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Volumn 13, Issue 5, 2013, Pages 727-742

Combined use of irreversible binding and MRM technology for low- and ultralow copy-number protein detection and quantitation

Author keywords

Detection limit; Irreversible binding; LLOD; Low and ultralow copy number proteins; MRM; Technology

Indexed keywords

BIOMATERIAL; BOVINE SERUM ALBUMIN; CYANOGEN BROMIDE; CYTOCHROME P450; PROTEIN;

EID: 84874800273     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201100460     Document Type: Article
Times cited : (25)

References (60)
  • 1
    • 0023753018 scopus 로고
    • Diagnosis of sickle cell anemia and beta-thalassemia with enzymatically amplified DNA and nonradioactive allele-specific oligonucleotide probes
    • Saiki, R. K., Chang, C. A., Levenson, C. H., Warren, T. C. et al., Diagnosis of sickle cell anemia and beta-thalassemia with enzymatically amplified DNA and nonradioactive allele-specific oligonucleotide probes. N. Engl. J. Med. 1988, 319, 537-541.
    • (1988) N. Engl. J. Med. , vol.319 , pp. 537-541
    • Saiki, R.K.1    Chang, C.A.2    Levenson, C.H.3    Warren, T.C.4
  • 2
    • 33846622299 scopus 로고    scopus 로고
    • AFM fishing nanotechnology is the way to reverse the Avogadro number in proteomics
    • Archakov, A. I., Ivanov, Y. D., Lisitsa, A. V., Zgoda, V. G., AFM fishing nanotechnology is the way to reverse the Avogadro number in proteomics. Proteomics 2007, 7, 4-9.
    • (2007) Proteomics , vol.7 , pp. 4-9
    • Archakov, A.I.1    Ivanov, Y.D.2    Lisitsa, A.V.3    Zgoda, V.G.4
  • 3
    • 19944408971 scopus 로고    scopus 로고
    • Limitations of current proteomics technologies
    • Garbis, S., Lubec, G., Fountoulakis, M., Limitations of current proteomics technologies. J. Chromatogr. A 2005, 1077, 1-18.
    • (2005) J. Chromatogr. A , vol.1077 , pp. 1-18
    • Garbis, S.1    Lubec, G.2    Fountoulakis, M.3
  • 4
    • 43549094212 scopus 로고    scopus 로고
    • Déjà vu in proteomics. A hit parade of repeatedly identified differentially expressed proteins
    • Petrak, J., Ivanek, R., Toman, O., Cmejla, R. et al., Déjà vu in proteomics. A hit parade of repeatedly identified differentially expressed proteins. Proteomics 2008, 8, 1744-1749.
    • (2008) Proteomics , vol.8 , pp. 1744-1749
    • Petrak, J.1    Ivanek, R.2    Toman, O.3    Cmejla, R.4
  • 5
    • 77955102352 scopus 로고    scopus 로고
    • Quantifying E. coli proteome and transcriptome with single-molecule sensitivity in single cells
    • Taniguchi, Y., Choi, P. J., Li, G. W., Chen, H. et al., Quantifying E. coli proteome and transcriptome with single-molecule sensitivity in single cells. Science 2010, 329, 533-538.
    • (2010) Science , vol.329 , pp. 533-538
    • Taniguchi, Y.1    Choi, P.J.2    Li, G.W.3    Chen, H.4
  • 6
    • 1842528125 scopus 로고    scopus 로고
    • Quantification of C-reactive protein in the serum of patients with rheumatoid arthritis using multiple reaction monitoring mass spectrometry and 13C-labeled peptide standards
    • Kuhn, E., Wu, J., Karl, J., Liao, H. et al., Quantification of C-reactive protein in the serum of patients with rheumatoid arthritis using multiple reaction monitoring mass spectrometry and 13C-labeled peptide standards. Proteomics 2004, 4, 1175-1186.
    • (2004) Proteomics , vol.4 , pp. 1175-1186
    • Kuhn, E.1    Wu, J.2    Karl, J.3    Liao, H.4
  • 7
    • 33645721632 scopus 로고    scopus 로고
    • Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins
    • Anderson, L., Hunter, C. L., Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins. Mol. Cell. Proteomics 2006, 5, 573-588.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 573-588
    • Anderson, L.1    Hunter, C.L.2
  • 8
    • 33846133955 scopus 로고    scopus 로고
    • Computational prediction of proteotypic peptides for quantitative proteomics
    • Mallick, P., Schirle, M., Chen, S. S., Flory, M. R. et al., Computational prediction of proteotypic peptides for quantitative proteomics. Nat. Biotechnol. 2007, 25, 125-131.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 125-131
    • Mallick, P.1    Schirle, M.2    Chen, S.S.3    Flory, M.R.4
  • 9
    • 68749094119 scopus 로고    scopus 로고
    • Full dynamic range proteome analysis of S. cerevisiae by targeted proteomics
    • Picotti, P., Bodenmiller, B., Mueller, L. N., Domon, B. et al., Full dynamic range proteome analysis of S. cerevisiae by targeted proteomics. Cell 2009, 138, 795-806.
    • (2009) Cell , vol.138 , pp. 795-806
    • Picotti, P.1    Bodenmiller, B.2    Mueller, L.N.3    Domon, B.4
  • 10
    • 79952276306 scopus 로고    scopus 로고
    • Generation of acetyllysine antibodies and affinity enrichment of acetylated peptides
    • Guan, K. L., Yu, W., Lin, Y., Xiong, Y. et al., Generation of acetyllysine antibodies and affinity enrichment of acetylated peptides. Nat. Protoc. 2010, 5, 1583-1595.
    • (2010) Nat. Protoc. , vol.5 , pp. 1583-1595
    • Guan, K.L.1    Yu, W.2    Lin, Y.3    Xiong, Y.4
  • 11
    • 0344494027 scopus 로고    scopus 로고
    • Applications of affinity chromatography in proteomics
    • Lee, W. C., Lee, K. H., Applications of affinity chromatography in proteomics. Anal. Biochem. 2004, 324, 1-10.
    • (2004) Anal. Biochem. , vol.324 , pp. 1-10
    • Lee, W.C.1    Lee, K.H.2
  • 12
    • 43249107694 scopus 로고    scopus 로고
    • Affinity as a tool in life science
    • Uhlen, M., Affinity as a tool in life science. Biotechniques 2008, 44, 649-654.
    • (2008) Biotechniques , vol.44 , pp. 649-654
    • Uhlen, M.1
  • 13
    • 50849141923 scopus 로고    scopus 로고
    • Nanomaterial based affinity matrix-assisted laser desorption/ionization mass spectrometry for biomolecule and pathogenic bacteria
    • Chiu, T. C., Huang, L. S., Lin, P. C., Chen, Y. C. et al., Nanomaterial based affinity matrix-assisted laser desorption/ionization mass spectrometry for biomolecule and pathogenic bacteria. Recent Pat. Nanotechnol. 2007, 1, 99-111.
    • (2007) Recent Pat. Nanotechnol. , vol.1 , pp. 99-111
    • Chiu, T.C.1    Huang, L.S.2    Lin, P.C.3    Chen, Y.C.4
  • 14
    • 58149125650 scopus 로고    scopus 로고
    • Comparison of ZnS semiconductor nanoparticles capped with various functional groups as the matrix and affinity probes for rapid analysis of cyclodextrins and proteins in surface-assisted laser desorption/ionization time of flight mass spectrometry
    • Kailasa, S. K., Kiran, K., Wu, H. F., Comparison of ZnS semiconductor nanoparticles capped with various functional groups as the matrix and affinity probes for rapid analysis of cyclodextrins and proteins in surface-assisted laser desorption/ionization time of flight mass spectrometry. Anal. Chem. 2008, 80, 9681-9688.
    • (2008) Anal. Chem. , vol.80 , pp. 9681-9688
    • Kailasa, S.K.1    Kiran, K.2    Wu, H.F.3
  • 15
    • 76749121378 scopus 로고    scopus 로고
    • Multifunctional ZrO(2) nanoparticles and ZrO(2)-SiO(2) nanorods for improved MALDI-MS analysis of cyclodextrins, peptides and phosphopeptides
    • Kailasa, S. K., Wu, H. F., Multifunctional ZrO(2) nanoparticles and ZrO(2)-SiO(2) nanorods for improved MALDI-MS analysis of cyclodextrins, peptides and phosphopeptides. Anal. Bioanal. Chem. 2010, 396, 1115-1125.
    • (2010) Anal. Bioanal. Chem. , vol.396 , pp. 1115-1125
    • Kailasa, S.K.1    Wu, H.F.2
  • 16
    • 38949205018 scopus 로고    scopus 로고
    • Bare silica nanoparticles as concentrating and affinity probes for rapid analysis of aminothiols, lyzozyme and peptide mixture using atmospheric-pressure matrix-assisted laser desorption/ionization ion trap and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Agrawal, K., Wu, H. F., Bare silica nanoparticles as concentrating and affinity probes for rapid analysis of aminothiols, lyzozyme and peptide mixture using atmospheric-pressure matrix-assisted laser desorption/ionization ion trap and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Rapid Commun. Mass Spectrom. 2008, 22, 283-290.
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 283-290
    • Agrawal, K.1    Wu, H.F.2
  • 17
    • 0034819837 scopus 로고    scopus 로고
    • Protein engineering of Bacillus megaterium CYP102. The oxidation of polycyclic aromatic hydrocarbons
    • Carmichael, A. B., Wong, L. L., Protein engineering of Bacillus megaterium CYP102. The oxidation of polycyclic aromatic hydrocarbons. Eur. J. Biochem. 2001, 268, 3117-3125.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3117-3125
    • Carmichael, A.B.1    Wong, L.L.2
  • 18
    • 80052552293 scopus 로고    scopus 로고
    • A systematic analysis of eluted fraction of plasma post immunoaffinity depletion: implications in biomarker discovery
    • Yadav, A. K., Bhardwaj, G., Basak, T., Kumar, D. et al., A systematic analysis of eluted fraction of plasma post immunoaffinity depletion: implications in biomarker discovery. PLoS One 2011, 6, e24442.
    • (2011) PLoS One , vol.6
    • Yadav, A.K.1    Bhardwaj, G.2    Basak, T.3    Kumar, D.4
  • 19
    • 75149116346 scopus 로고    scopus 로고
    • Rapid and precise determination of cellular amino acid flux rates using HPLC with automated derivatization with absorbance detection
    • Greene, J., Henderson, J. W., Jr., Wikswo, J. P., Rapid and precise determination of cellular amino acid flux rates using HPLC with automated derivatization with absorbance detection. Agilent Pub. 2009, 5990-3283EN.
    • (2009) Agilent Pub.
    • Greene, J.1    Henderson, J.W.2    Wikswo Jr., J.P.3
  • 20
    • 78449294619 scopus 로고    scopus 로고
    • A highly sensitive ultra performance liquid chromatography-tandem mass spectrometry (UPLC-MS/MS) technique for quantitation of protein free and bound efavirenz (EFV) in human seminal and blood plasma
    • Avery, L. B., Parsons, T. L., Meyers, D. J., Hubbard, W. C., A highly sensitive ultra performance liquid chromatography-tandem mass spectrometry (UPLC-MS/MS) technique for quantitation of protein free and bound efavirenz (EFV) in human seminal and blood plasma. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 2010, 878, 3217-3224.
    • (2010) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.878 , pp. 3217-3224
    • Avery, L.B.1    Parsons, T.L.2    Meyers, D.J.3    Hubbard, W.C.4
  • 21
    • 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., Burgess, M. et al., Developing multiplexed assays for Troponin I and Interleukin-33 in plasma by peptide immunoaffinity enrichment and targeted mass spectrometry. Clin. Chem. 2009, 55, 1108-1117.
    • (2009) Clin. Chem. , vol.55 , pp. 1108-1117
    • Kuhn, E.1    Addona, T.2    Keshishian, H.3    Burgess, M.4
  • 22
    • 35348863892 scopus 로고    scopus 로고
    • High sensitive detection of plasma proteins by multiple reaction monitoring of N-glycosites
    • Stahl-Zeng, J., Lange, V., Ossola, R., Eckhardt, K. et al., High sensitive detection of plasma proteins by multiple reaction monitoring of N-glycosites. Mol. Cell. Proteomics 2007, 6, 1809-1817.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1809-1817
    • Stahl-Zeng, J.1    Lange, V.2    Ossola, R.3    Eckhardt, K.4
  • 23
    • 34848903890 scopus 로고    scopus 로고
    • The implications of proteolytic background for shotgun proteomics
    • Picotti, P., Aebersold, R., Domon, B., The implications of proteolytic background for shotgun proteomics. Mol. Cell. Proteomics 2007, 6, 1589-1598.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1589-1598
    • Picotti, P.1    Aebersold, R.2    Domon, B.3
  • 24
    • 34250722602 scopus 로고    scopus 로고
    • Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks
    • Wolf-Yadlin, A., Hautaniemi, S., Lauffenburger, D. A., White, F. M., Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks. Proc. Natl. Acad. Sci. USA 2007, 104, 5860-5865.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 5860-5865
    • Wolf-Yadlin, A.1    Hautaniemi, S.2    Lauffenburger, D.A.3    White, F.M.4
  • 25
    • 63049092393 scopus 로고    scopus 로고
    • Affinity prefractionation for MS-based plasma proteomics
    • Pernemalm, M., Lewensohn, R., Lehtio, J., Affinity prefractionation for MS-based plasma proteomics. Proteomics 2009, 9, 1420-1427.
    • (2009) Proteomics , vol.9 , pp. 1420-1427
    • Pernemalm, M.1    Lewensohn, R.2    Lehtio, J.3
  • 26
    • 79551474552 scopus 로고    scopus 로고
    • Protein and peptide fractionation, enrichment and depletion: tools for the complex proteome
    • Ly, L., Wasinger, V. C., Protein and peptide fractionation, enrichment and depletion: tools for the complex proteome. Proteomics 2011, 11, 513-534.
    • (2011) Proteomics , vol.11 , pp. 513-534
    • Ly, L.1    Wasinger, V.C.2
  • 27
    • 77957665187 scopus 로고    scopus 로고
    • A quantitative targeted proteomics approach to validate predicted microRNA targets in C. elegans
    • Jovanovic, M., Reiter, L., Picotti, P., Lange, V. et al., A quantitative targeted proteomics approach to validate predicted microRNA targets in C. elegans. Nat. Methods 2010, 7, 837-842.
    • (2010) Nat. Methods , vol.7 , pp. 837-842
    • Jovanovic, M.1    Reiter, L.2    Picotti, P.3    Lange, V.4
  • 28
    • 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, J. P., Lenz, C. et al., Multiple reaction monitoring cubed for protein quantification at the low nanogram/milliliter level in nondepleted human serum. Anal. Chem. 2009, 81, 9343-9352.
    • (2009) Anal. Chem. , vol.81 , pp. 9343-9352
    • Fortin, T.1    Salvador, A.2    Charrier, J.P.3    Lenz, C.4
  • 29
    • 79955809067 scopus 로고    scopus 로고
    • Methods for peptide and protein quantitation by liquid chromatography-multiple reaction monitoring mass spectrometry
    • Zhang, H., Liu, Q., Zimmerman, L. J., Ham, A. J. et al., Methods for peptide and protein quantitation by liquid chromatography-multiple reaction monitoring mass spectrometry. Mol. Cell. Proteomics 2011, 10, M110.006593.
    • (2011) Mol. Cell. Proteomics , vol.10
    • Zhang, H.1    Liu, Q.2    Zimmerman, L.J.3    Ham, A.J.4
  • 30
    • 38349068918 scopus 로고    scopus 로고
    • Quantitative, multiplexed assays for low abundance prote ins in plasma by targeted mass spectrometry and stable isotope dilution
    • Keshishian, H., Addona, T., Burgess, M., Kuhn, E. et al., Quantitative, multiplexed assays for low abundance prote ins in plasma by targeted mass spectrometry and stable isotope dilution. Mol. Cell. Proteomics 2007, 6, 2212-2229.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 2212-2229
    • Keshishian, H.1    Addona, T.2    Burgess, M.3    Kuhn, E.4
  • 31
    • 79951518985 scopus 로고    scopus 로고
    • Mining the plasma proteome for disease application across seven logs of protein abundance
    • Zhang, Q., Faca, V. M., Hanash, S. M., Mining the plasma proteome for disease application across seven logs of protein abundance. J. Proteome Res. 2011, 10, 46-50.
    • (2011) J. Proteome Res. , vol.10 , pp. 46-50
    • Zhang, Q.1    Faca, V.M.2    Hanash, S.M.3
  • 32
    • 55049104915 scopus 로고    scopus 로고
    • Accurate inclusion mass screening. A bridge from unbiased discovery to targeted assay development for biomarker verification
    • Jaffe, J. D., Keshishian, H., Chang, B., Addona, T. A. et al., Accurate inclusion mass screening. A bridge from unbiased discovery to targeted assay development for biomarker verification. Mol. Cel. Proteomics 2008, 7, 1952-1962.
    • (2008) Mol. Cel. Proteomics , vol.7 , pp. 1952-1962
    • Jaffe, J.D.1    Keshishian, H.2    Chang, B.3    Addona, T.A.4
  • 33
    • 54049090766 scopus 로고    scopus 로고
    • Selected reaction monitoring for quantitative proteomics: a tutorial
    • Lange, V., Picotti, P., Domon, B., Aebersold, R., Selected reaction monitoring for quantitative proteomics: a tutorial. Mol. Syst. Biol. 2008, 4, 222, 1-14.
    • (2008) Mol. Syst. Biol. , vol.4 , Issue.222 , pp. 1-14
    • Lange, V.1    Picotti, P.2    Domon, B.3    Aebersold, R.4
  • 34
    • 53049087292 scopus 로고    scopus 로고
    • Application of silver nanoparticles capped with different functional groups as the matrix and affinity probes in surface-assisted laser desorption/ionization ion trap mass spectrometry for rapid analysis of sulfur drugs and biothiols in human urine
    • Shrivas, K., Wu, H. F., Application of silver nanoparticles capped with different functional groups as the matrix and affinity probes in surface-assisted laser desorption/ionization ion trap mass spectrometry for rapid analysis of sulfur drugs and biothiols in human urine. Rapid Comm. Mass Spectrom. 2008, 22, 2863-2872.
    • (2008) Rapid Comm. Mass Spectrom. , vol.22 , pp. 2863-2872
    • Shrivas, K.1    Wu, H.F.2
  • 35
    • 79951884309 scopus 로고    scopus 로고
    • Nanoparticle-based mass spectrometry for the analysis of biomolecules
    • Chiang, C. K., Chen, W. T., Chang, H. T., Nanoparticle-based mass spectrometry for the analysis of biomolecules. Chem. Soc. Rev. 2011, 40, 1269-1281.
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 1269-1281
    • Chiang, C.K.1    Chen, W.T.2    Chang, H.T.3
  • 36
    • 67449092269 scopus 로고    scopus 로고
    • Clinical quantitation of prostate-specific antigen specific biomarker in the low nanogram/milliliter range by conventional bore liquid chromatography tandem mass spectrometry (multiple reaction monitoring) coupling and correlation with ELISA tests
    • Fortin, T., Salvador, A., Charrier, J. P., Lenz, C. et al., Clinical quantitation of prostate-specific antigen specific biomarker in the low nanogram/milliliter range by conventional bore liquid chromatography tandem mass spectrometry (multiple reaction monitoring) coupling and correlation with ELISA tests. Mol. Cel. Proteomics 2009, 8, 1006-1015.
    • (2009) Mol. Cel. Proteomics , vol.8 , pp. 1006-1015
    • Fortin, T.1    Salvador, A.2    Charrier, J.P.3    Lenz, C.4
  • 37
    • 71049187147 scopus 로고    scopus 로고
    • Quantification of cardiovascular biomarker in patient plasma by targeted mass spectrometry and stable isotope dilution
    • Keshishian, H., Addona, T., Burgess, M., Mani, D. R. et al. Quantification of cardiovascular biomarker in patient plasma by targeted mass spectrometry and stable isotope dilution. Mol. Cell Proteomics 2009, 8, 2339-2349.
    • (2009) Mol. Cell Proteomics , vol.8 , pp. 2339-2349
    • Keshishian, H.1    Addona, T.2    Burgess, M.3    Mani, D.R.4
  • 38
    • 70549113220 scopus 로고    scopus 로고
    • Perspectives of targeted mass spectrometry for protein biomarker verification
    • Hüttenhain, R., Malmström, J., Picotti, P., Aebersold, R., Perspectives of targeted mass spectrometry for protein biomarker verification. Curr. Opin. Chem. Biol. 2009, 13, 518-525.
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 518-525
    • Hüttenhain, R.1    Malmström, J.2    Picotti, P.3    Aebersold, R.4
  • 39
    • 34548127562 scopus 로고    scopus 로고
    • Ionization and transmission efficiency in an electrospray ionization-mass spectrometry interface
    • Pagea, J. S., Kellya, R. T., Tanga, K., Smith, R. D., Ionization and transmission efficiency in an electrospray ionization-mass spectrometry interface. J. Am. Soc. Mass Spectrom. 2007, 18, 1582-1590
    • (2007) J. Am. Soc. Mass Spectrom. , vol.18 , pp. 1582-1590
    • Pagea, J.S.1    Kellya, R.T.2    Tanga, K.3    Smith, R.D.4
  • 40
    • 33846548168 scopus 로고    scopus 로고
    • Mass spectrometric detection of tissue proteins in plasma
    • Zhang, H., Liu, A., Loriaux, P., Wollscheid, B. et al., Mass spectrometric detection of tissue proteins in plasma. Mol. Cell. Proteomics 2006, 6, 64-71.
    • (2006) Mol. Cell. Proteomics , vol.6 , pp. 64-71
    • Zhang, H.1    Liu, A.2    Loriaux, P.3    Wollscheid, B.4
  • 41
    • 0001644020 scopus 로고    scopus 로고
    • The human plasma proteome: history, character, and diagnostic prospects
    • Anderson, N. L., Anderson, N. G., The human plasma proteome: history, character, and diagnostic prospects. Mol. Cell. Proteomics 2002, 1, 845-867.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 845-867
    • Anderson, N.L.1    Anderson, N.G.2
  • 43
    • 40549088497 scopus 로고    scopus 로고
    • Protein profiling of human plasma samples by two-dimensional electrophoresis
    • Cho, S. Y., Lee, E. Y., Kim, H. Y., Kang, M. J. et al., Protein profiling of human plasma samples by two-dimensional electrophoresis. Methods Mol. Biol. 2008, 428, 57-75.
    • (2008) Methods Mol. Biol. , vol.428 , pp. 57-75
    • Cho, S.Y.1    Lee, E.Y.2    Kim, H.Y.3    Kang, M.J.4
  • 44
    • 11144290985 scopus 로고    scopus 로고
    • Proteomic analysis of human serum by two-dimensional differential gel electrophoresis after depletion of high-abundant proteins
    • Chromy, B. A., Gonzales, A. D., Perkins, J., Choi, M. W. et al., Proteomic analysis of human serum by two-dimensional differential gel electrophoresis after depletion of high-abundant proteins. J. Proteome Res. 2004, 3, 1120-1127.
    • (2004) J. Proteome Res. , vol.3 , pp. 1120-1127
    • Chromy, B.A.1    Gonzales, A.D.2    Perkins, J.3    Choi, M.W.4
  • 45
    • 23944459569 scopus 로고    scopus 로고
    • Efficient prefractionation of low-abundance proteins in human plasma and construction of a two-dimensional map
    • Cho, S. Y., Lee, E. Y., Lee, J. S., Kim, H. Y. et al., Efficient prefractionation of low-abundance proteins in human plasma and construction of a two-dimensional map. Proteomic 2005, 5, 3386-3396.
    • (2005) Proteomic , vol.5 , pp. 3386-3396
    • Cho, S.Y.1    Lee, E.Y.2    Lee, J.S.3    Kim, H.Y.4
  • 46
    • 23944524368 scopus 로고    scopus 로고
    • Depletion of multiple high-abundance proteins improves protein profiling capacities of human serum and plasma
    • Echan, L. A., Tang, H. Y., Ali-Khan, N., Lee, K. et al., Depletion of multiple high-abundance proteins improves protein profiling capacities of human serum and plasma. Proteomics 2005, 5, 3292-3303.
    • (2005) Proteomics , vol.5 , pp. 3292-3303
    • Echan, L.A.1    Tang, H.Y.2    Ali-Khan, N.3    Lee, K.4
  • 47
    • 84869883685 scopus 로고    scopus 로고
    • Clinical use of phosphorylated proteins in blood serum analysed by immobilised metal ion affinity chromatography and mass spectrometry
    • Jaros, J. A., Guest, P. C., Ramoune, H., Rothermundt, M. et al., Clinical use of phosphorylated proteins in blood serum analysed by immobilised metal ion affinity chromatography and mass spectrometry. J. Proteomics 2012, 76, 36-42.
    • (2012) J. Proteomics , vol.76 , pp. 36-42
    • Jaros, J.A.1    Guest, P.C.2    Ramoune, H.3    Rothermundt, M.4
  • 48
    • 65349106511 scopus 로고    scopus 로고
    • Hydrophilic interaction chromatography for fractionation and enrichment of the phosphoproteome
    • McNulty, D. E., Annan, R. S., Hydrophilic interaction chromatography for fractionation and enrichment of the phosphoproteome. Methods Mol Biol. 2009, 527, 93-105.
    • (2009) Methods Mol Biol , vol.527 , pp. 93-105
    • McNulty, D.E.1    Annan, R.S.2
  • 49
    • 59149084542 scopus 로고    scopus 로고
    • Targeted proteomic strategy for clinical biomarker discovery
    • Schiess, R., Wollscheid, B., Aebersold, R., Targeted proteomic strategy for clinical biomarker discovery. Mol. Oncol. 2009, 3, 33-44.
    • (2009) Mol. Oncol. , vol.3 , pp. 33-44
    • Schiess, R.1    Wollscheid, B.2    Aebersold, R.3
  • 50
    • 79959424627 scopus 로고    scopus 로고
    • Quantitative, high-resolution proteomics for data-driven systems biology
    • Cox, J., Mann, M., Quantitative, high-resolution proteomics for data-driven systems biology. Annu. Rev. Biochem. 2011, 7, 273-299.
    • (2011) Annu. Rev. Biochem. , vol.7 , pp. 273-299
    • Cox, J.1    Mann, M.2
  • 51
    • 80855128254 scopus 로고    scopus 로고
    • Deep proteome and transcriptome mapping of a human cancer cell line
    • Nagaraj, N., Wisniewski, J. R., Geiger, T., Cox, J. et al., Deep proteome and transcriptome mapping of a human cancer cell line. Mol. Syst. Biol. 2011, 7, 1-8.
    • (2011) Mol. Syst. Biol. , vol.7 , pp. 1-8
    • Nagaraj, N.1    Wisniewski, J.R.2    Geiger, T.3    Cox, J.4
  • 52
    • 67650564834 scopus 로고    scopus 로고
    • Multi-site assessment of the precision and reproducibility of multiple reaction monitoring-based measurements of proteins in plasma
    • Addona, T., Abbatiello, S., Schilling, B., Skates, S. et al., Multi-site assessment of the precision and reproducibility of multiple reaction monitoring-based measurements of proteins in plasma. Nat. Biotechnol. 2009, 27, 12.
    • (2009) Nat. Biotechnol. , vol.27 , pp. 12
    • Addona, T.1    Abbatiello, S.2    Schilling, B.3    Skates, S.4
  • 53
    • 84878312675 scopus 로고    scopus 로고
    • Multidimensional nano-HPLC coupled with tandem mass spectrometry for analyzing biotinylated proteins
    • DOI 10.1007/s00216-012-6057-9
    • Sproß, J., Brauch, S., Mandel, F., Wagner, M. et al., Multidimensional nano-HPLC coupled with tandem mass spectrometry for analyzing biotinylated proteins. Anal. Bioanal. Chem. 2012. DOI 10.1007/s00216-012-6057-9
    • (2012) Anal. Bioanal. Chem.
    • Sproß, J.1    Brauch, S.2    Mandel, F.3    Wagner, M.4
  • 54
    • 79955087258 scopus 로고    scopus 로고
    • Immobilized enzyme reactors in proteomics
    • Ma, J., Zhang, L., Liang, Z., Shan, Y. et al., Immobilized enzyme reactors in proteomics. Trends Anal. Chem. 2011, 30, 691-702.
    • (2011) Trends Anal. Chem. , vol.30 , pp. 691-702
    • Ma, J.1    Zhang, L.2    Liang, Z.3    Shan, Y.4
  • 55
    • 70349762816 scopus 로고    scopus 로고
    • Integrated protein analysis platform based on column switch recycling size exclusion chromatography, microenzymatic reactor and μRPLC-ESI-MS/MS
    • Yuan, H., Zhou, Y., Zhang, L., Liang, Z. et al., Integrated protein analysis platform based on column switch recycling size exclusion chromatography, microenzymatic reactor and μRPLC-ESI-MS/MS. J. Chromatogr. A 2009, 1216, 7478-7482.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 7478-7482
    • Yuan, H.1    Zhou, Y.2    Zhang, L.3    Liang, Z.4
  • 56
    • 68049112516 scopus 로고    scopus 로고
    • Evaluation of a high intensity focused ultrasound-immobilized trypsin digestion and 18O-labeling method for quantitative proteomics
    • López-Ferrer, D., Hixson, K. K., Smallwood, H., Squier, T. C., Evaluation of a high intensity focused ultrasound-immobilized trypsin digestion and 18O-labeling method for quantitative proteomics. Anal. Chem. 2009, 81, 6272-6277.
    • (2009) Anal. Chem. , vol.81 , pp. 6272-6277
    • López-Ferrer, D.1    Hixson, K.K.2    Smallwood, H.3    Squier, T.C.4
  • 57
    • 84864153271 scopus 로고    scopus 로고
    • Nano-flow multidimensional liquid chromatography platform integrate combination of protein and peptide separation for proteome analysis
    • Xia, S., Tao, D., Yuan, H., Zhou, Y. et al., Nano-flow multidimensional liquid chromatography platform integrate combination of protein and peptide separation for proteome analysis. J. Sep. Sci. 2012, 35, 1764-1770.
    • (2012) J. Sep. Sci. , vol.35 , pp. 1764-1770
    • Xia, S.1    Tao, D.2    Yuan, H.3    Zhou, Y.4
  • 58
    • 70350648825 scopus 로고    scopus 로고
    • Integrated platform for proteome analysis with combination of protein and peptide separation via online digestion
    • Yuan, H., Zhang, L., Hou, C., Zhu, G. et al., Integrated platform for proteome analysis with combination of protein and peptide separation via online digestion. Anal. Chem. 2009, 81, 8708-8714.
    • (2009) Anal. Chem. , vol.81 , pp. 8708-8714
    • Yuan, H.1    Zhang, L.2    Hou, C.3    Zhu, G.4
  • 59
    • 84861895091 scopus 로고    scopus 로고
    • Integrated platform for proteome profiling with combination of microreversed phase based protein and peptide separation via online solvent exchange and protein digestion
    • Yuan, H., Zhou, Y., Xia, S., Zhang, L. et al., Integrated platform for proteome profiling with combination of microreversed phase based protein and peptide separation via online solvent exchange and protein digestion. Anal. Chem. 2012, 84, 5124-5132.
    • (2012) Anal. Chem. , vol.84 , pp. 5124-5132
    • Yuan, H.1    Zhou, Y.2    Xia, S.3    Zhang, L.4
  • 60
    • 61849115764 scopus 로고    scopus 로고
    • Glycoproteomic reactor for human plasma
    • Zhou, H., Hou, W., Denis, N. J., Zhou, H. et al., Glycoproteomic reactor for human plasma. J. Proteome Res. 2009, 8, 556-566.
    • (2009) J. Proteome Res. , vol.8 , pp. 556-566
    • Zhou, H.1    Hou, W.2    Denis, N.J.3    Zhou, H.4


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