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Volumn 43, Issue 3, 2012, Pages 1087-1108

Current challenges in software solutions for mass spectrometry-based quantitative proteomics

Author keywords

Label free; LC MS; Quantification software; Quantitative proteomics; Stable isotope labeling

Indexed keywords

DEUTERIUM; PEPTIDE; PROLINE;

EID: 84867045160     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-012-1289-8     Document Type: Review
Times cited : (95)

References (173)
  • 1
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • DOI 10.1038/nature01511
    • Aebersold R, Mann M (2003) Mass spectrometry-based proteomics. Nature 422:198-207 (Pubitemid 36362757)
    • (2003) Nature , vol.422 , Issue.6928 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 2
    • 70449331436 scopus 로고    scopus 로고
    • UniMaP: Finding unique mass and peptide signatures in the human proteome
    • doi:10.1093/bioinformatics/btp 516
    • Alexandridou A, Tsangaris GT, VougasKet al (2009) UniMaP: finding unique mass and peptide signatures in the human proteome. Bioinformatics 25:3035-3037. doi:10.1093/bioinformatics/btp 516
    • (2009) Bioinformatics , vol.25 , pp. 3035-3037
    • Alexandridou, A.1    Tsangaris, G.T.2    Vougas, K.3
  • 3
    • 40549107755 scopus 로고    scopus 로고
    • Comparative LC-MS: A landscape of peaks and valleys
    • DOI 10.1002/pmic.200700694
    • America AHP, Cordewener JHG (2008) Comparative LC-MS: a landscape of peaks and valleys. Proteomics 8:731-749. doi: 10.1002/pmic.200700694 (Pubitemid 351362933)
    • (2008) Proteomics , vol.8 , Issue.4 , pp. 731-749
    • America, A.H.P.1    Cordewener, J.H.G.2
  • 4
    • 0242485239 scopus 로고    scopus 로고
    • A universal denoising and peak picking algorithm for lc-ms based on matched filtration in the chromatographic time domain
    • DOI 10.1021/ac0301806
    • Andreev VP, Rejtar T, Chen H-S et al (2003) A universal denoising and peak picking algorithm for LC-MS based on matched filtration in the chromatographic time domain. Anal Chem 75:6314-6326. doi:10.1021/ac0301806 (Pubitemid 37420627)
    • (2003) Analytical Chemistry , vol.75 , Issue.22 , pp. 6314-6326
    • Andreev, V.P.1    Rejtar, T.2    Chen, H.-S.3    Moskovets, E.V.4    Ivanov, A.R.5    Karger, B.L.6
  • 5
    • 0038574979 scopus 로고    scopus 로고
    • Ion suppression in mass spectrometry
    • DOI 10.1373/49.7.1041
    • Annesley TM (2003) Ion suppression in mass spectrometry. Clin Chem 49:1041-1044 (Pubitemid 36751088)
    • (2003) Clinical Chemistry , vol.49 , Issue.7 , pp. 1041-1044
    • Annesley, T.M.1
  • 6
    • 26544479794 scopus 로고
    • The 1995 update to the atomic mass evaluation
    • Audi G, Wapstra A (1995) The 1995 update to the atomic mass evaluation. Nucl Phys A 595:409-480
    • (1995) Nucl Phys A , vol.595 , pp. 409-480
    • Audi, G.1    Wapstra, A.2
  • 7
    • 77956520064 scopus 로고    scopus 로고
    • Proteome-wide protein concentrations in the human heart
    • doi:10.1039/c004495d
    • Aye TT, Scholten A, Taouatas N et al (2010) Proteome-wide protein concentrations in the human heart. Mol BioSyst 6:1917-1927. doi:10.1039/c004495d
    • (2010) Mol BioSyst , vol.6 , pp. 1917-1927
    • Aye, T.T.1    Scholten, A.2    Taouatas, N.3
  • 8
    • 77956545752 scopus 로고    scopus 로고
    • Improving software performance for peptide electron transfer dissociation data analysis by implementation of charge state- and sequencedependent scoring
    • doi: 10.1074/mcp.M110.000422
    • Baker PR, Medzihradszky KF, Chalkley RJ (2010) Improving software performance for peptide electron transfer dissociation data analysis by implementation of charge state- and sequencedependent scoring. Mol Cell Proteomics 9:1795-1803. doi: 10.1074/mcp.M110.000422
    • (2010) Mol Cell Proteomics , vol.9 , pp. 1795-1803
    • Baker, P.R.1    Trinidad, J.C.2    Chalkley, R.J.3
  • 9
    • 79960181605 scopus 로고    scopus 로고
    • Modification site localization scoring integrated into a search engine
    • M111.008078 doi:10.1074/mcp.M111.008078
    • Baker PR, Trinidad JC, Chalkley RJ (2011) Modification site localization scoring integrated into a search engine. Mol Cell Proteomics 10:M111.008078. doi:10.1074/mcp.M111.008078
    • (2011) Mol Cell Proteomics , vol.10
    • Baker, P.R.1    Medzihradszky, K.F.2    Chalkley, R.J.3
  • 10
    • 2542640024 scopus 로고    scopus 로고
    • Protein identification by mass spectrometry: Issues to be considered
    • DOI 10.1074/mcp.R300012-MCP200
    • Baldwin MA (2004) Protein identification by mass spectrometry: issues to be considered. Mol Cell Proteomics 3:1-9. doi:10.1074/ mcp.R300012-MCP200 (Pubitemid 38697101)
    • (2004) Molecular and Cellular Proteomics , vol.3 , Issue.1 , pp. 1-9
    • Baldwin, M.A.1
  • 11
    • 34748916981 scopus 로고    scopus 로고
    • Quantitative mass spectrometry in proteomics: A critical review
    • DOI 10.1007/s00216-007-1486-6, Proteomics/Molecular Imaging
    • Bantscheff M, Schirle M, Sweetman G et al (2007) Quantitative mass spectrometry in proteomics: a critical review. Anal Bioanal Chem 389:1017-1031. doi:10.1007/s00216-007-1486-6 (Pubitemid 47482251)
    • (2007) Analytical and Bioanalytical Chemistry , vol.389 , Issue.4 , pp. 1017-1031
    • Bantscheff, M.1    Schirle, M.2    Sweetman, G.3    Rick, J.4    Kuster, B.5
  • 12
    • 52649098504 scopus 로고    scopus 로고
    • Robust and sensitive iTRAQ quantification on an LTQ Orbitrap mass spectrometer
    • doi:10.1074/ mcp.M800029-MCP200
    • Bantscheff M, Boesche M, Eberhard D et al (2008) Robust and sensitive iTRAQ quantification on an LTQ Orbitrap mass spectrometer. Mol Cell Proteomics 7:1702-1713. doi:10.1074/ mcp.M800029-MCP200
    • (2008) Mol Cell Proteomics , vol.7 , pp. 1702-1713
    • Bantscheff, M.1    Boesche, M.2    Eberhard, D.3
  • 13
    • 33749853607 scopus 로고    scopus 로고
    • A probability-based approach for high-throughput protein phosphorylation analysis and site localization
    • DOI 10.1038/nbt1240, PII NBT1240
    • Beausoleil SA, Villén J, Gerber SA et al (2006) A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol 24:1285-1292. doi:10. 1038/nbt1240 (Pubitemid 44564776)
    • (2006) Nature Biotechnology , vol.24 , Issue.10 , pp. 1285-1292
    • Beausoleil, S.A.1    Villen, J.2    Gerber, S.A.3    Rush, J.4    Gygi, S.P.5
  • 14
    • 79957745193 scopus 로고    scopus 로고
    • Recent developments in quantitative proteomics
    • doi:10.1016/j.mrgentox. 2010.06.016
    • Becker CH, Bern M (2011) Recent developments in quantitative proteomics. Mutat Res 722:171-182. doi:10.1016/j.mrgentox. 2010.06.016
    • (2011) Mutat Res , vol.722 , pp. 171-182
    • Becker, C.H.1    Bern, M.2
  • 15
    • 1842580753 scopus 로고    scopus 로고
    • Improving large-scale proteomics by clustering of mass spectrometry data
    • DOI 10.1002/pmic.200300652
    • Beer I, Barnea E, Ziv T, Admon A (2004) Improving large-scale proteomics by clustering of mass spectrometry data. Proteomics 4:950-960. doi:10.1002/pmic.200300652 (Pubitemid 38445955)
    • (2004) Proteomics , vol.4 , Issue.4 , pp. 950-960
    • Beer, I.1    Barnea, E.2    Ziv, T.3    Admon, A.4
  • 16
    • 0037236997 scopus 로고    scopus 로고
    • Initial implementation of external accumulation liquid chromatography/electrospray ionization fourier transform ion cyclotron resonance with automated gain control
    • DOI 10.1002/rcm.955
    • Belov ME, Rakov VS, Nikolaev EN et al (2003) Initial implementation of external accumulation liquid chromatography/electrospray ionization Fourier transform ion cyclotron resonance with automated gain control. Rapid Commun Mass Spectrom 17:627-636. doi:10.1002/rcm.955 (Pubitemid 36373161)
    • (2003) Rapid Communications in Mass Spectrometry , vol.17 , Issue.7 , pp. 627-636
    • Belov, M.E.1    Rakov, V.S.2    Nikolaev, E.N.3    Goshe, M.B.4    Anderson, G.A.5    Smith, R.D.6
  • 17
    • 76149113930 scopus 로고    scopus 로고
    • Deconvolution of mixture spectra from ion-trap data-independent- acquisition tandem mass spectrometry
    • doi:10.1021/ ac901801b
    • Bern M, Finney G, Hoopmann MR et al (2010) Deconvolution of mixture spectra from ion-trap data-independent-acquisition tandem mass spectrometry. Anal Chem 82:833-841. doi:10.1021/ ac901801b
    • (2010) Anal Chem , vol.82 , pp. 833-841
    • Bern, M.1    Finney, G.2    Hoopmann, M.R.3
  • 18
    • 64749108158 scopus 로고    scopus 로고
    • Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics
    • doi:10.1038/nprot.2009.21
    • Boersema PJ, Raijmakers R, Lemeer S et al (2009) Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics. Nat Protoc 4:484-494. doi:10.1038/nprot.2009.21
    • (2009) Nat Protoc , vol.4 , pp. 484-494
    • Boersema, P.J.1    Raijmakers, R.2    Lemeer, S.3
  • 19
    • 49849115071 scopus 로고
    • Computer analysis of low resolution mass spectra correction for natural abundance of 13C, 2H, 15N, 17O and 18O
    • doi:10.1016/0020-7381(70)87003-6.
    • Boone B, Mitchum RK, Schsppele SE (1970) Computer analysis of low resolution mass spectra correction for natural abundance of 13C, 2H, 15N, 17O and 18O. Int J Mass Spectrom Ion Phys 5:21-27. doi:10.1016/0020-7381(70)87003-6. http://www.sciencedirect. com/science/article/pii/0020738170870036
    • (1970) Int J Mass Spectrom Ion Phys , vol.5 , pp. 21-27
    • Boone, B.1    Mitchum, R.K.2    Schsppele, S.E.3
  • 20
    • 33646907086 scopus 로고    scopus 로고
    • Reporting protein identification data: The next generation of guidelines
    • DOI 10.1074/mcp.E600005-MCP200
    • Bradshaw RA, Burlingame AL, Carr S, Aebersold R (2006) Reporting protein identification data: the next generation of guidelines. Mol Cell Proteomics 5:787-788. doi:10.1074/mcp.E600005-MCP200 (Pubitemid 43792788)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.5 , pp. 787-788
    • Bradshaw, R.A.1    Burlingame, A.L.2    Carr, S.3    Aebersold, R.4
  • 22
    • 46849101222 scopus 로고    scopus 로고
    • Wavelet-based method for noise characterization and rejection in high-performance liquid chromatography coupled to mass spectrometry
    • DOI 10.1021/ac800166w
    • Cappadona S, Levander F, Jansson M et al (2008) Wavelet-based method for noise characterization and rejection in high-performance liquid chromatography coupled to mass spectrometry. Anal Chem 80:4960-4968. doi:10.1021/ac800166w (Pubitemid 351956303)
    • (2008) Analytical Chemistry , vol.80 , Issue.13 , pp. 4960-4968
    • Cappadona, S.1    Levander, F.2    Jansson, M.3    James, P.4    Cerutti, S.5    Pattini, L.6
  • 23
    • 80052034884 scopus 로고    scopus 로고
    • Deconvolution of overlapping isotopic clusters improves quantification of stable isotope-labeled peptides
    • doi:10.1016/ j.jprot 2011 04.022
    • Cappadona S, Muñoz J, Spee WPE et al (2011) Deconvolution of overlapping isotopic clusters improves quantification of stable isotope-labeled peptides. J Proteomics 74:2204-2209. doi:10.1016/ j.jprot.2011.04.022
    • (2011) J Proteomics , vol.74 , pp. 2204-2209
    • Cappadona, S.1    Muñoz, J.2    Wpe, S.3
  • 24
    • 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
    • doi:10.1074/ mcp.T400006-MCP200
    • Carr S, Aebersold R, Baldwin M et al (2004) 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 3:531-533. doi:10.1074/ mcp.T400006-MCP200
    • (2004) Mol Cell Proteomics , vol.3 , pp. 531-533
    • Carr, S.1    Aebersold, R.2    Baldwin, M.3
  • 25
    • 75249085783 scopus 로고    scopus 로고
    • Methods for combining peptide intensities to estimate relative protein abundance
    • doi:10.1093/bioinformatics/ btp610
    • Carrillo B, Yanofsky C, Laboissiere S et al (2010) Methods for combining peptide intensities to estimate relative protein abundance. Bioinformatics 26:98-103. doi:10.1093/bioinformatics/ btp610
    • (2010) Bioinformatics , vol.26 , pp. 98-103
    • Carrillo, B.1    Yanofsky, C.2    Laboissiere, S.3
  • 26
    • 78651083717 scopus 로고    scopus 로고
    • A self-validating quantitative mass spectrometry method for assessing the accuracy of high-content phosphoproteomic experiments
    • M110.003079 doi:10.1074/mcp.M110.003079
    • Casado P, Cutillas PR (2011) A self-validating quantitative mass spectrometry method for assessing the accuracy of high-content phosphoproteomic experiments. Mol Cell Proteomics 10:M110.003079. doi:10.1074/mcp.M110.003079
    • (2011) Mol Cell Proteomics , vol.10
    • Casado, P.1    Cutillas, P.R.2
  • 27
    • 24044491542 scopus 로고    scopus 로고
    • Comprehensive analysis of a multidimensional liquid chromatography mass spectrometry dataset acquired on a quadrupole selecting, quadrupole collision cells, time-of-flight mass spectrometer: II New developments in protein prospector allow for reliable and comprehensive automatic analysis of large datasets
    • DOI 10.1074/mcp.D500002-MCP200
    • Chalkley RJ, Baker PR, Huang L et al (2005) 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 4:1194-1204. doi:10.1074/mcp.D500002-MCP200 (Pubitemid 41223378)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.8 , 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    Burlingame, A.L.7
  • 28
    • 58149287749 scopus 로고    scopus 로고
    • Depth analysis of tandem mass spectrometry data from disparate instrument types
    • doi:10.1074/ mcp.M800021-MCP200
    • Chalkley RJ, Baker PR, Medzihradszky KF et al (2008) In-depth analysis of tandem mass spectrometry data from disparate instrument types. Mol Cell Proteomics 7:2386-2398. doi:10.1074/ mcp.M800021-MCP200
    • (2008) Mol Cell Proteomics , vol.7 , pp. 2386-2398
    • Chalkley, R.J.1    Baker, P.R.2    Medzihradszky, K.F.3
  • 29
    • 0036665581 scopus 로고    scopus 로고
    • Quantitative profiling of proteins in complex mixtures using liquid chromatography and mass spectrometry
    • DOI 10.1021/pr025517j
    • Chelius D, Bondarenko PV (2002) Quantitative profiling of proteins in complex mixtures using liquid chromatography and mass spectrometry. J Proteome Res 1:317-323 (Pubitemid 36395872)
    • (2002) Journal of Proteome Research , vol.1 , Issue.4 , pp. 317-323
    • Chelius, D.1    Bondarenko, P.V.2
  • 30
    • 77949778154 scopus 로고    scopus 로고
    • Time alignment algorithms based on selected mass traces for complex LC-MS data
    • doi:10.1021/pr9010124
    • Christin C, Hoefsloot HCJ, Smilde AK et al (2010) Time alignment algorithms based on selected mass traces for complex LC-MS data. J Proteome Res 9:1483-1495. doi:10.1021/pr9010124
    • (2010) J Proteome Res , vol.9 , pp. 1483-1495
    • Christin, C.1    Hcj, H.2    Smilde, A.K.3
  • 31
    • 37549029793 scopus 로고    scopus 로고
    • The properties of highdimensional data spaces: Implications for exploring gene and protein expression data
    • doi:10.1038/ nrc2294
    • Clarke R, Ressom HW, Wang A et al (2008) The properties of highdimensional data spaces: implications for exploring gene and protein expression data. Nat Rev Cancer 8:37-49. doi:10.1038/ nrc2294
    • (2008) Nat Rev Cancer , vol.8 , pp. 37-49
    • Clarke, R.1    Ressom, H.W.2    Wang, A.3
  • 32
    • 34247466401 scopus 로고    scopus 로고
    • Tools for computational processing of LC-MS datasets: A user's perspective
    • DOI 10.1016/j.cmpb.2007.03.001, PII S0169260707000545
    • Codrea MC, Jiménez CR, Heringa J, Marchiori E (2007) Tools for computational processing of LC-MS datasets: a users perspective. Comput Methods Programs Biomed 86:281-290. doi: 10.1016/j.cmpb.2007.03.001 (Pubitemid 46661021)
    • (2007) Computer Methods and Programs in Biomedicine , vol.86 , Issue.3 , pp. 281-290
    • Codrea, M.C.1    Jimenez, C.R.2    Heringa, J.3    Marchiori, E.4
  • 33
    • 80052385401 scopus 로고    scopus 로고
    • A case study on the comparison of different software tools for automated quantification of peptides
    • doi:10.1007/978-1-61779-148-2-25
    • Colaert N, Vandekerckhove J, Martens L, Gevaert K (2011) A case study on the comparison of different software tools for automated quantification of peptides. Methods Mol Biol 753:373-398. doi:10.1007/978-1-61779-148-2-25
    • (2011) Methods Mol Biol , vol.753 , pp. 373-398
    • Colaert, N.1    Vandekerckhove, J.2    Martens, L.3    Gevaert, K.4
  • 34
    • 46849122859 scopus 로고    scopus 로고
    • Top-down identification and quantification of stable isotope labeled proteins from Aspergillus flavus using online nano-flow reversed-phase liquid chromatography coupled to a LTQ-FTICR mass spectrometer
    • DOI 10.1021/ac800254z
    • Collier TS, Hawkridge AM, Georgianna DR et al (2008) Top-down identification and quantification of stable isotope labeled proteins from Aspergillus flavus using online nano-flow reversed-phase liquid chromatography coupled to a LTQ-FTICR mass spectrometer. Anal Chem 80:4994-5001. doi:10.1021/ ac800254z (Pubitemid 351956307)
    • (2008) Analytical Chemistry , vol.80 , Issue.13 , pp. 4994-5001
    • Collier, T.S.1    Hawkridge, A.M.2    Georgianna, D.R.3    Payne, G.A.4    Muddiman, D.C.5
  • 35
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteomewide protein quantification
    • doi: 10.1038/nbt.1511
    • Cox J, Mann M (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteomewide protein quantification. Nat Biotechnol 26:1367-1372. doi: 10.1038/nbt.1511
    • (2008) Nat Biotechnol , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 36
    • 79959424627 scopus 로고    scopus 로고
    • Quantitative, high-resolution proteomics for data-driven systems biology
    • doi:10.1146/annurev-biochem-061308-093216
    • Cox J, Mann M (2011) Quantitative, high-resolution proteomics for data-driven systems biology. Annu Rev Biochem 80:273-299. doi:10.1146/annurev- biochem-061308-093216
    • (2011) Annu Rev Biochem , vol.80 , pp. 273-299
    • Cox, J.1    Mann, M.2
  • 37
    • 34848822499 scopus 로고    scopus 로고
    • Quantitative profiles of five murine core proteomes using label-free functional proteomics
    • DOI 10.1074/mcp.M700037-MCP200
    • Cutillas PR, Vanhaesebroeck B (2007) Quantitative profile of five murine core proteomes using label-free functional proteomics. Mol Cell Proteomics 6:1560-1573. doi:10.1074/mcp.M700037- MCP200 (Pubitemid 47506167)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.9 , pp. 1560-1573
    • Cutillas, P.R.1    Wanhaesebroeck, B.2
  • 38
    • 24044467381 scopus 로고    scopus 로고
    • Quantification of gel-separated proteins and their phosphorylation sites by LC-MS using unlabeled internal standards
    • DOI 10.1074/mcp.M500078-MCP200
    • Cutillas PR, Geering B, Waterfield MD, Vanhaesebroeck B (2005) Quantification of gel-separated proteins and their phosphorylation sites by LC-MS using unlabeled internal standards: analysis of phosphoprotein dynamics in a B cell lymphoma cell line. Mol Cell Proteomics 4:1038-1051. doi:10.1074/mcp.M500078-MCP200 (Pubitemid 41223364)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.8 , pp. 1038-1051
    • Cutillas, P.R.1    Geering, B.2    Waterfield, M.D.3    Vanhaesebroeck, B.4
  • 39
    • 65249098316 scopus 로고    scopus 로고
    • Quantification of isotopically overlapping deamidated and 18O-labeled peptides using isotopic envelope mixture modeling
    • doi:10.1021/pr801054w
    • Dasari S, Wilmarth PA, Reddy AP et al (2009) Quantification of isotopically overlapping deamidated and 18O-labeled peptides using isotopic envelope mixture modeling. J Proteome Res 8:1263-1270. doi:10.1021/pr801054w
    • (2009) J Proteome Res , vol.8 , pp. 1263-1270
    • Dasari, S.1    Wilmarth, P.A.2    Reddy, A.P.3
  • 40
    • 48949104656 scopus 로고    scopus 로고
    • MzML: A single, unifying data format for mass spectrometer output
    • doi:10.1002/ pmic.200890049
    • Deutsch E (2008) mzML: a single, unifying data format for mass spectrometer output. Proteomics 8:2776-2777. doi:10.1002/ pmic.200890049
    • (2008) Proteomics , vol.8 , pp. 2776-2777
    • Deutsch, E.1
  • 41
    • 77954513767 scopus 로고    scopus 로고
    • The pros and cons of peptide-centric proteomics
    • doi: 10.1038/nbt0710-659
    • Duncan MW, Aebersold R, Caprioli RM (2010) The pros and cons of peptide-centric proteomics. Nat Biotechnol 28:659-664. doi: 10.1038/nbt0710-659
    • (2010) Nat Biotechnol , vol.28 , pp. 659-664
    • Duncan, M.W.1    Aebersold, R.2    Caprioli, R.M.3
  • 42
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • DOI 10.1038/nmeth1019, PII NMETH1019
    • Elias J, Gygi S (2007) Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat Methods 4:207-214 (Pubitemid 46358868)
    • (2007) Nature Methods , vol.4 , Issue.3 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 43
    • 72449173774 scopus 로고    scopus 로고
    • Current trends in quantitative proteomics
    • doi: 10.1002/jms.1692
    • Elliott MH, Smith DS, Parker CE, Borchers C (2009) Current trends in quantitative proteomics. J Mass Spectrom 44:1637-1660. doi: 10.1002/jms.1692
    • (2009) J Mass Spectrom , vol.44 , pp. 1637-1660
    • Elliott, M.H.1    Smith, D.S.2    Parker, C.E.3    Borchers, C.4
  • 45
    • 39449131119 scopus 로고    scopus 로고
    • Label-free comparative analysis of proteomics mixtures using chromatographic alignment of high-resolution muLC-MS data
    • DOI 10.1021/ac701649e
    • Finney GL, Blackler AR, Hoopmann MR et al (2008) Label-free comparative analysis of proteomics mixtures using chromatographic alignment of high-resolution muLC-MS data. Anal Chem 80:961-971. doi:10.1021/ac701649e (Pubitemid 351272325)
    • (2008) Analytical Chemistry , vol.80 , Issue.4 , pp. 961-971
    • Finney, G.L.1    Blackler, A.R.2    Hoopmann, M.R.3    Canterbury, J.D.4    Wu, C.C.5    MacCoss, M.J.6
  • 46
    • 33645653958 scopus 로고    scopus 로고
    • Improving the reliability and throughput of mass spectrometry-based proteomics by spectrum quality filtering
    • doi: 10.1002/pmic.200500309
    • Flikka K, Martens L, Vandekerckhove J et al (2006) Improving the reliability and throughput of mass spectrometry-based proteomics by spectrum quality filtering. Proteomics 6:2086-2094. doi: 10.1002/pmic.200500309
    • (2006) Proteomics , vol.6 , pp. 2086-2094
    • Flikka, K.1    Martens, L.2    Vandekerckhove, J.3
  • 47
    • 79955831978 scopus 로고    scopus 로고
    • Improved peptide identification by targeted fragmentation using CID, HCD and ETD on an LTQ-Orbitrap Velos
    • doi:10.1021/pr1011729
    • Frese CK, Altelaar AFM, Hennrich ML et al (2011) Improved peptide identification by targeted fragmentation using CID, HCD and ETD on an LTQ-Orbitrap Velos. J Proteome Res 10:2377-2388. doi:10.1021/pr1011729
    • (2011) J Proteome Res , vol.10 , pp. 2377-2388
    • Frese, C.K.1    Afm, A.2    Hennrich, M.L.3
  • 49
    • 67650729894 scopus 로고    scopus 로고
    • Post-acquisition ETD spectral processing for increased peptide identifications
    • doi:10.1016/j.jasms. 2009.03.006
    • Good DM, Wenger CD, McAlister GC et al (2009) Post-acquisition ETD spectral processing for increased peptide identifications. J Am Soc Mass Spectrom 20:1435-1440. doi:10.1016/j.jasms. 2009.03.006
    • (2009) J Am Soc Mass Spectrom , vol.20 , pp. 1435-1440
    • Good, D.M.1    Wenger, C.D.2    McAlister, G.C.3
  • 50
    • 54349101564 scopus 로고    scopus 로고
    • Optimizing identification and quantitation of 15 N-labeled proteins in comparative proteomics
    • Gouw J, Tops B, Mortensen P et al (2008) Optimizing identification and quantitation of 15 N-labeled proteins in comparative proteomics. Anal Chem 80:7796-7803
    • (2008) Anal Chem , vol.80 , pp. 7796-7803
    • Gouw, J.1    Tops, B.2    Mortensen, P.3
  • 51
    • 74049132731 scopus 로고    scopus 로고
    • Label-free, normalized quantification of complex mass spectrometry data for proteomic analysis
    • doi:10.1038/nbt.1592
    • Griffin NM, Yu J, Long F et al (2010) Label-free, normalized quantification of complex mass spectrometry data for proteomic analysis. Nat Biotechnol 28:83-89. doi:10.1038/nbt.1592
    • (2010) Nat Biotechnol , vol.28 , pp. 83-89
    • Griffin, N.M.1    Yu, J.2    Long, F.3
  • 52
    • 70149084269 scopus 로고    scopus 로고
    • Deterministic protein inference for shotgun proteomics data provides new insights into Arabidopsis pollen development and function
    • doi:10.1101/gr.089060.108
    • Grobei MA, Qeli E, Brunner E et al (2009) Deterministic protein inference for shotgun proteomics data provides new insights into Arabidopsis pollen development and function. Genome Res 19:1786-1800. doi:10.1101/gr.089060.108
    • (2009) Genome Res , vol.19 , pp. 1786-1800
    • Grobei, M.A.1    Qeli, E.2    Brunner, E.3
  • 53
    • 77954660028 scopus 로고    scopus 로고
    • Implementation and evaluation of relative and absolute quantification in shotgun proteomics with label-free methods
    • doi:10.1016/j.jprot.2010.05.011
    • Grossmann J, Roschitzki B, Panse C et al (2010) Implementation and evaluation of relative and absolute quantification in shotgun proteomics with label-free methods. J Proteomics 73:1740-1746. doi:10.1016/j.jprot.2010.05.011
    • (2010) J Proteomics , vol.73 , pp. 1740-1746
    • Grossmann, J.1    Roschitzki, B.2    Panse, C.3
  • 55
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • DOI 10.1038/13690
    • Gygi SP, Rist B, Gerber SA et al (1999) Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat Biotechnol 17:994-999. doi:10.1038/13690 (Pubitemid 29474856)
    • (1999) Nature Biotechnology , vol.17 , Issue.10 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 56
    • 0034789979 scopus 로고    scopus 로고
    • Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry
    • DOI 10.1038/nbt1001-946
    • Han DK, Eng J, Zhou H, Aebersold R (2001) Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry. Nat Biotechnol 19:946-951. doi:10.1038/nbt1001-946 (Pubitemid 32947573)
    • (2001) Nature Biotechnology , vol.19 , Issue.10 , pp. 946-951
    • Han, D.K.1    Eng, J.2    Zhou, H.3    Aebersold, R.4
  • 57
    • 0347334566 scopus 로고    scopus 로고
    • Mass spectrometric analysis of protein mixtures at low levels using cleavable 13C-isotope-coded affinity tag and multidimensional chromatography
    • doi:10.1074/ mcp.M300021-MCP200
    • Hansen KC, Schmitt-Ulms G, Chalkley RJ et al (2003) Mass spectrometric analysis of protein mixtures at low levels using cleavable 13C-isotope-coded affinity tag and multidimensional chromatography. Mol Cell Proteomics 2:299-314. doi:10.1074/ mcp.M300021-MCP200
    • (2003) Mol Cell Proteomics , vol.2 , pp. 299-314
    • Hansen, K.C.1    Schmitt-Ulms, G.2    Chalkley, R.J.3
  • 59
    • 20444508181 scopus 로고    scopus 로고
    • Mass spectrometry-based quantitative proteomics
    • doi:10.1586/ 14789450.1.3.317
    • Heck AJR, Krijgsveld J (2004) Mass spectrometry-based quantitative proteomics. Expert Rev Proteomics 1:317-326. doi:10.1586/ 14789450.1.3.317
    • (2004) Expert Rev Proteomics , vol.1 , pp. 317-326
    • Ajr, H.1    Krijgsveld, J.2
  • 60
    • 33751340274 scopus 로고    scopus 로고
    • Comparison of spectral counting and metabolic stable isotope labeling for use with quantitative microbial proteomics
    • DOI 10.1039/b610957h
    • Hendrickson EL, Xia Q, Wang T et al (2006) Comparison of spectral counting and metabolic stable isotope labeling for use with quantitative microbial proteomics. Analyst 131:1335-1341. doi: 10.1039/b610957h (Pubitemid 44809119)
    • (2006) Analyst , vol.131 , Issue.12 , pp. 1335-1341
    • Hendrickson, E.L.1    Xia, Q.2    Wang, T.3    Leigh, J.A.4    Hackett, M.5
  • 61
    • 77955455399 scopus 로고    scopus 로고
    • Quantifying the impact of chimera MS/MS spectra on peptide identification in large-scale proteomics studies
    • doi:10.1021/pr1003856
    • Houel S, Abernathy R, Renganathan K et al (2010) Quantifying the impact of chimera MS/MS spectra on peptide identification in large-scale proteomics studies. J Proteome Res 9:4152-4160. doi:10.1021/pr1003856
    • (2010) J Proteome Res , vol.9 , pp. 4152-4160
    • Houel, S.1    Abernathy, R.2    Renganathan, K.3
  • 62
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • DOI 10.1074/mcp.M500061-MCP200
    • Ishihama Y, Oda Y, Tabata T et al (2005) Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein. Mol Cell Proteomics 4:1265-1272. doi: 10.1074/mcp.M500061-MCP200 (Pubitemid 41448714)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.9 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3    Sato, T.4    Nagasu, T.5    Rappsilber, J.6    Mann, M.7
  • 63
    • 77954572010 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of T cell receptor signaling in diabetes prone and resistant mice
    • doi:10.1021/pr100035b
    • Iwai LK, Benoist C, Mathis D, White FM (2010) Quantitative phosphoproteomic analysis of T cell receptor signaling in diabetes prone and resistant mice. J Proteome Res 9:3135-3145. doi:10.1021/pr100035b
    • (2010) J Proteome Res , vol.9 , pp. 3135-3145
    • Iwai, L.K.1    Benoist, C.2    Mathis, D.3    White, F.M.4
  • 64
    • 79952112647 scopus 로고    scopus 로고
    • Bioinformatics for LC-MS/MS-based proteomics
    • doi:10.1007/978-1-60761-780-8-4
    • Jacob RJ (2010) Bioinformatics for LC-MS/MS-based proteomics. Methods Mol Biol 658:61-91. doi:10.1007/978-1-60761-780-8-4
    • (2010) Methods Mol Biol , vol.658 , pp. 61-91
    • Jacob, R.J.1
  • 65
    • 20844458723 scopus 로고    scopus 로고
    • Quantitative proteome analysis using differential stable isotopic labeling and microbore LC-MALDI MS and MS/MS
    • DOI 10.1021/pr049784w
    • Ji C, Li L (2005) Quantitative proteome analysis using differential stable isotopic labeling and microbore LC-MALDI MS and MS/ MS. J Proteome Res 4:734-742. doi:10.1021/pr049784w (Pubitemid 40863262)
    • (2005) Journal of Proteome Research , vol.4 , Issue.3 , pp. 734-742
    • Ji, C.1    Li, L.2
  • 66
    • 3543121341 scopus 로고    scopus 로고
    • Quantification in proteomics through stable isotope coding: A review
    • DOI 10.1021/pr0340734
    • Julka S, Regnier F (2004) Quantification in proteomics through stable isotope coding: a review. J Proteome Res 3:350-363 (Pubitemid 39207339)
    • (2004) Journal of Proteome Research , vol.3 , Issue.3 , pp. 350-363
    • Julka, S.1    Regnier, F.2
  • 67
    • 53049085543 scopus 로고    scopus 로고
    • Separating the wheat from the chaff: Unbiased filtering of background tandem mass spectra improves protein identification
    • doi:10.1021/pr800140v
    • Junqueira M, Spirin V, Santana Balbuena T et al (2008) Separating the wheat from the chaff: unbiased filtering of background tandem mass spectra improves protein identification. J Proteome Res 7:3382-3395. doi:10.1021/pr800140v
    • (2008) J Proteome Res , vol.7 , pp. 3382-3395
    • Junqueira, M.1    Spirin, V.2    Santana Balbuena, T.3
  • 68
    • 51249118496 scopus 로고    scopus 로고
    • Interferences and contaminants encountered in modern mass spectrometry
    • doi:10.1016/j.aca.2008.04.043
    • Keller BO, Sui J, Young AB, Whittal RM (2008) Interferences and contaminants encountered in modern mass spectrometry. Anal Chim Acta 627:71-81. doi:10.1016/j.aca.2008.04.043
    • (2008) Anal Chim Acta , vol.627 , pp. 71-81
    • Keller, B.O.1    Sui, J.2    Young, A.B.3    Whittal, R.M.4
  • 69
    • 79952012529 scopus 로고    scopus 로고
    • The emerging process of Top Down mass spectrometry for protein analysis: Biomarkers, protein-therapeutics, and achieving high throughput
    • doi:10.1039/c000896f
    • Kellie JF, Tran JC, Lee JE et al (2010) The emerging process of Top Down mass spectrometry for protein analysis: biomarkers, protein-therapeutics, and achieving high throughput. Mol Bio- Syst 6:1532-1539. doi:10.1039/c000896f
    • (2010) Mol Bio- Syst , vol.6 , pp. 1532-1539
    • Kellie, J.F.1    Tran, J.C.2    Lee, J.E.3
  • 70
    • 70349436819 scopus 로고    scopus 로고
    • Protein quantification across hundreds of experimental conditions
    • doi:10.1073/pnas.0904100106
    • Khan Z, Bloom JS, Garcia BA et al (2009) Protein quantification across hundreds of experimental conditions. Proc Natl Acad Sci USA 106:15544-15548. doi:10.1073/pnas.0904100106
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 15544-15548
    • Khan, Z.1    Bloom, J.S.2    Garcia, B.A.3
  • 71
    • 83655203194 scopus 로고    scopus 로고
    • Accurate proteome-wide protein quantification from high-resolution 15 N mass spectra
    • doi:10.1186/gb-2011-12-12-r122
    • Khan Z, Amini S, Bloom JS et al (2011) Accurate proteome-wide protein quantification from high-resolution 15 N mass spectra. Genome Biol 12:R122. doi:10.1186/gb-2011-12-12-r122
    • (2011) Genome Biol , vol.12
    • Khan, Z.1    Amini, S.2    Bloom, J.S.3
  • 72
    • 34547746723 scopus 로고    scopus 로고
    • Reproducibility assessment of relative quantitation strategies for LC-MS based proteomics
    • DOI 10.1021/ac070200u
    • Kim YJ, Zhan P, Feild B et al (2007) Reproducibility assessment of relative quantitation strategies for LC-MS based proteomics. Anal Chem 79:5651-5658. doi:10.1021/ac070200u (Pubitemid 47229811)
    • (2007) Analytical Chemistry , vol.79 , Issue.15 , pp. 5651-5658
    • Yeoun, J.K.1    Zhan, P.2    Feild, B.3    Ruben, S.M.4    He, T.5
  • 74
    • 70449385099 scopus 로고    scopus 로고
    • Automated calculation of unique peptide sequences for unambiguous identification of highly homologous proteins by mass spectrometry
    • doi:10.4172/jpb.1000003
    • Kohl M, Redlich G, Eisenacher M et al (2008) Automated calculation of unique peptide sequences for unambiguous identification of highly homologous proteins by mass spectrometry. J Proteomics Bioinform 01:006-010. doi:10.4172/jpb.1000003
    • (2008) J Proteomics Bioinform , vol.1 , pp. 006-010
    • Kohl, M.1    Redlich, G.2    Eisenacher, M.3
  • 75
    • 79957982498 scopus 로고    scopus 로고
    • Hierarchical clustering of shotgun proteomics data
    • M110.003822 doi:10.1074/mcp.M110.003822
    • Koskinen VR, Emery PA, Creasy DM, Cottrell JS (2011) Hierarchical clustering of shotgun proteomics data. Mol Cell Proteomics 10:M110.003822. doi:10.1074/mcp.M110.003822
    • (2011) Mol Cell Proteomics , vol.10
    • Koskinen, V.R.1    Emery, P.A.2    Creasy, D.M.3    Cottrell, J.S.4
  • 76
    • 84865591887 scopus 로고    scopus 로고
    • Applications of stable isotope dimethyl labeling in quantitative proteomics
    • in press
    • Kovanich D, Cappadona S, Raijmakers R et al (2012) Applications of stable isotope dimethyl labeling in quantitative proteomics. Anal Bioanal Chem (in press)
    • (2012) Anal Bioanal Chem
    • Kovanich, D.1    Cappadona, S.2    Raijmakers, R.3
  • 77
    • 71049194213 scopus 로고    scopus 로고
    • Development and evaluation of normalization methods for label-free relative quantification of endogenous peptides
    • doi:10.1074/mcp.M800514-MCP200
    • Kultima K, Nilsson A, Scholz B et al (2009) Development and evaluation of normalization methods for label-free relative quantification of endogenous peptides. Mol Cell Proteomics 8:2285-2295. doi:10.1074/mcp.M800514-MCP200
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2285-2295
    • Kultima, K.1    Nilsson, A.2    Scholz, B.3
  • 78
    • 67349208911 scopus 로고    scopus 로고
    • Bioinformatics analysis of mass spectrometry- based proteomics data sets
    • Kumar C, Mann M (2009) Bioinformatics analysis of mass spectrometry- based proteomics data sets. FEBS Lett 583:1703-1712
    • (2009) FEBS Lett , vol.583 , pp. 1703-1712
    • Kumar, C.1    Mann, M.2
  • 79
    • 67650753646 scopus 로고    scopus 로고
    • A comparison of MS/ MS-based, stable-isotope-labeled, quantitation performance on ESI-quadrupole TOF and MALDI-TOF/TOF mass spectrometers
    • doi:10.1002/pmic.200800412
    • Kuzyk MA, Ohlund LB, Elliott MH et al (2009) A comparison of MS/ MS-based, stable-isotope-labeled, quantitation performance on ESI-quadrupole TOF and MALDI-TOF/TOF mass spectrometers. Proteomics 9:3328-3340. doi:10.1002/pmic.200800412
    • (2009) Proteomics , vol.9 , pp. 3328-3340
    • Kuzyk, M.A.1    Ohlund, L.B.2    Elliott, M.H.3
  • 80
    • 79961176626 scopus 로고    scopus 로고
    • Building and searching tandem mass (MS/MS) spectral libraries for peptide identification in proteomics
    • doi:10.1016/j.ymeth.2011.01. 007
    • Lam H, Aebersold R (2011) Building and searching tandem mass (MS/MS) spectral libraries for peptide identification in proteomics. Methods 54:424-431. doi:10.1016/j.ymeth.2011.01. 007
    • (2011) Methods , vol.54 , pp. 424-431
    • Lam, H.1    Aebersold, R.2
  • 81
    • 73649110293 scopus 로고    scopus 로고
    • Artificial decoy spectral libraries for false discovery rate estimation in spectral library searching in proteomics
    • doi:10.1021/ pr900947u
    • Lam H, Deutsch EW, Aebersold R (2010) Artificial decoy spectral libraries for false discovery rate estimation in spectral library searching in proteomics. J Proteome Res 9:605-610. doi:10.1021/ pr900947u
    • (2010) J Proteome Res , vol.9 , pp. 605-610
    • Lam, H.1    Deutsch, E.W.2    Aebersold, R.3
  • 82
    • 54049090766 scopus 로고    scopus 로고
    • Selected reaction monitoring for quantitative proteomics: A tutorial
    • doi:10.1038/msb.2008.61
    • Lange V, Picotti P, Domon B, Aebersold R (2008) Selected reaction monitoring for quantitative proteomics: a tutorial. Mol Syst Biol 4:222. doi:10.1038/msb.2008.61
    • (2008) Mol Syst Biol , vol.4 , pp. 222
    • Lange, V.1    Picotti, P.2    Domon, B.3    Aebersold, R.4
  • 84
    • 17844394177 scopus 로고    scopus 로고
    • Statistical and computational methods for comparative proteomic profiling using liquid chromatography-tandem mass spectrometry
    • DOI 10.1074/mcp.R500005-MCP200
    • Listgarten J, Emili A (2005) Statistical and computational methods for comparative proteomic profiling using liquid chromatography- tandem mass spectrometry. Mol Cell Proteomics 4:419-434. doi:10.1074/mcp.R500005-MCP200 (Pubitemid 40590562)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.4 , pp. 419-434
    • Listgarten, J.1    Emili, A.2
  • 85
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • DOI 10.1021/ac0498563
    • Liu H, Sadygov RG, Yates JR (2004) A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal Chem 76:4193-4201. doi:10.1021/ac0498563 (Pubitemid 38943698)
    • (2004) Analytical Chemistry , vol.76 , Issue.14 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates III, J.R.3
  • 86
    • 33846165487 scopus 로고    scopus 로고
    • Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation
    • DOI 10.1038/nbt1270, PII NBT1270
    • Lu P, Vogel C, Wang R et al (2007) Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation. Nat Biotechnol 25:117-124. doi: 10.1038/nbt1270 (Pubitemid 46087910)
    • (2007) Nature Biotechnology , vol.25 , Issue.1 , pp. 117-124
    • Lu, P.1    Vogel, C.2    Wang, R.3    Yao, X.4    Marcotte, E.M.5
  • 87
    • 77951650200 scopus 로고    scopus 로고
    • Role of spectral counting in quantitative proteomics
    • doi:10.1586/epr.09.69
    • Lundgren DH, Hwang S-I, Wu L, Han DK (2010) Role of spectral counting in quantitative proteomics. Expert Rev Proteomics 7:39-53. doi:10.1586/epr.09.69
    • (2010) Expert Rev Proteomics , vol.7 , pp. 39-53
    • Lundgren, D.H.1    Hwang, S.-I.2    Wu, L.3    Han, D.K.4
  • 90
    • 68549092907 scopus 로고    scopus 로고
    • IDPicker 2.0: Improved protein assembly with high discrimination peptide identification filtering
    • doi:10.1021/pr900360j
    • Ma Z-Q, Dasari S, Chambers MC et al (2009) IDPicker 2.0: improved protein assembly with high discrimination peptide identification filtering. J Proteome Res 8:3872-3881. doi:10.1021/pr900360j
    • (2009) J Proteome Res , vol.8 , pp. 3872-3881
    • Ma, Z.-Q.1    Dasari, S.2    Chambers, M.C.3
  • 91
    • 0346122950 scopus 로고    scopus 로고
    • A correlation algorithm for the automated quantitative analysis of shotgun proteomics data
    • DOI 10.1021/ac034790h
    • MacCoss MJ, Wu CC, Liu H et al (2003) A correlation algorithm for the automated quantitative analysis of shotgun proteomics data. Anal Chem 75:6912-6921. doi:10.1021/ac034790h (Pubitemid 37523592)
    • (2003) Analytical Chemistry , vol.75 , Issue.24 , pp. 6912-6921
    • MacCoss, M.J.1    Wu, C.C.2    Liu, H.3    Sadygov, R.4    Yates III, J.R.5
  • 92
    • 0019300258 scopus 로고
    • Guidelines for data acquisition and data quality evaluation in environmental chemistry
    • DOI 10.1021/ac50064a004
    • MacDougall D, Crummett WB (1980) Guidelines for data acquisition and data quality evaluation in environmental chemistry. Anal Chem 52:2242-2249. doi:10.1021/ac50064a004 (Pubitemid 11165301)
    • (1980) Analytical Chemistry , vol.52 , Issue.14 , pp. 2242-2249
    • MacDougall, D.1    Lal, J.2    Amore, F.J.3
  • 93
    • 65249137629 scopus 로고    scopus 로고
    • Global and site-specific quantitative phosphoproteomics: Principles and applications
    • doi:10.1146/annurev. pharmtox.011008.145606
    • Macek B, Mann M, Olsen JV (2009) Global and site-specific quantitative phosphoproteomics: principles and applications. Annu Rev Pharmacol Toxicol 49:199-221. doi:10.1146/annurev. pharmtox.011008.145606
    • (2009) Annu Rev Pharmacol Toxicol , vol.49 , pp. 199-221
    • MacEk, B.1    Mann, M.2    Olsen, J.V.3
  • 95
    • 70349617072 scopus 로고    scopus 로고
    • Comparative analysis to guide quality improvements in proteomics
    • Mann M (2009) Comparative analysis to guide quality improvements in proteomics. Nat Methods 6:717-719
    • (2009) Nat Methods , vol.6 , pp. 717-719
    • Mann, M.1
  • 96
    • 80052347088 scopus 로고    scopus 로고
    • Bioinformatics challenges in mass spectrometrydriven proteomics
    • doi: 10.1007/978-1-61779-148-2-24
    • Martens L (2011) Bioinformatics challenges in mass spectrometrydriven proteomics. Methods Mol Biol 753:359-371. doi: 10.1007/978-1-61779-148-2-24
    • (2011) Methods Mol Biol , vol.753 , pp. 359-371
    • Martens, L.1
  • 97
    • 34548396821 scopus 로고    scopus 로고
    • Methods, algorithms and tools in computational proteomics: A practical point of view
    • DOI 10.1002/pmic.200700116
    • Matthiesen R (2007) Methods, algorithms and tools in computational proteomics: a practical point of view. Proteomics 7:2815-2832. doi:10.1002/pmic.200700116 (Pubitemid 47359923)
    • (2007) Proteomics , vol.7 , Issue.16 , pp. 2815-2832
    • Matthiesen, R.1
  • 98
    • 79551483264 scopus 로고    scopus 로고
    • Discussion on common data analysis strategies used in MS-based proteomics
    • doi:10.1002/pmic.201000404
    • Matthiesen R, Azevedo L, Amorim A, Carvalho AS (2011) Discussion on common data analysis strategies used in MS-based proteomics. Proteomics 11:604-619. doi:10.1002/pmic.201000404
    • (2011) Proteomics , vol.11 , pp. 604-619
    • Matthiesen, R.1    Azevedo, L.2    Amorim, A.3    Carvalho, A.S.4
  • 99
    • 41349120246 scopus 로고    scopus 로고
    • DeconMSn: A software tool for accurate parent ion monoisotopic mass determination for tandem mass spectra
    • DOI 10.1093/bioinformatics/btn063
    • Mayampurath AM, Jaitly N, Purvine SO et al (2008) DeconMSn: a software tool for accurate parent ion monoisotopic mass determination for tandem mass spectra. Bioinformatics 24:1021-1023. doi:10.1093/bioinformatics/btn063 (Pubitemid 351448041)
    • (2008) Bioinformatics , vol.24 , Issue.7 , 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    Smith, R.D.7
  • 100
    • 2342625386 scopus 로고    scopus 로고
    • Deconvolution of isobaric interferences in mass spectra
    • DOI 10.1016/j.jasms.2003.12.016, PII S1044030504000169
    • Meija J, Caruso JA (2004) Deconvolution of isobaric interferences in mass spectra. J Am Soc Mass Spectrom 15:654-658. doi:10. 1016/j.jasms.2003.12.016 (Pubitemid 38581091)
    • (2004) Journal of the American Society for Mass Spectrometry , vol.15 , Issue.5 , pp. 654-658
    • Meija, J.1    Caruso, J.A.2
  • 101
    • 79953719716 scopus 로고    scopus 로고
    • More than 100,000 detectable peptide species elute in single shotgun proteomics runs but the majority is inaccessible to data-dependent LC-MS/MS
    • doi:10.1021/pr101060v
    • Michalski A, Cox J, Mann M (2011) More than 100,000 detectable peptide species elute in single shotgun proteomics runs but the majority is inaccessible to data-dependent LC-MS/MS. J Proteome Res 10:1785-1793. doi:10.1021/pr101060v
    • (2011) J Proteome Res , vol.10 , pp. 1785-1793
    • Michalski, A.1    Cox, J.2    Mann, M.3
  • 103
    • 77958000048 scopus 로고    scopus 로고
    • Comparative assessment of site assignments in CID and electron transfer dissociation spectra of phosphopeptides discloses limited relocation of phosphate groups
    • doi:10.1074/mcp.M900619-MCP200
    • Mischerikow N, Altelaar AFM, Navarro JD et al (2010) Comparative assessment of site assignments in CID and electron transfer dissociation spectra of phosphopeptides discloses limited relocation of phosphate groups. Mol Cell Proteomics 9:2140-2148. doi:10.1074/mcp.M900619-MCP200
    • (2010) Mol Cell Proteomics , vol.9 , pp. 2140-2148
    • Mischerikow, N.1    Afm, A.2    Navarro, J.D.3
  • 104
    • 0036209134 scopus 로고    scopus 로고
    • Qscore: An algorithm for evaluating SEQUEST database search results
    • DOI 10.1016/S1044-0305(02)00352-5, PII S1044030502003525
    • Moore RE, Young MK, Lee TD (2002) Qscore: an algorithm for evaluating SEQUEST database search results. J Am Soc Mass Spectrom 13:378-386. doi:10.1016/S1044-0305(02)00352-5 (Pubitemid 34280088)
    • (2002) Journal of the American Society for Mass Spectrometry , vol.13 , Issue.4 , pp. 378-386
    • Moore, R.E.1    Young, M.K.2    Lee, T.D.3
  • 105
    • 73649131275 scopus 로고    scopus 로고
    • MSQuant, an open source platform for mass spectrometry-based quantitative proteomics
    • Mortensen P, Gouw J, Olsen JV et al (2010) MSQuant, an open source platform for mass spectrometry-based quantitative proteomics. J Proteome Res 9:393-403
    • (2010) J Proteome Res , vol.9 , pp. 393-403
    • Mortensen, P.1    Gouw, J.2    Olsen, J.V.3
  • 106
    • 38649095599 scopus 로고    scopus 로고
    • An assessment of software solutions for the analysis of mass spectrometry based quantitative proteomics data
    • DOI 10.1021/pr700758r
    • Mueller LN, Brusniak M-Y, Mani DR, Aebersold R (2008) An assessment of software solutions for the analysis of mass spectrometry based quantitative proteomics data. J Proteome Res 7:51-61. doi:10.1021/pr700758r (Pubitemid 351171115)
    • (2008) Journal of Proteome Research , vol.7 , Issue.1 , pp. 51-61
    • Mueller, L.N.1    Brusniak, M.-Y.2    Mani, D.R.3    Aebersold, R.4
  • 107
    • 79551500036 scopus 로고    scopus 로고
    • Less label, more free: Approaches in label-free quantitative mass spectrometry
    • doi:10.1002/pmic.201000553
    • Neilson KA, Ali NA, Muralidharan S et al (2011) Less label, more free: approaches in label-free quantitative mass spectrometry. Proteomics 11:535-553. doi:10.1002/pmic.201000553
    • (2011) Proteomics , vol.11 , pp. 535-553
    • Neilson, K.A.1    Ali, N.A.2    Muralidharan, S.3
  • 108
    • 77957221582 scopus 로고    scopus 로고
    • A survey of computational methods and error rate estimation procedures for peptide and protein identification in shotgun proteomics
    • doi: 10.1016/j.jprot.2010.08.009
    • Nesvizhskii AI (2010) A survey of computational methods and error rate estimation procedures for peptide and protein identification in shotgun proteomics. J Proteomics 73:2092-2123. doi: 10.1016/j.jprot.2010.08.009
    • (2010) J Proteomics , vol.73 , pp. 2092-2123
    • Nesvizhskii, A.I.1
  • 109
    • 27644555055 scopus 로고    scopus 로고
    • Interpretation of shotgun proteomic data: The protein inference problem
    • DOI 10.1074/mcp.R500012-MCP200
    • Nesvizhskii AI, Aebersold R (2005) Interpretation of shotgun proteomic data: the protein inference problem. Mol Cell Proteomics 4:1419-1440. doi:10.1074/mcp.R500012-MCP200 (Pubitemid 41555469)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.10 , pp. 1419-1440
    • Nesvizhskii, A.I.1    Aebersold, R.2
  • 110
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • DOI 10.1021/ac0341261
    • Nesvizhskii AI, Keller A, Kolker E, Aebersold R (2003) A statistical model for identifying proteins by tandem mass spectrometry. Anal Chem 75:4646-4658. doi:10.1021/ac0341261 (Pubitemid 37082259)
    • (2003) Analytical Chemistry , vol.75 , Issue.17 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 114
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong S, Mann M (2005) Mass spectrometry-based proteomics turns quantitative. Nat Chem Biol 1:252-262
    • (2005) Nat Chem Biol , vol.1 , pp. 252-262
    • Ong, S.1    Mann, M.2
  • 115
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong S-E, Blagoev B, Kratchmarova I et al (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 1:376-386
    • (2002) Mol Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.-E.1    Blagoev, B.2    Kratchmarova, I.3
  • 116
    • 70449412362 scopus 로고    scopus 로고
    • ITRAQ underestimation in simple and complex mixtures: The good, the bad and the ugly
    • doi:10.1021/pr900634c
    • Ow SY, Salim M, Noirel J et al (2009) iTRAQ underestimation in simple and complex mixtures: ''the good, the bad and the ugly. J Proteome Res 8:5347-5355. doi:10.1021/pr900634c
    • (2009) J Proteome Res , vol.8 , pp. 5347-5355
    • Ow, S.Y.1    Salim, M.2    Noirel, J.3
  • 117
    • 68049114653 scopus 로고    scopus 로고
    • Precursor acquisition independent from ion count: How to dive deeper into the proteomics ocean
    • doi:10.1021/ac 900888s
    • Panchaud A, Scherl A, Shaffer SA et al (2009) Precursor acquisition independent from ion count: how to dive deeper into the proteomics ocean. Anal Chem 81:6481-6488. doi:10.1021/ac 900888s
    • (2009) Anal Chem , vol.81 , pp. 6481-6488
    • Panchaud, A.1    Scherl, A.2    Shaffer, S.A.3
  • 119
    • 41549117597 scopus 로고    scopus 로고
    • A quantitative analysis software tool for mass spectrometry-based proteomics
    • DOI 10.1038/nmeth.1195, PII NMETH.1195
    • Park SK, Venable JD, Xu T, Yates JR (2008) A quantitative analysis software tool for mass spectrometry-based proteomics. Nat Methods 5:319-322. doi:10.1038/nmeth.1195 (Pubitemid 351459367)
    • (2008) Nature Methods , vol.5 , Issue.4 , pp. 319-322
    • Park, S.K.1    Venable, J.D.2    Xu, T.3    Yates III, J.R.4
  • 120
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJ, Creasy DM, Cottrell JS (1999) Probabilitybased protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20:3551-3567. doi:10.1002/(SICI)1522-2683(19991201)20:18\ 3551:AIDELPS3551[ 3.0.CO;2-2 (Pubitemid 30007252)
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 121
    • 77950841080 scopus 로고    scopus 로고
    • Peek a peak: A glance at statistics for quantitative label-free proteomics
    • doi:10.1586/epr.09.107
    • Podwojski K, Eisenacher M, Kohl M et al (2010) Peek a peak: a glance at statistics for quantitative label-free proteomics. Expert Rev Proteomics 7:249-261. doi:10.1586/epr.09.107
    • (2010) Expert Rev Proteomics , vol.7 , pp. 249-261
    • Podwojski, K.1    Eisenacher, M.2    Kohl, M.3
  • 124
    • 0031782137 scopus 로고    scopus 로고
    • Investigation of the quantitative capabilities of an electrospray ionization ion trap/linear time-of-flight mass spectrometer
    • Purves R, Gabryelski W, Li L (1998) Investigation of the quantitative capabilities of an electrospray ionization ion trap linear time-of-flight mass spectrometer. Rapid Commun Mass Spectrom 12:695-700 (Pubitemid 28244522)
    • (1998) Rapid Communications in Mass Spectrometry , vol.12 , Issue.11 , pp. 695-700
    • Purves, R.W.1    Gabryelski, W.2    Li, L.3
  • 125
    • 77954502710 scopus 로고    scopus 로고
    • Peptide classifier for protein inference and targeted quantitative proteomics
    • doi:10.1038/nbt0710-647
    • Qeli E, Ahrens CH (2010) Peptide classifier for protein inference and targeted quantitative proteomics. Nat Biotechnol 28:647-650. doi:10.1038/nbt0710-647
    • (2010) Nat Biotechnol , vol.28 , pp. 647-650
    • Qeli, E.1    Ahrens, C.H.2
  • 126
    • 84863304598 scopus 로고    scopus 로고
    • R Development Core Team R Foundation for Statistical Computing, Vienna, Austria
    • R Development Core Team (2008) R: a language and environment for statistical computing. R Foundation for Statistical Computing, Vienna, Austria. http://www.R-project.org
    • (2008) R A Language and Environment for Statistical Computing
  • 127
    • 0036470450 scopus 로고    scopus 로고
    • What does it mean to identify a protein in proteomics?
    • DOI 10.1016/S0968-0004(01)02021-7, PII S0968000401020217
    • Rappsilber J, Mann M (2002) What does it mean to identify a protein in proteomics? Trends Biochem Sci 27:74-78 (Pubitemid 34164322)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.2 , pp. 74-78
    • Rappsilber, J.1    Mann, M.2
  • 128
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • doi:10.1074/mcp.M400129-MCP200
    • Ross PL, Huang YN, Marchese JN et al (2004) Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol Cell Proteomics 3:1154-1169. doi:10.1074/mcp.M400129-MCP200
    • (2004) Mol Cell Proteomics , vol.3 , pp. 1154-1169
    • Ross, P.L.1    Huang, Y.N.2    Marchese, J.N.3
  • 129
    • 42549103254 scopus 로고    scopus 로고
    • Significance analysis of microarray for relative quantitation of LC/MS data in proteomics
    • DOI 10.1186/1471-2105-9-187
    • Roxas BAP, Li Q (2008) Significance analysis of microarray for relative quantitation of LC/MS data in proteomics. BMC Bioinformatics 9:187. doi:10.1186/1471-2105-9-187 (Pubitemid 351584197)
    • (2008) BMC Bioinformatics , vol.9 , pp. 187
    • Roxas, B.A.P.1    Li, Q.2
  • 131
    • 79952304665 scopus 로고    scopus 로고
    • Generic workflow for quality assessment of quantitative label-free LC-MS analysis
    • doi:10.1002/pmic.201000493
    • Sandin M, Krogh M, Hansson K, Levander F (2011) Generic workflow for quality assessment of quantitative label-free LC-MS analysis. Proteomics 11:1114-1124. doi:10.1002/pmic.201000493
    • (2011) Proteomics , vol.11 , pp. 1114-1124
    • Sandin, M.1    Krogh, M.2    Hansson, K.3    Levander, F.4
  • 132
    • 74049163277 scopus 로고    scopus 로고
    • Enriching quantitative proteomics with SI(N)
    • doi:10.1038/nbt0110-40
    • Sardiu ME, Washburn MP (2010) Enriching quantitative proteomics with SI(N). Nat Biotechnol 28:40-42. doi:10.1038/nbt0110-40
    • (2010) Nat Biotechnol , vol.28 , pp. 40-42
    • Sardiu, M.E.1    Washburn, M.P.2
  • 133
    • 78149391462 scopus 로고    scopus 로고
    • H-score, a mass accuracy driven rescoring approach for improved peptide identification in modification rich samples
    • doi:10.1021/pr1006813
    • Savitski MM, Mathieson T, Becher I, Bantscheff M (2010) H-score, a mass accuracy driven rescoring approach for improved peptide identification in modification rich samples. J Proteome Res 9:5511-5516. doi:10.1021/pr1006813
    • (2010) J Proteome Res , vol.9 , pp. 5511-5516
    • Savitski, M.M.1    Mathieson, T.2    Becher, I.3    Bantscheff, M.4
  • 134
    • 79953212975 scopus 로고    scopus 로고
    • Confident phosphorylation site localization using the Mascot Delta Score
    • M110.003830 doi: 10.1074/mcp.M110. 003830
    • Savitski MM, Lemeer S, Boesche M et al (2011) Confident phosphorylation site localization using the Mascot Delta Score. Mol Cell Proteomics 10:M110.003830. doi: 10.1074/mcp.M110. 003830
    • (2011) Mol Cell Proteomics , vol.10
    • Savitski, M.M.1    Lemeer, S.2    Boesche, M.3
  • 135
    • 77952538049 scopus 로고    scopus 로고
    • Quantitation in mass-spectrometrybased proteomics
    • doi: 10.1146/annurev-arplant-042809-112132
    • Schulze WX, Usadel B (2010) Quantitation in mass-spectrometrybased proteomics. Annu Rev Plant Biol 61:491-516. doi: 10.1146/annurev-arplant-042809- 112132
    • (2010) Annu Rev Plant Biol , vol.61 , pp. 491-516
    • Schulze, W.X.1    Usadel, B.2
  • 136
    • 79956322553 scopus 로고    scopus 로고
    • Global quantification of mammalian gene expression control
    • doi: 10.1038/nature10098
    • Schwanhäusser B, Busse D, Li N et al (2011) Global quantification of mammalian gene expression control. Nature 473:337-342. doi: 10.1038/nature10098
    • (2011) Nature , vol.473 , pp. 337-342
    • Schwanhäusser, B.1    Busse, D.2    Li, N.3
  • 137
    • 77149128956 scopus 로고    scopus 로고
    • De novo sequencing of peptides by MS/MS
    • doi: 10.1002/pmic.200900459
    • Seidler J, Zinn N, Boehm ME, Lehmann WD (2010) De novo sequencing of peptides by MS/MS. Proteomics 10:634-649. doi: 10.1002/pmic.200900459
    • (2010) Proteomics , vol.10 , pp. 634-649
    • Seidler, J.1    Zinn, N.2    Boehm, M.E.3    Lehmann, W.D.4
  • 138
    • 58149209843 scopus 로고
    • Determination of monoisotopic masses and ion populations for large biomolecules from resolved isotopic distributions
    • Senko M, Beu S, McLafferty F (1995) Determination of monoisotopic masses and ion populations for large biomolecules from resolved isotopic distributions. J Am Soc Mass Spectrom 6:229-233
    • (1995) J Am Soc Mass Spectrom , vol.6 , pp. 229-233
    • Senko, M.1    Beu, S.2    McLafferty, F.3
  • 139
    • 27744450286 scopus 로고    scopus 로고
    • I-Tracker: For quantitative proteomics using iTRAQ
    • DOI 10.1186/1471-2164-6-145
    • Shadforth IP, Dunkley TPJ, Lilley KS, Bessant C (2005) i-Tracker: for quantitative proteomics using iTRAQ. BMC Genomics 6:145. doi:10.1186/1471-2164- 6-145 (Pubitemid 41631205)
    • (2005) BMC Genomics , vol.6 , pp. 145
    • Shadforth, I.P.1    Dunkley, T.P.J.2    Lilley, K.S.3    Bessant, C.4
  • 140
    • 70449533143 scopus 로고    scopus 로고
    • A software program for more reliable precursor ion assignation from LC- MS analysis using LTQ ultra zoom scan
    • doi:10.1016/j.jprot.2009.08.009
    • Shinkawa T, Nagano K, Inomata N, Haramura M (2009) A software program for more reliable precursor ion assignation from LC- MS analysis using LTQ ultra zoom scan. J Proteomics 73:357-360. doi:10.1016/j.jprot.2009.08.009
    • (2009) J Proteomics , vol.73 , pp. 357-360
    • Shinkawa, T.1    Nagano, K.2    Inomata, N.3    Haramura, M.4
  • 142
    • 64149101160 scopus 로고    scopus 로고
    • Quantitative mass spectrometry-based techniques for clinical use: Biomarker identification and quantification
    • doi:10.1016/j.jchromb.2008. 11.023
    • Simpson KL, Whetton AD, Dive C (2009) Quantitative mass spectrometry-based techniques for clinical use: biomarker identification and quantification. J Chromatogr B Analyt Technol Biomed Life Sci 877:1240-1249. doi:10.1016/j.jchromb.2008. 11.023
    • (2009) J Chromatogr B Analyt Technol Biomed Life Sci , vol.877 , pp. 1240-1249
    • Simpson, K.L.1    Whetton, A.D.2    Dive, C.3
  • 143
    • 0036253914 scopus 로고    scopus 로고
    • An accurate mass tag strategy for quantitative and high-throughput proteome measurements
    • DOI 10.1002/1615-9861(200205)2:5<513::AID-PROT513>3.0.CO;2-W
    • Smith RD, Anderson GA, Lipton MS et al (2002) An accurate mass tag strategy for quantitative and high-throughput proteome measurements. Proteomics 2:513-523. doi:10.1002/1615-9861 (200205)2:5\513:AID-PROT513[3.0.CO;2-W (Pubitemid 34507341)
    • (2002) Proteomics , vol.2 , Issue.5 , pp. 513-523
    • Smith, R.D.1    Anderson, G.A.2    Lipton, M.S.3    Pasa-Tolic, L.4    Shen, Y.5    Conrads, T.P.6    Veenstra, T.D.7    Udseth, H.R.8
  • 144
    • 33644872577 scopus 로고    scopus 로고
    • Limma: Linear models for microarray data
    • Gentleman R, Carey VJ, Huber W et al (eds) Springer New York
    • Smyth G (2005) Limma: linear models for microarray data. In: Gentleman R, Carey VJ, Huber W et al (eds) Statistics for biology and health. Springer New York, pp 397-420
    • (2005) Statistics for Biology and Health , pp. 397-420
    • Smyth, G.1
  • 145
    • 4444335470 scopus 로고    scopus 로고
    • The ABCs (and XYZs) of peptide sequencing
    • Steen H, Mann M (2004) The ABCs (and XYZs) of peptide sequencing. Nat Rev Mol Cell Biol 5:699-711
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 699-711
    • Steen, H.1    Mann, M.2
  • 147
    • 56149086397 scopus 로고    scopus 로고
    • Decision tree-driven tandem mass spectrometry for shotgun proteomics
    • doi:10.1038/nmeth.1260
    • Swaney DL, McAlister GC, Coon JJ (2008) Decision tree-driven tandem mass spectrometry for shotgun proteomics. Nat Methods 5:959-964. doi:10.1038/nmeth. 1260
    • (2008) Nat Methods , vol.5 , pp. 959-964
    • Swaney, D.L.1    McAlister, G.C.2    Coon, J.J.3
  • 148
    • 0036393898 scopus 로고    scopus 로고
    • DTA select and contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb DL, McDonald WH, Yates JR (2002) DTA select and contrast: tools for assembling and comparing protein identifications from shotgun proteomics. J Proteome Res 1:21-26
    • (2002) J Proteome Res , vol.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates, J.R.3
  • 151
    • 79951531728 scopus 로고    scopus 로고
    • Overview of quantitative LC-MS techniques for proteomics and activitomics
    • doi:10.1007/978-1-60761-780-8-2
    • Timms JF, Cutillas PR (2010) Overview of quantitative LC-MS techniques for proteomics and activitomics. Methods Mol Biol 658:19-45. doi:10.1007/978-1-60761-780-8-2
    • (2010) Methods Mol Biol , vol.658 , pp. 19-45
    • Timms, J.F.1    Cutillas, P.R.2
  • 152
    • 71049189969 scopus 로고    scopus 로고
    • Normalization and statistical analysis of quantitative proteomics data generated by metabolic labeling
    • doi: 10.1074/mcp.M800462-MCP200
    • Ting L, Cowley MJ, Hoon SL et al (2009) Normalization and statistical analysis of quantitative proteomics data generated by metabolic labeling. Mol Cell Proteomics 8:2227-2242. doi: 10.1074/mcp.M800462-MCP200
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2227-2242
    • Ting, L.1    Cowley, M.J.2    Hoon, S.L.3
  • 153
    • 76649139789 scopus 로고    scopus 로고
    • IDEAL-Q, an automated tool for label-free quantitation analysis using an efficient peptide alignment approach and spectral data validation
    • doi:10.1074/mcp.M900177-MCP200
    • Tsou C-C, Tsai C-F, Tsui Y-H et al (2010) IDEAL-Q, an automated tool for label-free quantitation analysis using an efficient peptide alignment approach and spectral data validation. Mol Cell Proteomics 9:131-144. doi:10.1074/mcp.M900177-MCP200
    • (2010) Mol Cell Proteomics , vol.9 , pp. 131-144
    • Tsou, C.-C.1    Tsai, C.-F.2    Tsui, Y.-H.3
  • 154
    • 28644447919 scopus 로고    scopus 로고
    • Identification of post-translational modifications by blind search of mass spectra
    • DOI 10.1038/nbt1168
    • Tsur D, Tanner S, Zandi E et al (2005) Identification of posttranslational modifications by blind search of mass spectra. Nat Biotechnol 23:1562-1567. doi:10.1038/nbt1168 (Pubitemid 41752935)
    • (2005) Nature Biotechnology , vol.23 , Issue.12 , pp. 1562-1567
    • Tsur, D.1    Tanner, S.2    Zandi, E.3    Bafna, V.4    Pevzner, P.A.5
  • 156
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlü M, Morgan ME, Minden JS (1997) Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis 18:2071-2077. doi:10.1002/elps. 1150181133 (Pubitemid 27501267)
    • (1997) Electrophoresis , vol.18 , Issue.11 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 158
    • 35349002401 scopus 로고    scopus 로고
    • Using a Poisson approximation to predict the isotopic distribution of sulphur-containing peptides in a peptide-centric proteomic approach
    • DOI 10.1002/rcm.3237
    • Valkenborg D, Assam P, Thomas G et al (2007) Using a Poisson approximation to predict the isotopic distribution of sulphurcontaining peptides in a peptide-centric proteomic approach. Rapid Commun Mass Spectrom 21:3387-3391. doi:10.1002/rcm. 3237 (Pubitemid 47598793)
    • (2007) Rapid Communications in Mass Spectrometry , vol.21 , Issue.20 , pp. 3387-3391
    • Valkenborg, D.1    Assam, P.2    Thomas, G.3    Krols, L.4    Kas, K.5    Burzykowski, T.6
  • 159
    • 65649154049 scopus 로고    scopus 로고
    • StatQuant: A post-quantification analysis toolbox for improving quantitative mass spectrometry
    • doi:10.1093/bioinformatics/btp181
    • van Breukelen B, van den Toorn HWP, Drugan MM, Heck AJR (2009) StatQuant: a post-quantification analysis toolbox for improving quantitative mass spectrometry. Bioinformatics 25:1472-1473. doi:10.1093/bioinformatics/btp181
    • (2009) Bioinformatics , vol.25 , pp. 1472-1473
    • Van Breukelen, B.1    Van Den Toorn Hwp2    Drugan, M.M.3    Ajr, H.4
  • 160
    • 34548356772 scopus 로고    scopus 로고
    • An experimental correction for arginine-to-proline conversion artifacts in SILAC-based quantitative proteomics [1]
    • DOI 10.1038/nmeth0907-677, PII NMETH0907-677
    • Van Hoof D, Pinkse MWH, Oostwaard DWV et al (2007) An experimental correction for arginine-to-proline conversion artifacts in SILAC-based quantitative proteomics. Nat Methods 4:677-678. doi:10.1038/nmeth0907-677 (Pubitemid 47338150)
    • (2007) Nature Methods , vol.4 , Issue.9 , pp. 677-678
    • Van Hoof, D.1    Pinkse, M.W.H.2    Oostwaard, D.W.-V.3    Mummery, C.L.4    Heck, A.J.R.5    Krijgsveld, J.6
  • 161
    • 40549126588 scopus 로고    scopus 로고
    • Alignment of LC-MS images, with applications to biomarker discovery and protein identification
    • DOI 10.1002/pmic.200700791
    • Vandenbogaert M, Li-Thiao-Té S, Kaltenbach H-M et al (2008) Alignment of LC-MS images, with applications to biomarker discovery and protein identification. Proteomics 8:650-672. doi: 10.1002/pmic.200700791 (Pubitemid 351362928)
    • (2008) Proteomics , vol.8 , Issue.4 , pp. 650-672
    • Vandenbogaert, M.1    Li-Thiao-Te, S.2    Kaltenbach, H.-M.3    Zhang, R.4    Aittokallio, T.5    Schwikowski, B.6
  • 162
    • 35448967750 scopus 로고    scopus 로고
    • Top-down quantitation and characterization of SILAC-labeled proteins
    • DOI 10.1016/j.jasms.2007.09.001, PII S1044030507007659
    • Waanders LF, Hanke S, Mann M (2007) Top-down quantitation and characterization of SILAC-labeled proteins. J Am Soc Mass Spectrom 18:2058-2064. doi:10.1016/j.jasms.2007.09.001 (Pubitemid 47633966)
    • (2007) Journal of the American Society for Mass Spectrometry , vol.18 , Issue.11 , pp. 2058-2064
    • Waanders, L.F.1    Hanke, S.2    Mann, M.3
  • 163
    • 79953231670 scopus 로고    scopus 로고
    • Accurate quantification of more than 4000 mouse tissue proteins reveals minimal proteome changes during aging
    • M110.004523 doi: 10.1074/mcp.M110.004523
    • Walther DM, Mann M (2011) Accurate quantification of more than 4000 mouse tissue proteins reveals minimal proteome changes during aging. Mol Cell Proteomics 10:M110.004523. doi: 10.1074/mcp.M110.004523
    • (2011) Mol Cell Proteomics , vol.10
    • Walther, D.M.1    Mann, M.2
  • 164
    • 45249094536 scopus 로고    scopus 로고
    • Exploring the precursor ion exclusion feature of liquid chromatography-electrospray ionization quadrupole time-of-flight mass spectrometry for improving protein identification in shotgun proteome analysis
    • DOI 10.1021/ac800260w
    • Wang N, Li L (2008) Exploring the precursor ion exclusion feature of liquid chromatography-electrospray ionization quadrupole timeof- flight mass spectrometry for improving protein identification in shotgun proteome analysis. Anal Chem 80:4696-4710. doi: 10.1021/ac800260w (Pubitemid 351842350)
    • (2008) Analytical Chemistry , vol.80 , Issue.12 , pp. 4696-4710
    • Wang, N.1    Li, L.2
  • 165
    • 70349760656 scopus 로고    scopus 로고
    • High-resolution two-dimensional electrophoresis
    • doi:10.1007/978-1-60761- 157-8-2
    • Weiss W, Görg A (2009) High-resolution two-dimensional electrophoresis. Methods Mol Biol 564:13-32. doi:10.1007/978-1-60761- 157-8-2
    • (2009) Methods Mol Biol , vol.564 , pp. 13-32
    • Weiss, W.1    Görg, A.2
  • 167
    • 79961013401 scopus 로고    scopus 로고
    • Correct interpretation of comprehensive phosphorylation dynamics requires normalization by protein expression changes
    • M111.009654 doi:10.1074/mcp.M111.009654
    • Wu R, Dephoure N, Haas W et al (2011) Correct interpretation of comprehensive phosphorylation dynamics requires normalization by protein expression changes. Mol Cell Proteomics 10:M111.009654. doi:10.1074/mcp.M111. 009654
    • (2011) Mol Cell Proteomics , vol.10
    • Wu, R.1    Dephoure, N.2    Haas, W.3
  • 168
    • 19444363756 scopus 로고    scopus 로고
    • Mass spectrometry-based quantitative proteomic profiling
    • DOI 10.1093/bfgp/4.1.27, Proteomics Tools-Advances and Applications
    • Yan W, Chen SS (2005) Mass spectrometry-based quantitative proteomic profiling. Brief Funct Genomic Proteomic 4:27-38 (Pubitemid 40724165)
    • (2005) Briefings in Functional Genomics and Proteomics , vol.4 , Issue.1 , pp. 27-38
    • Yan, W.1    Chen, S.S.2
  • 170
    • 0035499083 scopus 로고    scopus 로고
    • Fractionation of isotopically labeled peptides in quantitative proteomics
    • DOI 10.1021/ac010583a
    • Zhang R, Sioma CS, Wang S, Regnier FE (2001) Fractionation of isotopically labeled peptides in quantitative proteomics. Anal Chem 73:5142-5149 (Pubitemid 33032229)
    • (2001) Analytical Chemistry , vol.73 , Issue.21 , pp. 5142-5149
    • Zhang, R.1    Sioma, C.S.2    Wang, S.3    Regnier, F.E.4
  • 171
    • 70549106483 scopus 로고    scopus 로고
    • Review of peak detection algorithms in liquid-chromatography-mass spectrometry
    • doi:10.2174/138920209789177638
    • Zhang J, Gonzalez E, Hestilow T et al (2009) Review of peak detection algorithms in liquid-chromatography-mass spectrometry. Curr Genomics 10:388-401. doi:10.2174/138920209789177638
    • (2009) Curr Genomics , vol.10 , pp. 388-401
    • Zhang, J.1    Gonzalez, E.2    Hestilow, T.3
  • 172
    • 74049115774 scopus 로고    scopus 로고
    • Mass spectrometry-based label-free quantitative proteomics
    • doi:10.1155/2010/840518
    • Zhu W, Smith JW, Huang C-M (2010) Mass spectrometry-based label-free quantitative proteomics. J Biomed Biotechnol 2010:840518. doi:10.1155/2010/ 840518
    • (2010) J Biomed Biotechnol , vol.2010 , pp. 840518
    • Zhu, W.1    Smith, J.W.2    Huang, C.-M.3


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