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Volumn 12, Issue 110, 2015, Pages

Heparan sulfate and heparin interactions with proteins

Author keywords

Cations; Heparan sulfate; Heparin; Polysaccharide; Protein binding; Redundancy

Indexed keywords

BINDING SITES; BIOACTIVITY; BIOCHEMISTRY; CELL MEMBRANES; DNA SEQUENCES; POLYSACCHARIDES; POSITIVE IONS; PROTEINS; REDUNDANCY; SULFUR COMPOUNDS;

EID: 84942019114     PISSN: 17425689     EISSN: 17425662     Source Type: Journal    
DOI: 10.1098/rsif.2015.0589     Document Type: Review
Times cited : (232)

References (162)
  • 1
    • 0015072728 scopus 로고
    • Evidence for a (1!4)-linked 4-O-(-L-idopyranosyluronic acid 2- sulfate)-(2-deoxy-2-sulfoamino-D-glucopyranosyl 6- sulfate) sequence in heparin. Long-range H-H coupling in 4-deoxy-hex-4-enopyranosides
    • Perlin AS, Mackie DM, Dietrich CP. 1971 Evidence for a (1!4)-linked 4-O-(-L-idopyranosyluronic acid 2- sulfate)-(2-deoxy-2-sulfoamino-D-glucopyranosyl 6- sulfate) sequence in heparin. Long-range H-H coupling in 4-deoxy-hex-4-enopyranosides. Carbohydr. Res. 18, 185-194. (doi:10.1016/S0008-6215(00)80341-9).
    • (1971) Carbohydr. Res. , vol.18 , pp. 185-194
    • Perlin, A.S.1    Mackie, D.M.2    Dietrich, C.P.3
  • 2
    • 9044227271 scopus 로고    scopus 로고
    • Characterization of sulfation patterns of beef and pig mucosal heparins by nuclear magnetic resonance spectroscopy
    • Casu B et al. 1996 Characterization of sulfation patterns of beef and pig mucosal heparins by nuclear magnetic resonance spectroscopy. Arzneimittelforschung 46, 472-477.
    • (1996) Arzneimittelforschung , vol.46 , pp. 472-477
    • Casu, B.1
  • 3
    • 0035984272 scopus 로고    scopus 로고
    • Heparin and heparan sulfate: Structure and function
    • Rabenstein DL. 2002 Heparin and heparan sulfate: structure and function. Nat. Prod. Rep. 19, 312-331. (doi:10.1039/b100916h).
    • (2002) Nat. Prod. Rep. , vol.19 , pp. 312-331
    • Rabenstein, D.L.1
  • 4
    • 0022346849 scopus 로고
    • Lack of correlation between 'in vitro' and 'in vivo' antithrombotic activity of heparin fractions and related compounds. Heparan sulfate as an antithrombotic agent 'in vivo'
    • Bianchini P, Osima B, Parma B, Nader HB, Dietrich CP. 1985 Lack of correlation between 'in vitro' and 'in vivo' antithrombotic activity of heparin fractions and related compounds. Heparan sulfate as an antithrombotic agent 'in vivo'. Thromb. Res. 40, 597-607. (doi:10.1016/0049-3848(85)90298-1).
    • (1985) Thromb. Res. , vol.40 , pp. 597-607
    • Bianchini, P.1    Osima, B.2    Parma, B.3    Nader, H.B.4    Dietrich, C.P.5
  • 5
    • 0032061391 scopus 로고    scopus 로고
    • Structure of heparan sulfate: Identification of variable and constant oligosaccharide domains in eight heparan sulfates of different origins
    • Noisy-le-grand
    • Dietrich CP et al. 1998 Structure of heparan sulfate: identification of variable and constant oligosaccharide domains in eight heparan sulfates of different origins. Cell Mol. Biol. (Noisy-le-grand). 44, 417-429.
    • (1998) Cell Mol. Biol , vol.44 , pp. 417-429
    • Dietrich, C.P.1
  • 6
    • 0022384993 scopus 로고
    • Molecular distinctions between heparan sulphate and heparin. Analysis of sulphation patterns indicates that heparan sulphate and heparin are separate families of N-sulphated polysaccharides
    • Gallagher JT, Walker A. 1985 Molecular distinctions between heparan sulphate and heparin. Analysis of sulphation patterns indicates that heparan sulphate and heparin are separate families of N-sulphated polysaccharides. Biochem. J. 230, 665-674.
    • (1985) Biochem. J. , vol.230 , pp. 665-674
    • Gallagher, J.T.1    Walker, A.2
  • 7
    • 0024319230 scopus 로고
    • Structure of heparin and heparin fragments
    • Casu B. 1989 Structure of heparin and heparin fragments. Ann. NY Acad. Sci. 556, 1-17. (doi:10.1111/j.1749-6632.1989.tb22485.x).
    • (1989) Ann. NY Acad. Sci , vol.556 , pp. 1-17
    • Casu, B.1
  • 8
    • 0000391007 scopus 로고
    • Correlation between structure and function of heparin
    • Rosenberg RD, Lam L. 1979 Correlation between structure and function of heparin. Proc. Natl Acad. Sci. USA 76, 1218-1222. (doi:10.1073/pnas.76.3.1218).
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 1218-1222
    • Rosenberg, R.D.1    Lam, L.2
  • 9
    • 0034533546 scopus 로고    scopus 로고
    • Characterization of unfractionated heparin: Comparison of materials from the last 50 years
    • Mulloy B, Gray E, Barrowcliffe TW. 2000 Characterization of unfractionated heparin: comparison of materials from the last 50 years. Thromb. Haemost. 84, 1052-1056.
    • (2000) Thromb. Haemost. , vol.84 , pp. 1052-1056
    • Mulloy, B.1    Gray, E.2    Barrowcliffe, T.W.3
  • 10
    • 84884749301 scopus 로고    scopus 로고
    • The solution structure of heparan sulfate differs from that of heparin: Implications for function
    • Khan S, Fung KW, Rodriguez E, Patel R, Gor J, Mulloy B, Perkins SJ. 2013 The solution structure of heparan sulfate differs from that of heparin: implications for function. J. Biol. Chem. 288, 27737-27751. (doi:10.1074/jbc.M113.492223).
    • (2013) J. Biol. Chem , vol.288 , pp. 27737-27751
    • Khan, S.1    Fung, K.W.2    Rodriguez, E.3    Patel, R.4    Gor, J.5    Mulloy, B.6    Perkins, S.J.7
  • 11
    • 73249136226 scopus 로고    scopus 로고
    • Semi-rigid solution structures of heparin by constrained X-ray scattering modelling: New insight into heparin- protein complexes
    • Khan S, Gor J, Mulloy B, Perkins SJ. 2010 Semi-rigid solution structures of heparin by constrained X-ray scattering modelling: new insight into heparin- protein complexes. J. Mol. Biol. 395, 504-521. (doi:10.1016/j.jmb.2009.10.064).
    • (2010) J. Mol. Biol , vol.395 , pp. 504-521
    • Khan, S.1    Gor, J.2    Mulloy, B.3    Perkins, S.J.4
  • 12
    • 84883716644 scopus 로고    scopus 로고
    • A non-hemorrhagic hybrid heparin/heparan sulfate with anticoagulant potential. Carbohydr
    • Brito AS et al. 2014 A non-hemorrhagic hybrid heparin/heparan sulfate with anticoagulant potential. Carbohydr. Polym. 99, 372-378. (doi:10.1016/j.carbpol.2013.08.063).
    • (2014) Polym , vol.99 , pp. 372-378
    • Brito, A.S.1
  • 14
    • 0016504233 scopus 로고
    • The heterogeneity of heparan sulfate from beef-lung tissue: P.m.r.-spectral evidence
    • Dietrich CP, Nader HB, Perlin AS. 1975 The heterogeneity of heparan sulfate from beef-lung tissue: p.m.r.-spectral evidence. Carbohydr. Res. 41, 334-338. (doi:10.1016/S0008-6215(00)87036-6).
    • (1975) Carbohydr. Res. , vol.41 , pp. 334-338
    • Dietrich, C.P.1    Nader, H.B.2    Perlin, A.S.3
  • 15
    • 0028346379 scopus 로고
    • Liver heparan sulfate structure. A novel molecular design
    • Lyon M, Deakin JA, Gallagher JT. 1994 Liver heparan sulfate structure. A novel molecular design. J. Biol. Chem. 269, 11208-11215.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11208-11215
    • Lyon, M.1    Deakin, J.A.2    Gallagher, J.T.3
  • 17
    • 0023280413 scopus 로고
    • Heparin sequences in the heparan sulfate chains of an endothelial cell proteoglycan
    • Nader HB, Dietrich CP, Buonassisi V, Colburn P. 1987 Heparin sequences in the heparan sulfate chains of an endothelial cell proteoglycan. Proc. Natl Acad. Sci. USA 84, 3565-3569. (doi:10.1073/pnas.84.11.3565).
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 3565-3569
    • Nader, H.B.1    Dietrich, C.P.2    Buonassisi, V.3    Colburn, P.4
  • 18
    • 84877712933 scopus 로고    scopus 로고
    • Comparative glycomics of leukocyte glycosaminoglycans
    • Shao C, Shi X, White M, Huang Y, Hartshorn K, Zaia J. 2013 Comparative glycomics of leukocyte glycosaminoglycans. FEBS J. 280, 2447-2461. (doi:10.1111/febs.12231).
    • (2013) FEBS J. , vol.280 , pp. 2447-2461
    • Shao, C.1    Shi, X.2    White, M.3    Huang, Y.4    Hartshorn, K.5    Zaia, J.6
  • 19
    • 0033520398 scopus 로고    scopus 로고
    • Heparin is a unique marker of progenitors in the glial cell lineage
    • Stringer SE, Mayer-Proschel M, Kalyani A, Rao M, Gallagher JT. 1999 Heparin is a unique marker of progenitors in the glial cell lineage. J. Biol. Chem. 274, 25455-25460. (doi:10.1074/jbc.274.36.25455).
    • (1999) J. Biol. Chem. , vol.274 , pp. 25455-25460
    • Stringer, S.E.1    Mayer-Proschel, M.2    Kalyani, A.3    Rao, M.4    Gallagher, J.T.5
  • 20
    • 84873024385 scopus 로고    scopus 로고
    • Heparan sulfate biosynthesis: Regulation and variability
    • Kreuger J, Kjellen L. 2012 Heparan sulfate biosynthesis: regulation and variability. J. Histochem. Cytochem. 60, 898-907. (doi:10.1369/0022155412464972).
    • (2012) J. Histochem. Cytochem. , vol.60 , pp. 898-907
    • Kreuger, J.1    Kjellen, L.2
  • 21
    • 84859835237 scopus 로고    scopus 로고
    • A highly efficient tree structure for the biosynthesis of heparan sulfate accounts for the commonly observed disaccharides and suggests a mechanism for domain synthesis
    • Rudd TR, Yates EA. 2012 A highly efficient tree structure for the biosynthesis of heparan sulfate accounts for the commonly observed disaccharides and suggests a mechanism for domain synthesis. Mol. Biosyst. 8, 1499-1506. (doi:10.1039/c2mb25019e).
    • (2012) Mol. Biosyst. , vol.8 , pp. 1499-1506
    • Rudd, T.R.1    Yates, E.A.2
  • 22
    • 1642539182 scopus 로고    scopus 로고
    • Altered expression of sulfotransferases, glucuronosyltransferases and mrp transporters in FVB/mrp12/2 mice
    • Bain LJ, Feldman RA. 2003 Altered expression of sulfotransferases, glucuronosyltransferases and mrp transporters in FVB/mrp12/2 mice. Xenobiotica 33, 1173-1183. (doi:10.1080/00498250310001609138).
    • (2003) Xenobiotica , vol.33 , pp. 1173-1183
    • Bain, L.J.1    Feldman, R.A.2
  • 23
    • 55549104048 scopus 로고    scopus 로고
    • Sulf loss influences N-, 2-O-, and 6-O-sulfation of multiple heparan sulfate proteoglycans and modulates fibroblast growth factor signaling
    • Lamanna WC, Frese MA, Balleininger M, Dierks T. 2008 Sulf loss influences N-, 2-O-, and 6-O-sulfation of multiple heparan sulfate proteoglycans and modulates fibroblast growth factor signaling. J. Biol. Chem. 283, 27724-27735. (doi:10.1074/jbc.M802130200).
    • (2008) J. Biol. Chem. , vol.283 , pp. 27724-27735
    • Lamanna, W.C.1    Frese, M.A.2    Balleininger, M.3    Dierks, T.4
  • 24
    • 0035253193 scopus 로고    scopus 로고
    • Heparan sulfate: Decoding a dynamic multifunctional cell regulator
    • Turnbull J, Powell A, Guimond S. 2001 Heparan sulfate: decoding a dynamic multifunctional cell regulator. Trends Cell Biol. 11, 75-82. (doi:10.1016/S0962-8924(00)01897-3).
    • (2001) Trends Cell Biol. , vol.11 , pp. 75-82
    • Turnbull, J.1    Powell, A.2    Guimond, S.3
  • 25
    • 0028304452 scopus 로고
    • Cell surface syndecan-1 on distinct cell types differs in fine structure and ligand binding of its heparan sulfate chains
    • Kato M, Wang H, Bernfield M, Gallagher JT, Turnbull JE. 1994 Cell surface syndecan-1 on distinct cell types differs in fine structure and ligand binding of its heparan sulfate chains. J. Biol. Chem. 269, 18881-18890.
    • (1994) J. Biol. Chem , vol.269 , pp. 18881-18890
    • Kato, M.1    Wang, H.2    Bernfield, M.3    Gallagher, J.T.4    Turnbull, J.E.5
  • 26
    • 0015451872 scopus 로고
    • Cell-cycle dependent desquamation of heparan sulfate from the cell surface
    • Kraemer PM, Tobey RA. 1972 Cell-cycle dependent desquamation of heparan sulfate from the cell surface. J. Cell Biol. 55, 713-717. (doi:10.1083/jcb.55.3.713).
    • (1972) J. Cell Biol. , vol.55 , pp. 713-717
    • Kraemer, P.M.1    Tobey, R.A.2
  • 27
    • 0021435832 scopus 로고
    • Incorporation of 35Ssulfate and 3H-glucosamine into heparan and chondroitin sulfates during the cell cycle of B16-F10 cells
    • Blair OC, Sartorelli AC. 1984 Incorporation of 35Ssulfate and 3H-glucosamine into heparan and chondroitin sulfates during the cell cycle of B16-F10 cells. Cytometry 5, 281-288. (doi:10.1002/cyto.990050311).
    • (1984) Cytometry , vol.5 , pp. 281-288
    • Blair, O.C.1    Sartorelli, A.C.2
  • 28
    • 0028021649 scopus 로고
    • Heparan sulfate proteoglycan and control of cell proliferation: Enhanced synthesis induced by phorbol ester (PMA) during G(1)-phase
    • Porcionatto MA, Pinto CR, Dietrich CP, Nader HB. 1994 Heparan sulfate proteoglycan and control of cell proliferation: enhanced synthesis induced by phorbol ester (PMA) during G(1)-phase. Braz. J. Med. Biol. Res. 27, 2185-2190.
    • (1994) Braz. J. Med. Biol. Res. , vol.27 , pp. 2185-2190
    • Porcionatto, M.A.1    Pinto, C.R.2    Dietrich, C.P.3    Nader, H.B.4
  • 29
    • 0032531271 scopus 로고    scopus 로고
    • Stimulation of heparan sulfate proteoglycan synthesis and secretion during G1 phase induced by growth factors and PMA
    • Porcionatto MA, Moreira CR, Lotfi CF, Armelin HA, Dietrich CP, Nader HB. 1998 Stimulation of heparan sulfate proteoglycan synthesis and secretion during G1 phase induced by growth factors and PMA. J. Cell. Biochem. 70, 563-572. (doi:10.1002/(SICI)1097-4644(19980915)70:4, 563::AIDJCB12.3.0.CO;2-I).
    • (1998) J. Cell. Biochem , vol.70 , pp. 563-572
    • Porcionatto, M.A.1    Moreira, C.R.2    Lotfi, C.F.3    Armelin, H.A.4    Dietrich, C.P.5    Nader, H.B.6
  • 31
    • 0033650826 scopus 로고    scopus 로고
    • Conformation and dynamics of heparin and heparan sulfate
    • Mulloy B, Forster MJ. 2000 Conformation and dynamics of heparin and heparan sulfate. Glycobiology 10, 1147-1156. (doi:10.1093/glycob/10.11.1147).
    • (2000) Glycobiology , vol.10 , pp. 1147-1156
    • Mulloy, B.1    Forster, M.J.2
  • 33
    • 42649106868 scopus 로고    scopus 로고
    • The heparanome and regulation of cell function: Structures, functions and challenges
    • Ori A, Wilkinson MC, Fernig DG. 2008 The heparanome and regulation of cell function: structures, functions and challenges. Front. Biosci. 13, 4309-4338. (doi:10.2741/3007).
    • (2008) Front. Biosci. , vol.13 , pp. 4309-4338
    • Ori, A.1    Wilkinson, M.C.2    Fernig, D.G.3
  • 34
    • 79957592466 scopus 로고    scopus 로고
    • A systems biology approach for the investigation of the heparin/heparan sulfate interactome
    • Ori A, Wilkinson MC, Fernig DG. 2011 A systems biology approach for the investigation of the heparin/heparan sulfate interactome. J. Biol. Chem. 286, 19892-19904. (doi:10.1074/jbc.M111.228114)
    • (2011) J. Biol. Chem , vol.286 , pp. 19892-19904
    • Ori, A.1    Wilkinson, M.C.2    Fernig, D.G.3
  • 35
    • 2442549670 scopus 로고    scopus 로고
    • Interactions of heparin/heparan sulfate with proteins: Appraisal of structural factors and experimental approaches
    • Powell AK, Yates EA, Fernig DG, Turnbull JE. 2004 Interactions of heparin/heparan sulfate with proteins: Appraisal of structural factors and experimental approaches. Glycobiology 14, R17-R30. (doi:10.1093/glycob/cwh051).
    • (2004) Glycobiology , vol.14 , pp. R17-R30
    • Powell, A.K.1    Yates, E.A.2    Fernig, D.G.3    Turnbull, J.E.4
  • 36
    • 84902215812 scopus 로고    scopus 로고
    • Demystifying heparan sulfate-protein interactions
    • Xu D, Esko JD. 2014 Demystifying heparan sulfate-protein interactions. Annu. Rev. Biochem. 83, 129-157. (doi:10.1146/annurev-biochem-060713-035314).
    • (2014) Annu. Rev. Biochem. , vol.83 , pp. 129-157
    • Xu, D.1    Esko, J.D.2
  • 37
    • 33746614761 scopus 로고    scopus 로고
    • Interactions between heparan sulfate and proteins: The concept of specificity
    • Kreuger J, Spillmann D, Li JP, Lindahl U. 2006 Interactions between heparan sulfate and proteins: The concept of specificity. J. Cell Biol. 174, 323-327. (doi:10.1083/jcb.200604035).
    • (2006) J. Cell Biol. , vol.174 , pp. 323-327
    • Kreuger, J.1    Spillmann, D.2    Li, J.P.3    Lindahl, U.4
  • 38
    • 0034907578 scopus 로고    scopus 로고
    • Heparan sulfate: Growth control with a restricted sequence menu
    • Gallagher JT. 2001 Heparan sulfate: growth control with a restricted sequence menu. J. Clin. Invest. 108, 357-361. (doi:10.1172/JCI13713).
    • (2001) J. Clin. Invest. , vol.108 , pp. 357-361
    • Gallagher, J.T.1
  • 39
    • 0036469507 scopus 로고    scopus 로고
    • Heparin-protein interactions
    • Capila I, Linhardt RJ. 2002 Heparin-protein interactions. Angew. Chem. 41, 391-412. (doi:10.1002/1521-3773(20020201)41:3, 390::aidanie390.3.0.co;2-b).
    • (2002) Angew. Chem. , vol.41 , pp. 391-412
    • Capila, I.1    Linhardt, R.J.2
  • 40
    • 70149088868 scopus 로고    scopus 로고
    • Interactions between heparan sulfate and proteins-design and functional implications
    • Lindahl U, Li JP. 2009 Interactions between heparan sulfate and proteins-design and functional implications. Int. Rev. Cell. Mol. Biol. 276, 105-159. (doi:10.1016/S1937-6448(09)76003-4).
    • (2009) Int. Rev. Cell. Mol. Biol. , vol.276 , pp. 105-159
    • Lindahl, U.1    Li, J.P.2
  • 41
    • 84880275146 scopus 로고    scopus 로고
    • Heparan sulfate-protein binding specificity
    • Mosc
    • Nugent MA, Zaia J, Spencer JL. 2013 Heparan sulfate-protein binding specificity. Biochemistry (Mosc). 78, 726-735. (doi:10.1134/S0006297913070055).
    • (2013) Biochemistry , vol.78 , pp. 726-735
    • Nugent, M.A.1    Zaia, J.2    Spencer, J.L.3
  • 42
    • 25844452894 scopus 로고    scopus 로고
    • Prospects for glycoinformatics
    • Perez S, Mulloy B. 2005 Prospects for glycoinformatics. Curr. Opin. Struct. Biol. 15, 517-524. (doi:10.1016/j.sbi.2005.08.005).
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 517-524
    • Perez, S.1    Mulloy, B.2
  • 43
    • 0027317486 scopus 로고
    • Mitogenic activity of acidic fibroblast growth factor is enhanced by highly sulfated oligosaccharides derived from heparin and heparan sulfate
    • Gambarini AG, Miyamoto CA, Lima GA, Nader HB, Dietrich CP. 1993 Mitogenic activity of acidic fibroblast growth factor is enhanced by highly sulfated oligosaccharides derived from heparin and heparan sulfate. Mol. Cell. Biochem. 124, 121-129. (doi:10.1007/BF00929204).
    • (1993) Mol. Cell. Biochem , vol.124 , pp. 121-129
    • Gambarini, A.G.1    Miyamoto, C.A.2    Lima, G.A.3    Nader, H.B.4    Dietrich, C.P.5
  • 44
    • 0031948943 scopus 로고    scopus 로고
    • Interactions of putative heparin-binding domains of basic fibroblast growth factor and its receptor, FGFR-1, with heparin using synthetic peptides
    • Kinsella L, Chen HL, Smith JA, Rudland PS, Fernig DG. 1998 Interactions of putative heparin-binding domains of basic fibroblast growth factor and its receptor, FGFR-1, with heparin using synthetic peptides. Glycoconj. J. 15, 419-422. (doi:10.1023/A:1006986104865).
    • (1998) Glycoconj. J. , vol.15 , pp. 419-422
    • Kinsella, L.1    Chen, H.L.2    Smith, J.A.3    Rudland, P.S.4    Fernig, D.G.5
  • 45
    • 0032571310 scopus 로고    scopus 로고
    • Interaction of heparan sulfate from mammary cells with acidic fibroblast growth factor (FGF) and basic FGF. Regulation of the activity of basic FGF by high and low affinity binding sites in heparan sulfate
    • Rahmoune H, Chen HL, Gallagher JT, Rudland PS, Fernig DG. 1998 Interaction of heparan sulfate from mammary cells with acidic fibroblast growth factor (FGF) and basic FGF. Regulation of the activity of basic FGF by high and low affinity binding sites in heparan sulfate. J. Biol. Chem. 273, 7303-7310. (doi:10.1074/jbc.273.13.7303).
    • (1998) J. Biol. Chem , vol.273 , pp. 7303-7310
    • Rahmoune, H.1    Chen, H.L.2    Gallagher, J.T.3    Rudland, P.S.4    Fernig, D.G.5
  • 46
    • 85016456375 scopus 로고    scopus 로고
    • Distribution of heparan sulfate oligosaccharides in murine mucopolysaccharidosis type IIIA
    • Mason K, Meikle P, Hopwood J, Fuller M. 2014 Distribution of heparan sulfate oligosaccharides in murine mucopolysaccharidosis type IIIA. Metabolites 4, 1088-1100. (doi:10.3390/metabo4041088).
    • (2014) Metabolites , vol.4 , pp. 1088-1100
    • Mason, K.1    Meikle, P.2    Hopwood, J.3    Fuller, M.4
  • 48
    • 4344598247 scopus 로고    scopus 로고
    • Heparanase gene silencing, tumor invasiveness, angiogenesis, and metastasis
    • Edovitsky E, Elkin M, Zcharia E, Peretz T, Vlodavsky I. 2004 Heparanase gene silencing, tumor invasiveness, angiogenesis, and metastasis. J. Natl Cancer Inst. 96, 1219-1230. (doi:10.1093/jnci/djh230).
    • (2004) J. Natl Cancer Inst , vol.96 , pp. 1219-1230
    • Edovitsky, E.1    Elkin, M.2    Zcharia, E.3    Peretz, T.4    Vlodavsky, I.5
  • 50
    • 0036301061 scopus 로고    scopus 로고
    • Prion protein interaction with glycosaminoglycan occurs with the formation of oligomeric complexes stabilized by Cu(II) bridges
    • Gonzalez-Iglesias R, Pajares MA, Ocal C, Espinosa JC, Oesch B, Gasset M. 2002 Prion protein interaction with glycosaminoglycan occurs with the formation of oligomeric complexes stabilized by Cu(II) bridges. J. Mol. Biol. 319, 527-540. (doi:10.1016/S0022-2836(02)00341-8).
    • (2002) J. Mol. Biol , vol.319 , pp. 527-540
    • Gonzalez-Iglesias, R.1    Pajares, M.A.2    Ocal, C.3    Espinosa, J.C.4    Oesch, B.5    Gasset, M.6
  • 51
    • 0028832566 scopus 로고
    • Differences in the interaction of heparin with arginine and lysine and the importance of these basic amino acids in the binding of heparin to acidic fibroblast growth factor
    • Fromm JR, Hileman RE, Caldwell EE, Weiler JM, Linhardt RJ. 1995 Differences in the interaction of heparin with arginine and lysine and the importance of these basic amino acids in the binding of heparin to acidic fibroblast growth factor. Arch. Biochem. Biophys. 323, 279-287. (doi:10.1006/abbi.1995.9963).
    • (1995) Arch. Biochem. Biophys , vol.323 , pp. 279-287
    • Fromm, J.R.1    Hileman, R.E.2    Caldwell, E.E.3    Weiler, J.M.4    Linhardt, R.J.5
  • 52
    • 84898069475 scopus 로고    scopus 로고
    • Fibroblast growth factor-based signaling through synthetic heparan sulfate blocks copolymers studied using high cell density threedimensional cell printing
    • Sterner E et al. 2014 Fibroblast growth factor-based signaling through synthetic heparan sulfate blocks copolymers studied using high cell density threedimensional cell printing. J. Biol. Chem. 289, 9754-9765. (doi:10.1074/jbc.M113.546937).
    • (2014) J. Biol. Chem , vol.289 , pp. 9754-9765
    • Sterner, E.1
  • 53
    • 78650440835 scopus 로고    scopus 로고
    • The latent ampholytic nature of glycosaminoglycan (GAG) oligosaccharides facilitates their separation by isoelectric focusing
    • Holman J, Skidmore MA, Rudd TR, Yates EA. 2010 The latent ampholytic nature of glycosaminoglycan (GAG) oligosaccharides facilitates their separation by isoelectric focusing. Anal. Methods 2, 1550-1554. (doi:10.1039/c0ay00340a).
    • (2010) Anal. Methods , vol.2 , pp. 1550-1554
    • Holman, J.1    Skidmore, M.A.2    Rudd, T.R.3    Yates, E.A.4
  • 54
    • 84879217983 scopus 로고    scopus 로고
    • An approach for separation and complete structural sequencing of heparin/heparan sulfate-like oligosaccharides
    • Huang R, Liu J, Sharp JS. 2013 An approach for separation and complete structural sequencing of heparin/heparan sulfate-like oligosaccharides. Anal. Chem. 85, 5787-5795. (doi:10.1021/ac400439a).
    • (2013) Anal. Chem. , vol.85 , pp. 5787-5795
    • Huang, R.1    Liu, J.2    Sharp, J.S.3
  • 55
    • 84879201986 scopus 로고    scopus 로고
    • Method development and analysis of free HS and HS in proteoglycans from pre- And postmenopausal women: Evidence for biosynthetic pathway changes in sulfotransferase and sulfatase enzymes
    • Wei W, Miller RL, Leary JA. 2013 Method development and analysis of free HS and HS in proteoglycans from pre- And postmenopausal women: evidence for biosynthetic pathway changes in sulfotransferase and sulfatase enzymes. Anal. Chem. 85, 5917-5923. (doi:10.1021/ac400690g).
    • (2013) Anal. Chem. , vol.85 , pp. 5917-5923
    • Wei, W.1    Miller, R.L.2    Leary, J.A.3
  • 56
    • 84904509423 scopus 로고    scopus 로고
    • Capillary electrophoresis for total glycosaminoglycan analysis
    • Ucakturk E, Cai C, Li L, Li G, Zhang F, Linhardt RJ. 2014 Capillary electrophoresis for total glycosaminoglycan analysis. Anal. Bioanal. Chem. 406, 4617-4626. (doi:10.1007/s00216-014-7859-8).
    • (2014) Anal. Bioanal. Chem. , vol.406 , pp. 4617-4626
    • Ucakturk, E.1    Cai, C.2    Li, L.3    Li, G.4    Zhang, F.5    Linhardt, R.J.6
  • 57
    • 0016874584 scopus 로고
    • Selective N-desulfation of heparin with dimethyl sulfoxide containing water or methanol
    • Inoue Y, Nagasawa K. 1976 Selective N-desulfation of heparin with dimethyl sulfoxide containing water or methanol. Carbohydr. Res. 46, 87-95. (doi:10.1016/S0008-6215(00)83533-8).
    • (1976) Carbohydr. Res. , vol.46 , pp. 87-95
    • Inoue, Y.1    Nagasawa, K.2
  • 58
    • 0026428315 scopus 로고
    • Sulfation of some chemically-modified heparins. Formation of a 3-sulfate analog of heparin
    • Rej RN, Ludwig-Baxter KG, Perlin AS. 1991 Sulfation of some chemically-modified heparins. Formation of a 3-sulfate analog of heparin. Carbohydr. Res. 210, 299-310. (doi:10.1016/0008-6215(91)80130-F).
    • (1991) Carbohydr. Res. , vol.210 , pp. 299-310
    • Rej, R.N.1    Ludwig-Baxter, K.G.2    Perlin, A.S.3
  • 59
    • 0029658229 scopus 로고    scopus 로고
    • 1H and 13C NMR spectral assignments of the major sequences of twelve systematically modified heparin derivatives
    • Yates EA, Santini F, Guerrini M, Naggi A, Torri G, Casu B. 1996 1H and 13C NMR spectral assignments of the major sequences of twelve systematically modified heparin derivatives. Carbohydr. Res. 294, 15-27. (doi:10.1016/S0008-6215(96)00213-3).
    • (1996) Carbohydr. Res. , vol.294 , pp. 15-27
    • Yates, E.A.1    Santini, F.2    Guerrini, M.3    Naggi, A.4    Torri, G.5    Casu, B.6
  • 60
    • 84857609340 scopus 로고    scopus 로고
    • Chemical reduction of carboxyl groups in heparin abolishes its vasodilatory activity
    • Paredes-Gamero EJ et al. 2012 Chemical reduction of carboxyl groups in heparin abolishes its vasodilatory activity. J. Cell. Biochem. 113, 1359-1367. (doi:10.1002/jcb.24008).
    • (2012) J. Cell. Biochem , vol.113 , pp. 1359-1367
    • Paredes-Gamero, E.J.1
  • 61
    • 77950795510 scopus 로고    scopus 로고
    • Generating heparan sulfate saccharide libraries for glycomics applications
    • Powell AK, Ahmed YA, Yates EA, Turnbull JE. 2010 Generating heparan sulfate saccharide libraries for glycomics applications. Nat. Protoc. 5, 821-833. (doi:10.1038/nprot.2010.17).
    • (2010) Nat. Protoc. , vol.5 , pp. 821-833
    • Powell, A.K.1    Ahmed, Y.A.2    Yates, E.A.3    Turnbull, J.E.4
  • 62
    • 84903852019 scopus 로고    scopus 로고
    • Characterisation of the interaction of neuropilin-1 with heparin and a heparan sulfate mimetic library of heparin-derived sugars
    • Uniewicz KA, Ori A, Ahmed YA, Yates EA, Fernig DG. 2014 Characterisation of the interaction of neuropilin-1 with heparin and a heparan sulfate mimetic library of heparin-derived sugars. PeerJ. 2, e461. (doi:10.7717/peerj.461).
    • (2014) PeerJ , vol.2 , pp. e461
    • Uniewicz, K.A.1    Ori, A.2    Ahmed, Y.A.3    Yates, E.A.4    Fernig, D.G.5
  • 63
    • 0032800308 scopus 로고    scopus 로고
    • Characterization of fibroblast growth factor 1 binding heparan sulfate domain
    • Kreuger J, Prydz K, Pettersson RF, Lindahl U, Salmivirta M. 1999 Characterization of fibroblast growth factor 1 binding heparan sulfate domain. Glycobiology 9, 723-729. (doi:10.1093/glycob/9.7.723).
    • (1999) Glycobiology , vol.9 , pp. 723-729
    • Kreuger, J.1    Prydz, K.2    Pettersson, R.F.3    Lindahl, U.4    Salmivirta, M.5
  • 64
    • 0035903106 scopus 로고    scopus 로고
    • Sequence analysis of heparan sulfate epitopes with graded affinities for fibroblast growth factors 1 and 2
    • Kreuger J, Salmivirta M, Sturiale L, Gimenez-Gallego G, Lindahl U. 2001 Sequence analysis of heparan sulfate epitopes with graded affinities for fibroblast growth factors 1 and 2. J. Biol. Chem. 276, 30744-30752. (doi:10.1074/jbc.M102628200).
    • (2001) J. Biol. Chem. , vol.276 , pp. 30744-30752
    • Kreuger, J.1    Salmivirta, M.2    Sturiale, L.3    Gimenez-Gallego, G.4    Lindahl, U.5
  • 65
    • 0027448951 scopus 로고
    • Minimal sequence in heparin/heparan sulfate required for binding of basic fibroblast growth factor
    • Maccarana M, Casu B, Lindahl U. 1993 Minimal sequence in heparin/heparan sulfate required for binding of basic fibroblast growth factor. J. Biol. Chem. 268, 23898-23905. (doi:10.1007/bf01209909).
    • (1993) J. Biol. Chem. , vol.268 , pp. 23898-23905
    • Maccarana, M.1    Casu, B.2    Lindahl, U.3
  • 66
    • 0026727774 scopus 로고
    • Identification of the basic fibroblast growth factor binding sequence in fibroblast heparan sulfate
    • Turnbull JE, Fernig DG, Ke Y, Wilkinson MC, Gallagher JT. 1992 Identification of the basic fibroblast growth factor binding sequence in fibroblast heparan sulfate. J. Biol. Chem. 267, 10337-10341.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10337-10341
    • Turnbull, J.E.1    Fernig, D.G.2    Ke, Y.3    Wilkinson, M.C.4    Gallagher, J.T.5
  • 67
    • 0027316282 scopus 로고
    • Heparan sulphate: Functional role as a modulator of fibroblast growth factor activity
    • Turnbull JE, Gallagher JT. 1993 Heparan sulphate: functional role as a modulator of fibroblast growth factor activity. Biochem. Soc. Trans. 21, 477-482.
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 477-482
    • Turnbull, J.E.1    Gallagher, J.T.2
  • 68
    • 18444362115 scopus 로고    scopus 로고
    • Minimal heparin/heparan sulfate sequences for binding to fibroblast growth factor-1
    • Guerrini M et al. 2002 Minimal heparin/heparan sulfate sequences for binding to fibroblast growth factor-1. Biochem. Biophys. Res. Commun. 292, 222-230. (doi:10.1006/bbrc.2002.6634).
    • (2002) Biochem. Biophys. Res. Commun , vol.292 , pp. 222-230
    • Guerrini, M.1
  • 69
    • 0022368634 scopus 로고
    • Contribution of monosaccharide residues in heparin binding to antithrombin III
    • Atha DH, Lormeau JC, Petitou M, Rosenberg RD, Choay J. 1985 Contribution of monosaccharide residues in heparin binding to antithrombin III. Biochemistry 24, 6723-6729. (doi:10.1021/bi00344a063).
    • (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
  • 70
    • 0023646713 scopus 로고
    • Contribution of 3-O- And 6-O-sulfated glucosamine residues in the heparin-induced conformational change in antithrombin III
    • Atha DH, Lormeau JC, Petitou M, Rosenberg RD, Choay J. 1987 Contribution of 3-O- And 6-O-sulfated glucosamine residues in the heparin-induced conformational change in antithrombin III. Biochemistry 26, 6454-6461. (doi:10.1021/bi00394a024).
    • (1987) Biochemistry , vol.26 , pp. 6454-6461
    • Atha, D.H.1    Lormeau, J.C.2    Petitou, M.3    Rosenberg, R.D.4    Choay, J.5
  • 71
    • 0034947648 scopus 로고    scopus 로고
    • Molecular diversity of heparan sulfate
    • Esko JD, Lindahl U. 2001 Molecular diversity of heparan sulfate. J. Clin. Invest. 108, 169-173. (doi:10.1172/JCI200113530).
    • (2001) J. Clin. Invest. , vol.108 , pp. 169-173
    • Esko, J.D.1    Lindahl, U.2
  • 72
    • 84898074624 scopus 로고    scopus 로고
    • A heparin-like glycosaminoglycan from shrimp containing high levels of 3-O-sulfated D-glucosamine groups in an unusual trisaccharide sequence
    • Chavante SF, Brito AS, Lima M, Yates E, Nader H, Guerrini M, Torri G, Bisio A. 2014 A heparin-like glycosaminoglycan from shrimp containing high levels of 3-O-sulfated D-glucosamine groups in an unusual trisaccharide sequence. Carbohydr. Res. 390, 59-66. (doi:10.1016/j.carres.2014.03.002).
    • (2014) Carbohydr. Res. , vol.390 , pp. 59-66
    • Chavante, S.F.1    Brito, A.S.2    Lima, M.3    Yates, E.4    Nader, H.5    Guerrini, M.6    Torri, G.7    Bisio, A.8
  • 73
    • 84877253457 scopus 로고    scopus 로고
    • Antithrombin stabilisation by sulfated carbohydrates correlates with anticoagulant activity
    • Lima MA et al. 2013 Antithrombin stabilisation by sulfated carbohydrates correlates with anticoagulant activity. Med. Chem. Commun. 4, 870-873. (doi:10.1039/c3md00048f ).
    • (2013) Med. Chem. Commun. , vol.4 , pp. 870-873
    • Lima, M.A.1
  • 74
    • 84871422681 scopus 로고    scopus 로고
    • An unusual antithrombinbinding heparin octasaccharide with an additional 3-O-sulfated glucosamine in the active pentasaccharide sequence
    • Guerrini M et al. 2013 An unusual antithrombinbinding heparin octasaccharide with an additional 3-O-sulfated glucosamine in the active pentasaccharide sequence. Biochem. J. 449, 343-351. (doi:10.1042/BJ20121309).
    • (2013) Biochem. J. , vol.449 , pp. 343-351
    • Guerrini, M.1
  • 75
    • 33750030783 scopus 로고    scopus 로고
    • Conformational transitions induced in heparin octasaccharides by binding with antithrombin III
    • Guerrini M, Guglieri S, Beccati D, Torri G, Viskov C, Mourier P. 2006 Conformational transitions induced in heparin octasaccharides by binding with antithrombin III. Biochem. J. 399, 191-198. (doi:10.1042/BJ20060656).
    • (2006) Biochem. J. , vol.399 , pp. 191-198
    • Guerrini, M.1    Guglieri, S.2    Beccati, D.3    Torri, G.4    Viskov, C.5    Mourier, P.6
  • 76
    • 55549136766 scopus 로고    scopus 로고
    • Antithrombin-binding octasaccharides and role of extensions of the active pentasaccharide sequence in the specificity and strength of interaction. Evidence for very high affinity induced by an unusual glucuronic acid residue
    • Guerrini M et al. 2008 Antithrombin-binding octasaccharides and role of extensions of the active pentasaccharide sequence in the specificity and strength of interaction. Evidence for very high affinity induced by an unusual glucuronic acid residue. J. Biol. Chem. 283, 26 662-26 675. (doi:10.1074/jbc.M801102200).
    • (2008) J. Biol. Chem. , vol.283 , pp. 26662-26675
    • Guerrini, M.1
  • 77
    • 84926628027 scopus 로고    scopus 로고
    • Antithrombin-binding oligosaccharides: Structural diversities in a unique function?
    • Guerrini M, Mourier PA, Torri G, Viskov C. 2014 Antithrombin-binding oligosaccharides: structural diversities in a unique function? Glycoconj. J. 31, 409-416. (doi:10.1007/s10719-014-9543-9).
    • (2014) Glycoconj. J. , vol.31 , pp. 409-416
    • Guerrini, M.1    Mourier, P.A.2    Torri, G.3    Viskov, C.4
  • 78
    • 84883679862 scopus 로고    scopus 로고
    • Heparin dodecasaccharide containing two antithrombin-binding pentasaccharides: Structural features and biological properties
    • Viskov C et al. 2013 Heparin dodecasaccharide containing two antithrombin-binding pentasaccharides: structural features and biological properties. J. Biol. Chem. 288, 25895-25907. (doi:10.1074/jbc.M113.485268).
    • (2013) J. Biol. Chem. , vol.288 , pp. 25895-25907
    • Viskov, C.1
  • 79
    • 68949090333 scopus 로고    scopus 로고
    • Interaction of antithrombin with sulfated, low molecular weight lignins: Opportunities for potent, selective modulation of antithrombin function
    • Henry BL, Connell J, Liang A, Krishnasamy C, Desai UR. 2009 Interaction of antithrombin with sulfated, low molecular weight lignins: opportunities for potent, selective modulation of antithrombin function. J. Biol. Chem. 284, 20897-20908. (doi:10.1074/jbc.M109.013359).
    • (2009) J. Biol. Chem. , vol.284 , pp. 20897-20908
    • Henry, B.L.1    Connell, J.2    Liang, A.3    Krishnasamy, C.4    Desai, U.R.5
  • 80
    • 0041846670 scopus 로고    scopus 로고
    • Crystal structure of antithrombin in a heparin-bound intermediate state
    • Johnson DJ, Huntington JA. 2003 Crystal structure of antithrombin in a heparin-bound intermediate state. Biochemistry 42, 8712-8719. (doi:10.1021/bi034524y).
    • (2003) Biochemistry , vol.42 , pp. 8712-8719
    • Johnson, D.J.1    Huntington, J.A.2
  • 81
    • 84869073602 scopus 로고    scopus 로고
    • On the specificity of heparin/heparan sulfate binding to proteins. Anion-binding sites on antithrombin and thrombin are fundamentally different
    • Mosier PD, Krishnasamy C, Kellogg GE, Desai UR. 2012 On the specificity of heparin/heparan sulfate binding to proteins. Anion-binding sites on antithrombin and thrombin are fundamentally different. PLoS ONE 7, e48632. (doi:10.1371/journal.pone.0048632).
    • (2012) PLoS ONE , vol.7 , pp. e48632
    • Mosier, P.D.1    Krishnasamy, C.2    Kellogg, G.E.3    Desai, U.R.4
  • 82
    • 85020708402 scopus 로고    scopus 로고
    • Dynamic properties of the native free antithrombin from molecular dynamics simulations: Computational evidence for solvent-exposed Arg393 side chain
    • Toth L, Fekete A, Balogh G, Bereczky Z, Komaromi I. 2014 Dynamic properties of the native free antithrombin from molecular dynamics simulations: computational evidence for solvent-exposed Arg393 side chain. J. Biomol. Struct. Dyn. 8, 1-14.
    • (2014) J. Biomol. Struct. Dyn , vol.8 , pp. 1-14
    • Toth, L.1    Fekete, A.2    Balogh, G.3    Bereczky, Z.4    Komaromi, I.5
  • 83
    • 0037047348 scopus 로고    scopus 로고
    • Fibroblast growth factor receptors 1 and 2 interact differently with heparin/heparan sulfate. Implications for dynamic assembly of a ternary signaling complex
    • Powell AK, Fernig DG, Turnbull JE. 2002 Fibroblast growth factor receptors 1 and 2 interact differently with heparin/heparan sulfate. Implications for dynamic assembly of a ternary signaling complex. J. Biol. Chem. 277, 28554-28563. (doi:10.1074/jbc.M111754200).
    • (2002) J. Biol. Chem , vol.277 , pp. 28554-28563
    • Powell, A.K.1    Fernig, D.G.2    Turnbull, J.E.3
  • 84
    • 78149420274 scopus 로고    scopus 로고
    • Comparable stabilisation, structural changes and activities can be induced in FGF by a variety of HS and non-GAG analogues: Implications for sequence-activity relationships
    • Rudd TR et al. 2010 Comparable stabilisation, structural changes and activities can be induced in FGF by a variety of HS and non-GAG analogues: implications for sequence-activity relationships. Org. Biomol. Chem. 8, 5390-5397. (doi:10.1039/c0ob00246a).
    • (2010) Org. Biomol. Chem. , vol.8 , pp. 5390-5397
    • Rudd, T.R.1
  • 85
    • 84893054542 scopus 로고    scopus 로고
    • Brittlestars contain highly sulfated chondroitin sulfates/dermatan sulfates that promote fibroblast growth factor 2- induced cell signaling
    • Ramachandra R et al. 2014 Brittlestars contain highly sulfated chondroitin sulfates/dermatan sulfates that promote fibroblast growth factor 2- induced cell signaling. Glycobiology 24, 195-207. (doi:10.1093/glycob/cwt100).
    • (2014) Glycobiology , vol.24 , pp. 195-207
    • Ramachandra, R.1
  • 86
    • 84869204033 scopus 로고    scopus 로고
    • Diversification of the structural determinants of fibroblast growth factor-heparin interactions: Implications for binding specificity
    • Xu R et al. 2012 Diversification of the structural determinants of fibroblast growth factor-heparin interactions: implications for binding specificity. J. Biol. Chem. 287, 40061-40073. (doi:10.1074/jbc.M112.398826).
    • (2012) J. Biol. Chem. , vol.287 , pp. 40061-40073
    • Xu, R.1
  • 87
    • 0033954312 scopus 로고    scopus 로고
    • Differential ability of heparan sulfate proteoglycans to assemble the fibroblast growth factor receptor complex in situ
    • Chang Z, Meyer K, Rapraeger AC, Friedl A. 2000 Differential ability of heparan sulfate proteoglycans to assemble the fibroblast growth factor receptor complex in situ. FASEB J. 14, 137-144.
    • (2000) FASEB J. , vol.14 , pp. 137-144
    • Chang, Z.1    Meyer, K.2    Rapraeger, A.C.3    Friedl, A.4
  • 88
    • 0242677706 scopus 로고    scopus 로고
    • Spatial and temporal expression of heparan sulfate in mouse development regulates FGF and FGF receptor assembly
    • Allen BL, Rapraeger AC. 2003 Spatial and temporal expression of heparan sulfate in mouse development regulates FGF and FGF receptor assembly. J. Cell. Biol. 163, 637-648. (doi:10.1083/jcb.200307053).
    • (2003) J. Cell. Biol , vol.163 , pp. 637-648
    • Allen, B.L.1    Rapraeger, A.C.2
  • 89
    • 64549158874 scopus 로고    scopus 로고
    • FGF-regulated Etv genes are essential for repressing Shh expression in mouse limb buds
    • Zhang Z, Verheyden JM, Hassell JA, Sun X. 2009 FGF-regulated Etv genes are essential for repressing Shh expression in mouse limb buds. Dev. Cell 16, 607-613. (doi:10.1016/j.devcel.2009.02.008).
    • (2009) Dev. Cell , vol.16 , pp. 607-613
    • Zhang, Z.1    Verheyden, J.M.2    Hassell, J.A.3    Sun, X.4
  • 90
    • 77956260099 scopus 로고    scopus 로고
    • Heparan sulfate domain organization and sulfation modulate FGF-induced cell signaling
    • Jastrebova N, Vanwildemeersch M, Lindahl U, Spillmann D. 2010 Heparan sulfate domain organization and sulfation modulate FGF-induced cell signaling. J. Biol. Chem. 285, 26842-26851. (doi:10.1074/jbc.M109.093542).
    • (2010) J. Biol. Chem , vol.285 , pp. 26842-26851
    • Jastrebova, N.1    Vanwildemeersch, M.2    Lindahl, U.3    Spillmann, D.4
  • 91
    • 0346100658 scopus 로고    scopus 로고
    • Highly diverse heparan sulfate analogue libraries: Providing access to expanded areas of sequence space for bioactivity screening
    • Yates EA, Guimond SE, Turnbull JE. 2004 Highly diverse heparan sulfate analogue libraries: providing access to expanded areas of sequence space for bioactivity screening. J. Med. Chem. 47, 277-280. (doi:10.1021/jm0309755).
    • (2004) J. Med. Chem. , vol.47 , pp. 277-280
    • Yates, E.A.1    Guimond, S.E.2    Turnbull, J.E.3
  • 92
    • 0037169480 scopus 로고    scopus 로고
    • Differential effects of heparin saccharides on the formation of specific fibroblast growth factor (FGF) and FGF receptor complexes
    • Ostrovsky O, Berman B, Gallagher J, Mulloy B, Fernig DG, Delehedde M, Ron D. 2002 Differential effects of heparin saccharides on the formation of specific fibroblast growth factor (FGF) and FGF receptor complexes. J. Biol. Chem. 277, 2444-2453. (doi:10.1074/jbc.M108540200).
    • (2002) J. Biol. Chem , vol.277 , pp. 2444-2453
    • Ostrovsky, O.1    Berman, B.2    Gallagher, J.3    Mulloy, B.4    Fernig, D.G.5    Delehedde, M.6    Ron, D.7
  • 93
    • 0346102457 scopus 로고    scopus 로고
    • VEGF is a chemoattractant for FGF-2-stimulated neural progenitors
    • Zhang H, Vutskits L, Pepper MS, Kiss JZ. 2003 VEGF is a chemoattractant for FGF-2-stimulated neural progenitors. J. Cell Biol. 163, 1375-1384. (doi:10.1083/jcb.200308040).
    • (2003) J. Cell Biol. , vol.163 , pp. 1375-1384
    • Zhang, H.1    Vutskits, L.2    Pepper, M.S.3    Kiss, J.Z.4
  • 94
    • 33748749862 scopus 로고    scopus 로고
    • N-glycosylation of fibroblast growth factor receptor 1 regulates ligand and heparan sulfate coreceptor binding
    • Duchesne L, Tissot B, Rudd TR, Dell A, Fernig DG. 2006 N-glycosylation of fibroblast growth factor receptor 1 regulates ligand and heparan sulfate coreceptor binding. J. Biol. Chem. 281, 27178- 27189. (doi:10.1074/jbc.M601248200).
    • (2006) J. Biol. Chem. , vol.281 , pp. 27178-27189
    • Duchesne, L.1    Tissot, B.2    Rudd, T.R.3    Dell, A.4    Fernig, D.G.5
  • 95
    • 0029866647 scopus 로고    scopus 로고
    • Heparin structure and interactions with basic fibroblast growth factor
    • Faham S, Hileman RE, Fromm JR, Linhardt RJ, Rees DC. 1996 Heparin structure and interactions with basic fibroblast growth factor. Science 271, 1116-1120. (doi:10.1126/science.271.5252.1116).
    • (1996) Science , vol.271 , pp. 1116-1120
    • Faham, S.1    Hileman, R.E.2    Fromm, J.R.3    Linhardt, R.J.4    Rees, D.C.5
  • 96
    • 0034718796 scopus 로고    scopus 로고
    • Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin
    • Pellegrini L, Burke DF, von Delft F, Mulloy B, Blundell TL. 2000 Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin. Nature 407, 1029-1034. (doi:10.1038/35039551).
    • (2000) Nature , vol.407 , pp. 1029-1034
    • Pellegrini, L.1    Burke, D.F.2    Von Delft, F.3    Mulloy, B.4    Blundell, T.L.5
  • 97
    • 0033635299 scopus 로고    scopus 로고
    • Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization
    • Schlessinger J et al. 2000 Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization. Mol. Cell 6, 743-750. (doi:10.1016/S1097-2765(00)00073-3).
    • (2000) Mol. Cell , vol.6 , pp. 743-750
    • Schlessinger, J.1
  • 98
    • 0027428744 scopus 로고
    • Activating and inhibitory heparin sequences for FGF-2 (basic FGF). Distinct requirements for FGF-1, FGF-2, and FGF-4
    • Guimond S, Maccarana M, Olwin BB, Lindahl U, Rapraeger AC. 1993 Activating and inhibitory heparin sequences for FGF-2 (basic FGF). Distinct requirements for FGF-1, FGF-2, and FGF-4. J. Biol. Chem. 268, 23906-23914.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23906-23914
    • Guimond, S.1    Maccarana, M.2    Olwin, B.B.3    Lindahl, U.4    Rapraeger, A.C.5
  • 99
    • 79957607304 scopus 로고    scopus 로고
    • Highly sulfated nonreducing endderived heparan sulfate domains bind fibroblast growth factor-2 with high affinity and are enriched in biologically active fractions
    • Naimy H, Buczek-Thomas JA, Nugent MA, Leymarie N, Zaia J. 2011 Highly sulfated nonreducing endderived heparan sulfate domains bind fibroblast growth factor-2 with high affinity and are enriched in biologically active fractions. J. Biol. Chem. 286, 19311-19319. (doi:10.1074/jbc.M110.204693).
    • (2011) J. Biol. Chem , vol.286 , pp. 19311-19319
    • Naimy, H.1    Buczek-Thomas, J.A.2    Nugent, M.A.3    Leymarie, N.4    Zaia, J.5
  • 100
    • 84911018648 scopus 로고    scopus 로고
    • Importance of the polarity of the glycosaminoglycan chain on the interaction with FGF-1
    • Munoz-Garcia JC et al. 2014 Importance of the polarity of the glycosaminoglycan chain on the interaction with FGF-1. Glycobiology 24, 1004-1009. (doi:10.1093/glycob/cwu071).
    • (2014) Glycobiology , vol.24 , pp. 1004-1009
    • Munoz-Garcia, J.C.1
  • 101
    • 84910051456 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of heparan sulfate and heparin
    • Liu J, Linhardt RJ. 2014 Chemoenzymatic synthesis of heparan sulfate and heparin. Nat. Prod. Rep. 31, 1676-1685. (doi:10.1039/C4NP00076E).
    • (2014) Nat. Prod. Rep. , vol.31 , pp. 1676-1685
    • Liu, J.1    Linhardt, R.J.2
  • 102
    • 84865235998 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of heparin oligosaccharides with both anti-factor Xa and anti-factor IIa activities
    • Xu Y, Pempe EH, Liu J. 2012 Chemoenzymatic synthesis of heparin oligosaccharides with both anti-factor Xa and anti-factor IIa activities. J. Biol. Chem. 287, 29054-29061. (doi:10.1074/jbc.M112.358523).
    • (2012) J. Biol. Chem. , vol.287 , pp. 29054-29061
    • Xu, Y.1    Pempe, E.H.2    Liu, J.3
  • 103
    • 84871582167 scopus 로고    scopus 로고
    • Divergent synthesis of 48 heparan sulfate-based disaccharides and probing the specific sugar-fibroblast growth factor-1 interaction
    • Hu YP et al. 2012 Divergent synthesis of 48 heparan sulfate-based disaccharides and probing the specific sugar-fibroblast growth factor-1 interaction. J. Am. Chem. Soc. 134, 20722-20727. (doi:10.1021/ja3090065).
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 20722-20727
    • Hu, Y.P.1
  • 104
    • 0033976204 scopus 로고    scopus 로고
    • A novel heparan sulphate with high degree of N-sulphation and high heparin cofactor-II activity from the brine shrimp Artemia franciscana
    • Chavante SF, Santos EA, Oliveira FW, Guerrini M, Torri G, Casu B, Dietrich CP, Nader HB. 2000 A novel heparan sulphate with high degree of N-sulphation and high heparin cofactor-II activity from the brine shrimp Artemia franciscana. Int. J. Biol. Macromol. 27, 49-57. (doi:10.1016/S0141-8130(99)00114-2).
    • (2000) Int. J. Biol. Macromol , vol.27 , pp. 49-57
    • Chavante, S.F.1    Santos, E.A.2    Oliveira, F.W.3    Guerrini, M.4    Torri, G.5    Casu, B.6    Dietrich, C.P.7    Nader, H.B.8
  • 105
    • 0031027986 scopus 로고    scopus 로고
    • Effect of nonspecific binding to plasma proteins on the antithrombin activities of unfractionated heparin, low-molecular-weight heparin, and dermatan sulfate
    • Cosmi B, Fredenburgh JC, Rischke J, Hirsh J, Young E, Weitz JI. 1997 Effect of nonspecific binding to plasma proteins on the antithrombin activities of unfractionated heparin, low-molecular-weight heparin, and dermatan sulfate. Circulation 95, 118-124. (doi:10.1161/01.CIR.95.1.118).
    • (1997) Circulation , vol.95 , pp. 118-124
    • Cosmi, B.1    Fredenburgh, J.C.2    Rischke, J.3    Hirsh, J.4    Young, E.5    Weitz, J.I.6
  • 106
    • 0032782009 scopus 로고    scopus 로고
    • Structural features and anticoagulant activities of a novel natural low molecular weight heparin from the shrimp Penaeus brasiliensis
    • Dietrich CP et al. 1999 Structural features and anticoagulant activities of a novel natural low molecular weight heparin from the shrimp Penaeus brasiliensis. Biochim. Biophys. Acta 1428, 273-283. (doi:10.1016/S0304-4165(99)00087-2).
    • (1999) Biochim. Biophys. Acta , vol.1428 , pp. 273-283
    • Dietrich, C.P.1
  • 107
    • 0033581924 scopus 로고    scopus 로고
    • Fibroblast growth factor receptor signalling is dictated by specific heparan sulphate saccharides
    • Guimond SE, Turnbull JE. 1999 Fibroblast growth factor receptor signalling is dictated by specific heparan sulphate saccharides. Curr. Biol. 9, 1343-1346. (doi:10.1016/S0960-9822(00)80060-3).
    • (1999) Curr. Biol. , vol.9 , pp. 1343-1346
    • Guimond, S.E.1    Turnbull, J.E.2
  • 108
    • 0033658646 scopus 로고    scopus 로고
    • Regulation of FGF-1 mitogenic activity by heparan sulfate oligosaccharides is dependent on specific structural features: Differential requirements for the modulation of FGF-1 and FGF-2
    • Pye DA, Vives RR, Hyde P, Gallagher JT. 2000 Regulation of FGF-1 mitogenic activity by heparan sulfate oligosaccharides is dependent on specific structural features: differential requirements for the modulation of FGF-1 and FGF-2. Glycobiology 10, 1183-1192. (doi:10.1093/glycob/10.11.1183).
    • (2000) Glycobiology , vol.10 , pp. 1183-1192
    • Pye, D.A.1    Vives, R.R.2    Hyde, P.3    Gallagher, J.T.4
  • 109
    • 0028039867 scopus 로고
    • Specific heparan sulfate saccharides mediate the activity of basic fibroblast growth factor
    • Walker A, Turnbull JE, Gallagher JT. 1994 Specific heparan sulfate saccharides mediate the activity of basic fibroblast growth factor. J. Biol. Chem. 269, 931-935.
    • (1994) J. Biol. Chem , vol.269 , pp. 931-935
    • Walker, A.1    Turnbull, J.E.2    Gallagher, J.T.3
  • 111
    • 34047121229 scopus 로고    scopus 로고
    • The heparanome - The enigma of encoding and decoding heparan sulfate sulfation
    • Lamanna WC, Kalus I, Padva M, Baldwin RJ, Merry CL, Dierks T. 2007 The heparanome-the enigma of encoding and decoding heparan sulfate sulfation. J. Biotechnol. 129, 290-307. (doi:10.1016/j.jbiotec.2007.01.022).
    • (2007) J. Biotechnol , vol.129 , pp. 290-307
    • Lamanna, W.C.1    Kalus, I.2    Padva, M.3    Baldwin, R.J.4    Merry, C.L.5    Dierks, T.6
  • 112
    • 0034666108 scopus 로고    scopus 로고
    • STRING: A web-server to retrieve and display the repeatedly occurring neighbourhood of a gene
    • Snel B, Lehmann G, Bork P, Huynen MA. 2000 STRING: A web-server to retrieve and display the repeatedly occurring neighbourhood of a gene Nucleic Acids Res. 28, 3442-3444. (doi:10.1093/nar/28.18.3442).
    • (2000) Nucleic Acids Res , vol.28 , pp. 3442-3444
    • Snel, B.1    Lehmann, G.2    Bork, P.3    Huynen, M.A.4
  • 113
    • 0021207035 scopus 로고
    • An inverse relationship between heparin content and antibody response in genetically selected mice. Sex effect and evidence of a polygenic control for skin heparin concentration
    • Straus AH, Sant'anna OA, Nader HB, Dietrich CP. 1984 An inverse relationship between heparin content and antibody response in genetically selected mice. Sex effect and evidence of a polygenic control for skin heparin concentration. Biochem. J. 220, 625-630.
    • (1984) Biochem. J. , vol.220 , pp. 625-630
    • Straus, A.H.1    Sant'anna, O.A.2    Nader, H.B.3    Dietrich, C.P.4
  • 114
    • 31044438562 scopus 로고    scopus 로고
    • The specificity of interactions between proteins and sulfated polysaccharides
    • Mulloy B. 2005 The specificity of interactions between proteins and sulfated polysaccharides. Anais da Academia Brasileira de Ciencias 77, 651- 664. (doi:10.1590/S0001-37652005000400007).
    • (2005) Anais da Academia Brasileira de Ciencias , vol.77 , pp. 651-664
    • Mulloy, B.1
  • 115
    • 77952374032 scopus 로고    scopus 로고
    • Conformational degeneracy restricts the effective information content of heparan sulfate
    • Rudd TR, Yates EA. 2010 Conformational degeneracy restricts the effective information content of heparan sulfate. Mol. Biosyst. 6, 902-908. (doi:10.1039/b923519a).
    • (2010) Mol. Biosyst. , vol.6 , pp. 902-908
    • Rudd, T.R.1    Yates, E.A.2
  • 116
    • 24644505197 scopus 로고    scopus 로고
    • Identification of common and specific growth factor binding sites in heparan sulfate proteoglycans
    • Chu CL, Goerges AL, Nugent MA. 2005 Identification of common and specific growth factor binding sites in heparan sulfate proteoglycans. Biochemistry 44, 12203-12213. (doi:10.1021/bi050241p).
    • (2005) Biochemistry , vol.44 , pp. 12203-12213
    • Chu, C.L.1    Goerges, A.L.2    Nugent, M.A.3
  • 118
    • 15844368097 scopus 로고    scopus 로고
    • Receptor specificity of the fibroblast growth factor family
    • Ornitz DM et al. 1996 Receptor specificity of the fibroblast growth factor family. J. Biol. Chem. 271, 15292-15297. (doi:10.1074/jbc.271.25.15292).
    • (1996) J. Biol. Chem , vol.271 , pp. 15292-15297
    • Ornitz, D.M.1
  • 119
    • 84877696797 scopus 로고    scopus 로고
    • Analysis of the fibroblast growth factor receptor (FGFR) signalling network with heparin as coreceptor: Evidence for the expansion of the core FGFR signalling network
    • Xu R, Rudd TR, Hughes AJ, Siligardi G, Fernig DG, Yates EA. 2013 Analysis of the fibroblast growth factor receptor (FGFR) signalling network with heparin as coreceptor: evidence for the expansion of the core FGFR signalling network. FEBS J. 280, 2260-2270. (doi:10.1111/febs.12201).
    • (2013) FEBS J , vol.280 , pp. 2260-2270
    • Xu, R.1    Rudd, T.R.2    Hughes, A.J.3    Siligardi, G.4    Fernig, D.G.5    Yates, E.A.6
  • 120
    • 84901448041 scopus 로고    scopus 로고
    • Heparin-protein interactions: From affinity and kinetics to biological roles. Application to an interaction network regulating angiogenesis
    • Peysselon F, Ricard-Blum S. 2014 Heparin-protein interactions: from affinity and kinetics to biological roles. Application to an interaction network regulating angiogenesis. Matrix Biol. 35, 73-81. (doi:10.1016/j.matbio.2013.11.001).
    • (2014) Matrix Biol , vol.35 , pp. 73-81
    • Peysselon, F.1    Ricard-Blum, S.2
  • 121
    • 84928608339 scopus 로고    scopus 로고
    • Heparin/heparan sulfate proteoglycans glycomic interactome in angiogenesis: Biological implications and therapeutical use
    • Chiodelli P, Bugatti A, Urbinati C, Rusnati M. 2015 Heparin/heparan sulfate proteoglycans glycomic interactome in angiogenesis: biological implications and therapeutical use. Molecules 20, 6342-6388. (doi:10.3390/molecules20046342).
    • (2015) Molecules , vol.20 , pp. 6342-6388
    • Chiodelli, P.1    Bugatti, A.2    Urbinati, C.3    Rusnati, M.4
  • 122
    • 84878661746 scopus 로고    scopus 로고
    • Perturbation of the heparin/heparinsulfate interactome of human breast cancer cells modulates pro-tumourigenic effects associated with PI3 K/Akt and MAPK/ERK signalling
    • Chen Y, Scully M, Dawson G, Goodwin C, Xia M, Lu X, Kakkar A. 2013 Perturbation of the heparin/heparinsulfate interactome of human breast cancer cells modulates pro-tumourigenic effects associated with PI3 K/Akt and MAPK/ERK signalling. Thromb. Haemost. 109, 1148-1157. (doi:10.1160/TH12-12-0935).
    • (2013) Thromb. Haemost , vol.109 , pp. 1148-1157
    • Chen, Y.1    Scully, M.2    Dawson, G.3    Goodwin, C.4    Xia, M.5    Lu, X.6    Kakkar, A.7
  • 123
    • 77956408223 scopus 로고    scopus 로고
    • Glycosaminoglycans as polyelectrolytes
    • Seyrek E, Dubin P. 2010 Glycosaminoglycans as polyelectrolytes. Adv. Colloid Interface Sci. 158, 119-129. (doi:10.1016/j.cis.2010.03.001).
    • (2010) Adv. Colloid Interface Sci , vol.158 , pp. 119-129
    • Seyrek, E.1    Dubin, P.2
  • 124
    • 21244497694 scopus 로고    scopus 로고
    • Characterization of polyanion-protein complexes by frontal analysis continuous capillary electrophoresis and small angle neutron scattering: Effect of polyanion flexibility
    • Hattori T, Bat-Aldar S, Kato R, Bohidar HB, Dubin PL. 2005 Characterization of polyanion-protein complexes by frontal analysis continuous capillary electrophoresis and small angle neutron scattering: effect of polyanion flexibility. Anal. Biochem. 342, 229-236. (doi:10.1016/j.ab.2005.03.043).
    • (2005) Anal. Biochem , vol.342 , pp. 229-236
    • Hattori, T.1    Bat-Aldar, S.2    Kato, R.3    Bohidar, H.B.4    Dubin, P.L.5
  • 125
    • 34250351975 scopus 로고    scopus 로고
    • Nonspecific electrostatic binding characteristics of the heparin-antithrombin interaction
    • Seyrek E, Dubin PL, Henriksen J. 2007 Nonspecific electrostatic binding characteristics of the heparin-antithrombin interaction. Biopolymers 86, 249-259. (doi:10.1002/bip.20731).
    • (2007) Biopolymers , vol.86 , pp. 249-259
    • Seyrek, E.1    Dubin, P.L.2    Henriksen, J.3
  • 126
    • 0038071858 scopus 로고    scopus 로고
    • Ionic strength dependence of protein-polyelectrolyte interactions
    • Seyrek E, Dubin PL, Tribet C, Gamble EA. 2003 Ionic strength dependence of protein-polyelectrolyte interactions. Biomacromolecules 4, 273-282. (doi:10.1021/bm025664a).
    • (2003) Biomacromolecules , vol.4 , pp. 273-282
    • Seyrek, E.1    Dubin, P.L.2    Tribet, C.3    Gamble, E.A.4
  • 127
    • 0033557331 scopus 로고    scopus 로고
    • The salt dependence of DNA recognition by NF-kB p50: A detailed kinetic analysis of the effects on affinity and specificity
    • Hart DJ, Speight RE, Cooper MA, Sutherland JD, Blackburn JM. 1999 The salt dependence of DNA recognition by NF-kB p50: A detailed kinetic analysis of the effects on affinity and specificity. Nucleic Acids Res. 27, 1063-1069. (doi:10.1093/nar/27.4.1063).
    • (1999) Nucleic Acids Res , vol.27 , pp. 1063-1069
    • Hart, D.J.1    Speight, R.E.2    Cooper, M.A.3    Sutherland, J.D.4    Blackburn, J.M.5
  • 128
    • 0032530648 scopus 로고    scopus 로고
    • Mechanism of heparin activation of antithrombin: Evidence for an induced-fit model of allosteric activation involving two interaction subsites
    • Desai UR, Petitou M, Bjork I, Olson ST. 1998 Mechanism of heparin activation of antithrombin: evidence for an induced-fit model of allosteric activation involving two interaction subsites. Biochemistry 37, 13033-13041. (doi:10.1021/bi981426h).
    • (1998) Biochemistry , vol.37 , pp. 13033-13041
    • Desai, U.R.1    Petitou, M.2    Bjork, I.3    Olson, S.T.4
  • 129
    • 0028218987 scopus 로고
    • Energetic characterization of the basic fibroblast growth factor-heparin interaction: Identification of the heparin binding domain
    • Thompson LD, Pantoliano MW, Springer BA. 1994 Energetic characterization of the basic fibroblast growth factor-heparin interaction: identification of the heparin binding domain. Biochemistry 33, 3831-3840. (doi:10.1021/bi00179a006).
    • (1994) Biochemistry , vol.33 , pp. 3831-3840
    • Thompson, L.D.1    Pantoliano, M.W.2    Springer, B.A.3
  • 130
    • 84876558368 scopus 로고    scopus 로고
    • Evaluate of heavy metal concentration in shrimp (Penaeus semisulcatus) and crab (Portunus pelagicus) with INAA method
    • Heidarieh M, Maragheh MG, Shamami MA, Behgar M, Ziaei F, Akbari Z. 2013 Evaluate of heavy metal concentration in shrimp (Penaeus semisulcatus) and crab (Portunus pelagicus) with INAA method. SpringerPlus 2, 72. (doi:10.1186/2193-1801-2-72).
    • (2013) SpringerPlus , vol.2 , pp. 72
    • Heidarieh, M.1    Maragheh, M.G.2    Shamami, M.A.3    Behgar, M.4    Ziaei, F.5    Akbari, Z.6
  • 132
    • 84929659263 scopus 로고    scopus 로고
    • HS3ST2 expression is critical for the abnormal phosphorylation of tau in Alzheimer's disease-related tau pathology
    • Sepulveda-Diaz JE et al. 2015 HS3ST2 expression is critical for the abnormal phosphorylation of tau in Alzheimer's disease-related tau pathology. Brain 138, 1339-1354. (doi:10.1093/brain/awv056).
    • (2015) Brain , vol.138 , pp. 1339-1354
    • Sepulveda-Diaz, J.E.1
  • 133
    • 0018866050 scopus 로고
    • Effect of monovalent cations on the heparinenhanced antithrombin III/thrombin reaction
    • Griffith MJ, Beavers G, Kingdon HS, Lundblad RL. 1980 Effect of monovalent cations on the heparinenhanced antithrombin III/thrombin reaction. Thromb. Res. 17, 29-39. (doi:10.1016/0049-3848(80)90291-1).
    • (1980) Thromb. Res. , vol.17 , pp. 29-39
    • Griffith, M.J.1    Beavers, G.2    Kingdon, H.S.3    Lundblad, R.L.4
  • 134
    • 0021437239 scopus 로고
    • Angiogenesis in vivo and selective mobilization of capillary endothelium in vitro by heparin-copper complex
    • Alessandri G, Raju K, Gullino PM. 1984 Angiogenesis in vivo and selective mobilization of capillary endothelium in vitro by heparin-copper complex. Microcirc. Endothel. Lymphatics 1, 329-346.
    • (1984) Microcirc. Endothel. Lymphatics , vol.1 , pp. 329-346
    • Alessandri, G.1    Raju, K.2    Gullino, P.M.3
  • 135
    • 33847775171 scopus 로고    scopus 로고
    • X-ray fluorescence microscopy reveals large-scale relocalization and extracellular translocation of cellular copper during angiogenesis
    • Finney L et al. 2007 X-ray fluorescence microscopy reveals large-scale relocalization and extracellular translocation of cellular copper during angiogenesis. Proc. Natl Acad. Sci. USA 104, 2247-2252. (doi:10.1073/pnas.0607238104).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 2247-2252
    • Finney, L.1
  • 136
    • 0028803674 scopus 로고
    • Multinuclear magnetic resonance studies of the interaction of inorganic cations with heparin
    • Rabenstein DL, Robert JM, Peng J. 1995 Multinuclear magnetic resonance studies of the interaction of inorganic cations with heparin. Carbohydr. Res. 278, 239-256. (doi:10.1016/0008-6215(95)00263-4).
    • (1995) Carbohydr. Res , vol.278 , pp. 239-256
    • Rabenstein, D.L.1    Robert, J.M.2    Peng, J.3
  • 137
    • 0026764695 scopus 로고
    • A potentiometric titration study of the interaction of heparin with metal cations
    • Grant D, Long WF, Williamson FB. 1992 A potentiometric titration study of the interaction of heparin with metal cations. Biochem. J. 285, 477-480.
    • (1992) Biochem. J. , vol.285 , pp. 477-480
    • Grant, D.1    Long, W.F.2    Williamson, F.B.3
  • 138
    • 0017895903 scopus 로고
    • The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides
    • Manning GS. 1978 The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides. Q. Rev. Biophys. 11, 179-246. (doi:10.1017/S0033583500002031).
    • (1978) Q. Rev. Biophys , vol.11 , pp. 179-246
    • Manning, G.S.1
  • 139
    • 0346693450 scopus 로고
    • Sodiumion diffusion in aqueous salt-free heparin solutions
    • Ander P, Lubas W. 1981 Sodium ion diffusionin aqueous salt-free heparin solutions. Macromolecules 14, 1058-1061. (doi:10.1021/ma50005a032).
    • (1981) Macromolecules , vol.14 , pp. 1058-1061
    • Ander, P.1    Lubas, W.2
  • 140
    • 0020535535 scopus 로고
    • Effect of ionic strength on the diffusion coefficient of chondroitin sulfate and heparin measured by quasielastic light scattering
    • Tivant P, Turq P, Drifford M, Magdelenat H, Menez R. 1983 Effect of ionic strength on the diffusion coefficient of chondroitin sulfate and heparin measured by quasielastic light scattering. Biopolymers 22, 643-662. (doi:10.1002/bip.360220209).
    • (1983) Biopolymers , vol.22 , pp. 643-662
    • Tivant, P.1    Turq, P.2    Drifford, M.3    Magdelenat, H.4    Menez, R.5
  • 141
    • 0036069514 scopus 로고    scopus 로고
    • The heparin2Ca2 interaction: Structure of the Ca2 binding site
    • Chevalier F, Angulo J, Lucas R, Nieto Pedro M, Martín-Lomas M. 2002 The heparin2Ca2 interaction: structure of the Ca2 binding site. Eur. J. Org. Chem. 2002, 2367-2376. (doi:10.1002/1099-0690(200207)2002:14, 2367::AID-EJOC2367.3.0.CO;2-K).
    • (2002) Eur. J. Org. Chem , vol.2002 , pp. 2367-2376
    • Chevalier, F.1    Angulo, J.2    Lucas, R.3    Nieto, P.M.4    Martín-Lomas, M.5
  • 142
    • 34548810245 scopus 로고    scopus 로고
    • Influence of substitution pattern and cation binding on conformation and activity in heparin derivatives
    • Rudd TR et al. 2007 Influence of substitution pattern and cation binding on conformation and activity in heparin derivatives. Glycobiology 17, 983-993. (doi:10.1093/glycob/cwm062).
    • (2007) Glycobiology , vol.17 , pp. 983-993
    • Rudd, T.R.1
  • 143
    • 84930505508 scopus 로고    scopus 로고
    • Heparan sulfate phage display antibodies recognise epitopes defined by a combination of sugar sequence and cation binding
    • Solari V, Rudd TR, Guimond SE, Powell AK, Turnbull JE, Yates EA. 2015 Heparan sulfate phage display antibodies recognise epitopes defined by a combination of sugar sequence and cation binding. Org. Biomol. Chem. 13, 6066-6072. (doi:10.1039/C5OB00564G).
    • (2015) Org. Biomol. Chem. , vol.13 , pp. 6066-6072
    • Solari, V.1    Rudd, T.R.2    Guimond, S.E.3    Powell, A.K.4    Turnbull, J.E.5    Yates, E.A.6
  • 144
    • 79951523439 scopus 로고    scopus 로고
    • Effect of solvent and counterions upon structure and NMR spin-spin coupling constants in heparin disaccharide
    • Hricovini M. 2011 Effect of solvent and counterions upon structure and NMR spin-spin coupling constants in heparin disaccharide. J. Phys. Chem. B 115, 1503-1511. (doi:10.1021/jp1098552).
    • (2011) J. Phys. Chem. B , vol.115 , pp. 1503-1511
    • Hricovini, M.1
  • 145
    • 0029910071 scopus 로고    scopus 로고
    • Divalent cations and heparin/heparan sulfate cooperate to control assembly and activity of the fibroblast growth factor receptor complex
    • Kan M, Wang F, To B, Gabriel JL, McKeehan WL. 1996 Divalent cations and heparin/heparan sulfate cooperate to control assembly and activity of the fibroblast growth factor receptor complex. J. Biol. Chem. 271, 26143-26148. (doi:10.1074/jbc.271.42.26143).
    • (1996) J. Biol. Chem. , vol.271 , pp. 26143-26148
    • Kan, M.1    Wang, F.2    To, B.3    Gabriel, J.L.4    McKeehan, W.L.5
  • 146
    • 66649105784 scopus 로고    scopus 로고
    • Cations modulate polysaccharide structure to determine FGF-FGFR signaling: A comparison of signaling and inhibitory polysaccharide interactions with FGF-1 in solution
    • Guimond SE et al. 2009 Cations modulate polysaccharide structure to determine FGF-FGFR signaling: A comparison of signaling and inhibitory polysaccharide interactions with FGF-1 in solution. Biochemistry 48, 4772-4779. (doi:10.1021/bi802318z).
    • (2009) Biochemistry , vol.48 , pp. 4772-4779
    • Guimond, S.E.1
  • 147
    • 84889027821 scopus 로고    scopus 로고
    • On the catalytic mechanism of polysaccharide lyases: Evidence of His and Tyr involvement in heparin lysis by heparinase I and the role of Ca2
    • Cordula CR et al. 2014 On the catalytic mechanism of polysaccharide lyases: evidence of His and Tyr involvement in heparin lysis by heparinase I and the role of Ca2. Mol. Biosyst. 10, 54-64. (doi:10.1039/C3MB70370C).
    • (2014) Mol. Biosyst. , vol.10 , pp. 54-64
    • Cordula, C.R.1
  • 148
    • 0035148547 scopus 로고    scopus 로고
    • Annexin V-heparin oligosaccharide complex suggests heparan sulfate-mediated assembly on cell surfaces
    • Capila I, Hernaiz MJ, Mo YD, Mealy TR, Campos B, Dedman JR, Linhardt RJ, Seaton BA. 2001 Annexin V-heparin oligosaccharide complex suggests heparan sulfate-mediated assembly on cell surfaces. Structure 9, 57-64. (doi:10.1016/S0969-2126(00)00549-9).
    • (2001) Structure , vol.9 , pp. 57-64
    • Capila, I.1    Hernaiz, M.J.2    Mo, Y.D.3    Mealy, T.R.4    Campos, B.5    Dedman, J.R.6    Linhardt, R.J.7    Seaton, B.A.8
  • 150
    • 79953201148 scopus 로고    scopus 로고
    • Characterization of annexin A1 glycan binding reveals binding to highly sulfated glycans with preference for highly sulfated heparan sulfate and heparin
    • Horlacher T, Noti C, de-Paz JL, Bindschadler P, Hecht ML, Smith DF, Fukuda MN, Seeberger PH. 2011 Characterization of annexin A1 glycan binding reveals binding to highly sulfated glycans with preference for highly sulfated heparan sulfate and heparin. Biochemistry 50, 2650-2659. (doi:10.1021/bi101121a).
    • (2011) Biochemistry , vol.50 , pp. 2650-2659
    • Horlacher, T.1    Noti, C.2    De-Paz, J.L.3    Bindschadler, P.4    Hecht, M.L.5    Smith, D.F.6    Fukuda, M.N.7    Seeberger, P.H.8
  • 151
    • 0026756361 scopus 로고
    • Ionic modulation of the effects of heparin on plasminogen activation by tissue plasminogen activator: The effects of ionic strength, divalent cations, and chloride
    • Young TN, Edelberg JM, Stack S, Pizzo SV. 1992 Ionic modulation of the effects of heparin on plasminogen activation by tissue plasminogen activator: The effects of ionic strength, divalent cations, and chloride. Arch. Biochem. Biophys. 296, 530-538. (doi:10.1016/0003-9861(92)90607-X).
    • (1992) Arch. Biochem. Biophys , vol.296 , pp. 530-538
    • Young, T.N.1    Edelberg, J.M.2    Stack, S.3    Pizzo, S.V.4
  • 152
    • 0013852463 scopus 로고
    • Structure of hen egg-white lysozyme: A three-dimensional Fourier synthesis at 2A° resolution
    • Blake CCF, Koenig DF, Mair GA, North ACT, Phillips DC, Sarma VR. 1965 Structure of hen egg-white lysozyme: A three-dimensional Fourier synthesis at 2A° resolution. Nature 206, 757-761. (doi:10.1038/206757a0).
    • (1965) Nature , vol.206 , pp. 757-761
    • Blake, C.C.F.1    Koenig, D.F.2    Mair, G.A.3    North, A.C.T.4    Phillips, D.C.5    Sarma, V.R.6
  • 153
    • 84869597372 scopus 로고    scopus 로고
    • Fundamental differences in model cell-surface polysaccharides revealed by complementary optical and spectroscopic techniques
    • Holder GM et al. 2012 Fundamental differences in model cell-surface polysaccharides revealed by complementary optical and spectroscopic techniques. Soft Matter 8, 6521-6527. (doi:10.1039/c2sm25239b).
    • (2012) Soft Matter , vol.8 , pp. 6521-6527
    • Holder, G.M.1
  • 154
    • 45049088288 scopus 로고    scopus 로고
    • Site-specific interactions of copper(II) ions with heparin revealed with complementary (SRCD, NMR, FTIR and EPR) spectroscopic techniques
    • Rudd TR et al. 2008 Site-specific interactions of copper(II) ions with heparin revealed with complementary (SRCD, NMR, FTIR and EPR) spectroscopic techniques. Carbohydr. Res. 343, 2184-2193. (doi:10.1016/j.carres.2007.12.019).
    • (2008) Carbohydr. Res. , vol.343 , pp. 2184-2193
    • Rudd, T.R.1
  • 155
    • 0032483520 scopus 로고    scopus 로고
    • Heparan sulfate oligosaccharides require 6-Osulfation for promotion of basic fibroblast growth factor mitogenic activity
    • Pye DA, Vives RR, Turnbull JE, Hyde P, Gallagher JT. 1998 Heparan sulfate oligosaccharides require 6-Osulfation for promotion of basic fibroblast growth factor mitogenic activity. J. Biol. Chem. 273, 22936-22942. (doi:10.1074/jbc.273.36.22936).
    • (1998) J. Biol. Chem. , vol.273 , pp. 22936-22942
    • Pye, D.A.1    Vives, R.R.2    Turnbull, J.E.3    Hyde, P.4    Gallagher, J.T.5
  • 156
    • 0037163107 scopus 로고    scopus 로고
    • Biosynthetic oligosaccharide libraries for identification of proteinbinding heparan sulfate motifs. Exploring the structural diversity by screening for fibroblast growth factor (FGF)1 and FGF2 binding
    • Jemth P, Kreuger J, Kusche-Gullberg M, Sturiale L, Gimenez-Gallego G, Lindahl U. 2002 Biosynthetic oligosaccharide libraries for identification of proteinbinding heparan sulfate motifs. Exploring the structural diversity by screening for fibroblast growth factor (FGF)1 and FGF2 binding. J. Biol. Chem. 277, 30567-30573.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30567-30573
    • Jemth, P.1    Kreuger, J.2    Kusche-Gullberg, M.3    Sturiale, L.4    Gimenez-Gallego, G.5    Lindahl, U.6
  • 159
    • 2442553816 scopus 로고    scopus 로고
    • Irreversible glucuronyl C5-epimerization in the biosynthesis of heparan sulfate
    • Hagner-McWhirter A, Li JP, Oscarson S, Lindahl U. 2004 Irreversible glucuronyl C5-epimerization in the biosynthesis of heparan sulfate. J. Biol. Chem. 279, 14631-14638. (doi:10.1074/jbc.M313760200).
    • (2004) J. Biol. Chem. , vol.279 , pp. 14631-14638
    • Hagner-McWhirter, A.1    Li, J.P.2    Oscarson, S.3    Lindahl, U.4
  • 160
    • 84864472945 scopus 로고    scopus 로고
    • Transport of fibroblast growth factor 2 in the pericellular matrix is controlled by the spatial distribution of its binding sites in heparan sulfate
    • Duchesne L, Octeau V, Bearon RN, Beckett A, Prior IA, Lounis B, Fernig DG. 2012 Transport of fibroblast growth factor 2 in the pericellular matrix is controlled by the spatial distribution of its binding sites in heparan sulfate. PLoS Biol. 10, e1001361. (doi:10.1371/journal.pbio.1001361).
    • (2012) PLoS Biol , vol.10 , pp. e1001361
    • Duchesne, L.1    Octeau, V.2    Bearon, R.N.3    Beckett, A.4    Prior, I.A.5    Lounis, B.6    Fernig, D.G.7
  • 161
    • 34547948541 scopus 로고    scopus 로고
    • Potentiation of fibroblast growth factor activity by synthetic heparin oligosaccharide glycodendrimers
    • De-Paz JL, Noti C, Bohm F, Werner S, Seeberger PH. 2007 Potentiation of fibroblast growth factor activity by synthetic heparin oligosaccharide glycodendrimers. Chem. Biol. 14, 879-887. (doi:10.1016/j.chembiol.2007.07.007).
    • (2007) Chem. Biol. , vol.14 , pp. 879-887
    • De-Paz, J.L.1    Noti, C.2    Bohm, F.3    Werner, S.4    Seeberger, P.H.5
  • 162
    • 0020618471 scopus 로고
    • Calcium inhibits the heparin-catalyzed antithrombin III/thrombin reaction by decreasing the apparent binding affinity of heparin for thrombin
    • Speight MO, Griffith MJ. 1983 Calcium inhibits the heparin-catalyzed antithrombin III/thrombin reaction by decreasing the apparent binding affinity of heparin for thrombin. Arch. Biochem. Biophys. 225, 958-963. (doi:10.1016/0003-9861(83)90111-X).
    • (1983) Arch. Biochem. Biophys. , vol.225 , pp. 958-963
    • Speight, M.O.1    Griffith, M.J.2


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