메뉴 건너뛰기




Volumn 47, Issue 10, 2008, Pages 3155-3161

Characterization of heparin oligosaccharides binding specifically to antithrombin III using mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SITES; CELL PROLIFERATION; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; PROTEINS;

EID: 40549123949     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi702043e     Document Type: Article
Times cited : (45)

References (58)
  • 2
    • 0011764529 scopus 로고
    • The Role of Galactose and Xylose in the Linkage of Heparin to Protein
    • Lindahl, U., and Roden, L. (1965) The Role of Galactose and Xylose in the Linkage of Heparin to Protein. J. Biol. Chem. 240, 2821-2826.
    • (1965) J. Biol. Chem , vol.240 , pp. 2821-2826
    • Lindahl, U.1    Roden, L.2
  • 3
    • 0000230148 scopus 로고
    • The Role of Serine in the Linkage of Heparin to Protein
    • Lindahl, U., Cifonelli, J. A., Lindahl, B., and Roden, L. (1965) The Role of Serine in the Linkage of Heparin to Protein. J. Biol. Chem. 240, 2817-2820.
    • (1965) J. Biol. Chem , vol.240 , pp. 2817-2820
    • Lindahl, U.1    Cifonelli, J.A.2    Lindahl, B.3    Roden, L.4
  • 4
    • 0019489909 scopus 로고
    • Biosynthesis of heparin. Transfer of N-acetylglucosamine to heparan sulfate oligosaccharides
    • Forsee, W. T., and Roden, L. (1981) Biosynthesis of heparin. Transfer of N-acetylglucosamine to heparan sulfate oligosaccharides. J. Biol. Chem. 256, 7240-7247.
    • (1981) J. Biol. Chem , vol.256 , pp. 7240-7247
    • Forsee, W.T.1    Roden, L.2
  • 5
    • 0027427953 scopus 로고
    • Biosynthesis of heparin/heparan sulfate. Identification of a 70 kDa protein catalyzing both the D-glucuronosyl- and the N-acetyl-D-glucosaminyl-transferase reactions
    • Lind, T., Lindahl, U., and Lidholt, K. (1993) Biosynthesis of heparin/heparan sulfate. Identification of a 70 kDa protein catalyzing both the D-glucuronosyl- and the N-acetyl-D-glucosaminyl-transferase reactions. J. Biol. Chem. 268, 20705-20708.
    • (1993) J. Biol. Chem , vol.268 , pp. 20705-20708
    • Lind, T.1    Lindahl, U.2    Lidholt, K.3
  • 6
    • 0020857860 scopus 로고
    • Assay of N-acetylheparosan deacetylase with a capsular polysaccharide from Escherichia coli K5 as substrate
    • Navia, J. L., Riesenfeld, J., Vann, W. F., Lindahl, U., and Roden, L. (1983) Assay of N-acetylheparosan deacetylase with a capsular polysaccharide from Escherichia coli K5 as substrate. Anal. Biochem. 135, 134-140.
    • (1983) Anal. Biochem , vol.135 , pp. 134-140
    • Navia, J.L.1    Riesenfeld, J.2    Vann, W.F.3    Lindahl, U.4    Roden, L.5
  • 7
    • 0015935891 scopus 로고
    • Biosynthesis of heparin. II. Formation of sulfamino groups
    • Lindahl, U., Backstrom, G., Jansson, L., and Hallen, A. (1973) Biosynthesis of heparin. II. Formation of sulfamino groups. J. Biol. Chem. 248, 7234-7241.
    • (1973) J. Biol. Chem , vol.248 , pp. 7234-7241
    • Lindahl, U.1    Backstrom, G.2    Jansson, L.3    Hallen, A.4
  • 8
    • 0019154319 scopus 로고
    • Biosynthesis of heparin. Assay and properties of the microsomal N-acetyl-D-glucosaminyl N-deacetylase
    • Riesenfeld, J., Hook, M., and Lindahl, U. (1980) Biosynthesis of heparin. Assay and properties of the microsomal N-acetyl-D-glucosaminyl N-deacetylase. J. Biol. Chem. 255, 922-928.
    • (1980) J. Biol. Chem , vol.255 , pp. 922-928
    • Riesenfeld, J.1    Hook, M.2    Lindahl, U.3
  • 9
    • 0020472835 scopus 로고
    • Biosynthesis of heparin. Concerted action of early polymer-modification reactions
    • Riesenfeld, J., Hook, M., and Lindahl, U. (1982) Biosynthesis of heparin. Concerted action of early polymer-modification reactions. J. Biol. Chem. 257, 421-425.
    • (1982) J. Biol. Chem , vol.257 , pp. 421-425
    • Riesenfeld, J.1    Hook, M.2    Lindahl, U.3
  • 10
    • 0025907137 scopus 로고
    • Biosynthesis of heparin. Use of Escherichia coli K5 capsular polysaccharide as a model substrate in enzymic polymer-modification reactions
    • Kusche, M., Hannesson, H. H., and Lindahl, U. (1991) Biosynthesis of heparin. Use of Escherichia coli K5 capsular polysaccharide as a model substrate in enzymic polymer-modification reactions. Biochem. J. 275, 151-158.
    • (1991) Biochem. J , vol.275 , pp. 151-158
    • Kusche, M.1    Hannesson, H.H.2    Lindahl, U.3
  • 11
    • 0025914498 scopus 로고
    • Coupling of N-deacetylation and N-sulfation in a Chinese hamster ovary cell mutant defective in heparan sulfate N-sulfotransferase
    • Bame, K. J., Reddy, R. V., and Esko, J. D. (1991) Coupling of N-deacetylation and N-sulfation in a Chinese hamster ovary cell mutant defective in heparan sulfate N-sulfotransferase. J. Biol. Chem. 266, 12461-12468.
    • (1991) J. Biol. Chem , vol.266 , pp. 12461-12468
    • Bame, K.J.1    Reddy, R.V.2    Esko, J.D.3
  • 12
    • 0026792841 scopus 로고
    • Biosynthesis of heparin. The D-glucuronosyl- and N-acetyl-D-glucosaminyltransferase reactions and their relation to polymer modification
    • Lidholt, K., and Lindahl, U. (1992) Biosynthesis of heparin. The D-glucuronosyl- and N-acetyl-D-glucosaminyltransferase reactions and their relation to polymer modification. Biochem. J. 287, 21-29.
    • (1992) Biochem. J , vol.287 , pp. 21-29
    • Lidholt, K.1    Lindahl, U.2
  • 13
    • 0015530554 scopus 로고
    • Biosynthesis of L-iduronic acid in heparin: Epimerization of D-glucuronic acid on the polymer level
    • Lindahl, U., Backstrom, G., Malmstrom, A., and Fransson, L. A. (1972) Biosynthesis of L-iduronic acid in heparin: Epimerization of D-glucuronic acid on the polymer level. Biochem. Biophys. Res. Commun. 46, 985-991.
    • (1972) Biochem. Biophys. Res. Commun , vol.46 , pp. 985-991
    • Lindahl, U.1    Backstrom, G.2    Malmstrom, A.3    Fransson, L.A.4
  • 14
    • 0016138795 scopus 로고
    • Biosynthesis of heparin. 3. Formation of iduronic acid residues
    • Hook, M., Lindahl, U., Backstrom, G., Malmstrom, A., and Fransson, L. (1974) Biosynthesis of heparin. 3. Formation of iduronic acid residues. J. Biol. Chem. 249, 3908-3915.
    • (1974) J. Biol. Chem , vol.249 , pp. 3908-3915
    • Hook, M.1    Lindahl, U.2    Backstrom, G.3    Malmstrom, A.4    Fransson, L.5
  • 16
    • 0025090881 scopus 로고
    • Biosynthesis of heparin. O-Sulfation of D-glucuronic acid units
    • Kusche, M., and Lindahl, U. (1990) Biosynthesis of heparin. O-Sulfation of D-glucuronic acid units. J. Biol. Chem. 265, 15403-15409.
    • (1990) J. Biol. Chem , vol.265 , pp. 15403-15409
    • Kusche, M.1    Lindahl, U.2
  • 17
    • 0019314440 scopus 로고
    • Biosynthesis of heparin. Concerted action of late polymer-modification reactions
    • Jacobsson, I., and Lindahl, U. (1980) Biosynthesis of heparin. Concerted action of late polymer-modification reactions. J. Biol. Chem. 255, 5094-5100.
    • (1980) J. Biol. Chem , vol.255 , pp. 5094-5100
    • Jacobsson, I.1    Lindahl, U.2
  • 18
    • 0035997376 scopus 로고    scopus 로고
    • Order out of chaos: Assembly of ligand binding sites in heparan sulfate
    • Esko, J. D., and Selleck, S. B. (2002) Order out of chaos: Assembly of ligand binding sites in heparan sulfate. Annu. Rev. Biochem. 71, 435-471.
    • (2002) Annu. Rev. Biochem , vol.71 , pp. 435-471
    • Esko, J.D.1    Selleck, S.B.2
  • 22
    • 0028773286 scopus 로고
    • Serpins: The uncut version
    • Goldsmith, E. J., and Mottonen, J. (1994) Serpins: The uncut version. Structure 2, 241-244.
    • (1994) Structure , vol.2 , pp. 241-244
    • Goldsmith, E.J.1    Mottonen, J.2
  • 23
    • 0015853889 scopus 로고
    • Anticoagulant action of heparin
    • Damus, P. S., Hicks, M., and Rosenberg, R. D. (1973) Anticoagulant action of heparin. Nature 246, 355-357.
    • (1973) Nature , vol.246 , pp. 355-357
    • Damus, P.S.1    Hicks, M.2    Rosenberg, R.D.3
  • 24
    • 0026529071 scopus 로고
    • Conversion of antithrombin from an inhibitor of thrombin to a substrate with reduced heparin affinity and enhanced conformational stability by binding of a tetradecapeptide corresponding to the P1 to P14 region of the putative reactive bond loop of the inhibitor
    • Bjork, I., Ylinenjarvi, K., Olson, S. T., and Bock, P. E. (1992) Conversion of antithrombin from an inhibitor of thrombin to a substrate with reduced heparin affinity and enhanced conformational stability by binding of a tetradecapeptide corresponding to the P1 to P14 region of the putative reactive bond loop of the inhibitor. J. Biol. Chem. 267, 1976-1982.
    • (1992) J. Biol. Chem , vol.267 , pp. 1976-1982
    • Bjork, I.1    Ylinenjarvi, K.2    Olson, S.T.3    Bock, P.E.4
  • 25
    • 0018409404 scopus 로고
    • Conformational changes accompanying the binding of antithrombin III to thrombin
    • Villanueva, G., and Danishefsky, I. (1979) Conformational changes accompanying the binding of antithrombin III to thrombin. Biochemistry 18, 810-817.
    • (1979) Biochemistry , vol.18 , pp. 810-817
    • Villanueva, G.1    Danishefsky, I.2
  • 26
    • 0021690695 scopus 로고
    • Extension and structural variability of the antithrombin-binding sequence in heparin
    • Lindahl, U., Thunberg, L., Backstrom, G., Riesenfeld, J., Nordling, K., and Bjork, I. (1984) Extension and structural variability of the antithrombin-binding sequence in heparin. J. Biol. Chem. 259, 12368-12376.
    • (1984) J. Biol. Chem , vol.259 , pp. 12368-12376
    • Lindahl, U.1    Thunberg, L.2    Backstrom, G.3    Riesenfeld, J.4    Nordling, K.5    Bjork, I.6
  • 28
    • 0020108082 scopus 로고
    • Further characterization of the antithrombin-binding sequence in heparin
    • Thunberg, L., Backstrom, G., and Lindahl, U. (1982) Further characterization of the antithrombin-binding sequence in heparin. Carbohydr. Res. 100, 393-410.
    • (1982) Carbohydr. Res , vol.100 , pp. 393-410
    • Thunberg, L.1    Backstrom, G.2    Lindahl, U.3
  • 29
    • 0021677341 scopus 로고
    • Sequence variation in heparin octasaccharides with high affinity for antithrombin III
    • Atha, D. H., Stephens, A. W., Rimon, A., and Rosenberg, R. D. (1984) Sequence variation in heparin octasaccharides with high affinity for antithrombin III. Biochemistry 23, 5801-5812.
    • (1984) Biochemistry , vol.23 , pp. 5801-5812
    • Atha, D.H.1    Stephens, A.W.2    Rimon, A.3    Rosenberg, R.D.4
  • 30
    • 0022368634 scopus 로고
    • Contribution of monosaccharide residues in heparin binding to antithrombin III
    • Atha, D. H., Lormeau, J. C., Petitou, M., Rosenberg, R. D., and Choay, J. (1985) Contribution of monosaccharide residues in heparin binding to antithrombin III. Biochemistry 24, 6723-6729.
    • (1985) Biochemistry , vol.24 , pp. 6723-6729
    • Atha, D.H.1    Lormeau, J.C.2    Petitou, M.3    Rosenberg, R.D.4    Choay, J.5
  • 31
    • 0019862158 scopus 로고
    • The antithrombin-binding sequence of heparin. Location of essential N-sulfate groups
    • Riesenfeld, J., Thunberg, L., Hook, M., and Lindahl, U. (1981) The antithrombin-binding sequence of heparin. Location of essential N-sulfate groups. J. Biol. Chem. 256, 2389-2394.
    • (1981) J. Biol. Chem , vol.256 , pp. 2389-2394
    • Riesenfeld, J.1    Thunberg, L.2    Hook, M.3    Lindahl, U.4
  • 32
    • 0020544564 scopus 로고
    • The antithrombin-binding sequence in heparin. Identification of an essential 6-O-sulfate group
    • Lindahl, U., Backstrom, G., and Thunberg, L. (1983) The antithrombin-binding sequence in heparin. Identification of an essential 6-O-sulfate group. J. Biol. Chem. 258, 9826-9830.
    • (1983) J. Biol. Chem , vol.258 , pp. 9826-9830
    • Lindahl, U.1    Backstrom, G.2    Thunberg, L.3
  • 33
    • 0001668795 scopus 로고
    • Evidence for a 3-O-sulfated D-glucosamine residue in the antithrombin-binding sequence of heparin
    • Lindahl, U., Backstrom, G., Thunberg, L., and Leder, I. G. (1980) Evidence for a 3-O-sulfated D-glucosamine residue in the antithrombin-binding sequence of heparin. Proc. Natl. Acad. Sci. U.S.A. 77, 6551-6555.
    • (1980) Proc. Natl. Acad. Sci. U.S.A , vol.77 , pp. 6551-6555
    • Lindahl, U.1    Backstrom, G.2    Thunberg, L.3    Leder, I.G.4
  • 34
    • 0024288551 scopus 로고
    • Binding of heparin to antithrombin III: A chemical proof of the critical role played by a 3-sulfated 2-amino-2-deoxy-D-glucose residue
    • Petitou, M., Duchaussoy, P., Lederman, I., Choay, J., and Sinay, P. (1988) Binding of heparin to antithrombin III: A chemical proof of the critical role played by a 3-sulfated 2-amino-2-deoxy-D-glucose residue. Carbohydr. Res. 179, 163-172.
    • (1988) Carbohydr. Res , vol.179 , pp. 163-172
    • Petitou, M.1    Duchaussoy, P.2    Lederman, I.3    Choay, J.4    Sinay, P.5
  • 35
    • 0027448951 scopus 로고
    • Minimal sequence in heparin/heparan sulfate required for binding of basic fibroblast growth factor
    • Maccarana, M., Casu, B., and Lindahl, U. (1993) Minimal sequence in heparin/heparan sulfate required for binding of basic fibroblast growth factor. J. Biol. Chem. 268, 23898-23905.
    • (1993) J. Biol. Chem , vol.268 , pp. 23898-23905
    • Maccarana, M.1    Casu, B.2    Lindahl, U.3
  • 36
    • 0032800308 scopus 로고    scopus 로고
    • Characterization of fibroblast growth factor 1 binding heparan sulfate domain
    • Kreuger, J., Prydz, K., Pettersson, R. F., Lindahl, U., and Salmivirta, M. (1999) Characterization of fibroblast growth factor 1 binding heparan sulfate domain. Glycobiology 9, 723-729.
    • (1999) Glycobiology , vol.9 , pp. 723-729
    • Kreuger, J.1    Prydz, K.2    Pettersson, R.F.3    Lindahl, U.4    Salmivirta, M.5
  • 37
    • 0032981696 scopus 로고    scopus 로고
    • A strategy for rapid sequencing of heparan sulfate and heparin saccharides
    • Turnbull, J. E., Hopwood, J. J., and Gallagher, J. T. (1999) A strategy for rapid sequencing of heparan sulfate and heparin saccharides. Proc. Natl. Acad. Sci. U.S.A. 96, 2698-2703.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 2698-2703
    • Turnbull, J.E.1    Hopwood, J.J.2    Gallagher, J.T.3
  • 40
    • 0025324531 scopus 로고
    • Structural variation in the antithrombin III binding site region and its occurrence in heparin from different sources
    • Loganathan, D., Wang, H. M., Mallis, L. M., and Linhardt, R. J. (1990) Structural variation in the antithrombin III binding site region and its occurrence in heparin from different sources. Biochemistry 29, 4362-4368.
    • (1990) Biochemistry , vol.29 , pp. 4362-4368
    • Loganathan, D.1    Wang, H.M.2    Mallis, L.M.3    Linhardt, R.J.4
  • 41
    • 0028855668 scopus 로고
    • Preparation and structural characterization of large heparin-derived oligosaccharides
    • Pervin, A., Gallo, C., Jandik, K. A., Han, X. J., and Linhardt, R. J. (1995) Preparation and structural characterization of large heparin-derived oligosaccharides. Glycobiology 5, 83-95.
    • (1995) Glycobiology , vol.5 , pp. 83-95
    • Pervin, A.1    Gallo, C.2    Jandik, K.A.3    Han, X.J.4    Linhardt, R.J.5
  • 42
    • 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. D. (2002) 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. 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.D.6
  • 43
    • 2942578189 scopus 로고    scopus 로고
    • Mapping critical biological motifs and biosynthetic pathways of heparan sulfate
    • Lawrence, R., Kuberan, B., Lech, M., Beeler, D. L., and Rosenberg, R. D. (2004) Mapping critical biological motifs and biosynthetic pathways of heparan sulfate. Glycobiology 14, 467-479.
    • (2004) Glycobiology , vol.14 , pp. 467-479
    • Lawrence, R.1    Kuberan, B.2    Lech, M.3    Beeler, D.L.4    Rosenberg, R.D.5
  • 44
    • 33646869917 scopus 로고    scopus 로고
    • Size-exclusion chromatography of heparin oligosaccharides at high and low pressure
    • Ziegler, A., and Zaia, J. (2006) Size-exclusion chromatography of heparin oligosaccharides at high and low pressure. J. Chromatogr. 837, 76-86.
    • (2006) J. Chromatogr , vol.837 , pp. 76-86
    • Ziegler, A.1    Zaia, J.2
  • 45
    • 31544445500 scopus 로고    scopus 로고
    • Multimers of the fibroblast 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. (2006) Multimers of the fibroblast growth factor (FGF)-FGF receptor-saccharide complex are formed on long oligomers of heparin. Biochem. J. 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
  • 46
    • 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., Hsu, A. R., Handel, T. M., and Leary, J. A. (2005) Chemokine-glycosaminoglycan binding: Specificity for CCR2 ligand binding to highly sulfated oligosaccharides using FTICR mass spectrometry. J. Biol. Chem. 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    Hsu, A.R.5    Handel, T.M.6    Leary, J.A.7
  • 47
    • 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. (2006) Effects of sulfate position on heparin octasaccharide binding to CCL2 examined by tandem mass spectrometry. J. Am. Soc. Mass Spectrom. 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
  • 48
    • 34548472635 scopus 로고    scopus 로고
    • CCR2 chemokines bind selectively to acetylated heparan sulfate octasaccharides
    • in press
    • Schenauer, M. R., Yu, Y., Sweeney, M. D., and Leary, J. A. (2008) CCR2 chemokines bind selectively to acetylated heparan sulfate octasaccharides. J. Biol. Chem. (in press).
    • (2008) J. Biol. Chem
    • Schenauer, M.R.1    Yu, Y.2    Sweeney, M.D.3    Leary, J.A.4
  • 50
    • 0026712126 scopus 로고
    • Chemiluminescence high-performance liquid chromatography for the determination of hyaluronic acid, chondroitin sulphate and dermatan sulphate
    • Akiyama, H., Shidawara, S., Mada, A., Toyoda, H., Toida, T., and Imanari, T. (1992) Chemiluminescence high-performance liquid chromatography for the determination of hyaluronic acid, chondroitin sulphate and dermatan sulphate. J. Chromatogr. 579, 203-207.
    • (1992) J. Chromatogr , vol.579 , pp. 203-207
    • Akiyama, H.1    Shidawara, S.2    Mada, A.3    Toyoda, H.4    Toida, T.5    Imanari, T.6
  • 51
    • 40549125327 scopus 로고    scopus 로고
    • Comparative glycomics of connective tissue glycosaminoglycans
    • submitted for publication
    • Hitchcock, A. M., Yates, K. E., Costello, C. E., and Zaia, J. (2008) Comparative glycomics of connective tissue glycosaminoglycans. J. Biol. Chem. (submitted for publication).
    • (2008) J. Biol. Chem
    • Hitchcock, A.M.1    Yates, K.E.2    Costello, C.E.3    Zaia, J.4
  • 52
    • 0842283940 scopus 로고    scopus 로고
    • Normal-phase nanoscale liquid chromatography-mass spectrometry of underivatized oligosaccharides at low-femtomole sensitivity
    • Wuhrer, M., Koeleman, C. A., Deelder, A. M., and Hokke, C. H. (2004) Normal-phase nanoscale liquid chromatography-mass spectrometry of underivatized oligosaccharides at low-femtomole sensitivity. Anal. Chem. 76, 833-838.
    • (2004) Anal. Chem , vol.76 , pp. 833-838
    • Wuhrer, M.1    Koeleman, C.A.2    Deelder, A.M.3    Hokke, C.H.4
  • 53
    • 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. (2005) Protein glycosylation analyzed by normal-phase nano-liquid chromatography-mass spectrometry of glycopeptides. Anal. Chem. 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
  • 56
    • 0026465688 scopus 로고
    • 1-N-Glycyl β-oligosaccharide derivatives as stable intermediates for the formation of glycoconjugate probes
    • Manger, I. D., Rademacher, T. W., and Dwek, R. A. (1992) 1-N-Glycyl β-oligosaccharide derivatives as stable intermediates for the formation of glycoconjugate probes. Biochemistry 31, 10724-10732.
    • (1992) Biochemistry , vol.31 , pp. 10724-10732
    • Manger, I.D.1    Rademacher, T.W.2    Dwek, R.A.3
  • 57
    • 0025908340 scopus 로고
    • Chemical synthesis of glycosaminoglycans: New approaches to antithrombotic drugs
    • Petitou, M., Lormeau, J. C., and Choay, J. (1991) Chemical synthesis of glycosaminoglycans: New approaches to antithrombotic drugs. Nature 350, 30-33.
    • (1991) Nature , vol.350 , pp. 30-33
    • Petitou, M.1    Lormeau, J.C.2    Choay, J.3
  • 58
    • 34548046764 scopus 로고    scopus 로고
    • Glycosaminoglycans 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. (2007) Glycosaminoglycans 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. 79, 6055-6063.
    • (2007) Anal. Chem , vol.79 , pp. 6055-6063
    • Abzalimov, R.R.1    Dubin, P.L.2    Kaltashov, I.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.