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Volumn 98, Issue , 2014, Pages 206-217

MRM validation of targeted nonglycosylated peptides from N-glycoprotein biomarkers using direct trypsin digestion of undepleted human plasma

Author keywords

Multiple reaction monitoring (MRM) validation; N glycoprotein; Nonglycosylated peptide; Rapid digestion; Undepleted plasma

Indexed keywords

BIOLOGICAL MARKER; CYSTEINE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GLYCAN; GLYCOPROTEIN; N GLYCOPROTEIN; OROSOMUCOID; PEPTIDE; TRYPSIN; TUMOR MARKER; UNCLASSIFIED DRUG; VITRONECTIN;

EID: 84893371597     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2014.01.003     Document Type: Article
Times cited : (14)

References (60)
  • 1
    • 83055168517 scopus 로고    scopus 로고
    • Targeted mass spectrometric approach for biomarker discovery and validation with nonglycosylated tryptic peptides from N-linked glycoproteins in human plasma
    • [M111 009290]
    • Lee J.Y., et al. Targeted mass spectrometric approach for biomarker discovery and validation with nonglycosylated tryptic peptides from N-linked glycoproteins in human plasma. Mol Cell Proteomics 2011, 10. [M111 009290]. 10.1074/mcp.M111.009290.
    • (2011) Mol Cell Proteomics , vol.10
    • Lee, J.Y.1
  • 2
    • 0033782777 scopus 로고    scopus 로고
    • Protein glucosylation and its role in protein folding
    • Parodi A.J. Protein glucosylation and its role in protein folding. Annu Rev Biochem 2000, 69:69-93. 10.1146/annurev.biochem.69.1.69.
    • (2000) Annu Rev Biochem , vol.69 , pp. 69-93
    • Parodi, A.J.1
  • 3
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler R., Hermjakob H., Sharon N. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim Biophys Acta 1999, 1473:4-8.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 4
    • 84866517384 scopus 로고    scopus 로고
    • Glycopeptide enrichment and separation for protein glycosylation analysis
    • Ongay S., Boichenko A., Govorukhina N., Bischoff R. Glycopeptide enrichment and separation for protein glycosylation analysis. J Sep Sci 2012, 35:2341-2372. 10.1002/jssc.201200434.
    • (2012) J Sep Sci , vol.35 , pp. 2341-2372
    • Ongay, S.1    Boichenko, A.2    Govorukhina, N.3    Bischoff, R.4
  • 5
    • 68249103612 scopus 로고    scopus 로고
    • Core fucose and bisecting GlcNAc, the direct modifiers of the N-glycan core: their functions and target proteins
    • Takahashi M., Kuroki Y., Ohtsubo K., Taniguchi N. Core fucose and bisecting GlcNAc, the direct modifiers of the N-glycan core: their functions and target proteins. Carbohydr Res 2009, 344:1387-1390. 10.1016/j.carres.2009.04.031.
    • (2009) Carbohydr Res , vol.344 , pp. 1387-1390
    • Takahashi, M.1    Kuroki, Y.2    Ohtsubo, K.3    Taniguchi, N.4
  • 6
    • 61849083675 scopus 로고    scopus 로고
    • A mutual regulation between cell-cell adhesion and N-glycosylation: implication of the bisecting GlcNAc for biological functions
    • Gu J., et al. A mutual regulation between cell-cell adhesion and N-glycosylation: implication of the bisecting GlcNAc for biological functions. J Proteome Res 2009, 8:431-435. 10.1021/pr800674g.
    • (2009) J Proteome Res , vol.8 , pp. 431-435
    • Gu, J.1
  • 7
    • 39049105125 scopus 로고    scopus 로고
    • Functional proteomics study reveals that N-Acetylglucosaminyltransferase V reinforces the invasive/metastatic potential of colon cancer through aberrant glycosylation on tissue inhibitor of metalloproteinase-1
    • Kim Y.S., et al. Functional proteomics study reveals that N-Acetylglucosaminyltransferase V reinforces the invasive/metastatic potential of colon cancer through aberrant glycosylation on tissue inhibitor of metalloproteinase-1. Mol Cell Proteomics 2008, 7:1-14. 10.1074/mcp.M700084-MCP200.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 1-14
    • Kim, Y.S.1
  • 8
    • 75849140063 scopus 로고    scopus 로고
    • Sweetening the pot: adding glycosylation to the biomarker discovery equation
    • Drake P.M., et al. Sweetening the pot: adding glycosylation to the biomarker discovery equation. Clin Chem 2010, 56:223-236. 10.1373/clinchem.2009.136333.
    • (2010) Clin Chem , vol.56 , pp. 223-236
    • Drake, P.M.1
  • 9
    • 78651063463 scopus 로고    scopus 로고
    • High-mannose glycans are elevated during breast cancer progression
    • [M110 002717]
    • de Leoz M.L., et al. High-mannose glycans are elevated during breast cancer progression. Mol Cell Proteomics 2011, 10. [M110 002717]. 10.1074/mcp.M110.002717.
    • (2011) Mol Cell Proteomics , vol.10
    • de Leoz, M.L.1
  • 10
    • 33644518378 scopus 로고    scopus 로고
    • Identification of target proteins of N-acetylglucosaminyl transferase V in human colon cancer and implications of protein tyrosine phosphatase kappa in enhanced cancer cell migration
    • Kim Y.S., et al. Identification of target proteins of N-acetylglucosaminyl transferase V in human colon cancer and implications of protein tyrosine phosphatase kappa in enhanced cancer cell migration. Proteomics 2006, 6:1187-1191. 10.1002/pmic.200500400.
    • (2006) Proteomics , vol.6 , pp. 1187-1191
    • Kim, Y.S.1
  • 11
    • 73849150680 scopus 로고    scopus 로고
    • Glycoproteomics in neurodegenerative diseases
    • Hwang H., et al. Glycoproteomics in neurodegenerative diseases. Mass Spectrom Rev 2010, 29:79-125. 10.1002/mas.20221.
    • (2010) Mass Spectrom Rev , vol.29 , pp. 79-125
    • Hwang, H.1
  • 12
    • 0033057177 scopus 로고    scopus 로고
    • The carcinoembryonic antigen (CEA) family: structures, suggested functions and expression in normal and malignant tissues
    • Hammarstrom S. The carcinoembryonic antigen (CEA) family: structures, suggested functions and expression in normal and malignant tissues. Semin Cancer Biol 1999, 9:67-81. 10.1006/scbi.1998.0119.
    • (1999) Semin Cancer Biol , vol.9 , pp. 67-81
    • Hammarstrom, S.1
  • 13
    • 15044354616 scopus 로고    scopus 로고
    • The role of CA125 in clinical practice
    • Moss E.L., Hollingworth J., Reynolds T.M. The role of CA125 in clinical practice. J Clin Pathol 2005, 58:308-312. 10.1136/jcp.2004.018077.
    • (2005) J Clin Pathol , vol.58 , pp. 308-312
    • Moss, E.L.1    Hollingworth, J.2    Reynolds, T.M.3
  • 14
    • 61849174789 scopus 로고    scopus 로고
    • Glycoproteomics for prostate cancer detection: changes in serum PSA glycosylation patterns
    • Meany D.L., Zhang Z., Sokoll L.J., Zhang H., Chan D.W. Glycoproteomics for prostate cancer detection: changes in serum PSA glycosylation patterns. J Proteome Res 2009, 8:613-619. 10.1021/pr8007539.
    • (2009) J Proteome Res , vol.8 , pp. 613-619
    • Meany, D.L.1    Zhang, Z.2    Sokoll, L.J.3    Zhang, H.4    Chan, D.W.5
  • 15
    • 70349784960 scopus 로고    scopus 로고
    • Quantitative site-specific analysis of protein glycosylation by LC-MS using different glycopeptide-enrichment strategies
    • Wohlgemuth J., Karas M., Eichhorn T., Hendriks R., Andrecht S. Quantitative site-specific analysis of protein glycosylation by LC-MS using different glycopeptide-enrichment strategies. Anal Biochem 2009, 395:178-188. 10.1016/j.ab.2009.08.023.
    • (2009) Anal Biochem , vol.395 , pp. 178-188
    • Wohlgemuth, J.1    Karas, M.2    Eichhorn, T.3    Hendriks, R.4    Andrecht, S.5
  • 16
    • 33845417633 scopus 로고    scopus 로고
    • Strategies for analysis of glycoprotein glycosylation
    • Geyer H., Geyer R. Strategies for analysis of glycoprotein glycosylation. Biochim Biophys Acta 2006, 1764:1853-1869. 10.1016/j.bbapap.2006.10.007.
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1853-1869
    • Geyer, H.1    Geyer, R.2
  • 17
    • 84871860708 scopus 로고    scopus 로고
    • Quantification of the N-glycosylated secretome by super-SILAC during breast cancer progression and in human blood samples
    • Boersema P.J., Geiger T., Wisniewski J.R., Mann M. Quantification of the N-glycosylated secretome by super-SILAC during breast cancer progression and in human blood samples. Mol Cell Proteomics 2012, 10.1074/mcp.M112.023614.
    • (2012) Mol Cell Proteomics
    • Boersema, P.J.1    Geiger, T.2    Wisniewski, J.R.3    Mann, M.4
  • 18
    • 21644459777 scopus 로고    scopus 로고
    • Combining lectin microcolumns with high-resolution separation techniques for enrichment of glycoproteins and glycopeptides
    • Madera M., Mechref Y., Novotny M.V. Combining lectin microcolumns with high-resolution separation techniques for enrichment of glycoproteins and glycopeptides. Anal Chem 2005, 77:4081-4090. 10.1021/ac050222l.
    • (2005) Anal Chem , vol.77 , pp. 4081-4090
    • Madera, M.1    Mechref, Y.2    Novotny, M.V.3
  • 19
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • Zielinska D.F., Gnad F., Wisniewski J.R., Mann M. Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Cell 2010, 141:897-907. 10.1016/j.cell.2010.04.012.
    • (2010) Cell , vol.141 , pp. 897-907
    • Zielinska, D.F.1    Gnad, F.2    Wisniewski, J.R.3    Mann, M.4
  • 20
    • 84873350739 scopus 로고    scopus 로고
    • Modulation of glycan detection on specific glycoproteins by lectin multimerization
    • Cao Z., et al. Modulation of glycan detection on specific glycoproteins by lectin multimerization. Anal Chem 2013, 85:1689-1698. 10.1021/ac302826a.
    • (2013) Anal Chem , vol.85 , pp. 1689-1698
    • Cao, Z.1
  • 21
    • 79960723943 scopus 로고    scopus 로고
    • A multiplexed bead assay for profiling glycosylation patterns on serum protein biomarkers of pancreatic cancer
    • Li C., et al. A multiplexed bead assay for profiling glycosylation patterns on serum protein biomarkers of pancreatic cancer. Electrophoresis 2011, 32:2028-2035. 10.1002/elps.201000693.
    • (2011) Electrophoresis , vol.32 , pp. 2028-2035
    • Li, C.1
  • 22
    • 50449090916 scopus 로고    scopus 로고
    • Lectin precipitation using phytohemagglutinin-L(4) coupled to avidin-agarose for serological biomarker discovery in colorectal cancer
    • Kim Y.S., et al. Lectin precipitation using phytohemagglutinin-L(4) coupled to avidin-agarose for serological biomarker discovery in colorectal cancer. Proteomics 2008, 8:3229-3235. 10.1002/pmic.200800034.
    • (2008) Proteomics , vol.8 , pp. 3229-3235
    • Kim, Y.S.1
  • 23
    • 84879899584 scopus 로고    scopus 로고
    • Altered expression of sialylated glycoproteins in ovarian cancer sera using lectin-based ELISA assay and quantitative glycoproteomics analysis
    • Wu J., Xie X., Nie S., Buckanovich R.J., Lubman D.M. Altered expression of sialylated glycoproteins in ovarian cancer sera using lectin-based ELISA assay and quantitative glycoproteomics analysis. J Proteome Res 2013, 12:3342-3352. 10.1021/pr400169n.
    • (2013) J Proteome Res , vol.12 , pp. 3342-3352
    • Wu, J.1    Xie, X.2    Nie, S.3    Buckanovich, R.J.4    Lubman, D.M.5
  • 24
    • 84878639123 scopus 로고    scopus 로고
    • Isobaric protein-level labeling strategy for serum glycoprotein quantification analysis by liquid chromatography-tandem mass spectrometry
    • Nie S., et al. Isobaric protein-level labeling strategy for serum glycoprotein quantification analysis by liquid chromatography-tandem mass spectrometry. Anal Chem 2013, 85:5353-5357. 10.1021/ac400838s.
    • (2013) Anal Chem , vol.85 , pp. 5353-5357
    • Nie, S.1
  • 25
    • 29144459934 scopus 로고    scopus 로고
    • Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry
    • Liu T., et al. Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res 2005, 4:2070-2080. 10.1021/pr0502065.
    • (2005) J Proteome Res , vol.4 , pp. 2070-2080
    • Liu, T.1
  • 26
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • Zhang H., Li X.J., Martin D.B., Aebersold R. Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol 2003, 21:660-666. 10.1038/nbt827.
    • (2003) Nat Biotechnol , vol.21 , pp. 660-666
    • Zhang, H.1    Li, X.J.2    Martin, D.B.3    Aebersold, R.4
  • 27
    • 61849164561 scopus 로고    scopus 로고
    • Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry
    • Chen R., et al. Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res 2009, 8:651-661. 10.1021/pr8008012.
    • (2009) J Proteome Res , vol.8 , pp. 651-661
    • Chen, R.1
  • 28
    • 4444269089 scopus 로고    scopus 로고
    • A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation
    • Hagglund P., Bunkenborg J., Elortza F., Jensen O.N., Roepstorff P. A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation. J Proteome Res 2004, 3:556-566.
    • (2004) J Proteome Res , vol.3 , pp. 556-566
    • Hagglund, P.1    Bunkenborg, J.2    Elortza, F.3    Jensen, O.N.4    Roepstorff, P.5
  • 29
    • 65249134633 scopus 로고    scopus 로고
    • Structural glycomics using hydrophilic interaction chromatography (HILIC) with mass spectrometry
    • Wuhrer M., de Boer A.R., Deelder A.M. Structural glycomics using hydrophilic interaction chromatography (HILIC) with mass spectrometry. Mass Spectrom Rev 2009, 28:192-206. 10.1002/mas.20195.
    • (2009) Mass Spectrom Rev , vol.28 , pp. 192-206
    • Wuhrer, M.1    de Boer, A.R.2    Deelder, A.M.3
  • 30
    • 45949094992 scopus 로고    scopus 로고
    • Profiling of N- and O-glycopeptides of erythropoietin by capillary zwitterionic type of hydrophilic interaction chromatography/electrospray ionization mass spectrometry
    • Takegawa Y., et al. Profiling of N- and O-glycopeptides of erythropoietin by capillary zwitterionic type of hydrophilic interaction chromatography/electrospray ionization mass spectrometry. J Sep Sci 2008, 31:1585-1593. 10.1002/jssc.200700679.
    • (2008) J Sep Sci , vol.31 , pp. 1585-1593
    • Takegawa, Y.1
  • 31
    • 77950907667 scopus 로고    scopus 로고
    • 2-D hydrophilic interaction liquid chromatography-RP separation in urinary proteomics-minimizing variability through improved downstream workflow compatibility
    • Loftheim H., et al. 2-D hydrophilic interaction liquid chromatography-RP separation in urinary proteomics-minimizing variability through improved downstream workflow compatibility. J Sep Sci 2010, 33:864-872. 10.1002/jssc.200900554.
    • (2010) J Sep Sci , vol.33 , pp. 864-872
    • Loftheim, H.1
  • 32
    • 79955840214 scopus 로고    scopus 로고
    • Elucidation of glycoprotein structures by unspecific proteolysis and direct nanoESI mass spectrometric analysis of ZIC-HILIC-enriched glycopeptides
    • Neue K., Mormann M., Peter-Katalinic J., Pohlentz G. Elucidation of glycoprotein structures by unspecific proteolysis and direct nanoESI mass spectrometric analysis of ZIC-HILIC-enriched glycopeptides. J Proteome Res 2011, 10:2248-2260. 10.1021/pr101082c.
    • (2011) J Proteome Res , vol.10 , pp. 2248-2260
    • Neue, K.1    Mormann, M.2    Peter-Katalinic, J.3    Pohlentz, G.4
  • 33
    • 84878630101 scopus 로고    scopus 로고
    • Glycopeptide enrichment for MALDI-TOF mass spectrometry analysis by hydrophilic interaction liquid chromatography solid phase extraction (HILIC SPE)
    • Jensen P.H., Mysling S., Hojrup P., Jensen O.N. Glycopeptide enrichment for MALDI-TOF mass spectrometry analysis by hydrophilic interaction liquid chromatography solid phase extraction (HILIC SPE). Methods Mol Biol 2013, 951:131-144. 10.1007/978-1-62703-146-2_10.
    • (2013) Methods Mol Biol , vol.951 , pp. 131-144
    • Jensen, P.H.1    Mysling, S.2    Hojrup, P.3    Jensen, O.N.4
  • 34
    • 39449132134 scopus 로고    scopus 로고
    • Synthesis and evaluation of superparamagnetic silica particles for extraction of glycopeptides in the microtiter plate format
    • Zou Z., et al. Synthesis and evaluation of superparamagnetic silica particles for extraction of glycopeptides in the microtiter plate format. Anal Chem 2008, 80:1228-1234. 10.1021/ac701950h.
    • (2008) Anal Chem , vol.80 , pp. 1228-1234
    • Zou, Z.1
  • 35
    • 35649011957 scopus 로고    scopus 로고
    • Exploring the sialiome using titanium dioxide chromatography and mass spectrometry
    • Larsen M.R., Jensen S.S., Jakobsen L.A., Heegaard N.H. Exploring the sialiome using titanium dioxide chromatography and mass spectrometry. Mol Cell Proteomics 2007, 6:1778-1787. 10.1074/mcp.M700086-MCP200.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1778-1787
    • Larsen, M.R.1    Jensen, S.S.2    Jakobsen, L.A.3    Heegaard, N.H.4
  • 36
    • 48849109894 scopus 로고    scopus 로고
    • Assessment of lectin and HILIC based enrichment protocols for characterization of serum glycoproteins by mass spectrometry
    • Calvano C.D., Zambonin C.G., Jensen O.N. Assessment of lectin and HILIC based enrichment protocols for characterization of serum glycoproteins by mass spectrometry. J Proteomics 2008, 71:304-317. 10.1016/j.jprot.2008.06.013.
    • (2008) J Proteomics , vol.71 , pp. 304-317
    • Calvano, C.D.1    Zambonin, C.G.2    Jensen, O.N.3
  • 37
    • 0001644020 scopus 로고    scopus 로고
    • The human plasma proteome: history, character, and diagnostic prospects
    • Anderson N.L., Anderson N.G. The human plasma proteome: history, character, and diagnostic prospects. Mol Cell Proteomics 2002, 1:845-867.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 845-867
    • Anderson, N.L.1    Anderson, N.G.2
  • 38
    • 84860869256 scopus 로고    scopus 로고
    • MRM-based multiplexed quantitation of 67 putative cardiovascular disease biomarkers in human plasma
    • Domanski D., et al. MRM-based multiplexed quantitation of 67 putative cardiovascular disease biomarkers in human plasma. Proteomics 2012, 12:1222-1243. 10.1002/pmic.201100568.
    • (2012) Proteomics , vol.12 , pp. 1222-1243
    • Domanski, D.1
  • 39
    • 84879974563 scopus 로고    scopus 로고
    • Multiplexed MRM-based quantitation of candidate cancer biomarker proteins in undepleted and non-enriched human plasma
    • Percy A.J., Chambers A.G., Yang J., Borchers C.H. Multiplexed MRM-based quantitation of candidate cancer biomarker proteins in undepleted and non-enriched human plasma. Proteomics 2013, 10.1002/pmic.201200316.
    • (2013) Proteomics
    • Percy, A.J.1    Chambers, A.G.2    Yang, J.3    Borchers, C.H.4
  • 40
    • 84887924792 scopus 로고    scopus 로고
    • Absolute quantitation of proteins in human blood by multiplexed multiple reaction monitoring mass spectrometry
    • Percy A.J., Chambers A.G., Parker C.E., Borchers C.H. Absolute quantitation of proteins in human blood by multiplexed multiple reaction monitoring mass spectrometry. Methods Mol Biol 2013, 1000:167-189. 10.1007/978-1-62703-405-0_13.
    • (2013) Methods Mol Biol , vol.1000 , pp. 167-189
    • Percy, A.J.1    Chambers, A.G.2    Parker, C.E.3    Borchers, C.H.4
  • 41
    • 0346668199 scopus 로고    scopus 로고
    • Absolute quantification of the G protein-coupled receptor rhodopsin by LC/MS/MS using proteolysis product peptides and synthetic peptide standards
    • Barnidge D.R., et al. Absolute quantification of the G protein-coupled receptor rhodopsin by LC/MS/MS using proteolysis product peptides and synthetic peptide standards. Anal Chem 2003, 75:445-451.
    • (2003) Anal Chem , vol.75 , pp. 445-451
    • Barnidge, D.R.1
  • 42
    • 84888259618 scopus 로고    scopus 로고
    • Standardization and quality control in proteomics
    • Albar J.P., Canals F. Standardization and quality control in proteomics. J Proteomics 2013, 95:1-2. 10.1016/j.jprot.2013.11.002.
    • (2013) J Proteomics , vol.95 , pp. 1-2
    • Albar, J.P.1    Canals, F.2
  • 43
    • 84889670672 scopus 로고    scopus 로고
    • Isotope dilution mass spectrometry for absolute quantification in proteomics: concepts and strategies
    • Villanueva J., Carrascal M., Abian J. Isotope dilution mass spectrometry for absolute quantification in proteomics: concepts and strategies. J Proteomics 2013, 96C:184-199. 10.1016/j.jprot.2013.11.004.
    • (2013) J Proteomics , vol.96 C , pp. 184-199
    • Villanueva, J.1    Carrascal, M.2    Abian, J.3
  • 44
    • 84888295045 scopus 로고    scopus 로고
    • Method and platform standardization in MRM-based quantitative plasma proteomics
    • Percy A.J., et al. Method and platform standardization in MRM-based quantitative plasma proteomics. J Proteomics 2013, 95:66-76. 10.1016/j.jprot.2013.07.026.
    • (2013) J Proteomics , vol.95 , pp. 66-76
    • Percy, A.J.1
  • 45
    • 84888304733 scopus 로고    scopus 로고
    • Application of clinical assay quality control (QC) to multivariate proteomics data: a workflow exemplified by 2-DE QC
    • Jackson D., Bramwell D. Application of clinical assay quality control (QC) to multivariate proteomics data: a workflow exemplified by 2-DE QC. J Proteomics 2013, 95:22-37. 10.1016/j.jprot.2013.07.025.
    • (2013) J Proteomics , vol.95 , pp. 22-37
    • Jackson, D.1    Bramwell, D.2
  • 46
    • 77950675887 scopus 로고    scopus 로고
    • Verification of protein disulfide bond arrangement by in-gel tryptic digestion under entirely neutral pH conditions
    • Saito K., et al. Verification of protein disulfide bond arrangement by in-gel tryptic digestion under entirely neutral pH conditions. Proteomics 2010, 10:1505-1509. 10.1002/pmic.200900056.
    • (2010) Proteomics , vol.10 , pp. 1505-1509
    • Saito, K.1
  • 47
    • 77957344363 scopus 로고    scopus 로고
    • A quantitative study of the effects of chaotropic agents, surfactants, and solvents on the digestion efficiency of human plasma proteins by trypsin
    • Proc J.L., et al. A quantitative study of the effects of chaotropic agents, surfactants, and solvents on the digestion efficiency of human plasma proteins by trypsin. J Proteome Res 2010, 9:5422-5437. 10.1021/pr100656u.
    • (2010) J Proteome Res , vol.9 , pp. 5422-5437
    • Proc, J.L.1
  • 48
    • 0026557860 scopus 로고
    • Vitronectin in liver disorders: biochemical and immunohistochemical studies
    • Inuzuka S., et al. Vitronectin in liver disorders: biochemical and immunohistochemical studies. Hepatology 1992, 15:629-636.
    • (1992) Hepatology , vol.15 , pp. 629-636
    • Inuzuka, S.1
  • 49
    • 73649124980 scopus 로고    scopus 로고
    • Simple method for quantitative analysis of N-linked glycoproteins in hepatocellular carcinoma specimens
    • Lee H.J., et al. Simple method for quantitative analysis of N-linked glycoproteins in hepatocellular carcinoma specimens. J Proteome Res 2010, 9:308-318. 10.1021/pr900649b.
    • (2010) J Proteome Res , vol.9 , pp. 308-318
    • Lee, H.J.1
  • 50
    • 84855188603 scopus 로고    scopus 로고
    • Development of glycoprotein capture-based label-free method for the high-throughput screening of differential glycoproteins in hepatocellular carcinoma
    • [M110 006445]
    • Chen R., et al. Development of glycoprotein capture-based label-free method for the high-throughput screening of differential glycoproteins in hepatocellular carcinoma. Mol Cell Proteomics 2011, 10. [M110 006445]. 10.1074/mcp.M110.006445.
    • (2011) Mol Cell Proteomics , vol.10
    • Chen, R.1
  • 51
    • 33744485866 scopus 로고    scopus 로고
    • Diagnostic accuracy of serum asialo-alpha1-acid glycoprotein concentration for the differential diagnosis of liver cirrhosis and hepatocellular carcinoma
    • Kim K.A., et al. Diagnostic accuracy of serum asialo-alpha1-acid glycoprotein concentration for the differential diagnosis of liver cirrhosis and hepatocellular carcinoma. Clin Chim Acta 2006, 369:46-51. 10.1016/j.cca.2006.01.002.
    • (2006) Clin Chim Acta , vol.369 , pp. 46-51
    • Kim, K.A.1
  • 52
    • 57149113710 scopus 로고    scopus 로고
    • Combination of alpha-1-acid glycoprotein and alpha-fetoprotein as an improved diagnostic tool for hepatocellular carcinoma
    • Bachtiar I., et al. Combination of alpha-1-acid glycoprotein and alpha-fetoprotein as an improved diagnostic tool for hepatocellular carcinoma. Clin Chim Acta 2009, 399:97-101. 10.1016/j.cca.2008.09.024.
    • (2009) Clin Chim Acta , vol.399 , pp. 97-101
    • Bachtiar, I.1
  • 53
    • 30844466361 scopus 로고    scopus 로고
    • Development of a rapid, immunochromatographic strip test for serum asialo alpha1-acid glycoprotein in patients with hepatic disease
    • Lee E.Y., et al. Development of a rapid, immunochromatographic strip test for serum asialo alpha1-acid glycoprotein in patients with hepatic disease. J Immunol Methods 2006, 308:116-123. 10.1016/j.jim.2005.10.010.
    • (2006) J Immunol Methods , vol.308 , pp. 116-123
    • Lee, E.Y.1
  • 54
    • 77952900317 scopus 로고    scopus 로고
    • Survival signals of hepatic stellate cells in liver regeneration are regulated by glycosylation changes in rat vitronectin, especially decreased sialylation
    • Sano K., et al. Survival signals of hepatic stellate cells in liver regeneration are regulated by glycosylation changes in rat vitronectin, especially decreased sialylation. J Biol Chem 2010, 285:17301-17309. 10.1074/jbc.M109.077016.
    • (2010) J Biol Chem , vol.285 , pp. 17301-17309
    • Sano, K.1
  • 55
    • 34447326970 scopus 로고    scopus 로고
    • Changes in glycosylation of vitronectin modulate multimerization and collagen binding during liver regeneration
    • Sano K., Asanuma-Date K., Arisaka F., Hattori S., Ogawa H. Changes in glycosylation of vitronectin modulate multimerization and collagen binding during liver regeneration. Glycobiology 2007, 17:784-794. 10.1093/glycob/cwm031.
    • (2007) Glycobiology , vol.17 , pp. 784-794
    • Sano, K.1    Asanuma-Date, K.2    Arisaka, F.3    Hattori, S.4    Ogawa, H.5
  • 56
    • 0033839433 scopus 로고    scopus 로고
    • The changes in glycosylation after partial hepatectomy enhance collagen binding of vitronectin in plasma
    • Uchibori-Iwaki H., et al. The changes in glycosylation after partial hepatectomy enhance collagen binding of vitronectin in plasma. Glycobiology 2000, 10:865-874.
    • (2000) Glycobiology , vol.10 , pp. 865-874
    • Uchibori-Iwaki, H.1
  • 57
    • 0036739115 scopus 로고    scopus 로고
    • A preliminary evaluation of the differences in the glycosylation of alpha-1-acid glycoprotein between individual liver diseases
    • Anderson N., et al. A preliminary evaluation of the differences in the glycosylation of alpha-1-acid glycoprotein between individual liver diseases. Biomed Chromatogr 2002, 16:365-372. 10.1002/bmc.167.
    • (2002) Biomed Chromatogr , vol.16 , pp. 365-372
    • Anderson, N.1
  • 58
    • 84862778495 scopus 로고    scopus 로고
    • Large-scale isotype-specific quantification of serum amyloid A 1/2 by multiple reaction monitoring in crude sera
    • Sung H.J., et al. Large-scale isotype-specific quantification of serum amyloid A 1/2 by multiple reaction monitoring in crude sera. J Proteomics 2012, 75:2170-2180. 10.1016/j.jprot.2012.01.018.
    • (2012) J Proteomics , vol.75 , pp. 2170-2180
    • Sung, H.J.1
  • 59
    • 84862808990 scopus 로고    scopus 로고
    • A lectin-coupled, multiple reaction monitoring based quantitative analysis of human plasma glycoproteins by mass spectrometry
    • Ahn Y.H., Shin P.M., Ji E.S., Kim H., Yoo J.S. A lectin-coupled, multiple reaction monitoring based quantitative analysis of human plasma glycoproteins by mass spectrometry. Anal Bioanal Chem 2012, 402:2101-2112. 10.1007/s00216-011-5646-3.
    • (2012) Anal Bioanal Chem , vol.402 , pp. 2101-2112
    • Ahn, Y.H.1    Shin, P.M.2    Ji, E.S.3    Kim, H.4    Yoo, J.S.5
  • 60
    • 84895072645 scopus 로고    scopus 로고
    • Demonstrating the feasibility of large-scale development of standardized assays to quantify human proteins
    • Kennedy J.J., et al. Demonstrating the feasibility of large-scale development of standardized assays to quantify human proteins. Nat Methods 2013, 10.1038/nmeth.2763.
    • (2013) Nat Methods
    • Kennedy, J.J.1


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