메뉴 건너뛰기




Volumn 8, Issue 4, 2011, Pages 325-336

Analysis of glycosaminoglycans using mass spectrometry

Author keywords

Chondroitin sulfate; Dermatan sulfate; Glycosaminoglycan; Heparan sulfate; Heparin; Hyaluronan; Keratan sulfate; Mass spectrometry; Proteoglycan

Indexed keywords

CHONDROITIN SULFATE; DERMATAN SULFATE; GLYCOSAMINOGLYCAN; HEPARAN SULFATE; HYALURONIC ACID; KERATAN SULFATE; OLIGOSACCHARIDE;

EID: 82155170654     PISSN: 15701646     EISSN: None     Source Type: Journal    
DOI: 10.2174/157016411798220871     Document Type: Review
Times cited : (45)

References (137)
  • 1
    • 0034643323 scopus 로고    scopus 로고
    • Specificities of heparan sulphate proteoglycans in developmental processes
    • Perrimon, N. and Bernfield, M. Specificities of heparan sulphate proteoglycans in developmental processes. Nature, 2000, 404, 725-728.
    • (2000) Nature , vol.404 , pp. 725-728
    • Perrimon, N.1    Bernfield, M.2
  • 2
    • 34247610845 scopus 로고    scopus 로고
    • Heparan Sulphate Proteoglycans Finetune Mammalian Physiology
    • Bishop, J. R. Schuksz, M. and Esko, J. D. Heparan sulphate proteoglycans finetune mammalian physiology. Nature, 2007, 446, 1030-1037.
    • (2007) Nature , vol.446 , pp. 1030-1037
    • Bishop, J.R.1    Schuksz, M.2    Esko, J.D.3
  • 3
    • 33751187897 scopus 로고    scopus 로고
    • The Molecular Diversity of Glycosa-minoglycans Shapes Animal Development
    • Bulow, H. E. and Hobert, O. The Molecular Diversity of Glycosa-minoglycans Shapes Animal Development. Annu. Rev. Cell Dev. Biol., 2006, 22, 375-407.
    • (2006) Annu. Rev. Cell Dev. Biol , vol.22 , pp. 375-407
    • Bulow, H.E.1    Hobert, O.2
  • 4
    • 0035979765 scopus 로고    scopus 로고
    • Regulation of Wnt Signaling and Embryo Patterning By An Extracellular Sulfatase
    • Dhoot, G. K.; Gustafsson, M. K.; Ai, X.; Sun, W.; Standiford, D. M. and Emerson, C. P.Jr. Regulation of Wnt signaling and embryo patterning by an extracellular sulfatase.Science, 2001, 293, 1663-1666.
    • (2001) Science , vol.293 , pp. 1663-1666
    • Dhoot, G.K.1    Gustafsson, M.K.2    Ai, X.3    Sun, W.4    Standiford, D.M.5    Emerson Jr., C.P.6
  • 5
    • 0038823611 scopus 로고    scopus 로고
    • Caenorhabditis elegans early embryogenesis and vulval morphogenesis require chondroitin biosynthesis
    • Hwang, H. Y.; Olson, S. K.; Esko, J. D. and Horvitz, H. R. (2003) Caenorhabditis elegans early embryogenesis and vulval morphogenesis require chondroitin biosynthesis. Nature, 2001, 423, 439-443
    • (2003) Nature , vol.423 , pp. 439-443
    • Hwang, H.Y.1    Olson, S.K.2    Esko, J.D.3    Horvitz, H.R.4
  • 7
    • 0037154175 scopus 로고    scopus 로고
    • Tumor cell surface heparan sulfate as cryptic promoters or inhibitors of tumor growth and Metastasis
    • Liu, D.; Shriver, Z.; Venkataraman, G.; Shabrawi, Y. and Sasisekharan, R. Tumor cell surface heparan sulfate as cryptic promoters or inhibitors of tumor growth and Metastasis. Proc. Natl. Acad. Sci. USA, 2002, 99, 568-573.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 568-573
    • Liu, D.1    Shriver, Z.2    Venkataraman, G.3    Shabrawi, Y.4    Sasisekharan, R.5
  • 8
    • 1642342232 scopus 로고    scopus 로고
    • Structural and conformational aspects of the anticoagulant and anti-thrombotic activity of heparin and dermatan sulfate
    • Casu, B.; Guerrini, M. and Torri, G. Structural and conformational aspects of the anticoagulant and anti-thrombotic activity of heparin and dermatan sulfate. Curr. Pharm. Des., 2004, 10, 939-949.
    • (2004) Curr. Pharm. Des , vol.10 , pp. 939-949
    • Casu, B.1    Guerrini, M.2    Torri, G.3
  • 13
    • 0034904048 scopus 로고    scopus 로고
    • Molecular properties and in-volvement of heparanase in cancer metastasis and angiogenesis
    • Vlodavsky, I. and Friedmann, Y. Molecular properties and in-volvement of heparanase in cancer metastasis and angiogenesis. J. Clin. Invest., 2001, 108, 341-347.
    • (2001) J. Clin. Invest , vol.108 , pp. 341-347
    • Vlodavsky, I.1    Friedmann, Y.2
  • 14
    • 24344496911 scopus 로고    scopus 로고
    • The terminal phase of cytokinesis in the Caenorhabditis elegans early embryo requires protein glycosylation
    • Wang, H.; Spang, A.; Sullivan, M. A.; Hryhorenko, J. and Hagen, F. K. The terminal phase of cytokinesis in the Caenorhabditis elegans early embryo requires protein glycosylation. Mol. Biol. Cell., 2005, 16, 4202-4213.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4202-4213
    • Wang, H.1    Spang, A.2    Sullivan, M.A.3    Hryhorenko, J.4    Hagen, F.K.5
  • 16
    • 0030001849 scopus 로고    scopus 로고
    • Expression cloning and molecular charac-terization of HAS protein, a eukaryotic hyaluronan synthase
    • Itano, N. and Kimata, K. Expression cloning and molecular charac-terization of HAS protein, a eukaryotic hyaluronan synthase. J. Biol. Chem., 1996, 271, 9875-9878.
    • (1996) J. Biol. Chem , vol.271 , pp. 9875-9878
    • Itano, N.1    Kimata, K.2
  • 17
    • 0027520198 scopus 로고
    • Serum-derived hyaluronan-associated protein (SHAP) is the heavy chain of the inter alpha-trypsin inhibitor
    • Huang, L.; Yoneda, M. and Kimata, K. A serum-derived hyaluronan-associated protein (SHAP) is the heavy chain of the inter alpha-trypsin inhibitor. J. Biol. Chem., 1993, 268, 26725-26730
    • (1993) J. Biol. Chem , vol.268 , pp. 26725-26730
    • Huang, L.1    Yoneda, M.2    Kimata, K.A.3
  • 18
    • 64149113544 scopus 로고    scopus 로고
    • Airway smooth muscle cells synthesize hyaluronan cable structures independent of inter-alpha-inhibitor heavy chain attachment
    • Lauer, M. E.; Fulop, C.; Mukhopadhyay, D.; Comhair, S.; Erzu-rum, S. C. and Hascall, V. C. Airway smooth muscle cells synthesize hyaluronan cable structures independent of inter-alpha-inhibitor heavy chain attachment. J. Biol. Chem., 2009, 284, 5313-5323.
    • (2009) J. Biol. Chem , vol.284 , pp. 5313-5323
    • Lauer, M.E.1    Fulop, C.2    Mukhopadhyay, D.3    Comhair, S.4    Erzu-Rum, S.C.5    Hascall, V.C.6
  • 19
    • 0033785674 scopus 로고    scopus 로고
    • Keratan sulfate: Structure, biosynthesis, and function
    • Funderburgh, J. L. Keratan sulfate: structure, biosynthesis, and function. Glycobiology, 2000, 10, 951-958.
    • (2000) Glycobiology , vol.10 , pp. 951-958
    • Funderburgh, J.L.1
  • 21
    • 0037059771 scopus 로고    scopus 로고
    • The mode of action of heparan and dermatan sulfates in the regulation of hepatocyte growth factor/scatter factor
    • Lyon, M.; Deakin, J. A. and Gallagher, J. T. The mode of action of heparan and dermatan sulfates in the regulation of hepatocyte growth factor/scatter factor. J. Biol. Chem., 2002, 277, 1040-1046
    • (2002) J. Biol. Chem , vol.277 , pp. 1040-1046
    • Lyon, M.1    Deakin, J.A.2    Gallagher, J.T.3
  • 22
    • 0032561306 scopus 로고    scopus 로고
    • Dermatan sulfate released after injury is a potent promoter of fibroblast growth factor-2 function
    • Penc, S. F.; Pomahac, B.; Winkler, T.; Dorschner, R. A.; Eriksson, E.; Herndon, M. and Gallo, R. L. Dermatan sulfate released after injury is a potent promoter of fibroblast growth factor-2 function. J. Biol. Chem., 1998, 273, 28116-28121.
    • (1998) J. Biol. Chem , vol.273 , pp. 28116-28121
    • Penc, S.F.1    Pomahac, B.2    Winkler, T.3    Dorschner, R.A.4    Eriksson, E.5    Herndon, M.6    Gallo, R.L.7
  • 23
    • 0037044757 scopus 로고    scopus 로고
    • Derma-tan sulfate binds and potentiates activity of keratinocyte growth factor (FGF-7)
    • Trowbridge, J. M.; Rudisill, J. A.; Ron, D. and Gallo, R. L. Derma-tan sulfate binds and potentiates activity of keratinocyte growth factor (FGF-7). J. Biol. Chem., 2002, 277, 42815-42820.
    • (2002) J. Biol. Chem , vol.277 , pp. 42815-42820
    • Trowbridge, J.M.1    Rudisill, J.A.2    Ron, D.3    Gallo, R.L.4
  • 24
    • 0026499491 scopus 로고
    • Quanti-tation of chondroitin 4-sulfate and chondroitin 6-sulfate in pathologic joint fluid
    • Shinmei, M.; Miyauchi, S.; Machida, A. and Miyazaki, K. Quanti-tation of chondroitin 4-sulfate and chondroitin 6-sulfate in pathologic joint fluid. Arthritis and rheumatism, 1992, 35, 1304-1308
    • (1992) Arthritis and Rheumatism , vol.35 , pp. 1304-1308
    • Shinmei, M.1    Miyauchi, S.2    Machida, A.3    Miyazaki, K.4
  • 25
  • 27
    • 0031650075 scopus 로고    scopus 로고
    • Proteoglycans: Master regulators of molecular encounter?
    • Lander, A. D. Proteoglycans: master regulators of molecular encounter?. Matrix Biol.,1998, 17, 465-472.
    • (1998) Matrix Biol , vol.17 , pp. 465-472
    • Lander, A.D.1
  • 28
    • 5644236458 scopus 로고    scopus 로고
    • Heparan sulfate structure in mice with genetically modified heparan sulfate production
    • Ledin, J.; Staatz, W.; Li, J. P.; Gotte, M.; Selleck, S.; Kjellen, L. and Spillmann, D. Heparan sulfate structure in mice with genetically modified heparan sulfate production. J. Biol. Chem., 2004, 279, 42732-42741.
    • (2004) J. Biol. Chem , vol.279 , pp. 42732-42741
    • Ledin, J.1    Staatz, W.2    Li, J.P.3    Gotte, M.4    Selleck, S.5    Kjellen, L.6    Spillmann, D.7
  • 29
    • 70350038006 scopus 로고    scopus 로고
    • Rapid purification and high sensitivity analysis of heparin sulfate from cells and tissues: Towards glycomics profiling
    • Guimond, S. E.; Puvirajesinghe, T. M.; Skidmore, M. A.; Kalus, I. Dierks, T.; Yates, E. A. and Turnbull, J. E. Rapid purification and high sensitivity analysis of heparin sulfate from cells and tissues: towards glycomics profiling. J. Biol. Chem., 2009, 284, 25714-25722.
    • (2009) J. Biol. Chem , vol.284 , pp. 25714-25722
    • Guimond, S.E.1    Puvirajesinghe, T.M.2    Skidmore, M.A.3    Kalus, I.4    Dierks, T.5    Yates, E.A.6    Turnbull, J.E.7
  • 31
    • 82155175795 scopus 로고    scopus 로고
    • Elimination for Release of O-Linked Glycosaminoglycans from Proteoglycans
    • Conrad, H. E.-Elimination for Release of O-Linked Glycosaminoglycans from Proteoglycans, Curr. Prot. Mol. Biol., 2001, 17.15A, 1-3.
    • (2001) Curr. Prot. Mol. Biol , vol.17 , Issue.15 , pp. 1-3
    • Conrad, H.E.1
  • 32
    • 42049122573 scopus 로고    scopus 로고
    • Comparative Glycomics of Connective Tissue Glycosaminoglycans
    • Hitchcock, A.; Yates, K. E.; Costello, C. and Zaia, J. Comparative Glycomics of Connective Tissue Glycosaminoglycans. Proteomics, 2008, 8, 1384-1397.
    • (2008) Proteomics , vol.8 , pp. 1384-1397
    • Hitchcock, A.1    Yates, K.E.2    Costello, C.3    Zaia, J.4
  • 33
    • 59249098157 scopus 로고    scopus 로고
    • Improved Workup for Glycosaminoglycan Disaccharide Analysis using Capillary Electrophoresis with Laser-Induced Fluorescence Detection
    • Hitchcock, A.; Bowman, M.; Staples, G. and Zaia, J. Improved Workup for Glycosaminoglycan Disaccharide Analysis using Capillary Electrophoresis with Laser-Induced Fluorescence Detection. Electrophoresis, 2008, 29, 4538-4548.
    • (2008) Electrophoresis , vol.29 , pp. 4538-4548
    • Hitchcock, A.1    Bowman, M.2    Staples, G.3    Zaia, J.4
  • 34
    • 66449127755 scopus 로고    scopus 로고
    • Organ-specific heparan sulfate structural phe-notypes
    • Shi, X. and Zaia, J. Organ-specific heparan sulfate structural phe-notypes. J. Biol. Chem., 2009, 284, 11806-11814.
    • (2009) J. Biol. Chem , vol.284 , pp. 11806-11814
    • Shi, X.1    Zaia, J.2
  • 36
    • 20444477092 scopus 로고    scopus 로고
    • Detection and Quantification of Sulfated Disaccharides from Keratan Sulfate and Chon-droitin/Dermatan Sulfate during Chick Corneal Development by ESI-MS/MS
    • Zhang, Y.; Conrad, A. H.; Tasheva, E. S.; An, K.; Corpuz, L. M. Kariya, Y.; Suzuki, K. and Conrad, G. W. Detection and Quantification of Sulfated Disaccharides from Keratan Sulfate and Chon-droitin/Dermatan Sulfate during Chick Corneal Development by ESI-MS/MS. Invest. Ophthal. Visual Sci., 2005, 46, 1604-1614.
    • (2005) Invest. Ophthal. Visual Sci , vol.46 , pp. 1604-1614
    • Zhang, Y.1    Conrad, A.H.2    Tasheva, E.S.3    An, K.4    Corpuz, L.M.5    Kariya, Y.6    Suzuki, K.7    Conrad, G.W.8
  • 37
    • 0029068089 scopus 로고
    • Utility of non-covalent complexes in the matrixassisted laser desorption ionization mass spectrometry of heparin-derived oligosaccharides
    • Juhasz, P. and Biemann, K. Utility of non-covalent complexes in the matrixassisted laser desorption ionization mass spectrometry of heparin-derived oligosaccharides. Carbohydr. Res., 1995, 270, 131-147.
    • (1995) Carbohydr. Res , vol.270 , pp. 131-147
    • Juhasz, P.1    Biemann, K.2
  • 38
    • 0028346026 scopus 로고
    • Mass spectrometric molecular-weight determination of highly acidic compounds of biological significance via their complexes with basic polypeptides
    • Juhasz, P. and Biemann, K. Mass spectrometric molecular-weight determination of highly acidic compounds of biological significance via their complexes with basic polypeptides. Proc. Natl. Acad. Sci. USA, 1994, 91, 4333-4337.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4333-4337
    • Juhasz, P.1    Biemann, K.2
  • 39
    • 0034641723 scopus 로고    scopus 로고
    • Cleavage of the antithrombin III binding site in heparin by heparinases and its implication in the generation of low molecular weight heparin
    • Shriver, Z.; Sundaram, M.; Venkataraman, G.; Fareed, J.; Linhardt, R.; Biemann, K. and Sasisekharan, R. Cleavage of the antithrombin III binding site in heparin by heparinases and its implication in the generation of low molecular weight heparin. Proc. Natl. Acad. Sci. USA, 2000, 97, 10365-10370.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10365-10370
    • Shriver, Z.1    Sundaram, M.2    Venkataraman, G.3    Fareed, J.4    Linhardt, R.5    Biemann, K.6    Sasisekharan, R.7
  • 40
    • 0032514699 scopus 로고    scopus 로고
    • Mass spectrometric evidence for the enzymatic mechanism of the depolymerization of heparinlike glycosaminoglycans by heparinase II
    • Rhomberg, A. J.; Shriver, Z.; Biemann, K. and Sasisekharan, R. Mass spectrometric evidence for the enzymatic mechanism of the depolymerization of heparinlike glycosaminoglycans by heparinase II. Proc. Natl. Acad. Sci. USA, 1998, 95, 12232-12237.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12232-12237
    • Rhomberg, A.J.1    Shriver, Z.2    Biemann, K.3    Sasisekharan, R.4
  • 41
    • 0032516018 scopus 로고    scopus 로고
    • Mass spectrometric and capillary electrophoretic investigation of the enzymatic degradation of heparin-like Glycosaminoglycans
    • Rhomberg, A. J.; Ernst, S.; Sasisekharan, R. and Biemann, K. Mass spectrometric and capillary electrophoretic investigation of the enzymatic degradation of heparin-like Glycosaminoglycans. Proc. Natl. Acad. Sci. USA, 1998, 95, 4176-4181.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4176-4181
    • Rhomberg, A.J.1    Ernst, S.2    Sasisekharan, R.3    Biemann, K.4
  • 42
    • 0032516052 scopus 로고    scopus 로고
    • Direct evidence for a predominantly exolytic processive mechanism for depolymerization of heparin-like glycosaminoglycans by heparinase I
    • Ernst, S.; Rhomberg, A. J.; Biemann, K. and Sasisekharan, R. Direct evidence for a predominantly exolytic processive mechanism for depolymerization of heparin-like glycosaminoglycans by heparinase I. Proc. Natl. Acad. Sci. USA, 1998, 95, 4182-4187.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4182-4187
    • Ernst, S.1    Rhomberg, A.J.2    Biemann, K.3    Sasisekharan, R.4
  • 44
    • 33645218878 scopus 로고    scopus 로고
    • Matrix-Assisted Laser Desorption/Ionization Mass Spectrometric Analysis of Uncomplexed
    • Laremore, T. N.; Murugesan, S.; Park, T. J.; Avci, F. Y.; Zagor-evski, D. V. and Linhardt, R. J. Matrix-Assisted Laser Desorption/Ionization Mass Spectrometric Analysis of Uncomplexed Highly Sulfated Oligosaccharides Using Ionic Liquid Matrices. Anal. Chem., 2006,78, 1774-1779.
    • (2006) Anal. Chem , vol.78 , pp. 1774-1779
    • Laremore, T.N.1    Murugesan, S.2    Park, T.J.3    Avci, F.Y.4    Zagor-Evski, D.V.5    Linhardt, R.J.6
  • 45
    • 33947716025 scopus 로고    scopus 로고
    • Improved matrix-assisted laser desorption/ionization mass spectrometric detection of glycosaminoglycan disaccharides as cesium salts
    • Laremore, T. N. and Linhardt, R. J. Improved matrix-assisted laser desorption/ionization mass spectrometric detection of glycosaminoglycan disaccharides as cesium salts. Rapid Commun. Mass Spectrom., 2007, 21, 1315-1320.
    • (2007) Rapid Commun. Mass Spectrom , vol.21 , pp. 1315-1320
    • Laremore, T.N.1    Linhardt, R.J.2
  • 46
    • 33847238426 scopus 로고    scopus 로고
    • Ionic liquid matrix for direct UVMALDI-TOF-MS analysis of dermatan sulfate and chondroitin sulfate oligosaccharides
    • Laremore, T. N.; Zhang, F. and Linhardt, R. J. Ionic liquid matrix for direct UVMALDI-TOF-MS analysis of dermatan sulfate and chondroitin sulfate oligosaccharides. Anal. Chem., 2007, 79, 1604-1610.
    • (2007) Anal. Chem , vol.79 , pp. 1604-1610
    • Laremore, T.N.1    Zhang, F.2    Linhardt, R.J.3
  • 48
    • 57749201601 scopus 로고    scopus 로고
    • Desorption/ionization mass spectrometric analysis of polysulfated-derived oligosaccharides using pyrenemethylguanidine
    • Ohara, K.; Jacquinet, J. C.; Jouanneau, D.; Helbert, W.; Smietana, M. and Vasseur, J. J. Matrix-assisted laser desorption/ionization mass spectrometric analysis of polysulfated-derived oligosaccharides using pyrenemethylguanidine. J. Am. Soc. Mass Spectrom., 2009, 20, 131-137.
    • (2009) J. Am. Soc. Mass Spectrom , vol.20 , pp. 131-137
    • Ohara, K.1    Jacquinet, J.C.2    Jouanneau, D.3    Helbert, W.4    Smietana, M.5    Vasseur, J.J.6
  • 49
    • 34249315132 scopus 로고    scopus 로고
    • Matrix assisted laser desorption ionization-time of flight mass spectrometry analysis of hyaluronan oligosaccharides
    • Sakai, S.; Hirano, K.; Toyoda, H.; Linhardt, R. J. and Toida, T. Matrix assisted laser desorption ionization-time of flight mass spectrometry analysis of hyaluronan oligosaccharides. Anal. Chim. Acta., 2007, 593, 207-213.
    • (2007) Anal. Chim. Acta , vol.593 , pp. 207-213
    • Sakai, S.1    Hirano, K.2    Toyoda, H.3    Linhardt, R.J.4    Toida, T.5
  • 50
    • 33646164172 scopus 로고    scopus 로고
    • The signal-to-noise ratio as a measure of HA oligomer concentration: A MALDI-TOF MS Study
    • Busse, K.; Averbeck, M.; Anderegg, U.; Arnold, K.; Simon, J. C. and Schiller, J. The signal-to-noise ratio as a measure of HA oligomer concentration: a MALDI-TOF MS Study. Carbohydr. Res., 2006, 341, 1065-1070.
    • (2006) Carbohydr. Res , vol.341 , pp. 1065-1070
    • Busse, K.1    Averbeck, M.2    Anderegg, U.3    Arnold, K.4    Simon, J.C.5    Schiller, J.6
  • 51
    • 0041315653 scopus 로고    scopus 로고
    • Rapid chemoen-zymatic synthesis of monodisperse hyaluronan oligosaccharides with immobilized enzyme reactors
    • DeAngelis, P. L.; Oatman, L. C. and Gay, D. F. Rapid chemoen-zymatic synthesis of monodisperse hyaluronan oligosaccharides with immobilized enzyme reactors. J. Biol. Chem., 2003, 278, 35199-35203.
    • (2003) J. Biol. Chem , vol.278 , pp. 35199-35203
    • Deangelis, P.L.1    Oatman, L.C.2    Gay, D.F.3
  • 52
    • 51649091074 scopus 로고    scopus 로고
    • Mass Spectrometric Ionization of Carbohydrates
    • (Gross, M. G., Ed.)
    • Zaia, J. Mass Spectrometric Ionization of Carbohydrates. in Encyclopedia of Mass Spectrometry, vol 6 (Gross, M. G., Ed.)., 2007
    • (2007) Encyclopedia of Mass Spectrometry , vol.6
    • Zaia, J.1
  • 53
    • 24944569191 scopus 로고    scopus 로고
    • Heparin sequencing using enzymatic digestion and ESI-MSn with HOST: A heparin/HS oligosaccharide sequencing tool
    • Saad, O. M. and Leary, J. A. Heparin sequencing using enzymatic digestion and ESI-MSn with HOST: a heparin/HS oligosaccharide sequencing tool. Anal. Chem., 2005, 77, 5902-5911.
    • (2005) Anal. Chem , vol.77 , pp. 5902-5911
    • Saad, O.M.1    Leary, J.A.2
  • 54
    • 25144469685 scopus 로고    scopus 로고
    • Compositional profiling of heparin/heparan sulfate using mass spectrometry: Assay for specificity of a novel extracellular human endosulfatase
    • Saad, O. M.; Ebel, H.; Uchimura, K.; Rosen, S. D.; Bertozzi, C. R. and Leary, J. A. Compositional profiling of heparin/heparan sulfate using mass spectrometry: assay for specificity of a novel extracellular human endosulfatase. Glycobiology, 2005, 15, 818-826.
    • (2005) Glycobiology , vol.15 , pp. 818-826
    • Saad, O.M.1    Ebel, H.2    Uchimura, K.3    Rosen, S.D.4    Bertozzi, C.R.5    Leary, J.A.6
  • 55
    • 0035417423 scopus 로고    scopus 로고
    • Evidence of block and randomly sequenced chondroitin polysaccharides: Sequential enzymatic digestion and quantification using ion trap tandem mass spectrometry
    • Desaire, H.; Sirich, T. L. and Leary, J. A. Evidence of block and randomly sequenced chondroitin polysaccharides: sequential enzymatic digestion and quantification using ion trap tandem mass spectrometry. Anal. Chem., 2001, 73, 3513-3520.
    • (2001) Anal. Chem , vol.73 , pp. 3513-3520
    • Desaire, H.1    Sirich, T.L.2    Leary, J.A.3
  • 56
    • 25144521846 scopus 로고    scopus 로고
    • Quantification of isomers from a mixture of twelve heparin and heparan sulfate disaccharides using tandem mass spectrometry
    • Behr, J. R.; Matsumoto, Y.; White, F. M. and Sasisekharan, R. Quantification of isomers from a mixture of twelve heparin and heparan sulfate disaccharides using tandem mass spectrometry. Rapid Commun. Mass Spectrom., 2005, 19, 2553-2562.
    • (2005) Rapid Commun. Mass Spectrom , vol.19 , pp. 2553-2562
    • Behr, J.R.1    Matsumoto, Y.2    White, F.M.3    Sasisekharan, R.4
  • 57
    • 71449090682 scopus 로고    scopus 로고
    • Determination of sulfation pattern in brain glycosaminoglycans by chipbased electrospray ionization ion trap mass spectrometry
    • Flangea, C.; Schiopu, C.; Sisu, E., Serb, A.; Przybylski, M.; Seidler, D. G. and Zamfir, A. D. Determination of sulfation pattern in brain glycosaminoglycans by chipbased electrospray ionization ion trap mass spectrometry. Anal. Bioanal. Chem., 2009, 395, 2489-2498.
    • (2009) Anal. Bioanal. Chem , vol.395 , pp. 2489-2498
    • Flangea, C.1    Schiopu, C.2    Sisu, E.3    Serb, A.4    Przybylski, M.5    Seidler, D.G.6    Zamfir, A.D.7
  • 58
    • 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.; Warrior, R.; Cummings, R. D. and Esko, J. D. 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    Warrior, R.5    Cummings, R.D.6    Esko, J.D.7
  • 60
    • 66349123838 scopus 로고    scopus 로고
    • Quantification of heparin sulfate disaccharides using ion-pairing reversed-phase microflow high-performance liquid chromatography with electrospray ionization trap mass spectrometry
    • Zhang, Z.; Xie, J.; Liu, H.; Liu, J. and Linhardt, R. J. Quantification of heparin sulfate disaccharides using ion-pairing reversed-phase microflow high-performance liquid chromatography with electrospray ionization trap mass spectrometry. Anal. Chem., 2009, 81, 4349-4355.
    • (2009) Anal. Chem , vol.81 , pp. 4349-4355
    • Zhang, Z.1    Xie, J.2    Liu, H.3    Liu, J.4    Linhardt, R.J.5
  • 62
    • 0037342766 scopus 로고    scopus 로고
    • Determination of monosaccharides and disaccharides in mucopolysaccharidoses patients by electrospray ionisation mass spectrometry
    • Ramsay, S. L.; Meikle, P. J. and Hopwood, J. J. Determination of monosaccharides and disaccharides in mucopolysaccharidoses patients by electrospray ionisation mass spectrometry. Mol. Genet. Metab., 2003, 78, 193-204.
    • (2003) Mol. Genet. Metab , vol.78 , pp. 193-204
    • Ramsay, S.L.1    Meikle, P.J.2    Hopwood, J.J.3
  • 63
    • 1642447923 scopus 로고    scopus 로고
    • Monitoring dose response of enzyme replacement therapy in feline mucopolysaccharidosis type VI by tandem mass spectrometry
    • Crawley, A.; Ramsay, S. L.; Byers, S.; Hopwood, J. and Meikle, P. J. Monitoring dose response of enzyme replacement therapy in feline mucopolysaccharidosis type VI by tandem mass spectrometry. Pediatr. Res., 2004, 55, 585-591.
    • (2004) Pediatr. Res , vol.55 , pp. 585-591
    • Crawley, A.1    Ramsay, S.L.2    Byers, S.3    Hopwood, J.4    Meikle, P.J.5
  • 64
    • 33745686152 scopus 로고    scopus 로고
    • Charac-terization of sulfated oligosaccharides in mucopolysaccharidosis type IIIA by electrospray ionization mass spectrometry
    • Mason, K. E.; Meikle, P. J.; Hopwood, J. J. and Fuller, M. Charac-terization of sulfated oligosaccharides in mucopolysaccharidosis type IIIA by electrospray ionization mass spectrometry. Anal. Chem., 2006, 78, 4534-4542.
    • (2006) Anal. Chem , vol.78 , pp. 4534-4542
    • Mason, K.E.1    Meikle, P.J.2    Hopwood, J.J.3    Fuller, M.4
  • 65
    • 77953082989 scopus 로고    scopus 로고
    • Determination of urinary oligosaccharides by high-performance liquid chromatography/electrospray ionizationtandem mass spectrometry: Application to Hunter syndrome
    • Nielsen, T. C.; Rozek, T.; Hopwood, J. J. and Fuller, M. Determi-nation of urinary oligosaccharides by high-performance liquid chromatography/electrospray ionizationtandem mass spectrometry: Application to Hunter syndrome. Anal. Biochem., 2010, 402, 113-120.
    • (2010) Anal. Biochem , vol.402 , pp. 113-120
    • Nielsen, T.C.1    Rozek, T.2    Hopwood, J.J.3    Fuller, M.4
  • 66
    • 26444450533 scopus 로고    scopus 로고
    • The Effect of the Mobile Phase Additives On Sensitiv-ity In the Analysis of Peptides and Proteins By High-performance Liquid Chromatographyelectrospray Mass Spectrometry
    • Garcia, M. C. The effect of the mobile phase additives on sensitiv-ity in the analysis of peptides and proteins by high-performance liquid chromatographyelectrospray mass spectrometry. J. Chromatogr., 2005, B 825, 111.
    • (2005) J. Chromatogr , vol.825 , pp. 111
    • Garcia, M.C.1
  • 67
    • 0019120992 scopus 로고
    • High-performance liquid chro-matographic separation of unsaturated disaccharides derived from heparan sulfate and heparin
    • Lee, G. J.-L. and Tieckelmann, H. High-performance liquid chromatographic separation of unsaturated disaccharides derived from heparan sulfate and heparin. J. Chromatogr., 1980, 195, 402.
    • (1980) J. Chromatogr , vol.195 , pp. 402
    • Lee, G.J.-L.1    Tieckelmann, H.2
  • 68
    • 0037167009 scopus 로고    scopus 로고
    • Analysis of Heparan Sulfate Oligosaccharides with Ion Pair-Reverse Phase Capillary High Performance Liquid Chromatography-Microelectrospray Ionization Time-of-Flight Mass Spectrometry
    • Kuberan, B.; Lech, M.; Zhang, L.; Wu, Z. L.; Beeler, D. L. and Rosenberg, R. Analysis of Heparan Sulfate Oligosaccharides with Ion Pair-Reverse Phase Capillary High Performance Liquid Chromatography-Microelectrospray Ionization Time-of-Flight Mass Spectrometry. J. Am. Chem. Soc., 2002, 124, 8707-8718.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 8707-8718
    • Kuberan, B.1    Lech, M.2    Zhang, L.3    Wu, Z.L.4    Beeler, D.L.5    Rosenberg, R.6
  • 69
    • 1642453684 scopus 로고    scopus 로고
    • LC/MS sequencing approach for highly sulfated heparin-derived oligosaccharides
    • Thanawiroon, C.; Rice, K. G.; Toida, T. and Linhardt, R. J. LC/MS sequencing approach for highly sulfated heparin-derived oligosaccharides. J. Biol. Chem., 2004, 279, 2608-2615.
    • (2004) J. Biol. Chem , vol.279 , pp. 2608-2615
    • Thanawiroon, C.1    Rice, K.G.2    Toida, T.3    Linhardt, R.J.4
  • 70
    • 30744447270 scopus 로고    scopus 로고
    • Ion-pairing re-versed-phased chromatography/mass spectrometry of heparin
    • Henriksen, J.; Roepstorff, P. and Ringborg, L. H. Ion-pairing re-versed-phased chromatography/mass spectrometry of heparin. Carbohydr. Res., 2006, 341, 382-387.
    • (2006) Carbohydr. Res , vol.341 , pp. 382-387
    • Henriksen, J.1    Roepstorff, P.2    Ringborg, L.H.3
  • 71
    • 39449139029 scopus 로고    scopus 로고
    • Ultraperformance ion-pair liquid chromatography coupled to electrospray time-of-flight mass spectrometry for compositional profiling and quantification of heparin and heparan sulfate
    • Korir, A. K.; Limtiaco, J. F.; Gutierrez, S. M. and Larive, C. K. Ultraperformance ion-pair liquid chromatography coupled to electrospray time-of-flight mass spectrometry for compositional profiling and quantification of heparin and heparan sulfate. Anal. Chem., 2008, 80, 1297-1306.
    • (2008) Anal. Chem , vol.80 , pp. 1297-1306
    • Korir, A.K.1    Limtiaco, J.F.2    Gutierrez, S.M.3    Larive, C.K.4
  • 72
    • 71749085244 scopus 로고    scopus 로고
    • Ultraperformance liquid chromatography with electrospray ionization ion trap mass spectrometry for chondroitin disaccharide analysis
    • Solakyildirim, K.; Zhang, Z. and Linhardt, R. J. Ultraperformance liquid chromatography with electrospray ionization ion trap mass spectrometry for chondroitin disaccharide analysis. Anal. Biochem., 2010, 397, 24-28.
    • (2010) Anal. Biochem , vol.397 , pp. 24-28
    • Solakyildirim, K.1    Zhang, Z.2    Linhardt, R.J.3
  • 74
    • 77952149942 scopus 로고    scopus 로고
    • High-performance Liquid Chromatog-raphy-mass Spectrometry For Mapping and Sequencing Glycosami- Noglycan-derived Oligosaccharides
    • Volpi, N. and Linhardt, R. J. High-performance liquid chromatography-mass spectrometry for mapping and sequencing glycosami-noglycan-derived oligosaccharides Nat. Protoc., 2010, 5, 993-1004.
    • (2010) Nat. Protoc , vol.5 , pp. 993-1004
    • Volpi, N.1    Linhardt, R.J.2
  • 75
    • 0025173758 scopus 로고
    • Hydrophilic-Interaction Chromatography for the Separation of Peptides, Nucleic Acids and Other Polar Compounds
    • Alpert, A. Hydrophilic-Interaction Chromatography for the Separation of Peptides, Nucleic Acids and Other Polar Compounds. J. Chromatogr., 1990, 499, 177-196.
    • (1990) J. Chromatogr , vol.499 , pp. 177-196
    • Alpert, A.1
  • 76
    • 0034719127 scopus 로고    scopus 로고
    • Oglycan analysis of natural human neutrophil gelatinase B using a combination of normal phase-HPLC and online tandem mass spectrometry: Implications for the domain organization of the enzyme
    • Mattu, T. S.; Royle, L.; Langridge, J.; Wormald, M. R.; Van den Steen, P. E.; Van Damme, J.; Opdenakker, G.; Harvey, D. J.; Dwek, R. A. and Rudd, P. M. Oglycan analysis of natural human neutrophil gelatinase B using a combination of normal phase-HPLC and online tandem mass spectrometry: implications for the domain organization of the enzyme. Biochemistry, 2000, 39, 15695-15704.
    • (2000) Biochemistry , vol.39 , pp. 15695-15704
    • Mattu, T.S.1    Royle, L.2    Langridge, J.3    Wormald, M.R.4    Van den Steen, P.E.5    van Damme, J.6    Opdenakker, G.7    Harvey, D.J.8    Dwek, R.A.9    Rudd, P.M.10
  • 77
    • 13244291497 scopus 로고    scopus 로고
    • Protein glycosylation analyzed by normal-phase nano-liquid chromatography--mass spectrometry of glycopeptides
    • Wuhrer, M.; Koeleman, C. A.; Hokke, C. H. and Deelder, A. M. Protein glycosylation analyzed by normal-phase nano-liquid chromatography--mass spectrometry of glycopeptides. Anal. Chem., 2005, 77, 886-894.
    • (2005) Anal. Chem , vol.77 , pp. 886-894
    • Wuhrer, M.1    Koeleman, C.A.2    Hokke, C.H.3    Deelder, A.M.4
  • 78
    • 0842283940 scopus 로고    scopus 로고
    • Normalphase nanoscale liquid chromatography - Mass spectrometry of underivatized oligosaccharides at low-femtomole sensitivity
    • Wuhrer, M.; Koeleman, C. A. M.; Deelder, A. M. and Hokke, C. N. Normalphase nanoscale liquid chromatography - Mass spectrometry of underivatized oligosaccharides at low-femtomole sensitivity. Anal. Chem., 2004, 76, 833-838.
    • (2004) Anal. Chem , vol.76 , pp. 833-838
    • Wuhrer, M.1    Koeleman, C.A.M.2    Deelder, A.M.3    Hokke, C.N.4
  • 79
    • 40549123949 scopus 로고    scopus 로고
    • Characterization of heparin oligosaccharides binding specifically to antithrom-bin III using mass spectrometry
    • Naimy, H.; Leymarie, N.; Bowman, M. and Zaia, J. Characterization of heparin oligosaccharides binding specifically to antithrom-bin III using mass spectrometry. Biochemistry, 2008, 47, 3155-3161.
    • (2008) Biochemistry , vol.47 , pp. 3155-3161
    • Naimy, H.1    Leymarie, N.2    Bowman, M.3    Zaia, J.4
  • 81
    • 75649140258 scopus 로고    scopus 로고
    • Improved hydrophilic interaction chromatography LC/MS of heparinoids using a chip with postcolumn makeup flow
    • Staples, G. O.; Naimy, H.; Yin, H.; Kileen, K.; Kraiczek, K.; Costello, C. E. and Zaia, J. Improved hydrophilic interaction chromatography LC/MS of heparinoids using a chip with postcolumn makeup flow. Anal. Chem., 2010, 82, 516-522.
    • (2010) Anal. Chem , vol.82 , pp. 516-522
    • Staples, G.O.1    Naimy, H.2    Yin, H.3    Kileen, K.4    Kraiczek, K.5    Costello, C.E.6    Zaia, J.7
  • 82
    • 0035863643 scopus 로고    scopus 로고
    • Compositional analysis of glycosaminoglycans by electrospray mass spectrometry
    • Zaia, J. and Costello, C. E. Compositional analysis of glycosaminoglycans by electrospray mass spectrometry. Anal. Chem., 2001, 73, 233-239.
    • (2001) Anal. Chem , vol.73 , pp. 233-239
    • Zaia, J.1    Costello, C.E.2
  • 83
    • 33845583633 scopus 로고    scopus 로고
    • Optimized extraction of glycosaminoglycans from normal and osteoarthritic cartilage for glycomics profiling
    • Hitchcock, A. M.; Yates, K. E.; Shortkroff, S.; Costello, C. E. and Zaia, J. Optimized extraction of glycosaminoglycans from normal and osteoarthritic cartilage for glycomics profiling. Glycobiology, 2006, 17, 25-35.
    • (2006) Glycobiology , vol.17 , pp. 25-35
    • Hitchcock, A.M.1    Yates, K.E.2    Shortkroff, S.3    Costello, C.E.4    Zaia, J.5
  • 84
    • 33144464276 scopus 로고    scopus 로고
    • Glycoform quantification of chondroitin/dermatan sulfate using an LC/MS/MS platform
    • Hitchcock, A. M.; Costello, C. E. and Zaia, J. Glycoform quantification of chondroitin/dermatan sulfate using an LC/MS/MS platform. Biochemistry, 2006, 45, 2350-2361.
    • (2006) Biochemistry , vol.45 , pp. 2350-2361
    • Hitchcock, A.M.1    Costello, C.E.2    Zaia, J.3
  • 85
    • 9144223196 scopus 로고    scopus 로고
    • On-line size-exclusion chromatography/mass spectrometry of low molecular mass heparin
    • Henriksen, J.; Ringborg, L. H. and Roepstorrf, P. On-line size-exclusion chromatography/mass spectrometry of low molecular mass heparin. J. Mass Spectrom., 2004, 39, 1305-1312.
    • (2004) J. Mass Spectrom , vol.39 , pp. 1305-1312
    • Henriksen, J.1    Ringborg, L.H.2    Roepstorrf, P.3
  • 86
    • 0026206352 scopus 로고
    • High-performance liquid chromatography of mono and oligo-saccharides on a graphitized carbon column
    • Koizumi, K.; Okada, Y. and Fukuda, M. High-performance liquid chromatography of mono and oligo-saccharides on a graphitized carbon column. Carbohydr. Res., 1991, 215, 67.
    • (1991) Carbohydr. Res , vol.215 , pp. 67
    • Koizumi, K.1    Okada, Y.2    Fukuda, M.3
  • 87
    • 0026794731 scopus 로고
    • High-performance liquid chromatography of oligosaccharide alditols and glycopeptides on a graphitizedcarbon column
    • Davies, M.; Smith, K. D.; Harbin, A.-M. and Hounsell, E. F. High-performance liquid chromatography of oligosaccharide alditols and glycopeptides on a graphitizedcarbon column. J. Chromatogr., 1992, 609, 125.
    • (1992) J. Chromatogr , vol.609 , pp. 125
    • Davies, M.1    Smith, K.D.2    Harbin, A.-M.3    Hounsell, E.F.4
  • 88
    • 27244441764 scopus 로고    scopus 로고
    • Nanoliquid chromatography-mass spectrometry of oligosaccharides employing graphitized carbon chromatography on microchip with a high-accuracy mass analyzer
    • Niñonuevo, M.; An, H.; Yin, H.; Killeen, K.; Grimm, R.; Ward, R.; German, B. and Lebrilla, C. Nanoliquid chromatography-mass spectrometry of oligosaccharides employing graphitized carbon chromatography on microchip with a high-accuracy mass analyzer. Electrophoresis, 2005, 26, 3641-3649.
    • (2005) Electrophoresis , vol.26 , pp. 3641-3649
    • Niñonuevo, M.1    An, H.2    Yin, H.3    Killeen, K.4    Grimm, R.5    Ward, R.6    German, B.7    Lebrilla, C.8
  • 89
    • 60549101068 scopus 로고    scopus 로고
    • Use of activated graphitized carbon chips for liquid chromatography/mass spectro-metric and tandem mass spectrometric analysis of tryptic glycopep-tides
    • Alley, W. R.Jr. Mechref Y., Novotny M. V. Use of activated graphitized carbon chips for liquid chromatography/mass spectro-metric and tandem mass spectrometric analysis of tryptic glycopep-tides. Rapid Commun. Mass Spectrom., 2009, 23, 495-505.
    • (2009) Rapid Commun. Mass Spectrom , vol.23 , pp. 495-505
    • Alley, W.R.1    Mechref, Y.2    Novotny, M.V.3
  • 91
    • 34249015574 scopus 로고    scopus 로고
    • Graphitized Carbon LC-MS Characterization of the Chondroitin Sulfate Oligosaccharides of Aggrecan
    • Estrella, R. P.; Whitelock, J. M.; Packer, N. H. and Karlsson, N. G. Graphitized Carbon LC-MS Characterization of the Chondroitin Sulfate Oligosaccharides of Aggrecan. Anal. Chem., 2007, 79, 3597-3606.
    • (2007) Anal. Chem , vol.79 , pp. 3597-3606
    • Estrella, R.P.1    Whitelock, J.M.2    Packer, N.H.3    Karlsson, N.G.4
  • 92
    • 66149155441 scopus 로고    scopus 로고
    • Small-scale enzymatic digestion of glycoproteins and proteoglycans for analysis of oligosaccharides by LC-MS and FACE gel electrophoresis
    • Estrella, R. P.; Whitelock, J. M.; Roubin, R. H.; Packer, N. H. and Karlsson, N. G. Small-scale enzymatic digestion of glycoproteins and proteoglycans for analysis of oligosaccharides by LC-MS and FACE gel electrophoresis. Methods Mol. Biol., 2009, 534, 171-192
    • (2009) Methods Mol. Biol , vol.534 , pp. 171-192
    • Estrella, R.P.1    Whitelock, J.M.2    Roubin, R.H.3    Packer, N.H.4    Karlsson, N.G.5
  • 93
    • 20444404610 scopus 로고    scopus 로고
    • Analysis of proteogly-cans derived sulphated disaccharides by liquid chromatogra-phy/mass spectrometry
    • Barroso, B.; Didraga, M. and Bischoff, R. Analysis of proteogly-cans derived sulphated disaccharides by liquid chromatogra-phy/mass spectrometry. J. Chromatogr. A., 2005, 1080, 43-48.
    • (2005) J. Chromatogr. A , vol.1080 , pp. 43-48
    • Barroso, B.1    Didraga, M.2    Bischoff, R.3
  • 94
    • 72449162024 scopus 로고    scopus 로고
    • Heparan Sulfate Separation, Sequencing, and Isomeric Differ-entiation: Ion Mobility Spectrometry Reveals Specific Iduronic and Glucuronic Acid-Containing Hexasaccharides
    • Schenauer, M. R.; Meissen, J. K.; Seo, Y.; Ames, J. B. and Leary, J. A. Heparan Sulfate Separation, Sequencing, and Isomeric Differ-entiation: Ion Mobility Spectrometry Reveals Specific Iduronic and Glucuronic Acid-Containing Hexasaccharides. Anal. Chem., 2009, 81, 10179-10185.
    • (2009) Anal. Chem , vol.81 , pp. 10179-10185
    • Schenauer, M.R.1    Meissen, J.K.2    Seo, Y.3    Ames, J.B.4    Leary, J.A.5
  • 95
    • 4344648993 scopus 로고    scopus 로고
    • Capillary electrophoresis-mass spectrometry for glycoscreening in biomedical research
    • Zamfir, A. and Peter-Katalini, J. Capillary electrophoresis-mass spectrometry for glycoscreening in biomedical research. Electrophoresis, 2004, 25, 1949-1963.
    • (2004) Electrophoresis , vol.25 , pp. 1949-1963
    • Zamfir, A.1    Peter-Katalini, J.2
  • 96
    • 66149147898 scopus 로고    scopus 로고
    • The structural elucidation of glycosaminoglycans
    • Prabhakar, V.; Capila, I. and Sasisekharan, R. The structural elucidation of glycosaminoglycans. Methods Mol. Biol., 2009, 534, 147-156.
    • (2009) Methods Mol. Biol , vol.534 , pp. 147-156
    • Prabhakar, V.1    Capila, I.2    Sasisekharan, R.3
  • 97
    • 0037232592 scopus 로고    scopus 로고
    • Identification of hyaluronic acid oligosaccharides by direct coupling of capillary electrophoresis with electrospray ion trap mass spectrometry
    • Kuhn, A. V.; Ruttinger, H. H.; Neubert, R. H. and Raith, K. Identification of hyaluronic acid oligosaccharides by direct coupling of capillary electrophoresis with electrospray ion trap mass spectrometry. Rapid Commun. Mass Spectrom., 2003, 17, 576-582.
    • (2003) Rapid Commun. Mass Spectrom , vol.17 , pp. 576-582
    • Kuhn, A.V.1    Ruttinger, H.H.2    Neubert, R.H.3    Raith, K.4
  • 98
    • 0035918014 scopus 로고    scopus 로고
    • Pressure-assisted capillary electrophoresis-electrospray ion trap mass spectrometry for the analysis of heparin depolymerised disaccharides
    • Ruiz-Calero, V.; Moyano, E.; Puignou, L. and Galceran, M. T. (2001) Pressure-assisted capillary electrophoresis-electrospray ion trap mass spectrometry for the analysis of heparin depolymerised disaccharides. J. Chromatogr. A., 2003, 914, 277-291.
    • (2001) J. Chromatogr. A , vol.2003 , Issue.914 , pp. 277-291
    • Ruiz-Calero, V.1    Moyano, E.2    Puignou, L.3    Galceran, M.T.4
  • 99
    • 0036034096 scopus 로고    scopus 로고
    • Structural characterization of chondroitin/dermatan sulfate oligosaccharides from bovine aorta by capillary electrophoresis and electrospray ionization quadrupole time-of-flight tandem mass spectrometry
    • Zamfir, A.; Seidler, D. G.; Kresse, H. and Peter-Katalinc, J. Structural characterization of chondroitin/dermatan sulfate oligosaccharides from bovine aorta by capillary electrophoresis and electrospray ionization quadrupole time-of-flight tandem mass spectrometry. Rapid Commun, Mass SP, 2002, 16, 2015-2024.
    • (2002) Rapid Commun Mass SP , vol.16 , pp. 2015-2024
    • Zamfir, A.1    Seidler, D.G.2    Kresse, H.3    Peter-Katalinc, J.4
  • 100
    • 0034898516 scopus 로고    scopus 로고
    • Glycoscreening by on-line sheathless capillary electrophoresis/electrospray ionization-quadrupole time of flight-tandem mass spectrometry
    • Zamfir, A. and Peter-Katalini, J. Glycoscreening by on-line sheathless capillarelectro-phoresis/electrospray ionization-quadrupole time of flight-tandem mass spectrometry. Electrophoresis, 2001, 22, 2448-2457.
    • (2001) Electrophoresis , vol.22 , pp. 2448-2457
    • Zamfir, A.1    Peter-Katalini, J.2
  • 101
    • 4344702952 scopus 로고    scopus 로고
    • Online sheathless capillary electrophoresis/nanoelectrospray ionization-tandem mass spectrometry for the analysis of glycosaminoglycan oligosaccharides
    • Zamfir, A.; Seidler, D. G.; Schonherr, E.; Kresse, H. and Peter-Katalini,J.Online sheathless capillary electrophoresis/nanoelectrospray ionization-tandem mass spectrometry for the analysis of glycosaminoglycan oligosaccharides. Electrophoresis, 2004, 25, 2010-2016.
    • (2004) Electrophoresis , vol.25 , pp. 2010-2016
    • Zamfir, A.1    Seidler, D.G.2    Schonherr, E.3    Kresse, H.4    Peter-Katalini, J.5
  • 102
    • 0142157732 scopus 로고    scopus 로고
    • Capillary electrophoretic separation of heparin oligosaccharides under conditions amenable to mass spectrometric detection
    • Gunay, N. S. and Linhardt, R. J. Capillary electrophoretic separation of heparin oligosaccharides under conditions amenable to mass spectrometric detection. J. Chromatogr. A., 2003, 1014, 225-233
    • (2003) J. Chromatogr. A , vol.1014 , pp. 225-233
    • Gunay, N.S.1    Linhardt, R.J.2
  • 103
    • 34447324693 scopus 로고    scopus 로고
    • Frontal analysis capillary electrophoresis hyphenated to electros-pray ionization mass spectrometry for the characterization of the antithrombin/heparin pentasaccharide complex
    • Fermas, S.; Gonnet, F.; Varenne, A.; Gareil, P. and Daniel, R. Frontal analysis capillary electrophoresis hyphenated to electros-pray ionization mass spectrometry for the characterization of the antithrombin/heparin pentasaccharide complex. Anal. Chem., 2007, 79, 4987-4993.
    • (2007) Anal. Chem , vol.79 , pp. 4987-4993
    • Fermas, S.1    Gonnet, F.2    Varenne, A.3    Gareil, P.4    Daniel, R.5
  • 104
    • 66149147074 scopus 로고    scopus 로고
    • Labelling heparan sulphate saccharides with chromophore, fluorescence and mass tags for HPLC and MS separations
    • Skidmore, M.; Atrih, A.; Yates, E. and Turnbull, J. E. Labelling heparan sulphate saccharides with chromophore, fluorescence and mass tags for HPLC and MS separations. Methods Mol. Biol., 2009, 534, 157-169.
    • (2009) Methods Mol. Biol , vol.534 , pp. 157-169
    • Skidmore, M.1    Atrih, A.2    Yates, E.3    Turnbull, J.E.4
  • 105
    • 34547767471 scopus 로고    scopus 로고
    • Novel tags for the stable isotopic labeling of carbohydrates and quantitative analysis by mass spectrometry
    • Bowman, M. and Zaia, J. Novel tags for the stable isotopic labeling of carbohydrates and quantitative analysis by mass spectrometry. Anal. Chem., 2007, 76, 5777-5784.
    • (2007) Anal. Chem , vol.76 , pp. 5777-5784
    • Bowman, M.1    Zaia, J.2
  • 106
    • 77950421797 scopus 로고    scopus 로고
    • Comparative glycomics using a tetra-plex stableisotope coded tag
    • Bowman, M. J. and Zaia, J. Comparative glycomics using a tetra-plex stableisotope coded tag. Anal. Chem., 2010, 82, 3023-3031
    • (2010) Anal. Chem , vol.82 , pp. 3023-3031
    • Bowman, M.J.1    Zaia, J.2
  • 107
    • 33646864567 scopus 로고    scopus 로고
    • A tandem mass spectrometric approach to determination of chon-droitin/dermatan sulfate oligosaccharide glycoforms
    • Miller, M. J. C.; Costello, C. E.; Malmström, A. and Zaia, J. A tandem mass spectrometric approach to determination of chon-droitin/dermatan sulfate oligosaccharide glycoforms. Glycobiology, 2006, 16, 502-513.
    • (2006) Glycobiology , vol.16 , pp. 502-513
    • Miller, M.J.C.1    Costello, C.E.2    Malmström, A.3    Zaia, J.4
  • 108
    • 0142195724 scopus 로고    scopus 로고
    • Tandem mass spectrometric strategies for determination of sulfation positions and uronic acid epimerization in chondroitin sulfate oligosaccharides
    • Zaia, J.; Li, X.-Q.; Chan, S.-Y. and Costello, C. E. Tandem mass spectrometric strategies for determination of sulfation positions and uronic acid epimerization in chondroitin sulfate oligosaccharides. J. Am. Soc. Mass Spectrom., 2003,14, 1270-1281.
    • (2003) J. Am. Soc. Mass Spectrom , vol.14 , pp. 1270-1281
    • Zaia, J.1    Li, X.-Q.2    Chan, S.-Y.3    Costello, C.E.4
  • 109
    • 33846419104 scopus 로고    scopus 로고
    • Analysis of oversulfation in a chondroitin sulfate oligosaccharide fraction from bovine aorta by nanoelectrospray ionization quadrupole time-of-flight and Fourier-transform ion cyclotron resonance mass spectrometry
    • Mormann, M.; Zamfir, A. D.; Seidler, D. G.; Kresse, H. and Peter-Katalinic, J. Analysis of oversulfation in a chondroitin sulfate oli-gosaccharide fraction from bovine aorta by nanoelectrospray ionization quadrupole time-of-flight and Fourier-transform ion cyclotron resonance mass spectrometry. J. Am. Soc. Mass Spectrom., 2007, 18, 179-187.
    • (2007) J. Am. Soc. Mass Spectrom , vol.18 , pp. 179-187
    • Mormann, M.1    Zamfir, A.D.2    Seidler, D.G.3    Kresse, H.4    Peter-Katalinic, J.5
  • 110
    • 0242693288 scopus 로고    scopus 로고
    • Structural investigation of chondroitin/dermatan sulfate oligosaccharides from human skin fibroblast decorin
    • Zamfir, A.; Seidler, D. G.; Kresse, H. and Peter-Katalini, J. Structural investigation of chondroitin/dermatan sulfate oligosaccharides from human skin fibroblast decorin. Glycobiology, 2003, 13, 733-742.
    • (2003) Glycobiology , vol.13 , pp. 733-742
    • Zamfir, A.1    Seidler, D.G.2    Kresse, H.3    Peter-Katalini, J.4
  • 111
    • 0037151058 scopus 로고    scopus 로고
    • The structural motif in chondroitin sulfate for adhesion of Plasmodium falciparum-infected erythrocytes comprises disaccharide units of 4-O-sulfated and non-sulfated N-acetylgalactosamine linked to glucuronic acid
    • Chai, W.; Beeson, J. G. and Lawson, A. M. The structural motif in chondroitin sulfate for adhesion of Plasmodium falciparum-infected erythrocytes comprises disaccharide units of 4-O-sulfated and non-sulfated N-acetylgalactosamine linked to glucuronic acid. J. Biol. Chem., 2002, 277, 22438-22446.
    • (2002) J. Biol. Chem , vol.277 , pp. 22438-22446
    • Chai, W.1    Beeson, J.G.2    Lawson, A.M.3
  • 112
    • 67651207436 scopus 로고    scopus 로고
    • Analysis of novel over-and under-sulfated glycosaminoglycan sequences by enzyme cleavage and multiple stage MS
    • Zamfir, A. D.; Flangea, C.; Sisu, E.; Serb, A. F.; Dinca, N.; Bruckner, P. and Seidler, D. G. Analysis of novel over-and under-sulfated glycosaminoglycan sequences by enzyme cleavage and multiple stage MS. Proteomics, 2009, 9, 3435-3444.
    • (2009) Proteomics , vol.9 , pp. 3435-3444
    • Zamfir, A.D.1    Flangea, C.2    Sisu, E.3    Serb, A.F.4    Dinca, N.5    Bruckner, P.6    Seidler, D.G.7
  • 113
    • 80051552809 scopus 로고    scopus 로고
    • Multistage Tandem Mass Spectrometry of Chondroitin Sulfate and Dermatan Sulfate
    • accepted 10/5/10
    • Bielik, A. M. and Zaia, J. Multistage Tandem Mass Spectrometry of Chondroitin Sulfate and Dermatan Sulfate. Int. J. Mass Spectrom., 2011, accepted 10/5/10.
    • (2011) Int. J. Mass Spectrom
    • Bielik, A.M.1    Zaia, J.2
  • 114
    • 7244239255 scopus 로고    scopus 로고
    • Competing fragmentation processes in tandem mass spectra of heparin-like glycosaminoglycans
    • Naggar, E. F.; Costello, C. E. and Zaia, J. Competing fragmentation processes in tandem mass spectra of heparin-like glycosaminoglycans. J. Am. Soc. Mass Spectrom., 2004, 15, 1534-1544.
    • (2004) J. Am. Soc. Mass Spectrom , vol.15 , pp. 1534-1544
    • Naggar, E.F.1    Costello, C.E.2    Zaia, J.3
  • 115
    • 0038290630 scopus 로고    scopus 로고
    • Tandem mass spectrometry of sulfated heparin-like glycosaminoglycan oligosaccharides
    • Zaia, J. and Costello, C. E. Tandem mass spectrometry of sulfated heparin-like glycosaminoglycan oligosaccharides. Anal. Chem., 2003, 75, 2445-2455.
    • (2003) Anal. Chem , vol.75 , pp. 2445-2455
    • Zaia, J.1    Costello, C.E.2
  • 116
    • 0036682699 scopus 로고    scopus 로고
    • Influence of charge state on product ion mass spectra and the determination of 4S/6S sulfation sequence of chondroitin sulfate oligosaccharides
    • McClellan, J. M.; Costello, C. E.; O'Connor, P. B. and Zaia, J. Influence of charge state on product ion mass spectra and the determination of 4S/6S sulfation sequence of chondroitin sulfate oligosaccharides. Anal. Chem., 2002, 74, 3760-3771.
    • (2002) Anal. Chem , vol.74 , pp. 3760-3771
    • McClellan, J.M.1    Costello, C.E.2    O'Connor, P.B.3    Zaia, J.4
  • 117
    • 33846453967 scopus 로고    scopus 로고
    • Electron detachmentdissociation of glycosaminoglycan tetrasaccharides
    • Wolff, J. J.; Amster, I. J.; Chi, L. and Linhardt, R. J. Electron detachmentdissociation of glycosaminoglycan tetrasaccharides. J. Am. Soc. Mass Spectrom., 2007, 18, 234-244.
    • (2007) J. Am. Soc. Mass Spectrom , vol.18 , pp. 234-244
    • Wolff, J.J.1    Amster, I.J.2    Chi, L.3    Linhardt, R.J.4
  • 118
    • 50849102623 scopus 로고    scopus 로고
    • Evaluation of the Experimental Parameters Which Control Electron Detachment Dissociation, and Their Effect on the Fragmentation Efficiency of Glycosaminoglycan Carbohydrates
    • Leach, F. E.; Wolff, J. J.; Laremore, T. N.; Linhardt, R. J. and Amster, I. J. Evaluation of the Experimental Parameters Which Control Electron Detachment Dissociation, and Their Effect on the Fragmentation Efficiency of Glycosaminoglycan Carbohydrates. Int. J. Mass Spectrom., 2008, 276, 110-115.
    • (2008) Int. J. Mass Spectrom , vol.276 , pp. 110-115
    • Leach, F.E.1    Wolff, J.J.2    Laremore, T.N.3    Linhardt, R.J.4    Amster, I.J.5
  • 119
    • 33847612428 scopus 로고    scopus 로고
    • Distinguishing glucuronic from iduronic acid in glycosaminoglycan tetrasaccha-rides by using electron detachment dissociation
    • Wolff, J. J.; Chi, L.; Linhardt, R. J. and Amster, I. J. Distinguishing glucuronic from iduronic acid in glycosaminoglycan tetra-saccharides by using electron detachment dissociation. Anal. Chem., 2007, 79, 2015-2022.
    • (2007) Anal. Chem , vol.79 , pp. 2015-2022
    • Wolff, J.J.1    Chi, L.2    Linhardt, R.J.3    Amster, I.J.4
  • 120
    • 0242291106 scopus 로고    scopus 로고
    • Applications of electron-ion dissociation reactions for analysis of polycationic chitooligosaccharides in Fourier trans-form mass spectrometry
    • Budnik, B. A.; Haselmann, K. F.; Elkin, Y. N.; Gorbach, V. I. and Zubarev, R. A. Applications of electron-ion dissociation reactions for analysis of polycationic chitooligosaccharides in Fourier trans-form mass spectrometry. Anal. Chem., 2003, 75, 5994-6001.
    • (2003) Anal. Chem , vol.75 , pp. 5994-6001
    • Budnik, B.A.1    Haselmann, K.F.2    Elkin, Y.N.3    Gorbach, V.I.4    Zubarev, R.A.5
  • 123
    • 45549094069 scopus 로고    scopus 로고
    • A Tool for the Computer-Assisted Annotation of Mass Spectra of Glycans
    • Ceroni, A.; Maass, K.; Geyer, H.; Geyer, R.; Dell, A. and Haslam, S. M. 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    Dell, A.5    Haslam, S.M.6
  • 124
    • 0035997376 scopus 로고    scopus 로고
    • Order out of chaos: Assembly of ligand binding sites in heparan sulfate
    • Esko, J. D. and Selleck, S. B. Order out of chaos: assembly of ligand binding sites in heparan sulfate. Annu. Rev. Biochem., 2002, 71, 435-471.
    • (2002) Annu. Rev. Biochem , vol.71 , pp. 435-471
    • Esko, J.D.1    Selleck, S.B.2
  • 125
    • 25444451599 scopus 로고    scopus 로고
    • Chemokine-glycosaminoglycan binding: Specificity for CCR2 ligand binding to highly sulfated oligosaccharides using FTICR mass spectrometry
    • Yu, Y.; Sweeney, M. D.; Saad, O. M.; Crown, S. E.; Handel, T. M. and Leary, J. A. Chemokine-glycosaminoglycan binding: specificity for CCR2 ligand binding to highly sulfated oligosaccharides using FTICR mass spectrometry. J. Biol. Chem., 2005, 280, 32200-32208.
    • (2005) J. Biol. Chem , vol.280 , pp. 32200-32208
    • Yu, Y.1    Sweeney, M.D.2    Saad, O.M.3    Crown, S.E.4    Handel, T.M.5    Leary, J.A.6
  • 126
    • 33748755553 scopus 로고    scopus 로고
    • Heterodimerization of CCR2 chemokines and regulation by glycosaminoglycan binding
    • Crown, S. E.; Yu, Y.; Sweeney, M. D.; Leary, J. A. and Handel, T. M. Heterodimerization of CCR2 chemokines and regulation by glycosaminoglycan binding. J. Biol. Chem., 2006, 281, 25438-25446
    • (2006) J. Biol. Chem , vol.281 , pp. 25438-25446
    • Crown, S.E.1    Yu, Y.2    Sweeney, M.D.3    Leary, J.A.4    Handel, T.M.5
  • 127
    • 34548472635 scopus 로고    scopus 로고
    • CCR2 Chemokines Bind Selectively to Acetylated Heparan Sulfate Octasaccharides
    • Schenauer, M. R.; Yu, Y.; Sweeney, M. D. and Leary, J. A. CCR2 Chemokines Bind Selectively to Acetylated Heparan Sulfate Octasaccharides. J. Biol. Chem., 2007, 282, 25182-25188
    • (2007) J. Biol. Chem , vol.282 , pp. 25182-25188
    • Schenauer, M.R.1    Yu, Y.2    Sweeney, M.D.3    Leary, J.A.4
  • 128
    • 33746261450 scopus 로고    scopus 로고
    • Effects of Sulfate Position On Heparin Octasaccharide Binding to CCL2 Examined By Tandem Mass Spectrometry
    • Sweeney, M. D.; Yu, Y. and Leary, J. A. Effects of Sulfate Position on Heparin Octasaccharide Binding to CCL2 Examined by Tandem Mass Spectrometry. J. Am. Soc.Mass Spectrom., 2006, 17, 1114-1119.
    • (2006) J. Am. Soc.Mass Spectrom , vol.17 , pp. 1114-1119
    • Sweeney, M.D.1    Yu, Y.2    Leary, J.A.3
  • 129
    • 33645114817 scopus 로고    scopus 로고
    • Potential Inhibitors of Chemokine Function: Analysis of Noncovalent Complexes of CC Chemokine and Small Polyanionic Molecules by ESI FT-ICR Mass Spectrometry
    • Yu, Y.; Sweeney, M. D.; Saad, O. M. and Leary, J. A. Potential Inhibitors of Chemokine Function: Analysis of Noncovalent Complexes of CC Chemokine and Small Polyanionic Molecules by ESI FT-ICR Mass Spectrometry. J. Am. Soc. Mass Spectrom., 2006, 17, 524-535.
    • (2006) J. Am. Soc. Mass Spectrom , vol.17 , pp. 524-535
    • Yu, Y.1    Sweeney, M.D.2    Saad, O.M.3    Leary, J.A.4
  • 130
    • 62149152738 scopus 로고    scopus 로고
    • Differentiation of 3-O-sulfated heparin disaccharide isomers: Identification of structural aspects of the heparin CCL2 binding motif
    • Meissen, J. K.; Sweeney, M. D.; Girardi, M.; Lawrence, R.; Esko, J. D. and Leary, J. A. Differentiation of 3-O-sulfated heparin disaccharide isomers: identification of structural aspects of the heparin CCL2 binding motif. J. Am. Soc. Mass Spectrom., 2009, 20, 652-657.
    • (2009) J. Am. Soc. Mass Spectrom , vol.20 , pp. 652-657
    • Meissen, J.K.1    Sweeney, M.D.2    Girardi, M.3    Lawrence, R.4    Esko, J.D.5    Leary, J.A.6
  • 131
    • 67049115690 scopus 로고    scopus 로고
    • Pattern and temporal sequence of sulfation of CCR5 N-terminal peptides by tyrosylpro-tein sulfotransferase-2: An assessment of the effects of N-terminal residues
    • Jen, C. H.; Moore, K. L. and Leary, J. A. Pattern and temporal sequence of sulfation of CCR5 N-terminal peptides by tyrosylpro-tein sulfotransferase-2: an assessment of the effects of N-terminal residues, Biochemistry, 2009, 48, 5332-5338.
    • (2009) Biochemistry , vol.48 , pp. 5332-5338
    • Jen, C.H.1    Moore, K.L.2    Leary, J.A.3
  • 132
    • 77956874062 scopus 로고    scopus 로고
    • Competitive binding study of chemokine, sulfated receptor, and glycosaminoglycan interactions by nano-electrospray ionization mass spectrometry
    • Jen, C. H. and Leary, J. A. A competitive binding study of chemokine, sulfated receptor, and glycosaminoglycan interactions by nano-electrospray ionization mass spectrometry. Anal. Bio-chem., 2010, 407, 134-140.
    • (2010) Anal. Bio-Chem , vol.407 , pp. 134-140
    • Jen, C.H.1    Leary, J.A.A.2
  • 133
    • 31544445500 scopus 로고    scopus 로고
    • Multimers of the fibro-blast growth factor (FGF)-FGF receptor-saccharide complex are formed on long oligomers of heparin
    • Harmer, N. J.; Robinson, C. J.; Adam, L. E.; Ilag, L. L.; Robinson, C. V.; Gallagher, J. T. and Blundell, T. L. Multimers of the fibro-blast growth factor (FGF)-FGF receptor-saccharide complex are formed on long oligomers of heparin. Biochem. J., 2006, 393, 741-748.
    • (2006) Biochem. J , vol.393 , pp. 741-748
    • Harmer, N.J.1    Robinson, C.J.2    Adam, L.E.3    Ilag, L.L.4    Robinson, C.V.5    Gallagher, J.T.6    Blundell, T.L.7
  • 134
    • 34548046764 scopus 로고    scopus 로고
    • Glycosamino-glycans as naturally occurring combinatorial libraries: Developing a mass spectrometry-based strategy for characterization of anti-thrombin interaction with low molecular weight heparin and heparin oligomers
    • Abzalimov, R. R.; Dubin, P. L. and Kaltashov, I. A. Glycosamino-glycans as naturally occurring combinatorial libraries: developing a mass spectrometry-based strategy for characterization of anti-thrombin interaction with low molecular weight heparin and heparin oligomers. Anal. Chem., 2007, 79, 6055-6063.
    • (2007) Anal. Chem , vol.79 , pp. 6055-6063
    • Abzalimov, R.R.1    Dubin, P.L.2    Kaltashov, I.A.3
  • 135
    • 33646869917 scopus 로고    scopus 로고
    • Size-exclusion chromatography of heparin oligosaccharides at high and low pressure
    • Ziegler, A. and Zaia, J. Size-exclusion chromatography of heparin oligosaccharides at high and low pressure. J. Chromatogr. B. Analyt. Technol. Biomed Life Sci., 2006, 837, 76-86.
    • (2006) J. Chromatogr. B. AnaLyt. Technol. Biomed Life Sci , vol.837 , pp. 76-86
    • Ziegler, A.1    Zaia, J.2
  • 136
    • 77951684925 scopus 로고    scopus 로고
    • Screening for anticoagulant heparan sulfate octasaccharides and fine structure characterization using tandem mass spectrometry
    • Naimy, H.; Leymarie, N. and Zaia, J. Screening for anticoagulant heparan sulfate octasaccharides and fine structure characterization using tandem mass spectrometry. Biochemistry, 2010, 49, 3743-3752.
    • (2010) Biochemistry , vol.49 , pp. 3743-3752
    • Naimy, H.1    Leymarie, N.2    Zaia, J.3
  • 137
    • 0034307401 scopus 로고    scopus 로고
    • Sequencing sulfated oligosaccharides from mucins by liquid chromatography and electrospray ionization tandem mass spectrometry
    • Thomsson, K. A.; Karlsson, H. and Hansson, G. Sequencing sulfated oligosaccharides from mucins by liquid chromatography and electrospray ionization tandem mass spectrometry. Anal. Chem., 2000, 72, 4543-4549.
    • (2000) Anal. Chem , vol.72 , pp. 4543-4549
    • Thomsson, K.A.1    Karlsson, H.2    Hansson, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.