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Volumn 5, Issue 22, 2013, Pages 2837-2856

Pre-analytical and analytical variability in absolute quantitative MRM-based plasma proteomic studies

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MARKER; CARBON 13; NITROGEN 15; PLASMA PROTEIN; TRYPSIN;

EID: 84887905619     PISSN: 17576180     EISSN: 17576199     Source Type: Journal    
DOI: 10.4155/bio.13.245     Document Type: Review
Times cited : (37)

References (142)
  • 1
    • 79953184687 scopus 로고    scopus 로고
    • Enhanced sensitivity for selected reaction monitoring mass spectrometry-based targeted proteomics using a dual stage electrodynamic ion funnel interface
    • doi:10.1074/mcp.M000062-MCP201
    • Hossain M, Robinson EW, Liu T et al. Enhanced sensitivity for selected reaction monitoring mass spectrometry-based targeted proteomics using a dual stage electrodynamic ion funnel interface. Mol. Cell. Proteomics 10(2), doi:10.1074/mcp.M000062-MCP201 (2011
    • (2011) Mol. Cell. Proteomics , vol.10 , Issue.2
    • Hossain, M.1    Robinson, E.W.2    Liu, T.3
  • 2
    • 67651173106 scopus 로고    scopus 로고
    • Proteomics by mass spectrometry: Approaches, advances, and applications
    • Yates JR, Ruse CI, Nakorchevsky A. Proteomics by mass spectrometry: Approaches, advances, and applications. Annu. Rev. Biomed. Eng. 11, 49-79 (2009
    • (2009) Annu. Rev. Biomed. Eng , vol.11 , pp. 49-79
    • Yates, J.R.1    Ruse, C.I.2    Nakorchevsky, A.3
  • 3
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • Domon B, Aebersold R. Mass spectrometry and protein analysis. Science 312(5771), 212-217 (2006
    • (2006) Science , vol.312 , Issue.5771 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 6
    • 32444436985 scopus 로고    scopus 로고
    • Top-down approaches for measuring expression ratios of intact yeast proteins using Fourier transform mass spectrometry
    • DOI 10.1021/ac050993p
    • Du Y, Parks BA, Sohn S, Kwast KE, Kelleher NL. Top-down approaches for measuring expression ratios of intact yeast proteins using Fourier transform mass spectrometry. Anal. Chem. 78(3), 686-694 (2006 (Pubitemid 43228574)
    • (2006) Analytical Chemistry , vol.78 , Issue.3 , pp. 686-694
    • Du, Y.1    Parks, B.A.2    Sohn, S.3    Kwast, K.E.4    Kelleher, N.L.5
  • 7
    • 0036645727 scopus 로고    scopus 로고
    • Processing complex mixtures of intact proteins for direct analysis by mass spectrometry
    • DOI 10.1021/ac020049i
    • Meng F, Cargile BJ, Patrie SM, Johnson JR, McLoughlin SM, Kelleher NL. Processing complex mixtures of intact proteins for direct analysis by mass spectrometry. Anal. Chem. 74(13), 2923-2929 (2002 (Pubitemid 34755203)
    • (2002) Analytical Chemistry , vol.74 , Issue.13 , pp. 2923-2929
    • Meng, F.1    Cargile, B.J.2    Patrie, S.M.3    Johnson, J.R.4    McLoughlin, S.M.5    Kelleher, N.L.6
  • 10
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb DL, McDonald WH, Yates Jr 3rd. DTASelect and contrast: Tools for assembling and comparing protein identifications from shotgun proteomics. J. Proteome Res. 1(1), 21-26 (2002
    • (2002) J. Proteome Res , vol.1 , Issue.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates III, J.R.3
  • 11
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • DOI 10.1038/85686
    • Washburn MP, Wolters D, Yates Jr 3rd. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotech. 19(3), 242-247 (2001 (Pubitemid 32220565)
    • (2001) Nature Biotechnology , vol.19 , Issue.3 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 12
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong S, Mann M. Mass spectrometry-based proteomics turns quantitative. Nat. Chem. Biol. 1(5), 252-262 (2005
    • (2005) Nat. Chem. Biol , vol.1 , Issue.5 , pp. 252-262
    • Ong, S.1    Mann, M.2
  • 13
    • 77952538049 scopus 로고    scopus 로고
    • Quantitation in mass-spectrometry-based proteomics
    • Schulze WX, Usadel B. Quantitation in mass-spectrometry-based proteomics. Annu. Rev. Plant Biol. 61, 491-516 (2010
    • (2010) Annu. Rev. Plant Biol , vol.61 , pp. 491-516
    • Schulze, W.X.1    Usadel, B.2
  • 16
    • 84861990380 scopus 로고    scopus 로고
    • Selected reaction monitoring-based proteomics: Workflows, potential, pitfalls and future directions
    • Picotti P, Aebersold R. Selected reaction monitoring-based proteomics: Workflows, potential, pitfalls and future directions. Nat. Methods 9(6), 555-566 (2012
    • (2012) Nat. Methods , vol.9 , Issue.6 , pp. 555-566
    • Picotti, P.1    Aebersold, R.2
  • 17
    • 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, Turecek F, Gelb MH, Aebersold R. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechol. 17(10), 994-999 (1999 (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
  • 18
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross PL, Huang YN, Marchese JN et al. Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol. Cell. Proteomics 3(12), 1154-1169 (2004
    • (2004) Mol. Cell. Proteomics , vol.3 , Issue.12 , pp. 1154-1169
    • Ross, P.L.1    Huang, Y.N.2    Marchese, J.N.3
  • 19
    • 84864134650 scopus 로고    scopus 로고
    • Relative protein quantification by MS/MS using the tandem mass tag technology
    • Dayon L, Sanchez JC. Relative protein quantification by MS/MS using the tandem mass tag technology. Methods Mol. Biol. 893, 115-127 (2012
    • (2012) Methods Mol. Biol , vol.893 , pp. 115-127
    • Dayon, L.1    Sanchez, J.C.2
  • 21
    • 70549113220 scopus 로고    scopus 로고
    • Perspectives of targeted mass spectrometry for protein biomarker verification
    • Huttenhain R, Malmstrom J, Picotti P, Aebersold R. Perspectives of targeted mass spectrometry for protein biomarker verification. Curr. Opin. Chem. Biol. 13(5-6), 518-525 (2009
    • (2009) Curr. Opin. Chem. Biol , vol.13 , Issue.5-6 , pp. 518-525
    • Huttenhain, R.1    Malmstrom, J.2    Picotti, P.3    Aebersold, R.4
  • 22
    • 67649511917 scopus 로고    scopus 로고
    • Isotope dilution strategies for absolute quantitative proteomics
    • Brun V, Masselon C, Garin J, Dupuis A. Isotope dilution strategies for absolute quantitative proteomics. J. Proteomics 72, 740-749 (2009
    • (2009) J. Proteomics , vol.72 , pp. 740-749
    • Brun, V.1    Masselon, C.2    Garin, J.3    Dupuis, A.4
  • 23
    • 33645721632 scopus 로고    scopus 로고
    • Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins
    • Anderson L, Hunter CL. Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins. Mol. Cell. Proteomics 5(4), 573-588 (2006
    • (2006) Mol. Cell. Proteomics , vol.5 , Issue.4 , pp. 573-588
    • Anderson, L.1    Hunter, C.L.2
  • 25
    • 79955865815 scopus 로고    scopus 로고
    • In-depth proteomics of ovarian cancer ascites: Combining shotgun proteomics and selected reaction monitoring mass spectrometry
    • Elschenbroich S, Ignatchenko V, Clarke B et al. In-depth proteomics of ovarian cancer ascites: Combining shotgun proteomics and selected reaction monitoring mass spectrometry. J. Proteome Res. 10(5), 2286-2299 (2011
    • (2011) J. Proteome Res , vol.10 , Issue.5 , pp. 2286-2299
    • Elschenbroich, S.1    Ignatchenko, V.2    Clarke, B.3
  • 26
    • 79955481027 scopus 로고    scopus 로고
    • Priority actions for the non-communicable disease crisis
    • Beaglehole R, Bonita R, Horton R et al. Priority actions for the non-communicable disease crisis. Lancet 377(9775), 1438-1447 (2011
    • (2011) Lancet , vol.377 , Issue.9775 , pp. 1438-1447
    • Beaglehole, R.1    Bonita, R.2    Horton, R.3
  • 27
    • 33845338724 scopus 로고    scopus 로고
    • Projections of global mortality and burden of disease from 2002 to 2030
    • Mathers CD, Loncar D. Projections of global mortality and burden of disease from 2002 to 2030. PLoS Med. 3(11), e442 (2006
    • (2006) PLoS Med , vol.3 , Issue.11
    • Mathers, C.D.1    Loncar, D.2
  • 28
    • 0142095224 scopus 로고    scopus 로고
    • C-reactive protein and atherothrombosis-beyond a biomarker: An actual partaker of lesion formation
    • Verma S, Yeh ET. C-reactive protein and atherothrombosis-beyond a biomarker: An actual partaker of lesion formation. Am. J. Physiol. Regul. Integr. Comp. Physiol. 5(285), 5 (2003
    • (2003) Am. J. Physiol. Regul. Integr. Comp. Physiol , vol.5 , Issue.285 , pp. 5
    • Verma, S.1    Yeh, E.T.2
  • 29
    • 65849453194 scopus 로고    scopus 로고
    • Inflammatory biomarkers in coronary artery disease
    • 53
    • Zakynthinos E, Pappa N. Inflammatory biomarkers in coronary artery disease. J. Cardiol. 53, 53(3), 317-333 (2009
    • (2009) J. Cardiol , vol.53 , Issue.3 , pp. 317-333
    • Zakynthinos, E.1    Pappa, N.2
  • 30
    • 0001644020 scopus 로고    scopus 로고
    • The human plasma proteome: History, character, and diagnostic prospects
    • Anderson NL, Anderson NG. The human plasma proteome: History, character, and diagnostic prospects. Mol. Cell. Proteomics 1(11), 845-867 (2002
    • (2002) Mol. Cell. Proteomics , vol.1 , Issue.11 , pp. 845-867
    • Anderson, N.L.1    Anderson, N.G.2
  • 31
    • 38349037650 scopus 로고    scopus 로고
    • Isotope-labeled protein standards: Toward absolute quantitative proteomics
    • Brun V, Dupuis A, Adrait A et al. Isotope-labeled protein standards: Toward absolute quantitative proteomics. Mol. Cell. Proteomics 6(12), 2139-2149 (2007
    • (2007) Mol. Cell. Proteomics , vol.6 , Issue.12 , pp. 2139-2149
    • Brun, V.1    Dupuis, A.2    Adrait, A.3
  • 32
    • 80052389537 scopus 로고    scopus 로고
    • Production and use of stable isotope-labeled proteins for absolute quantitative proteomics
    • Lebert D, Dupuis A, Garin J, Bruley C, Brun V. Production and use of stable isotope-labeled proteins for absolute quantitative proteomics. Methods Mol. Biol. 753, 93-115 (2011
    • (2011) Methods Mol. Biol , vol.753 , pp. 93-115
    • Lebert, D.1    Dupuis, A.2    Garin, J.3    Bruley, C.4    Brun, V.5
  • 33
    • 13444260275 scopus 로고    scopus 로고
    • The absolute quantification strategy: A general procedure for the quantification of proteins and post-translational modifications
    • DOI 10.1016/j.ymeth.2004.08.018
    • Kirkpatrick DS, Gerber SA, Gygi SP. The absolute quantification strategy: A general procedure for the quantification of proteins and post-Translational modifications. Methods 35(3), 265-273 (2005 (Pubitemid 40255592)
    • (2005) Methods , vol.35 , Issue.3 SPEC.ISSUE. , pp. 265-273
    • Kirkpatrick, D.S.1    Gerber, S.A.2    Gygi, S.P.3
  • 34
    • 79551662220 scopus 로고    scopus 로고
    • Absolute quantification of protein and post-Translational modification abundance with stable isotope-labeled synthetic peptides
    • Kettenbach AN, Rush J, Gerber SA. Absolute quantification of protein and post-Translational modification abundance with stable isotope-labeled synthetic peptides. Nat. Protoc. 6(2), 175-186 (2011
    • (2011) Nat. Protoc , vol.6 , Issue.2 , pp. 175-186
    • Kettenbach, A.N.1    Rush, J.2    Gerber, S.A.3
  • 35
    • 84879974563 scopus 로고    scopus 로고
    • Multiplexed MRM-based quantitation of candidate cancer biomarker proteins in undepleted and non-enriched human plasma
    • Percy AJ, Chambers AG, Yang J, Borchers CH. Multiplexed MRM-based quantitation of candidate cancer biomarker proteins in undepleted and non-enriched human plasma. Proteomics 13(14), 2202-2215 (2013
    • (2013) Proteomics , vol.13 , Issue.14 , pp. 2202-2215
    • Percy, A.J.1    Chambers, A.G.2    Yang, J.3    Borchers, C.H.4
  • 36
    • 84865584319 scopus 로고    scopus 로고
    • Comparison of standard-flow and nano-flow liquid chromatography systems for MRM-based quantitation of putative plasma biomarker proteins
    • Percy AJ, Chambers AG, Yang J, Domanski D, Borchers CH. Comparison of standard-flow and nano-flow liquid chromatography systems for MRM-based quantitation of putative plasma biomarker proteins. Anal. Bioanal. Chem. 404(4), 1089-1101 (2012
    • (2012) Anal. Bioanal. Chem , vol.4044 , pp. 1089-1101
    • Percy, A.J.1    Chambers, A.G.2    Yang, J.3    Domanski, D.4    Borchers, C.H.5
  • 37
    • 84874610996 scopus 로고    scopus 로고
    • Multiplexed quantitation of endogenous proteins in dried blood spots by multiple reaction monitoring mass spectrometry
    • Chambers AG, Percy AJ, Yang J, Camenzind AG, Borchers CH. Multiplexed quantitation of endogenous proteins in dried blood spots by multiple reaction monitoring mass spectrometry. Mol. Cell. Proteomics 12(3), 781-791 (2013
    • (2013) Mol. Cell. Proteomics , vol.12 , Issue.3 , pp. 781-791
    • Chambers, A.G.1    Percy, A.J.2    Yang, J.3    Camenzind, A.G.4    Borchers, C.H.5
  • 38
    • 84860869256 scopus 로고    scopus 로고
    • MRM-based multiplexed quantitation of 67 putative cardiovascular disease biomarkers in human plasma
    • Domanski D, Percy AJ, Yang J et al. MRM-based multiplexed quantitation of 67 putative cardiovascular disease biomarkers in human plasma. Proteomics 12(8), 1222-1243 (2012
    • (2012) Proteomics , vol.12 , Issue.8 , pp. 1222-1243
    • Domanski, D.1    Percy, A.J.2    Yang, J.3
  • 39
    • 71049137289 scopus 로고    scopus 로고
    • Multiple reaction monitoring-based, multiplexed, absolute quantitation of 45 proteins in human plasma
    • Kuzyk MA, Smith D, Yang J et al. Multiple reaction monitoring-based, multiplexed, absolute quantitation of 45 proteins in human plasma. Mol. Cell. Proteomics 8(8), 1860-1877 (2009
    • (2009) Mol. Cell. Proteomics , vol.8 , Issue.8 , pp. 1860-1877
    • Kuzyk, M.A.1    Smith, D.2    Yang, J.3
  • 40
    • 38349068918 scopus 로고    scopus 로고
    • Quantitative, multiplexed assays for low abundance proteins in plasma by targeted mass spectrometry and stable isotope dilution
    • Keshishian H, Addona T, Burgess M, Kuhn E, Carr SA. Quantitative, multiplexed assays for low abundance proteins in plasma by targeted mass spectrometry and stable isotope dilution. Mol. Cell. Proteomics 6, 2212-2229 (2007
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 2212-2229
    • Keshishian, H.1    Addona, T.2    Burgess, M.3    Kuhn, E.4    Carr, S.A.5
  • 41
    • 71049187147 scopus 로고    scopus 로고
    • Quantification of cardiovascular biomarkers in patient plasma by targeted mass spectrometry and stable isotope dilution
    • Keshishian H, Addona T, Burgess M et al. Quantification of cardiovascular biomarkers in patient plasma by targeted mass spectrometry and stable isotope dilution. Mol. Cell. Proteomics 8, 2339-2349 (2009
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2339-2349
    • Keshishian, H.1    Addona, T.2    Burgess, M.3
  • 42
    • 82955196277 scopus 로고    scopus 로고
    • MRM assay for quantitation of complement components in human blood plasma-A feasibility study on multiple sclerosis
    • Rezeli M, Végvári A, Ottervald J, Olsson T, Laurell T, Marko-Varga G. MRM assay for quantitation of complement components in human blood plasma-A feasibility study on multiple sclerosis. J. Proteomics 75(1), 211-220 (2011
    • (2011) J. Proteomics , vol.75 , Issue.1 , pp. 211-220
    • Rezeli, M.1    Végvári, A.2    Ottervald, J.3    Olsson, T.4    Laurell, T.5    Marko-Varga, G.6
  • 43
    • 84864082548 scopus 로고    scopus 로고
    • Analysis of serum total and free PSA using immunoaffinity depletion coupled to MRM: Correlation with clinical immunoassay tests
    • Liu T, Hossain M, Schepmoes AA et al. Analysis of serum total and free PSA using immunoaffinity depletion coupled to MRM: Correlation with clinical immunoassay tests. J. Proteomics 75(15), 4747-4757 (2012
    • (2012) J. Proteomics , vol.75 , Issue.15 , pp. 4747-4757
    • Liu, T.1    Hossain, M.2    Schepmoes, A.A.3
  • 44
    • 84863923380 scopus 로고    scopus 로고
    • Reproducible quantification of cancer-Associated proteins in body fluids using targeted proteomics
    • Hüttenhain R, Soste M, Selevsek N et al. Reproducible quantification of cancer-Associated proteins in body fluids using targeted proteomics. Sci. Transl. Med. 4(142), 1-13 (2012
    • (2012) Sci. Transl. Med , vol.4 , Issue.142 , pp. 1-13
    • Hüttenhain, R.1    Soste, M.2    Selevsek, N.3
  • 45
    • 84870923756 scopus 로고    scopus 로고
    • High-Throughput SISCAPA quantitation of peptides from human plasma digests by ultrafast, liquid chromatography-free mass spectrometry
    • Razavi M, Frick LE, LaMarr WA et al. High-Throughput SISCAPA quantitation of peptides from human plasma digests by ultrafast, liquid chromatography-free mass spectrometry. J. Proteome Res. 11(12), 5642-5649 (2012
    • (2012) J. Proteome Res , vol.11 , Issue.12 , pp. 5642-5649
    • Razavi, M.1    Frick, L.E.2    LaMarr, W.A.3
  • 46
    • 76649109590 scopus 로고    scopus 로고
    • An automated and multiplexed method for high throughput peptide immunoaffinity enrichment and multiple reaction monitoring mass spectrometry-based quantification of protein biomarkers
    • Whiteaker JR, Zhao L, Anderson L, Paulovich AG. An automated and multiplexed method for high throughput peptide immunoaffinity enrichment and multiple reaction monitoring mass spectrometry-based quantification of protein biomarkers. Mol. Cell. Proteomics 9(1), 184-196 (2010
    • (2010) Mol. Cell. Proteomics , vol.9 , Issue.1 , pp. 184-196
    • Whiteaker, J.R.1    Zhao, L.2    Anderson, L.3    Paulovich, A.G.4
  • 47
    • 66449083773 scopus 로고    scopus 로고
    • Developing multiplexed assays for troponin I and interleukin-33 in plasma by peptide immunoaffinity enrichment and targeted mass spectrometry
    • Kuhn E, Addona T, Keshishian H et al. Developing multiplexed assays for troponin I and interleukin-33 in plasma by peptide immunoaffinity enrichment and targeted mass spectrometry. Clin. Chem. 55(6), 1108-1117 (2009
    • (2009) Clin. Chem , vol.55 , Issue.6 , pp. 1108-1117
    • Kuhn, E.1    Addona, T.2    Keshishian, H.3
  • 48
    • 84866538934 scopus 로고    scopus 로고
    • Antibody-free, targeted mass-spectrometric approach for quantification of proteins at low picogram per milliliter levels in human plasma/serum
    • Shi T, Fillmore TL, Sun X et al. Antibody-free, targeted mass-spectrometric approach for quantification of proteins at low picogram per milliliter levels in human plasma/serum. Proc. Natl Acad. Sci. USA 109(38), 15395-15400 (2012
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , Issue.38 , pp. 15395-15400
    • Shi, T.1    Fillmore, T.L.2    Sun, X.3
  • 49
    • 32044435777 scopus 로고    scopus 로고
    • Considerations for the use of blood plasma and serum for proteomic analysis
    • doi:10.5580
    • Lundblad RL. Considerations for the use of blood plasma and serum for proteomic analysis. The Internet Journal of Genomics and Proteomics. 1(2) doi:10.5580 (2005
    • (2005) The Internet Journal of Genomics and Proteomics , vol.1 , pp. 2
    • Lundblad, R.L.1
  • 50
    • 33748936698 scopus 로고    scopus 로고
    • Quality and reliability of routine coagulation testing: Can we trust that sample?
    • DOI 10.1097/01.mbc.0000245290.57021.46, PII 0000172120061000000001
    • Lippi G, Franchini M, Montagnana M, Salvagno GL, Poli G, Guidi GC. Quality and reliability of routine coagulation testing: Can we trust that sample? Blood Coagul. Fibrinolysis 17(7), 513-519 (2006 (Pubitemid 44434960)
    • (2006) Blood Coagulation and Fibrinolysis , vol.17 , Issue.7 , pp. 513-519
    • Lippi, G.1    Franchini, M.2    Montagnana, M.3    Salvagno, G.L.4    Poli, G.5    Guidi, G.C.6
  • 51
    • 84862333271 scopus 로고    scopus 로고
    • Pre-analytical variables for plasma and serum proteome analyses
    • Ivanov AR, Lazarev AV (Eds). Springer, Heidelberg, Germany
    • Gelfand CA, Omenn GS. Pre-Analytical variables for plasma and serum proteome analyses. In: Sample Preparation in Biological Mass Spectrometry. Ivanov AR, Lazarev AV (Eds). Springer, Heidelberg, Germany, 269-290 (2011
    • (2011) Sample Preparation in Biological Mass Spectrometry , pp. 269-290
    • Gelfand, C.A.1    Omenn, G.S.2
  • 52
    • 84873155319 scopus 로고    scopus 로고
    • Biological and methodical challenges of blood-based proteomics in the field of neurological research
    • Lista S, Faltraco F, Hampel H. Biological and methodical challenges of blood-based proteomics in the field of neurological research. Prog. Neurobiol. 101-102, 18-34 (2013
    • (2013) Prog. Neurobiol , vol.101-102 , pp. 18-34
    • Lista, S.1    Faltraco, F.2    Hampel, H.3
  • 53
    • 33747202452 scopus 로고    scopus 로고
    • Effects of preanalytical variables on peptide and protein measurements in human serum and plasma: Implications for clinical proteomics
    • DOI 10.1586/14789450.3.4.409
    • Rai AJ, Vitzthum F. Effects of pre-Analytical variables on peptide and protein measurements in human serum and plasma: Implications for clinical proteomics. Expert Rev. Proteomics 3(4), 409-426 (2006 (Pubitemid 44231984)
    • (2006) Expert Review of Proteomics , vol.3 , Issue.4 , pp. 409-426
    • Rai, A.J.1    Vitzthum, F.2
  • 54
    • 79960115783 scopus 로고    scopus 로고
    • Minimizing pre-Analytical variation of plasma samples by proper blood collection and handling
    • Yi J, Craft D, Gelfand CA. Minimizing pre-Analytical variation of plasma samples by proper blood collection and handling. Methods Mol. Biol. 728, 137-149 (2011
    • (2011) Methods Mol. Biol , vol.728 , pp. 137-149
    • Yi, J.1    Craft, D.2    Gelfand, C.A.3
  • 55
    • 75749119372 scopus 로고    scopus 로고
    • Analytical validation of protein-based multiplex assays: A workshop report by the NCI-FDA Interagency Oncology Task Force on Molecular Diagnostics
    • Rodriguez H, Težak Z, Mesri M et al. Analytical validation of protein-based multiplex assays: A workshop report by the NCI-FDA Interagency Oncology Task Force on Molecular Diagnostics. Clin. Chem. 56(2), 237-243 (2010
    • (2010) Clin. Chem , vol.56 , Issue.2 , pp. 237-243
    • Rodriguez, H.1    Težak, Z.2    Mesri, M.3
  • 56
    • 76649122499 scopus 로고    scopus 로고
    • A CPTAC inter-laboratory study characterizing a yeast performance standard for benchmarking LC-MS platform performance
    • Paulovich AG, Billheimer DD, Ham A-JL et al. A CPTAC inter-laboratory study characterizing a yeast performance standard for benchmarking LC-MS platform performance. Mol. Cell. Proteomics 9, 242-254 (2010
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 242-254
    • Paulovich, A.G.1    Billheimer, D.D.2    Ham, A.-J.L.3
  • 57
    • 78649694616 scopus 로고    scopus 로고
    • Reconstructing the pipeline by introducing multiplexed multiple reaction monitoring mass spectrometry for cancer biomarker verification: An NCI-CPTC initiative perspective
    • Rodriguez H, Rivers R, Kinsinger C et al. Reconstructing the pipeline by introducing multiplexed multiple reaction monitoring mass spectrometry for cancer biomarker verification: An NCI-CPTC initiative perspective. Proteomics Clin. Appl. 4(12), 904-914 (2010
    • (2010) Proteomics Clin. Appl , vol.4 , Issue.12 , pp. 904-914
    • Rodriguez, H.1    Rivers, R.2    Kinsinger, C.3
  • 58
    • 84863012827 scopus 로고    scopus 로고
    • Recommendations for mass spectrometry data quality metrics for open access data (corollary to the Amsterdam Principles
    • Kinsinger CR, Apffel J, Baker M et al. Recommendations for mass spectrometry data quality metrics for open access data (corollary to the Amsterdam Principles). J. Proteome Res. 11(2), 1412-1419 (2011
    • (2011) J. Proteome Res , vol.11 , Issue.2 , pp. 1412-1419
    • Kinsinger, C.R.1    Apffel, J.2    Baker, M.3
  • 59
    • 67650564834 scopus 로고    scopus 로고
    • Multi-site assessment of the precision and reproducibility of multiple reaction monitoring-based measurements of proteins in plasma
    • Addona TA, Abbatiello SE, Schilling B et al. Multi-site assessment of the precision and reproducibility of multiple reaction monitoring-based measurements of proteins in plasma. Nat. Biotechnol. 27(7), 633-641 (2009
    • (2009) Nat. Biotechnol , vol.27 , Issue.7 , pp. 633-641
    • Addona, T.A.1    Abbatiello, S.E.2    Schilling, B.3
  • 60
    • 77957344363 scopus 로고    scopus 로고
    • A quantitative study of the effects of chaotropic agents, surfactants, and solvents on the digestion efficiency of human plasma proteins by trypsin
    • Proc JL, Kuzyk MA, Hardie DB et al. A quantitative study of the effects of chaotropic agents, surfactants, and solvents on the digestion efficiency of human plasma proteins by trypsin. J. Proteome Res. 9(10), 5422-5437 (2010
    • (2010) J. Proteome Res , vol.9 , Issue.10 , pp. 5422-5437
    • Proc, J.L.1    Kuzyk, M.A.2    Hardie, D.B.3
  • 61
    • 0036188342 scopus 로고    scopus 로고
    • Serum interleukin 6, plasma VEGF, serum VEGF, and VEGF platelet load in breast cancer patients
    • Benoy I, Salgado R, Colpaert C, Weytjens R, Vermeulen PB, Dirix LY. Serum interleukin 6, plasma VEGF, serum VEGF, and VEGF platelet load in breast cancer patients. Clin. Breast Cancer 2(4), 311-315 (2002 (Pubitemid 34196274)
    • (2002) Clinical Breast Cancer , vol.2 , Issue.4 , pp. 311-315
    • Benoy, I.1    Salgado, R.2    Colpaert, C.3    Weytjens, R.4    Vermeulen, P.B.5    Dirix, L.Y.6
  • 62
    • 0019176687 scopus 로고
    • Clinical chemical values for some common laboratory animals
    • Caisey JD, King DJ. Clinical chemical values for some common laboratory animals. Clin. Chem. 26(13), 1877-1879 (1980 (Pubitemid 11205484)
    • (1980) Clinical Chemistry , vol.26 , Issue.13 , pp. 1877-1879
    • Caisey, J.D.1    King, D.J.2
  • 64
    • 38349133054 scopus 로고    scopus 로고
    • The HUPO human plasma proteome project
    • Omenn GS. The HUPO human plasma proteome project. Proteomics Clin. Appl. 1(8), 769-779 (2007
    • (2007) Proteomics Clin. Appl , vol.1 , Issue.8 , pp. 769-779
    • Omenn, G.S.1
  • 65
    • 1642579024 scopus 로고    scopus 로고
    • The Human Proteome Organization Plasma Proteome Project pilot phase: Reference specimens, technology platform comparisons, and standardized data submissions and analyses
    • DOI 10.1002/pmic.200300686
    • Omenn GS. The Human Proteome Organization Plasma Proteome Project pilot phase: Reference specimens, technology platform comparisons, and standardized data submissions and analyses. Proteomics 4, 1235-1240 (2004 (Pubitemid 38648012)
    • (2004) Proteomics , vol.4 , Issue.5 , pp. 1235-1240
    • Omenn, G.S.1
  • 66
    • 84859324942 scopus 로고    scopus 로고
    • Standard operating procedures and protocols for the preparation and analysis of plasma samples using the itraq methodology
    • Ivanov A, Lazarev A (Eds). Springer NY USA
    • Ohlund LB, Hardie DB, Elliott MHet al. Standard operating procedures and protocols for the preparation and analysis of plasma samples using the iTRAQ methodology. In: Sample Preparation in Biological Mass Spectrometry. Ivanov A, Lazarev A (Eds). Springer, NY, USA, 575-624 (2011
    • (2011) Sample Preparation in Biological Mass Spectrometry , pp. 575-624
    • Ohlund, L.B.1    Hardie, D.B.2    Elliott, M.H.3
  • 67
    • 67650624097 scopus 로고    scopus 로고
    • Thrombin induces broad spectrum proteolysis in human serum samples
    • O'Mullan P, Craft D, Yi J, Gelfand CA. Thrombin induces broad spectrum proteolysis in human serum samples. Clin. Chem. Lab. Med. 47(6), 685-693 (2009
    • (2009) Clin. Chem. Lab. Med , vol.47 , Issue.6 , pp. 685-693
    • O'Mullan, P.1    Craft, D.2    Yi, J.3    Gelfand, C.A.4
  • 69
    • 4344576101 scopus 로고    scopus 로고
    • An investigation of plasma collection, stabilization, and storage procedures for proteomic analysis of clinical samples
    • Hulmes JD, Bethea D, Ho K et al. An investigation of plasma collection, stabilization, and storage procedures for proteomic analysis of clinical samples. Clin. Proteomics 1(1), 17-31 (2004 (Pubitemid 41271307)
    • (2004) Clinical Proteomics , vol.1 , Issue.1 , pp. 17-31
    • Hulmes, J.D.1    Bethea, D.2    Ho, K.3    Huang, S.-P.4    Ricci, D.L.5    Opiteck, G.J.6    Hefta, S.A.7
  • 70
    • 34249315396 scopus 로고    scopus 로고
    • Inhibition of intrinsic proteolytic activities moderates preanalytical variability and instability of human plasma
    • DOI 10.1021/pr060550h
    • Yi J, Kim C, Gelfand CA. Inhibition of intrinsic proteolytic activities moderates pre-Analytical variability and instability of human plasma. J. Proteome Res. 6(5), 1768-1781 (2007 (Pubitemid 46814501)
    • (2007) Journal of Proteome Research , vol.6 , Issue.5 , pp. 1768-1781
    • Yi, J.1    Kim, C.2    Gelfand, C.A.3
  • 71
    • 84862012968 scopus 로고    scopus 로고
    • Comparison of blood collection tubes and processing protocols for plasma proteomics studies
    • Aguilar-Mahecha A, Kuzyk MA, Domanski D, Borchers CH, Basik M. Comparison of blood collection tubes and processing protocols for plasma proteomics studies. PLoS ONE 7(6), e38290 (2012
    • (2012) PLoS ONE , vol.7 , Issue.6
    • Aguilar-Mahecha, A.1    Kuzyk, M.A.2    Domanski, D.3    Borchers, C.H.4    Basik, M.5
  • 73
    • 84871411392 scopus 로고    scopus 로고
    • Remarkable temporal stability of high-Abundance human plasma proteins assessed by targeted mass spectrometry
    • Randall SA, McKay MJ, Pascovici D et al. Remarkable temporal stability of high-Abundance human plasma proteins assessed by targeted mass spectrometry. Proteomics Clin. Appl. 6(11-12), 626-634 (2012
    • (2012) Proteomics Clin. Appl , vol.6 , Issue.11-12 , pp. 626-634
    • Randall, S.A.1    McKay, M.J.2    Pascovici, D.3
  • 74
    • 72149134626 scopus 로고    scopus 로고
    • The stability of the circulating human proteome to variations in sample collection and handling procedures measured with an aptamer-based proteomics array
    • Ostroff R, Foreman T, Keeney TR, Stratford S, Walker JJ, Zichi D. The stability of the circulating human proteome to variations in sample collection and handling procedures measured with an aptamer-based proteomics array. J. Proteomics 73, 649-666 (2010
    • (2010) J. Proteomics , vol.73 , pp. 649-666
    • Ostroff, R.1    Foreman, T.2    Keeney, T.R.3    Stratford, S.4    Walker, J.J.5    Zichi, D.6
  • 77
    • 84880439493 scopus 로고    scopus 로고
    • Proteomic approaches in circadian biology
    • Robles MS, Mann M. Proteomic approaches in circadian biology. Handb. Exp. Pharmacol. 217, 389-407 (2013
    • (2013) Handb. Exp. Pharmacol , vol.217 , pp. 389-407
    • Robles, M.S.1    Mann, M.2
  • 79
    • 78650441382 scopus 로고    scopus 로고
    • Impact of the storage temperature on human plasma proteomic analysis: Implications for the use of human plasma collections in research
    • Insenser M, Martínez-García M, Nieto RM, San-Millán JL, Escobar-Morreale HF. Impact of the storage temperature on human plasma proteomic analysis: Implications for the use of human plasma collections in research. Proteomics Clin. Appl. 4(8-9), 739-744 (2010
    • (2010) Proteomics Clin. Appl , vol.4 , Issue.8-9 , pp. 739-744
    • Insenser, M.1    Martínez-García, M.2    Nieto, R.M.3    San-Millán, J.L.4    Escobar-Morreale, H.F.5
  • 82
    • 74349131234 scopus 로고    scopus 로고
    • Procédure pour tester l'impact des variables préanalytiques sur des analyses peptidiques et protéiques et proposition de codage des procédures préanalytiques
    • Betsou F, Beaudeux J-L, Berthelaix A et al. Procédure pour tester l'impact des variables préanalytiques sur des analyses peptidiques et protéiques et proposition de codage des procédures préanalytiques. Ann. Biol. Clin. (Paris) 67(6), 641-649 (2009
    • (2009) Ann. Biol. Clin. (Paris , vol.67 , Issue.6 , pp. 641-649
    • Betsou, F.1    Beaudeux, J.-L.2    Berthelaix, A.3
  • 83
    • 60849109966 scopus 로고    scopus 로고
    • Standard operating procedures for serum and plasma collection: Early detection research network consensus statement standard operating procedure integration working group
    • Tuck MK, Chan DW, Chia D et al. Standard operating procedures for serum and plasma collection: Early detection research network consensus statement standard operating procedure integration working group. J. Proteome Res. 8, 113-117 (2009
    • (2009) J. Proteome Res , vol.8 , pp. 113-117
    • Tuck, M.K.1    Chan, D.W.2    Chia, D.3
  • 84
    • 75749111638 scopus 로고    scopus 로고
    • High-Abundance protein depletion: Comparison of methods for human plasma biomarker discovery
    • Polaskova V, Kapur A, Khan A, Molloy MP, Baker MS. High-Abundance protein depletion: Comparison of methods for human plasma biomarker discovery. Electrophoresis 31(3), 471-482 (2010
    • (2010) Electrophoresis , vol.31 , Issue.3 , pp. 471-482
    • Polaskova, V.1    Kapur, A.2    Khan, A.3    Molloy, M.P.4    Baker, M.S.5
  • 85
    • 8844233567 scopus 로고    scopus 로고
    • Mass Spectrometric Quantitation of Peptides and Proteins Using Stable Isotope Standards and Capture by Anti-Peptide Antibodies (SISCAPA)
    • DOI 10.1021/pr034086h
    • Anderson NL, Anderson NG, Haines LR, Hardie DB, Olafson RW, Pearson TW. Mass spectrometric quantitation of peptides and proteins using stable isotope standards and capture by anti-peptide antibodies (SISCAPA). J. Proteome Res. 3(2), 235-244 (2004 (Pubitemid 38500990)
    • (2004) Journal of Proteome Research , vol.3 , Issue.2 , pp. 235-244
    • Anderson, N.L.1    Anderson, N.G.2    Haines, L.R.3    Hardie, D.B.4    Olafson, R.W.5    Pearson, T.W.6
  • 87
    • 79953305842 scopus 로고    scopus 로고
    • Evaluation of large scale quantitative proteomic assay development using peptide affinity-based mass spectrometry
    • Whiteaker JR, Zhao L, Abbatiello SE et al. Evaluation of large scale quantitative proteomic assay development using peptide affinity-based mass spectrometry. Mol. Cell. Proteomics 10(4), M110.005645 (2011
    • (2011) Mol. Cell. Proteomics , vol.10 , Issue.4
    • Whiteaker, J.R.1    Zhao, L.2    Abbatiello, S.E.3
  • 88
    • 77649273179 scopus 로고    scopus 로고
    • Automated screening of monoclonal antibodies for SISCAPA assays using a magnetic bead processor and liquid chromatography-selected reaction monitoring-mass spectrometry
    • Schoenherr RM, Zhao L, Whiteaker JR et al. Automated screening of monoclonal antibodies for SISCAPA assays using a magnetic bead processor and liquid chromatography-selected reaction monitoring-mass spectrometry. J Immunol. Methods 353(1-2), 49-61 (2010
    • (2010) J Immunol. Methods , vol.353 , Issue.1-2 , pp. 49-61
    • Schoenherr, R.M.1    Zhao, L.2    Whiteaker, J.R.3
  • 89
    • 36049046122 scopus 로고    scopus 로고
    • An immunoaffinity tandem mass spectrometry (iMALDI) assay for detection of Francisella tularensis
    • DOI 10.1016/j.aca.2007.10.025, PII S0003267007017527
    • Jiang J, Parker CE, Fuller JR, Kawula TH, Borchers CH. An immunoaffinity tandem mass spectrometry (iMALDI) assay for detection of Francisella tularensis. Anal. Chim. Acta 605, 70-79. (2007 (Pubitemid 350088652)
    • (2007) Analytica Chimica Acta , vol.605 , Issue.1 , pp. 70-79
    • Jiang, J.1    Parker, C.E.2    Fuller, J.R.3    Kawula, T.H.4    Borchers, C.H.5
  • 91
    • 77956878144 scopus 로고    scopus 로고
    • Towards the development of an immuno MALDI (iMALDI) mass spectrometry assay for the diagnosis of hypertension
    • Reid JD, Holmes DT, Mason DR, Shah B, Borchers CH. Towards the development of an immuno MALDI (iMALDI) mass spectrometry assay for the diagnosis of hypertension. J. Am. Soc. Mass Spectrom. 21(10), 1680-1686 (2010
    • (2010) J. Am. Soc. Mass Spectrom , vol.21 , Issue.10 , pp. 1680-1686
    • Reid, J.D.1    Holmes, D.T.2    Mason, D.R.3    Shah, B.4    Borchers, C.H.5
  • 92
    • 84858438931 scopus 로고    scopus 로고
    • Duplexed iMALDI for the detection of angiotensin I and angiotensin II
    • Mason DR, Reid JD, Camenzind AG, Holmes DT, Borchers CH Duplexed iMALDI for the detection of angiotensin I and angiotensin II. Methods 56(2), 213-222 (2012
    • (2012) Methods , vol.56 , Issue.2 , pp. 213-222
    • Mason, D.R.1    Reid, J.D.2    Camenzind, A.G.3    Holmes, D.T.4    Borchers, C.H.5
  • 93
    • 75749111638 scopus 로고    scopus 로고
    • High-Abundance protein depletion: Comparison of methods for human plasma biomarker discovery
    • Polaskova V, Kapur A, Khan A, Molloy MP, Baker MS. High-Abundance protein depletion: Comparison of methods for human plasma biomarker discovery. Electrophoresis 31(3), 471-482 (2010
    • (2010) Electrophoresis , vol.31 , Issue.3 , pp. 471-482
    • Polaskova, V.1    Kapur, A.2    Khan, A.3    Molloy, M.P.4    Baker, M.S.5
  • 94
    • 78649519193 scopus 로고    scopus 로고
    • Online monitoring of immunoaffinity-based depletion of high-Abundance blood proteins by UV spectrophotometry using enhanced green fluorescence protein and FITC-labeled human serum albumin
    • Kim K, Yu J, Min H et al. Online monitoring of immunoaffinity-based depletion of high-Abundance blood proteins by UV spectrophotometry using enhanced green fluorescence protein and FITC-labeled human serum albumin. Proteome Sci. 8, 62 (2010
    • (2010) Proteome Sci , vol.8 , pp. 62
    • Kim, K.1    Yu, J.2    Min, H.3
  • 95
    • 3042815334 scopus 로고    scopus 로고
    • Trypsin cleaves exclusively C-terminal to arginine and lysine residues
    • DOI 10.1074/mcp.T400003-MCP200
    • Olsen JV, Ong SE, Mann M. Trypsin cleaves exclusively C-Terminal to arginine and lysine residues. Mol. Cell. Proteomics 3(6), 608-614 (2004 (Pubitemid 38878520)
    • (2004) Molecular and Cellular Proteomics , vol.3 , Issue.6 , pp. 608-614
    • Olsen, J.V.1    Ong, S.-E.2    Mann, M.3
  • 96
    • 34848903890 scopus 로고    scopus 로고
    • The implications of proteolytic background for shotgun proteomics
    • DOI 10.1074/mcp.M700029-MCP200
    • Picotti P, Aebersold R, Domon B. The implications of proteolytic background for shotgun proteomics. Mol. Cell. Proteomics 6(9), 1589-1598 (2007 (Pubitemid 47506169)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.9 , pp. 1589-1598
    • Picott, P.1    Aebersold, R.2    Domont, B.3
  • 97
    • 43949131094 scopus 로고    scopus 로고
    • Fast and efficient proteolysis by microwave-assisted protein digestion using trypsin-immobilized magnetic silica microspheres
    • DOI 10.1021/ac800023r
    • Lin S, Yao G, Qi D et al. Fast and efficient proteolysis by microwave-Assisted protein digestion using trypsin-immobilized magnetic silica microspheres. Anal. Chem. 80(10), 3655-3665 (2008 (Pubitemid 351705865)
    • (2008) Analytical Chemistry , vol.80 , Issue.10 , pp. 3655-3665
    • Lin, S.1    Yao, G.2    Qi, D.3    Li, Y.4    Deng, C.5    Yang, P.6    Zhang, X.7
  • 98
    • 77955922158 scopus 로고    scopus 로고
    • Reproducible microwave-Assisted acid hydrolysis of proteins using a household microwave oven and its combination with LC-ESI-MS/MS for mapping protein sequences and modifications
    • Wang N, Li L. Reproducible microwave-Assisted acid hydrolysis of proteins using a household microwave oven and its combination with LC-ESI-MS/MS for mapping protein sequences and modifications. J. Am. Soc. Mass Spectrom. 21(9), 1573-1587 (2010
    • (2010) J. Am. Soc. Mass Spectrom , vol.21 , Issue.9 , pp. 1573-1587
    • Wang, N.1    Li, L.2
  • 99
    • 84863916307 scopus 로고    scopus 로고
    • Microwave-Assisted protein solubilization for mass spectrometry-based shotgun proteome analysis
    • Ye X, Li L. Microwave-Assisted protein solubilization for mass spectrometry-based shotgun proteome analysis. Anal. Chem. 84(14), 6181-6191 (2012
    • (2012) Anal. Chem , vol.84 , Issue.14 , pp. 6181-6191
    • Ye, X.1    Li, L.2
  • 100
    • 26844475051 scopus 로고    scopus 로고
    • Ultra fast trypsin digestion of proteins by high intensity focused ultrasound
    • DOI 10.1021/pr050112v
    • López-Ferrer D, Capelo JL, Vázquez J. Ultra fast trypsin digestion of proteins by high intensity focused ultrasound. J. Proteome Res. 4, 1569-1574 (2005 (Pubitemid 41464782)
    • (2005) Journal of Proteome Research , vol.4 , Issue.5 , pp. 1569-1574
    • Lopez-Ferrer, D.1    Capelo, J.L.2    Vazquez, J.3
  • 101
    • 53049107743 scopus 로고    scopus 로고
    • Application of pressurized solvents for ultrafast trypsin hydrolysis in proteomics: Proteomics on the fly
    • López-Ferrer D, Petritis K, Hixson KK et al. Application of pressurized solvents for ultrafast trypsin hydrolysis in proteomics: Proteomics on the fly. J. Proteome Res. 7(8), 3276-3281 (2008
    • (2008) J. Proteome Res , vol.7 , Issue.8 , pp. 3276-3281
    • López-Ferrer, D.1    Petritis, K.2    Hixson, K.K.3
  • 102
    • 57649093650 scopus 로고    scopus 로고
    • On-line digestion system for protein characterization and proteome analysis
    • López-Ferrer D, Petritis K, Lourette NM et al. On-line digestion system for protein characterization and proteome analysis. Anal. Chem. 23, 8930-8936 (2008
    • (2008) Anal. Chem , vol.23 , pp. 8930-8936
    • López-Ferrer, D.1    Petritis, K.2    Lourette, N.M.3
  • 103
    • 84868327851 scopus 로고    scopus 로고
    • Large-scale quantitative assessment of different in-solution protein digestion protocols reveals superior cleavage efficiency of tandem LysC/trypsin proteolysis over trypsin digestion
    • Glatter T, Ludwig C, Ahrné E, Aebersold R, Heck AJ, Schmidt A. Large-scale quantitative assessment of different in-solution protein digestion protocols reveals superior cleavage efficiency of tandem LysC/trypsin proteolysis over trypsin digestion. J. Proteome Res. 11(11), 5145-5156 (2012
    • (2012) J. Proteome Res , vol.11 , Issue.11 , pp. 5145-5156
    • Glatter, T.1    Ludwig, C.2    Ahrné, E.3    Aebersold, R.4    Heck, A.J.5    Schmidt, A.6
  • 104
    • 34248598796 scopus 로고    scopus 로고
    • Trends in sample preparation for classical and second generation proteomics
    • DOI 10.1016/j.chroma.2007.01.045, PII S002196730700091X, Advances in Sample Preparation Part II
    • Canas B, Pineiro C, Calvo E, Lopez-Ferrer D, Gallardo JM. Trends in sample preparation for classical and second generation proteomics. J. Chromatog. A 1153, 235-258 (2007 (Pubitemid 46755189)
    • (2007) Journal of Chromatography A , vol.1153 , Issue.1-2 , pp. 235-258
    • Canas, B.1    Pineiro, C.2    Calvo, E.3    Lopez-Ferrer, D.4    Gallardo, J.M.5
  • 105
    • 33750143252 scopus 로고    scopus 로고
    • Evaluation of the application of sodium deoxycholate to proteomic analysis of rat hippocampal plasma membrane
    • DOI 10.1021/pr060112a
    • Zhou J, Zhou TY, Cao R et al. Evaluation of the application of sodium deoxycholate to proteomic analysis of rat hippocampal plasma membrane.rat hippocampal plasma membrane. J. Proteome Res. 5, 2547-2553 (2006 (Pubitemid 44595157)
    • (2006) Journal of Proteome Research , vol.5 , Issue.10 , pp. 2547-2553
    • Zhou, J.1    Zhou, T.2    Cao, R.3    Liu, Z.4    Shen, J.5    Chen, P.6    Wang, X.7    Liang, S.8
  • 106
    • 43049130709 scopus 로고    scopus 로고
    • Sodium-deoxycholate-Assisted tryptic digestion and identification of proteolytically resistant proteins
    • Lin Y, Zhou J, Bi D, Chen P, Wang X, Liang S. Sodium-deoxycholate- Assisted tryptic digestion and identification of proteolytically resistant proteins. Anal. Biochem. 377(2), 259-266 (2008
    • (2008) Anal. Biochem , vol.377 , Issue.2 , pp. 259-266
    • Lin, Y.1    Zhou, J.2    Bi, D.3    Chen, P.4    Wang, X.5    Liang, S.6
  • 107
    • 84855877960 scopus 로고    scopus 로고
    • Systematic and quantitative comparison of digest efficiency and specificity reveals the impact of trypsin quality on MS-based proteomics
    • Burkhart JM, Schumbrutzki C, Wortelkamp S, Sickmann A, Zahedi RP. Systematic and quantitative comparison of digest efficiency and specificity reveals the impact of trypsin quality on MS-based proteomics. J. Proteomics 75(4), 1454-1462 (2012
    • (2012) J. Proteomics , vol.75 , Issue.4 , pp. 1454-1462
    • Burkhart, J.M.1    Schumbrutzki, C.2    Wortelkamp, S.3    Sickmann, A.4    Zahedi, R.P.5
  • 110
    • 84862177872 scopus 로고    scopus 로고
    • The use of multiplexed MRM for the discovery of biomarkers to differentiate iron-deficiency anemia from anemia of inflammation
    • Domanski D, Cohen Freue G, Sojo L et al. The use of multiplexed MRM for the discovery of biomarkers to differentiate iron-deficiency anemia from anemia of inflammation. J. Proteomics 75(12), 3514-3528 (2012
    • (2012) J. Proteomics , vol.75 , Issue.12 , pp. 3514-3528
    • Domanski, D.1    Cohen Freue, G.2    Sojo, L.3
  • 111
    • 80052521703 scopus 로고    scopus 로고
    • High-flow multiplexed MRM-based analysis of proteins in human plasma without depletion or enrichment
    • Domanski D, Smith DS, Miller CA et al. High-flow multiplexed MRM-based analysis of proteins in human plasma without depletion or enrichment. Clin. Lab. Med. 31(3), 371-384 (2011
    • (2011) Clin. Lab. Med , vol.31 , Issue.3 , pp. 371-384
    • Domanski, D.1    Smith, D.S.2    Miller, C.A.3
  • 112
    • 84871983086 scopus 로고    scopus 로고
    • Quantitative analysis of peptides and proteins in biomedicine by targeted mass spectrometry
    • Gillette MA, Carr SA. Quantitative analysis of peptides and proteins in biomedicine by targeted mass spectrometry. Nat. Methods 10, 28-34 (2013
    • (2013) Nat. Methods , vol.10 , pp. 28-34
    • Gillette, M.A.1    Carr, S.A.2
  • 113
    • 84860880032 scopus 로고    scopus 로고
    • Interlaboratory evaluation of automated, multiplexed peptide immunoaffinity enrichment coupled to multiple reaction monitoring mass spectrometry for quantifying proteins in plasma
    • Kuhn E, Whiteaker JR, Mani DR et al. Interlaboratory evaluation of automated, multiplexed peptide immunoaffinity enrichment coupled to multiple reaction monitoring mass spectrometry for quantifying proteins in plasma. Mol. Cell. Proteomics 11(6), M111.013854 (2012
    • (2012) Mol. Cell. Proteomics , vol.11 , Issue.6
    • Kuhn, E.1    Whiteaker, J.R.2    Mani, D.R.3
  • 114
    • 55849104840 scopus 로고    scopus 로고
    • Protein standard absolute quantification (PSAQ) for improved investigation of staphylococcal food poisoning outbreaks
    • Dupuis A, Hennekinne JA, Garin J, Brun V. Protein standard absolute quantification (PSAQ) for improved investigation of staphylococcal food poisoning outbreaks. Proteomics 8(22), 4633-4636 (2008
    • (2008) Proteomics , vol.8 , Issue.22 , pp. 4633-4636
    • Dupuis, A.1    Hennekinne, J.A.2    Garin, J.3    Brun, V.4
  • 115
    • 84860868949 scopus 로고    scopus 로고
    • Mass Spectrometry-based Absolute Protein Quantification: PSAQ™ Strategy Makes Use Of "noncanonical" proteotypic peptides
    • Jaquinod M, Trauchessec M, Huillet C et al. Mass spectrometry-based absolute protein quantification: PSAQ™ strategy makes use of "noncanonical" proteotypic peptides. Proteomics 12(8), 1217-1221 (2012
    • (2012) Proteomics , vol.12 , Issue.8 , pp. 1217-1221
    • Jaquinod, M.1    Trauchessec, M.2    Huillet, C.3
  • 116
    • 84856707623 scopus 로고    scopus 로고
    • Accurate quantification of cardiovascular biomarkers in serum using Protein Standard Absolute Quantification (PSAQ™) and selected reaction monitoring
    • Huillet C, Adrait A, Lebert D et al. Accurate quantification of cardiovascular biomarkers in serum using Protein Standard Absolute Quantification (PSAQ™) and selected reaction monitoring. Mol. Cell. Proteomics 11(2), M111.008235 (2012
    • (2012) Mol. Cell. Proteomics , vol.11 , Issue.2
    • Huillet, C.1    Adrait, A.2    Lebert, D.3
  • 117
    • 78649834299 scopus 로고    scopus 로고
    • Simultaneous quantification of apolipoprotein a-I and apolipoprotein B by liquid chromatography-multiple reaction monitoring-mass spectrometry
    • Agger SA, Marney LC, Hoofnagle AN. Simultaneous quantification of apolipoprotein a-I and apolipoprotein B by liquid chromatography-multiple reaction monitoring-mass spectrometry. Clin. Chem. 56(12), 1804-1813 (2010
    • (2010) Clin. Chem , vol.56 , Issue.12 , pp. 1804-1813
    • Agger, S.A.1    Marney, L.C.2    Hoofnagle, A.N.3
  • 118
    • 67650432879 scopus 로고    scopus 로고
    • The fundamental flaws of immunoassays and potential solutions using tandem mass spectrometry
    • Hoofnagle AN, Wener MH. The fundamental flaws of immunoassays and potential solutions using tandem mass spectrometry. J. Immunol. Methods 347(1-2), 3-11 (2009
    • (2009) J. Immunol. Methods , vol.347 , Issue.1-2 , pp. 3-11
    • Hoofnagle, A.N.1    Wener, M.H.2
  • 119
    • 0022640659 scopus 로고
    • Stable isotopes in pharmacology studies: Present and future
    • Browne TR. Stable isotopes in pharmacology studies: Present and future. J. Clin. Pharmacol. 26(6), 485-489 (1986 (Pubitemid 16095938)
    • (1986) Journal of Clinical Pharmacology , vol.26 , Issue.6 , pp. 485-489
    • Browne, T.R.1
  • 120
    • 0025346679 scopus 로고
    • Stable isotopes in the management and diagnosis of inborn errors of metabolism
    • Parsons HG. Stable isotopes in the management and diagnosis of inborn errors of metabolism. Can. J. Physiol. Pharmacol. 68(7), 950-954 (1990 (Pubitemid 20242620)
    • (1990) Canadian Journal of Physiology and Pharmacology , vol.68 , Issue.7 , pp. 950-954
    • Parsons, H.G.1
  • 121
    • 84867026555 scopus 로고    scopus 로고
    • PSAQ™ standards for accurate MS-based quantification of proteins: From the concept to biomedical applications
    • Picard G, Lebert D, Louwagie M et al. PSAQ™ standards for accurate MS-based quantification of proteins: From the concept to biomedical applications. J. Mass Spectrom. 47(10), 1353-1363 (2012
    • (2012) J. Mass Spectrom , vol.47 , Issue.10 , pp. 1353-1363
    • Picard, G.1    Lebert, D.2    Louwagie, M.3
  • 122
    • 68749094119 scopus 로고    scopus 로고
    • Full dynamic range proteome analysis of S. Cerevisiae by targeted proteomics
    • Picotti P, Bodenmiller B, Mueller LN, Domon B, Aebersold R. Full dynamic range proteome analysis of S. cerevisiae by targeted proteomics. Cell 138(4), 795-806 (2009
    • (2009) Cell , vol.138 , Issue.4 , pp. 795-806
    • Picotti, P.1    Bodenmiller, B.2    Mueller, L.N.3    Domon, B.4    Aebersold, R.5
  • 123
    • 70649087115 scopus 로고    scopus 로고
    • Multiple reaction monitoring cubed for protein quantification at the low nanogram/milliliter level in nondepleted human serum
    • Fortin T, Salvador A, Charrier JP et al. Multiple reaction monitoring cubed for protein quantification at the low nanogram/milliliter level in nondepleted human serum. Anal. Chem. 81(22), 9343-9352 (2009
    • (2009) Anal. Chem , vol.81 , Issue.22 , pp. 9343-9352
    • Fortin, T.1    Salvador, A.2    Charrier, J.P.3
  • 124
    • 84860850312 scopus 로고    scopus 로고
    • MRM3 quantitation for highest selectivity of proteins in complex matrices
    • Suppl
    • Hunter C. MRM3 quantitation for highest selectivity of proteins in complex matrices. J. Biomol. Tech. 21(3 Suppl.), S34-S35 (2010
    • (2010) J. Biomol. Tech , vol.21 , Issue.3
    • Hunter, C.1
  • 125
    • 84860854049 scopus 로고    scopus 로고
    • Advancing the sensitivity of selected reaction monitoring-based targeted quantitative proteomics
    • Shi T, Su D, Liu T et al. Advancing the sensitivity of selected reaction monitoring-based targeted quantitative proteomics. Proteomics 12(8), 1074-1092 (2012
    • (2012) Proteomics , vol.12 , Issue.8 , pp. 1074-1092
    • Shi, T.1    Su, D.2    Liu, T.3
  • 126
    • 84887924792 scopus 로고    scopus 로고
    • Absolute quantitation of proteins in human blood by multiplexed multiple reaction monitoring mass spectrometry
    • Percy AJ, Chambers AG, Parker CE, Borchers CH. Absolute quantitation of proteins in human blood by multiplexed multiple reaction monitoring mass spectrometry. Methods Mol. Biol. 1000, 167-189 (2013
    • (2013) Methods Mol. Biol , vol.1000 , pp. 167-189
    • Percy, A.J.1    Chambers, A.G.2    Parker, C.E.3    Borchers, C.H.4
  • 127
    • 75749126208 scopus 로고    scopus 로고
    • Automated detection of inaccurate and imprecise transitions in peptide quantification by multiple reaction monitoring mass spectrometry
    • Abbatiello SE, Mani DR, Keshishian H, Carr SA. Automated detection of inaccurate and imprecise transitions in peptide quantification by multiple reaction monitoring mass spectrometry. Clin. Chem. 56(2), 291-305 (2010
    • (2010) Clin. Chem , vol.56 , Issue.2 , pp. 291-305
    • Abbatiello, S.E.1    Mani, D.R.2    Keshishian, H.3    Carr, S.A.4
  • 128
    • 79953227740 scopus 로고    scopus 로고
    • Increased selectivity, analytical precision, and throughput in targeted proteomics
    • Kiyonami R, Schoen A, Prakash A et al. Increased selectivity, analytical precision, and throughput in targeted proteomics. Mol. Cell. Proteomics 10(2), M110.002931 (2011
    • (2011) Mol. Cell. Proteomics , vol.10 , Issue.2
    • Kiyonami, R.1    Schoen, A.2    Prakash, A.3
  • 129
    • 84863900597 scopus 로고    scopus 로고
    • A computational tool to detect and avoid redundancy in selected reaction monitoring
    • Röst H, Malmström L, Aebersold R. A computational tool to detect and avoid redundancy in selected reaction monitoring. Mol. Cell. Proteomics 11(8), 540-549 (2012
    • (2012) Mol. Cell. Proteomics , vol.11 , Issue.8 , pp. 540-549
    • Röst, H.1    Malmström, L.2    Aebersold, R.3
  • 130
    • 84861860481 scopus 로고    scopus 로고
    • Targeted data extraction of the MS/MS spectra generated by data-independent acquisition: A new concept for consistent and accurate proteome analysis
    • Gillet LC, Navarro P, Tate S et al. Targeted data extraction of the MS/MS spectra generated by data-independent acquisition: A new concept for consistent and accurate proteome analysis. Mol. Cell. Proteomics 11(6), O111.016717 (2012
    • (2012) Mol. Cell. Proteomics , vol.11 , Issue.6
    • Gillet, L.C.1    Navarro, P.2    Tate, S.3
  • 131
    • 75749100667 scopus 로고    scopus 로고
    • Quantitative clinical proteomics by liquid chromatography-Tandem mass spectrometry: Assessing the platform
    • Hoofnagle AN. Quantitative clinical proteomics by liquid chromatography-Tandem mass spectrometry: Assessing the platform. Clin. Chem. Lab. Med. 56(2), 161-164 (2010
    • (2010) Clin. Chem. Lab. Med , vol.56 , Issue.2 , pp. 161-164
    • Hoofnagle, A.N.1
  • 132
    • 84882236106 scopus 로고    scopus 로고
    • Quantitative clinical chemistry proteomics (qCCP) using mass spectrometry: General characteristics and application
    • Lehmann S, Hoofnagle A, Hochstrasser D et al. Quantitative clinical chemistry proteomics (qCCP) using mass spectrometry: General characteristics and application. Clin. Chem. Lab. Med. 51(5), 919-935 (2013
    • (2013) Clin. Chem. Lab. Med , vol.51 , Issue.5 , pp. 919-935
    • Lehmann, S.1    Hoofnagle, A.2    Hochstrasser, D.3
  • 133
    • 84877813399 scopus 로고    scopus 로고
    • Selectivity of LC-MS/MS analysis: Implication for proteomics experiments
    • Gallien S, Duriez E, Demeure K, Domon B. Selectivity of LC-MS/MS analysis: Implication for proteomics experiments. J. Proteomics 81, 148-158 (2013
    • (2013) J. Proteomics , vol.81 , pp. 148-158
    • Gallien, S.1    Duriez, E.2    Demeure, K.3    Domon, B.4
  • 134
    • 79956155894 scopus 로고    scopus 로고
    • The journey to regulation of protein-based multiplex quantitative assays
    • Boja ES, Jortani SA, Ritchie J et al. The journey to regulation of protein-based multiplex quantitative assays. Clin. Chem. 57(4), 560-567 (2011
    • (2011) Clin. Chem , vol.57 , Issue.4 , pp. 560-567
    • Boja, E.S.1    Jortani, S.A.2    Ritchie, J.3
  • 135
    • 67349196123 scopus 로고    scopus 로고
    • A HUPO test sample study reveals common problems in mass spectrometry-based proteomics
    • Bell AW, Deutsch EW, Au CE et al. A HUPO test sample study reveals common problems in mass spectrometry-based proteomics. Nat. Methods 6(6), 423-430 (2009
    • (2009) Nat. Methods , vol.6 , Issue.6 , pp. 423-430
    • Bell, A.W.1    Deutsch, E.W.2    Au, C.E.3
  • 136
    • 33750285086 scopus 로고    scopus 로고
    • The HUPO proteomics standards initiative - Overcoming the fragmentation of proteomics data
    • DOI 10.1002/pmic.200600537
    • Hermjakob H. The HUPO proteomics standards initiative-overcoming the fragmentation of proteomics data. Proteomics 6(Suppl. 2), 34-38 (2006 (Pubitemid 44625766)
    • (2006) Proteomics , vol.1 , Issue.1-2 SUPPL. , pp. 34-38
    • Hermjakob, H.1
  • 137
    • 79960179572 scopus 로고    scopus 로고
    • The human proteome project: Current state and future direction
    • Legrain P, Aebersold R, Archakov A et al. The human proteome project: Current state and future direction. Mol. Cell. Proteomics 10(7), M111.00993 (2011
    • (2011) Mol. Cell. Proteomics , vol.10 , Issue.7
    • Legrain, P.1    Aebersold, R.2    Archakov, A.3
  • 140
    • 1842559788 scopus 로고    scopus 로고
    • Reproducibility of SELDI-TOF protein patterns in serum: Comparing datasets from different experiments
    • DOI 10.1093/bioinformatics/btg484
    • Baggerly KA, Morris JS, Coombes KR. Reproducibility of SELDI-TOF protein patterns in serum: Comparing datasets from different experiments. Bioinformatics 20(5), 777-785 (2003 (Pubitemid 38443834)
    • (2004) Bioinformatics , vol.20 , Issue.5 , pp. 777-785
    • Baggerly, K.A.1    Morris, J.S.2    Coombes, K.R.3
  • 141
    • 78649885451 scopus 로고    scopus 로고
    • Platform for establishing interlaboratory reproducibility of selected reaction monitoring-based mass spectrometry peptide assays
    • Prakash A, Rezai T, Krastins B et al. Platform for establishing interlaboratory reproducibility of selected reaction monitoring-based mass spectrometry peptide assays. J. Proteome Res. 9(12), 6678-6688 (2010
    • (2010) J. Proteome Res , vol.9 , Issue.12 , pp. 6678-6688
    • Prakash, A.1    Rezai, T.2    Krastins, B.3
  • 142
    • 84874048939 scopus 로고    scopus 로고
    • Standardized protocols for quality control of MRM-based plasma proteomic workflow
    • Percy AJ, Chambers AG, Smith DS, Borchers CH. Standardized protocols for quality control of MRM-based plasma proteomic workflow. J. Proteome Res. 12(1), 222-233 (2013
    • (2013) J. Proteome Res , vol.121 , pp. 222-233
    • Percy, A.J.1    Chambers, A.G.2    Smith, D.S.3    Borchers, C.H.4


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