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Volumn 742, Issue , 2011, Pages 227-247

Application of Mass Spectrometry to Study Proteomics and Interactomics in Cystic Fibrosis

Author keywords

Cystic fibrosis; LC MS MS; mass spectrometer; MudPIT; multidimensional; proteome; proteomics; spectral counting

Indexed keywords

TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 80052534076     PISSN: 10643745     EISSN: 19406029     Source Type: Book Series    
DOI: 10.1007/978-1-61779-120-8_14     Document Type: Chapter
Times cited : (11)

References (159)
  • 1
    • 50649123290 scopus 로고    scopus 로고
    • CFTR function and prospects for therapy
    • Riordan, J. R. (2008) CFTR function and prospects for therapy. Annu Rev Biochem 77, 701–726.
    • (2008) Annu Rev Biochem , vol.77 , pp. 701-726
    • Riordan, J.R.1
  • 2
    • 33750842131 scopus 로고    scopus 로고
    • Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis
    • Wang, X., Venable, J., LaPointe, P., Hutt, D. M., Koulov, A. V., Coppinger, J., et al. (2006) Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis. Cell 127, 803–815.
    • (2006) Cell , vol.127 , pp. 803-815
    • Wang, X.1    Venable, J.2    Lapointe, P.3    Hutt, D.M.4    Koulov, A.V.5    Coppinger, J.6
  • 3
    • 67349208911 scopus 로고    scopus 로고
    • Bioinformatics analysis of mass spectrometrybased proteomics data sets
    • Kumar, C., and Mann, M. (2009) Bioinformatics analysis of mass spectrometrybased proteomics data sets. FEBS Lett 583, 1703–1712.
    • (2009) FEBS Lett , vol.583 , pp. 1703-1712
    • Kumar, C.1    Mann, M.2
  • 4
    • 67651173106 scopus 로고    scopus 로고
    • Proteomics by mass spectrometry: Approaches, advances, and applications
    • Yates, J. R., Ruse, C. I., and Nakorchevsky, A. (2009) Proteomics by mass spectrometry: approaches, advances, and applications. Annu Rev Biomed Eng 11, 49–79.
    • (2009) Annu Rev Biomed Eng , vol.11 , pp. 49-79
    • Yates, J.R.1    Ruse, C.I.2    Nakorchevsky, A.3
  • 5
    • 10644294652 scopus 로고    scopus 로고
    • Global proteomic approach unmasks involvement of keratins 8 and 18 in the delivery of cystic fibrosis transmembrane conductance regulator (CFTR)/deltaF508CFTR to the plasma membrane
    • Davezac, N., Tondelier, D., Lipecka, J., Fanen, P., Demaugre, F., Debski, J., et al. (2004) Global proteomic approach unmasks involvement of keratins 8 and 18 in the delivery of cystic fibrosis transmembrane conductance regulator (CFTR)/deltaF508CFTR to the plasma membrane. Proteomics 4, 3833–3844.
    • (2004) Proteomics , vol.4 , pp. 3833-3844
    • Davezac, N.1    Tondelier, D.2    Lipecka, J.3    Fanen, P.4    Demaugre, F.5    Debski, J.6
  • 7
    • 46749108883 scopus 로고    scopus 로고
    • Chemical rescue of deltaF508CFTR mimics genetic repair in cystic fibrosis bronchial epithelial cells
    • Singh, O. V., Pollard, H. B., and Zeitlin, P. L. (2008) Chemical rescue of deltaF508CFTR mimics genetic repair in cystic fibrosis bronchial epithelial cells. Mol Cell Proteomics 7, 1099–1110.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 1099-1110
    • Singh, O.V.1    Pollard, H.B.2    Zeitlin, P.L.3
  • 8
    • 33749256500 scopus 로고    scopus 로고
    • De novo biosynthetic profiling of high abundance proteins in cystic fibrosis lung epithelial cells
    • Pollard, H. B., Eidelman, O., Jozwik, C., Huang, W., Srivastava, M., Ji, X. D., et al. (2006) De novo biosynthetic profiling of high abundance proteins in cystic fibrosis lung epithelial cells. Mol Cell Proteomics 5, 1628–1637.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 1628-1637
    • Pollard, H.B.1    Eidelman, O.2    Jozwik, C.3    Huang, W.4    Srivastava, M.5    Ji, X.D.6
  • 9
    • 33644835493 scopus 로고    scopus 로고
    • Pharmacoproteomics of 4phenylbutyrate-treated IB3-1 cystic fibrosis bronchial epithelial cells
    • Singh, O. V., Vij, N., Mogayzel, P. J., Jr., Jozwik, C., Pollard, H. B., and Zeitlin, P. L. (2006) Pharmacoproteomics of 4phenylbutyrate-treated IB3-1 cystic fibrosis bronchial epithelial cells. JProteomeRes5, 562–571.
    • (2006) Jproteomeres , vol.5 , pp. 562-571
    • Singh, O.V.1    Vij, N.2    Mogayzel, P.J.3    Jozwik, C.4    Pollard, H.B.5    Zeitlin, P.L.6
  • 10
    • 20044365463 scopus 로고    scopus 로고
    • High abundance protein profiling of cystic fibrosis lung epithelial cells
    • Pollard, H. B., Ji, X. D., Jozwik, C., and Jacobowitz, D. M. (2005) High abundance protein profiling of cystic fibrosis lung epithelial cells. Proteomics 5, 2210–2226.
    • (2005) Proteomics , vol.5 , pp. 2210-2226
    • Pollard, H.B.1    Ji, X.D.2    Jozwik, C.3    Jacobowitz, D.M.4
  • 11
    • 34247177900 scopus 로고    scopus 로고
    • Proteomic biomarker discovery for the monogenic disease cystic fibrosis
    • Penque, D. (2007) Proteomic biomarker discovery for the monogenic disease cystic fibrosis. Expert Rev Proteomics 4, 199–209.
    • (2007) Expert Rev Proteomics , vol.4 , pp. 199-209
    • Penque, D.1
  • 12
    • 72649099616 scopus 로고    scopus 로고
    • SELDI-TOF biomarker signatures for cystic fibrosis, asthma and chronic obstructive pulmonary disease
    • Gomes-Alves, P., Imrie, M., Gray, R. D., Nogueira, P., Ciordia, S., Pacheco, P., et al. (2010) SELDI-TOF biomarker signatures for cystic fibrosis, asthma and chronic obstructive pulmonary disease. Clin Biochem 43, 168–177.
    • (2010) Clin Biochem , vol.43 , pp. 168-177
    • Gomes-Alves, P.1    Imrie, M.2    Gray, R.D.3    Nogueira, P.4    Ciordia, S.5    Pacheco, P.6
  • 14
    • 52749097637 scopus 로고    scopus 로고
    • Proteomic and computational analysis of bronchoalveolar proteins during the course of the acute respiratory distress syndrome
    • Chang, D. W., Hayashi, S., Gharib, S. A., Vaisar, T., King, S. T., and Tsuchiya, M. (2008) Proteomic and computational analysis of bronchoalveolar proteins during the course of the acute respiratory distress syndrome. Am J Respir Crit Care Med 178, 701–709.
    • (2008) Am J Respir Crit Care Med , vol.178 , pp. 701-709
    • Chang, D.W.1    Hayashi, S.2    Gharib, S.A.3    Vaisar, T.4    King, S.T.5    Tsuchiya, M.6
  • 15
    • 44449086044 scopus 로고    scopus 로고
    • Spectral index for assessment of differential protein expression in shotgun proteomics
    • Fu, X., Gharib, S. A., Green, P. S., Aitken, M. L., Frazer, D. A., Park, D. R., et al. (2008) Spectral index for assessment of differential protein expression in shotgun proteomics. J Proteome Res 7, 845–854.
    • (2008) J Proteome Res , vol.7 , pp. 845-854
    • Fu, X.1    Gharib, S.A.2    Green, P.S.3    Aitken, M.L.4    Frazer, D.A.5    Park, D.R.6
  • 17
    • 51349144874 scopus 로고    scopus 로고
    • Biomarkers for cystic fibrosis lung disease: Application of SELDI-TOF mass spec trometry to BAL fluid
    • MacGregor, G., Gray, R. D., Hilliard, T. N., Imrie, M., Boyd, A. C., Alton, E. W., et al. (2008) Biomarkers for cystic fibrosis lung disease: application of SELDI-TOF mass spec trometry to BAL fluid. J Cyst Fibros 7, 352–358.
    • (2008) J Cyst Fibros , vol.7 , pp. 352-358
    • Macgregor, G.1    Gray, R.D.2    Hilliard, T.N.3    Imrie, M.4    Boyd, A.C.5    Alton, E.W.6
  • 18
    • 70350457544 scopus 로고    scopus 로고
    • From proteomics to prescription-the search for COPD biomarkers
    • Nicholas, B. L., O’Connor, C. D., and Djukanovic, R. (2009) From proteomics to prescription-the search for COPD biomarkers. COPD 6, 298–303.
    • (2009) COPD , vol.6 , pp. 298-303
    • Nicholas, B.L.1    O’Connor, C.D.2    Djukanovic, R.3
  • 19
    • 70349336549 scopus 로고    scopus 로고
    • Induced sputum: A window to lung pathology
    • Nicholas, B., and Djukanovic, R. (2009) Induced sputum: a window to lung pathology. Biochem Soc Trans 37, 868–872.
    • (2009) Biochem Soc Trans , vol.37 , pp. 868-872
    • Nicholas, B.1    Djukanovic, R.2
  • 20
    • 85139052844 scopus 로고    scopus 로고
    • Nicholas, B., Skipp, P., Mould, R., Rennard, S., Davies, D. E., O‘Connor, C. D., et al. (2006) Shotgun proteomic analysis of human-induced sputum. Proteomics 6, 4390–4401.
    • Nicholas, B., Skipp, P., Mould, R., Rennard, S., Davies, D. E., O‘Connor, C. D., et al. (2006) Shotgun proteomic analysis of human-induced sputum. Proteomics 6, 4390–4401.
  • 21
    • 70449729515 scopus 로고    scopus 로고
    • Biomarkers of lung-related diseases: Current knowledge by proteomic approaches
    • Lau, A. T., and Chiu, J. F. (2009) Biomarkers of lung-related diseases: current knowledge by proteomic approaches. JCellPhysiol221, 535–543.
    • (2009) Jcellphysiol , vol.221 , pp. 535-543
    • Lau, A.T.1    Chiu, J.F.2
  • 22
    • 33846834167 scopus 로고    scopus 로고
    • Direct interaction with filamins modulates the stability and plasma membrane expression of CFTR
    • Thelin, W. R., Chen, Y., Gentzsch, M., Kreda, S. M., Sallee, J. L., Scarlett, C. O., et al. (2007) Direct interaction with filamins modulates the stability and plasma membrane expression of CFTR. J Clin Invest 117, 364–374.
    • (2007) J Clin Invest , vol.117 , pp. 364-374
    • Thelin, W.R.1    Chen, Y.2    Gentzsch, M.3    Kreda, S.M.4    Sallee, J.L.5    Scarlett, C.O.6
  • 23
    • 70449521295 scopus 로고    scopus 로고
    • Low temperature restoring effect on F508del-CFTR misprocessing: A proteomic approach
    • Gomes-Alves, P., Neves, S., Coelho, A. V., and Penque, D. (2009) Low temperature restoring effect on F508del-CFTR misprocessing: a proteomic approach. JProteomics 73, 218–230.
    • (2009) Jproteomics , vol.73 , pp. 218-230
    • Gomes-Alves, P.1    Neves, S.2    Coelho, A.V.3    Penque, D.4
  • 24
    • 76849090407 scopus 로고    scopus 로고
    • Rescue of F508del-CFTR by RXR motif inactivation triggers proteome modulation associated with the unfolded protein response
    • Gomes-Alves, P., Couto, F., Pesquita, C., Coelho, A. V., and Penque, D. (2010) Rescue of F508del-CFTR by RXR motif inactivation triggers proteome modulation associated with the unfolded protein response. Biochim Biophys Acta 1804, 856–865.
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 856-865
    • Gomes-Alves, P.1    Couto, F.2    Pesquita, C.3    Coelho, A.V.4    Penque, D.5
  • 25
    • 75749157016 scopus 로고    scopus 로고
    • Targeted quantitation of overexpressed and endogenous cystic fibrosis transmembrane conductance regulator using multiple reaction monitoring tandem mass spectrometry and oxygen stable isotope dilution
    • Jiang, H., Ramos, A. A., and Yao, X. (2010) Targeted quantitation of overexpressed and endogenous cystic fibrosis transmembrane conductance regulator using multiple reaction monitoring tandem mass spectrometry and oxygen stable isotope dilution. Anal Chem 82, 336–342.
    • (2010) Anal Chem , vol.82 , pp. 336-342
    • Jiang, H.1    Ramos, A.A.2    Yao, X.3
  • 26
    • 67651173106 scopus 로고    scopus 로고
    • Proteomics by mass spectrometry: Approaches, advances, and applications
    • Yates, J., Ruse, C. I., and Nakorchevsky, A. (2009) Proteomics by mass spectrometry: approaches, advances, and applications. Annu Rev Biomed Eng 11, 49–79.
    • (2009) Annu Rev Biomed Eng , vol.11 , pp. 49-79
    • Yates, J.1    Ruse, C.I.2    Nakorchevsky, A.3
  • 27
    • 0025677738 scopus 로고
    • Mass spectrometry of peptides and proteins by matrix-assisted ultraviolet laser desorption/ionization
    • Hillenkamp, F., and Karas, M. (1990) Mass spectrometry of peptides and proteins by matrix-assisted ultraviolet laser desorption/ionization. Methods Enzymol 193, 280–295.
    • (1990) Methods Enzymol , vol.193 , pp. 280-295
    • Hillenkamp, F.1    Karas, M.2
  • 28
    • 0042318496 scopus 로고    scopus 로고
    • The origin of macromolecule ionization by laser irradiation (Nobel Lecture)
    • Tanaka, K. (2003) The origin of macromolecule ionization by laser irradiation (Nobel Lecture). Angew Chem Int Ed Engl 42, 3860–3870.
    • (2003) Angew Chem Int Ed Engl , vol.42 , pp. 3860-3870
    • Tanaka, K.1
  • 29
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn, J. B., Mann, M., Meng, C. K., Wong, S. F., and Whitehouse, C. M. (1989) Electrospray ionization for mass spectrometry of large biomolecules. Science 246, 64–71.
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 30
    • 44649169019 scopus 로고    scopus 로고
    • Improved repeatability and matrixassisted desorption/ionization – time of flight mass spectrometry compatibility in capillary isoelectric focusing
    • Silvertand, L. H., Torano, J. S., de Jong, G. J., and van Bennekom, W. P. (2008) Improved repeatability and matrixassisted desorption/ionization – time of flight mass spectrometry compatibility in capillary isoelectric focusing. Electrophoresis 29, 1985–1996.
    • (2008) Electrophoresis , vol.29 , pp. 1985-1996
    • Silvertand, L.H.1    Torano, J.S.2    de Jong, G.J.3    van Bennekom, W.P.4
  • 31
    • 26844536197 scopus 로고    scopus 로고
    • Simple and robust two-layer matrix/sample preparation method for MALDI MS/MS analysis of peptides
    • Zheng, J., Li, N., Ridyard, M., Dai, H., Robbins, S. M., and Li, L. (2005) Simple and robust two-layer matrix/sample preparation method for MALDI MS/MS analysis of peptides. JProteomeRes4, 1709–1716.
    • (2005) Jproteomeres , vol.4 , pp. 1709-1716
    • Zheng, J.1    Li, N.2    Ridyard, M.3    Dai, H.4    Robbins, S.M.5    Li, L.6
  • 32
    • 0032439034 scopus 로고    scopus 로고
    • Rapid identification and screening of proteins from whole cell lysates of human erythroleukemia cells in the liquid phase, using non-porous reversed phase highperformance liquid chromatography separations of proteins followed by matrix-assisted laser desorption/ionization mass spectrometry analysis and sequence database searching
    • Chen, Y., Wall, D., and Lubman, D. M. (1998) Rapid identification and screening of proteins from whole cell lysates of human erythroleukemia cells in the liquid phase, using non-porous reversed phase highperformance liquid chromatography separations of proteins followed by matrix-assisted laser desorption/ionization mass spectrometry analysis and sequence database searching. Rapid Commun Mass Spectrom 12, 1994–2003.
    • (1998) Rapid Commun Mass Spectrom , vol.12 , pp. 1994-2003
    • Chen, Y.1    Wall, D.2    Lubman, D.M.3
  • 33
    • 0035870175 scopus 로고    scopus 로고
    • Packed capillary reversed-phase liquid chromatography with high-performance electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry for proteomics
    • Shen, Y., Zhao, R., Belov, M. E., Conrads, T. P., Anderson, G. A., Tangm, K., et al. (2001) Packed capillary reversed-phase liquid chromatography with high-performance electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry for proteomics. Anal Chem 73, 1766–1775.
    • (2001) Anal Chem , vol.73 , pp. 1766-1775
    • Shen, Y.1    Zhao, R.2    Belov, M.E.3    Conrads, T.P.4    Anderson, G.A.5    Tangm, K.6
  • 34
    • 0034651731 scopus 로고    scopus 로고
    • Atmospheric pressure matrix-assisted laser desorption/ionization mass spectrometry
    • Laiko, V. V., Baldwin, M. A., and Burlingame, A. L. (2000) Atmospheric pressure matrix-assisted laser desorption/ionization mass spectrometry. Anal Chem 72, 652–657.
    • (2000) Anal Chem , vol.72 , pp. 652-657
    • Laiko, V.V.1    Baldwin, M.A.2    Burlingame, A.L.3
  • 35
    • 0034013944 scopus 로고    scopus 로고
    • Recent advancements in surface-enhanced laser desorption/ionization-time of flightmass spectrometry
    • Merchant, M., and Weinberger, S. R. (2000) Recent advancements in surface-enhanced laser desorption/ionization-time of flightmass spectrometry. Electrophoresis 21, 1164–1177.
    • (2000) Electrophoresis , vol.21 , pp. 1164-1177
    • Merchant, M.1    Weinberger, S.R.2
  • 36
    • 0036684144 scopus 로고    scopus 로고
    • Origin and number of charges observed on multiply-protonated native proteins produced by ESI
    • Felitsyn, N., Peschke, M., and Kebarle, P. (2002) Origin and number of charges observed on multiply-protonated native proteins produced by ESI. Int J Mass Spectrom 219, 39–62.
    • (2002) Int J Mass Spectrom , vol.219 , pp. 39-62
    • Felitsyn, N.1    Peschke, M.2    Kebarle, P.3
  • 37
    • 0242669999 scopus 로고    scopus 로고
    • High-efficiency on-line solid-phase extraction coupling to 15-150-microm-i.d. column liquid chromatography for proteomic analysis
    • Shen, Y., Moore, R. J., Zhao, R., Blonder, J., Auberry, D. L., Masselon, C., et al. (2003) High-efficiency on-line solid-phase extraction coupling to 15-150-microm-i.d. column liquid chromatography for proteomic analysis. Anal Chem 75, 3264–3273.
    • (2003) Anal Chem , vol.75 , pp. 3264-3273
    • Shen, Y.1    Moore, R.J.2    Zhao, R.3    Blonder, J.4    Auberry, D.L.5    Masselon, C.6
  • 38
    • 0036749343 scopus 로고    scopus 로고
    • Proteomics based on high-efficiency capillary separations
    • Shen, Y., and Smith, R. D. (2002) Proteomics based on high-efficiency capillary separations. Electrophoresis 23, 3106–3124.
    • (2002) Electrophoresis , vol.23 , pp. 3106-3124
    • Shen, Y.1    Smith, R.D.2
  • 40
    • 53849145298 scopus 로고    scopus 로고
    • Mass spectrometry for proteomics
    • Han, X., Aslanian, A., and Yates, J. R., 3rd. (2008) Mass spectrometry for proteomics. Curr Opin Chem Biol 12, 483–490.
    • (2008) Curr Opin Chem Biol , vol.12 , pp. 483-490
    • Han, X.1    Aslanian, A.2    Yates, J.R.3
  • 41
    • 3042689578 scopus 로고    scopus 로고
    • Mass spectral analysis in proteomics
    • Yates, J. R., 3rd. (2004) Mass spectral analysis in proteomics. Annu Rev Biophys Biomol Struct 33, 297–316.
    • (2004) Annu Rev Biophys Biomol Struct , vol.33 , pp. 297-316
    • Yates, J.R.1
  • 42
    • 34548291476 scopus 로고    scopus 로고
    • Accurate mass measurements in proteomics
    • Liu, T., Belov, M. E., Jaitly, N., Qian, W. J., and Smith, R. D. (2007) Accurate mass measurements in proteomics. Chem Rev 107, 3621–3653.
    • (2007) Chem Rev , vol.107 , pp. 3621-3653
    • Liu, T.1    Belov, M.E.2    Jaitly, N.3    Qian, W.J.4    Smith, R.D.5
  • 43
    • 57249091714 scopus 로고    scopus 로고
    • Orbitrap mass spectrometry: Instrumentation, ion motion and applications
    • Perry, R. H., Cooks, R. G., and Noll, R. J. (2008) Orbitrap mass spectrometry: instrumentation, ion motion and applications. Mass Spectrom Rev 27, 661–699.
    • (2008) Mass Spectrom Rev , vol.27 , pp. 661-699
    • Perry, R.H.1    Cooks, R.G.2    Noll, R.J.3
  • 44
    • 33745576884 scopus 로고    scopus 로고
    • Recent developments in ion-trap mass spectrometry and related technologies
    • Brancia, F. L. (2006) Recent developments in ion-trap mass spectrometry and related technologies. Expert Rev Proteomics 3, 143–151.
    • (2006) Expert Rev Proteomics , vol.3 , pp. 143-151
    • Brancia, F.L.1
  • 45
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • Domon, B., and Aebersold, R. (2006) Mass spectrometry and protein analysis. Science 312, 212–217.
    • (2006) Science , vol.312 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 46
    • 0038788809 scopus 로고    scopus 로고
    • Product ion spectral simplification using time-delayed fragment ion capture with tandem linear ion traps
    • Hager, J. W. (2003) Product ion spectral simplification using time-delayed fragment ion capture with tandem linear ion traps. Rapid Commun Mass Spectrom 17, 1389–1398.
    • (2003) Rapid Commun Mass Spectrom , vol.17 , pp. 1389-1398
    • Hager, J.W.1
  • 47
    • 0037398266 scopus 로고    scopus 로고
    • Interfacing the orbitrap mass analyzer to an electrospray ion source
    • Hardman, M., and Makarov, A. A. (2003) Interfacing the orbitrap mass analyzer to an electrospray ion source. Anal Chem 75, 1699–1705.
    • (2003) Anal Chem , vol.75 , pp. 1699-1705
    • Hardman, M.1    Makarov, A.A.2
  • 49
    • 33745264884 scopus 로고    scopus 로고
    • Dynamic range of mass accuracy in LTQ orbitrap hybrid mass spectrometer
    • Makarov, A., Denisov, E., Lange, O., and Horning, S. (2006) Dynamic range of mass accuracy in LTQ orbitrap hybrid mass spectrometer. J Am Soc Mass Spectrom 17, 977–982.
    • (2006) J am Soc Mass Spectrom , vol.17 , pp. 977-982
    • Makarov, A.1    Denisov, E.2    Lange, O.3    Horning, S.4
  • 50
    • 3042789073 scopus 로고    scopus 로고
    • Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
    • Syka, J. E., Coon, J. J., Schroeder, M. J., Shabanowitz, J., and Hunt, D. F. (2004) Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc Natl Acad Sci USA 101, 9528–9533.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9528-9533
    • Syka, J.E.1    Coon, J.J.2    Schroeder, M.J.3    Shabanowitz, J.4    Hunt, D.F.5
  • 51
    • 48349147103 scopus 로고    scopus 로고
    • Top-down identification and characterization of biomolecules by mass spectrometry
    • Breuker, K., Jin, M., Han, X., Jiang, H., and McLafferty, F. W. (2008) Top-down identification and characterization of biomolecules by mass spectrometry. J Am Soc Mass Spectrom 19, 1045–1053.
    • (2008) J am Soc Mass Spectrom , vol.19 , pp. 1045-1053
    • Breuker, K.1    Jin, M.2    Han, X.3    Jiang, H.4    McLafferty, F.W.5
  • 52
    • 0030960366 scopus 로고    scopus 로고
    • Rapid “de novo” peptide sequencing by a combination of nanoelectrospray, isotopic labeling and a quadrupole/time-of-flight mass spectrometer
    • Shevchenko, A., Chernushevich, I., Ens, W., Standing, K. G., Thomson, B., Wilm, M., et al. (1997) Rapid “de novo” peptide sequencing by a combination of nanoelectrospray, isotopic labeling and a quadrupole/time-of-flight mass spectrometer. Rapid Commun Mass Spectrom 11, 1015–1024.
    • (1997) Rapid Commun Mass Spectrom , vol.11 , pp. 1015-1024
    • Shevchenko, A.1    Chernushevich, I.2    Ens, W.3    Standing, K.G.4    Thomson, B.5    Wilm, M.6
  • 53
    • 0034811750 scopus 로고    scopus 로고
    • A combined linear ion trap time-of-flight system with improved performance and MS(n) capabilities
    • Collings, B. A., Campbell, J. M., Mao, D., and Douglas, D. J. (2001) A combined linear ion trap time-of-flight system with improved performance and MS(n) capabilities. Rapid Commun Mass Spectrom 15, 1777–1795.
    • (2001) Rapid Commun Mass Spectrom , vol.15 , pp. 1777-1795
    • Collings, B.A.1    Campbell, J.M.2    Mao, D.3    Douglas, D.J.4
  • 54
    • 12444305375 scopus 로고    scopus 로고
    • Linear ion traps in mass spectrometry
    • Douglas, D. J., Frank, A. J., and Mao, D. (2005) Linear ion traps in mass spectrometry. Mass Spectrom Rev 24, 1–29.
    • (2005) Mass Spectrom Rev , vol.24 , pp. 1-29
    • Douglas, D.J.1    Frank, A.J.2    Mao, D.3
  • 55
    • 0001325675 scopus 로고    scopus 로고
    • A two-dimensional quadrupole ion trap mass spectrometer
    • Schwartz, J. C., Senko, M. W., and Syka, J. E. (2002) A two-dimensional quadrupole ion trap mass spectrometer. J Am Soc Mass Spectrom 13, 659–669.
    • (2002) J am Soc Mass Spectrom , vol.13 , pp. 659-669
    • Schwartz, J.C.1    Senko, M.W.2    Syka, J.E.3
  • 56
    • 30744476222 scopus 로고    scopus 로고
    • Performance of a linear ion trap-Orbitrap hybrid for peptide analysis
    • Yates, J. R., Cociorva, D., Liao, L., and Zabrouskov, V. (2006) Performance of a linear ion trap-Orbitrap hybrid for peptide analysis. Anal Chem 78, 493–500.
    • (2006) Anal Chem , vol.78 , pp. 493-500
    • Yates, J.R.1    Cociorva, D.2    Liao, L.3    Zabrouskov, V.4
  • 57
    • 33646899550 scopus 로고    scopus 로고
    • Top-down protein sequencing and MS3 on a hybrid linear quadrupole ion trap-orbitrap mass spectrometer
    • Macek, B., Waanders, L. F., Olsen, J. V., and Mann, M. (2006) Top-down protein sequencing and MS3 on a hybrid linear quadrupole ion trap-orbitrap mass spectrometer. MolCellProteomics5, 949–958.
    • (2006) Molcellproteomics , vol.5 , pp. 949-958
    • Macek, B.1    Waanders, L.F.2    Olsen, J.V.3    Mann, M.4
  • 59
    • 58149401890 scopus 로고    scopus 로고
    • The impact of peptide abundance and dynamic range on stable-isotope-based quantitative proteomic analyses
    • Bakalarski, C. E., Elias, J. E., Villén, J., Haas, W., Gerber, S. A., Everley, P. A., et al. (2008) The impact of peptide abundance and dynamic range on stable-isotope-based quantitative proteomic analyses. JProteomeRes7, 4756–4765.
    • (2008) Jproteomeres , vol.7 , pp. 4756-4765
    • Bakalarski, C.E.1    Elias, J.E.2    Villén, J.3    Haas, W.4    Gerber, S.A.5    Everley, P.A.6
  • 60
    • 65349115741 scopus 로고    scopus 로고
    • A high confidence, manually validated human blood plasma protein reference set
    • Schenk, S., Schoenhals, G. J., Souza, G. D., and Mann, M. (2008) A high confidence, manually validated human blood plasma protein reference set. BMC Med Genomics 1, 41–75.
    • (2008) BMC Med Genomics , vol.1 , pp. 41-75
    • Schenk, S.1    Schoenhals, G.J.2    Souza, G.D.3    Mann, M.4
  • 62
    • 45549100467 scopus 로고    scopus 로고
    • A hybrid method for peptide identification using integer linear optimization, local database search, and quadrupole time-of-flight or OrbiTrap tandem mass spectrometry
    • DiMaggio, P. A., Jr., Floudas, C. A., Lu, B., and Yates, J. R., 3rd. (2008) A hybrid method for peptide identification using integer linear optimization, local database search, and quadrupole time-of-flight or OrbiTrap tandem mass spectrometry. JProteomeRes7, 1584–1593.
    • (2008) Jproteomeres , vol.7 , pp. 1584-1593
    • Dimaggio, P.A.1    Floudas, C.A.2    Lu, B.3    Yates, J.R.4
  • 63
    • 41449095461 scopus 로고    scopus 로고
    • Improving protein identification sensitivity by combining MS and MS/MS information for shotgun proteomics using LTQ-Orbitrap high mass accuracy data
    • Lu, B., Motoyama, A., Ruse, C., Venable, J., and Yates, J. R., 3rd. (2008) Improving protein identification sensitivity by combining MS and MS/MS information for shotgun proteomics using LTQ-Orbitrap high mass accuracy data. Anal Chem 80, 2018–2025.
    • (2008) Anal Chem , vol.80 , pp. 2018-2025
    • Lu, B.1    Motoyama, A.2    Ruse, C.3    Venable, J.4    Yates, J.R.5
  • 65
    • 13844312665 scopus 로고    scopus 로고
    • Differential proteomics: An overview of gel and non-gel based approaches
    • Monteoliva, L., and Albar, J. P. (2004) Differential proteomics: an overview of gel and non-gel based approaches. Brief Funct Genomic Proteomic 3, 220–239.
    • (2004) Brief Funct Genomic Proteomic , vol.3 , pp. 220-239
    • Monteoliva, L.1    Albar, J.P.2
  • 66
    • 34748866570 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis of membrane proteins
    • Braun, R. J., Kinkl, N., Beer, M., and Ueffing, M. (2007) Two-dimensional electrophoresis of membrane proteins. Anal Bioanal Chem 389, 1033–1045.
    • (2007) Anal Bioanal Chem , vol.389 , pp. 1033-1045
    • Braun, R.J.1    Kinkl, N.2    Beer, M.3    Ueffing, M.4
  • 67
    • 12144283108 scopus 로고    scopus 로고
    • Recent advances in capillary separations for proteomics
    • Cooper, J. W., Wang, Y., and Lee, C. S. (2004) Recent advances in capillary separations for proteomics. Electrophoresis 25, 3913–3926.
    • (2004) Electrophoresis , vol.25 , pp. 3913-3926
    • Cooper, J.W.1    Wang, Y.2    Lee, C.S.3
  • 68
    • 34548293752 scopus 로고    scopus 로고
    • Multidimensional separations-based shotgun proteomics
    • Fournier, M. L., Gilmore, J., Martin-Brown, S. A., and Washburn, M. P. (2007) Multidimensional separations-based shotgun proteomics. Chem Rev 107, 3654–3686.
    • (2007) Chem Rev , vol.107 , pp. 3654-3686
    • Fournier, M.L.1    Gilmore, J.2    Martin-Brown, S.A.3    Washburn, M.P.4
  • 69
    • 0037102411 scopus 로고    scopus 로고
    • High-efficiency nanoscale liquid chromatography coupled on-line with mass spectrometry using nanoelectrospray ionization for proteomics
    • Shen, Y., Zhao, R., Berger, S. J., Anderson, G. A., Rodriguez, N., and Smith, R. D. (2002) High-efficiency nanoscale liquid chromatography coupled on-line with mass spectrometry using nanoelectrospray ionization for proteomics. Anal Chem 74, 4235–4249.
    • (2002) Anal Chem , vol.74 , pp. 4235-4249
    • Shen, Y.1    Zhao, R.2    Berger, S.J.3    Anderson, G.A.4    Rodriguez, N.5    Smith, R.D.6
  • 70
    • 28544453069 scopus 로고    scopus 로고
    • Making broad proteome protein measurements in 1–5 min using high-speed RPLC separations and high-accuracy mass measurements
    • Shen, Y., Strittmatter, E. F., Zhang, R., Metz, T. O., Moore, R. J., Li, F., et al. (2005) Making broad proteome protein measurements in 1–5 min using high-speed RPLC separations and high-accuracy mass measurements. Anal Chem 77, 7763–7773.
    • (2005) Anal Chem , vol.77 , pp. 7763-7773
    • Shen, Y.1    Strittmatter, E.F.2    Zhang, R.3    Metz, T.O.4    Moore, R.J.5    Li, F.6
  • 71
    • 20544441071 scopus 로고    scopus 로고
    • Advanced nanoscale separations and mass spectrometry for sensitive high-throughput proteomics
    • Shen, Y., and Smith, R. D. (2005) Advanced nanoscale separations and mass spectrometry for sensitive high-throughput proteomics. Expert Rev Proteomics 2, 431–447.
    • (2005) Expert Rev Proteomics , vol.2 , pp. 431-447
    • Shen, Y.1    Smith, R.D.2
  • 72
    • 27944473996 scopus 로고    scopus 로고
    • Injection valve for ultrahigh-pressure liquid chromatography
    • Anspach, J. A., Maloney, T. D., Brice, R. W., and Colon, L. A. (2005) Injection valve for ultrahigh-pressure liquid chromatography. Anal Chem 77, 7489–7494.
    • (2005) Anal Chem , vol.77 , pp. 7489-7494
    • Anspach, J.A.1    Maloney, T.D.2    Brice, R.W.3    Colon, L.A.4
  • 73
    • 34250156717 scopus 로고    scopus 로고
    • Ultrahigh-pressure liquid chromatography using a 1–mm id column packed with 1.5-microm porous particles
    • Anspach, J. A., Maloney, T. D., and Colon, L. A. (2007) Ultrahigh-pressure liquid chromatography using a 1–mm id column packed with 1.5-microm porous particles. JSepSci 30, 1207–1213.
    • (2007) Jsepsci , vol.30 , pp. 1207-1213
    • Anspach, J.A.1    Maloney, T.D.2    Colon, L.A.3
  • 74
    • 33746263848 scopus 로고    scopus 로고
    • Automated ultra-high-pressure multidimensional protein identification technology (UHP-MudPIT) for improved peptide identification of proteomic samples
    • Motoyama, A., Venable, J. D., Ruse, C. I., and Yates, J. R., 3rd. (2006) Automated ultra-high-pressure multidimensional protein identification technology (UHP-MudPIT) for improved peptide identification of proteomic samples. Anal Chem 78, 5109–5118.
    • (2006) Anal Chem , vol.78 , pp. 5109-5118
    • Motoyama, A.1    Venable, J.D.2    Ruse, C.I.3    Yates, J.R.4
  • 75
    • 33847778786 scopus 로고    scopus 로고
    • Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry
    • Chi, A., Huttenhower, C., Geer, L. Y., Coon, J. J., Syka, J. E., Bai, D. L., et al. (2007) Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry. Proc Natl Acad Sci USA 104, 2193–2198.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2193-2198
    • Chi, A.1    Huttenhower, C.2    Geer, L.Y.3    Coon, J.J.4    Syka, J.E.5    Bai, D.L.6
  • 76
    • 36448962323 scopus 로고    scopus 로고
    • MudPIT: Multidimensional protein identification technology
    • Delahunty, C. M., and Yates, J. R., 3rd. (2007) MudPIT: multidimensional protein identification technology. Biotechniques 43, 563–567.
    • (2007) Biotechniques , vol.43 , pp. 563-567
    • Delahunty, C.M.1    Yates, J.R.2
  • 77
    • 41149121749 scopus 로고    scopus 로고
    • Comparison of the practical resolving power of one-and two-dimensional highperformance liquid chromatography analy sis of metabolomic samples
    • Stoll, D. R., Wang, X., and Carr, P. W. (2008) Comparison of the practical resolving power of one-and two-dimensional highperformance liquid chromatography analy sis of metabolomic samples. Anal Chem 80, 268–278.
    • (2008) Anal Chem , vol.80 , pp. 268-278
    • Stoll, D.R.1    Wang, X.2    Carr, P.W.3
  • 78
    • 29144446187 scopus 로고    scopus 로고
    • A double-vented tetraphasic continuous column approach to mudpit analysis on long capillary columns demonstrates superior proteomic coverage
    • Guzzetta, A. W., and Chien, A. S. (2005) A double-vented tetraphasic continuous column approach to mudpit analysis on long capillary columns demonstrates superior proteomic coverage. JProteomeRes4, 2412–2419.
    • (2005) Jproteomeres , vol.4 , pp. 2412-2419
    • Guzzetta, A.W.1    Chien, A.S.2
  • 80
    • 34249052872 scopus 로고    scopus 로고
    • Anion and cation mixed-bed ion exchange for enhanced multidimensional separations of peptides and phosphopeptides
    • Motoyama, A., Xu, T., Ruse, C. I., Wohlschlegel, J. A., and Yates, J. R., 3rd. (2007) Anion and cation mixed-bed ion exchange for enhanced multidimensional separations of peptides and phosphopeptides. Anal Chem 79, 3623–3634.
    • (2007) Anal Chem , vol.79 , pp. 3623-3634
    • Motoyama, A.1    Xu, T.2    Ruse, C.I.3    Wohlschlegel, J.A.4    Yates, J.R.5
  • 81
    • 51549102028 scopus 로고    scopus 로고
    • Comparison of twodimensional fractionation techniques for shotgun proteomics
    • Dowell, J. A., Frost, D. C., Zhang, J., and Li, L. (2008) Comparison of twodimensional fractionation techniques for shotgun proteomics. Anal Chem 80, 6715–6723.
    • (2008) Anal Chem , vol.80 , pp. 6715-6723
    • Dowell, J.A.1    Frost, D.C.2    Zhang, J.3    Li, L.4
  • 82
    • 65249137629 scopus 로고    scopus 로고
    • Global and site-specific quantitative phosphoproteomics: Principles and applications
    • Macek, B., Mann, M., and Olsen, J. V. (2009) Global and site-specific quantitative phosphoproteomics: principles and applications. Annu Rev Pharmacol Toxicol 49, 199–221.
    • (2009) Annu Rev Pharmacol Toxicol , vol.49 , pp. 199-221
    • Macek, B.1    Mann, M.2    Olsen, J.V.3
  • 83
    • 0036198435 scopus 로고    scopus 로고
    • Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae
    • Ficarro, S. B., McCleland, M. L., Stukenberg, P. T., Burke, D. J., Ross, M. M., Shabanowitz, J., et al. (2002) Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae. Nat Biotechnol 20, 301–305.
    • (2002) Nat Biotechnol , vol.20 , pp. 301-305
    • Ficarro, S.B.1    McCleland, M.L.2    Stukenberg, P.T.3    Burke, D.J.4    Ross, M.M.5    Shabanowitz, J.6
  • 84
    • 55249116044 scopus 로고    scopus 로고
    • Immobilized metal affinity chromatography revisited: PH/Acid control toward high selectivity in phosphoproteomics
    • Tsai, C. F., et al. (2008) Immobilized metal affinity chromatography revisited: pH/Acid control toward high selectivity in phosphoproteomics. JProteomeRes7, 4058–4069.
    • (2008) Jproteomeres , vol.7 , pp. 4058-4069
    • Tsai, C.F.1
  • 86
    • 34848886063 scopus 로고    scopus 로고
    • Immobilized zirconium ion affinity chromatography for specific enrichment of phosphopeptides in phosphoproteome analysis
    • Feng, S., et al. (2007) Immobilized zirconium ion affinity chromatography for specific enrichment of phosphopeptides in phosphoproteome analysis. MolCellProteomics6, 1656–1665.
    • (2007) Molcellproteomics , vol.6 , pp. 1656-1665
    • Feng, S.1
  • 87
    • 34249661724 scopus 로고    scopus 로고
    • Enrichment of multiphosphorylated peptides by immobilized metal affinity chromatography using Ga(III)-and Fe(III)complexes
    • Sykora, C., Hoffmann, R., and Hoffmann, P. (2007) Enrichment of multiphosphorylated peptides by immobilized metal affinity chromatography using Ga(III)-and Fe(III)complexes. Protein Pept Lett 14, 489–496.
    • (2007) Protein Pept Lett , vol.14 , pp. 489-496
    • Sykora, C.1    Hoffmann, R.2    Hoffmann, P.3
  • 88
    • 3242688830 scopus 로고    scopus 로고
    • Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2DNanoLC-ESI-MS/MS and titanium oxide precolumns
    • Pinkse, M. W., Uitto, P. M., Hilhorst, M. J., Ooms, B., and Heck, A. J. (2004) Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2DNanoLC-ESI-MS/MS and titanium oxide precolumns. Anal Chem 76, 3935–3943.
    • (2004) Anal Chem , vol.76 , pp. 3935-3943
    • Pinkse, M.W.1    Uitto, P.M.2    Hilhorst, M.J.3    Ooms, B.4    Heck, A.J.5
  • 89
    • 43449130945 scopus 로고    scopus 로고
    • Synapse proteomics: Current status and quantitative applications
    • Li, K. W., and Jimenez, C. R. (2008) Synapse proteomics: current status and quantitative applications. Expert Rev Proteomics 5, 353–360.
    • (2008) Expert Rev Proteomics , vol.5 , pp. 353-360
    • Li, K.W.1    Jimenez, C.R.2
  • 90
    • 34548446793 scopus 로고    scopus 로고
    • Proteomic analysis of protein complexes
    • Zhou, M., and Veenstra, T. D. (2007) Proteomic analysis of protein complexes. Proteomics 7, 2688–2697.
    • (2007) Proteomics , vol.7 , pp. 2688-2697
    • Zhou, M.1    Veenstra, T.D.2
  • 91
    • 44449124267 scopus 로고    scopus 로고
    • Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis
    • Cantin, G. T., et al. (2008) Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. JProteomeRes7, 1346–1351.
    • (2008) Jproteomeres7 , pp. 1346-1351
    • Cantin, G.T.1
  • 92
    • 40549130385 scopus 로고    scopus 로고
    • Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography
    • Han, G., et al. (2008) Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics 8, 1346–1361.
    • (2008) Proteomics , vol.8 , pp. 1346-1361
    • Han, G.1
  • 93
    • 43849091451 scopus 로고    scopus 로고
    • Hydrophilic interaction chromatography reduces the complexity of the phosphoproteome and improves global phosphopeptide isolation and detection
    • McNulty, D. E., and Annan, R. S. (2008) Hydrophilic interaction chromatography reduces the complexity of the phosphoproteome and improves global phosphopeptide isolation and detection. Mol Cell Proteomics 7, 971–980.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 971-980
    • McNulty, D.E.1    Annan, R.S.2
  • 94
    • 51649085326 scopus 로고    scopus 로고
    • Mass spectrometry and the emerging field of glycomics
    • Zaia, J. (2008) Mass spectrometry and the emerging field of glycomics. Chem Biol 15, 881–892.
    • (2008) Chem Biol , vol.15 , pp. 881-892
    • Zaia, J.1
  • 95
    • 67349272331 scopus 로고    scopus 로고
    • Glycoproteomics: Past, present and future
    • Tissot, B., et al. (2009) Glycoproteomics: past, present and future. FEBS Lett 583, 1728–1735.
    • (2009) FEBS Lett , vol.583 , pp. 1728-1735
    • Tissot, B.1
  • 96
    • 65549120632 scopus 로고    scopus 로고
    • Comparative glycoproteomics: Approaches and applications
    • Wei, X., and Li, L. (2009) Comparative glycoproteomics: approaches and applications. Brief Funct Genom Proteomic 8, 104–113.
    • (2009) Brief Funct Genom Proteomic , vol.8 , pp. 104-113
    • Wei, X.1    Li, L.2
  • 97
    • 70449970103 scopus 로고    scopus 로고
    • Lectin-based glycoproteomics to explore and analyze hepatocellular carcinoma-related glycoprotein markers
    • Dai, Z., Zhou, J., Qiu, S. J., Liu, Y. K., and Fan, J. (2009) Lectin-based glycoproteomics to explore and analyze hepatocellular carcinoma-related glycoprotein markers. Electrophoresis 30, 2957–2966.
    • (2009) Electrophoresis , vol.30 , pp. 2957-2966
    • Dai, Z.1    Zhou, J.2    Qiu, S.J.3    Liu, Y.K.4    Fan, J.5
  • 98
    • 64649101157 scopus 로고    scopus 로고
    • Microarrays in glycoproteomics research
    • Yue, T., and Haab, B. B. (2009) Microarrays in glycoproteomics research. Clin Lab Med 29, 15–29.
    • (2009) Clin Lab Med , vol.29 , pp. 15-29
    • Yue, T.1    Haab, B.B.2
  • 99
    • 66149083648 scopus 로고    scopus 로고
    • Enrichment strategies for glycopeptides
    • Ito, S., Hayama, K., and Hirabayashi, J. (2009) Enrichment strategies for glycopeptides. Methods Mol Biol 534, 195–203.
    • (2009) Methods Mol Biol , vol.534 , pp. 195-203
    • Ito, S.1    Hayama, K.2    Hirabayashi, J.3
  • 100
    • 85139016245 scopus 로고    scopus 로고
    • Atwood, J. A., 3rd., et al. (2006) Glycoproteomics of trypanosoma cruzi trypomastigotes using subcellular fractionation, lectin affinity, and stable isotope labeling. JProteome Res 5, 3376–3384.
    • Atwood, J. A., 3rd., et al. (2006) Glycoproteomics of trypanosoma cruzi trypomastigotes using subcellular fractionation, lectin affinity, and stable isotope labeling. JProteome Res 5, 3376–3384.
  • 101
    • 33847001297 scopus 로고    scopus 로고
    • Ultratrace LC/MS proteomic analysis using 10-microm-i.d. Porous layer open tubular poly(styrenedivinylbenzene) capillary columns
    • Yue, G., Luo, Q., Zhang, J., Wu, S. L., and Karger, B. L. (2007) Ultratrace LC/MS proteomic analysis using 10-microm-i.d. Porous layer open tubular poly(styrenedivinylbenzene) capillary columns. Anal Chem 79, 938–946.
    • (2007) Anal Chem , vol.79 , pp. 938-946
    • Yue, G.1    Luo, Q.2    Zhang, J.3    Wu, S.L.4    Karger, B.L.5
  • 102
    • 33749537286 scopus 로고    scopus 로고
    • Targeted glycoproteomics: Serial lectin affinity chromatography in the selection of O-glycosylation sites on proteins from the human blood proteome
    • Durham, M., and Regnier, F. E. (2006) Targeted glycoproteomics: serial lectin affinity chromatography in the selection of O-glycosylation sites on proteins from the human blood proteome. J Chromatogr 1132, 165–173.
    • (2006) J Chromatogr , vol.1132 , pp. 165-173
    • Durham, M.1    Regnier, F.E.2
  • 103
    • 56049090769 scopus 로고    scopus 로고
    • Acetylation of nonhistone proteins modulates cellular signalling at multiple levels
    • Spange, S., Wagner, T., Heinzel, T., and Kramer, O. H. H. (2009) Acetylation of nonhistone proteins modulates cellular signalling at multiple levels. Int J Biochem Cell Biol 4, 185–198.
    • (2009) Int J Biochem Cell Biol , vol.4 , pp. 185-198
    • Spange, S.1    Wagner, T.2    Heinzel, T.3    Kramer, O.H.H.4
  • 104
    • 77449116892 scopus 로고    scopus 로고
    • Acetylation goes global: The emergence of acetylation biology
    • Norris, K. L., Lee, J. Y., and Yao, T. P. (2009) Acetylation goes global: the emergence of acetylation biology. Sci Signal 2, 76–83.
    • (2009) Sci Signal , vol.2 , pp. 76-83
    • Norris, K.L.1    Lee, J.Y.2    Yao, T.P.3
  • 105
    • 70349971418 scopus 로고    scopus 로고
    • Introducing the acetylome
    • Smith, K. T., and Workman, J. L. (2009) Introducing the acetylome. Nat Biotechnol 27, 917–919.
    • (2009) Nat Biotechnol , vol.27 , pp. 917-919
    • Smith, K.T.1    Workman, J.L.2
  • 106
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and coregulates major cellular functions
    • Choudhary, C., et al. (2009) Lysine acetylation targets protein complexes and coregulates major cellular functions. Science 325, 834–840.
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1
  • 107
    • 77950428804 scopus 로고    scopus 로고
    • Reduced histone deacetylase 7 activity restores function to misfolded CFTR in cystic fibrosis
    • Hutt, D. M., et al. (2010) Reduced histone deacetylase 7 activity restores function to misfolded CFTR in cystic fibrosis. Nat Chem Biol 6, 25–33.
    • (2010) Nat Chem Biol , vol.6 , pp. 25-33
    • Hutt, D.M.1
  • 108
    • 68649100255 scopus 로고    scopus 로고
    • The proteostasis boundary in misfolding diseases of membrane traffic
    • Hutt, D. M., Powers, E. T., and Balch, W. E. (2009) The proteostasis boundary in misfolding diseases of membrane traffic. FEBS Lett 583, 2639–2646.
    • (2009) FEBS Lett , vol.583 , pp. 2639-2646
    • Hutt, D.M.1    Powers, E.T.2    Balch, W.E.3
  • 109
    • 0141502007 scopus 로고    scopus 로고
    • Shotgun proteomics: Integrating technologies to answer biological questions
    • McDonald, W. H., and Yates, J. R., 3rd. (2003) Shotgun proteomics: integrating technologies to answer biological questions. Curr Opin Mol Ther 5, 302–309.
    • (2003) Curr Opin Mol Ther , vol.5 , pp. 302-309
    • McDonald, W.H.1    Yates, J.R.2
  • 110
    • 33749615256 scopus 로고    scopus 로고
    • Chemistry. Mass spectrometry: Bottom-up or top-down?
    • Chait, B. T. (2006) Chemistry. Mass spectrometry: bottom-up or top-down? Science 314, 65–66.
    • (2006) Science , vol.314 , pp. 65-66
    • Chait, B.T.1
  • 111
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J., McCormack, A., and Yates, J. (1994) An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. JAm Soc Mass Spectrom 5, 976–989.
    • (1994) Jam Soc Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.1    McCormack, A.2    Yates, J.3
  • 112
    • 0042972838 scopus 로고    scopus 로고
    • A new algorithm for the evaluation of shotgun peptide sequencing in proteomics: Support vector machine classification of peptide MS/MS spectra and SEQUEST scores
    • Anderson, D. C., Li, W., Payan, D. G., and Noble, W. S. (2003) A new algorithm for the evaluation of shotgun peptide sequencing in proteomics: support vector machine classification of peptide MS/MS spectra and SEQUEST scores. J Proteome Res 2, 137–146.
    • (2003) J Proteome Res , vol.2 , pp. 137-146
    • Anderson, D.C.1    Li, W.2    Payan, D.G.3    Noble, W.S.4
  • 113
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller, A., Nesvizhskii, A. I., Kolker, E., and Aebersold, R. (2002) Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal Chem 74, 5383–5392.
    • (2002) Anal Chem , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 114
    • 18444391517 scopus 로고    scopus 로고
    • Shotgun identification of protein modifications from protein complexes and lens tissue
    • MacCoss, M. J., et al. (2002) Shotgun identification of protein modifications from protein complexes and lens tissue. Proc Natl Acad Sci USA 99, 7900–7905.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 7900-7905
    • Maccoss, M.J.1
  • 115
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., and Cottrell, J. S. (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551–3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 116
    • 0043064042 scopus 로고    scopus 로고
    • A hypergeometric probability model for protein identification and validation using tan dem mass spectral data and protein sequence databases
    • Sadygov, R., and Yates, J. R., 3rd. (2003) A hypergeometric probability model for protein identification and validation using tan dem mass spectral data and protein sequence databases. Anal Chem 75, 3792–3798.
    • (2003) Anal Chem , vol.75 , pp. 3792-3798
    • Sadygov, R.1    Yates, J.R.2
  • 117
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb, D. L., McDonald, H. W., and Yates, J. R., III (2002) DTASelect and contrast: tools for assembling and comparing protein identifications from shotgun proteomics. JProteome Res 1, 21–36.
    • (2002) Jproteome Res , vol.1 , pp. 21-36
    • Tabb, D.L.1    McDonald, H.W.2    Yates, J.R.3
  • 118
    • 20544436245 scopus 로고    scopus 로고
    • Proteomic analysis of isolated chlamydomonas centrioles reveals orthologs of ciliary-disease genes
    • Keller, L. C., Romijn, E. P., Zamora, I., Yates, J. R., 3rd., and Marshall, W. F. (2005) Proteomic analysis of isolated chlamydomonas centrioles reveals orthologs of ciliary-disease genes. Curr Biol 15, 1090–1098.
    • (2005) Curr Biol , vol.15 , pp. 1090-1098
    • Keller, L.C.1    Romijn, E.P.2    Zamora, I.3    Yates, J.R.4    Marshall, W.F.5
  • 119
    • 0034484286 scopus 로고    scopus 로고
    • Method for screening peptide fragment ion mass spectra prior to database searching
    • Moore, R. E., Young, M. K., and Lee, T. D. (2000) Method for screening peptide fragment ion mass spectra prior to database searching. J Am Soc Mass Spectrom 11, 422–426.
    • (2000) J am Soc Mass Spectrom , vol.11 , pp. 422-426
    • Moore, R.E.1    Young, M.K.2    Lee, T.D.3
  • 120
    • 43349083804 scopus 로고    scopus 로고
    • Using bibliospec for creating and searching tandem MS peptide libraries
    • Frewen, B., and MacCoss, M. J. (2007) Using bibliospec for creating and searching tandem MS peptide libraries. Curr Protoc Bioinformatics 13 13, 17.
    • (2007) Curr Protoc Bioinformatics , vol.13 , Issue.13 , pp. 17
    • Frewen, B.1    Maccoss, M.J.2
  • 121
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotopecoded affinity tags
    • Gygi, S. P., et al. (1999) Quantitative analysis of complex protein mixtures using isotopecoded affinity tags. Nat Biotechnol 17, 994–999.
    • (1999) Nat Biotechnol , vol.17 , pp. 994-999
    • Gygi, S.P.1
  • 122
    • 67651146342 scopus 로고    scopus 로고
    • The emerging role of ICP-MS in proteomic analysis
    • Bettmer, J., et al. (2009) The emerging role of ICP-MS in proteomic analysis. J Proteomics 72, 989–1005.
    • (2009) J Proteomics , vol.72 , pp. 989-1005
    • Bettmer, J.1
  • 123
    • 0030068923 scopus 로고    scopus 로고
    • Protease-catalyzed incorporation of 18O into peptide fragments and its application for protein sequencing by electrospray and matrix-assisted laser desorption/ionization mass spectrometry
    • Schnolzer, M., Jedrzejewski, P., and Lehmann, W. D. (1996) Protease-catalyzed incorporation of 18O into peptide fragments and its application for protein sequencing by electrospray and matrix-assisted laser desorption/ionization mass spectrometry. Electrophoresis 17, 945–953.
    • (1996) Electrophoresis , vol.17 , pp. 945-953
    • Schnolzer, M.1    Jedrzejewski, P.2    Lehmann, W.D.3
  • 124
    • 12444345515 scopus 로고    scopus 로고
    • Tandem mass tags: A novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS
    • Thompson, A., et al. (2003) Tandem mass tags: a novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS. Anal Chem 75, 1895–1904.
    • (2003) Anal Chem , vol.75 , pp. 1895-1904
    • Thompson, A.1
  • 125
    • 35848949043 scopus 로고    scopus 로고
    • Decoding protein modifications using topdown mass spectrometry
    • Siuti, N., and Kelleher, N. L. (2007) Decoding protein modifications using topdown mass spectrometry. Nat Methods 4, 817–821.
    • (2007) Nat Methods , vol.4 , pp. 817-821
    • Siuti, N.1    Kelleher, N.L.2
  • 126
    • 31044442964 scopus 로고    scopus 로고
    • Stepwise deamidation of ribonuclease A at five sites determined by top down mass spectrometry
    • Zabrouskov, V., et al. (2006) Stepwise deamidation of ribonuclease A at five sites determined by top down mass spectrometry. Biochemistry 45, 987–992.
    • (2006) Biochemistry , vol.45 , pp. 987-992
    • Zabrouskov, V.1
  • 127
    • 28444443740 scopus 로고    scopus 로고
    • Quantitative mass spectral evidence for the absence of circulating brain natriuretic peptide (BNP-32) in severe human heart failure
    • Hawkridge, A. M., et al. (2005) Quantitative mass spectral evidence for the absence of circulating brain natriuretic peptide (BNP-32) in severe human heart failure. Proc Natl Acad Sci USA 102, 17442–17447.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17442-17447
    • Hawkridge, A.M.1
  • 128
    • 60349108482 scopus 로고    scopus 로고
    • Toward a full characterization of the human 20 s proteasome subunits and their isoforms by a combination of proteomic approaches
    • Uttenweiler-Joseph, S., et al. (2008) Toward a full characterization of the human 20 s proteasome subunits and their isoforms by a combination of proteomic approaches. Methods Mol Biol 484, 111–130.
    • (2008) Methods Mol Biol , vol.484 , pp. 111-130
    • Uttenweiler-Joseph, S.1
  • 129
    • 33745700686 scopus 로고    scopus 로고
    • Quantitative analysis of modified proteins and their positional isomers by tandem mass spectrometry: Human histone H4
    • Pesavento, J. J., Mizzen, C. A., and Kelleher, N. L. (2006) Quantitative analysis of modified proteins and their positional isomers by tandem mass spectrometry: human histone H4. Anal Chem 78, 4271–4280.
    • (2006) Anal Chem , vol.78 , pp. 4271-4280
    • Pesavento, J.J.1    Mizzen, C.A.2    Kelleher, N.L.3
  • 130
    • 32444436985 scopus 로고    scopus 로고
    • Top-down approaches for measuring expression ratios of intact yeast proteins using Fourier transform mass spectrometry
    • Du, Y., Parks, B. A., Sohn, S., Kwast, K. E., and Kelleher, N. L. (2006) Top-down approaches for measuring expression ratios of intact yeast proteins using Fourier transform mass spectrometry. Anal Chem 78, 686–694.
    • (2006) Anal Chem , vol.78 , pp. 686-694
    • Du, Y.1    Parks, B.A.2    Sohn, S.3    Kwast, K.E.4    Kelleher, N.L.5
  • 131
    • 35448967750 scopus 로고    scopus 로고
    • Top-down quantitation and characterization of SILAC-labeled proteins
    • Waanders, L. F., Hanke, S., and Mann, M. (2007) Top-down quantitation and characterization of SILAC-labeled proteins. JAm Soc Mass Spectrom 18, 2058–2064.
    • (2007) Jam Soc Mass Spectrom , vol.18 , pp. 2058-2064
    • Waanders, L.F.1    Hanke, S.2    Mann, M.3
  • 132
    • 33847393182 scopus 로고    scopus 로고
    • Proteomic profiling of intact proteins using WAX-RPLC 2-D separations and FTICR mass spectrometry
    • Sharma, S., et al. (2007) Proteomic profiling of intact proteins using WAX-RPLC 2-D separations and FTICR mass spectrometry. J Proteome Res 6, 602–610.
    • (2007) J Proteome Res , vol.6 , pp. 602-610
    • Sharma, S.1
  • 133
    • 41149086763 scopus 로고    scopus 로고
    • Automated proteomics of E. coli via top-down electron-transfer dissociation mass spectrometry
    • Bunger, M. K., Cargile, B. J., Ngunjiri, A., Bundy, J. L., and Stephenson, J. L., Jr. (2008) Automated proteomics of E. coli via top-down electron-transfer dissociation mass spectrometry. Anal Chem 80, 1459–1467.
    • (2008) Anal Chem , vol.80 , pp. 1459-1467
    • Bunger, M.K.1    Cargile, B.J.2    Ngunjiri, A.3    Bundy, J.L.4    Stephenson, J.L.5
  • 134
    • 0041706161 scopus 로고    scopus 로고
    • Metabolic labelingofC.elegansandD.melanogasterfor quantitative proteomics
    • Krijgsveld, J., et al. (2003) Metabolic labelingofC.elegansandD.melanogasterfor quantitative proteomics. Nat Biotechnol 21, 927–931.
    • (2003) Nat Biotechnol , vol.21 , pp. 927-931
    • Krijgsveld, J.1
  • 135
    • 4444346217 scopus 로고    scopus 로고
    • Metabolic labeling of mammalian organisms with stable isotopes for quantitative proteomic analysis
    • Wu, C. C., MacCoss, M. J., Howell, K. E., Matthews, D. E., and Yates, J. R., 3rd. (2004) Metabolic labeling of mammalian organisms with stable isotopes for quantitative proteomic analysis. Anal Chem 76, 4951–4959.
    • (2004) Anal Chem , vol.76 , pp. 4951-4959
    • Wu, C.C.1    Maccoss, M.J.2    Howell, K.E.3    Matthews, D.E.4    Yates, J.R.5
  • 136
    • 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., 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
  • 137
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong, S. E., and 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.E.1    Mann, M.2
  • 138
    • 1942501808 scopus 로고    scopus 로고
    • A novel proteomic approach for specific identification of tyrosine kinase substrates using [13C]tyrosine
    • Ibarrola, N., Molina, H., Iwahori, A., and Pandey, A. (2004) A novel proteomic approach for specific identification of tyrosine kinase substrates using [13C]tyrosine. JBiol Chem 279, 15805–15813.
    • (2004) Jbiol Chem , vol.279 , pp. 15805-15813
    • Ibarrola, N.1    Molina, H.2    Iwahori, A.3    Pandey, A.4
  • 139
    • 28644448658 scopus 로고    scopus 로고
    • Stable isotope labeling of arabidopsis thaliana cells and quantitative proteomics by mass spectrometry
    • Gruhler, A., Schulze, W. X., Matthiesen, R., Mann, M., and Jensen, O. N. (2005) Stable isotope labeling of arabidopsis thaliana cells and quantitative proteomics by mass spectrometry. MolCellProteomics4, 1697–1709.
    • (2005) Molcellproteomics , vol.4 , pp. 1697-1709
    • Gruhler, A.1    Schulze, W.X.2    Matthiesen, R.3    Mann, M.4    Jensen, O.N.5
  • 140
    • 15944377809 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway
    • Gruhler, A., et al. (2005) Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway. MolCellProteomics 4, 310–327.
    • (2005) Molcellproteomics , vol.4 , pp. 310-327
    • Gruhler, A.1
  • 142
    • 47549099572 scopus 로고    scopus 로고
    • SILAC mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function
    • Kruger, M., et al. (2008) SILAC mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function. Cell 134, 353–364.
    • (2008) Cell , vol.134 , pp. 353-364
    • Kruger, M.1
  • 143
    • 0037326081 scopus 로고    scopus 로고
    • Mass spectrometric-based approaches in quantitative proteomics
    • Ong, S. E., Foster, L. J., and Mann, M. (2003) Mass spectrometric-based approaches in quantitative proteomics. Methods 29, 124–130.
    • (2003) Methods , vol.29 , pp. 124-130
    • Ong, S.E.1    Foster, L.J.2    Mann, M.3
  • 144
    • 52649167339 scopus 로고    scopus 로고
    • Prevention of amino acid conversion in SILAC experiments with embryonic stem cells
    • Bendall, S. C., et al. (2008) Prevention of amino acid conversion in SILAC experiments with embryonic stem cells. Mol Cell Proteomics 7, 1587–1597.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 1587-1597
    • Bendall, S.C.1
  • 145
    • 34548356772 scopus 로고    scopus 로고
    • An experimental correction for arginine-to-proline conversion artifacts in SILAC-based quantitative proteomics
    • Van Hoof, D., et al. (2007) An experimental correction for arginine-to-proline conversion artifacts in SILAC-based quantitative proteomics. Nat Methods 4, 677–678.
    • (2007) Nat Methods , vol.4 , pp. 677-678
    • van Hoof, D.1
  • 146
    • 41549117597 scopus 로고    scopus 로고
    • A quantitative analysis software tool for mass spectrometry-based proteomics
    • Park, S. K., Venable, J. D., Xu, T., and Yates, J. R., 3rd. (2008) A quantitative analysis software tool for mass spectrometry-based proteomics. Nat Methods 5, 319–322.
    • (2008) Nat Methods , vol.5 , pp. 319-322
    • Park, S.K.1    Venable, J.D.2    Xu, T.3    Yates, J.R.4
  • 147
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotopecoded affinity tags
    • Gygi, S. P., et al. (1999) Quantitative analysis of complex protein mixtures using isotopecoded affinity tags. Nat Biotechnol 17, 994–999.
    • (1999) Nat Biotechnol , vol.17 , pp. 994-999
    • Gygi, S.P.1
  • 148
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross, P. L., et al. (2004) Multiplexed protein quantitation in saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. MolCellProteomics3, 1154–1169.
    • (2004) Molcellproteomics3 , pp. 1154-1169
    • Ross, P.L.1
  • 149
    • 0037795741 scopus 로고    scopus 로고
    • Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
    • Gerber, S. A., Rush, J., Stemman, O., Kirschner, M. W., and Gygi, S. P. (2003) Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc Natl Acad Sci USA 100, 6940–6945.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6940-6945
    • Gerber, S.A.1    Rush, J.2    Stemman, O.3    Kirschner, M.W.4    Gygi, S.P.5
  • 150
    • 23144442824 scopus 로고    scopus 로고
    • Multiplexed absolute quantification in proteomics using artificial QCAT proteins of concatenated signature peptides
    • Beynon, R. J., Doherty, M. K., Pratt, J. M., and Gaskell, S. J. (2005) Multiplexed absolute quantification in proteomics using artificial QCAT proteins of concatenated signature peptides. Nat Methods 2, 587–589.
    • (2005) Nat Methods , vol.2 , pp. 587-589
    • Beynon, R.J.1    Doherty, M.K.2    Pratt, J.M.3    Gaskell, S.J.4
  • 151
    • 44449162195 scopus 로고    scopus 로고
    • Absolute SILAC for accurate quantitation of proteins in complex mixtures down to the attomole level
    • Hanke, S., Besir, H., Oesterhelt, D., and Mann, M. (2008) Absolute SILAC for accurate quantitation of proteins in complex mixtures down to the attomole level. JProteome Res 7, 1118–1130.
    • (2008) Jproteome Res , vol.7 , pp. 1118-1130
    • Hanke, S.1    Besir, H.2    Oesterhelt, D.3    Mann, M.4
  • 152
    • 35648942133 scopus 로고    scopus 로고
    • 8-plex quantitation of changes in cerebrospinal fluid protein expression in subjects undergoing intravenous immunoglobulin treatment for Alzheimer’s disease
    • Choe, L., et al. (2007) 8-plex quantitation of changes in cerebrospinal fluid protein expression in subjects undergoing intravenous immunoglobulin treatment for Alzheimer’s disease. Proteomics 7, 3651–3660.
    • (2007) Proteomics , vol.7 , pp. 3651-3660
    • Choe, L.1
  • 153
    • 85139062683 scopus 로고    scopus 로고
    • Improving the fundamentals of MSn on 2D linear ion traps: New ion activation and isolation techniques
    • Schwartz, J., Syka, J., and Quarmby, S. (2005) Improving the fundamentals of MSn on 2D linear ion traps: new ion activation and isolation techniques. Am Soc Mass Spectrom 54, 67–76.
    • (2005) Am Soc Mass Spectrom , vol.54 , pp. 67-76
    • Schwartz, J.1    Syka, J.2    Quarmby, S.3
  • 154
    • 36348987990 scopus 로고    scopus 로고
    • iTRAQ reagentbased quantitative proteomic analysis on a linear ion trap mass spectrometer
    • Griffin, T. J., et al. (2007) iTRAQ reagentbased quantitative proteomic analysis on a linear ion trap mass spectrometer. JProteome Res 6, 4200–4209.
    • (2007) Jproteome Res , vol.6 , pp. 4200-4209
    • Griffin, T.J.1
  • 155
    • 50849096388 scopus 로고    scopus 로고
    • Peptide and protein quantification using iTRAQ with electron transfer dissociation
    • Phanstiel, D., Zhang, Y., Marto, J. A., and Coon, J. J. (2008) Peptide and protein quantification using iTRAQ with electron transfer dissociation. J Am Soc Mass Spectrom 19, 1255–1262.
    • (2008) J am Soc Mass Spectrom , vol.19 , pp. 1255-1262
    • Phanstiel, D.1    Zhang, Y.2    Marto, J.A.3    Coon, J.J.4
  • 156
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • Liu, H., Sadygov, R. G., and Yates, J. R., 3rd. (2004) A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal Chem 76, 4193–4201.
    • (2004) Anal Chem , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates, J.R.3
  • 157
    • 26444506068 scopus 로고    scopus 로고
    • Correlation of relative abundance ratios derived from peptide ion chromatograms and spectrum counting for quantitative proteomic analysis using stable isotope labeling
    • Zybailov, B., Coleman, M. K., Florens, L., and Washburn, M. P. (2005) Correlation of relative abundance ratios derived from peptide ion chromatograms and spectrum counting for quantitative proteomic analysis using stable isotope labeling. Anal Chem 77, 6218–6224.
    • (2005) Anal Chem , vol.77 , pp. 6218-6224
    • Zybailov, B.1    Coleman, M.K.2    Florens, L.3    Washburn, M.P.4
  • 158
    • 38649095599 scopus 로고    scopus 로고
    • An assessment of software solutions for the analysis of mass spectrometry based quantitative proteomics data
    • Mueller, L. N., Brusniak, M. Y., Mani, D. R., and Aebersold, R. (2008) An assessment of software solutions for the analysis of mass spectrometry based quantitative proteomics data. JProteomeRes7, 51–61.
    • (2008) Jproteomeres , vol.7 , pp. 51-61
    • Mueller, L.N.1    Brusniak, M.Y.2    Mani, D.R.3    Aebersold, R.4
  • 159
    • 33646555756 scopus 로고    scopus 로고
    • Enhanced analysis of metastatic prostate cancer using stable isotopes and high mass accuracy instrumentation
    • Everley, P. A., et al. (2006) Enhanced analysis of metastatic prostate cancer using stable isotopes and high mass accuracy instrumentation. JProteomeRes5, 1224–1231.
    • (2006) Jproteomeres5 , pp. 1224-1231
    • Everley, P.A.1


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