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Volumn 6, Issue 1, 2009, Pages 32-42

Recent developments in mass spectrometry analysis of phosphoproteomes

Author keywords

Enrichment of phosphopeptides; Mass spectrometry; Phosphopeptides; Phosphoproteins; Phosphoproteomics; Phosphorylation; Quantitative phosphoproteomics; Shotgun proteomics

Indexed keywords

EUKARYOTA;

EID: 64749087403     PISSN: 15701646     EISSN: None     Source Type: Journal    
DOI: 10.2174/157016409787847394     Document Type: Article
Times cited : (7)

References (99)
  • 1
    • 29544453143 scopus 로고    scopus 로고
    • Development of a simplified, economical polyacrylamide gel staining protocol for phosphoproteins
    • Agrawal, G.K. and Thelen, J.J. (2005). Development of a simplified, economical polyacrylamide gel staining protocol for phosphoproteins. Proteomics 5: 4684-8.
    • (2005) Proteomics , vol.5 , pp. 4684-4688
    • Agrawal, G.K.1    Thelen, J.J.2
  • 2
    • 0035253691 scopus 로고    scopus 로고
    • A multidimensional electrospray MS-based approach to phosphopeptide mapping
    • Annan, R.S., Huddleston, M.J., Verma, R., Deshaies, R.J. and Carr, S.A. (2001). A multidimensional electrospray MS-based approach to phosphopeptide mapping. Anal. Chem. 73: 393-04.
    • (2001) Anal. Chem , vol.73 , pp. 393-404
    • Annan, R.S.1    Huddleston, M.J.2    Verma, R.3    Deshaies, R.J.4    Carr, S.A.5
  • 3
    • 50049110046 scopus 로고    scopus 로고
    • Characterization of the human cerebrospinal fluid phosphoproteome by titanium oxide affinity chromatography and mass spectrometry
    • Bahl J.M.C., Jensen, S.S., Larsen, M.R. and Heegaard, N.H.H. (2008). Characterization of the human cerebrospinal fluid phosphoproteome by titanium oxide affinity chromatography and mass spectrometry. Anal. Chem. 80: 1308-16.
    • (2008) Anal. Chem , vol.80 , pp. 1308-1316
    • Bahl, J.M.C.1    Jensen, S.S.2    Larsen, M.R.3    Heegaard, N.H.H.4
  • 5
    • 0036636552 scopus 로고    scopus 로고
    • A novel precursor ion discovery method on a hybrid quadrupole orthogonal acceleration time-of-flight (Q-TOF) mass spectrometer for studying protein phosphorylation
    • Bateman, R.H., Carruthers, R., Hoyes, J.B., Jones, C.J., Langridge, I., Miller, A. and Vissers, J.P.C. (2002). A novel precursor ion discovery method on a hybrid quadrupole orthogonal acceleration time-of-flight (Q-TOF) mass spectrometer for studying protein phosphorylation, J. Am. Soc. Mass Spectrom. 13: 792-3.
    • (2002) J. Am. Soc. Mass Spectrom , vol.13 , pp. 792-793
    • Bateman, R.H.1    Carruthers, R.2    Hoyes, J.B.3    Jones, C.J.4    Langridge, I.5    Miller, A.6    Vissers, J.P.C.7
  • 7
    • 0037106398 scopus 로고    scopus 로고
    • Identification and relative quantitation of protein mixtures by enzymatic digestion followed by capillary reversed-phase liquid chromatography-tandem mass spectrometry
    • Bondarenko, P., Chelius, D. and Shaler, T. (2002). Identification and relative quantitation of protein mixtures by enzymatic digestion followed by capillary reversed-phase liquid chromatography-tandem mass spectrometry. Anal. Chem. 74: 4741-9.
    • (2002) Anal. Chem , vol.74 , pp. 4741-4749
    • Bondarenko, P.1    Chelius, D.2    Shaler, T.3
  • 8
    • 48349147103 scopus 로고    scopus 로고
    • Topdown identification and characterization of biomolecules by mass spectrometry
    • Breuker, K., Jin, M., Han, X., Jiang, H. and McLafferty, F.W. (2008). Topdown identification and characterization of biomolecules by mass spectrometry. J. Am. Soc. Mass Spectrom. 19: 1045-53.
    • (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
  • 9
    • 44449124267 scopus 로고    scopus 로고
    • Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis
    • Cantin, G.T., Yi, W., Lu, B.W., Park, S.K., Xu, T., Lee, J.D. and Yates, J.R. (2008). Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J. Proteome Res. 7: 1346-51.
    • (2008) J. Proteome Res , vol.7 , pp. 1346-1351
    • Cantin, G.T.1    Yi, W.2    Lu, B.W.3    Park, S.K.4    Xu, T.5    Lee, J.D.6    Yates, J.R.7
  • 10
    • 0030218817 scopus 로고    scopus 로고
    • Selective detection and sequencing of phosphopeptides at the femtomole level by mass spectrometry
    • Carr, S.A., Huddleston, M.J. and Annan, R.S. (1996). Selective detection and sequencing of phosphopeptides at the femtomole level by mass spectrometry. Anal. Biochem. 239: 180-92.
    • (1996) Anal. Biochem , vol.239 , pp. 180-192
    • Carr, S.A.1    Huddleston, M.J.2    Annan, R.S.3
  • 11
    • 24944442458 scopus 로고    scopus 로고
    • Fe3O4/TiO2 core/shell nanoparticles as affinity probes for the analysis of phosphopeptides using TiO2 surfaceassisted laser desorption/ionization mass spectrometry
    • Chen, C.T. and Chen, Y.C. (2005). Fe3O4/TiO2 core/shell nanoparticles as affinity probes for the analysis of phosphopeptides using TiO2 surfaceassisted laser desorption/ionization mass spectrometry. Anal. Chem. 77: 5912-9.
    • (2005) Anal. Chem , vol.77 , pp. 5912-5919
    • Chen, C.T.1    Chen, Y.C.2
  • 12
    • 34548392335 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation on a proteome-scale
    • Collins, M.O., Yu, L. and Choudhary, J.S. (2007). Analysis of protein phosphorylation on a proteome-scale. Proteomics 7: 2751-68.
    • (2007) Proteomics , vol.7 , pp. 2751-2768
    • Collins, M.O.1    Yu, L.2    Choudhary, J.S.3
  • 14
    • 7244221587 scopus 로고    scopus 로고
    • Infrared multiphoton dissociation (IRMPD) and collisionally activated dissociation of peptides in a quadrupole ion trap with selective IRMPD of phosphopeptides
    • Crowe, M.C. and Brodbelt, J.S. (2004). Infrared multiphoton dissociation (IRMPD) and collisionally activated dissociation of peptides in a quadrupole ion trap with selective IRMPD of phosphopeptides. J. Am. Soc. Mass Spectrom. 15: 1581-92.
    • (2004) J. Am. Soc. Mass Spectrom , vol.15 , pp. 1581-1592
    • Crowe, M.C.1    Brodbelt, J.S.2
  • 18
    • 64749109310 scopus 로고    scopus 로고
    • Mass Spectrometry, de novo sequencing of peptides
    • John Wiley & Sons, Inc, Hoboken, NJ
    • Dass, C. (2009b). Mass Spectrometry, de novo sequencing of peptides. In Wiley Encyclopedia of Chemical Biology, Online, 2009. John Wiley & Sons, Inc., Hoboken, NJ.
    • (2009) Wiley Encyclopedia of Chemical Biology, Online
    • Dass, C.1
  • 19
    • 0028857483 scopus 로고
    • Amino acid sequence determination of phosphoenkephalins using liquid secondary ionization mass spectrometry
    • Dass, C. and Mahalakshmi, P. (1995). Amino acid sequence determination of phosphoenkephalins using liquid secondary ionization mass spectrometry. Rapid Commun. Mass Spectrom. 9: 1148-54.
    • (1995) Rapid Commun. Mass Spectrom , vol.9 , pp. 1148-1154
    • Dass, C.1    Mahalakshmi, P.2
  • 20
    • 0032237775 scopus 로고    scopus 로고
    • Fragmentation of phosphopeptides in an ion trap mass spectrometer
    • DeGnore, J.P. and Qin, J. (1998). Fragmentation of phosphopeptides in an ion trap mass spectrometer. J. Am. Soc. Mass Spectrom. 9: 1175-88.
    • (1998) J. Am. Soc. Mass Spectrom , vol.9 , pp. 1175-1188
    • DeGnore, J.P.1    Qin, J.2
  • 21
    • 34848886063 scopus 로고    scopus 로고
    • Immobilized zirconium ion affinity chromatography for specific enrichment of phosphopeptides in phosphoproteome analysis
    • Feng, S., Ye, M.I., Zhou, H.J., Jiang, X.G., Jiang, X.N., Zou, H.F. and Gong, B. (2007). Immobilized zirconium ion affinity chromatography for specific enrichment of phosphopeptides in phosphoproteome analysis. Mol. Cell Proteomics 6: 1656-65.
    • (2007) Mol. Cell Proteomics , vol.6 , pp. 1656-1665
    • Feng, S.1    Ye, M.I.2    Zhou, H.J.3    Jiang, X.G.4    Jiang, X.N.5    Zou, H.F.6    Gong, B.7
  • 23
    • 0035878151 scopus 로고    scopus 로고
    • Selective, sensitive, and rapid phosphopeptide identification in enzymatic digests using ESI-FTICR- MS with infrared multiphoton dissociation
    • Flora, J.W. and Muddiman, D.C. (2001). Selective, sensitive, and rapid phosphopeptide identification in enzymatic digests using ESI-FTICR- MS with infrared multiphoton dissociation. Anal. Chem. 73: 3305-11.
    • (2001) Anal. Chem , vol.73 , pp. 3305-3311
    • Flora, J.W.1    Muddiman, D.C.2
  • 24
    • 0023219635 scopus 로고
    • Liquid secondary ionization mass spectrometric characterization of 2 synthetic phosphotyrosine-containing peptides
    • Gibson, B.W., Falick, A.M., Burlingame, A.L., Nadasdi, L., Nguyen, A.C. and Kenyon, G.L. (1987). Liquid secondary ionization mass spectrometric characterization of 2 synthetic phosphotyrosine-containing peptides, J. Am. Chem. Soc. 109: 5343-8.
    • (1987) J. Am. Chem. Soc , vol.109 , pp. 5343-5348
    • Gibson, B.W.1    Falick, A.M.2    Burlingame, A.L.3    Nadasdi, L.4    Nguyen, A.C.5    Kenyon, G.L.6
  • 25
    • 0035356565 scopus 로고    scopus 로고
    • Phosphoprotein isotope-coded affinity tag approach for isolating and quantitating phosphopeptides in proteome-wide analyses
    • Goshe, M.B., Conrads, T.P., Panisko, E.A., Angell, N.H., Veenstra, T.D. and Smith, R.D. (2001). Phosphoprotein isotope-coded affinity tag approach for isolating and quantitating phosphopeptides in proteome-wide analyses. Anal. Chem. 73: 2578-86.
    • (2001) Anal. Chem , vol.73 , pp. 2578-2586
    • Goshe, M.B.1    Conrads, T.P.2    Panisko, E.A.3    Angell, N.H.4    Veenstra, T.D.5    Smith, R.D.6
  • 26
    • 0036652968 scopus 로고    scopus 로고
    • A mass spectrometrybased proteomic approach for identification of serine/threoninephosphorylated proteins by enrichment with phospho-specific antibodies - Identification of a novel protein, Frigg, as a protein kinase A substrate
    • Gronborg, M., Kristiansen, T.Z., Stensballe, A., Andersen, J.S., Ohara, O., Mann, M., Jensen, O.N. and Pandey, A. (2002). A mass spectrometrybased proteomic approach for identification of serine/threoninephosphorylated proteins by enrichment with phospho-specific antibodies - Identification of a novel protein, Frigg, as a protein kinase A substrate. Mol. Cell Proteomics 1: 517-27.
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 517-527
    • Gronborg, M.1    Kristiansen, T.Z.2    Stensballe, A.3    Andersen, J.S.4    Ohara, O.5    Mann, M.6    Jensen, O.N.7    Pandey, A.8
  • 27
    • 27844510036 scopus 로고    scopus 로고
    • Manipulating the fragmentation patterns of phosphopeptides via gas-phase boron derivatization: Determining phosphorylation sites in peptides with multiple serines
    • Gronert, S., Li, K.H. and Horiuchi, M. (2005). Manipulating the fragmentation patterns of phosphopeptides via gas-phase boron derivatization: Determining phosphorylation sites in peptides with multiple serines. J. Am. Soc. Mass Spectrom. 16: 1905-14.
    • (2005) J. Am. Soc. Mass Spectrom , vol.16 , pp. 1905-1914
    • Gronert, S.1    Li, K.H.2    Horiuchi, M.3
  • 28
    • 39749091667 scopus 로고    scopus 로고
    • Taking aim at shotgun phosphoproteomics
    • Hoffert, J.D. and Knepper, M.A. (2008). Taking aim at shotgun phosphoproteomics. Anal. Biochem. 375: 1-10.
    • (2008) Anal. Biochem , vol.375 , pp. 1-10
    • Hoffert, J.D.1    Knepper, M.A.2
  • 29
    • 33646485094 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics of vasopressin-sensitive renal cells: Regulation of aquaporin-2 phosphorylation at two sites
    • Hoffert, J.D., Pisitkun, T., Wang, G.H., Shen, R.F. and Knepper, M.A. (2006). Quantitative phosphoproteomics of vasopressin-sensitive renal cells: Regulation of aquaporin-2 phosphorylation at two sites. Proc. Natl. Acad. Sci. USA 103: 7159-64.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7159-7164
    • Hoffert, J.D.1    Pisitkun, T.2    Wang, G.H.3    Shen, R.F.4    Knepper, M.A.5
  • 30
    • 34948851348 scopus 로고    scopus 로고
    • An automated platform for analysis of phosphoproteomic datasets: Application to kidney collecting duct phosphoproteins
    • Hoffert, J.D., Wang, G.H., Pisitkun, T., Shen, R.F. and Knepper, M.A. (2007). An automated platform for analysis of phosphoproteomic datasets: Application to kidney collecting duct phosphoproteins. J. Proteome Res. 6: 3501-8.
    • (2007) J. Proteome Res , vol.6 , pp. 3501-3508
    • Hoffert, J.D.1    Wang, G.H.2    Pisitkun, T.3    Shen, R.F.4    Knepper, M.A.5
  • 31
    • 0000279508 scopus 로고
    • Selective detection of phosphopeptides in complex-mixtures by electrospray liquid-chormatography mass-spectrometry
    • Huddleston, M.J., Annan, R.S., Bean, M.F. and Carr, S.A. (1993). Selective detection of phosphopeptides in complex-mixtures by electrospray liquid-chormatography mass-spectrometry. J. Am. Soc. Mass Spectrom. 4: 710-7.
    • (1993) J. Am. Soc. Mass Spectrom , vol.4 , pp. 710-717
    • Huddleston, M.J.1    Annan, R.S.2    Bean, M.F.3    Carr, S.A.4
  • 32
    • 42749086358 scopus 로고    scopus 로고
    • Novel reversible biotinylated probe for the selective enrichment of phosphorylated peptides from complex mixtures
    • Jalili, P.R. and Ball, H.L. (2008). Novel reversible biotinylated probe for the selective enrichment of phosphorylated peptides from complex mixtures. J. Am. Soc. Mass Spectrom. 19: 741-50.
    • (2008) J. Am. Soc. Mass Spectrom , vol.19 , pp. 741-750
    • Jalili, P.R.1    Ball, H.L.2
  • 33
    • 4043050834 scopus 로고    scopus 로고
    • Proteome analysis in the bovine liquid adrenal medulla using chromatography with tandem mass spectrometry
    • Jalili, P.R. and Dass, C. (2004). Proteome analysis in the bovine liquid adrenal medulla using chromatography with tandem mass spectrometry. Rapid Commun. Mass Spectrom. 18: 1877-84.
    • (2004) Rapid Commun. Mass Spectrom , vol.18 , pp. 1877-1884
    • Jalili, P.R.1    Dass, C.2
  • 34
    • 2642520417 scopus 로고    scopus 로고
    • Top-down proteomics
    • Kelleher, N.L. (2004). Top-down proteomics. Anal. Chem. 76: 196A-203A.
    • (2004) Anal. Chem , vol.76
    • Kelleher, N.L.1
  • 35
    • 48349085761 scopus 로고    scopus 로고
    • Towards liquid chromatography time-scale peptide sequencing and characterization of post-translational modifications in the negative ion mode using electron detachment dissociation tandem mass spectrometry
    • Kjeldsen, F., Horning, O.B., Jensen, S.S., Giessing, A.M.B. and Jensen, O.N. (2008). Towards liquid chromatography time-scale peptide sequencing and characterization of post-translational modifications in the negative ion mode using electron detachment dissociation tandem mass spectrometry. J. Am. Soc. Mass Spectrom. 19: 1156-62.
    • (2008) J. Am. Soc. Mass Spectrom , vol.19 , pp. 1156-1162
    • Kjeldsen, F.1    Horning, O.B.2    Jensen, S.S.3    Giessing, A.M.B.4    Jensen, O.N.5
  • 36
    • 9144254626 scopus 로고    scopus 로고
    • Derivatization of phosphorylated peptides with S- and N- nucleophiles for enhanced ionization efficiency in matrix-assisted laser desorption/ ionization mass spectrometry
    • Klemm, C., Schroder, S., Gluckmann, M., Beyermann, M. and Krause, E. (2004). Derivatization of phosphorylated peptides with S- and N- nucleophiles for enhanced ionization efficiency in matrix-assisted laser desorption/ ionization mass spectrometry. Rapid Commun. Mass Spectrom. 18: 2697-705.
    • (2004) Rapid Commun. Mass Spectrom , vol.18 , pp. 2697-2705
    • Klemm, C.1    Schroder, S.2    Gluckmann, M.3    Beyermann, M.4    Krause, E.5
  • 38
  • 40
    • 33645217942 scopus 로고    scopus 로고
    • Selective zirconium dioxide-based enrichment of phosphorylated peptides for mass spectrometric analysis
    • Kweon, H.K. and Hakansson, K. (2006). Selective zirconium dioxide-based enrichment of phosphorylated peptides for mass spectrometric analysis. Anal. Chem. 78: 1743-9.
    • (2006) Anal. Chem , vol.78 , pp. 1743-1749
    • Kweon, H.K.1    Hakansson, K.2
  • 41
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns
    • Larsen, M.R., Thingholm, T.E., Jensen, O.N., Roepstorff, P. and Jorgensen, T.J.D. (2005). Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol. Cell Proteomics 4: 873-86.
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 873-886
    • Larsen, M.R.1    Thingholm, T.E.2    Jensen, O.N.3    Roepstorff, P.4    Jorgensen, T.J.D.5
  • 42
    • 0033562834 scopus 로고    scopus 로고
    • Iron(lll)-immobilized metal ion affinity chromatography and mass spectrometry for the purification and characterization of synthetic phosphopeptides
    • Li, S.H. and Dass, C. (1999). Iron(lll)-immobilized metal ion affinity chromatography and mass spectrometry for the purification and characterization of synthetic phosphopeptides. Anal. Biochem. 270: 9-14.
    • (1999) Anal. Biochem , vol.270 , pp. 9-14
    • Li, S.H.1    Dass, C.2
  • 43
    • 53249097734 scopus 로고    scopus 로고
    • Quantitative proteomics in the study phosphoserine mediated-signal transduction pathway
    • Liang, X., Hajivandi, M., Predki, P. and Pope, M.R. (2008). Quantitative proteomics in the study phosphoserine mediated-signal transduction pathway. Curr. Proteomics 5: 146-56.
    • (2008) Curr. Proteomics , vol.5 , pp. 146-156
    • Liang, X.1    Hajivandi, M.2    Predki, P.3    Pope, M.R.4
  • 44
    • 33745209192 scopus 로고    scopus 로고
    • Phosphopeptides enrichment using online two-dimensional strong cation exchange followed by reversedphase liquid chromatography/mass spectrometry
    • Lim, K.B. and Kassel, D.B. (2006). Phosphopeptides enrichment using online two-dimensional strong cation exchange followed by reversedphase liquid chromatography/mass spectrometry. Anal. Biochem. 354: 213-9.
    • (2006) Anal. Biochem , vol.354 , pp. 213-219
    • Lim, K.B.1    Kassel, D.B.2
  • 45
    • 33847374660 scopus 로고    scopus 로고
    • Rapid enrichment of phosphopeptides from tryptic digests of proteins using iron oxide nanocomposites of magnetic particles coated with zirconia as the concentrating probes
    • Lo, C.Y., Chen, W.Y., Chen, C.T. and Chen, Y.C. (2007). Rapid enrichment of phosphopeptides from tryptic digests of proteins using iron oxide nanocomposites of magnetic particles coated with zirconia as the concentrating probes. J. Proteome Res. 6: 887-93.
    • (2007) J. Proteome Res , vol.6 , pp. 887-893
    • Lo, C.Y.1    Chen, W.Y.2    Chen, C.T.3    Chen, Y.C.4
  • 46
    • 33847194634 scopus 로고    scopus 로고
    • Automatic validation of phosphopeptide identifications from tandem mass spectra
    • Lu, B.W., Ruse, C., Xu, T., Park, S.K. and Yates, J. (2007). Automatic validation of phosphopeptide identifications from tandem mass spectra. Anal. Chem. 79: 1301-10.
    • (2007) Anal. Chem , vol.79 , pp. 1301-1310
    • Lu, B.W.1    Ruse, C.2    Xu, T.3    Park, S.K.4    Yates, J.5
  • 48
    • 0642371059 scopus 로고    scopus 로고
    • Differential analysis of phosphorylated proteins in resting and thrombin-stimulated human platelets
    • Marcus, K., Moebius, J. and Meyer, H.E. (2003). Differential analysis of phosphorylated proteins in resting and thrombin-stimulated human platelets. Anal. Bioanal. Chem. 376: 973-93.
    • (2003) Anal. Bioanal. Chem , vol.376 , pp. 973-993
    • Marcus, K.1    Moebius, J.2    Meyer, H.E.3
  • 49
    • 0348014634 scopus 로고    scopus 로고
    • Improved beta-elimination-based affinity purification strategy for enrichment of phosphopeptides
    • McLachlin, D.T. and Chait, B.T. (2003). Improved beta-elimination-based affinity purification strategy for enrichment of phosphopeptides. Anal. Chem. 75: 6826-36.
    • (2003) Anal. Chem , vol.75 , pp. 6826-6836
    • McLachlin, D.T.1    Chait, B.T.2
  • 50
    • 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: 971-80.
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 971-980
    • McNulty, D.E.1    Annan, R.S.2
  • 51
    • 33847782587 scopus 로고    scopus 로고
    • Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry
    • Molina, H., Horn, D.M., Tang, N., Mathivanan, S. and Pandey, A. (2007). Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc. Natl. Acad. Sci. USA 104: 2199-204.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2199-2204
    • Molina, H.1    Horn, D.M.2    Tang, N.3    Mathivanan, S.4    Pandey, A.5
  • 52
    • 54749158155 scopus 로고    scopus 로고
    • Multidimensional LC separations in shotgun proteomics
    • Motoyama, A. and Yates, J.R. (2008). Multidimensional LC separations in shotgun proteomics. Anal. Chem. 80: 7187-93.
    • (2008) Anal. Chem , vol.80 , pp. 7187-7193
    • Motoyama, A.1    Yates, J.R.2
  • 53
    • 0036112145 scopus 로고    scopus 로고
    • Fragmentation of phosphopeptides by atmospheric pressure MALDI and ESI/ion trap mass spectrometry
    • Moyer, S.C., Cotter, R.J. and Woods, A.S. (2002). Fragmentation of phosphopeptides by atmospheric pressure MALDI and ESI/ion trap mass spectrometry. J. Am. Soc. Mass Spectrom. 13: 274-83.
    • (2002) J. Am. Soc. Mass Spectrom , vol.13 , pp. 274-283
    • Moyer, S.C.1    Cotter, R.J.2    Woods, A.S.3
  • 54
    • 41149098111 scopus 로고    scopus 로고
    • Absolute and site-specific quantification of protein phosphorylation using integrated elemental and molecular mass spectrometry: Its potential to assess phosphopeptide enrichment procedures
    • Navaza, A.P., Encinar, J.R., Carrascal, M., Abian, J. and Sanz-Medel, A. (2008). Absolute and site-specific quantification of protein phosphorylation using integrated elemental and molecular mass spectrometry: Its potential to assess phosphopeptide enrichment procedures. Anal. Chem. 80: 1777-87.
    • (2008) Anal. Chem , vol.80 , pp. 1777-1787
    • Navaza, A.P.1    Encinar, J.R.2    Carrascal, M.3    Abian, J.4    Sanz-Medel, A.5
  • 55
    • 0035067251 scopus 로고    scopus 로고
    • Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome
    • Oda, Y., Nagasu, T. and Chait, B.T. (2001). Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome. Nat. Biotechnol. 19: 379-82.
    • (2001) Nat. Biotechnol , vol.19 , pp. 379-382
    • Oda, Y.1    Nagasu, T.2    Chait, B.T.3
  • 56
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen, J.V., Blagoev, B., Gnad, F., Macek, B., Kumar, C., Mortensen, P. and Mann, M. (2006). Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127: 635-48.
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 57
    • 0036583926 scopus 로고    scopus 로고
    • Stable-isotope Labeling by Amino Acids in Cell Culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S.E., Blagoev, B., Kratchmarova, I., Kristensen, D.B., Steen, H., Pandey, A. and Mann, M. (2002). Stable-isotope Labeling by Amino Acids in Cell Culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell Proteomics 1: 376-86.
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 58
    • 0034602654 scopus 로고    scopus 로고
    • Analysis of receptor signaling pathways by mass spectrometry: Identification of Vav-2 as a substrate of the epidermal and platelet-derived growth factor receptors
    • Pandey, A., Podtelejnikov, A.V., Blagoev, B., Bustelo, X.R., Mann, M. and Lodish, H.F. (2000). Analysis of receptor signaling pathways by mass spectrometry: Identification of Vav-2 as a substrate of the epidermal and platelet-derived growth factor receptors. Proc. Natl. Acad. Sci. USA 97: 179-84.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 179-184
    • Pandey, A.1    Podtelejnikov, A.V.2    Blagoev, B.3    Bustelo, X.R.4    Mann, M.5    Lodish, H.F.6
  • 59
    • 52049110575 scopus 로고    scopus 로고
    • Advances in the analysis of protein phosphorylation
    • Paradela, A. and Albar, J.P. (2008). Advances in the analysis of protein phosphorylation. J. Proteome Res. 7: 1809-18.
    • (2008) J. Proteome Res , vol.7 , pp. 1809-1818
    • Paradela, A.1    Albar, J.P.2
  • 60
    • 3242688830 scopus 로고    scopus 로고
    • Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-nanoLC-ESI-MS/MS and titanium oxide precolumns
    • Pinkse, M.W.H., Uitto, P.M., Hilhorst, M.J., Ooms, B. and Heck, A.J.R. (2004). Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-nanoLC-ESI-MS/MS and titanium oxide precolumns. Anal. Chem. 76: 3935-43.
    • (2004) Anal. Chem , vol.76 , pp. 3935-3943
    • Pinkse, M.W.H.1    Uitto, P.M.2    Hilhorst, M.J.3    Ooms, B.4    Heck, A.J.R.5
  • 61
    • 27744563093 scopus 로고    scopus 로고
    • State-of-the-art in phosphoproteomics
    • Reinders, J. and Sickmann, A. (2005). State-of-the-art in phosphoproteomics. Proteomics 5: 4052-61.
    • (2005) Proteomics , vol.5 , pp. 4052-4061
    • Reinders, J.1    Sickmann, A.2
  • 63
    • 27844600289 scopus 로고    scopus 로고
    • Phosphoproteomics by mass spectrometry and classical protein chemistry approaches
    • Salih, E. (2005). Phosphoproteomics by mass spectrometry and classical protein chemistry approaches. Mass Spectrom. Rev. 24: 828-46.
    • (2005) Mass Spectrom. Rev , vol.24 , pp. 828-846
    • Salih, E.1
  • 64
    • 3042575877 scopus 로고    scopus 로고
    • Titania as a chemo-affinity support for the column-switching HPLC analysis of phosphopeptides: Application to the characterization of phosphorylation sites in proteins by combination with protease digestion and electrospray ionization mass Spectrometry
    • Sano, A. and Nakamura, H. (2004). Titania as a chemo-affinity support for the column-switching HPLC analysis of phosphopeptides: Application to the characterization of phosphorylation sites in proteins by combination with protease digestion and electrospray ionization mass Spectrometry. Anal. Sci. 20: 861-4.
    • (2004) Anal. Sci , vol.20 , pp. 861-864
    • Sano, A.1    Nakamura, H.2
  • 65
    • 0035863653 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation by a combination of elastase digestion and neutral loss tandem mass spectrometry
    • Schlosser, A., Pipkorn, R., Bossemeyer, D. and Lehmann, W.D. (2001). Analysis of protein phosphorylation by a combination of elastase digestion and neutral loss tandem mass spectrometry. Anal. Chem. 73: 170-6.
    • (2001) Anal. Chem , vol.73 , pp. 170-176
    • Schlosser, A.1    Pipkorn, R.2    Bossemeyer, D.3    Lehmann, W.D.4
  • 66
    • 33749332751 scopus 로고    scopus 로고
    • Temporal dynamics of tyrosine phosphorylation in insulin signaling
    • Schmelzle, K., Kane, S., Gridley, S., Lienhard, G.E. and White, F.M. (2006). Temporal dynamics of tyrosine phosphorylation in insulin signaling. Diabetes 55: 2171-9.
    • (2006) Diabetes , vol.55 , pp. 2171-2179
    • Schmelzle, K.1    Kane, S.2    Gridley, S.3    Lienhard, G.E.4    White, F.M.5
  • 67
    • 4444305698 scopus 로고    scopus 로고
    • Characterization of dynamic and steady-state protein phosphorylation using a fluorescent phosphoprotein gel stain and mass spectrometry
    • Schulenberg, B., Goodman, T.N., Aggeler, R., Capaldi, R.A. and Patton, W.F. (2004). Characterization of dynamic and steady-state protein phosphorylation using a fluorescent phosphoprotein gel stain and mass spectrometry. Electrophoresis 25: 2526-32.
    • (2004) Electrophoresis , vol.25 , pp. 2526-2532
    • Schulenberg, B.1    Goodman, T.N.2    Aggeler, R.3    Capaldi, R.A.4    Patton, W.F.5
  • 68
    • 0035173029 scopus 로고    scopus 로고
    • Phosphopeptide/phosphoprotein mapping by electron capture dissociation mass spectrometry
    • Shi, S.D.H., Hemling, M.E., Carr, S.A., Horn, D.M., Lindh, I. and McLafferty, F.W. (2001). Phosphopeptide/phosphoprotein mapping by electron capture dissociation mass spectrometry. Anal. Chem. 73: 19-22.
    • (2001) Anal. Chem , vol.73 , pp. 19-22
    • Shi, S.D.H.1    Hemling, M.E.2    Carr, S.A.3    Horn, D.M.4    Lindh, I.5    McLafferty, F.W.6
  • 69
    • 23144451918 scopus 로고    scopus 로고
    • Quantitative detection of phosphoproteins by combination of two-dimensional difference gel electrophoresis and phosphospecific fluorescent staining
    • Stasyk, T., Morandell, S., Bakry, R., Feuerstein, I., Huck, C.W., Stecher, G., Bonn, G.K. and Huber, L.A. (2005). Quantitative detection of phosphoproteins by combination of two-dimensional difference gel electrophoresis and phosphospecific fluorescent staining. Electrophoresis 26: 2850-4.
    • (2005) Electrophoresis , vol.26 , pp. 2850-2854
    • Stasyk, T.1    Morandell, S.2    Bakry, R.3    Feuerstein, I.4    Huck, C.W.5    Stecher, G.6    Bonn, G.K.7    Huber, L.A.8
  • 70
    • 0035298820 scopus 로고    scopus 로고
    • Detection of tyrosine phosphorylated peptides by precursor ion scanning quadrupole TOF mass spectrometry in positive ion mode
    • Steen, H., Kuster, B., Fernandez, M., Pandey, A. and Mann, M. (2001). Detection of tyrosine phosphorylated peptides by precursor ion scanning quadrupole TOF mass spectrometry in positive ion mode. Anal. Chem. 73: 1440-8.
    • (2001) Anal. Chem , vol.73 , pp. 1440-1448
    • Steen, H.1    Kuster, B.2    Fernandez, M.3    Pandey, A.4    Mann, M.5
  • 71
    • 0036674813 scopus 로고    scopus 로고
    • A new derivatization strategy for the analysis of phosphopeptides by precursor ion scanning in positive ion mode
    • Steen, H. and Mann, M. (2002). A new derivatization strategy for the analysis of phosphopeptides by precursor ion scanning in positive ion mode. J. Am. Soc. Mass Spectrom. 13: 996-1003.
    • (2002) J. Am. Soc. Mass Spectrom , vol.13 , pp. 996-1003
    • Steen, H.1    Mann, M.2
  • 74
    • 27144470222 scopus 로고    scopus 로고
    • Sun, X.S., Chiu, J.F. and He, Q.Y. (2005). Application of immobilized metal affinity chromatography in proteomics. Expert Rev. Proteomics 2: 649-57.
    • Sun, X.S., Chiu, J.F. and He, Q.Y. (2005). Application of immobilized metal affinity chromatography in proteomics. Expert Rev. Proteomics 2: 649-57.
  • 75
  • 76
    • 0345600791 scopus 로고    scopus 로고
    • GutenTag: High-throughput sequence tagging via an empirically derived fragmentation model
    • Tabb, D.L., Saraf, A. and Yates, J.R. (2003). GutenTag: High-throughput sequence tagging via an empirically derived fragmentation model. Anal. Chem. 75: 6415-21.
    • (2003) Anal. Chem , vol.75 , pp. 6415-6421
    • Tabb, D.L.1    Saraf, A.2    Yates, J.R.3
  • 77
    • 34547228179 scopus 로고    scopus 로고
    • Specific capture of phosphopeptides on MALDI-TOF-MS targets modified by magnetic affinity nanoparticles
    • Tan. F., Zhang, Y.J., Wang, J.L., Wei, J.Y., Qin, P.B., Cai, Y. and Qian, X.H. (2007). Specific capture of phosphopeptides on MALDI-TOF-MS targets modified by magnetic affinity nanoparticles. Rapid Commun. Mass Spectrom. 21: 2407-14.
    • (2007) Rapid Commun. Mass Spectrom , vol.21 , pp. 2407-2414
    • Tan, F.1    Zhang, Y.J.2    Wang, J.L.3    Wei, J.Y.4    Qin, P.B.5    Cai, Y.6    Qian, X.H.7
  • 78
    • 27544511899 scopus 로고    scopus 로고
    • InsPecT: Identification of posttransiationally modified peptides from tandem mass spectra
    • Tanner, S., Shu, H.J., Frank, A., Wang, L.C., Zandi, E., Mumby, M., Pevzner, P.A. and Bafna, V. (2005). InsPecT: Identification of posttransiationally modified peptides from tandem mass spectra. Anal. Chem. 77: 4626-39.
    • (2005) Anal. Chem , vol.77 , pp. 4626-4639
    • Tanner, S.1    Shu, H.J.2    Frank, A.3    Wang, L.C.4    Zandi, E.5    Mumby, M.6    Pevzner, P.A.7    Bafna, V.8
  • 79
    • 23144441172 scopus 로고    scopus 로고
    • Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry
    • Tao, W.A., Wollscheid, B., O'Brien, R., Eng, J.K., Li, X.J., Bodenmiller, B., Watts, J.D., Hood, L., et al. (2005). Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry. Nat. Methods 2: 591-8.
    • (2005) Nat. Methods , vol.2 , pp. 591-598
    • Tao, W.A.1    Wollscheid, B.2    O'Brien, R.3    Eng, J.K.4    Li, X.J.5    Bodenmiller, B.6    Watts, J.D.7    Hood, L.8
  • 80
    • 0041474713 scopus 로고    scopus 로고
    • Web and database software for identification of intact proteins using "Top Down" mass spectrometry
    • Taylor, G.K., Kim, Y.B., Forbes, A.J., Meng, F.Y., McCarthy, R. and Kelleher, N.L. (2003). Web and database software for identification of intact proteins using "Top Down" mass spectrometry. Anal. Chem. 75: 4081-6.
    • (2003) Anal. Chem , vol.75 , pp. 4081-4086
    • Taylor, G.K.1    Kim, Y.B.2    Forbes, A.J.3    Meng, F.Y.4    McCarthy, R.5    Kelleher, N.L.6
  • 81
    • 42249086071 scopus 로고    scopus 로고
    • Integrated analytical strategies for the study of phosphorylation and glycosylation in proteins
    • Temporini, C., Callerli, E., Massolini, G. and Caccialanza, G. (2008). Integrated analytical strategies for the study of phosphorylation and glycosylation in proteins. Mass Spectrom. Rev. 27: 207-36.
    • (2008) Mass Spectrom. Rev , vol.27 , pp. 207-236
    • Temporini, C.1    Callerli, E.2    Massolini, G.3    Caccialanza, G.4
  • 83
    • 24044553566 scopus 로고    scopus 로고
    • protein phosphorylation with high sensitivity. Mol. Cell Proteomics 4: 1134-44.
    • protein phosphorylation with high sensitivity. Mol. Cell Proteomics 4: 1134-44.
  • 84
    • 32144450291 scopus 로고    scopus 로고
    • Phosphopeptide detection using automated online IMAC-capillary LC-ESI- MS/MS
    • Wang, J.L., Zhang, Y.J., Jiang, H., Cai, Y. and Qian, X.H. (2006). Phosphopeptide detection using automated online IMAC-capillary LC-ESI- MS/MS. Proteomics 6: 404-11.
    • (2006) Proteomics , vol.6 , pp. 404-411
    • Wang, J.L.1    Zhang, Y.J.2    Jiang, H.3    Cai, Y.4    Qian, X.H.5
  • 85
    • 41549135248 scopus 로고    scopus 로고
    • Highly efficient enrichment of phosphopeptides by magnetic nanoparticles coated with zirconium phosphonate for phosphoproteome analysis
    • Wei, J.Y., Zhang, Y.J., Wang, J.L., Tan, F., Liu, J.F., Cai, Y. and Qian, X.H. (2008). Highly efficient enrichment of phosphopeptides by magnetic nanoparticles coated with zirconium phosphonate for phosphoproteome analysis. Rapid Commun. Mass Spectrom. 22: 1069-80.
    • (2008) Rapid Commun. Mass Spectrom , vol.22 , pp. 1069-1080
    • Wei, J.Y.1    Zhang, Y.J.2    Wang, J.L.3    Tan, F.4    Liu, J.F.5    Cai, Y.6    Qian, X.H.7
  • 86
    • 33644674733 scopus 로고    scopus 로고
    • Automated identification and quantification of protein phosphorylation sites by LC/MS on a hybrid triple quadrupole linear ion trap mass spectrometer
    • Williamson, B.L., Marchese, J. and Morrice, N.A. (2006). Automated identification and quantification of protein phosphorylation sites by LC/MS on a hybrid triple quadrupole linear ion trap mass spectrometer. Mol. Cell Proteomics 5: 337-46.
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 337-346
    • Williamson, B.L.1    Marchese, J.2    Morrice, N.A.3
  • 87
    • 0030033198 scopus 로고    scopus 로고
    • Parent ion scans of unseparated peptide mixtures
    • Wilm, M., Neubauer, G. and Mann, M. (1996). Parent ion scans of unseparated peptide mixtures. Anal. Chem. 68: 527-33.
    • (1996) Anal. Chem , vol.68 , pp. 527-533
    • Wilm, M.1    Neubauer, G.2    Mann, M.3
  • 88
    • 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. and White, F.M. (2007). Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks. Proc. Natl. Acad. Sci. USA 104: 5860-5.
    • (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
  • 89
    • 28444487185 scopus 로고    scopus 로고
    • Enrichment of phosphorylated proteins and peptides from complex mixtures using metal oxide/hydroxide affinity chromatography (MOAC)
    • Wolschin, F., Wienkoop, S. and Weckwerth, W. (2005a). Enrichment of phosphorylated proteins and peptides from complex mixtures using metal oxide/hydroxide affinity chromatography (MOAC). Proteomics 5: 4389-97.
    • (2005) Proteomics , vol.5 , pp. 4389-4397
    • Wolschin, F.1    Wienkoop, S.2    Weckwerth, W.3
  • 90
    • 29144521559 scopus 로고    scopus 로고
    • An integrated strategy for identification and relative quantification of sitespecific protein phosphorylation using liquid chromatography coupled to MS2/MS3
    • Wolschin, F., Lehmann, U., Glinski, M. and Weckwerth, W. (2005b). An integrated strategy for identification and relative quantification of sitespecific protein phosphorylation using liquid chromatography coupled to MS2/MS3. Rapid Commun. Mass Spectrom. 19: 3626-32.
    • (2005) Rapid Commun. Mass Spectrom , vol.19 , pp. 3626-3632
    • Wolschin, F.1    Lehmann, U.2    Glinski, M.3    Weckwerth, W.4
  • 91
    • 84890499160 scopus 로고    scopus 로고
    • Combining metaloxide affinity chromatography (MOAC) and selective mass spectrometry for robust identification of in vivo phosphorylation sites
    • Wolschin, F. and Weckwerth, W. (2005). Combining metaloxide affinity chromatography (MOAC) and selective mass spectrometry for robust identification of in vivo phosphorylation sites. Plant Methods 1: 9.
    • (2005) Plant Methods , vol.1 , pp. 9
    • Wolschin, F.1    Weckwerth, W.2
  • 92
    • 51649095905 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of human brain by calcium phosphate precipitation and mass spectrometry
    • Xia, Q.W., Cheng, D.M., Duong, D.M., Gearing, M., Lah, J.J., Levey, A.I. and Peng, J.M. (2008). Phosphoproteomic analysis of human brain by calcium phosphate precipitation and mass spectrometry. J. Proteome Res. 7: 2845-51.
    • (2008) J. Proteome Res , vol.7 , pp. 2845-2851
    • Xia, Q.W.1    Cheng, D.M.2    Duong, D.M.3    Gearing, M.4    Lah, J.J.5    Levey, A.I.6    Peng, J.M.7
  • 94
    • 33845382689 scopus 로고    scopus 로고
    • Phosphoproteomics of human platelets: A quest for novel activation pathways
    • Zahedi, R.P., Begonja, A.J., Gambaryan, S. and Sickmann, A. (2006). Phosphoproteomics of human platelets: A quest for novel activation pathways. Biochim. Biophys. Acta 1764: 1963-76.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 1963-1976
    • Zahedi, R.P.1    Begonja, A.J.2    Gambaryan, S.3    Sickmann, A.4
  • 95
    • 0024322517 scopus 로고
    • Threonine phosphorylation is associated with mitosis in hela-cells
    • Zhao, J.Y., Kuang, J., Adlakha, R.C. and Rao, P.N. (1989). Threonine phosphorylation is associated with mitosis in hela-cells. FEBS Lett. 249: 389-95.
    • (1989) FEBS Lett , vol.249 , pp. 389-395
    • Zhao, J.Y.1    Kuang, J.2    Adlakha, R.C.3    Rao, P.N.4
  • 96
    • 48349098876 scopus 로고    scopus 로고
    • The highly selective capture of phosphopeptides by zirconium phosphonate-modified magnetic nanoparticles for phosphoproteome analysis
    • Zhao, L., Wu, R., Han, G., Zhou, H., Ren, L., Tian, R.I. and Zou, H. (2008). The highly selective capture of phosphopeptides by zirconium phosphonate-modified magnetic nanoparticles for phosphoproteome analysis. J. Am. Soc. Mass Spectrom. 19: 1176-86.
    • (2008) J. Am. Soc. Mass Spectrom , vol.19 , pp. 1176-1186
    • Zhao, L.1    Wu, R.2    Han, G.3    Zhou, H.4    Ren, L.5    Tian, R.I.6    Zou, H.7
  • 97
    • 34447498653 scopus 로고    scopus 로고
    • Highly specific enrichment of phosphopeptides by zirconium dioxide nanoparticles for phosphoproteome analysis
    • Zhou, H.J., Tian, R., Ye, M., Xu, S.Y., Feng, S., Pan, C., Jiang, X., Li, X., et al. (2007). Highly specific enrichment of phosphopeptides by zirconium dioxide nanoparticles for phosphoproteome analysis. Electrophoresis 28: 2201-15.
    • (2007) Electrophoresis , vol.28 , pp. 2201-2215
    • Zhou, H.J.1    Tian, R.2    Ye, M.3    Xu, S.Y.4    Feng, S.5    Pan, C.6    Jiang, X.7    Li, X.8
  • 98
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • Zhou, H.L., Watts, J.D. and Aebersold, R. (2001). A systematic approach to the analysis of protein phosphorylation. Nat. Biotechnol. 19: 375-8.
    • (2001) Nat. Biotechnol , vol.19 , pp. 375-378
    • Zhou, H.L.1    Watts, J.D.2    Aebersold, R.3
  • 99
    • 0033024981 scopus 로고    scopus 로고
    • Analysis of phosphoenkephalins by combined high performance liquid chromatography and electrospray ionization mass spectrometry
    • Zhu, X.R. and Dass, C. (1999). Analysis of phosphoenkephalins by combined high performance liquid chromatography and electrospray ionization mass spectrometry. J. Liquid Chromatogr. Rel. Technol. 22: 1635-47.
    • (1999) J. Liquid Chromatogr. Rel. Technol , vol.22 , pp. 1635-1647
    • Zhu, X.R.1    Dass, C.2


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