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Volumn 20, Issue 4, 2015, Pages 6342-6388

Heparin/heparan sulfate proteoglycans glycomic interactome in angiogenesis: Biological implications and therapeutical use

Author keywords

Angiogenesis; Glycomic; Heparan sulfate proteoglycan; Heparin; Interactome

Indexed keywords

ANGIOGENESIS MODULATOR; HEPARIN; PROTEIN BINDING; PROTEOHEPARAN SULFATE;

EID: 84928608339     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules20046342     Document Type: Review
Times cited : (124)

References (326)
  • 2
    • 0030576517 scopus 로고    scopus 로고
    • Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis
    • Hanahan, D.; Folkman, J. Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis. Cell 1996, 86, 353-364.
    • (1996) Cell , vol.86 , pp. 353-364
    • Hanahan, D.1    Folkman, J.2
  • 3
    • 0028929803 scopus 로고
    • Angiogenesis in cancer, vascular, rheumatoid and other disease
    • Folkman, J. Angiogenesis in cancer, vascular, rheumatoid and other disease. Nat. Med. 1995, 1, 27-31.
    • (1995) Nat. Med. , vol.1 , pp. 27-31
    • Folkman, J.1
  • 4
    • 84899471324 scopus 로고    scopus 로고
    • Integrin function in vascular biology: A view from 2013
    • Plow, E.F.; Meller, J.; Byzova, T.V. Integrin function in vascular biology: A view from 2013. Curr. Opin. Hematol. 2014, 21, 241-247.
    • (2014) Curr. Opin. Hematol. , vol.21 , pp. 241-247
    • Plow, E.F.1    Meller, J.2    Byzova, T.V.3
  • 5
    • 84859854623 scopus 로고    scopus 로고
    • Vascular endothelial-cadherin and vascular stability
    • Dejana, E.; Giampietro, C. Vascular endothelial-cadherin and vascular stability. Curr. Opin. Hematol. 2012, 19, 218-223.
    • (2012) Curr. Opin. Hematol. , vol.19 , pp. 218-223
    • Dejana, E.1    Giampietro, C.2
  • 6
    • 33746802333 scopus 로고    scopus 로고
    • Extracellular angiogenic growth factor interactions: An angiogenesis interactome survey
    • Rusnati, M.; Presta, M. Extracellular angiogenic growth factor interactions: An angiogenesis interactome survey. Endothelium 2006, 13, 93-111.
    • (2006) Endothelium , vol.13 , pp. 93-111
    • Rusnati, M.1    Presta, M.2
  • 7
    • 84896975948 scopus 로고    scopus 로고
    • Role of upa/upar in the modulation of angiogenesis
    • Montuori, N.; Ragno, P. Role of upa/upar in the modulation of angiogenesis. Chem. Immunol. Allergy 2014, 99, 105-122.
    • (2014) Chem. Immunol. Allergy , vol.99 , pp. 105-122
    • Montuori, N.1    Ragno, P.2
  • 8
    • 1042289788 scopus 로고    scopus 로고
    • Fibroblast growth factor-2-mediated capillary morphogenesis of endothelial cells requires signals via flt-1/vascular endothelial growth factor receptor-1: Possible involvement of c-akt
    • Kanda, S.; Miyata, Y.; Kanetake, H. Fibroblast growth factor-2-mediated capillary morphogenesis of endothelial cells requires signals via flt-1/vascular endothelial growth factor receptor-1: Possible involvement of c-akt. J. Biol. Chem. 2004, 279, 4007-4016.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4007-4016
    • Kanda, S.1    Miyata, Y.2    Kanetake, H.3
  • 9
    • 78651403569 scopus 로고    scopus 로고
    • Vascular endothelial growth factor a (vegf-a) induces endothelial and cancer cell migration through direct binding to integrin α9β1: Identification of a specific α9β1 binding site
    • Oommen, S.; Gupta, S.K.; Vlahakis, N.E. Vascular endothelial growth factor a (vegf-a) induces endothelial and cancer cell migration through direct binding to integrin α9β1: Identification of a specific α9β1 binding site. J. Biol. Chem. 2011, 286, 1083-1092.
    • (2011) J. Biol. Chem. , vol.286 , pp. 1083-1092
    • Oommen, S.1    Gupta, S.K.2    Vlahakis, N.E.3
  • 10
    • 0034282885 scopus 로고    scopus 로고
    • The interaction of neuropilin-1 with vascular endothelial growth factor and its receptor flt-1
    • Fuh, G.; Garcia, K.C.; de Vos, A.M. The interaction of neuropilin-1 with vascular endothelial growth factor and its receptor flt-1. J. Biol. Chem. 2000, 275, 26690-26695.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26690-26695
    • Fuh, G.1    Garcia, K.C.2    De Vos, A.M.3
  • 11
    • 79251501315 scopus 로고    scopus 로고
    • Fibroblast growth factors: From molecular evolution to roles in development, metabolism and disease
    • Itoh, N.; Ornitz, D.M. Fibroblast growth factors: From molecular evolution to roles in development, metabolism and disease. J. Biochem. 2011, 149, 121-130.
    • (2011) J. Biochem. , vol.149 , pp. 121-130
    • Itoh, N.1    Ornitz, D.M.2
  • 12
    • 84906673934 scopus 로고    scopus 로고
    • Isoforms of receptors of fibroblast growth factors
    • Gong, S.G. Isoforms of receptors of fibroblast growth factors. J. Cell. Physiol. 2014, 229, 1887-1895.
    • (2014) J. Cell. Physiol. , vol.229 , pp. 1887-1895
    • Gong, S.G.1
  • 14
    • 0030608611 scopus 로고    scopus 로고
    • Alphavbeta3 integrin mediates the cell-adhesive capacity and biological activity of basic fibroblast growth factor (fgf-2) in cultured endothelial cells
    • Rusnati, M.; Tanghetti, E.; Dell'Era, P.; Gualandris, A.; Presta, M. Alphavbeta3 integrin mediates the cell-adhesive capacity and biological activity of basic fibroblast growth factor (fgf-2) in cultured endothelial cells. Mol. Biol. Cell 1997, 8, 2449-2461.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2449-2461
    • Rusnati, M.1    Tanghetti, E.2    Dell'Era, P.3    Gualandris, A.4    Presta, M.5
  • 17
    • 70350196360 scopus 로고    scopus 로고
    • Histidine-rich glycoprotein inhibited high mobility group box 1 in complex with heparin-induced angiogenesis in matrigel plug assay
    • Wake, H.; Mori, S.; Liu, K.; Takahashi, H.K.; Nishibori, M. Histidine-rich glycoprotein inhibited high mobility group box 1 in complex with heparin-induced angiogenesis in matrigel plug assay. Eur. J. Pharmacol. 2009, 623, 89-95.
    • (2009) Eur. J. Pharmacol. , vol.623 , pp. 89-95
    • Wake, H.1    Mori, S.2    Liu, K.3    Takahashi, H.K.4    Nishibori, M.5
  • 18
    • 36248971218 scopus 로고    scopus 로고
    • Angiogenic response of endothelial cells to heparin-binding domain of fibronectin
    • Viji, R.I.; Kumar, V.B.; Kiran, M.S.; Sudhakaran, P.R. Angiogenic response of endothelial cells to heparin-binding domain of fibronectin. Int. J. Biochem. Cell Biol. 2008, 40, 215-226.
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 215-226
    • Viji, R.I.1    Kumar, V.B.2    Kiran, M.S.3    Sudhakaran, P.R.4
  • 20
    • 84871687791 scopus 로고    scopus 로고
    • Activated blood coagulation factor x (fxa) induces angiogenic growth factor expression in human retinal pigment epithelial cells
    • Hollborn, M.; Kohen, L.; Werschnik, C.; Tietz, L.; Wiedemann, P.; Bringmann, A. Activated blood coagulation factor x (fxa) induces angiogenic growth factor expression in human retinal pigment epithelial cells. Investig. Ophthalmol. Vis. Sci. 2012, 53, 5930-5939.
    • (2012) Investig. Ophthalmol. Vis. Sci. , vol.53 , pp. 5930-5939
    • Hollborn, M.1    Kohen, L.2    Werschnik, C.3    Tietz, L.4    Wiedemann, P.5    Bringmann, A.6
  • 21
    • 0036556878 scopus 로고    scopus 로고
    • Induction of endothelial cell proliferation by angiogenic factors released by activated monocytes
    • Pakala, R.; Watanabe, T.; Benedict, C.R. Induction of endothelial cell proliferation by angiogenic factors released by activated monocytes. Cardiovasc. Radiat. Med. 2002, 3, 95-101.
    • (2002) Cardiovasc. Radiat. Med. , vol.3 , pp. 95-101
    • Pakala, R.1    Watanabe, T.2    Benedict, C.R.3
  • 22
    • 0030605839 scopus 로고    scopus 로고
    • Synergistic induction of endothelial tissue factor by tumor necrosis factor and vascular endothelial growth factor: Functional analysis of the tumor necrosis factor receptors
    • Clauss, M.; Grell, M.; Fangmann, C.; Fiers, W.; Scheurich, P.; Risau, W. Synergistic induction of endothelial tissue factor by tumor necrosis factor and vascular endothelial growth factor: Functional analysis of the tumor necrosis factor receptors. FEBS Lett. 1996, 390, 334-338.
    • (1996) FEBS Lett. , vol.390 , pp. 334-338
    • Clauss, M.1    Grell, M.2    Fangmann, C.3    Fiers, W.4    Scheurich, P.5    Risau, W.6
  • 23
    • 28544442675 scopus 로고    scopus 로고
    • Interleukin-8 differentially regulates migration of tumor-associated and normal human brain endothelial cells
    • Charalambous, C.; Pen, L.B.; Su, Y.S.; Milan, J.; Chen, T.C.; Hofman, F.M. Interleukin-8 differentially regulates migration of tumor-associated and normal human brain endothelial cells. Cancer Res. 2005, 65, 10347-10354.
    • (2005) Cancer Res. , vol.65 , pp. 10347-10354
    • Charalambous, C.1    Pen, L.B.2    Su, Y.S.3    Milan, J.4    Chen, T.C.5    Hofman, F.M.6
  • 24
    • 13544266205 scopus 로고    scopus 로고
    • Monocyte chemoattractant protein-1-induced angiogenesis is mediated by vascular endothelial growth factor-a
    • Hong, K.H.; Ryu, J.; Han, K.H. Monocyte chemoattractant protein-1-induced angiogenesis is mediated by vascular endothelial growth factor-a. Blood 2005, 105, 1405-1407.
    • (2005) Blood , vol.105 , pp. 1405-1407
    • Hong, K.H.1    Ryu, J.2    Han, K.H.3
  • 25
    • 0031459886 scopus 로고    scopus 로고
    • Basic fibroblast growth factor (bfgf) regulates the expression of the cc chemokine monocyte chemoattractant protein-1 (mcp-1) in autocrine-activated endothelial cells
    • Wempe, F.; Lindner, V.; Augustin, H.G. Basic fibroblast growth factor (bfgf) regulates the expression of the cc chemokine monocyte chemoattractant protein-1 (mcp-1) in autocrine-activated endothelial cells. Arterioscler. Thromb. Vasc. Biol. 1997, 17, 2471-2478.
    • (1997) Arterioscler. Thromb. Vasc. Biol. , vol.17 , pp. 2471-2478
    • Wempe, F.1    Lindner, V.2    Augustin, H.G.3
  • 27
    • 0033880998 scopus 로고    scopus 로고
    • The role of human immunodeficiency virus-i in the pathogenesis of acquired immunodeficiency syndrome-related kaposi's sarcoma: The importance of an inflammatory and angiogenic milieu
    • Dezube, B.J. The role of human immunodeficiency virus-i in the pathogenesis of acquired immunodeficiency syndrome-related kaposi's sarcoma: The importance of an inflammatory and angiogenic milieu. Semin. Oncol. 2000, 27, 420-423.
    • (2000) Semin. Oncol. , vol.27 , pp. 420-423
    • Dezube, B.J.1
  • 29
    • 0034031079 scopus 로고    scopus 로고
    • High-level expression of angiogenic factors is associated with advanced tumor stage in human neuroblastomas
    • Eggert, A.; Ikegaki, N.; Kwiatkowski, J.; Zhao, H.; Brodeur, G.M.; Himelstein, B.P. High-level expression of angiogenic factors is associated with advanced tumor stage in human neuroblastomas. Clin. Cancer Res. 2000, 6, 1900-1908.
    • (2000) Clin. Cancer Res. , vol.6 , pp. 1900-1908
    • Eggert, A.1    Ikegaki, N.2    Kwiatkowski, J.3    Zhao, H.4    Brodeur, G.M.5    Himelstein, B.P.6
  • 32
    • 84902215812 scopus 로고    scopus 로고
    • Demystifying heparan sulfate-protein interactions
    • Xu, D.; Esko, J.D. Demystifying heparan sulfate-protein interactions. Annu. Rev. Biochem. 2014, 83, 129-157.
    • (2014) Annu. Rev. Biochem. , vol.83 , pp. 129-157
    • Xu, D.1    Esko, J.D.2
  • 33
    • 84877919950 scopus 로고    scopus 로고
    • Pathophysiology of heparan sulphate: Many diseases, few drugs
    • Lindahl, U.; Kjellen, L. Pathophysiology of heparan sulphate: Many diseases, few drugs. J. Intern. Med. 2013, 273, 555-571.
    • (2013) J. Intern. Med. , vol.273 , pp. 555-571
    • Lindahl, U.1    Kjellen, L.2
  • 34
    • 0034947648 scopus 로고    scopus 로고
    • Molecular diversity of heparan sulfate
    • Esko, J.D.; Lindahl, U. Molecular diversity of heparan sulfate. J. Clin. Investig. 2001, 108, 169-173.
    • (2001) J. Clin. Investig. , vol.108 , pp. 169-173
    • Esko, J.D.1    Lindahl, U.2
  • 35
    • 0028579734 scopus 로고
    • Perlecan, basal lamina proteoglycan, promotes basic fibroblast growth factor-receptor binding, mitogenesis, and angiogenesis
    • Aviezer, D.; Hecht, D.; Safran, M.; Eisinger, M.; David, G.; Yayon, A. Perlecan, basal lamina proteoglycan, promotes basic fibroblast growth factor-receptor binding, mitogenesis, and angiogenesis. Cell 1994, 79, 1005-1013.
    • (1994) Cell , vol.79 , pp. 1005-1013
    • Aviezer, D.1    Hecht, D.2    Safran, M.3    Eisinger, M.4    David, G.5    Yayon, A.6
  • 36
    • 0026463887 scopus 로고
    • Endothelial cells interact with the core protein of basement membrane perlecan through beta 1 and beta 3 integrins: An adhesion modulated by glycosaminoglycan
    • Hayashi, K.; Madri, J.A.; Yurchenco, P.D. Endothelial cells interact with the core protein of basement membrane perlecan through beta 1 and beta 3 integrins: An adhesion modulated by glycosaminoglycan. J. Cell Biol. 1992, 119, 945-959.
    • (1992) J. Cell Biol. , vol.119 , pp. 945-959
    • Hayashi, K.1    Madri, J.A.2    Yurchenco, P.D.3
  • 37
    • 0029704210 scopus 로고    scopus 로고
    • Interaction of angiogenic basic fibroblast growth factor with endothelial cell heparan sulfate proteoglycans. Biological implications in neovascularization
    • Rusnati, M.; Presta, M. Interaction of angiogenic basic fibroblast growth factor with endothelial cell heparan sulfate proteoglycans. Biological implications in neovascularization. Int. J. Clin. Lab. Res. 1996, 26, 15-23.
    • (1996) Int. J. Clin. Lab. Res. , vol.26 , pp. 15-23
    • Rusnati, M.1    Presta, M.2
  • 38
    • 33846850636 scopus 로고    scopus 로고
    • Anticoagulant heparan sulfate: Structural specificity and biosynthesis
    • Liu, J.; Pedersen, L.C. Anticoagulant heparan sulfate: Structural specificity and biosynthesis. Appl. Microbiol. Biotechnol. 2007, 74, 263-272.
    • (2007) Appl. Microbiol. Biotechnol. , vol.74 , pp. 263-272
    • Liu, J.1    Pedersen, L.C.2
  • 39
    • 0036317550 scopus 로고    scopus 로고
    • The lipase gene family
    • Wong, H.; Schotz, M.C. The lipase gene family. J. Lipid Res. 2002, 43, 993-999.
    • (2002) J. Lipid Res. , vol.43 , pp. 993-999
    • Wong, H.1    Schotz, M.C.2
  • 40
    • 0022004194 scopus 로고
    • Heparinlike molecules with anticoagulant activity are synthesized by cultured endothelial cells
    • Marcum, J.A.; Rosenberg, R.D. Heparinlike molecules with anticoagulant activity are synthesized by cultured endothelial cells. Biochem. Biophys. Res. Commun. 1985, 126, 365-372.
    • (1985) Biochem. Biophys. Res. Commun. , vol.126 , pp. 365-372
    • Marcum, J.A.1    Rosenberg, R.D.2
  • 42
    • 21044433780 scopus 로고    scopus 로고
    • Biotechnological engineering of heparin/heparan sulphate: A novel area of multi-target drug discovery
    • Rusnati, M.; Oreste, P.; Zoppetti, G.; Presta, M. Biotechnological engineering of heparin/heparan sulphate: A novel area of multi-target drug discovery. Curr. Pharm. Des. 2005, 11, 2489-2499.
    • (2005) Curr. Pharm. Des. , vol.11 , pp. 2489-2499
    • Rusnati, M.1    Oreste, P.2    Zoppetti, G.3    Presta, M.4
  • 43
    • 23944454401 scopus 로고    scopus 로고
    • The heparin-binding site of antithrombin is crucial for antiangiogenic activity
    • Zhang, W.; Swanson, R.; Izaguirre, G.; Xiong, Y.; Lau, L.F.; Olson, S.T. The heparin-binding site of antithrombin is crucial for antiangiogenic activity. Blood 2005, 106, 1621-1628.
    • (2005) Blood , vol.106 , pp. 1621-1628
    • Zhang, W.1    Swanson, R.2    Izaguirre, G.3    Xiong, Y.4    Lau, L.F.5    Olson, S.T.6
  • 44
    • 84964698250 scopus 로고    scopus 로고
    • Toward a robust computational screening strategy for identifying glycosaminoglycan sequences that display high specificity for target proteins
    • Sankaranarayanan, N.V.; Desai, U.R. Toward a robust computational screening strategy for identifying glycosaminoglycan sequences that display high specificity for target proteins. Glycobiology 2014, 24, 1323-1333.
    • (2014) Glycobiology , vol.24 , pp. 1323-1333
    • Sankaranarayanan, N.V.1    Desai, U.R.2
  • 45
    • 0027935755 scopus 로고
    • Minimal sequence in heparin/heparan sulfate required for binding of basic fibroblast growth factor
    • Maccarana, M.; Casu, B.; Lindahl, U. Minimal sequence in heparin/heparan sulfate required for binding of basic fibroblast growth factor. J. Biol. Chem. 1994, 269, 3903-3903.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3903-3903
    • Maccarana, M.1    Casu, B.2    Lindahl, U.3
  • 46
    • 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, P.D.; Krishnasamy, C.; Kellogg, G.E.; Desai, U.R. On the specificity of heparin/heparan sulfate binding to proteins. Anion-binding sites on antithrombin and thrombin are fundamentally different. PLoS ONE 2012, 7, e48632.
    • (2012) PLoS ONE , vol.7 , pp. e48632
    • Mosier, P.D.1    Krishnasamy, C.2    Kellogg, G.E.3    Desai, U.R.4
  • 47
    • 33746614761 scopus 로고    scopus 로고
    • Interactions between heparan sulfate and proteins: The concept of specificity
    • Kreuger, J.; Spillmann, D.; Li, J.P.; Lindahl, U. Interactions between heparan sulfate and proteins: The concept of specificity. J. Cell Biol. 2006, 174, 323-327.
    • (2006) J. Cell Biol. , vol.174 , pp. 323-327
    • Kreuger, J.1    Spillmann, D.2    Li, J.P.3    Lindahl, U.4
  • 49
    • 75149113108 scopus 로고    scopus 로고
    • Importance of the spatial display of charged residues in heparin-peptide interactions
    • Rullo, A.; Nitz, M. Importance of the spatial display of charged residues in heparin-peptide interactions. Biopolymers 2010, 93, 290-298.
    • (2010) Biopolymers , vol.93 , pp. 290-298
    • Rullo, A.1    Nitz, M.2
  • 51
    • 33644977975 scopus 로고    scopus 로고
    • Vegf165-binding sites within heparan sulfate encompass two highly sulfated domains and can be liberated by k5 lyase
    • Robinson, C.J.; Mulloy, B.; Gallagher, J.T.; Stringer, S.E. Vegf165-binding sites within heparan sulfate encompass two highly sulfated domains and can be liberated by k5 lyase. J. Biol. Chem. 2006, 281, 1731-1740.
    • (2006) J. Biol. Chem. , vol.281 , pp. 1731-1740
    • Robinson, C.J.1    Mulloy, B.2    Gallagher, J.T.3    Stringer, S.E.4
  • 52
    • 79960677449 scopus 로고    scopus 로고
    • Sulfated glycosaminoglycans are required for specific and sensitive fibroblast growth factor (fgf) 19 signaling via fgf receptor 4 and betaklotho
    • Nakamura, M.; Uehara, Y.; Asada, M.; Honda, E.; Nagai, N.; Kimata, K.; Suzuki, M.; Imamura, T. Sulfated glycosaminoglycans are required for specific and sensitive fibroblast growth factor (fgf) 19 signaling via fgf receptor 4 and betaklotho. J. Biol. Chem. 2011, 286, 26418-26423.
    • (2011) J. Biol. Chem. , vol.286 , pp. 26418-26423
    • Nakamura, M.1    Uehara, Y.2    Asada, M.3    Honda, E.4    Nagai, N.5    Kimata, K.6    Suzuki, M.7    Imamura, T.8
  • 53
    • 4644364673 scopus 로고    scopus 로고
    • Angiopoietin-3 is tethered on the cell surface via heparan sulfate proteoglycans
    • Xu, Y.; Liu, Y.J.; Yu, Q. Angiopoietin-3 is tethered on the cell surface via heparan sulfate proteoglycans. J. Biol. Chem. 2004, 279, 41179-41188.
    • (2004) J. Biol. Chem. , vol.279 , pp. 41179-41188
    • Xu, Y.1    Liu, Y.J.2    Yu, Q.3
  • 54
    • 0030999829 scopus 로고    scopus 로고
    • Interaction of heparin with human angiogenin
    • Soncin, F.; Strydom, D.J.; Shapiro, R. Interaction of heparin with human angiogenin. J. Biol. Chem. 1997, 272, 9818-9824.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9818-9824
    • Soncin, F.1    Strydom, D.J.2    Shapiro, R.3
  • 55
    • 0027745824 scopus 로고
    • A heparin-binding form of placenta growth factor (plgf-2) is expressed in human umbilical vein endothelial cells and in placenta
    • Hauser, S.; Weich, H.A. A heparin-binding form of placenta growth factor (plgf-2) is expressed in human umbilical vein endothelial cells and in placenta. Growth Factors 1993, 9, 259-268.
    • (1993) Growth Factors , vol.9 , pp. 259-268
    • Hauser, S.1    Weich, H.A.2
  • 56
    • 0031055886 scopus 로고    scopus 로고
    • Characterization of heparin and heparan sulfate domains binding to the long splice variant of platelet-derived growth factor a chain
    • Feyzi, E.; Lustig, F.; Fager, G.; Spillmann, D.; Lindahl, U.; Salmivirta, M. Characterization of heparin and heparan sulfate domains binding to the long splice variant of platelet-derived growth factor a chain. J. Biol. Chem. 1997, 272, 5518-5524.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5518-5524
    • Feyzi, E.1    Lustig, F.2    Fager, G.3    Spillmann, D.4    Lindahl, U.5    Salmivirta, M.6
  • 58
    • 77953314365 scopus 로고    scopus 로고
    • Hb-egf function in cardiac valve development requires interaction with heparan sulfate proteoglycans
    • Iwamoto, R.; Mine, N.; Kawaguchi, T.; Minami, S.; Saeki, K.; Mekada, E. Hb-egf function in cardiac valve development requires interaction with heparan sulfate proteoglycans. Development 2010, 137, 2205-2214.
    • (2010) Development , vol.137 , pp. 2205-2214
    • Iwamoto, R.1    Mine, N.2    Kawaguchi, T.3    Minami, S.4    Saeki, K.5    Mekada, E.6
  • 59
    • 0033231683 scopus 로고    scopus 로고
    • Identification of cell-binding site of angiomodulin (agm/taf/mac25) that interacts with heparan sulfates on cell surface
    • Sato, J.; Hasegawa, S.; Akaogi, K.; Yasumitsu, H.; Yamada, S.; Sugahara, K.; Miyazaki, K. Identification of cell-binding site of angiomodulin (agm/taf/mac25) that interacts with heparan sulfates on cell surface. J. Cell. Biochem. 1999, 75, 187-195.
    • (1999) J. Cell. Biochem. , vol.75 , pp. 187-195
    • Sato, J.1    Hasegawa, S.2    Akaogi, K.3    Yasumitsu, H.4    Yamada, S.5    Sugahara, K.6    Miyazaki, K.7
  • 60
    • 81755180517 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans mediate the angiogenic activity of the vascular endothelial growth factor receptor-2 agonist gremlin
    • Chiodelli, P.; Mitola, S.; Ravelli, C.; Oreste, P.; Rusnati, M.; Presta, M. Heparan sulfate proteoglycans mediate the angiogenic activity of the vascular endothelial growth factor receptor-2 agonist gremlin. Arterioscler. Thromb. Vasc. Biol. 2011, 31, e116-e127.
    • (2011) Arterioscler. Thromb. Vasc. Biol. , vol.31 , pp. e116-e127
    • Chiodelli, P.1    Mitola, S.2    Ravelli, C.3    Oreste, P.4    Rusnati, M.5    Presta, M.6
  • 61
    • 33745439051 scopus 로고    scopus 로고
    • Heparin/heparan sulphate binding in the tgf-beta cytokine superfamily
    • Rider, C.C. Heparin/heparan sulphate binding in the tgf-beta cytokine superfamily. Biochem. Soc. Trans. 2006, 34, 458-460.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 458-460
    • Rider, C.C.1
  • 63
    • 77957814286 scopus 로고    scopus 로고
    • Wss25 inhibits growth of xenografted hepatocellular cancer cells in nude mice by disrupting angiogenesis via blocking bone morphogenetic protein (bmp)/smad/id1 signaling
    • Qiu, H.; Yang, B.; Pei, Z.C.; Zhang, Z.; Ding, K. Wss25 inhibits growth of xenografted hepatocellular cancer cells in nude mice by disrupting angiogenesis via blocking bone morphogenetic protein (bmp)/smad/id1 signaling. J. Biol. Chem. 2010, 285, 32638-32646.
    • (2010) J. Biol. Chem. , vol.285 , pp. 32638-32646
    • Qiu, H.1    Yang, B.2    Pei, Z.C.3    Zhang, Z.4    Ding, K.5
  • 64
    • 79952438215 scopus 로고    scopus 로고
    • Heparin inhibits interferon-gamma signaling in human endometrial stromal cells by interference with the cellular binding of interferon-gamma
    • Fluhr, H.; Spratte, J.; Heidrich, S.; Ehrhardt, J.; Steinmuller, F.; Zygmunt, M. Heparin inhibits interferon-gamma signaling in human endometrial stromal cells by interference with the cellular binding of interferon-gamma. Fertil. Steril. 2011, 95, 1272-1277.
    • (2011) Fertil. Steril. , vol.95 , pp. 1272-1277
    • Fluhr, H.1    Spratte, J.2    Heidrich, S.3    Ehrhardt, J.4    Steinmuller, F.5    Zygmunt, M.6
  • 65
    • 84875584466 scopus 로고    scopus 로고
    • Heparin inhibits tnf-alpha signaling in human endometrial stromal cells by interaction with nf-kappab
    • Spratte, J.; Meyer zu Schwabedissen, H.; Endlich, N.; Zygmunt, M.; Fluhr, H. Heparin inhibits tnf-alpha signaling in human endometrial stromal cells by interaction with nf-kappab. Mol. Hum. Reprod. 2013, 19, 227-236.
    • (2013) Mol. Hum. Reprod. , vol.19 , pp. 227-236
    • Spratte, J.1    Meyer Zu Schwabedissen, H.2    Endlich, N.3    Zygmunt, M.4    Fluhr, H.5
  • 66
    • 33746910147 scopus 로고    scopus 로고
    • Quantitative investigation of the interaction between granulocyte-macrophage colony-stimulating factor and heparin by capillary zone electrophoresis
    • Liang, A.; Du, Y.; Wang, K.; Lin, B. Quantitative investigation of the interaction between granulocyte-macrophage colony-stimulating factor and heparin by capillary zone electrophoresis. J. Sep. Sci. 2006, 29, 1637-1641.
    • (2006) J. Sep. Sci. , vol.29 , pp. 1637-1641
    • Liang, A.1    Du, Y.2    Wang, K.3    Lin, B.4
  • 67
    • 83255165440 scopus 로고    scopus 로고
    • Characterization of the interaction of interleukin-8 with hyaluronan, chondroitin sulfate, dermatan sulfate and their sulfated derivatives by spectroscopy and molecular modeling
    • Pichert, A.; Samsonov, S.A.; Theisgen, S.; Thomas, L.; Baumann, L.; Schiller, J.; Beck-Sickinger, A.G.; Huster, D.; Pisabarro, M.T. Characterization of the interaction of interleukin-8 with hyaluronan, chondroitin sulfate, dermatan sulfate and their sulfated derivatives by spectroscopy and molecular modeling. Glycobiology 2012, 22, 134-145.
    • (2012) Glycobiology , vol.22 , pp. 134-145
    • Pichert, A.1    Samsonov, S.A.2    Theisgen, S.3    Thomas, L.4    Baumann, L.5    Schiller, J.6    Beck-Sickinger, A.G.7    Huster, D.8    Pisabarro, M.T.9
  • 68
    • 62149152738 scopus 로고    scopus 로고
    • Differentiation of 3-o-sulfated heparin disaccharide isomers: Identification of structural aspects of the heparin ccl2 binding motif
    • Meissen, J.K.; Sweeney, M.D.; Girardi, M.; Lawrence, R.; Esko, J.D.; Leary, J.A. Differentiation of 3-o-sulfated heparin disaccharide isomers: Identification of structural aspects of the heparin ccl2 binding motif. J. Am. Soc. Mass Spectrom. 2009, 20, 652-657.
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 652-657
    • Meissen, J.K.1    Sweeney, M.D.2    Girardi, M.3    Lawrence, R.4    Esko, J.D.5    Leary, J.A.6
  • 72
    • 84872342951 scopus 로고    scopus 로고
    • Molecular interaction studies of HIV-1 matrix protein p17 and heparin: Identification of the heparin-binding motif of p17 as a target for the development of multitarget antagonists
    • Bugatti, A.; Giagulli, C.; Urbinati, C.; Caccuri, F.; Chiodelli, P.; Oreste, P.; Fiorentini, S.; Orro, A.; Milanesi, L.; D'Ursi, P.; et al. Molecular interaction studies of HIV-1 matrix protein p17 and heparin: Identification of the heparin-binding motif of p17 as a target for the development of multitarget antagonists. J. Biol. Chem. 2013, 288, 1150-1161.
    • (2013) J. Biol. Chem. , vol.288 , pp. 1150-1161
    • Bugatti, A.1    Giagulli, C.2    Urbinati, C.3    Caccuri, F.4    Chiodelli, P.5    Oreste, P.6    Fiorentini, S.7    Orro, A.8    Milanesi, L.9    D'Ursi, P.10
  • 73
    • 79953204312 scopus 로고    scopus 로고
    • Pregnancy-specific glycoprotein 1 induces endothelial tubulogenesis through interaction with cell surface proteoglycans
    • Lisboa, F.A.; Warren, J.; Sulkowski, G.; Aparicio, M.; David, G.; Zudaire, E.; Dveksler, G.S. Pregnancy-specific glycoprotein 1 induces endothelial tubulogenesis through interaction with cell surface proteoglycans. J. Biol. Chem. 2011, 286, 7577-7586.
    • (2011) J. Biol. Chem. , vol.286 , pp. 7577-7586
    • Lisboa, F.A.1    Warren, J.2    Sulkowski, G.3    Aparicio, M.4    David, G.5    Zudaire, E.6    Dveksler, G.S.7
  • 74
    • 17844406113 scopus 로고    scopus 로고
    • Heparan sulfate regulates the antiangiogenic activity of endothelial monocyte-activating polypeptide-II at acidic pH
    • Chang, S.Y.; Ko, H.J.; Heo, T.H.; Kang, C.Y. Heparan sulfate regulates the antiangiogenic activity of endothelial monocyte-activating polypeptide-II at acidic pH. Mol. Pharmacol. 2005, 67, 1534-1543.
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1534-1543
    • Chang, S.Y.1    Ko, H.J.2    Heo, T.H.3    Kang, C.Y.4
  • 75
    • 0032568608 scopus 로고    scopus 로고
    • Cyr61, a product of a growth factor-inducible immediate early gene, promotes angiogenesis and tumor growth
    • Babic, A.M.; Kireeva, M.L.; Kolesnikova, T.V.; Lau, L.F. Cyr61, a product of a growth factor-inducible immediate early gene, promotes angiogenesis and tumor growth. Proc. Natl. Acad. Sci. USA 1998, 95, 6355-6360.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6355-6360
    • Babic, A.M.1    Kireeva, M.L.2    Kolesnikova, T.V.3    Lau, L.F.4
  • 78
    • 28344448202 scopus 로고    scopus 로고
    • Fibrinogen and fibrin structure and functions
    • Mosesson, M.W. Fibrinogen and fibrin structure and functions. J. Thromb. Haemost. 2005, 3, 1894-1904.
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 1894-1904
    • Mosesson, M.W.1
  • 79
    • 84867280833 scopus 로고    scopus 로고
    • Heparin cofactor II, a serine protease inhibitor, promotes angiogenesis via activation of the amp-activated protein kinase-endothelial nitric-oxide synthase signaling pathway
    • Ikeda, Y.; Aihara, K.; Yoshida, S.; Iwase, T.; Tajima, S.; Izawa-Ishizawa, Y.; Kihira, Y.; Ishizawa, K.; Tomita, S.; Tsuchiya, K.; et al. Heparin cofactor II, a serine protease inhibitor, promotes angiogenesis via activation of the amp-activated protein kinase-endothelial nitric-oxide synthase signaling pathway. J. Biol. Chem. 2012, 287, 34256-34263.
    • (2012) J. Biol. Chem. , vol.287 , pp. 34256-34263
    • Ikeda, Y.1    Aihara, K.2    Yoshida, S.3    Iwase, T.4    Tajima, S.5    Izawa-Ishizawa, Y.6    Kihira, Y.7    Ishizawa, K.8    Tomita, S.9    Tsuchiya, K.10
  • 80
    • 78650939979 scopus 로고    scopus 로고
    • Heparan sulfate regulates vegf165- and vegf121-mediated vascular hyperpermeability
    • Xu, D.; Fuster, M.M.; Lawrence, R.; Esko, J.D. Heparan sulfate regulates vegf165- and vegf121-mediated vascular hyperpermeability. J. Biol. Chem. 2011, 286, 737-745.
    • (2011) J. Biol. Chem. , vol.286 , pp. 737-745
    • Xu, D.1    Fuster, M.M.2    Lawrence, R.3    Esko, J.D.4
  • 82
    • 1942470528 scopus 로고    scopus 로고
    • Kinetic model for fgf, fgfr, and proteoglycan signal transduction complex assembly
    • Ibrahimi, O.A.; Zhang, F.; Hrstka, S.C.; Mohammadi, M.; Linhardt, R.J. Kinetic model for fgf, fgfr, and proteoglycan signal transduction complex assembly. Biochemistry 2004, 43, 4724-4730.
    • (2004) Biochemistry , vol.43 , pp. 4724-4730
    • Ibrahimi, O.A.1    Zhang, F.2    Hrstka, S.C.3    Mohammadi, M.4    Linhardt, R.J.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, A.K.; Fernig, D.G.; Turnbull, J.E. 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. 2002, 277, 28554-28563.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28554-28563
    • Powell, A.K.1    Fernig, D.G.2    Turnbull, J.E.3
  • 85
    • 0035907320 scopus 로고    scopus 로고
    • Binding of heparin/heparan sulfate to fibroblast growth factor receptor 4
    • Loo, B.M.; Kreuger, J.; Jalkanen, M.; Lindahl, U.; Salmivirta, M. Binding of heparin/heparan sulfate to fibroblast growth factor receptor 4. J. Biol. Chem. 2001, 276, 16868-16876.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16868-16876
    • Loo, B.M.1    Kreuger, J.2    Jalkanen, M.3    Lindahl, U.4    Salmivirta, M.5
  • 86
    • 84887816355 scopus 로고    scopus 로고
    • Characterization of the interaction between robo1 and heparin and other glycosaminoglycans
    • Zhang, F.; Moniz, H.A.; Walcott, B.; Moremen, K.W.; Linhardt, R.J.; Wang, L. Characterization of the interaction between robo1 and heparin and other glycosaminoglycans. Biochimie 2013, 95, 2345-2353.
    • (2013) Biochimie , vol.95 , pp. 2345-2353
    • Zhang, F.1    Moniz, H.A.2    Walcott, B.3    Moremen, K.W.4    Linhardt, R.J.5    Wang, L.6
  • 88
    • 84872697413 scopus 로고    scopus 로고
    • Mapping of heparin/heparan sulfate binding sites on alphavbeta3 integrin by molecular docking
    • Ballut, L.; Sapay, N.; Chautard, E.; Imberty, A.; Ricard-Blum, S. Mapping of heparin/heparan sulfate binding sites on alphavbeta3 integrin by molecular docking. J. Mol. Recognit. JMR 2013, 26, 76-85.
    • (2013) J. Mol. Recognit. JMR , vol.26 , pp. 76-85
    • Ballut, L.1    Sapay, N.2    Chautard, E.3    Imberty, A.4    Ricard-Blum, S.5
  • 89
    • 79955386559 scopus 로고    scopus 로고
    • Heparan sulfate modification of the transmembrane receptor cd47 is necessary for inhibition of t cell receptor signaling by thrombospondin-1
    • Kaur, S.; Kuznetsova, S.A.; Pendrak, M.L.; Sipes, J.M.; Romeo, M.J.; Li, Z.; Zhang, L.; Roberts, D.D. Heparan sulfate modification of the transmembrane receptor cd47 is necessary for inhibition of t cell receptor signaling by thrombospondin-1. J. Biol. Chem. 2011, 286, 14991-15002.
    • (2011) J. Biol. Chem. , vol.286 , pp. 14991-15002
    • Kaur, S.1    Kuznetsova, S.A.2    Pendrak, M.L.3    Sipes, J.M.4    Romeo, M.J.5    Li, Z.6    Zhang, L.7    Roberts, D.D.8
  • 90
    • 84903783537 scopus 로고    scopus 로고
    • Characterisation of the conformational changes in platelet factor 4 induced by polyanions: Towards in vitro prediction of antigenicity
    • Brandt, S.; Krauel, K.; Gottschalk, K.E.; Renne, T.; Helm, C.A.; Greinacher, A.; Block, S. Characterisation of the conformational changes in platelet factor 4 induced by polyanions: Towards in vitro prediction of antigenicity. Thromb. Haemost. 2014, 112, 53-64.
    • (2014) Thromb. Haemost. , vol.112 , pp. 53-64
    • Brandt, S.1    Krauel, K.2    Gottschalk, K.E.3    Renne, T.4    Helm, C.A.5    Greinacher, A.6    Block, S.7
  • 91
    • 77957115311 scopus 로고    scopus 로고
    • Histidine-rich glycoprotein functions cooperatively with cell surface heparan sulfate on phagocytes to promote necrotic cell uptake
    • Poon, I.K.; Parish, C.R.; Hulett, M.D. Histidine-rich glycoprotein functions cooperatively with cell surface heparan sulfate on phagocytes to promote necrotic cell uptake. J. Leukoc. Biol. 2010, 88, 559-569.
    • (2010) J. Leukoc. Biol. , vol.88 , pp. 559-569
    • Poon, I.K.1    Parish, C.R.2    Hulett, M.D.3
  • 92
    • 0027983991 scopus 로고
    • Histidine-rich glycoprotein and platelet factor 4 mask heparan sulfate proteoglycans recognized by acidic and basic fibroblast growth factor
    • Brown, K.J.; Parish, C.R. Histidine-rich glycoprotein and platelet factor 4 mask heparan sulfate proteoglycans recognized by acidic and basic fibroblast growth factor. Biochemistry 1994, 33, 13918-13927.
    • (1994) Biochemistry , vol.33 , pp. 13918-13927
    • Brown, K.J.1    Parish, C.R.2
  • 93
    • 33748748060 scopus 로고    scopus 로고
    • Heparin displaces interferon-gamma-inducible chemokines (ip-10, i-tac, and mig) sequestered in the vasculature and inhibits the transendothelial migration and arterial recruitment of t cells
    • Ranjbaran, H.; Wang, Y.; Manes, T.D.; Yakimov, A.O.; Akhtar, S.; Kluger, M.S.; Pober, J.S.; Tellides, G. Heparin displaces interferon-gamma-inducible chemokines (ip-10, i-tac, and mig) sequestered in the vasculature and inhibits the transendothelial migration and arterial recruitment of t cells. Circulation 2006, 114, 1293-1300.
    • (2006) Circulation , vol.114 , pp. 1293-1300
    • Ranjbaran, H.1    Wang, Y.2    Manes, T.D.3    Yakimov, A.O.4    Akhtar, S.5    Kluger, M.S.6    Pober, J.S.7    Tellides, G.8
  • 94
    • 79960676666 scopus 로고    scopus 로고
    • Pigment epithelium-derived factor (pedf) shares binding sites in collagen with heparin/heparan sulfate proteoglycans
    • Sekiya, A.; Okano-Kosugi, H.; Yamazaki, C.M.; Koide, T. Pigment epithelium-derived factor (pedf) shares binding sites in collagen with heparin/heparan sulfate proteoglycans. J. Biol. Chem. 2011, 286, 26364-26374.
    • (2011) J. Biol. Chem. , vol.286 , pp. 26364-26374
    • Sekiya, A.1    Okano-Kosugi, H.2    Yamazaki, C.M.3    Koide, T.4
  • 96
    • 28544434955 scopus 로고    scopus 로고
    • Laminin alpha5 chain metastasis- and angiogenesis-inhibiting peptide blocks fibroblast growth factor 2 activity by binding to the heparan sulfate chains of cd44
    • Hibino, S.; Shibuya, M.; Hoffman, M.P.; Engbring, J.A.; Hossain, R.; Mochizuki, M.; Kudoh, S.; Nomizu, M.; Kleinman, H.K. Laminin alpha5 chain metastasis- and angiogenesis-inhibiting peptide blocks fibroblast growth factor 2 activity by binding to the heparan sulfate chains of cd44. Cancer Res. 2005, 65, 10494-10501.
    • (2005) Cancer Res. , vol.65 , pp. 10494-10501
    • Hibino, S.1    Shibuya, M.2    Hoffman, M.P.3    Engbring, J.A.4    Hossain, R.5    Mochizuki, M.6    Kudoh, S.7    Nomizu, M.8    Kleinman, H.K.9
  • 98
    • 0027440460 scopus 로고
    • Interaction of plasminogen activators and plasminogen with heparin: Effect of ionic strength
    • Rijken, D.C.; de Munk, G.A.; Jie, A.F. Interaction of plasminogen activators and plasminogen with heparin: Effect of ionic strength. Thromb. Haemost. 1993, 70, 867-872.
    • (1993) Thromb. Haemost. , vol.70 , pp. 867-872
    • Rijken, D.C.1    De Munk, G.A.2    Jie, A.F.3
  • 99
    • 57149114934 scopus 로고    scopus 로고
    • Hip/rpl29 antagonizes vegf and fgf2 stimulated angiogenesis by interfering with hs-dependent responses
    • D'Souza, S.; Yang, W.; Marchetti, D.; Muir, C.; Farach-Carson, M.C.; Carson, D.D. Hip/rpl29 antagonizes vegf and fgf2 stimulated angiogenesis by interfering with hs-dependent responses. J. Cell. Biochem. 2008, 105, 1183-1193.
    • (2008) J. Cell. Biochem. , vol.105 , pp. 1183-1193
    • D'Souza, S.1    Yang, W.2    Marchetti, D.3    Muir, C.4    Farach-Carson, M.C.5    Carson, D.D.6
  • 100
    • 33846025442 scopus 로고    scopus 로고
    • Antiangiogenic antithrombin blocks the heparan sulfate-dependent binding of proangiogenic growth factors to their endothelial cell receptors: Evidence for differential binding of antiangiogenic and anticoagulant forms of antithrombin to proangiogenic heparan sulfate domains
    • Zhang, W.; Swanson, R.; Xiong, Y.; Richard, B.; Olson, S.T. Antiangiogenic antithrombin blocks the heparan sulfate-dependent binding of proangiogenic growth factors to their endothelial cell receptors: Evidence for differential binding of antiangiogenic and anticoagulant forms of antithrombin to proangiogenic heparan sulfate domains. J. Biol. Chem. 2006, 281, 37302-37310.
    • (2006) J. Biol. Chem. , vol.281 , pp. 37302-37310
    • Zhang, W.1    Swanson, R.2    Xiong, Y.3    Richard, B.4    Olson, S.T.5
  • 101
    • 70350746158 scopus 로고    scopus 로고
    • Characterization of the human sulfatase sulf1 and its high affinity heparin/heparan sulfate interaction domain
    • Frese, M.A.; Milz, F.; Dick, M.; Lamanna, W.C.; Dierks, T. Characterization of the human sulfatase sulf1 and its high affinity heparin/heparan sulfate interaction domain. J. Biol. Chem. 2009, 284, 28033-28044.
    • (2009) J. Biol. Chem. , vol.284 , pp. 28033-28044
    • Frese, M.A.1    Milz, F.2    Dick, M.3    Lamanna, W.C.4    Dierks, T.5
  • 102
    • 33749008541 scopus 로고    scopus 로고
    • Oligomannurarate sulfate, a novel heparanase inhibitor simultaneously targeting basic fibroblast growth factor, combats tumor angiogenesis and metastasis
    • Zhao, H.; Liu, H.; Chen, Y.; Xin, X.; Li, J.; Hou, Y.; Zhang, Z.; Zhang, X.; Xie, C.; Geng, M.; et al. Oligomannurarate sulfate, a novel heparanase inhibitor simultaneously targeting basic fibroblast growth factor, combats tumor angiogenesis and metastasis. Cancer Res. 2006, 66, 8779-8787.
    • (2006) Cancer Res. , vol.66 , pp. 8779-8787
    • Zhao, H.1    Liu, H.2    Chen, Y.3    Xin, X.4    Li, J.5    Hou, Y.6    Zhang, Z.7    Zhang, X.8    Xie, C.9    Geng, M.10
  • 103
    • 0033960605 scopus 로고    scopus 로고
    • The potential mechanism for the effect of heparin on tissue plasminogen activator-mediated plasminogen activation
    • Liang, J.F.; Li, Y.; Yang, V.C. The potential mechanism for the effect of heparin on tissue plasminogen activator-mediated plasminogen activation. Thromb. Res. 2000, 97, 349-358.
    • (2000) Thromb. Res. , vol.97 , pp. 349-358
    • Liang, J.F.1    Li, Y.2    Yang, V.C.3
  • 104
    • 0034665981 scopus 로고    scopus 로고
    • Binding of the ng2 proteoglycan to kringle domains modulates the functional properties of angiostatin and plasmin(ogen)
    • Goretzki, L.; Lombardo, C.R.; Stallcup, W.B. Binding of the ng2 proteoglycan to kringle domains modulates the functional properties of angiostatin and plasmin(ogen). J. Biol. Chem. 2000, 275, 28625-28633.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28625-28633
    • Goretzki, L.1    Lombardo, C.R.2    Stallcup, W.B.3
  • 105
    • 0030976894 scopus 로고    scopus 로고
    • Extracellular cleavage of the vascular endothelial growth factor 189-amino acid form by urokinase is required for its mitogenic effect
    • Plouet, J.; Moro, F.; Bertagnolli, S.; Coldeboeuf, N.; Mazarguil, H.; Clamens, S.; Bayard, F. Extracellular cleavage of the vascular endothelial growth factor 189-amino acid form by urokinase is required for its mitogenic effect. J. Biol. Chem. 1997, 272, 13390-13396.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13390-13396
    • Plouet, J.1    Moro, F.2    Bertagnolli, S.3    Coldeboeuf, N.4    Mazarguil, H.5    Clamens, S.6    Bayard, F.7
  • 107
    • 68949085385 scopus 로고    scopus 로고
    • A surface plasmon resonance-based solution affinity assay for heparan sulfate-binding proteins
    • Cochran, S.; Li, C.P.; Ferro, V. A surface plasmon resonance-based solution affinity assay for heparan sulfate-binding proteins. Glycoconj. J. 2009, 26, 577-587.
    • (2009) Glycoconj. J. , vol.26 , pp. 577-587
    • Cochran, S.1    Li, C.P.2    Ferro, V.3
  • 108
    • 0026723142 scopus 로고
    • The binding of vascular endothelial growth factor to its receptors is dependent on cell surface-associated heparin-like molecules
    • Gitay-Goren, H.; Soker, S.; Vlodavsky, I.; Neufeld, G. The binding of vascular endothelial growth factor to its receptors is dependent on cell surface-associated heparin-like molecules. J. Biol. Chem. 1992, 267, 6093-6098.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6093-6098
    • Gitay-Goren, H.1    Soker, S.2    Vlodavsky, I.3    Neufeld, G.4
  • 109
    • 0028142828 scopus 로고
    • Variations in the size and sulfation of heparin modulate the effect of heparin on the binding of vegf165 to its receptors
    • Soker, S.; Goldstaub, D.; Svahn, C.M.; Vlodavsky, I.; Levi, B.Z.; Neufeld, G. Variations in the size and sulfation of heparin modulate the effect of heparin on the binding of vegf165 to its receptors. Biochem. Biophys. Res. Commun. 1994, 203, 1339-1347.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 1339-1347
    • Soker, S.1    Goldstaub, D.2    Svahn, C.M.3    Vlodavsky, I.4    Levi, B.Z.5    Neufeld, G.6
  • 110
    • 0033915671 scopus 로고    scopus 로고
    • 2.5 kda and 5.0 kda heparin fragments specifically inhibit microvessel sprouting and network formation in vegf165-mediated mammalian angiogenesis
    • Norrby, K. 2.5 kda and 5.0 kda heparin fragments specifically inhibit microvessel sprouting and network formation in vegf165-mediated mammalian angiogenesis. Int. J. Exp. Pathol. 2000, 81, 191-198.
    • (2000) Int. J. Exp. Pathol. , vol.81 , pp. 191-198
    • Norrby, K.1
  • 112
    • 0032729740 scopus 로고    scopus 로고
    • Alginate oligosaccharides stimulate vegf-mediated growth and migration of human endothelial cells
    • Kawada, A.; Hiura, N.; Tajima, S.; Takahara, H. Alginate oligosaccharides stimulate vegf-mediated growth and migration of human endothelial cells. Arch. Dermatol. Res. 1999, 291, 542-547.
    • (1999) Arch. Dermatol. Res. , vol.291 , pp. 542-547
    • Kawada, A.1    Hiura, N.2    Tajima, S.3    Takahara, H.4
  • 113
    • 0032776557 scopus 로고    scopus 로고
    • Structural features in heparin that interact with vegf165 and modulate its biological activity
    • Ono, K.; Hattori, H.; Takeshita, S.; Kurita, A.; Ishihara, M. Structural features in heparin that interact with vegf165 and modulate its biological activity. Glycobiology 1999, 9, 705-711.
    • (1999) Glycobiology , vol.9 , pp. 705-711
    • Ono, K.1    Hattori, H.2    Takeshita, S.3    Kurita, A.4    Ishihara, M.5
  • 114
    • 0026727774 scopus 로고
    • Identification of the basic fibroblast growth factor binding sequence in fibroblast heparan sulfate
    • Turnbull, J.E.; Fernig, D.G.; Ke, Y.; Wilkinson, M.C.; Gallagher, J.T. Identification of the basic fibroblast growth factor binding sequence in fibroblast heparan sulfate. J. Biol. Chem. 1992, 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
  • 116
    • 0028346380 scopus 로고
    • Interaction of hepatocyte growth factor with heparan sulfate. Elucidation of the major heparan sulfate structural determinants
    • Lyon, M.; Deakin, J.A.; Mizuno, K.; Nakamura, T.; Gallagher, J.T. Interaction of hepatocyte growth factor with heparan sulfate. Elucidation of the major heparan sulfate structural determinants. J. Biol. Chem. 1994, 269, 11216-11223.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11216-11223
    • Lyon, M.1    Deakin, J.A.2    Mizuno, K.3    Nakamura, T.4    Gallagher, J.T.5
  • 117
    • 0030789434 scopus 로고    scopus 로고
    • The interaction of the transforming growth factor-betas with heparin/heparan sulfate is isoform-specific
    • Lyon, M.; Rushton, G.; Gallagher, J.T. The interaction of the transforming growth factor-betas with heparin/heparan sulfate is isoform-specific. J. Biol. Chem. 1997, 272, 18000-18006.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18000-18006
    • Lyon, M.1    Rushton, G.2    Gallagher, J.T.3
  • 118
    • 0029871283 scopus 로고    scopus 로고
    • Structural characteristics of heparin-line domain required for interaction of midkine with embryonic neurons
    • Kaneda, N.; Talukder, A.H.; Ishihara, M.; Hara, S.; Yoshida, K.; Muramatsu, T. Structural characteristics of heparin-line domain required for interaction of midkine with embryonic neurons. Biochem. Biophys. Res. Commun. 1996, 220, 108-112.
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 108-112
    • Kaneda, N.1    Talukder, A.H.2    Ishihara, M.3    Hara, S.4    Yoshida, K.5    Muramatsu, T.6
  • 119
    • 0034686015 scopus 로고    scopus 로고
    • Structural requirements of heparan sulfate for the binding to the tumor-derived adhesion factor/angiomodulin that induces cord-like structures to ecv-304 human carcinoma cells
    • Kishibe, J.; Yamada, S.; Okada, Y.; Sato, J.; Ito, A.; Miyazaki, K.; Sugahara, K. Structural requirements of heparan sulfate for the binding to the tumor-derived adhesion factor/angiomodulin that induces cord-like structures to ecv-304 human carcinoma cells. J. Biol. Chem. 2000, 275, 15321-15329.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15321-15329
    • Kishibe, J.1    Yamada, S.2    Okada, Y.3    Sato, J.4    Ito, A.5    Miyazaki, K.6    Sugahara, K.7
  • 120
    • 84898603944 scopus 로고    scopus 로고
    • Ovarian cancer cell heparan sulfate 6-o-sulfotransferases regulate an angiogenic program induced by heparin-binding epidermal growth factor (egf)-like growth factor/egf receptor signaling
    • Cole, C.L.; Rushton, G.; Jayson, G.C.; Avizienyte, E. Ovarian cancer cell heparan sulfate 6-o-sulfotransferases regulate an angiogenic program induced by heparin-binding epidermal growth factor (egf)-like growth factor/egf receptor signaling. J. Biol. Chem. 2014, 289, 10488-10501.
    • (2014) J. Biol. Chem. , vol.289 , pp. 10488-10501
    • Cole, C.L.1    Rushton, G.2    Jayson, G.C.3    Avizienyte, E.4
  • 122
    • 0032546954 scopus 로고    scopus 로고
    • Defining the interleukin-8-binding domain of heparan sulfate
    • Spillmann, D.; Witt, D.; Lindahl, U. Defining the interleukin-8-binding domain of heparan sulfate. J. Biol. Chem. 1998, 273, 15487-15493.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15487-15493
    • Spillmann, D.1    Witt, D.2    Lindahl, U.3
  • 123
    • 0035896615 scopus 로고    scopus 로고
    • Characterization of the stromal cell-derived factor-1alpha-heparin complex
    • Sadir, R.; Baleux, F.; Grosdidier, A.; Imberty, A.; Lortat-Jacob, H. Characterization of the stromal cell-derived factor-1alpha-heparin complex. J. Biol. Chem. 2001, 276, 8288-8296.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8288-8296
    • Sadir, R.1    Baleux, F.2    Grosdidier, A.3    Imberty, A.4    Lortat-Jacob, H.5
  • 124
    • 0026670384 scopus 로고
    • Binding of interferon-gamma to heparan sulfate is restricted to the heparin-like domains and involves carboxylic-but not n-sulfated-groups
    • Lortat-Jacob, H.; Grimaud, J.A. Binding of interferon-gamma to heparan sulfate is restricted to the heparin-like domains and involves carboxylic - but not n-sulfated - groups. Biochim. Biophys. Acta 1992, 1117, 126-130.
    • (1992) Biochim. Biophys. Acta , vol.1117 , pp. 126-130
    • Lortat-Jacob, H.1    Grimaud, J.A.2
  • 125
    • 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.; Leary, J.A. Effects of sulfate position on heparin octasaccharide binding to ccl2 examined by tandem mass spectrometry. J. Am. Soc. Mass Spectrom. 2006, 17, 1114-1119.
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1114-1119
    • Sweeney, M.D.1    Yu, Y.2    Leary, J.A.3
  • 126
    • 0036721004 scopus 로고    scopus 로고
    • Characterization of the binding site on heparan sulfate for macrophage inflammatory protein 1alpha
    • Stringer, S.E.; Forster, M.J.; Mulloy, B.; Bishop, C.R.; Graham, G.J.; Gallagher, J.T. Characterization of the binding site on heparan sulfate for macrophage inflammatory protein 1alpha. Blood 2002, 100, 1543-1550.
    • (2002) Blood , vol.100 , pp. 1543-1550
    • Stringer, S.E.1    Forster, M.J.2    Mulloy, B.3    Bishop, C.R.4    Graham, G.J.5    Gallagher, J.T.6
  • 128
    • 0028068096 scopus 로고
    • Distinct role of 2-o-, n-, and 6-o-sulfate groups of heparin in the formation of the ternary complex with basic fibroblast growth factor and soluble fgf receptor-1
    • Rusnati, M.; Coltrini, D.; Caccia, P.; Dell'Era, P.; Zoppetti, G.; Oreste, P.; Valsasina, B.; Presta, M. Distinct role of 2-o-, n-, and 6-o-sulfate groups of heparin in the formation of the ternary complex with basic fibroblast growth factor and soluble fgf receptor-1. Biochem. Biophys. Res. Commun. 1994, 203, 450-458.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 450-458
    • Rusnati, M.1    Coltrini, D.2    Caccia, P.3    Dell'Era, P.4    Zoppetti, G.5    Oreste, P.6    Valsasina, B.7    Presta, M.8
  • 129
    • 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, K.A.; Ori, A.; Ahmed, Y.A.; Yates, E.A.; Fernig, D.G. Characterisation of the interaction of neuropilin-1 with heparin and a heparan sulfate mimetic library of heparin-derived sugars. Peer J. 2014, 2, e461.
    • (2014) Peer J. , vol.2 , pp. e461
    • Uniewicz, K.A.1    Ori, A.2    Ahmed, Y.A.3    Yates, E.A.4    Fernig, D.G.5
  • 130
    • 0034737433 scopus 로고    scopus 로고
    • Interaction of thrombospondin-1 and heparan sulfate from endothelial cells. Structural requirements of heparan sulfate
    • Feitsma, K.; Hausser, H.; Robenek, H.; Kresse, H.; Vischer, P. Interaction of thrombospondin-1 and heparan sulfate from endothelial cells. Structural requirements of heparan sulfate. J. Biol. Chem. 2000, 275, 9396-9402.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9396-9402
    • Feitsma, K.1    Hausser, H.2    Robenek, H.3    Kresse, H.4    Vischer, P.5
  • 132
    • 0142009678 scopus 로고    scopus 로고
    • Binding of endostatin to endothelial heparan sulphate shows a differential requirement for specific sulphates
    • Blackhall, F.H.; Merry, C.L.; Lyon, M.; Jayson, G.C.; Folkman, J.; Javaherian, K.; Gallagher, J.T. Binding of endostatin to endothelial heparan sulphate shows a differential requirement for specific sulphates. Biochem. J. 2003, 375, 131-139.
    • (2003) Biochem. J. , vol.375 , pp. 131-139
    • Blackhall, F.H.1    Merry, C.L.2    Lyon, M.3    Jayson, G.C.4    Folkman, J.5    Javaherian, K.6    Gallagher, J.T.7
  • 134
    • 84895185867 scopus 로고    scopus 로고
    • Molecular docking of heparin oligosaccharides with hep-ii heparin-binding domain of fibronectin reveals an interplay between the different positions of sulfate groups
    • Carpentier, M.; Denys, A.; Allain, F.; Vergoten, G. Molecular docking of heparin oligosaccharides with hep-ii heparin-binding domain of fibronectin reveals an interplay between the different positions of sulfate groups. Glycoconj. J. 2014, 31, 161-169.
    • (2014) Glycoconj. J. , vol.31 , pp. 161-169
    • Carpentier, M.1    Denys, A.2    Allain, F.3    Vergoten, G.4
  • 135
    • 84929627872 scopus 로고    scopus 로고
    • Angiogenic growth factors interactome and drug discovery: The contribution of surface plasmon resonance
    • in press
    • Rusnati, M.; Presta, M. Angiogenic growth factors interactome and drug discovery: The contribution of surface plasmon resonance. Cytokine Growth Factor Rev. 2014, in press.
    • (2014) Cytokine Growth Factor Rev.
    • Rusnati, M.1    Presta, M.2
  • 137
    • 0027418048 scopus 로고
    • Preparation of affinity-fractionated, heparin-derived oligosaccharides and their effects on selected biological activities mediated by basic fibroblast growth factor
    • Ishihara, M.; Tyrrell, D.J.; Stauber, G.B.; Brown, S.; Cousens, L.S.; Stack, R.J. Preparation of affinity-fractionated, heparin-derived oligosaccharides and their effects on selected biological activities mediated by basic fibroblast growth factor. J. Biol. Chem. 1993, 268, 4675-4683.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4675-4683
    • Ishihara, M.1    Tyrrell, D.J.2    Stauber, G.B.3    Brown, S.4    Cousens, L.S.5    Stack, R.J.6
  • 138
    • 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, B.B.; Lindahl, U.; Rapraeger, A.C. Activating and inhibitory heparin sequences for fgf-2 (basic fgf). Distinct requirements for fgf-1, fgf-2, and fgf-4. J. Biol. Chem. 1993, 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
  • 140
    • 0037071542 scopus 로고    scopus 로고
    • Fibroblast growth factor-specific modulation of cellular response by syndecan-4
    • Horowitz, A.; Tkachenko, E.; Simons, M. Fibroblast growth factor-specific modulation of cellular response by syndecan-4. J. Cell Biol. 2002, 157, 715-725.
    • (2002) J. Cell Biol. , vol.157 , pp. 715-725
    • Horowitz, A.1    Tkachenko, E.2    Simons, M.3
  • 141
    • 0027389354 scopus 로고
    • Internalization of basic fibroblast growth factor (bfgf) in cultured endothelial cells: Role of the low affinity heparin-like bfgf receptors
    • Rusnati, M.; Urbinati, C.; Presta, M. Internalization of basic fibroblast growth factor (bfgf) in cultured endothelial cells: Role of the low affinity heparin-like bfgf receptors. J. Cell. Physiol. 1993, 154, 152-161.
    • (1993) J. Cell. Physiol. , vol.154 , pp. 152-161
    • Rusnati, M.1    Urbinati, C.2    Presta, M.3
  • 142
    • 0024410420 scopus 로고
    • Basic fibroblast growth factor is released from endothelial extracellular matrix in a biologically active form
    • Presta, M.; Maier, J.A.; Rusnati, M.; Ragnotti, G. Basic fibroblast growth factor is released from endothelial extracellular matrix in a biologically active form. J. Cell. Physiol. 1989, 140, 68-74.
    • (1989) J. Cell. Physiol. , vol.140 , pp. 68-74
    • Presta, M.1    Maier, J.A.2    Rusnati, M.3    Ragnotti, G.4
  • 144
    • 0022477372 scopus 로고
    • Heparin protects basic and acidic fgf from inactivation
    • Gospodarowicz, D.; Cheng, J. Heparin protects basic and acidic fgf from inactivation. J. Cell. Physiol. 1986, 128, 475-484.
    • (1986) J. Cell. Physiol. , vol.128 , pp. 475-484
    • Gospodarowicz, D.1    Cheng, J.2
  • 145
    • 0024579448 scopus 로고
    • Interaction of heparin with human basic fibroblast growth factor: Protection of the angiogenic protein from proteolytic degradation by a glycosaminoglycan
    • Sommer, A.; Rifkin, D.B. Interaction of heparin with human basic fibroblast growth factor: Protection of the angiogenic protein from proteolytic degradation by a glycosaminoglycan. J. Cell. Physiol. 1989, 138, 215-220.
    • (1989) J. Cell. Physiol. , vol.138 , pp. 215-220
    • Sommer, A.1    Rifkin, D.B.2
  • 146
    • 0025001394 scopus 로고
    • Heparin and heparan sulfate increase the radius of diffusion and action of basic fibroblast growth factor
    • Flaumenhaft, R.; Moscatelli, D.; Rifkin, D.B. Heparin and heparan sulfate increase the radius of diffusion and action of basic fibroblast growth factor. J. Cell Biol. 1990, 111, 1651-1659.
    • (1990) J. Cell Biol. , vol.111 , pp. 1651-1659
    • Flaumenhaft, R.1    Moscatelli, D.2    Rifkin, D.B.3
  • 147
    • 18544372310 scopus 로고    scopus 로고
    • Short heparin sequences spaced by glycol-split uronate residues are antagonists of fibroblast growth factor 2 and angiogenesis inhibitors
    • Casu, B.; Guerrini, M.; Naggi, A.; Perez, M.; Torri, G.; Ribatti, D.; Carminati, P.; Giannini, G.; Penco, S.; Pisano, C.; et al. Short heparin sequences spaced by glycol-split uronate residues are antagonists of fibroblast growth factor 2 and angiogenesis inhibitors. Biochemistry 2002, 41, 10519-10528.
    • (2002) Biochemistry , vol.41 , pp. 10519-10528
    • Casu, B.1    Guerrini, M.2    Naggi, A.3    Perez, M.4    Torri, G.5    Ribatti, D.6    Carminati, P.7    Giannini, G.8    Penco, S.9    Pisano, C.10
  • 148
    • 0025950158 scopus 로고
    • A dual receptor system is required for basic fibroblast growth factor activity
    • Klagsbrun, M.; Baird, A. A dual receptor system is required for basic fibroblast growth factor activity. Cell 1991, 67, 229-231.
    • (1991) Cell , vol.67 , pp. 229-231
    • Klagsbrun, M.1    Baird, A.2
  • 149
    • 0028075526 scopus 로고
    • Different effects of mucosal, bovine lung and chemically modified heparin on selected biological properties of basic fibroblast growth factor
    • Coltrini, D.; Rusnati, M.; Zoppetti, G.; Oreste, P.; Grazioli, G.; Naggi, A.; Presta, M. Different effects of mucosal, bovine lung and chemically modified heparin on selected biological properties of basic fibroblast growth factor. Biochem. J. 1994, 303, 583-590.
    • (1994) Biochem. J. , vol.303 , pp. 583-590
    • Coltrini, D.1    Rusnati, M.2    Zoppetti, G.3    Oreste, P.4    Grazioli, G.5    Naggi, A.6    Presta, M.7
  • 150
    • 70450208952 scopus 로고    scopus 로고
    • The heparin-binding domain confers diverse functions of vegf-a in development and disease: A structure-function study
    • Krilleke, D.; Ng, Y.S.; Shima, D.T. The heparin-binding domain confers diverse functions of vegf-a in development and disease: A structure-function study. Biochem. Soc. Trans. 2009, 37, 1201-1206.
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 1201-1206
    • Krilleke, D.1    Ng, Y.S.2    Shima, D.T.3
  • 151
    • 0028218987 scopus 로고
    • Energetic characterization of the basic fibroblast growth factor-heparin interaction: Identification of the heparin binding domain
    • Thompson, L.D.; Pantoliano, M.W.; Springer, B.A. Energetic characterization of the basic fibroblast growth factor-heparin interaction: Identification of the heparin binding domain. Biochemistry 1994, 33, 3831-3840.
    • (1994) Biochemistry , vol.33 , pp. 3831-3840
    • Thompson, L.D.1    Pantoliano, M.W.2    Springer, B.A.3
  • 152
    • 34347244140 scopus 로고    scopus 로고
    • Basic fibroblast growth factor: Lysine 134 is essential for its neuroprotective activity
    • Rose, K.; Kriha, D.; Pallast, S.; Junker, V.; Klumpp, S.; Krieglstein, J. Basic fibroblast growth factor: Lysine 134 is essential for its neuroprotective activity. Neurochem. Int. 2007, 51, 25-31.
    • (2007) Neurochem. Int. , vol.51 , pp. 25-31
    • Rose, K.1    Kriha, D.2    Pallast, S.3    Junker, V.4    Klumpp, S.5    Krieglstein, J.6
  • 153
    • 0034718796 scopus 로고    scopus 로고
    • Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin
    • Pellegrini, L.; Burke, D.F.; von Delft, F.; Mulloy, B.; Blundell, T.L. Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin. Nature 2000, 407, 1029-1034.
    • (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
  • 156
    • 0141844583 scopus 로고    scopus 로고
    • The n-terminal domain of hepatocyte growth factor inhibits the angiogenic behavior of endothelial cells independently from binding to the c-met receptor
    • Merkulova-Rainon, T.; England, P.; Ding, S.; Demerens, C.; Tobelem, G. The n-terminal domain of hepatocyte growth factor inhibits the angiogenic behavior of endothelial cells independently from binding to the c-met receptor. J. Biol. Chem. 2003, 278, 37400-37408.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37400-37408
    • Merkulova-Rainon, T.1    England, P.2    Ding, S.3    Demerens, C.4    Tobelem, G.5
  • 159
    • 0025976609 scopus 로고
    • Interferon-gamma binds to heparan sulfate by a cluster of amino acids located in the c-terminal part of the molecule
    • Lortat-Jacob, H.; Grimaud, J.A. Interferon-gamma binds to heparan sulfate by a cluster of amino acids located in the c-terminal part of the molecule. FEBS Lett. 1991, 280, 152-154.
    • (1991) FEBS Lett. , vol.280 , pp. 152-154
    • Lortat-Jacob, H.1    Grimaud, J.A.2
  • 160
    • 0026776936 scopus 로고
    • Transforming growth factor-beta 1 is a heparin-binding protein: Identification of putative heparin-binding regions and isolation of heparins with varying affinity for tgf-beta 1
    • McCaffrey, T.A.; Falcone, D.J.; Du, B. Transforming growth factor-beta 1 is a heparin-binding protein: Identification of putative heparin-binding regions and isolation of heparins with varying affinity for tgf-beta 1. J. Cell. Physiol. 1992, 152, 430-440.
    • (1992) J. Cell. Physiol. , vol.152 , pp. 430-440
    • McCaffrey, T.A.1    Falcone, D.J.2    Du, B.3
  • 163
    • 0032491615 scopus 로고    scopus 로고
    • Lysine 58 and histidine 66 at the c-terminal alpha-helix of monocyte chemoattractant protein-1 are essential for glycosaminoglycan binding
    • Chakravarty, L.; Rogers, L.; Quach, T.; Breckenridge, S.; Kolattukudy, P.E. Lysine 58 and histidine 66 at the c-terminal alpha-helix of monocyte chemoattractant protein-1 are essential for glycosaminoglycan binding. J. Biol. Chem. 1998, 273, 29641-29647.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29641-29647
    • Chakravarty, L.1    Rogers, L.2    Quach, T.3    Breckenridge, S.4    Kolattukudy, P.E.5
  • 165
    • 0028894975 scopus 로고
    • Heparan sulfates mediate the binding of basic fibroblast growth factor to a specific receptor on neural precursor cells
    • Brickman, Y.G.; Ford, M.D.; Small, D.H.; Bartlett, P.F.; Nurcombe, V. Heparan sulfates mediate the binding of basic fibroblast growth factor to a specific receptor on neural precursor cells. J. Biol. Chem. 1995, 270, 24941-24948.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24941-24948
    • Brickman, Y.G.1    Ford, M.D.2    Small, D.H.3    Bartlett, P.F.4    Nurcombe, V.5
  • 166
    • 71049175228 scopus 로고    scopus 로고
    • Identification of heparin-binding sites in proteins by selective labeling
    • Ori, A.; Free, P.; Courty, J.; Wilkinson, M.C.; Fernig, D.G. Identification of heparin-binding sites in proteins by selective labeling. Mol. Cell. Proteomics 2009, 8, 2256-2265.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2256-2265
    • Ori, A.1    Free, P.2    Courty, J.3    Wilkinson, M.C.4    Fernig, D.G.5
  • 167
    • 24344438588 scopus 로고    scopus 로고
    • Endostatin phenylalanines 31 and 34 define a receptor binding site
    • Stahl, S.; Gaetzner, S.; Mueller, T.D.; Felbor, U. Endostatin phenylalanines 31 and 34 define a receptor binding site. Genes Cells 2005, 10, 929-939.
    • (2005) Genes Cells , vol.10 , pp. 929-939
    • Stahl, S.1    Gaetzner, S.2    Mueller, T.D.3    Felbor, U.4
  • 168
    • 20144376911 scopus 로고    scopus 로고
    • Identification and characterization of heparin/heparan sulfate binding domains of the endoglycosidase heparanase
    • Levy-Adam, F.; Abboud-Jarrous, G.; Guerrini, M.; Beccati, D.; Vlodavsky, I.; Ilan, N. Identification and characterization of heparin/heparan sulfate binding domains of the endoglycosidase heparanase. J. Biol. Chem. 2005, 280, 20457-20466.
    • (2005) J. Biol. Chem. , vol.280 , pp. 20457-20466
    • Levy-Adam, F.1    Abboud-Jarrous, G.2    Guerrini, M.3    Beccati, D.4    Vlodavsky, I.5    Ilan, N.6
  • 169
    • 33644845278 scopus 로고    scopus 로고
    • Structure of murine angiogenin: Features of the substrate- and cell-binding regions and prospects for inhibitor-binding studies. Acta Crystallogr. Sect. D Biol
    • Holloway, D.E.; Chavali, G.B.; Hares, M.C.; Subramanian, V.; Acharya, K.R. Structure of murine angiogenin: Features of the substrate- and cell-binding regions and prospects for inhibitor-binding studies. Acta Crystallogr. Sect. D Biol. Crystallogr. 2005, 61, 1568-1578.
    • (2005) Crystallogr. , vol.61 , pp. 1568-1578
    • Holloway, D.E.1    Chavali, G.B.2    Hares, M.C.3    Subramanian, V.4    Acharya, K.R.5
  • 170
    • 0028262977 scopus 로고
    • Nuclear translocation of angiogenin in proliferating endothelial cells is essential to its angiogenic activity
    • Moroianu, J.; Riordan, J.F. Nuclear translocation of angiogenin in proliferating endothelial cells is essential to its angiogenic activity. Proc. Natl. Acad. Sci. USA 1994, 91, 1677-1681.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1677-1681
    • Moroianu, J.1    Riordan, J.F.2
  • 171
    • 0027427538 scopus 로고
    • Identification of novel heparin-releasable proteins, as well as the cytokines midkine and pleiotrophin, in human postheparin plasma
    • Novotny, W.F.; Maffi, T.; Mehta, R.L.; Milner, P.G. Identification of novel heparin-releasable proteins, as well as the cytokines midkine and pleiotrophin, in human postheparin plasma. Arterioscler. Thromb. 1993, 13, 1798-1805.
    • (1993) Arterioscler. Thromb. , vol.13 , pp. 1798-1805
    • Novotny, W.F.1    Maffi, T.2    Mehta, R.L.3    Milner, P.G.4
  • 173
    • 4444347398 scopus 로고    scopus 로고
    • Chondroitin sulfate chains on syndecan-1 and syndecan-4 from normal murine mammary gland epithelial cells are structurally and functionally distinct and cooperate with heparan sulfate chains to bind growth factors. A novel function to control binding of midkine, pleiotrophin, and basic fibroblast growth factor
    • Deepa, S.S.; Yamada, S.; Zako, M.; Goldberger, O.; Sugahara, K. Chondroitin sulfate chains on syndecan-1 and syndecan-4 from normal murine mammary gland epithelial cells are structurally and functionally distinct and cooperate with heparan sulfate chains to bind growth factors. A novel function to control binding of midkine, pleiotrophin, and basic fibroblast growth factor. J. Biol. Chem. 2004, 279, 37368-37376.
    • (2004) J. Biol. Chem. , vol.279 , pp. 37368-37376
    • Deepa, S.S.1    Yamada, S.2    Zako, M.3    Goldberger, O.4    Sugahara, K.5
  • 175
    • 84855860082 scopus 로고    scopus 로고
    • Hgf/c-met targeted therapeutics: Novel strategies for cancer medicine
    • Yap, T.A.; Sandhu, S.K.; Alam, S.M.; de Bono, J.S. Hgf/c-met targeted therapeutics: Novel strategies for cancer medicine. Curr. Drug Targets 2011, 12, 2045-2058.
    • (2011) Curr. Drug Targets , vol.12 , pp. 2045-2058
    • Yap, T.A.1    Sandhu, S.K.2    Alam, S.M.3    De Bono, J.S.4
  • 176
    • 0035980123 scopus 로고    scopus 로고
    • Dissociation of heparan sulfate and receptor binding domains of hepatocyte growth factor reveals that heparan sulfate-c-met interaction facilitates signaling
    • Rubin, J.S.; Day, R.M.; Breckenridge, D.; Atabey, N.; Taylor, W.G.; Stahl, S.J.; Wingfield, P.T.; Kaufman, J.D.; Schwall, R.; Bottaro, D.P. Dissociation of heparan sulfate and receptor binding domains of hepatocyte growth factor reveals that heparan sulfate-c-met interaction facilitates signaling. J. Biol. Chem. 2001, 276, 32977-32983.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32977-32983
    • Rubin, J.S.1    Day, R.M.2    Breckenridge, D.3    Atabey, N.4    Taylor, W.G.5    Stahl, S.J.6    Wingfield, P.T.7    Kaufman, J.D.8    Schwall, R.9    Bottaro, D.P.10
  • 177
    • 0028784965 scopus 로고
    • Characterization of heparan sulfate oligosaccharides that bind to hepatocyte growth factor
    • Ashikari, S.; Habuchi, H.; Kimata, K. Characterization of heparan sulfate oligosaccharides that bind to hepatocyte growth factor. J. Biol. Chem. 1995, 270, 29586-29593.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29586-29593
    • Ashikari, S.1    Habuchi, H.2    Kimata, K.3
  • 180
    • 0028234605 scopus 로고
    • Hepatocyte growth factor immobilized onto culture substrates through heparin and matrigel enhances DNA synthesis in primary rat hepatocytes
    • Kato, S.; Ishii, T.; Hara, H.; Sugiura, N.; Kimata, K.; Akamatsu, N. Hepatocyte growth factor immobilized onto culture substrates through heparin and matrigel enhances DNA synthesis in primary rat hepatocytes. Exp. Cell Res. 1994, 211, 53-58.
    • (1994) Exp. Cell Res. , vol.211 , pp. 53-58
    • Kato, S.1    Ishii, T.2    Hara, H.3    Sugiura, N.4    Kimata, K.5    Akamatsu, N.6
  • 182
    • 77953545354 scopus 로고    scopus 로고
    • Bsa conjugates bearing multiple copies of the basic domain of HIV-1 tat: Prototype for the development of multitarget inhibitors of extracellular tat
    • Bugatti, A.; Chiodelli, P.; Rosenbluh, J.; Loyter, A.; Rusnati, M. Bsa conjugates bearing multiple copies of the basic domain of HIV-1 tat: Prototype for the development of multitarget inhibitors of extracellular tat. Antivir. Res. 2010, 87, 30-39.
    • (2010) Antivir. Res. , vol.87 , pp. 30-39
    • Bugatti, A.1    Chiodelli, P.2    Rosenbluh, J.3    Loyter, A.4    Rusnati, M.5
  • 185
    • 0030862924 scopus 로고    scopus 로고
    • HIV-1 tat protein exits from cells via a leaderless secretory pathway and binds to extracellular matrix-associated heparan sulfate proteoglycans through its basic region
    • Chang, H.C.; Samaniego, F.; Nair, B.C.; Buonaguro, L.; Ensoli, B. HIV-1 tat protein exits from cells via a leaderless secretory pathway and binds to extracellular matrix-associated heparan sulfate proteoglycans through its basic region. Aids 1997, 11, 1421-1431.
    • (1997) Aids , vol.11 , pp. 1421-1431
    • Chang, H.C.1    Samaniego, F.2    Nair, B.C.3    Buonaguro, L.4    Ensoli, B.5
  • 186
    • 0033988237 scopus 로고    scopus 로고
    • Identification of specific molecular structures of human immunodeficiency virus type 1 tat relevant for its biological effects on vascular endothelial cells
    • Mitola, S.; Soldi, R.; Zanon, I.; Barra, L.; Gutierrez, M.I.; Berkhout, B.; Giacca, M.; Bussolino, F. Identification of specific molecular structures of human immunodeficiency virus type 1 tat relevant for its biological effects on vascular endothelial cells. J. Virol. 2000, 74, 344-353.
    • (2000) J. Virol. , vol.74 , pp. 344-353
    • Mitola, S.1    Soldi, R.2    Zanon, I.3    Barra, L.4    Gutierrez, M.I.5    Berkhout, B.6    Giacca, M.7    Bussolino, F.8
  • 189
    • 0026501666 scopus 로고
    • Compartmentalization of pdgf on extracellular binding sites dependent on exon-6-encoded sequences
    • Raines, E.W.; Ross, R. Compartmentalization of pdgf on extracellular binding sites dependent on exon-6-encoded sequences. J. Cell Biol. 1992, 116, 533-543.
    • (1992) J. Cell Biol. , vol.116 , pp. 533-543
    • Raines, E.W.1    Ross, R.2
  • 190
    • 0037205421 scopus 로고    scopus 로고
    • Heparin amplifies platelet-derived growth factor (pdgf)- bb-induced pdgf alpha -receptor but not pdgf beta-receptor tyrosine phosphorylation in heparan sulfate-deficient cells. Effects on signal transduction and biological responses
    • Rolny, C.; Spillmann, D.; Lindahl, U.; Claesson-Welsh, L. Heparin amplifies platelet-derived growth factor (pdgf)- bb-induced pdgf alpha -receptor but not pdgf beta-receptor tyrosine phosphorylation in heparan sulfate-deficient cells. Effects on signal transduction and biological responses. J. Biol. Chem. 2002, 277, 19315-19321.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19315-19321
    • Rolny, C.1    Spillmann, D.2    Lindahl, U.3    Claesson-Welsh, L.4
  • 191
    • 84877110299 scopus 로고    scopus 로고
    • Transforming growth factor beta family members in regulation of vascular function: In the light of vascular conditional knockouts
    • Jakobsson, L.; van Meeteren, L.A. Transforming growth factor beta family members in regulation of vascular function: In the light of vascular conditional knockouts. Exp. Cell Res. 2013, 319, 1264-1270.
    • (2013) Exp. Cell Res. , vol.319 , pp. 1264-1270
    • Jakobsson, L.1    Van Meeteren, L.A.2
  • 193
    • 0035310360 scopus 로고    scopus 로고
    • Recombinant soluble betaglycan is a potent and isoform-selective transforming growth factor-beta neutralizing agent
    • Vilchis-Landeros, M.M.; Montiel, J.L.; Mendoza, V.; Mendoza-Hernandez, G.; Lopez-Casillas, F. Recombinant soluble betaglycan is a potent and isoform-selective transforming growth factor-beta neutralizing agent. Biochem. J. 2001, 355, 215-222.
    • (2001) Biochem. J. , vol.355 , pp. 215-222
    • Vilchis-Landeros, M.M.1    Montiel, J.L.2    Mendoza, V.3    Mendoza-Hernandez, G.4    Lopez-Casillas, F.5
  • 194
    • 47249139521 scopus 로고    scopus 로고
    • Monocyte chemotactic protein (mcp)-1 promotes angiogenesis via a novel transcription factor, mcp-1-induced protein (mcpip)
    • Niu, J.; Azfer, A.; Zhelyabovska, O.; Fatma, S.; Kolattukudy, P.E. Monocyte chemotactic protein (mcp)-1 promotes angiogenesis via a novel transcription factor, mcp-1-induced protein (mcpip). J. Biol. Chem. 2008, 283, 14542-14551.
    • (2008) J. Biol. Chem. , vol.283 , pp. 14542-14551
    • Niu, J.1    Azfer, A.2    Zhelyabovska, O.3    Fatma, S.4    Kolattukudy, P.E.5
  • 195
    • 2542498611 scopus 로고    scopus 로고
    • Identification of the glycosaminoglycan binding site of the CC chemokine, MCP-1: Implications for structure and function in vivo
    • Lau, E.K.; Paavola, C.D.; Johnson, Z.; Gaudry, J.P.; Geretti, E.; Borlat, F.; Kungl, A.J.; Proudfoot, A.E.; Handel, T.M. Identification of the glycosaminoglycan binding site of the CC chemokine, MCP-1: Implications for structure and function in vivo. J. Biol. Chem. 2004, 279, 22294-22305.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22294-22305
    • Lau, E.K.1    Paavola, C.D.2    Johnson, Z.3    Gaudry, J.P.4    Geretti, E.5    Borlat, F.6    Kungl, A.J.7    Proudfoot, A.E.8    Handel, T.M.9
  • 196
    • 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.; Leary, J.A. Chemokine-glycosaminoglycan binding: Specificity for CCR2 ligand binding to highly sulfated oligosaccharides using FTICR mass spectrometry. J. Biol. Chem. 2005, 280, 32200-32208.
    • (2005) J. Biol. Chem. , vol.280 , pp. 32200-32208
    • Yu, Y.1    Sweeney, M.D.2    Saad, O.M.3    Crown, S.E.4    Hsu, A.R.5    Handel, T.M.6    Leary, J.A.7
  • 197
    • 0035884649 scopus 로고    scopus 로고
    • Multimerization of monocyte chemoattractant protein-1 is not required for glycosaminoglycan-dependent transendothelial chemotaxis
    • Ali, S.; Palmer, A.C.; Fritchley, S.J.; Maley, Y.; Kirby, J.A. Multimerization of monocyte chemoattractant protein-1 is not required for glycosaminoglycan-dependent transendothelial chemotaxis. Biochem. J. 2001, 358, 737-745.
    • (2001) Biochem. J. , vol.358 , pp. 737-745
    • Ali, S.1    Palmer, A.C.2    Fritchley, S.J.3    Maley, Y.4    Kirby, J.A.5
  • 198
  • 199
    • 0030055212 scopus 로고    scopus 로고
    • Heparin decreases the blood clearance of interferon-gamma and increases its activity by limiting the processing of its carboxyl-terminal sequence
    • Lortat-Jacob, H.; Baltzer, F.; Grimaud, J.A. Heparin decreases the blood clearance of interferon-gamma and increases its activity by limiting the processing of its carboxyl-terminal sequence. J. Biol. Chem. 1996, 271, 16139-16143.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16139-16143
    • Lortat-Jacob, H.1    Baltzer, F.2    Grimaud, J.A.3
  • 200
    • 0031054407 scopus 로고    scopus 로고
    • Examination of the mechanism by which heparin antagonizes activation of a model endothelium by interferon-gamma (ifn-gamma)
    • Douglas, M.S.; Rix, D.A.; Dark, J.H.; Talbot, D.; Kirby, J.A. Examination of the mechanism by which heparin antagonizes activation of a model endothelium by interferon-gamma (ifn-gamma). Clin. Exp. Immunol. 1997, 107, 578-584.
    • (1997) Clin. Exp. Immunol. , vol.107 , pp. 578-584
    • Douglas, M.S.1    Rix, D.A.2    Dark, J.H.3    Talbot, D.4    Kirby, J.A.5
  • 202
    • 79957624872 scopus 로고    scopus 로고
    • HIV-1 p17 matrix protein interacts with heparan sulfate side chain of CD44v3, syndecan-2, and syndecan-4 proteoglycans expressed on human activated CD4+ t cells affecting tumor necrosis factor alpha and interleukin 2 production
    • De Francesco, M.A.; Baronio, M.; Poiesi, C. HIV-1 p17 matrix protein interacts with heparan sulfate side chain of CD44v3, syndecan-2, and syndecan-4 proteoglycans expressed on human activated CD4+ t cells affecting tumor necrosis factor alpha and interleukin 2 production. J. Biol. Chem. 2011, 286, 19541-19548.
    • (2011) J. Biol. Chem. , vol.286 , pp. 19541-19548
    • De Francesco, M.A.1    Baronio, M.2    Poiesi, C.3
  • 203
    • 38949104363 scopus 로고    scopus 로고
    • HIV-1 p17 binds heparan sulfate proteoglycans to activated cd4(+) t cells
    • Poiesi, C.; De Francesco, M.A.; Baronio, M.; Manca, N. HIV-1 p17 binds heparan sulfate proteoglycans to activated cd4(+) t cells. Virus Res. 2008, 132, 25-32.
    • (2008) Virus Res. , vol.132 , pp. 25-32
    • Poiesi, C.1    De Francesco, M.A.2    Baronio, M.3    Manca, N.4
  • 204
    • 0036484836 scopus 로고    scopus 로고
    • In vivo activation of jak2/stat-3 pathway during angiogenesis induced by gm-csf
    • Valdembri, D.; Serini, G.; Vacca, A.; Ribatti, D.; Bussolino, F. In vivo activation of jak2/stat-3 pathway during angiogenesis induced by gm-csf. FASEB J. 2002, 16, 225-227.
    • (2002) FASEB J. , vol.16 , pp. 225-227
    • Valdembri, D.1    Serini, G.2    Vacca, A.3    Ribatti, D.4    Bussolino, F.5
  • 205
    • 0033615689 scopus 로고    scopus 로고
    • Acidic ph modulates the interaction between human granulocyte-macrophage colony-stimulating factor and glycosaminoglycans
    • Wettreich, A.; Sebollela, A.; Carvalho, M.A.; Azevedo, S.P.; Borojevic, R.; Ferreira, S.T.; Coelho-Sampaio, T. Acidic ph modulates the interaction between human granulocyte-macrophage colony-stimulating factor and glycosaminoglycans. J. Biol. Chem. 1999, 274, 31468-31475.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31468-31475
    • Wettreich, A.1    Sebollela, A.2    Carvalho, M.A.3    Azevedo, S.P.4    Borojevic, R.5    Ferreira, S.T.6    Coelho-Sampaio, T.7
  • 206
    • 0026340085 scopus 로고
    • On the binding of tumor necrosis factor (tnf) to heparin and the release in vivo of the tnf-binding protein i by heparin
    • Lantz, M.; Thysell, H.; Nilsson, E.; Olsson, I. On the binding of tumor necrosis factor (tnf) to heparin and the release in vivo of the tnf-binding protein i by heparin. J. Clin. Investig. 1991, 88, 2026-2031.
    • (1991) J. Clin. Investig. , vol.88 , pp. 2026-2031
    • Lantz, M.1    Thysell, H.2    Nilsson, E.3    Olsson, I.4
  • 207
    • 0037163862 scopus 로고    scopus 로고
    • Tumour necrosis factor-alpha interacts with biglycan and decorin
    • Tufvesson, E.; Westergren-Thorsson, G. Tumour necrosis factor-alpha interacts with biglycan and decorin. FEBS Lett. 2002, 530, 124-128.
    • (2002) FEBS Lett. , vol.530 , pp. 124-128
    • Tufvesson, E.1    Westergren-Thorsson, G.2
  • 208
  • 209
    • 40949156166 scopus 로고    scopus 로고
    • Distinct heparin binding sites on vegf165 and its receptors revealed by their interaction with a non sulfated glycoaminoglycan (napac)
    • Di Benedetto, M.; Starzec, A.; Vassy, R.; Perret, G.Y.; Crepin, M. Distinct heparin binding sites on vegf165 and its receptors revealed by their interaction with a non sulfated glycoaminoglycan (napac). Biochim. Biophys. Acta 2008, 1780, 723-732.
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 723-732
    • Di Benedetto, M.1    Starzec, A.2    Vassy, R.3    Perret, G.Y.4    Crepin, M.5
  • 210
    • 0033517753 scopus 로고    scopus 로고
    • The fourth immunoglobulin-like loop in the extracellular domain of flt-1, a vegf receptor, includes a major heparin-binding site
    • Park, M.; Lee, S.T. The fourth immunoglobulin-like loop in the extracellular domain of flt-1, a vegf receptor, includes a major heparin-binding site. Biochem. Biophys. Res. Commun. 1999, 264, 730-734.
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 730-734
    • Park, M.1    Lee, S.T.2
  • 212
    • 79958008007 scopus 로고    scopus 로고
    • Targeting tumor angiogenesis with tsp-1-based compounds: Rational design of antiangiogenic mimetics of endogenous inhibitors
    • Taraboletti, G.; Rusnati, M.; Ragona, L.; Colombo, G. Targeting tumor angiogenesis with tsp-1-based compounds: Rational design of antiangiogenic mimetics of endogenous inhibitors. Oncotarget 2010, 1, 662-673.
    • (2010) Oncotarget , vol.1 , pp. 662-673
    • Taraboletti, G.1    Rusnati, M.2    Ragona, L.3    Colombo, G.4
  • 213
    • 0036070105 scopus 로고    scopus 로고
    • A recombinant nh(2)-terminal heparin-binding domain of the adhesive glycoprotein, thrombospondin-1, promotes endothelial tube formation and cell survival: A possible role for syndecan-4 proteoglycan
    • Ferrari do Outeiro-Bernstein, M.A.; Nunes, S.S.; Andrade, A.C.; Alves, T.R.; Legrand, C.; Morandi, V. A recombinant nh(2)-terminal heparin-binding domain of the adhesive glycoprotein, thrombospondin-1, promotes endothelial tube formation and cell survival: A possible role for syndecan-4 proteoglycan. Matrix Biol. 2002, 21, 311-324.
    • (2002) Matrix Biol. , vol.21 , pp. 311-324
    • Ferrari Do Outeiro-Bernstein, M.A.1    Nunes, S.S.2    Andrade, A.C.3    Alves, T.R.4    Legrand, C.5    Morandi, V.6
  • 217
    • 10344262597 scopus 로고    scopus 로고
    • The chemokine system - A major regulator of angiogenesis in health and disease
    • Rosenkilde, M.M.; Schwartz, T.W. The chemokine system - A major regulator of angiogenesis in health and disease. APMIS 2004, 112, 481-495.
    • (2004) APMIS , vol.112 , pp. 481-495
    • Rosenkilde, M.M.1    Schwartz, T.W.2
  • 218
    • 0037022198 scopus 로고    scopus 로고
    • Different affinities of glycosaminoglycan oligosaccharides for monomeric and dimeric interleukin-8: A model for chemokine regulation at inflammatory sites
    • Goger, B.; Halden, Y.; Rek, A.; Mosl, R.; Pye, D.; Gallagher, J.; Kungl, A.J. Different affinities of glycosaminoglycan oligosaccharides for monomeric and dimeric interleukin-8: A model for chemokine regulation at inflammatory sites. Biochemistry 2002, 41, 1640-1646.
    • (2002) Biochemistry , vol.41 , pp. 1640-1646
    • Goger, B.1    Halden, Y.2    Rek, A.3    Mosl, R.4    Pye, D.5    Gallagher, J.6    Kungl, A.J.7
  • 220
    • 84873545229 scopus 로고    scopus 로고
    • A chemokine self-presentation mechanism involving formation of endothelial surface microstructures
    • Whittall, C.; Kehoe, O.; King, S.; Rot, A.; Patterson, A.; Middleton, J. A chemokine self-presentation mechanism involving formation of endothelial surface microstructures. J. Immunol. 2013, 190, 1725-1736.
    • (2013) J. Immunol. , vol.190 , pp. 1725-1736
    • Whittall, C.1    Kehoe, O.2    King, S.3    Rot, A.4    Patterson, A.5    Middleton, J.6
  • 222
    • 0032478616 scopus 로고    scopus 로고
    • Noncompetitive, chemokine-mediated inhibition of basic fibroblast growth factor-induced endothelial cell proliferation
    • Presta, M.; Belleri, M.; Vecchi, A.; Hesselgesser, J.; Mantovani, A.; Horuk, R. Noncompetitive, chemokine-mediated inhibition of basic fibroblast growth factor-induced endothelial cell proliferation. J. Biol. Chem. 1998, 273, 7911-7919.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7911-7919
    • Presta, M.1    Belleri, M.2    Vecchi, A.3    Hesselgesser, J.4    Mantovani, A.5    Horuk, R.6
  • 223
    • 2342551058 scopus 로고    scopus 로고
    • Cell adhesion and signaling on the fibronectin 1st type iii repeat; requisite roles for cell surface proteoglycans and integrins
    • Mercurius, K.O.; Morla, A.O. Cell adhesion and signaling on the fibronectin 1st type iii repeat; requisite roles for cell surface proteoglycans and integrins. BMC Cell Biol. 2001, 2, 18.
    • (2001) BMC Cell Biol. , vol.2 , pp. 18
    • Mercurius, K.O.1    Morla, A.O.2
  • 224
  • 225
    • 0030050626 scopus 로고    scopus 로고
    • Heparin-binding epidermal growth factor-like growth factor: P91 activation induction of plasminogen activator/inhibitor, and tubular morphogenesis in human microvascular endothelial cells
    • Ushiro, S.; Ono, M.; Izumi, H.; Kohno, K.; Taniguchi, N.; Higashiyama, S.; Kuwano, M. Heparin-binding epidermal growth factor-like growth factor: P91 activation induction of plasminogen activator/inhibitor, and tubular morphogenesis in human microvascular endothelial cells. Jpn. J. Cancer Res. Gann 1996, 87, 68-77.
    • (1996) Jpn. J. Cancer Res. Gann , vol.87 , pp. 68-77
    • Ushiro, S.1    Ono, M.2    Izumi, H.3    Kohno, K.4    Taniguchi, N.5    Higashiyama, S.6    Kuwano, M.7
  • 227
    • 80051540053 scopus 로고    scopus 로고
    • Hsulf-1 gene exhibits anticancer efficacy through negatively regulating vegfr-2 signaling in human cancers
    • Ji, W.; Yang, J.; Wang, D.; Cao, L.; Tan, W.; Qian, H.; Sun, B.; Qian, Q.; Yin, Z.; Wu, M.; et al. Hsulf-1 gene exhibits anticancer efficacy through negatively regulating vegfr-2 signaling in human cancers. PLoS ONE 2011, 6, e23274.
    • (2011) PLoS ONE , vol.6 , pp. e23274
    • Ji, W.1    Yang, J.2    Wang, D.3    Cao, L.4    Tan, W.5    Qian, H.6    Sun, B.7    Qian, Q.8    Yin, Z.9    Wu, M.10
  • 228
    • 0023193162 scopus 로고
    • Protamine sulfate inhibits mitogenic activities of the extracellular matrix and fibroblast growth factor, but potentiates that of epidermal growth factor
    • Neufeld, G.; Gospodarowicz, D. Protamine sulfate inhibits mitogenic activities of the extracellular matrix and fibroblast growth factor, but potentiates that of epidermal growth factor. J. Cell. Physiol. 1987, 132, 287-294.
    • (1987) J. Cell. Physiol. , vol.132 , pp. 287-294
    • Neufeld, G.1    Gospodarowicz, D.2
  • 229
    • 0029876408 scopus 로고    scopus 로고
    • A distinct basic fibroblast growth factor (fgf-2)/fgf receptor interaction distinguishes urokinase-type plasminogen activator induction from mitogenicity in endothelial cells
    • Rusnati, M.; Dell'Era, P.; Urbinati, C.; Tanghetti, E.; Massardi, M.L.; Nagamine, Y.; Monti, E.; Presta, M. A distinct basic fibroblast growth factor (fgf-2)/fgf receptor interaction distinguishes urokinase-type plasminogen activator induction from mitogenicity in endothelial cells. Mol. Biol. Cell 1996, 7, 369-381.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 369-381
    • Rusnati, M.1    Dell'Era, P.2    Urbinati, C.3    Tanghetti, E.4    Massardi, M.L.5    Nagamine, Y.6    Monti, E.7    Presta, M.8
  • 230
    • 0019949388 scopus 로고
    • Protamine is an inhibitor of angiogenesis
    • Taylor, S.; Folkman, J. Protamine is an inhibitor of angiogenesis. Nature 1982, 297, 307-312.
    • (1982) Nature , vol.297 , pp. 307-312
    • Taylor, S.1    Folkman, J.2
  • 232
    • 0037911627 scopus 로고    scopus 로고
    • Structural elements of kallistatin required for inhibition of angiogenesis
    • Miao, R.Q.; Chen, V.; Chao, L.; Chao, J. Structural elements of kallistatin required for inhibition of angiogenesis. Am. J. Physiol. Cell Physiol. 2003, 284, C1604-C1613.
    • (2003) Am. J. Physiol. Cell Physiol. , vol.284 , pp. C1604-C1613
    • Miao, R.Q.1    Chen, V.2    Chao, L.3    Chao, J.4
  • 233
    • 33744539889 scopus 로고    scopus 로고
    • The anti-angiogenic his/pro-rich fragment of histidine-rich glycoprotein binds to endothelial cell heparan sulfate in a Zn2+-dependent manner
    • Vanwildemeersch, M.; Olsson, A.K.; Gottfridsson, E.; Claesson-Welsh, L.; Lindahl, U.; Spillmann, D. The anti-angiogenic his/pro-rich fragment of histidine-rich glycoprotein binds to endothelial cell heparan sulfate in a Zn2+-dependent manner. J. Biol. Chem. 2006, 281, 10298-10304.
    • (2006) J. Biol. Chem. , vol.281 , pp. 10298-10304
    • Vanwildemeersch, M.1    Olsson, A.K.2    Gottfridsson, E.3    Claesson-Welsh, L.4    Lindahl, U.5    Spillmann, D.6
  • 234
    • 0029060187 scopus 로고
    • The ip-10 chemokine binds to a specific cell surface heparan sulfate site shared with platelet factor 4 and inhibits endothelial cell proliferation
    • Luster, A.D.; Greenberg, S.M.; Leder, P. The ip-10 chemokine binds to a specific cell surface heparan sulfate site shared with platelet factor 4 and inhibits endothelial cell proliferation. J. Exp. Med. 1995, 182, 219-231.
    • (1995) J. Exp. Med. , vol.182 , pp. 219-231
    • Luster, A.D.1    Greenberg, S.M.2    Leder, P.3
  • 235
    • 0030116792 scopus 로고    scopus 로고
    • Inhibitory effect of platelet factor 4 on human erythroleukemic cells is dependent on cell surface heparan sulfate
    • Maurer, A.M.; Han, Z.C.; Dhermy, D.; Briere, J. Inhibitory effect of platelet factor 4 on human erythroleukemic cells is dependent on cell surface heparan sulfate. J. Lab. Clin. Med. 1996, 127, 382-390.
    • (1996) J. Lab. Clin. Med. , vol.127 , pp. 382-390
    • Maurer, A.M.1    Han, Z.C.2    Dhermy, D.3    Briere, J.4
  • 236
    • 0037411112 scopus 로고    scopus 로고
    • Interaction of platelet factor 4 with fibroblast growth factor 2 is stabilised by heparan sulphate
    • Chadderton, N.S.; Stringer, S.E. Interaction of platelet factor 4 with fibroblast growth factor 2 is stabilised by heparan sulphate. Int. J. Biochem. Cell Biol. 2003, 35, 1052-1055.
    • (2003) Int. J. Biochem. Cell Biol. , vol.35 , pp. 1052-1055
    • Chadderton, N.S.1    Stringer, S.E.2
  • 238
    • 0031031465 scopus 로고    scopus 로고
    • Selective expression and processing of biglycan during migration of bovine aortic endothelial cells. The role of endogenous basic fibroblast growth factor
    • Kinsella, M.G.; Tsoi, C.K.; Jarvelainen, H.T.; Wight, T.N. Selective expression and processing of biglycan during migration of bovine aortic endothelial cells. The role of endogenous basic fibroblast growth factor. J. Biol. Chem. 1997, 272, 318-325.
    • (1997) J. Biol. Chem. , vol.272 , pp. 318-325
    • Kinsella, M.G.1    Tsoi, C.K.2    Jarvelainen, H.T.3    Wight, T.N.4
  • 239
    • 0025013701 scopus 로고
    • Extracellular matrix-resident growth factors and enzymes: Possible involvement in tumor metastasis and angiogenesis
    • Vlodavsky, I.; Korner, G.; Ishai-Michaeli, R.; Bashkin, P.; Bar-Shavit, R.; Fuks, Z. Extracellular matrix-resident growth factors and enzymes: Possible involvement in tumor metastasis and angiogenesis. Cancer Metastasis Rev. 1990, 9, 203-226.
    • (1990) Cancer Metastasis Rev. , vol.9 , pp. 203-226
    • Vlodavsky, I.1    Korner, G.2    Ishai-Michaeli, R.3    Bashkin, P.4    Bar-Shavit, R.5    Fuks, Z.6
  • 240
    • 70349326274 scopus 로고    scopus 로고
    • The repertoire of glycan determinants in the human glycome
    • Cummings, R.D. The repertoire of glycan determinants in the human glycome. Mol. BioSyst. 2009, 5, 1087-1104.
    • (2009) Mol. BioSyst. , vol.5 , pp. 1087-1104
    • Cummings, R.D.1
  • 241
    • 70350445903 scopus 로고    scopus 로고
    • Therapeutically targeting protein-glycan interactions
    • Rek, A.; Krenn, E.; Kungl, A.J. Therapeutically targeting protein-glycan interactions. Br. J. Pharmacol. 2009, 157, 686-694.
    • (2009) Br. J. Pharmacol. , vol.157 , pp. 686-694
    • Rek, A.1    Krenn, E.2    Kungl, A.J.3
  • 243
    • 77955276032 scopus 로고    scopus 로고
    • Hspg-binding peptide corresponding to the exon 6a-encoded domain of vegf inhibits tumor growth by blocking angiogenesis in murine model
    • Lee, T.Y.; Folkman, J.; Javaherian, K. Hspg-binding peptide corresponding to the exon 6a-encoded domain of vegf inhibits tumor growth by blocking angiogenesis in murine model. PLoS ONE 2010, 5, e9945.
    • (2010) PLoS ONE , vol.5 , pp. e9945
    • Lee, T.Y.1    Folkman, J.2    Javaherian, K.3
  • 244
    • 36849053590 scopus 로고    scopus 로고
    • Inhibition of the mitogenic, angiogenic and tumorigenic activities of pleiotrophin by a synthetic peptide corresponding to its c-thrombospondin repeat-i domain
    • Hamma-Kourbali, Y.; Bernard-Pierrot, I.; Heroult, M.; Dalle, S.; Caruelle, D.; Milhiet, P.E.; Fernig, D.G.; Delbe, J.; Courty, J. Inhibition of the mitogenic, angiogenic and tumorigenic activities of pleiotrophin by a synthetic peptide corresponding to its c-thrombospondin repeat-i domain. J. Cell. Physiol. 2008, 214, 250-259.
    • (2008) J. Cell. Physiol. , vol.214 , pp. 250-259
    • Hamma-Kourbali, Y.1    Bernard-Pierrot, I.2    Heroult, M.3    Dalle, S.4    Caruelle, D.5    Milhiet, P.E.6    Fernig, D.G.7    Delbe, J.8    Courty, J.9
  • 245
    • 38348999283 scopus 로고    scopus 로고
    • Bovine lactoferricin inhibits basic fibroblast growth factor- and vascular endothelial growth factor165-induced angiogenesis by competing for heparin-like binding sites on endothelial cells
    • Mader, J.S.; Smyth, D.; Marshall, J.; Hoskin, D.W. Bovine lactoferricin inhibits basic fibroblast growth factor- and vascular endothelial growth factor165-induced angiogenesis by competing for heparin-like binding sites on endothelial cells. Am. J. Pathol. 2006, 169, 1753-1766.
    • (2006) Am. J. Pathol. , vol.169 , pp. 1753-1766
    • Mader, J.S.1    Smyth, D.2    Marshall, J.3    Hoskin, D.W.4
  • 246
    • 77954874525 scopus 로고    scopus 로고
    • Recombinant platelet factor 4: A therapeutic, anti-neoplastic chimera?
    • Lippi, G.; Favaloro, E.J. Recombinant platelet factor 4: A therapeutic, anti-neoplastic chimera? Semin. Thromb. Hemost. 2010, 36, 558-569.
    • (2010) Semin. Thromb. Hemost. , vol.36 , pp. 558-569
    • Lippi, G.1    Favaloro, E.J.2
  • 247
    • 84878617011 scopus 로고    scopus 로고
    • Inhibition of tumor cell migration by LD22-4, an N-terminal fragment of 24-kDa FGF2, is mediated by neuropilin 1
    • Zhang, L.; Parry, G.C.; Levin, E.G. Inhibition of tumor cell migration by LD22-4, an N-terminal fragment of 24-kDa FGF2, is mediated by neuropilin 1. Cancer Res. 2013, 73, 3316-3325.
    • (2013) Cancer Res. , vol.73 , pp. 3316-3325
    • Zhang, L.1    Parry, G.C.2    Levin, E.G.3
  • 249
    • 84863075395 scopus 로고    scopus 로고
    • Binding affinities of vascular endothelial growth factor (vegf) for heparin-derived oligosaccharides
    • Zhao, W.; McCallum, S.A.; Xiao, Z.; Zhang, F.; Linhardt, R.J. Binding affinities of vascular endothelial growth factor (vegf) for heparin-derived oligosaccharides. Biosci. Rep. 2011, 32, 71-81.
    • (2011) Biosci. Rep. , vol.32 , pp. 71-81
    • Zhao, W.1    McCallum, S.A.2    Xiao, Z.3    Zhang, F.4    Linhardt, R.J.5
  • 250
    • 84920457610 scopus 로고    scopus 로고
    • Antiangiogenic and anticancer effect of an orally active low molecular weight heparin conjugates and its application to lung cancer chemoprevention
    • Kim, J.; Al-Hilal, T.A.; Chung, S.W.; Kim, S.Y.; Ryu, G.H.; Son, W.C.; Byun, Y. Antiangiogenic and anticancer effect of an orally active low molecular weight heparin conjugates and its application to lung cancer chemoprevention. J. Control. Release 2015, 199, 122-131.
    • (2015) J. Control. Release , vol.199 , pp. 122-131
    • Kim, J.1    Al-Hilal, T.A.2    Chung, S.W.3    Kim, S.Y.4    Ryu, G.H.5    Son, W.C.6    Byun, Y.7
  • 251
    • 84922291857 scopus 로고    scopus 로고
    • Lht7, a chemically modified heparin, inhibits multiple stages of angiogenesis by blocking vegf, fgf2 and pdgf-b signaling pathways
    • Chung, S.W.; Bae, S.M.; Lee, M.; Al-Hilal, T.A.; Lee, C.K.; Kim, J.K.; Kim, I.S.; Kim, S.Y.; Byun, Y. Lht7, a chemically modified heparin, inhibits multiple stages of angiogenesis by blocking vegf, fgf2 and pdgf-b signaling pathways. Biomaterials 2014, 37C, 271-278.
    • (2014) Biomaterials , vol.37 C , pp. 271-278
    • Chung, S.W.1    Bae, S.M.2    Lee, M.3    Al-Hilal, T.A.4    Lee, C.K.5    Kim, J.K.6    Kim, I.S.7    Kim, S.Y.8    Byun, Y.9
  • 253
    • 77956418569 scopus 로고    scopus 로고
    • A small oxazine compound as an anti-tumor agent: A novel pyranoside mimetic that binds to vegf, hb-egf, and tnf-alpha
    • Basappa; Murugan, S.; Kavitha, C.V.; Purushothaman, A.; Nevin, K.G.; Sugahara, K.; Rangappa, K.S. A small oxazine compound as an anti-tumor agent: A novel pyranoside mimetic that binds to vegf, hb-egf, and tnf-alpha. Cancer Lett. 2010, 297, 231-243.
    • (2010) Cancer Lett. , vol.297 , pp. 231-243
    • Basappa1    Murugan, S.2    Kavitha, C.V.3    Purushothaman, A.4    Nevin, K.G.5    Sugahara, K.6    Rangappa, K.S.7
  • 254
    • 17844369947 scopus 로고    scopus 로고
    • Study for anti-angiogenic activities of polysaccharides isolated from antrodia cinnamomea in endothelial cells
    • Cheng, J.J.; Huang, N.K.; Chang, T.T.; Wang, D.L.; Lu, M.K. Study for anti-angiogenic activities of polysaccharides isolated from antrodia cinnamomea in endothelial cells. Life Sci. 2005, 76, 3029-3042.
    • (2005) Life Sci. , vol.76 , pp. 3029-3042
    • Cheng, J.J.1    Huang, N.K.2    Chang, T.T.3    Wang, D.L.4    Lu, M.K.5
  • 255
    • 0037437728 scopus 로고    scopus 로고
    • Oversulfation of fucoidan enhances its anti-angiogenic and antitumor activities
    • Koyanagi, S.; Tanigawa, N.; Nakagawa, H.; Soeda, S.; Shimeno, H. Oversulfation of fucoidan enhances its anti-angiogenic and antitumor activities. Biochem. Pharmacol. 2003, 65, 173-179.
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 173-179
    • Koyanagi, S.1    Tanigawa, N.2    Nakagawa, H.3    Soeda, S.4    Shimeno, H.5
  • 256
    • 0035955644 scopus 로고    scopus 로고
    • Vascular endothelial growth factor 165 (vegf(165)) activities are inhibited by carboxymethyl benzylamide dextran that competes for heparin binding to vegf(165) and vegf(165).Kdr complexes
    • Hamma-Kourbali, Y.; Vassy, R.; Starzec, A.; Le Meuth-Metzinger, V.; Oudar, O.; Bagheri-Yarmand, R.; Perret, G.; Crepin, M. Vascular endothelial growth factor 165 (vegf(165)) activities are inhibited by carboxymethyl benzylamide dextran that competes for heparin binding to vegf(165) and vegf(165).Kdr complexes. J. Biol. Chem. 2001, 276, 39748-39754.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39748-39754
    • Hamma-Kourbali, Y.1    Vassy, R.2    Starzec, A.3    Le Meuth-Metzinger, V.4    Oudar, O.5    Bagheri-Yarmand, R.6    Perret, G.7    Crepin, M.8
  • 257
    • 84862854758 scopus 로고    scopus 로고
    • Synthesis of a heparan sulfate mimetic library targeting fgf and vegf via click chemistry on a monosaccharide template
    • Liu, L.; Li, C.; Cochran, S.; Jimmink, S.; Ferro, V. Synthesis of a heparan sulfate mimetic library targeting fgf and vegf via click chemistry on a monosaccharide template. ChemMedChem 2012, 7, 1267-1275.
    • (2012) ChemMedChem , vol.7 , pp. 1267-1275
    • Liu, L.1    Li, C.2    Cochran, S.3    Jimmink, S.4    Ferro, V.5
  • 258
    • 33644804663 scopus 로고    scopus 로고
    • Discovery of a sulfated tetrapeptide that binds to vascular endothelial growth factor
    • Maynard, H.D.; Hubbell, J.A. Discovery of a sulfated tetrapeptide that binds to vascular endothelial growth factor. Acta Biomater. 2005, 1, 451-459.
    • (2005) Acta Biomater. , vol.1 , pp. 451-459
    • Maynard, H.D.1    Hubbell, J.A.2
  • 259
    • 33845995846 scopus 로고    scopus 로고
    • Low molecular weight fucoidan increases vegf165-induced endothelial cell migration by enhancing vegf165 binding to vegfr-2 and nrp1
    • Lake, A.C.; Vassy, R.; Di Benedetto, M.; Lavigne, D.; Le Visage, C.; Perret, G.Y.; Letourneur, D. Low molecular weight fucoidan increases vegf165-induced endothelial cell migration by enhancing vegf165 binding to vegfr-2 and nrp1. J. Biol. Chem. 2006, 281, 37844-37852.
    • (2006) J. Biol. Chem. , vol.281 , pp. 37844-37852
    • Lake, A.C.1    Vassy, R.2    Di Benedetto, M.3    Lavigne, D.4    Le Visage, C.5    Perret, G.Y.6    Letourneur, D.7
  • 262
    • 80054767321 scopus 로고    scopus 로고
    • Anti-proliferative effects of o-acyl-low-molecular-weight heparin derivatives on bovine pulmonary artery smooth muscle cells
    • Garg, H.G.; Mrabat, H.; Yu, L.; Hales, C.A.; Li, B.; Moore, C.N.; Zhang, F.; Linhardt, R.J. Anti-proliferative effects of o-acyl-low-molecular-weight heparin derivatives on bovine pulmonary artery smooth muscle cells. Glycoconj. J. 2011, 28, 419-426.
    • (2011) Glycoconj. J. , vol.28 , pp. 419-426
    • Garg, H.G.1    Mrabat, H.2    Yu, L.3    Hales, C.A.4    Li, B.5    Moore, C.N.6    Zhang, F.7    Linhardt, R.J.8
  • 263
    • 0035864893 scopus 로고    scopus 로고
    • Sulfated beta-(1 - >4)-galacto-oligosaccharides and their effect on angiogenesis
    • Kasbauer, C.W.; Paper, D.H.; Franz, G. Sulfated beta-(1 - >4)-galacto-oligosaccharides and their effect on angiogenesis. Carbohydr. Res. 2001, 330, 427-430.
    • (2001) Carbohydr. Res. , vol.330 , pp. 427-430
    • Kasbauer, C.W.1    Paper, D.H.2    Franz, G.3
  • 264
    • 0029779357 scopus 로고    scopus 로고
    • Sulfated malto-oligosaccharides bind to basic fgf, inhibit endothelial cell proliferation, and disrupt endothelial cell tube formation
    • Foxall, C.; Wei, Z.; Schaefer, M.E.; Casabonne, M.; Fugedi, P.; Peto, C.; Castellot, J.J., Jr.; Brandley, B.K. Sulfated malto-oligosaccharides bind to basic fgf, inhibit endothelial cell proliferation, and disrupt endothelial cell tube formation. J. Cell. Physiol. 1996, 168, 657-667.
    • (1996) J. Cell. Physiol. , vol.168 , pp. 657-667
    • Foxall, C.1    Wei, Z.2    Schaefer, M.E.3    Casabonne, M.4    Fugedi, P.5    Peto, C.6    Castellot, J.J.7    Brandley, B.K.8
  • 266
    • 0026472599 scopus 로고
    • Inhibition by pentosan polysulfate (pps) of heparin-binding growth factors released from tumor cells and blockage by pps of tumor growth in animals
    • Zugmaier, G.; Lippman, M.E.; Wellstein, A. Inhibition by pentosan polysulfate (pps) of heparin-binding growth factors released from tumor cells and blockage by pps of tumor growth in animals. J. Natl. Cancer Inst. 1992, 84, 1716-1724.
    • (1992) J. Natl. Cancer Inst. , vol.84 , pp. 1716-1724
    • Zugmaier, G.1    Lippman, M.E.2    Wellstein, A.3
  • 267
    • 19944427241 scopus 로고    scopus 로고
    • Antiangiogenic activity of semisynthetic biotechnological heparins: Low-molecular-weight-sulfated escherichia coli k5 polysaccharide derivatives as fibroblast growth factor antagonists
    • Presta, M.; Oreste, P.; Zoppetti, G.; Belleri, M.; Tanghetti, E.; Leali, D.; Urbinati, C.; Bugatti, A.; Ronca, R.; Nicoli, S.; et al. Antiangiogenic activity of semisynthetic biotechnological heparins: Low-molecular-weight-sulfated escherichia coli k5 polysaccharide derivatives as fibroblast growth factor antagonists. Arterioscler. Thromb. Vasc. Biol. 2005, 25, 71-76.
    • (2005) Arterioscler. Thromb. Vasc. Biol. , vol.25 , pp. 71-76
    • Presta, M.1    Oreste, P.2    Zoppetti, G.3    Belleri, M.4    Tanghetti, E.5    Leali, D.6    Urbinati, C.7    Bugatti, A.8    Ronca, R.9    Nicoli, S.10
  • 269
    • 0030453898 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of 2-amino-2-deoxy- and 6-amino-6-deoxy-cyclomaltoheptaose polysulfates as synergists for angiogenesis inhibition
    • Sakairi, N.; Kuzuhara, H.; Okamoto, T.; Yajima, M. Synthesis and biological evaluation of 2-amino-2-deoxy- and 6-amino-6-deoxy-cyclomaltoheptaose polysulfates as synergists for angiogenesis inhibition. Bioorg. Med. Chem. 1996, 4, 2187-2192.
    • (1996) Bioorg. Med. Chem. , vol.4 , pp. 2187-2192
    • Sakairi, N.1    Kuzuhara, H.2    Okamoto, T.3    Yajima, M.4
  • 270
    • 0029077986 scopus 로고
    • Selective inhibition of cell proliferation and DNA synthesis by the polysulphated carbohydrate l-carrageenan
    • Hoffman, R.; Burns, W.W., III; Paper, D.H. Selective inhibition of cell proliferation and DNA synthesis by the polysulphated carbohydrate l-carrageenan. Cancer Chemother. Pharmacol. 1995, 36, 325-334.
    • (1995) Cancer Chemother. Pharmacol. , vol.36 , pp. 325-334
    • Hoffman, R.1    Burns, W.W.2    Paper, D.H.3
  • 273
    • 0042695922 scopus 로고    scopus 로고
    • Studies of marine sulfated polymannuroguluronate on endothelial cell proliferation and endothelial immunity and related mechanisms
    • Wang, L.; Geng, M.; Li, J.; Guan, H.; Ding, J. Studies of marine sulfated polymannuroguluronate on endothelial cell proliferation and endothelial immunity and related mechanisms. J. Pharmacol. Sci. 2003, 92, 367-373.
    • (2003) J. Pharmacol. Sci. , vol.92 , pp. 367-373
    • Wang, L.1    Geng, M.2    Li, J.3    Guan, H.4    Ding, J.5
  • 274
    • 1842851788 scopus 로고    scopus 로고
    • Application of the four-component ugi condensation for the preparation of sulfated glycoconjugate libraries
    • Liu, L.; Ping Li, C.; Cochran, S.; Ferro, V. Application of the four-component ugi condensation for the preparation of sulfated glycoconjugate libraries. Bioorg. Med. Chem. Lett. 2004, 14, 2221-2226.
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 2221-2226
    • Liu, L.1    Ping Li, C.2    Cochran, S.3    Ferro, V.4
  • 275
    • 26944445758 scopus 로고    scopus 로고
    • An experimental and molecular-modeling study of the binding of linked sulfated tetracyclitols to fgf-1 and fgf-2
    • Cochran, S.; Li, C.P.; Bytheway, I. An experimental and molecular-modeling study of the binding of linked sulfated tetracyclitols to fgf-1 and fgf-2. ChemBioChem 2005, 6, 1882-1890.
    • (2005) ChemBioChem , vol.6 , pp. 1882-1890
    • Cochran, S.1    Li, C.P.2    Bytheway, I.3
  • 276
    • 1842530198 scopus 로고    scopus 로고
    • Characterization of growth factor-binding structures in heparin/heparan sulfate using an octasaccharide library
    • Ashikari-Hada, S.; Habuchi, H.; Kariya, Y.; Itoh, N.; Reddi, A.H.; Kimata, K. Characterization of growth factor-binding structures in heparin/heparan sulfate using an octasaccharide library. J. Biol. Chem. 2004, 279, 12346-12354.
    • (2004) J. Biol. Chem. , vol.279 , pp. 12346-12354
    • Ashikari-Hada, S.1    Habuchi, H.2    Kariya, Y.3    Itoh, N.4    Reddi, A.H.5    Kimata, K.6
  • 278
    • 0033003733 scopus 로고    scopus 로고
    • Interaction of the transactivating protein hiv-1 tat with sulphated polysaccharides
    • Watson, K.; Gooderham, N.J.; Davies, D.S.; Edwards, R.J. Interaction of the transactivating protein hiv-1 tat with sulphated polysaccharides. Biochem. Pharmacol. 1999, 57, 775-783.
    • (1999) Biochem. Pharmacol. , vol.57 , pp. 775-783
    • Watson, K.1    Gooderham, N.J.2    Davies, D.S.3    Edwards, R.J.4
  • 279
    • 34548818511 scopus 로고    scopus 로고
    • Sulfated polymannuroguluronate, a novel anti-aids drug candidate, inhibits hiv-1 tat-induced angiogenesis in kaposi's sarcoma cells
    • Lu, C.X.; Li, J.; Sun, Y.X.; Qi, X.; Wang, Q.J.; Xin, X.L.; Geng, M.Y. Sulfated polymannuroguluronate, a novel anti-aids drug candidate, inhibits hiv-1 tat-induced angiogenesis in kaposi's sarcoma cells. Biochem. Pharmacol. 2007, 74, 1330-1339.
    • (2007) Biochem. Pharmacol. , vol.74 , pp. 1330-1339
    • Lu, C.X.1    Li, J.2    Sun, Y.X.3    Qi, X.4    Wang, Q.J.5    Xin, X.L.6    Geng, M.Y.7
  • 280
    • 0036092976 scopus 로고    scopus 로고
    • Sulfated polysaccharides increase plasma levels of sdf-1 in monkeys and mice: Involvement in mobilization of stem/progenitor cells
    • Sweeney, E.A.; Lortat-Jacob, H.; Priestley, G.V.; Nakamoto, B.; Papayannopoulou, T. Sulfated polysaccharides increase plasma levels of sdf-1 in monkeys and mice: Involvement in mobilization of stem/progenitor cells. Blood 2002, 99, 44-51.
    • (2002) Blood , vol.99 , pp. 44-51
    • Sweeney, E.A.1    Lortat-Jacob, H.2    Priestley, G.V.3    Nakamoto, B.4    Papayannopoulou, T.5
  • 281
    • 16544377605 scopus 로고    scopus 로고
    • Fucoidan modulates the effect of transforming growth factor (tgf)-beta1 on fibroblast proliferation and wound repopulation in in vitro models of dermal wound repair
    • O'Leary, R.; Rerek, M.; Wood, E.J. Fucoidan modulates the effect of transforming growth factor (tgf)-beta1 on fibroblast proliferation and wound repopulation in in vitro models of dermal wound repair. Biol. Pharm. Bull. 2004, 27, 266-270.
    • (2004) Biol. Pharm. Bull. , vol.27 , pp. 266-270
    • O'Leary, R.1    Rerek, M.2    Wood, E.J.3
  • 282
    • 4644266139 scopus 로고    scopus 로고
    • Synthesis of tailor-made glycoconjugate mimetics of heparan sulfate that bind ifn-gamma in the nanomolar range
    • Lubineau, A.; Lortat-Jacob, H.; Gavard, O.; Sarrazin, S.; Bonnaffe, D. Synthesis of tailor-made glycoconjugate mimetics of heparan sulfate that bind ifn-gamma in the nanomolar range. Chemistry 2004, 10, 4265-4282.
    • (2004) Chemistry , vol.10 , pp. 4265-4282
    • Lubineau, A.1    Lortat-Jacob, H.2    Gavard, O.3    Sarrazin, S.4    Bonnaffe, D.5
  • 283
    • 84876689693 scopus 로고    scopus 로고
    • Antitumor efficacy of the heparanase inhibitor sst0001 alone and in combination with antiangiogenic agents in the treatment of human pediatric sarcoma models
    • Cassinelli, G.; Lanzi, C.; Tortoreto, M.; Cominetti, D.; Petrangolini, G.; Favini, E.; Zaffaroni, N.; Pisano, C.; Penco, S.; Vlodavsky, I.; et al. Antitumor efficacy of the heparanase inhibitor sst0001 alone and in combination with antiangiogenic agents in the treatment of human pediatric sarcoma models. Biochem. Pharmacol. 2013, 85, 1424-1432.
    • (2013) Biochem. Pharmacol. , vol.85 , pp. 1424-1432
    • Cassinelli, G.1    Lanzi, C.2    Tortoreto, M.3    Cominetti, D.4    Petrangolini, G.5    Favini, E.6    Zaffaroni, N.7    Pisano, C.8    Penco, S.9    Vlodavsky, I.10
  • 284
    • 0030198685 scopus 로고    scopus 로고
    • Suramin is a potent inhibitor of vascular endothelial growth factor. A contribution to the molecular basis of its antiangiogenic action
    • Waltenberger, J.; Mayr, U.; Frank, H.; Hombach, V. Suramin is a potent inhibitor of vascular endothelial growth factor. A contribution to the molecular basis of its antiangiogenic action. J. Mol. Cell. Cardiol. 1996, 28, 1523-1529.
    • (1996) J. Mol. Cell. Cardiol. , vol.28 , pp. 1523-1529
    • Waltenberger, J.1    Mayr, U.2    Frank, H.3    Hombach, V.4
  • 285
    • 0028318791 scopus 로고
    • Suramin, an anticancer and angiosuppressive agent, inhibits endothelial cell binding of basic fibroblast growth factor, migration, proliferation, and induction of urokinase-type plasminogen activator
    • Takano, S.; Gately, S.; Neville, M.E.; Herblin, W.F.; Gross, J.L.; Engelhard, H.; Perricone, M.; Eidsvoog, K.; Brem, S. Suramin, an anticancer and angiosuppressive agent, inhibits endothelial cell binding of basic fibroblast growth factor, migration, proliferation, and induction of urokinase-type plasminogen activator. Cancer Res. 1994, 54, 2654-2660.
    • (1994) Cancer Res. , vol.54 , pp. 2654-2660
    • Takano, S.1    Gately, S.2    Neville, M.E.3    Herblin, W.F.4    Gross, J.L.5    Engelhard, H.6    Perricone, M.7    Eidsvoog, K.8    Brem, S.9
  • 286
    • 0037457306 scopus 로고    scopus 로고
    • Inhibition of heparanase activity and heparanase-induced angiogenesis by suramin analogues
    • Marchetti, D.; Reiland, J.; Erwin, B.; Roy, M. Inhibition of heparanase activity and heparanase-induced angiogenesis by suramin analogues. Int. J. Cancer 2003, 104, 167-174.
    • (2003) Int. J. Cancer , vol.104 , pp. 167-174
    • Marchetti, D.1    Reiland, J.2    Erwin, B.3    Roy, M.4
  • 288
    • 84862235777 scopus 로고    scopus 로고
    • Discovery of novel sulfonated small molecules that inhibit vascular tube formation
    • Raman, K.; Karuturi, R.; Swarup, V.P.; Desai, U.R.; Kuberan, B. Discovery of novel sulfonated small molecules that inhibit vascular tube formation. Bioorg. Med. Chem. Lett. 2012, 22, 4467-4470.
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , pp. 4467-4470
    • Raman, K.1    Karuturi, R.2    Swarup, V.P.3    Desai, U.R.4    Kuberan, B.5
  • 289
    • 70449389897 scopus 로고    scopus 로고
    • Polysulfated/sulfonated compounds for the development of drugs at the crossroad of viral infection and oncogenesis
    • Rusnati, M.; Urbinati, C. Polysulfated/sulfonated compounds for the development of drugs at the crossroad of viral infection and oncogenesis. Curr. Pharm. Des. 2009, 15, 2946-2957.
    • (2009) Curr. Pharm. Des. , vol.15 , pp. 2946-2957
    • Rusnati, M.1    Urbinati, C.2
  • 290
    • 56349167518 scopus 로고    scopus 로고
    • Polyanionic drugs and viral oncogenesis: A novel approach to control infection, tumor-associated inflammation and angiogenesis
    • Urbinati, C.; Chiodelli, P.; Rusnati, M. Polyanionic drugs and viral oncogenesis: A novel approach to control infection, tumor-associated inflammation and angiogenesis. Molecules 2008, 13, 2758-2785.
    • (2008) Molecules , vol.13 , pp. 2758-2785
    • Urbinati, C.1    Chiodelli, P.2    Rusnati, M.3
  • 291
    • 84893358163 scopus 로고    scopus 로고
    • Emerging sulfated flavonoids and other polyphenols as drugs: Nature as an inspiration
    • Correia-da-Silva, M.; Sousa, E.; Pinto, M.M. Emerging sulfated flavonoids and other polyphenols as drugs: Nature as an inspiration. Med. Res. Rev. 2014, 34, 223-279.
    • (2014) Med. Res. Rev. , vol.34 , pp. 223-279
    • Correia-da-Silva, M.1    Sousa, E.2    Pinto, M.M.3
  • 292
    • 34447277610 scopus 로고    scopus 로고
    • Heparin-mimicking sulfonic acid polymers as multitarget inhibitors of human immunodeficiency virus type 1 tat and gp120 proteins
    • Bugatti, A.; Urbinati, C.; Ravelli, C.; De Clercq, E.; Liekens, S.; Rusnati, M. Heparin-mimicking sulfonic acid polymers as multitarget inhibitors of human immunodeficiency virus type 1 tat and gp120 proteins. Antimicrob. Agents Chemother. 2007, 51, 2337-2345.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 2337-2345
    • Bugatti, A.1    Urbinati, C.2    Ravelli, C.3    De Clercq, E.4    Liekens, S.5    Rusnati, M.6
  • 293
    • 0033061257 scopus 로고    scopus 로고
    • Modulation of fibroblast growth factor-2 receptor binding, signaling, and mitogenic activity by heparin-mimicking polysulfonated compounds
    • Liekens, S.; Leali, D.; Neyts, J.; Esnouf, R.; Rusnati, M.; Dell'Era, P.; Maudgal, P.C.; de Clercq, E.; Presta, M. Modulation of fibroblast growth factor-2 receptor binding, signaling, and mitogenic activity by heparin-mimicking polysulfonated compounds. Mol. Pharmacol. 1999, 56, 204-213.
    • (1999) Mol. Pharmacol. , vol.56 , pp. 204-213
    • Liekens, S.1    Leali, D.2    Neyts, J.3    Esnouf, R.4    Rusnati, M.5    Dell'Era, P.6    Maudgal, P.C.7    De Clercq, E.8    Presta, M.9
  • 294
    • 69749127705 scopus 로고    scopus 로고
    • Compositional analysis of heparin/heparan sulfate interacting with fibroblast growth factor. Fibroblast growth factor receptor complexes
    • Zhang, F.; Zhang, Z.; Lin, X.; Beenken, A.; Eliseenkova, A.V.; Mohammadi, M.; Linhardt, R.J. Compositional analysis of heparin/heparan sulfate interacting with fibroblast growth factor. Fibroblast growth factor receptor complexes. Biochemistry 2009, 48, 8379-8386.
    • (2009) Biochemistry , vol.48 , pp. 8379-8386
    • Zhang, F.1    Zhang, Z.2    Lin, X.3    Beenken, A.4    Eliseenkova, A.V.5    Mohammadi, M.6    Linhardt, R.J.7
  • 295
    • 29744433264 scopus 로고    scopus 로고
    • Synthesis, biological activity, and preliminary pharmacokinetic evaluation of analogues of a phosphosulfomannan angiogenesis inhibitor (pi-88)
    • Karoli, T.; Liu, L.; Fairweather, J.K.; Hammond, E.; Li, C.P.; Cochran, S.; Bergefall, K.; Trybala, E.; Addison, R.S.; Ferro, V. Synthesis, biological activity, and preliminary pharmacokinetic evaluation of analogues of a phosphosulfomannan angiogenesis inhibitor (pi-88). J. Med. Chem. 2005, 48, 8229-8236.
    • (2005) J. Med. Chem. , vol.48 , pp. 8229-8236
    • Karoli, T.1    Liu, L.2    Fairweather, J.K.3    Hammond, E.4    Li, C.P.5    Cochran, S.6    Bergefall, K.7    Trybala, E.8    Addison, R.S.9    Ferro, V.10
  • 296
    • 56849098340 scopus 로고    scopus 로고
    • The marine-derived oligosaccharide sulfate (mdos), a novel multiple tyrosine kinase inhibitor, combats tumor angiogenesis both in vitro and in vivo
    • Ma, J.; Xin, X.; Meng, L.; Tong, L.; Lin, L.; Geng, M.; Ding, J. The marine-derived oligosaccharide sulfate (mdos), a novel multiple tyrosine kinase inhibitor, combats tumor angiogenesis both in vitro and in vivo. PLoS ONE 2008, 3, e3774.
    • (2008) PLoS ONE , vol.3 , pp. e3774
    • Ma, J.1    Xin, X.2    Meng, L.3    Tong, L.4    Lin, L.5    Geng, M.6    Ding, J.7
  • 297
    • 0842264049 scopus 로고    scopus 로고
    • Antiangiogenic antithrombin down-regulates the expression of the proangiogenic heparan sulfate proteoglycan, perlecan, in endothelial cells
    • Zhang, W.; Chuang, Y.J.; Swanson, R.; Li, J.; Seo, K.; Leung, L.; Lau, L.F.; Olson, S.T. Antiangiogenic antithrombin down-regulates the expression of the proangiogenic heparan sulfate proteoglycan, perlecan, in endothelial cells. Blood 2004, 103, 1185-1191.
    • (2004) Blood , vol.103 , pp. 1185-1191
    • Zhang, W.1    Chuang, Y.J.2    Swanson, R.3    Li, J.4    Seo, K.5    Leung, L.6    Lau, L.F.7    Olson, S.T.8
  • 298
    • 0030945178 scopus 로고    scopus 로고
    • Suppression of autocrine and paracrine functions of basic fibroblast growth factor by stable expression of perlecan antisense cdna
    • Aviezer, D.; Iozzo, R.V.; Noonan, D.M.; Yayon, A. Suppression of autocrine and paracrine functions of basic fibroblast growth factor by stable expression of perlecan antisense cdna. Mol. Cell. Biol. 1997, 17, 1938-1946.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1938-1946
    • Aviezer, D.1    Iozzo, R.V.2    Noonan, D.M.3    Yayon, A.4
  • 301
    • 24744454378 scopus 로고    scopus 로고
    • Heparin regulates vascular endothelial growth factor165-dependent mitogenic activity, tube formation, and its receptor phosphorylation of human endothelial cells. Comparison of the effects of heparin and modified heparins
    • Ashikari-Hada, S.; Habuchi, H.; Kariya, Y.; Kimata, K. Heparin regulates vascular endothelial growth factor165-dependent mitogenic activity, tube formation, and its receptor phosphorylation of human endothelial cells. Comparison of the effects of heparin and modified heparins. J. Biol. Chem. 2005, 280, 31508-31515.
    • (2005) J. Biol. Chem. , vol.280 , pp. 31508-31515
    • Ashikari-Hada, S.1    Habuchi, H.2    Kariya, Y.3    Kimata, K.4
  • 302
    • 0026591876 scopus 로고
    • Basic fibroblast growth factor is internalized through both receptor-mediated and heparan sulfate-mediated mechanisms
    • Roghani, M.; Moscatelli, D. Basic fibroblast growth factor is internalized through both receptor-mediated and heparan sulfate-mediated mechanisms. J. Biol. Chem. 1992, 267, 22156-22162.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22156-22162
    • Roghani, M.1    Moscatelli, D.2
  • 303
    • 0029926101 scopus 로고    scopus 로고
    • Sulfate moieties in the subendothelial extracellular matrix are involved in basic fibroblast growth factor sequestration, dimerization, and stimulation of cell proliferation
    • Miao, H.Q.; Ishai-Michaeli, R.; Atzmon, R.; Peretz, T.; Vlodavsky, I. Sulfate moieties in the subendothelial extracellular matrix are involved in basic fibroblast growth factor sequestration, dimerization, and stimulation of cell proliferation. J. Biol. Chem. 1996, 271, 4879-4886.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4879-4886
    • Miao, H.Q.1    Ishai-Michaeli, R.2    Atzmon, R.3    Peretz, T.4    Vlodavsky, I.5
  • 304
    • 1842737772 scopus 로고    scopus 로고
    • Qsulf1, a heparan sulfate 6-o-endosulfatase, inhibits fibroblast growth factor signaling in mesoderm induction and angiogenesis
    • Wang, S.; Ai, X.; Freeman, S.D.; Pownall, M.E.; Lu, Q.; Kessler, D.S.; Emerson, C.P., Jr. Qsulf1, a heparan sulfate 6-o-endosulfatase, inhibits fibroblast growth factor signaling in mesoderm induction and angiogenesis. Proc. Natl. Acad. Sci. USA 2004, 101, 4833-4838.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4833-4838
    • Wang, S.1    Ai, X.2    Freeman, S.D.3    Pownall, M.E.4    Lu, Q.5    Kessler, D.S.6    Emerson, C.P.7
  • 305
    • 33644657201 scopus 로고    scopus 로고
    • Hsulf-2, an extracellular endoglucosamine-6-sulfatase, selectively mobilizes heparin-bound growth factors and chemokines: Effects on vegf, fgf-1, and sdf-1
    • Uchimura, K.; Morimoto-Tomita, M.; Bistrup, A.; Li, J.; Lyon, M.; Gallagher, J.; Werb, Z.; Rosen, S.D. Hsulf-2, an extracellular endoglucosamine-6-sulfatase, selectively mobilizes heparin-bound growth factors and chemokines: Effects on vegf, fgf-1, and sdf-1. BMC Biochem. 2006, 7, 2.
    • (2006) BMC Biochem. , vol.7 , pp. 2
    • Uchimura, K.1    Morimoto-Tomita, M.2    Bistrup, A.3    Li, J.4    Lyon, M.5    Gallagher, J.6    Werb, Z.7    Rosen, S.D.8
  • 306
    • 1242342737 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans function as receptors for fibroblast growth factor-2 activation of extracellular signal-regulated kinases 1 and 2
    • Chua, C.C.; Rahimi, N.; Forsten-Williams, K.; Nugent, M.A. Heparan sulfate proteoglycans function as receptors for fibroblast growth factor-2 activation of extracellular signal-regulated kinases 1 and 2. Circ. Res. 2004, 94, 316-323.
    • (2004) Circ. Res. , vol.94 , pp. 316-323
    • Chua, C.C.1    Rahimi, N.2    Forsten-Williams, K.3    Nugent, M.A.4
  • 308
    • 8844261143 scopus 로고    scopus 로고
    • Cell surface biology mediated by low affinity multivalent protein-glycan interactions
    • Collins, B.E.; Paulson, J.C. Cell surface biology mediated by low affinity multivalent protein-glycan interactions. Curr. Opin. Chem. Biol. 2004, 8, 617-625.
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 617-625
    • Collins, B.E.1    Paulson, J.C.2
  • 309
    • 67650704885 scopus 로고    scopus 로고
    • Raman spectroscopic investigation of peptide-glycosaminoglycan interactions
    • Ishwar, A.R.; Jeong, K.J.; Panitch, A.; Akkus, O. Raman spectroscopic investigation of peptide-glycosaminoglycan interactions. Appl. Spectrosc. 2009, 63, 636-641.
    • (2009) Appl. Spectrosc. , vol.63 , pp. 636-641
    • Ishwar, A.R.1    Jeong, K.J.2    Panitch, A.3    Akkus, O.4
  • 310
    • 2342516264 scopus 로고    scopus 로고
    • Conformational requirements of suramin to target angiogenic growth factors
    • Raj, P.A.; Marcus, E.; Rein, R. Conformational requirements of suramin to target angiogenic growth factors. Angiogenesis 1998, 2, 183-199.
    • (1998) Angiogenesis , vol.2 , pp. 183-199
    • Raj, P.A.1    Marcus, E.2    Rein, R.3
  • 311
    • 84880038115 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of glycosaminoglycans: Re-creating, re-modeling and re-designing nature's longest or most complex carbohydrate chains
    • DeAngelis, P.L.; Liu, J.; Linhardt, R.J. Chemoenzymatic synthesis of glycosaminoglycans: Re-creating, re-modeling and re-designing nature's longest or most complex carbohydrate chains. Glycobiology 2013, 23, 764-777.
    • (2013) Glycobiology , vol.23 , pp. 764-777
    • DeAngelis, P.L.1    Liu, J.2    Linhardt, R.J.3
  • 312
    • 84880556130 scopus 로고    scopus 로고
    • Toward the solid-phase synthesis of heparan sulfate oligosaccharides: Evaluation of iduronic acid and idose building blocks
    • Guedes, N.; Czechura, P.; Echeverria, B.; Ruiz, A.; Michelena, O.; Martin-Lomas, M.; Reichardt, N.C. Toward the solid-phase synthesis of heparan sulfate oligosaccharides: Evaluation of iduronic acid and idose building blocks. J. Org. Chem. 2013, 78, 6911-6934.
    • (2013) J. Org. Chem. , vol.78 , pp. 6911-6934
    • Guedes, N.1    Czechura, P.2    Echeverria, B.3    Ruiz, A.4    Michelena, O.5    Martin-Lomas, M.6    Reichardt, N.C.7
  • 313
    • 15744392518 scopus 로고    scopus 로고
    • Use of sulfated linked cyclitols as heparan sulfate mimetics to probe the heparin/heparan sulfate binding specificity of proteins
    • Freeman, C.; Liu, L.; Banwell, M.G.; Brown, K.J.; Bezos, A.; Ferro, V.; Parish, C.R. Use of sulfated linked cyclitols as heparan sulfate mimetics to probe the heparin/heparan sulfate binding specificity of proteins. J. Biol. Chem. 2005, 280, 8842-8849.
    • (2005) J. Biol. Chem. , vol.280 , pp. 8842-8849
    • Freeman, C.1    Liu, L.2    Banwell, M.G.3    Brown, K.J.4    Bezos, A.5    Ferro, V.6    Parish, C.R.7
  • 315
    • 33745119433 scopus 로고    scopus 로고
    • Finding a needle in a haystack: Development of a combinatorial virtual screening approach for identifying high specificity heparin/heparan sulfate sequence(s)
    • Raghuraman, A.; Mosier, P.D.; Desai, U.R. Finding a needle in a haystack: Development of a combinatorial virtual screening approach for identifying high specificity heparin/heparan sulfate sequence(s). J. Med. Chem. 2006, 49, 3553-3562.
    • (2006) J. Med. Chem. , vol.49 , pp. 3553-3562
    • Raghuraman, A.1    Mosier, P.D.2    Desai, U.R.3
  • 317
    • 0023763085 scopus 로고
    • Activity of pentosan polysulphate and derived compounds on vascular endothelial cell proliferation and migration induced by acidic and basic fgf in vitro
    • Herbert, J.M.; Cottineau, M.; Driot, F.; Pereillo, J.M.; Maffrand, J.P. Activity of pentosan polysulphate and derived compounds on vascular endothelial cell proliferation and migration induced by acidic and basic fgf in vitro. Biochem. Pharmacol. 1988, 37, 4281-4288.
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 4281-4288
    • Herbert, J.M.1    Cottineau, M.2    Driot, F.3    Pereillo, J.M.4    Maffrand, J.P.5
  • 322
    • 0035851094 scopus 로고    scopus 로고
    • Fibroblast growth factor-2 antagonist activity and angiostatic capacity of sulfated escherichia coli k5 polysaccharide derivatives
    • Leali, D.; Belleri, M.; Urbinati, C.; Coltrini, D.; Oreste, P.; Zoppetti, G.; Ribatti, D.; Rusnati, M.; Presta, M. Fibroblast growth factor-2 antagonist activity and angiostatic capacity of sulfated escherichia coli k5 polysaccharide derivatives. J. Biol. Chem. 2001, 276, 37900-37908.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37900-37908
    • Leali, D.1    Belleri, M.2    Urbinati, C.3    Coltrini, D.4    Oreste, P.5    Zoppetti, G.6    Ribatti, D.7    Rusnati, M.8    Presta, M.9
  • 323
    • 68049098118 scopus 로고    scopus 로고
    • Sulfated k5 escherichia coli polysaccharide derivatives: A novel class of candidate antiviral microbicides
    • Rusnati, M.; Vicenzi, E.; Donalisio, M.; Oreste, P.; Landolfo, S.; Lembo, D. Sulfated k5 escherichia coli polysaccharide derivatives: A novel class of candidate antiviral microbicides. Pharmacol. Ther. 2009, 123, 310-322.
    • (2009) Pharmacol. Ther. , vol.123 , pp. 310-322
    • Rusnati, M.1    Vicenzi, E.2    Donalisio, M.3    Oreste, P.4    Landolfo, S.5    Lembo, D.6
  • 324
    • 0347379921 scopus 로고    scopus 로고
    • Sulfated derivatives of escherichia coli k5 polysaccharides as modulators of fibroblast growth factor signaling
    • Borgenstrom, M.; Jalkanen, M.; Salmivirta, M. Sulfated derivatives of escherichia coli k5 polysaccharides as modulators of fibroblast growth factor signaling. J. Biol. Chem. 2003, 278, 49882-49889.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49882-49889
    • Borgenstrom, M.1    Jalkanen, M.2    Salmivirta, M.3
  • 325
    • 33748745944 scopus 로고    scopus 로고
    • Modulatory effects of escherichia coli capsular-derived sulfaminoheparosans and heparins on tissue factor-mediated activation of platelets: Flow cytometric analysis
    • Maddineni, J.; Jeske, W.P.; Baltasar, F.; Cornelli, U.; Manoni, M.; Hoppensteadt, D.A.; Fareed, J. Modulatory effects of escherichia coli capsular-derived sulfaminoheparosans and heparins on tissue factor-mediated activation of platelets: Flow cytometric analysis. Clin. Appl. Thromb. Hemost. 2006, 12, 311-317.
    • (2006) Clin. Appl. Thromb. Hemost. , vol.12 , pp. 311-317
    • Maddineni, J.1    Jeske, W.P.2    Baltasar, F.3    Cornelli, U.4    Manoni, M.5    Hoppensteadt, D.A.6    Fareed, J.7
  • 326
    • 84861884600 scopus 로고    scopus 로고
    • Semi-synthetic heparinoids
    • Springer: Berlin Heidelberg, Germany
    • Oreste, P.; Zoppetti, G. Semi-synthetic heparinoids. In Handbook of Experimental Pharmacology; Springer: Berlin Heidelberg, Germany 2012; pp. 403-422.
    • (2012) Handbook of Experimental Pharmacology , pp. 403-422
    • Oreste, P.1    Zoppetti, G.2


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