system for evaluating and publishing proteomic data and high throughput biological experiments. J Proteome Res 2006, 5:112-121.
    • (2006) J Proteome Res , vol.5 , pp. 112-121
    • Rauch, A.1    Bellew, M.2    Eng, J.3    Fitzgibbon, M.4    Holzman, T.5    Hussey, P.6
  • 288
    • 67650479361 scopus 로고    scopus 로고
    • NCBI Peptidome: a new public repository for mass spectrometry peptide identifications
    • Slotta D.J., Barrett T., Edgar R. NCBI Peptidome: a new public repository for mass spectrometry peptide identifications. Nat Biotechnol 2009, 27:600-601.
    • (2009) Nat Biotechnol , vol.27 , pp. 600-601
    • Slotta, D.J.1    Barrett, T.2    Edgar, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.