메뉴 건너뛰기




Volumn 407, Issue 1, 2010, Pages 19-33

Large-scale phosphoproteome of human whole saliva using disulfide-thiol interchange covalent chromatography and mass spectrometry

Author keywords

Biomarkers; Covalent chromatography; Diagnostics; Mass spectrometry; Oral; Phosphoproteomics; Saliva

Indexed keywords

AMINO ACIDS; BARIUM COMPOUNDS; DIAGNOSIS; ELECTROSPRAY IONIZATION; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; PEPTIDES; PLASMA DIAGNOSTICS; SODIUM HYDROXIDE; SULFUR COMPOUNDS;

EID: 77956874230     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2010.07.012     Document Type: Article
Times cited : (47)

References (64)
  • 1
    • 14344257981 scopus 로고    scopus 로고
    • Toward defining the human parotid gland salivary proteome and peptidome: identification and characterization using 2D SDS-PAGE, ultrafiltration, HPLC, and mass spectrometry,
    • Hardt M., Thomas L.R., Dixon S.E., Newport G., Agabian N., Prakobphol A., Hall S.C., Witkowska H.E., Fisher S.J. Toward defining the human parotid gland salivary proteome and peptidome: identification and characterization using 2D SDS-PAGE, ultrafiltration, HPLC, and mass spectrometry,. Biochemistry 2005, 4:2885-2899.
    • (2005) Biochemistry , vol.4 , pp. 2885-2899
    • Hardt, M.1    Thomas, L.R.2    Dixon, S.E.3    Newport, G.4    Agabian, N.5    Prakobphol, A.6    Hall, S.C.7    Witkowska, H.E.8    Fisher, S.J.9
  • 2
    • 17844368916 scopus 로고    scopus 로고
    • Large-scale identification of proteins in human salivary proteome by liquid chromatography/mass spectrometry and two-dimensional gel electrophoresis-mass spectrometry
    • Hu S., Xie Y., Ramachandran P., Ogorzalek Loo R.R., Li Y., Loo J.A., Wong D.T. Large-scale identification of proteins in human salivary proteome by liquid chromatography/mass spectrometry and two-dimensional gel electrophoresis-mass spectrometry. Proteomics 2005, 5:1714-1728.
    • (2005) Proteomics , vol.5 , pp. 1714-1728
    • Hu, S.1    Xie, Y.2    Ramachandran, P.3    Ogorzalek Loo, R.R.4    Li, Y.5    Loo, J.A.6    Wong, D.T.7
  • 4
    • 33748530287 scopus 로고    scopus 로고
    • Towards a simple, saliva-based test for the detection of oral cancer: oral fluid (saliva), which is the mirror of the body, is a perfect medium to be explored for health and disease surveillance
    • Wong D.T. Towards a simple, saliva-based test for the detection of oral cancer: oral fluid (saliva), which is the mirror of the body, is a perfect medium to be explored for health and disease surveillance. J. Calif. Dent. Assoc. 2006, 34:283-285.
    • (2006) J. Calif. Dent. Assoc. , vol.34 , pp. 283-285
    • Wong, D.T.1
  • 6
    • 51349132896 scopus 로고    scopus 로고
    • The proteomes of human parotid and submandibular/sublingual gland salivas collected as the ductal secretions
    • Denny P., Hagen F.K., Hardt M., Liao L., Yan W., Arellanno M., et al. The proteomes of human parotid and submandibular/sublingual gland salivas collected as the ductal secretions. J. Proteome Res. 2008, 7:1994-2006.
    • (2008) J. Proteome Res. , vol.7 , pp. 1994-2006
    • Denny, P.1    Hagen, F.K.2    Hardt, M.3    Liao, L.4    Yan, W.5    Arellanno, M.6
  • 7
    • 0027277098 scopus 로고
    • On target with a new mechanism for the regulation of protein phosphorylation
    • Hubbard M.J., Cohen P. On target with a new mechanism for the regulation of protein phosphorylation. Trends Biochem. Sci. 1993, 18:172-177.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 172-177
    • Hubbard, M.J.1    Cohen, P.2
  • 8
    • 24944553549 scopus 로고    scopus 로고
    • MAP kinase pathways
    • Qi M., Elion E.A. MAP kinase pathways. J. Cell Sci. 2005, 118:3569-3572.
    • (2005) J. Cell Sci. , vol.118 , pp. 3569-3572
    • Qi, M.1    Elion, E.A.2
  • 9
    • 0034614490 scopus 로고    scopus 로고
    • Signaling: 2000 and beyond
    • Hunter T. Signaling: 2000 and beyond. Cell 2000, 100:113-127.
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 10
    • 0025912228 scopus 로고
    • Epithelial secretion of vinblastine by human intestinal adenocarcinoma cell (HCT-8 and T84) layers expressing P-glycoprotein
    • Hunter J., Hirst B.H., Simmons N.L. Epithelial secretion of vinblastine by human intestinal adenocarcinoma cell (HCT-8 and T84) layers expressing P-glycoprotein. Br. J. Cancer 1991, 64:437-444.
    • (1991) Br. J. Cancer , vol.64 , pp. 437-444
    • Hunter, J.1    Hirst, B.H.2    Simmons, N.L.3
  • 12
    • 0036606717 scopus 로고    scopus 로고
    • Natural variation in the extent of phosphorylation of bone phosphoproteins as a function of in vivo new bone formation induced by demineralized bone matrix in soft tissue and bony environments
    • Salih E., Wang J., Mah J., Fluckiger R. Natural variation in the extent of phosphorylation of bone phosphoproteins as a function of in vivo new bone formation induced by demineralized bone matrix in soft tissue and bony environments. Biochem. J. 2002, 364:465-474.
    • (2002) Biochem. J. , vol.364 , pp. 465-474
    • Salih, E.1    Wang, J.2    Mah, J.3    Fluckiger, R.4
  • 13
    • 0029950732 scopus 로고    scopus 로고
    • Phosphorylation of purified bovine bone sialoprotein and osteopontin by protein kinases
    • Salih E., Zhou H.Y., Glimcher M.J. Phosphorylation of purified bovine bone sialoprotein and osteopontin by protein kinases. J. Biol. Chem. 1996, 271:16897-16905.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16897-16905
    • Salih, E.1    Zhou, H.Y.2    Glimcher, M.J.3
  • 14
    • 2442461058 scopus 로고    scopus 로고
    • Complete topographical distribution of both the in vivo and in vitro phosphorylation sites of bone sialoprotein and their biological implications
    • Salih E., Fluckiger R. Complete topographical distribution of both the in vivo and in vitro phosphorylation sites of bone sialoprotein and their biological implications. J. Biol. Chem. 2004, 279:19808-19815.
    • (2004) J. Biol. Chem. , vol.279 , pp. 19808-19815
    • Salih, E.1    Fluckiger, R.2
  • 15
    • 0015086726 scopus 로고
    • Purification and partial characterization of four proteins from human parotid saliva
    • Bennick A., Connell G.E. Purification and partial characterization of four proteins from human parotid saliva. Biochem. J. 1971, 123:455-464.
    • (1971) Biochem. J. , vol.123 , pp. 455-464
    • Bennick, A.1    Connell, G.E.2
  • 16
    • 0015150991 scopus 로고
    • Proline-rich proteins from human parotid saliva: I. Isolation and partial characterization
    • Oppenheim F.G., Hay D.I., Franzblau C. Proline-rich proteins from human parotid saliva: I. Isolation and partial characterization. Biochemistry 1971, 10:4233-4238.
    • (1971) Biochemistry , vol.10 , pp. 4233-4238
    • Oppenheim, F.G.1    Hay, D.I.2    Franzblau, C.3
  • 18
    • 0023888810 scopus 로고
    • Histatins, a novel family of histidine-rich proteins in human parotid secretion: isolation, characterization, primary structure, and fungistatic effects on Candida albicans
    • Oppenheim F.G., Xu T., McMillian F.M., Levitz S.M., Diamond R.D., Offner G.D., Troxler R.F. Histatins, a novel family of histidine-rich proteins in human parotid secretion: isolation, characterization, primary structure, and fungistatic effects on Candida albicans. J. Biol. Chem. 1988, 263:472-477.
    • (1988) J. Biol. Chem. , vol.263 , pp. 472-477
    • Oppenheim, F.G.1    Xu, T.2    McMillian, F.M.3    Levitz, S.M.4    Diamond, R.D.5    Offner, G.D.6    Troxler, R.F.7
  • 19
    • 0022623229 scopus 로고
    • The primary structure and functional characterization of the neutral histidine-rich polypeptide from human parotid secretion
    • Oppenheim F.G., Yang Y.C., Diamond R.D., Hyslop D., Offner G.D., Troxler R.F. The primary structure and functional characterization of the neutral histidine-rich polypeptide from human parotid secretion. J. Biol. Chem. 1986, 261:1177-1182.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1177-1182
    • Oppenheim, F.G.1    Yang, Y.C.2    Diamond, R.D.3    Hyslop, D.4    Offner, G.D.5    Troxler, R.F.6
  • 20
    • 0017348985 scopus 로고
    • Complete covalent structure of statherin, a tyrosine-rich acidic peptide which inhibits calcium phosphate precipitation from human parotid saliva
    • Schlesinger D.H., Hay D.I. Complete covalent structure of statherin, a tyrosine-rich acidic peptide which inhibits calcium phosphate precipitation from human parotid saliva. J. Biol. Chem. 1977, 252:1689-1695.
    • (1977) J. Biol. Chem. , vol.252 , pp. 1689-1695
    • Schlesinger, D.H.1    Hay, D.I.2
  • 21
    • 0023096430 scopus 로고
    • Inhibition of calcium phosphate precipitation by human salivary acidic proline-rich proteins: structure-activity relationships
    • Hay D.I., Carlson E.R., Schluckebier S.K., Moreno E.C., Schlesinger D.H. Inhibition of calcium phosphate precipitation by human salivary acidic proline-rich proteins: structure-activity relationships. Calcif. Tissue Int. 1987, 40:126-132.
    • (1987) Calcif. Tissue Int. , vol.40 , pp. 126-132
    • Hay, D.I.1    Carlson, E.R.2    Schluckebier, S.K.3    Moreno, E.C.4    Schlesinger, D.H.5
  • 22
    • 0026719753 scopus 로고
    • Inhibition of calcium phosphate precipitation by human salivary statherin: structure-activity relationships
    • Schwartz S.S., Hay D.I., Schluckebier S.K. Inhibition of calcium phosphate precipitation by human salivary statherin: structure-activity relationships. Calcif. Tissue Int. 1992, 50:511-517.
    • (1992) Calcif. Tissue Int. , vol.50 , pp. 511-517
    • Schwartz, S.S.1    Hay, D.I.2    Schluckebier, S.K.3
  • 23
    • 0035241690 scopus 로고    scopus 로고
    • Mass spectrometry in proteomics
    • Aebersold R., Goodlett D.R. Mass spectrometry in proteomics. Chem. Rev. 2001, 101:269-295.
    • (2001) Chem. Rev. , vol.101 , pp. 269-295
    • Aebersold, R.1    Goodlett, D.R.2
  • 24
    • 33847616949 scopus 로고    scopus 로고
    • Reproducible isolation of distinct, overlapping segments of the phosphoproteome
    • Bodenmiller B., Mueller L.N., Mueller M., Domon B., Aebersold R. Reproducible isolation of distinct, overlapping segments of the phosphoproteome. Nat. Methods 2007, 4:231-237.
    • (2007) Nat. Methods , vol.4 , pp. 231-237
    • Bodenmiller, B.1    Mueller, L.N.2    Mueller, M.3    Domon, B.4    Aebersold, R.5
  • 25
    • 27744563093 scopus 로고    scopus 로고
    • State-of-the-art in phosphoproteomics
    • Reinders J., Sickmann A. State-of-the-art in phosphoproteomics. Proteomics 2005, 5:4052-4061.
    • (2005) Proteomics , vol.5 , pp. 4052-4061
    • Reinders, J.1    Sickmann, A.2
  • 26
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • Zhou H., Watts J.D., Aebersold R. A systematic approach to the analysis of protein phosphorylation. Nat. Biotechnol. 2001, 19:375-378.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 375-378
    • Zhou, H.1    Watts, J.D.2    Aebersold, R.3
  • 28
    • 0033565503 scopus 로고    scopus 로고
    • Immobilized gallium(III) affinity chromatography of phosphopeptides
    • Posewitz M.C., Tempst P. Immobilized gallium(III) affinity chromatography of phosphopeptides. Anal. Chem. 1999, 71:2883-2892.
    • (1999) Anal. Chem. , vol.71 , pp. 2883-2892
    • Posewitz, M.C.1    Tempst, P.2
  • 29
    • 2642583142 scopus 로고    scopus 로고
    • Improved detection of hydrophilic phosphopeptides using graphite powder microcolumns and mass spectrometry: evidence for in vivo doubly phosphorylated dynamin I and dynamin III
    • Larsen M.R., Graham M.E., Robinson P.J., Roepstorff P. Improved detection of hydrophilic phosphopeptides using graphite powder microcolumns and mass spectrometry: evidence for in vivo doubly phosphorylated dynamin I and dynamin III. Mol. Cell. Proteomics 2004, 3:456-465.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 456-465
    • Larsen, M.R.1    Graham, M.E.2    Robinson, P.J.3    Roepstorff, P.4
  • 32
    • 3042806641 scopus 로고    scopus 로고
    • Mapping phosphorylation sites: a new strategy based on the use of isotopically labelled DTT and mass spectrometry
    • Amoresano A., Marino G., Cirulli C., Quemeneur E. Mapping phosphorylation sites: a new strategy based on the use of isotopically labelled DTT and mass spectrometry. Eur. J. Mass Spectrom. (Chichester, Engl.) 2004, 10:401-412.
    • (2004) Eur. J. Mass Spectrom. (Chichester, Engl.) , vol.10 , pp. 401-412
    • Amoresano, A.1    Marino, G.2    Cirulli, C.3    Quemeneur, E.4
  • 33
    • 0036468952 scopus 로고    scopus 로고
    • Phosphoprotein isotope-coded affinity tags: application to the enrichment and identification of low-abundance phosphoproteins
    • Goshe M.B., Veenstra T.D., Panisko E.A., Conrads T.P., Angell N.H., Smith R.D. Phosphoprotein isotope-coded affinity tags: application to the enrichment and identification of low-abundance phosphoproteins. Anal. Chem. 2002, 74:607-616.
    • (2002) Anal. Chem. , vol.74 , pp. 607-616
    • Goshe, M.B.1    Veenstra, T.D.2    Panisko, E.A.3    Conrads, T.P.4    Angell, N.H.5    Smith, R.D.6
  • 34
    • 0346101744 scopus 로고    scopus 로고
    • Phosphospecific proteolysis for mapping sites of protein phosphorylation
    • Knights C.D., Liu Y., Appella E., Kulesz-Martin M. Phosphospecific proteolysis for mapping sites of protein phosphorylation. J. Biol. Chem. 2003, 278:52890-52900.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52890-52900
    • Knights, C.D.1    Liu, Y.2    Appella, E.3    Kulesz-Martin, M.4
  • 35
    • 0348014634 scopus 로고    scopus 로고
    • Improved β-elimination-based affinity purification strategy for enrichment of phosphopeptides
    • McLachlin D.T., Chait B.T. Improved β-elimination-based affinity purification strategy for enrichment of phosphopeptides. Anal. Chem. 2003, 75:6826-6836.
    • (2003) Anal. Chem. , vol.75 , pp. 6826-6836
    • McLachlin, D.T.1    Chait, B.T.2
  • 36
    • 0037240684 scopus 로고    scopus 로고
    • In vivo and in vitro phosphorylation regions of bone sialoprotein
    • Salih E. In vivo and in vitro phosphorylation regions of bone sialoprotein. Connect. Tissue Res. 2003, 44(Suppl. 1):223-229.
    • (2003) Connect. Tissue Res. , vol.44 , Issue.SUPPL. 1 , pp. 223-229
    • Salih, E.1
  • 37
    • 0038353301 scopus 로고    scopus 로고
    • 3H]carboxymethyl-dithiothreitol: identification of the phosphorylation sites by N-terminal peptide sequencing and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • 3H]carboxymethyl-dithiothreitol: identification of the phosphorylation sites by N-terminal peptide sequencing and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Anal. Biochem. 2003, 31:143-158.
    • (2003) Anal. Biochem. , vol.31 , pp. 143-158
    • Salih, E.1
  • 38
    • 13844313887 scopus 로고    scopus 로고
    • Quantitative analysis of both protein expression and serine/threonine post-translational modifications through stable isotope labeling with dithiothreitol
    • Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., Hart G.W., Burlingame A.L. Quantitative analysis of both protein expression and serine/threonine post-translational modifications through stable isotope labeling with dithiothreitol. Proteomics 2005, 5:388-398.
    • (2005) Proteomics , vol.5 , pp. 388-398
    • Vosseller, K.1    Hansen, K.C.2    Chalkley, R.J.3    Trinidad, J.C.4    Wells, L.5    Hart, G.W.6    Burlingame, A.L.7
  • 39
    • 0033827629 scopus 로고    scopus 로고
    • Comparative quantification and identification of phosphoproteins using stable isotope labeling and liquid chromatography/mass spectrometry
    • Weckwerth W., Willmitzer L., Fiehn O. Comparative quantification and identification of phosphoproteins using stable isotope labeling and liquid chromatography/mass spectrometry. Rapid Commun. Mass Spectrom. 2000, 14:1677-1681.
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 1677-1681
    • Weckwerth, W.1    Willmitzer, L.2    Fiehn, O.3
  • 40
    • 27844600289 scopus 로고    scopus 로고
    • Phosphoproteomics by mass spectrometry and classical protein chemistry approaches
    • Salih E. Phosphoproteomics by mass spectrometry and classical protein chemistry approaches. Mass Spectrom. Rev. 2005, 24:828-846.
    • (2005) Mass Spectrom. Rev. , vol.24 , pp. 828-846
    • Salih, E.1
  • 41
    • 0015906866 scopus 로고
    • Covalent chromatography: preparation of fully active papain from dried papaya latex
    • Brocklehurst K., Carlsson J., Kierstan M.P., Crook E.M. Covalent chromatography: preparation of fully active papain from dried papaya latex. Biochem. J. 1973, 133:573-584.
    • (1973) Biochem. J. , vol.133 , pp. 573-584
    • Brocklehurst, K.1    Carlsson, J.2    Kierstan, M.P.3    Crook, E.M.4
  • 42
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptide with amino acid sequences in a protein database
    • Eng J., McCornack A., Yates J.R. An approach to correlate tandem mass spectral data of peptide with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 1994, 5:976-989.
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.1    McCornack, A.2    Yates, J.R.3
  • 43
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: the yeast proteome
    • Peng J., Elias J.E., Thoreen C.C., Licklider L.J., Gygi S.P. Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: the yeast proteome. J. Proteome Res. 2003, 2:43-50.
    • (2003) J. Proteome Res. , vol.2 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 46
    • 0026178605 scopus 로고
    • Selective effects of histidine-rich polypeptides on the aggregation and viability of Streptococcus mutans and Streptococcus sanguis
    • Payne J.B., Iacono V.J., Crawford I.T., Lepre B.M., Bernzweig E., Grossbard B.L. Selective effects of histidine-rich polypeptides on the aggregation and viability of Streptococcus mutans and Streptococcus sanguis. Oral Microbiol. Immunol. 1991, 6:169-176.
    • (1991) Oral Microbiol. Immunol. , vol.6 , pp. 169-176
    • Payne, J.B.1    Iacono, V.J.2    Crawford, I.T.3    Lepre, B.M.4    Bernzweig, E.5    Grossbard, B.L.6
  • 47
    • 0025772230 scopus 로고
    • Intrasteric regulation of protein kinases and phosphatases
    • Kemp B.E., Pearson R.B. Intrasteric regulation of protein kinases and phosphatases. Biochim. Biophys. Acta 1991, 1094:67-76.
    • (1991) Biochim. Biophys. Acta , vol.1094 , pp. 67-76
    • Kemp, B.E.1    Pearson, R.B.2
  • 48
    • 0026355413 scopus 로고
    • Protein kinase phosphorylation site sequences and consensus specificity motifs: tabulations
    • Pearson R.B., Kemp B.E. Protein kinase phosphorylation site sequences and consensus specificity motifs: tabulations. Methods Enzymol. 1991, 200:62-81.
    • (1991) Methods Enzymol. , vol.200 , pp. 62-81
    • Pearson, R.B.1    Kemp, B.E.2
  • 49
    • 14644422603 scopus 로고    scopus 로고
    • Different isoforms and post-translational modifications of human salivary acidic proline-rich proteins
    • Inzitari R., Cabras T., Onnis G., Olmi C. Different isoforms and post-translational modifications of human salivary acidic proline-rich proteins. Proteomics 2005, 5:805-815.
    • (2005) Proteomics , vol.5 , pp. 805-815
    • Inzitari, R.1    Cabras, T.2    Onnis, G.3    Olmi, C.4
  • 52
    • 33847194634 scopus 로고    scopus 로고
    • Automatic validation of phosphopeptide identifications from tandem mass spectra
    • Lu B., Ruse C., Xu T., Park S.K., Yates J. Automatic validation of phosphopeptide identifications from tandem mass spectra. Anal. Chem. 2007, 79:1301-1310.
    • (2007) Anal. Chem. , vol.79 , pp. 1301-1310
    • Lu, B.1    Ruse, C.2    Xu, T.3    Park, S.K.4    Yates, J.5
  • 53
    • 1042275609 scopus 로고    scopus 로고
    • Chemical probes and tandem mass spectrometry: a strategy for the quantitative analysis of proteomes and subproteomes
    • Zhang H., Yan W., Aebersold R. Chemical probes and tandem mass spectrometry: a strategy for the quantitative analysis of proteomes and subproteomes. Curr. Opin. Chem. Biol. 2004, 8:66-75.
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 66-75
    • Zhang, H.1    Yan, W.2    Aebersold, R.3
  • 54
    • 77956877639 scopus 로고    scopus 로고
    • Emergence of phosphoproteomics through combination of mass spectrometry and classical protein chemistry
    • Toronto University Press, Toronto, Canada, W.L. Landis, J. Sodek (Eds.)
    • Salih E. Emergence of phosphoproteomics through combination of mass spectrometry and classical protein chemistry. The Chemistry and Biology of Mineralized Tissues 2004, 208-211. Toronto University Press, Toronto, Canada. W.L. Landis, J. Sodek (Eds.).
    • (2004) The Chemistry and Biology of Mineralized Tissues , pp. 208-211
    • Salih, E.1
  • 55
    • 28644452554 scopus 로고    scopus 로고
    • A catalogue of human saliva proteins identified by free flow electrophoresis-based peptide separation and tandem mass spectrometry
    • Xie H., Rhodus N.L., Griffin R.J., Carlis J.V., Griffin T.J. A catalogue of human saliva proteins identified by free flow electrophoresis-based peptide separation and tandem mass spectrometry. Mol. Cell. Proteomics 2005, 4:1826-1830.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1826-1830
    • Xie, H.1    Rhodus, N.L.2    Griffin, R.J.3    Carlis, J.V.4    Griffin, T.J.5
  • 57
  • 58
    • 67649213067 scopus 로고    scopus 로고
    • Phosphopeptide fragmentation and analysis by mass spectrometry
    • Boersema P.J., Mohammed S., Heck A.J.R. Phosphopeptide fragmentation and analysis by mass spectrometry. J. Mass Spectrom. 2009, 44:861-878.
    • (2009) J. Mass Spectrom. , vol.44 , pp. 861-878
    • Boersema, P.J.1    Mohammed, S.2    Heck, A.J.R.3
  • 59
    • 38649083118 scopus 로고    scopus 로고
    • Assigning significance to peptides identified by tandem mass spectrometry using decoy databases
    • Kall L., Storey J.D., MacCoss M.J., Noble W.S. Assigning significance to peptides identified by tandem mass spectrometry using decoy databases. J. Proteome Res. 2008, 7:29-34.
    • (2008) J. Proteome Res. , vol.7 , pp. 29-34
    • Kall, L.1    Storey, J.D.2    MacCoss, M.J.3    Noble, W.S.4
  • 60
    • 0025997659 scopus 로고
    • 2+ ions for their detection during peptide microsequencing
    • 2+ ions for their detection during peptide microsequencing. Biochem. J. 1991, 280:261-265.
    • (1991) Biochem. J. , vol.280 , pp. 261-265
    • Byford, M.F.1
  • 61
  • 63
    • 2642545646 scopus 로고    scopus 로고
    • O-Sulfonation of serine and threonine: mass spectrometric detection and characterization of a new posttranslational modification in diverse proteins throughout the eukaryotes
    • Medzihradszby K.F., Darula Z., Perlson E., Fainzilber M. O-Sulfonation of serine and threonine: mass spectrometric detection and characterization of a new posttranslational modification in diverse proteins throughout the eukaryotes. Mol. Cell. Proteomics 2004, 3:429-440.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 429-440
    • Medzihradszby, K.F.1    Darula, Z.2    Perlson, E.3    Fainzilber, M.4
  • 64
    • 0035965793 scopus 로고    scopus 로고
    • The human tuftelin gene: cloning and characterization
    • Mao Z., Shay B., Hekmati M., Fermon E. The human tuftelin gene: cloning and characterization. Gene 2001, 279:181-196.
    • (2001) Gene , vol.279 , pp. 181-196
    • Mao, Z.1    Shay, B.2    Hekmati, M.3    Fermon, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.