메뉴 건너뛰기




Volumn 16, Issue 2, 2016, Pages 241-256

Chemoenzymatic method for glycomics: Isolation, identification, and quantitation

Author keywords

Glycomics; Glycoproteomics; IGIG; Isobaric labeling; Mass spectrometry

Indexed keywords

GLYCAN; AMIDASE; GLYCOPROTEIN; POLYSACCHARIDE;

EID: 84956591629     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201500266     Document Type: Review
Times cited : (20)

References (120)
  • 1
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • Arnold, J. N., Wormald, M. R., Sim, R. B., Rudd, P. M., Dwek, R. A., The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu. Rev. Immunol. 2007, 25, 21-50.
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 21-50
    • Arnold, J.N.1    Wormald, M.R.2    Sim, R.B.3    Rudd, P.M.4    Dwek, R.A.5
  • 2
    • 34249874096 scopus 로고    scopus 로고
    • Mutation in the key enzyme of sialic acid biosynthesis causes severe glomerular proteinuria and is rescued by N-acetylmannosamine
    • Galeano, B., Klootwijk, R., Manoli, I., Sun, M. et al., Mutation in the key enzyme of sialic acid biosynthesis causes severe glomerular proteinuria and is rescued by N-acetylmannosamine. J. Clin. Invest. 2007, 117, 1585-1594.
    • (2007) J. Clin. Invest. , vol.117 , pp. 1585-1594
    • Galeano, B.1    Klootwijk, R.2    Manoli, I.3    Sun, M.4
  • 5
    • 0035937424 scopus 로고    scopus 로고
    • Glycosylation, immunity, and autoimmunity
    • Lowe, J. B., Glycosylation, immunity, and autoimmunity. Cell 2001, 104, 809-812.
    • (2001) Cell , vol.104 , pp. 809-812
    • Lowe, J.B.1
  • 6
    • 0037069682 scopus 로고    scopus 로고
    • HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites
    • Kwong, P. D., Doyle, M. L., Casper, D. J., Cicala, C. et al., HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites. Nature 2002, 420, 678-682.
    • (2002) Nature , vol.420 , pp. 678-682
    • Kwong, P.D.1    Doyle, M.L.2    Casper, D.J.3    Cicala, C.4
  • 7
    • 33847105538 scopus 로고    scopus 로고
    • Diastolic heart failure Evidence of increased myocardial collagen turnover linked to diastolic dysfunction
    • Martos, R., Baugh, J., Ledwidge, M., C O'Loughlin, C. et al., Diastolic heart failure Evidence of increased myocardial collagen turnover linked to diastolic dysfunction. Circulation 2007, 115, 888-895.
    • (2007) Circulation , vol.115 , pp. 888-895
    • Martos, R.1    Baugh, J.2    Ledwidge, M.C.3    O'Loughlin, C.4
  • 8
    • 84921367281 scopus 로고    scopus 로고
    • Glycoproteins identified from heart failure and treatment models
    • Yang, S., Chen, L., Sun, S., Shah, P. et al., Glycoproteins identified from heart failure and treatment models. Proteomics 2015, 15, 567-579.
    • (2015) Proteomics , vol.15 , pp. 567-579
    • Yang, S.1    Chen, L.2    Sun, S.3    Shah, P.4
  • 9
    • 77950410995 scopus 로고    scopus 로고
    • Alterations in glycosylation as biomarkers for cancer detection
    • Reis, C. A., Osorio, H., Silva, L., Gomes, C., David, L., Alterations in glycosylation as biomarkers for cancer detection. J. Clin. Pathol. 2010, 63, 322-329.
    • (2010) J. Clin. Pathol. , vol.63 , pp. 322-329
    • Reis, C.A.1    Osorio, H.2    Silva, L.3    Gomes, C.4    David, L.5
  • 10
    • 61649087668 scopus 로고    scopus 로고
    • Glycosylation as a strategy to improve antibody-based therapeutics
    • Jefferis, R., Glycosylation as a strategy to improve antibody-based therapeutics. Nat. Rev. Drug Discov. 2009, 8, 226-234.
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 226-234
    • Jefferis, R.1
  • 12
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • Spiro, R. G., Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology 2002, 12, 43R-56R.
    • (2002) Glycobiology , vol.12 , pp. 43R-56R
    • Spiro, R.G.1
  • 13
    • 28544444249 scopus 로고    scopus 로고
    • Glycomics: an integrated systems approach to structure-function relationships of glycans
    • Raman, R., Raguram, S., Venkataraman, G., Paulson, J. C., Sasisekharan, R., Glycomics: an integrated systems approach to structure-function relationships of glycans. Nat. Methods 2005, 2, 817-824.
    • (2005) Nat. Methods , vol.2 , pp. 817-824
    • Raman, R.1    Raguram, S.2    Venkataraman, G.3    Paulson, J.C.4    Sasisekharan, R.5
  • 14
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius, A., Aebi, M., Roles of N-linked glycans in the endoplasmic reticulum. Annu. Rev. Biochem. 2004, 73, 1019-1049.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 15
    • 0022003140 scopus 로고
    • Deglycosylation of asparagine-linked glycans by peptide: N-glycosidase F
    • Tarentino, A. L., Gomez, C. M., Plummer Jr, T. H., Deglycosylation of asparagine-linked glycans by peptide: N-glycosidase F. Biochemistry 1985, 24, 4665-4671.
    • (1985) Biochemistry , vol.24 , pp. 4665-4671
    • Tarentino, A.L.1    Gomez, C.M.2    Plummer, T.H.3
  • 16
    • 0014408452 scopus 로고
    • Structures and immunochemical properties of oligosaccharides isolated from pig submaxillary mucins
    • Carlson, D. M., Structures and immunochemical properties of oligosaccharides isolated from pig submaxillary mucins. J. Biol. Chem. 1968, 243, 616-626.
    • (1968) J. Biol. Chem. , vol.243 , pp. 616-626
    • Carlson, D.M.1
  • 17
    • 0017833163 scopus 로고
    • [4]Microdetermination of sugar composition by radioisotope labeling
    • Takasaki, S., Kobata, A., [4]Microdetermination of sugar composition by radioisotope labeling. Methods Enzymol. 1978, 50, 50-54.
    • (1978) Methods Enzymol , vol.50 , pp. 50-54
    • Takasaki, S.1    Kobata, A.2
  • 18
    • 33845519906 scopus 로고    scopus 로고
    • Use of a 2, 5-dihydroxybenzoic acid/aniline MALDI matrix for improved detection and on-target derivatization of glycans: a preliminary report
    • Snovida, S. I., Chen, V. C., Perreault, H., Use of a 2, 5-dihydroxybenzoic acid/aniline MALDI matrix for improved detection and on-target derivatization of glycans: a preliminary report. Anal. Chem. 2006, 78, 8561-8568.
    • (2006) Anal. Chem. , vol.78 , pp. 8561-8568
    • Snovida, S.I.1    Chen, V.C.2    Perreault, H.3
  • 19
    • 80052329656 scopus 로고    scopus 로고
    • Hydrophobic derivatization of N-linked glycans for increased ion abundance in electrospray ionization mass spectrometry
    • Walker, S. H., Lilley, L. M., Enamorado, M. F., Comins, D. L., Muddiman, D. C., Hydrophobic derivatization of N-linked glycans for increased ion abundance in electrospray ionization mass spectrometry. J. Am. Soc. Mass Spectrom. 2011, 22, 1309-1317.
    • (2011) J. Am. Soc. Mass Spectrom. , vol.22 , pp. 1309-1317
    • Walker, S.H.1    Lilley, L.M.2    Enamorado, M.F.3    Comins, D.L.4    Muddiman, D.C.5
  • 20
    • 0029164230 scopus 로고
    • Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid
    • Bigge, J., Patel, T., Bruce, J., Goulding, P. et al., Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid. Anal. Biochem. 1995, 230, 229-238.
    • (1995) Anal. Biochem. , vol.230 , pp. 229-238
    • Bigge, J.1    Patel, T.2    Bruce, J.3    Goulding, P.4
  • 21
    • 28544438397 scopus 로고    scopus 로고
    • Versatile fluorescent derivatization of glycans for glycomic analysis
    • Xia, B., Kawar, Z. S., Ju, T., Alvarez, R. A. et al., Versatile fluorescent derivatization of glycans for glycomic analysis. Nat. Methods 2005, 2, 845-850.
    • (2005) Nat. Methods , vol.2 , pp. 845-850
    • Xia, B.1    Kawar, Z.S.2    Ju, T.3    Alvarez, R.A.4
  • 22
    • 41449087577 scopus 로고    scopus 로고
    • HPLC-based analysis of serum N-glycans on a 96-well plate platform with dedicated database software
    • Royle, L., Campbell, M. P., Radcliffe, C. M., White, D. M. et al., HPLC-based analysis of serum N-glycans on a 96-well plate platform with dedicated database software. Anal. Biochem. 2008, 376, 1-12.
    • (2008) Anal. Biochem. , vol.376 , pp. 1-12
    • Royle, L.1    Campbell, M.P.2    Radcliffe, C.M.3    White, D.M.4
  • 23
    • 16344380985 scopus 로고    scopus 로고
    • Automatic annotation of matrix-assisted laser desorption/ionization N-glycan spectra
    • Goldberg, D., Sutton-Smith, M., Paulson, J., Dell, A., Automatic annotation of matrix-assisted laser desorption/ionization N-glycan spectra. Proteomics 2005, 5, 865-875.
    • (2005) Proteomics , vol.5 , pp. 865-875
    • Goldberg, D.1    Sutton-Smith, M.2    Paulson, J.3    Dell, A.4
  • 24
    • 84862168794 scopus 로고    scopus 로고
    • Structural analysis of N-and O-glycans released from glycoproteins
    • Jensen, P. H., Karlsson, N. G., Kolarich, D., Packer, N. H., Structural analysis of N-and O-glycans released from glycoproteins. Nat. Protoc. 2012, 7, 1299-1310.
    • (2012) Nat. Protoc. , vol.7 , pp. 1299-1310
    • Jensen, P.H.1    Karlsson, N.G.2    Kolarich, D.3    Packer, N.H.4
  • 25
    • 57749107717 scopus 로고    scopus 로고
    • Evolutionary differences in glycosaminoglycan fine structure detected by quantitative glycan reductive isotope labeling
    • Lawrence, R., Olson, S. K., Steele, R. E., Wang, L. et al., Evolutionary differences in glycosaminoglycan fine structure detected by quantitative glycan reductive isotope labeling. J. Biol. Chem. 2008, 283, 33674-33684.
    • (2008) J. Biol. Chem. , vol.283 , pp. 33674-33684
    • Lawrence, R.1    Olson, S.K.2    Steele, R.E.3    Wang, L.4
  • 27
    • 34548012656 scopus 로고    scopus 로고
    • Comparative glycomic mapping through quantitative permethylation and stable-isotope labeling
    • Kang, P., Mechref, Y., Kyselova, Z., Goetz, J. A., Novotny, M. V., Comparative glycomic mapping through quantitative permethylation and stable-isotope labeling. Anal. Chem. 2007, 79, 6064-6073.
    • (2007) Anal. Chem. , vol.79 , pp. 6064-6073
    • Kang, P.1    Mechref, Y.2    Kyselova, Z.3    Goetz, J.A.4    Novotny, M.V.5
  • 28
    • 34447312516 scopus 로고    scopus 로고
    • Tools for glycomics: relative quantitation of glycans by isotopic permethylation using 13CH3I
    • Alvarez-Manilla, G., Warren, N. L., Abney, T., Atwood, J. et al., Tools for glycomics: relative quantitation of glycans by isotopic permethylation using 13CH3I. Glycobiology 2007, 17, 677-687.
    • (2007) Glycobiology , vol.17 , pp. 677-687
    • Alvarez-Manilla, G.1    Warren, N.L.2    Abney, T.3    Atwood, J.4
  • 29
    • 84859900756 scopus 로고    scopus 로고
    • Carbonyl-reactive tandem mass tags for the proteome-wide quantification of N-linked glycans
    • Hahne, H., Neubert, P., Kuhn, K., Etienne, C. et al., Carbonyl-reactive tandem mass tags for the proteome-wide quantification of N-linked glycans. Anal. Chem. 2012, 84, 3716-3724.
    • (2012) Anal. Chem. , vol.84 , pp. 3716-3724
    • Hahne, H.1    Neubert, P.2    Kuhn, K.3    Etienne, C.4
  • 30
    • 84883468014 scopus 로고    scopus 로고
    • Glycan Analysis by isobaric aldehyde reactive tags and mass spectrometry
    • Yang, S., Yuan, W., Yang, W., Zhou, J. et al., Glycan Analysis by isobaric aldehyde reactive tags and mass spectrometry. Anal. Chem. 2013, 85, 8188-8195.
    • (2013) Anal. Chem. , vol.85 , pp. 8188-8195
    • Yang, S.1    Yuan, W.2    Yang, W.3    Zhou, J.4
  • 31
    • 34447097453 scopus 로고    scopus 로고
    • Analysis of protein glycosylation by mass spectrometry
    • Morelle, W., Michalski, J.-C., Analysis of protein glycosylation by mass spectrometry. Nat. Protoc. 2007, 2, 1585-1602.
    • (2007) Nat. Protoc. , vol.2 , pp. 1585-1602
    • Morelle, W.1    Michalski, J.-C.2
  • 32
    • 0026766923 scopus 로고
    • Analysis of carbohydrate-mediated heterogeneity and characterization of N-linked oligosaccharides of glycoproteins by high performance capillary electrophoresis
    • Taverna, M., Baillet, A., Biou, D., Schlüter, M. et al., Analysis of carbohydrate-mediated heterogeneity and characterization of N-linked oligosaccharides of glycoproteins by high performance capillary electrophoresis. Electrophoresis 1992, 13, 359-366.
    • (1992) Electrophoresis , vol.13 , pp. 359-366
    • Taverna, M.1    Baillet, A.2    Biou, D.3    Schlüter, M.4
  • 33
    • 84878652441 scopus 로고    scopus 로고
    • Glycomic analysis using glycoprotein immobilization for glycan extraction
    • Yang, S., Li, Y., Shah, P., Zhang, H., Glycomic analysis using glycoprotein immobilization for glycan extraction. Anal. Chem. 2013, 85, 5555-5561.
    • (2013) Anal. Chem. , vol.85 , pp. 5555-5561
    • Yang, S.1    Li, Y.2    Shah, P.3    Zhang, H.4
  • 34
    • 84863269972 scopus 로고    scopus 로고
    • Glycan analysis by reversible reaction to hydrazide beads and mass spectrometry
    • Yang, S., Zhang, H., Glycan analysis by reversible reaction to hydrazide beads and mass spectrometry. Anal. Chem. 2012, 84, 2232-2238.
    • (2012) Anal. Chem. , vol.84 , pp. 2232-2238
    • Yang, S.1    Zhang, H.2
  • 35
    • 84912573847 scopus 로고    scopus 로고
    • Imaging of N-linked glycans from formalin-fixed paraffin-embedded tissue sections using MALDI mass spectrometry
    • Toghi Eshghi, S., Yang, S., Wang, X., Shah, P. et al., Imaging of N-linked glycans from formalin-fixed paraffin-embedded tissue sections using MALDI mass spectrometry. ACS Chem. Biol. 2014, 9, 2149-2156.
    • (2014) ACS Chem. Biol. , vol.9 , pp. 2149-2156
    • Toghi Eshghi, S.1    Yang, S.2    Wang, X.3    Shah, P.4
  • 36
    • 84906965809 scopus 로고    scopus 로고
    • MALDI imaging mass spectrometry profiling of N-glycans in formalin-fixed paraffin embedded clinical tissue blocks and tissue microarrays
    • Powers, T. W., Neely, B. A., Shao, Y., Tang, H. et al., MALDI imaging mass spectrometry profiling of N-glycans in formalin-fixed paraffin embedded clinical tissue blocks and tissue microarrays. PLoS One 2014, 9, 1-11.
    • (2014) PLoS One , vol.9 , pp. 1-11
    • Powers, T.W.1    Neely, B.A.2    Shao, Y.3    Tang, H.4
  • 37
    • 23844499696 scopus 로고    scopus 로고
    • A rapid sample preparation method for mass spectrometric characterization of N-linked glycans
    • Yu, Y. Q., Gilar, M., Kaska, J., Gebler, J. C., A rapid sample preparation method for mass spectrometric characterization of N-linked glycans. Rapid Commun. Mass Spectrom. 2005, 19, 2331-2336.
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , pp. 2331-2336
    • Yu, Y.Q.1    Gilar, M.2    Kaska, J.3    Gebler, J.C.4
  • 38
    • 84885163658 scopus 로고    scopus 로고
    • The GlycoFilter: a simple and comprehensive sample preparation platform for proteomics, N-glycomics and glycosylation site assignment
    • Zhou, H., Froehlich, J. W., Briscoe, A. C., Lee, R. S., The GlycoFilter: a simple and comprehensive sample preparation platform for proteomics, N-glycomics and glycosylation site assignment. Mol. Cell. Proteomics 2013, 12, 2981-2991.
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 2981-2991
    • Zhou, H.1    Froehlich, J.W.2    Briscoe, A.C.3    Lee, R.S.4
  • 39
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wiśniewski, J. R., Zougman, A., Nagaraj, N., Mann, M., Universal sample preparation method for proteome analysis. Nat. Methods 2009, 6, 359-362.
    • (2009) Nat. Methods , vol.6 , pp. 359-362
    • Wiśniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 40
    • 79953292549 scopus 로고    scopus 로고
    • Cotton HILIC SPE microtips for microscale purification and enrichment of glycans and glycopeptides
    • Selman, M. H., Hemayatkar, M., Deelder, A. M., Wuhrer, M., Cotton HILIC SPE microtips for microscale purification and enrichment of glycans and glycopeptides. Anal. Chem. 2011, 83, 2492-2499.
    • (2011) Anal. Chem. , vol.83 , pp. 2492-2499
    • Selman, M.H.1    Hemayatkar, M.2    Deelder, A.M.3    Wuhrer, M.4
  • 41
    • 84857869147 scopus 로고    scopus 로고
    • Annotation of a serum N-glycan library for rapid identification of structures
    • Aldredge, D., An, H. J., Tang, N., Waddell, K., Lebrilla, C. B., Annotation of a serum N-glycan library for rapid identification of structures. J. Proteome Res. 2012, 11, 1958-1968.
    • (2012) J. Proteome Res. , vol.11 , pp. 1958-1968
    • Aldredge, D.1    An, H.J.2    Tang, N.3    Waddell, K.4    Lebrilla, C.B.5
  • 42
    • 33745913025 scopus 로고    scopus 로고
    • Profiling of glycans in serum for the discovery of potential biomarkers for ovarian cancer
    • An, H. J., Miyamoto, S., Lancaster, K. S., Kirmiz, C. et al., Profiling of glycans in serum for the discovery of potential biomarkers for ovarian cancer. J. Proteome Res. 2006, 5, 1626-1635.
    • (2006) J. Proteome Res. , vol.5 , pp. 1626-1635
    • An, H.J.1    Miyamoto, S.2    Lancaster, K.S.3    Kirmiz, C.4
  • 43
  • 44
    • 0027441378 scopus 로고
    • Use of hydrazine to release in intact and unreduced form both N-and O-linked oligosaccharides from glycoproteins
    • Patel, T., Bruce, J., Merry, A., Bigge, C. et al., Use of hydrazine to release in intact and unreduced form both N-and O-linked oligosaccharides from glycoproteins. Biochemistry 1993, 32, 679-693.
    • (1993) Biochemistry , vol.32 , pp. 679-693
    • Patel, T.1    Bruce, J.2    Merry, A.3    Bigge, C.4
  • 45
    • 33846542649 scopus 로고    scopus 로고
    • A serum glycomics approach to breast cancer biomarkers
    • Kirmiz, C., Li, B., An, H. J., Clowers, B. H. et al., A serum glycomics approach to breast cancer biomarkers. Mol. Cell. Proteomics 2007, 6, 43-55.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 43-55
    • Kirmiz, C.1    Li, B.2    An, H.J.3    Clowers, B.H.4
  • 46
    • 18844434899 scopus 로고    scopus 로고
    • Structural determination of N-linked glycans by matrix-assisted laser desorption/ionization and electrospray ionization mass spectrometry
    • Harvey, D. J., Structural determination of N-linked glycans by matrix-assisted laser desorption/ionization and electrospray ionization mass spectrometry. Proteomics 2005, 5, 1774-1786.
    • (2005) Proteomics , vol.5 , pp. 1774-1786
    • Harvey, D.J.1
  • 47
  • 48
    • 0029741839 scopus 로고    scopus 로고
    • Stabilization of sialic acids in N-linked oligosaccharides and gangliosides for analysis by positive ion matrix-assisted laser desorption/ionization mass spectrometry
    • Powell, A. K., Harvey, D. J., Stabilization of sialic acids in N-linked oligosaccharides and gangliosides for analysis by positive ion matrix-assisted laser desorption/ionization mass spectrometry. Rapid Commun. Mass Spectrom. 1996, 10, 1027-1032.
    • (1996) Rapid Commun. Mass Spectrom. , vol.10 , pp. 1027-1032
    • Powell, A.K.1    Harvey, D.J.2
  • 49
    • 22044456565 scopus 로고    scopus 로고
    • Glycoproteomics of N-glycosylation by in-gel deglycosylation and matrix-assisted laser desorption/ionisation-time of flight mass spectrometry mapping: Application to congenital disorders of glycosylation
    • Šagi, D., Kienz, P., Denecke, J., Marquardt, T., Peter-Katalinić, J., Glycoproteomics of N-glycosylation by in-gel deglycosylation and matrix-assisted laser desorption/ionisation-time of flight mass spectrometry mapping: Application to congenital disorders of glycosylation. Proteomics 2005, 5, 2689-2701.
    • (2005) Proteomics , vol.5 , pp. 2689-2701
    • Šagi, D.1    Kienz, P.2    Denecke, J.3    Marquardt, T.4    Peter-Katalinić, J.5
  • 50
    • 33846590457 scopus 로고    scopus 로고
    • Effect of glycosylation on the protein pattern in 2-D-gel electrophoresis
    • Kleinert, P., Kuster, T., Arnold, D., Jaeken, J. et al., Effect of glycosylation on the protein pattern in 2-D-gel electrophoresis. Proteomics 2007, 7, 15-22.
    • (2007) Proteomics , vol.7 , pp. 15-22
    • Kleinert, P.1    Kuster, T.2    Arnold, D.3    Jaeken, J.4
  • 51
    • 57049137606 scopus 로고    scopus 로고
    • A strategy to reveal potential glycan markers from serum glycoproteins associated with breast cancer progression
    • Hamid, U. M. A., Royle, L., Saldova, R., Radcliffe, C. M. et al., A strategy to reveal potential glycan markers from serum glycoproteins associated with breast cancer progression. Glycobiology 2008, 18, 1105-1118.
    • (2008) Glycobiology , vol.18 , pp. 1105-1118
    • Hamid, U.M.A.1    Royle, L.2    Saldova, R.3    Radcliffe, C.M.4
  • 52
    • 0031571138 scopus 로고    scopus 로고
    • Sequencing of N-linked oligosaccharides directly from protein gels: in-gel deglycosylation followed by matrix-assisted laser desorption/ionization mass spectrometry and normal-phase high-performance liquid chromatography
    • Küster, B., Wheeler, S. F., Hunter, A. P., Dwek, R. A., Harvey, D. J., Sequencing of N-linked oligosaccharides directly from protein gels: in-gel deglycosylation followed by matrix-assisted laser desorption/ionization mass spectrometry and normal-phase high-performance liquid chromatography. Anal. Biochem. 1997, 250, 82-101.
    • (1997) Anal. Biochem. , vol.250 , pp. 82-101
    • Küster, B.1    Wheeler, S.F.2    Hunter, A.P.3    Dwek, R.A.4    Harvey, D.J.5
  • 54
    • 0036874367 scopus 로고    scopus 로고
    • Sequential analysis of N-and O-linked glycosylation of 2D-PAGE separated glycoproteins
    • Wilson, N. L., Schulz, B. L., Karlsson, N. G., Packer, N. H., Sequential analysis of N-and O-linked glycosylation of 2D-PAGE separated glycoproteins. J. Proteome Res. 2002, 1, 521-529.
    • (2002) J. Proteome Res. , vol.1 , pp. 521-529
    • Wilson, N.L.1    Schulz, B.L.2    Karlsson, N.G.3    Packer, N.H.4
  • 55
    • 34347346201 scopus 로고    scopus 로고
    • Protein immobilization strategies for protein biochips
    • Rusmini, F., Zhong, Z., Feijen, J., Protein immobilization strategies for protein biochips. Biomacromolecules 2007, 8, 1775-1789.
    • (2007) Biomacromolecules , vol.8 , pp. 1775-1789
    • Rusmini, F.1    Zhong, Z.2    Feijen, J.3
  • 56
    • 0031269226 scopus 로고    scopus 로고
    • Immobilization of protein molecules onto homogeneous and mixed carboxylate-terminated self-assembled monolayers
    • Patel, N., Davies, M. C., Hartshorne, M., Heaton, R. J. et al., Immobilization of protein molecules onto homogeneous and mixed carboxylate-terminated self-assembled monolayers. Langmuir 1997, 13, 6485-6490.
    • (1997) Langmuir , vol.13 , pp. 6485-6490
    • Patel, N.1    Davies, M.C.2    Hartshorne, M.3    Heaton, R.J.4
  • 57
    • 0025944815 scopus 로고
    • Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors
    • Johnsson, B., Löfås, S., Lindquist, G., Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors. Anal. Biochem. 1991, 198, 268-277.
    • (1991) Anal. Biochem. , vol.198 , pp. 268-277
    • Johnsson, B.1    Löfås, S.2    Lindquist, G.3
  • 58
    • 33745488964 scopus 로고    scopus 로고
    • Immobilization of proteins on agarose beads, monitored in real time by bead injection spectroscopy
    • Ruzicka, J., Carroll, A. D., Lähdesmäki, I., Immobilization of proteins on agarose beads, monitored in real time by bead injection spectroscopy. Analyst 2006, 131, 799-808.
    • (2006) Analyst , vol.131 , pp. 799-808
    • Ruzicka, J.1    Carroll, A.D.2    Lähdesmäki, I.3
  • 59
    • 84887688118 scopus 로고    scopus 로고
    • Glycomic analysis by glycoprotein immoblization for glycan extraction and liquid chromatography on mcirofluidic chip
    • Yang, S., Toghi Eshighi, S., Chiu, H., DeVoe, D., Zhang, H., Glycomic analysis by glycoprotein immoblization for glycan extraction and liquid chromatography on mcirofluidic chip. Anal. Chem. 2013, 85, 10117-10125.
    • (2013) Anal. Chem. , vol.85 , pp. 10117-10125
    • Yang, S.1    Toghi Eshighi, S.2    Chiu, H.3    DeVoe, D.4    Zhang, H.5
  • 60
    • 62649124791 scopus 로고    scopus 로고
    • Protein immobilization on epoxy-activated thin polymer films: effect of surface wettability and enzyme loading
    • Chen, B., Pernodet, N., Rafailovich, M. H., Bakhtina, A., Gross, R. A., Protein immobilization on epoxy-activated thin polymer films: effect of surface wettability and enzyme loading. Langmuir 2008, 24, 13457-13464.
    • (2008) Langmuir , vol.24 , pp. 13457-13464
    • Chen, B.1    Pernodet, N.2    Rafailovich, M.H.3    Bakhtina, A.4    Gross, R.A.5
  • 61
    • 0942279584 scopus 로고    scopus 로고
    • Protein immobilization on carbon nanotubes via a two-step process of diimide-activated amidation
    • Jiang, K., Schadler, L. S., Siegel, R. W., Zhang, X. et al., Protein immobilization on carbon nanotubes via a two-step process of diimide-activated amidation. J. Mater. Chem. 2004, 14, 37-39.
    • (2004) J. Mater. Chem. , vol.14 , pp. 37-39
    • Jiang, K.1    Schadler, L.S.2    Siegel, R.W.3    Zhang, X.4
  • 62
    • 0033740123 scopus 로고    scopus 로고
    • Protein immobilization to a partially cross-linked organic monolayer
    • Viitala, T., Vikholm, I., Peltonen, J., Protein immobilization to a partially cross-linked organic monolayer. Langmuir 2000, 16, 4953-4961.
    • (2000) Langmuir , vol.16 , pp. 4953-4961
    • Viitala, T.1    Vikholm, I.2    Peltonen, J.3
  • 63
    • 4644243451 scopus 로고    scopus 로고
    • Engineering surfaces for bioconjugation: developing strategies and quantifying the extent of the reactions
    • Gauvreau, V., Chevallier, P., Vallières, K., Petitclerc, É. et al., Engineering surfaces for bioconjugation: developing strategies and quantifying the extent of the reactions. Bioconjugate Chem. 2004, 15, 1146-1156.
    • (2004) Bioconjugate Chem. , vol.15 , pp. 1146-1156
    • Gauvreau, V.1    Chevallier, P.2    Vallières, K.3    Petitclerc, E.4
  • 64
    • 33646755397 scopus 로고    scopus 로고
    • Self-assembling protein arrays on DNA chips by auto-labeling fusion proteins with a single DNA address
    • Jongsma, M. A., Litjens, R. H., Self-assembling protein arrays on DNA chips by auto-labeling fusion proteins with a single DNA address. Proteomics 2006, 6, 2650-2655.
    • (2006) Proteomics , vol.6 , pp. 2650-2655
    • Jongsma, M.A.1    Litjens, R.H.2
  • 65
    • 0037418506 scopus 로고    scopus 로고
    • Maleimide-functionalized self-assembled monolayers for the preparation of peptide and carbohydrate biochips
    • Houseman, B. T., Gawalt, E. S., Mrksich, M., Maleimide-functionalized self-assembled monolayers for the preparation of peptide and carbohydrate biochips. Langmuir 2003, 19, 1522-1531.
    • (2003) Langmuir , vol.19 , pp. 1522-1531
    • Houseman, B.T.1    Gawalt, E.S.2    Mrksich, M.3
  • 66
    • 77951275912 scopus 로고    scopus 로고
    • Synthesis of pyridyl disulfide-functionalized nanoparticles for conjugating thiol-containing small molecules, peptides, and proteins
    • van der Vlies, A. J., O'Neil, C. P., Hasegawa, U., Hammond, N., Hubbell, J. A., Synthesis of pyridyl disulfide-functionalized nanoparticles for conjugating thiol-containing small molecules, peptides, and proteins. Bioconjugate Chem. 2010, 21, 653-662.
    • (2010) Bioconjugate Chem. , vol.21 , pp. 653-662
    • van der Vlies, A.J.1    O'Neil, C.P.2    Hasegawa, U.3    Hammond, N.4    Hubbell, J.A.5
  • 67
    • 11944251666 scopus 로고
    • 48000-fold acceleration of hybridization by chemically modified oligonucleotides
    • Corey, D. R., 48000-fold acceleration of hybridization by chemically modified oligonucleotides. J. Am. Chem. Soc. 1995, 117, 9373-9374.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 9373-9374
    • Corey, D.R.1
  • 69
    • 0027627662 scopus 로고
    • Preparation of activated supports containing low pK amino groups. A new tool for protein immobilization via the carboxyl coupling method
    • Fernandez-Lafuente, R., Rosell, C., Rodriguez, V., Santana, C. et al., Preparation of activated supports containing low pK amino groups. A new tool for protein immobilization via the carboxyl coupling method. Enzyme Microb. Tech. 1993, 15, 546-550.
    • (1993) Enzyme Microb. Tech. , vol.15 , pp. 546-550
    • Fernandez-Lafuente, R.1    Rosell, C.2    Rodriguez, V.3    Santana, C.4
  • 70
    • 0344394382 scopus 로고    scopus 로고
    • Novel bifunctional epoxy/thiol-reactive support to immobilize thiol containing proteins by the epoxy chemistry
    • Grazú, V., Abian, O., Mateo, C., Batista-Viera, F. et al., Novel bifunctional epoxy/thiol-reactive support to immobilize thiol containing proteins by the epoxy chemistry. Biomacromolecules 2003, 4, 1495-1501.
    • (2003) Biomacromolecules , vol.4 , pp. 1495-1501
    • Grazú, V.1    Abian, O.2    Mateo, C.3    Batista-Viera, F.4
  • 71
    • 84927565834 scopus 로고    scopus 로고
    • Glycomic Analysis of Glycans Released from Glycoproteins Using Chemical Immobilization and Mass Spectrometry
    • Yang, S., Zhang, H., Glycomic Analysis of Glycans Released from Glycoproteins Using Chemical Immobilization and Mass Spectrometry. Curr. Protoc. Chem. Biol. 2015, 191-208.
    • (2015) Curr. Protoc. Chem. Biol. , pp. 191-208
    • Yang, S.1    Zhang, H.2
  • 72
    • 84875773658 scopus 로고    scopus 로고
    • Mass spectrometric analysis of sialylated glycans with use of solid-phase labeling of sialic acids
    • Shah, P., Yang, S., Sun, S., Aiyetan, P. et al., Mass spectrometric analysis of sialylated glycans with use of solid-phase labeling of sialic acids. Anal. Chem. 2013, 85, 3606-3613.
    • (2013) Anal. Chem. , vol.85 , pp. 3606-3613
    • Shah, P.1    Yang, S.2    Sun, S.3    Aiyetan, P.4
  • 74
    • 84871438500 scopus 로고    scopus 로고
    • Solid-phase glycan isolation for glycomics analysis
    • Yang, S., Zhang, H., Solid-phase glycan isolation for glycomics analysis. Protoemics Clin. Appl. 2012, 6, 596-608.
    • (2012) Protoemics Clin. Appl. , vol.6 , pp. 596-608
    • Yang, S.1    Zhang, H.2
  • 75
    • 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.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 660-666
    • Zhang, H.1    Li, X.-j.2    Martin, D.B.3    Aebersold, R.4
  • 76
    • 57549096380 scopus 로고    scopus 로고
    • Manipulating replication processes within a dynamic covalent framework
    • del Amo, V., Slawin, A. M., Philp, D., Manipulating replication processes within a dynamic covalent framework. Org. Lett. 2008, 10, 4589-4592.
    • (2008) Org. Lett. , vol.10 , pp. 4589-4592
    • del Amo, V.1    Slawin, A.M.2    Philp, D.3
  • 77
    • 80053305894 scopus 로고    scopus 로고
    • Promoting peptide α-helix formation with dynamic covalent oxime side-chain cross-links
    • SetháHorne, W., Promoting peptide α-helix formation with dynamic covalent oxime side-chain cross-links. Chem. Commun. 2011, 47, 10915-10917.
    • (2011) Chem. Commun. , vol.47 , pp. 10915-10917
    • SetháHorne, W.1
  • 78
    • 84886893246 scopus 로고    scopus 로고
    • Matrix assisted laser desorption ionization imaging mass spectrometry workflow for spatial profiling analysis of N-linked glycan expression in tissues
    • Powers, T. W., Jones, E. E., Betesh, L. R., Romano, P. R. et al., Matrix assisted laser desorption ionization imaging mass spectrometry workflow for spatial profiling analysis of N-linked glycan expression in tissues. Anal. Chem. 2013, 85, 9799-9806.
    • (2013) Anal. Chem. , vol.85 , pp. 9799-9806
    • Powers, T.W.1    Jones, E.E.2    Betesh, L.R.3    Romano, P.R.4
  • 79
    • 43249099890 scopus 로고    scopus 로고
    • In vivo imaging of membrane-associated glycans in developing zebrafish
    • Laughlin, S. T., Baskin, J. M., Amacher, S. L., Bertozzi, C. R., In vivo imaging of membrane-associated glycans in developing zebrafish. Science 2008, 320, 664-667.
    • (2008) Science , vol.320 , pp. 664-667
    • Laughlin, S.T.1    Baskin, J.M.2    Amacher, S.L.3    Bertozzi, C.R.4
  • 80
    • 73649129882 scopus 로고    scopus 로고
    • In vivo imaging of Caenorhabditis elegans glycans
    • Laughlin, S. T., Bertozzi, C. R., In vivo imaging of Caenorhabditis elegans glycans. ACS Chem. Biol. 2009, 4, 1068-1072.
    • (2009) ACS Chem. Biol. , vol.4 , pp. 1068-1072
    • Laughlin, S.T.1    Bertozzi, C.R.2
  • 81
    • 84956595017 scopus 로고    scopus 로고
    • in: Varki, A., Cummings, R. D., Esko, J. D., Freeze, H. H., Eds.), Cold Spring Harbor Laboratory Press, New York
    • Varki, A., in: Varki, A., Cummings, R. D., Esko, J. D., Freeze, H. H. et al., (Eds.), N-glycans, Cold Spring Harbor Laboratory Press, New York 2009, pp. 633-648.
    • (2009) N-glycans , pp. 633-648
    • Varki, A.1
  • 82
    • 77956931053 scopus 로고    scopus 로고
    • A systematic approach to protein glycosylation analysis: a path through the maze
    • Mariño, K., Bones, J., Kattla, J. J., Rudd, P. M., A systematic approach to protein glycosylation analysis: a path through the maze. Nat. Chem. Biol. 2010, 6, 713-723.
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 713-723
    • Mariño, K.1    Bones, J.2    Kattla, J.J.3    Rudd, P.M.4
  • 83
    • 0030571019 scopus 로고    scopus 로고
    • A rapid high-resolution high-performance liquid chromatographic method for separating glycan mixtures and analyzing oligosaccharide profiles
    • Guile, G. R., Rudd, P. M., Wing, D. R., Prime, S. B., Dwek, R. A., A rapid high-resolution high-performance liquid chromatographic method for separating glycan mixtures and analyzing oligosaccharide profiles. Anal. Biochem. 1996, 240, 210-226.
    • (1996) Anal. Biochem. , vol.240 , pp. 210-226
    • Guile, G.R.1    Rudd, P.M.2    Wing, D.R.3    Prime, S.B.4    Dwek, R.A.5
  • 84
    • 0032432970 scopus 로고    scopus 로고
    • Practice and mechanism of HPLC oligosaccharide separation with a cyclodextrin bonded phase
    • Berthod, A., Chang, S. S., Kullman, J. P., Armstrong, D. W., Practice and mechanism of HPLC oligosaccharide separation with a cyclodextrin bonded phase. Talanta 1998, 47, 1001-1012.
    • (1998) Talanta , vol.47 , pp. 1001-1012
    • Berthod, A.1    Chang, S.S.2    Kullman, J.P.3    Armstrong, D.W.4
  • 85
    • 0344239773 scopus 로고    scopus 로고
    • Glycosylation differences between the normal and pathogenic prion protein isoforms
    • Rudd, P. M., Endo, T., Colominas, C., Groth, D. et al., Glycosylation differences between the normal and pathogenic prion protein isoforms. Proc. Natl. Acad. Sci. 1999, 96, 13044-13049.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 13044-13049
    • Rudd, P.M.1    Endo, T.2    Colominas, C.3    Groth, D.4
  • 86
    • 79953704533 scopus 로고    scopus 로고
    • Novel glycan biomarkers for the detection of lung cancer
    • Arnold, J. N., Saldova, R., Galligan, M. C., Murphy, T. B. et al., Novel glycan biomarkers for the detection of lung cancer. J. Proteome Res. 2011, 10, 1755-1764.
    • (2011) J. Proteome Res. , vol.10 , pp. 1755-1764
    • Arnold, J.N.1    Saldova, R.2    Galligan, M.C.3    Murphy, T.B.4
  • 87
    • 79952389488 scopus 로고    scopus 로고
    • Glycomic and glycoproteomic analysis of serum from patients with stomach cancer reveals potential markers arising from host defense response mechanisms
    • Bones, J., Byrne, J. C., O'Donoghue, N., McManus, C. et al., Glycomic and glycoproteomic analysis of serum from patients with stomach cancer reveals potential markers arising from host defense response mechanisms. J. Proteome Res. 2010, 10, 1246-1265.
    • (2010) J. Proteome Res. , vol.10 , pp. 1246-1265
    • Bones, J.1    Byrne, J.C.2    O'Donoghue, N.3    McManus, C.4
  • 88
    • 84883420677 scopus 로고    scopus 로고
    • Increase in sialylation and branching in the mouse serum N-glycome correlates with inflammation and ovarian tumour progression
    • 1-e71159,10.
    • Saldova, R., Piccard, H., Pérez-Garay, M., Harvey, D. J. et al., Increase in sialylation and branching in the mouse serum N-glycome correlates with inflammation and ovarian tumour progression. PLOS ONE 2013, 8, e71159, 1-10.
    • (2013) PLOS ONE , vol.8 , pp. e71159
    • Saldova, R.1    Piccard, H.2    Pérez-Garay, M.3    Harvey, D.J.4
  • 89
    • 78650351800 scopus 로고    scopus 로고
    • Ultra performance liquid chromatographic profiling of serum N-glycans for fast and efficient identification of cancer associated alterations in glycosylation
    • Bones, J., Mittermayr, S., O'Donoghue, N., Guttman, A. s., Rudd, P. M., Ultra performance liquid chromatographic profiling of serum N-glycans for fast and efficient identification of cancer associated alterations in glycosylation. Anal. Chem. 2010, 82, 10208-10215.
    • (2010) Anal. Chem. , vol.82 , pp. 10208-10215
    • Bones, J.1    Mittermayr, S.2    O'Donoghue, N.3    Guttman, A.s.4    Rudd, P.M.5
  • 90
    • 0034664035 scopus 로고    scopus 로고
    • APCI-MS/MS: A powerful tool for the analysis of bound residues resulting from the interaction of pesticides with DOM and humic substances
    • Klaus, U., Pfeifer, T., Spiteller, M., APCI-MS/MS: A powerful tool for the analysis of bound residues resulting from the interaction of pesticides with DOM and humic substances. Environ. Sci. Technol. 2000, 34, 3514-3520.
    • (2000) Environ. Sci. Technol. , vol.34 , pp. 3514-3520
    • Klaus, U.1    Pfeifer, T.2    Spiteller, M.3
  • 91
    • 83055182135 scopus 로고    scopus 로고
    • Evaluation of HCD-and CID-type fragmentation within their respective detection platforms for murine phosphoproteomics
    • M111. 009910
    • Jedrychowski, M. P., Huttlin, E. L., Haas, W., Sowa, M. E. et al., Evaluation of HCD-and CID-type fragmentation within their respective detection platforms for murine phosphoproteomics. Mol. Cell. Proteomics 2011, 10, M111. 009910, 1-9.
    • (2011) Mol. Cell. Proteomics , vol.10 , pp. 1-9
    • Jedrychowski, M.P.1    Huttlin, E.L.2    Haas, W.3    Sowa, M.E.4
  • 92
    • 79953174969 scopus 로고    scopus 로고
    • Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-linked glycoproteome of Campylobacter jejuni
    • M000031-MCP000201
    • Scott, N. E., Parker, B. L., Connolly, A. M., Paulech, J. et al., Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-linked glycoproteome of Campylobacter jejuni. Mol. Cell. Proteomics 2011, 10, M000031-MCP000201.
    • (2011) Mol. Cell. Proteomics , vol.10
    • Scott, N.E.1    Parker, B.L.2    Connolly, A.M.3    Paulech, J.4
  • 93
    • 45549094069 scopus 로고    scopus 로고
    • GlycoWorkbench: a tool for the computer-assisted annotation of mass spectra of glycans†
    • Ceroni, A., Maass, K., Geyer, H., Geyer, R. et al., GlycoWorkbench: a tool for the computer-assisted annotation of mass spectra of glycans†. J. Proteome Res. 2008, 7, 1650-1659.
    • (2008) J. Proteome Res. , vol.7 , pp. 1650-1659
    • Ceroni, A.1    Maass, K.2    Geyer, H.3    Geyer, R.4
  • 94
    • 84892432247 scopus 로고    scopus 로고
    • SimGlycan™ Software*: a new predictive carbohydrate analysis tool for MS/MS data
    • Albanese, J., Glueckmann, M., Lenz, C., SimGlycan™ Software*: a new predictive carbohydrate analysis tool for MS/MS data. Appl. Biosyst. 2010, p1-p7.
    • (2010) Appl. Biosyst. , pp. p1-p7
    • Albanese, J.1    Glueckmann, M.2    Lenz, C.3
  • 95
    • 80054696065 scopus 로고    scopus 로고
    • Size-selective enrichment of N-linked glycans using highly ordered Mesoporous carbon material and detection by MALDI-TOF MS
    • Qin, H., Zhao, L., Li, R., Wu, R. a., Zou, H., Size-selective enrichment of N-linked glycans using highly ordered Mesoporous carbon material and detection by MALDI-TOF MS. Anal. Chem. 2011, 83, 7721-7728.
    • (2011) Anal. Chem. , vol.83 , pp. 7721-7728
    • Qin, H.1    Zhao, L.2    Li, R.3    Wu, R.A.4    Zou, H.5
  • 96
    • 34250313689 scopus 로고    scopus 로고
    • Rapid and Simple Solid-Phase Esterification of Sialic Acid Residues for Quantitative Glycomics by Mass Spectrometry
    • Miura, Y., Shinohara, Y., Furukawa, J., Nagahori, N., Nishimura, S. I., Rapid and Simple Solid-Phase Esterification of Sialic Acid Residues for Quantitative Glycomics by Mass Spectrometry. Chem. Eur. J. 2007, 13, 4797-4804.
    • (2007) Chem. Eur. J. , vol.13 , pp. 4797-4804
    • Miura, Y.1    Shinohara, Y.2    Furukawa, J.3    Nagahori, N.4    Nishimura, S.I.5
  • 97
    • 48349127752 scopus 로고    scopus 로고
    • On the use of DHB/aniline and DHB/N, N-dimethylaniline matrices for improved detection of carbohydrates: automated identification of oligosaccharides and quantitative analysis of sialylated glycans by MALDI-TOF mass spectrometry
    • Snovida, S. I., Rak-Banville, J. M., Perreault, H., On the use of DHB/aniline and DHB/N, N-dimethylaniline matrices for improved detection of carbohydrates: automated identification of oligosaccharides and quantitative analysis of sialylated glycans by MALDI-TOF mass spectrometry. J. Am. Soc. Mass Spectrom. 2008, 19, 1138-1146.
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 1138-1146
    • Snovida, S.I.1    Rak-Banville, J.M.2    Perreault, H.3
  • 98
    • 0025012287 scopus 로고
    • Isolation and separation of the glycan strands from murein of Escherichia coli by reversed-phase high-performance liquid chromatography
    • Harz, H., Burgdorf, K., Höltje, J.-V., Isolation and separation of the glycan strands from murein of Escherichia coli by reversed-phase high-performance liquid chromatography. Anal. Biochem. 1990, 190, 120-128.
    • (1990) Anal. Biochem. , vol.190 , pp. 120-128
    • Harz, H.1    Burgdorf, K.2    Höltje, J.-V.3
  • 99
    • 65349151261 scopus 로고    scopus 로고
    • Profile of native N-linked glycan structures from human serum using high performance liquid chromatography on a microfluidic chip and time-of-flight mass spectrometry
    • Chu, C. S., Niñonuevo, M. R., Clowers, B. H., Perkins, P. D. et al., Profile of native N-linked glycan structures from human serum using high performance liquid chromatography on a microfluidic chip and time-of-flight mass spectrometry. Proteomics 2009, 9, 1939-1951.
    • (2009) Proteomics , vol.9 , pp. 1939-1951
    • Chu, C.S.1    Niñonuevo, M.R.2    Clowers, B.H.3    Perkins, P.D.4
  • 100
    • 80052236392 scopus 로고    scopus 로고
    • Comprehensive native glycan profiling with isomer separation and quantitation for the discovery of cancer biomarkers
    • Hua, S., An, H. J., Ozcan, S., Ro, G. S. et al., Comprehensive native glycan profiling with isomer separation and quantitation for the discovery of cancer biomarkers. Analyst 2011, 136, 3663-3671.
    • (2011) Analyst , vol.136 , pp. 3663-3671
    • Hua, S.1    An, H.J.2    Ozcan, S.3    Ro, G.S.4
  • 101
    • 33749990332 scopus 로고    scopus 로고
    • Capillary electrophoresis with laser-induced fluorescence detection for detailed studies on N-linked oligosaccharide profile of therapeutic recombinant monoclonal antibodies
    • Kamoda, S., Ishikawa, R., Kakehi, K., Capillary electrophoresis with laser-induced fluorescence detection for detailed studies on N-linked oligosaccharide profile of therapeutic recombinant monoclonal antibodies. J. Chromatogr. A 2006, 1133, 332-339.
    • (2006) J. Chromatogr. A , vol.1133 , pp. 332-339
    • Kamoda, S.1    Ishikawa, R.2    Kakehi, K.3
  • 102
    • 79551499066 scopus 로고    scopus 로고
    • Glycan analysis by modern instrumental methods
    • Pabst, M., Altmann, F., Glycan analysis by modern instrumental methods. Proteomics 2011, 11, 631-643.
    • (2011) Proteomics , vol.11 , pp. 631-643
    • Pabst, M.1    Altmann, F.2
  • 103
    • 58149347362 scopus 로고    scopus 로고
    • Capillary electrophoresis-electrospray ionization mass spectrometry for rapid and sensitive N-glycan analysis of glycoproteins as 9-fluorenylmethyl derivatives
    • Nakano, M., Higo, D., Arai, E., Nakagawa, T. et al., Capillary electrophoresis-electrospray ionization mass spectrometry for rapid and sensitive N-glycan analysis of glycoproteins as 9-fluorenylmethyl derivatives. Glycobiology 2009, 19, 135-143.
    • (2009) Glycobiology , vol.19 , pp. 135-143
    • Nakano, M.1    Higo, D.2    Arai, E.3    Nakagawa, T.4
  • 104
    • 77951151811 scopus 로고    scopus 로고
    • Improved sample preparation method for glycan analysis of glycoproteins by CE-LIF and CE-MS
    • Szabo, Z., Guttman, A., Rejtar, T., Karger, B. L., Improved sample preparation method for glycan analysis of glycoproteins by CE-LIF and CE-MS. Electrophoresis 2010, 31, 1389-1395.
    • (2010) Electrophoresis , vol.31 , pp. 1389-1395
    • Szabo, Z.1    Guttman, A.2    Rejtar, T.3    Karger, B.L.4
  • 105
    • 77953853129 scopus 로고    scopus 로고
    • 2-picoline-borane: A non-toxic reducing agent for oligosaccharide labeling by reductive amination
    • Ruhaak, L. R., Steenvoorden, E., Koeleman, C. A., Deelder, A. M., Wuhrer, M., 2-picoline-borane: A non-toxic reducing agent for oligosaccharide labeling by reductive amination. Proteomics 2010, 10, 2330-2336.
    • (2010) Proteomics , vol.10 , pp. 2330-2336
    • Ruhaak, L.R.1    Steenvoorden, E.2    Koeleman, C.A.3    Deelder, A.M.4    Wuhrer, M.5
  • 106
    • 38549168031 scopus 로고    scopus 로고
    • Detection of carbohydrates using new labeling reagent 1-(2-naphthyl)-3-methyl-5-pyrazolone by capillary zone electrophoresis with absorbance (UV)
    • You, J., Sheng, X., Ding, C., Sun, Z. et al., Detection of carbohydrates using new labeling reagent 1-(2-naphthyl)-3-methyl-5-pyrazolone by capillary zone electrophoresis with absorbance (UV). Anal. Chim. Acta 2008, 609, 66-75.
    • (2008) Anal. Chim. Acta , vol.609 , pp. 66-75
    • You, J.1    Sheng, X.2    Ding, C.3    Sun, Z.4
  • 107
    • 77956062358 scopus 로고    scopus 로고
    • Glycan labeling strategies and their use in identification and quantification
    • Ruhaak, L., Zauner, G., Huhn, C., Bruggink, C. et al., Glycan labeling strategies and their use in identification and quantification. Anal. Bioanal. Chem. 2010, 397, 3457-3481.
    • (2010) Anal. Bioanal. Chem. , vol.397 , pp. 3457-3481
    • Ruhaak, L.1    Zauner, G.2    Huhn, C.3    Bruggink, C.4
  • 108
    • 3543121341 scopus 로고    scopus 로고
    • Quantification in proteomics through stable isotope coding: a review
    • Julka, S., Regnier, F., Quantification in proteomics through stable isotope coding: a review. J. Proteome Res. 2004, 3, 350-363.
    • (2004) J. Proteome Res. , vol.3 , pp. 350-363
    • Julka, S.1    Regnier, F.2
  • 109
    • 0037307837 scopus 로고    scopus 로고
    • Stable isotope-coded proteomic mass spectrometry
    • Goshe, M. B., Smith, R. D., Stable isotope-coded proteomic mass spectrometry. Curr. Opin. Biotechnol. 2003, 14, 101-109.
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 101-109
    • Goshe, M.B.1    Smith, R.D.2
  • 110
    • 0037307816 scopus 로고    scopus 로고
    • Advances in quantitative proteomics via stable isotope tagging and mass spectrometry
    • Tao, W. A., Aebersold, R., Advances in quantitative proteomics via stable isotope tagging and mass spectrometry. Curr. Opin. Biotechnol. 2003, 14, 110-118.
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 110-118
    • Tao, W.A.1    Aebersold, R.2
  • 111
    • 68549133585 scopus 로고    scopus 로고
    • IDAWG: metabolic incorporation of stable isotope labels for quantitative glycomics of cultured cells
    • Orlando, R., Lim, J.-M., Atwood III, J. A., Angel, P. M. et al., IDAWG: metabolic incorporation of stable isotope labels for quantitative glycomics of cultured cells. J. Proteome Res. 2009, 8, 3816-3823.
    • (2009) J. Proteome Res. , vol.8 , pp. 3816-3823
    • Orlando, R.1    Lim, J.-M.2    Atwood, J.A.3    Angel, P.M.4
  • 112
    • 80052327326 scopus 로고    scopus 로고
    • Stable-isotope labeled hydrophobic hydrazide reagents for the relative quantification of N-linked glycans by electrospray ionization mass spectrometry
    • Walker, S. H., Budhathoki-Uprety, J., Novak, B. M., Muddiman, D. C., Stable-isotope labeled hydrophobic hydrazide reagents for the relative quantification of N-linked glycans by electrospray ionization mass spectrometry. Anal. Chem. 2011, 83, 6738-6745.
    • (2011) Anal. Chem. , vol.83 , pp. 6738-6745
    • Walker, S.H.1    Budhathoki-Uprety, J.2    Novak, B.M.3    Muddiman, D.C.4
  • 113
    • 34547767471 scopus 로고    scopus 로고
    • Tags for the stable isotopic labeling of carbohydrates and quantitative analysis by mass spectrometry
    • Bowman, M. J., Zaia, J., Tags for the stable isotopic labeling of carbohydrates and quantitative analysis by mass spectrometry. Anal. Chem. 2007, 79, 5777-5784.
    • (2007) Anal. Chem. , vol.79 , pp. 5777-5784
    • Bowman, M.J.1    Zaia, J.2
  • 114
    • 84862001943 scopus 로고    scopus 로고
    • Ultrasensitive capillary electrophoretic analysis of potentially immunogenic carbohydrate residues in biologics: Galactose-α-1, 3-galactose containing oligosaccharides
    • Szabo, Z., Guttman, A., Bones, J., Shand, R. L. et al., Ultrasensitive capillary electrophoretic analysis of potentially immunogenic carbohydrate residues in biologics: Galactose-α-1, 3-galactose containing oligosaccharides. Mol. Pharm. 2012, 9, 1612-1619.
    • (2012) Mol. Pharm. , vol.9 , pp. 1612-1619
    • Szabo, Z.1    Guttman, A.2    Bones, J.3    Shand, R.L.4
  • 115
    • 84890104706 scopus 로고    scopus 로고
    • Site-specific glycan-peptide analysis for determination of N-glycoproteome heterogeneity
    • Parker, B. L., Thaysen-Andersen, M., Solis, N., Scott, N. E. et al., Site-specific glycan-peptide analysis for determination of N-glycoproteome heterogeneity. J. Proteome Res. 2013, 12, 5791-5800.
    • (2013) J. Proteome Res. , vol.12 , pp. 5791-5800
    • Parker, B.L.1    Thaysen-Andersen, M.2    Solis, N.3    Scott, N.E.4
  • 116
    • 70349113034 scopus 로고    scopus 로고
    • Determination of glycosylation sites and site-specific heterogeneity in glycoproteins
    • An, H. J., Froehlich, J. W., Lebrilla, C. B., Determination of glycosylation sites and site-specific heterogeneity in glycoproteins. Curr. Opin. Chem. Biol. 2009, 13, 421-426.
    • (2009) Curr. Opin. Chem. Biol , vol.13 , pp. 421-426
    • An, H.J.1    Froehlich, J.W.2    Lebrilla, C.B.3
  • 117
    • 84943178408 scopus 로고    scopus 로고
    • An integrated glycoprotein immobilization method for glycopeptide and glycan analysis of cardiac hypertrophy
    • Yang, S., Mishra, S., Chen, L., Zhou, J.-y. et al., An integrated glycoprotein immobilization method for glycopeptide and glycan analysis of cardiac hypertrophy. Anal. Chem. 2015, DOI 10.1021/acs.analchem.5b01663
    • (2015) Anal. Chem.
    • Yang, S.1    Mishra, S.2    Chen, L.3    Zhou, J.-y.4
  • 118
    • 0038783497 scopus 로고    scopus 로고
    • Derivatization of carbohydrates for chromatographic, electrophoretic and mass spectrometric structure analysis
    • Lamari, F. N., Kuhn, R., Karamanos, N. K., Derivatization of carbohydrates for chromatographic, electrophoretic and mass spectrometric structure analysis. J. Chromatogr. B 2003, 793, 15-36.
    • (2003) J. Chromatogr. B , vol.793 , pp. 15-36
    • Lamari, F.N.1    Kuhn, R.2    Karamanos, N.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.