메뉴 건너뛰기




Volumn 99, Issue 6, 2016, Pages 935-953

The sweet spot: How gags help chemokines guide migrating cells

Author keywords

Chemokine receptor; Heparan sulfate; Structure function relationships

Indexed keywords

CHEMOKINE; GLYCOSAMINOGLYCAN; HEPARIN; LIGAND;

EID: 84971441746     PISSN: 07415400     EISSN: 19383673     Source Type: Journal    
DOI: 10.1189/jlb.3MR0915-440R     Document Type: Review
Times cited : (103)

References (167)
  • 1
    • 0030778204 scopus 로고    scopus 로고
    • Effective intercellular communication distances are determined by the relative time constants for cyto/chemokine secretion and diffusion
    • Francis, K., Palsson, B. O. (1997) Effective intercellular communication distances are determined by the relative time constants for cyto/chemokine secretion and diffusion. Proc. Natl. Acad. Sci. U. S. A. 94, 12258-12262.
    • (1997) Proc. Natl. Acad. Sci. U. S. A , vol.94 , pp. 12258-12262
    • Francis, K.1    Palsson, B.O.2
  • 2
    • 0025719982 scopus 로고
    • Cytokines in context
    • Nathan, C., Sporn, M. (1991) Cytokines in context. J. Cell Biol. 113, 981-986.
    • (1991) J. Cell Biol , vol.113 , pp. 981-986
    • Nathan, C.1    Sporn, M.2
  • 3
    • 34247610845 scopus 로고    scopus 로고
    • Heparan sulphate proteoglycans fine-tune mammalian physiology
    • Bishop, J. R., Schuksz, M., Esko, J. D. (2007) Heparan sulphate proteoglycans fine-tune mammalian physiology. Nature 446, 1030-1037.
    • (2007) Nature , vol.446 , pp. 1030-1037
    • Bishop, J.R.1    Schuksz, M.2    Esko, J.D.3
  • 4
    • 84939968330 scopus 로고    scopus 로고
    • Proteoglycan form and function: A comprehensive nomenclature of proteoglycans
    • Iozzo, R. V., Schaefer, L. (2015) Proteoglycan form and function: A comprehensive nomenclature of proteoglycans. Matrix Biol. 42, 11-55.
    • (2015) Matrix Biol , vol.42 , pp. 11-55
    • Iozzo, R.V.1    Schaefer, L.2
  • 5
    • 53249151669 scopus 로고    scopus 로고
    • Biological implications of glycosaminoglycan interactions with haemopoietic cytokines
    • Coombe, D. R. (2008) Biological implications of glycosaminoglycan interactions with haemopoietic cytokines. Immunol. Cell Biol. 86, 598-607.
    • (2008) Immunol. Cell Biol , vol.86 , pp. 598-607
    • Coombe, D.R.1
  • 6
    • 70149088868 scopus 로고    scopus 로고
    • Interactions between heparan sulfate and proteins-design and functional implications
    • Lindahl, U., Li, J. P. (2009) Interactions between heparan sulfate and proteins-design and functional implications. Int. Rev. Cell Mol. Biol. 276, 105-159.
    • (2009) Int. Rev. Cell Mol. Biol , vol.276 , pp. 105-159
    • Lindahl, U.1    Li, J.P.2
  • 8
    • 84878942800 scopus 로고    scopus 로고
    • Molecular mechanisms of fibroblast growth factor signaling in physiology and pathology
    • Belov, A. A., Mohammadi, M. (2013) Molecular mechanisms of fibroblast growth factor signaling in physiology and pathology. Cold Spring Harb. Perspect. Biol. 5, a015958.
    • (2013) Cold Spring Harb. Perspect. Biol , vol.5
    • Belov, A.A.1    Mohammadi, M.2
  • 9
    • 77956260099 scopus 로고    scopus 로고
    • Heparan sulfate domain organization and sulfation modulate FGFinduced cell signaling
    • Jastrebova, N., Vanwildemeersch, M., Lindahl, U., Spillmann, D. (2010) Heparan sulfate domain organization and sulfation modulate FGFinduced cell signaling. J. Biol. Chem. 285, 26842-26851.
    • (2010) J. Biol. Chem , vol.285 , pp. 26842-26851
    • Jastrebova, N.1    Vanwildemeersch, M.2    Lindahl, U.3    Spillmann, D.4
  • 10
    • 0033658646 scopus 로고    scopus 로고
    • Regulation of FGF-1 mitogenic activity by heparan sulfate oligosaccharides is dependent on specific structural features: Differential requirements for the modulation of FGF-1 and FGF-2
    • Pye, D. A., Vivès, R. R., Hyde, P., Gallagher, J. T. (2000) Regulation of FGF-1 mitogenic activity by heparan sulfate oligosaccharides is dependent on specific structural features: differential requirements for the modulation of FGF-1 and FGF-2. Glycobiology 10, 1183-1192.
    • (2000) Glycobiology , vol.10 , pp. 1183-1192
    • Pye, D.A.1    Vivès, R.R.2    Hyde, P.3    Gallagher, J.T.4
  • 11
    • 84936110439 scopus 로고    scopus 로고
    • Chemokine-guided cell positioning in the lymph node orchestrates the generation ofadaptive immune responses
    • Lian, J., Luster, A. D. (2015) Chemokine-guided cell positioning in the lymph node orchestrates the generation ofadaptive immune responses. Curr. Opin. Cell Biol. 36, 1-6.
    • (2015) Curr. Opin. Cell Biol , vol.36 , pp. 1-6
    • Lian, J.1    Luster, A.D.2
  • 12
    • 84861426163 scopus 로고    scopus 로고
    • The chemokine superfamily revisited
    • Zlotnik, A., Yoshie, O. (2012) The chemokine superfamily revisited. Immunity 36, 705-716.
    • (2012) Immunity , vol.36 , pp. 705-716
    • Zlotnik, A.1    Yoshie, O.2
  • 13
    • 0037022280 scopus 로고    scopus 로고
    • Structural diversity of heparan sulfate binding domains in chemokines
    • LortatJacob, H., Grosdidier, A., Imberty, A. (2002) Structural diversity of heparan sulfate binding domains in chemokines. Proc. Natl. Acad. Sci. U. S. A. 99, 1229-1234.
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 1229-1234
    • Lortatjacob, H.1    Grosdidier, A.2    Imberty, A.3
  • 14
    • 78649364068 scopus 로고    scopus 로고
    • Endothelial heparan sulfate controls chemokine presentation in recruitment of lymphocytes and dendritic cells to lymph nodes [published correction in Immunity (2011) 34:820]
    • Bao, X., Moseman, E. A., Saito, H., Petryniak, B., Thiriot, A., Hatakeyama, S., Ito, Y., Kawashima, H., Yamaguchi, Y., Lowe, J. B., von Andrian, U. H., Fukuda, M. (2010) Endothelial heparan sulfate controls chemokine presentation in recruitment of lymphocytes and dendritic cells to lymph nodes [published correction in Immunity (2011) 34:820]. Immunity 33, 817-829.
    • (2010) Immunity , vol.33 , pp. 817-829
    • Bao, X.1    Moseman, E.A.2    Saito, H.3    Petryniak, B.4    Thiriot, A.5    Hatakeyama, S.6    Ito, Y.7    Kawashima, H.8    Yamaguchi, Y.9    Lowe, J.B.10    Von Andrian, U.H.11    Fukuda, M.12
  • 15
    • 77956940793 scopus 로고    scopus 로고
    • A chemotactic gradient sequestered on endothelial heparan sulfate induces directional intraluminal crawling of neutrophils
    • Massena, S., Christoffersson, G., Hjertstrom, E., Zcharia, E., Vlodavsky, I., Ausmees, N., Rolny, C., Li, J. P., Phillipson, M. (2010) A chemotactic gradient sequestered on endothelial heparan sulfate induces directional intraluminal crawling of neutrophils. Blood 116, 1924-1931.
    • (2010) Blood , vol.116 , pp. 1924-1931
    • Massena, S.1    Christoffersson, G.2    Hjertstrom, E.3    Zcharia, E.4    Vlodavsky, I.5    Ausmees, N.6    Rolny, C.7    Li, J.P.8    Phillipson, M.9
  • 19
    • 79952105330 scopus 로고    scopus 로고
    • Chemokine oligomerization and interactions with receptors and glycosaminoglycans: The role of structural dynamics in function
    • Salanga, C. L., Handel, T. M. (2011) Chemokine oligomerization and interactions with receptors and glycosaminoglycans: the role of structural dynamics in function. Exp. Cell Res. 317, 590-601.
    • (2011) Exp. Cell Res , vol.317 , pp. 590-601
    • Salanga, C.L.1    Handel, T.M.2
  • 20
    • 0022384993 scopus 로고
    • Molecular distinctions between heparan sulphate and heparin: Analysis of sulphation patterns indicates that heparan sulphate and heparin are separate families ofN-sulphated polysaccharides
    • Gallagher, J. T., Walker, A. (1985) Molecular distinctions between heparan sulphate and heparin: analysis of sulphation patterns indicates that heparan sulphate and heparin are separate families ofN-sulphated polysaccharides. Biochem. J. 230, 665-674.
    • (1985) Biochem. J , vol.230 , pp. 665-674
    • Gallagher, J.T.1    Walker, A.2
  • 21
    • 84884749301 scopus 로고    scopus 로고
    • The solution structure of heparan sulfate differs from that of heparin: Implications for function
    • Khan, S., Fung, K. W., Rodriguez, E., Patel, R., Gor, J., Mulloy, B., Perkins, S. J. (2013) The solution structure of heparan sulfate differs from that of heparin: implications for function. J. Biol. Chem. 288, 27737-27751.
    • (2013) J. Biol. Chem , vol.288 , pp. 27737-27751
    • Khan, S.1    Fung, K.W.2    Rodriguez, E.3    Patel, R.4    Gor, J.5    Mulloy, B.6    Perkins, S.J.7
  • 22
    • 84939607385 scopus 로고    scopus 로고
    • Fell-Muir lecture: Heparan sulphate and the art of cell regulation: A polymer chain conducts the protein orchestra
    • Gallagher, J. (2015) Fell-Muir lecture: heparan sulphate and the art of cell regulation: a polymer chain conducts the protein orchestra. Int. J. Exp. Pathol. 96, 203-231.
    • (2015) Int. J. Exp. Pathol , vol.96 , pp. 203-231
    • Gallagher, J.1
  • 23
    • 84896902938 scopus 로고    scopus 로고
    • Chemokines and chemokine receptors: Positioning cells for host defense and immunity
    • Grifith, J. W., Sokol, C. L., Luster, A. D. (2014) Chemokines and chemokine receptors: positioning cells for host defense and immunity. Annu. Rev. Immunol. 32, 659-702.
    • (2014) Annu. Rev. Immunol , vol.32 , pp. 659-702
    • Grifith, J.W.1    Sokol, C.L.2    Luster, A.D.3
  • 24
    • 7044269092 scopus 로고    scopus 로고
    • Chemokines: Role in inflammation and immune surveillance
    • Moser, B., Willimann, K. (2004) Chemokines: role in inflammation and immune surveillance. Ann. Rheum. Dis. 63(Suppl 2), 284-289.
    • (2004) Ann. Rheum. Dis , vol.63 , pp. 284-289
    • Moser, B.1    Willimann, K.2
  • 25
    • 84862182338 scopus 로고    scopus 로고
    • The biochemistry and biology ofthe atypical chemokine receptors
    • Graham, G. J., Locati, M., Mantovani, A., Rot, A., Thelen, M. (2012) The biochemistry and biology ofthe atypical chemokine receptors. Immunol. Lett. 145, 30-38.
    • (2012) Immunol. Lett , vol.145 , pp. 30-38
    • Graham, G.J.1    Locati, M.2    Mantovani, A.3    Rot, A.4    Thelen, M.5
  • 26
    • 84873926627 scopus 로고    scopus 로고
    • Chemokine receptor oligomerization and allostery
    • Stephens, B., Handel, T. M. (2013) Chemokine receptor oligomerization and allostery. Prog. Mol. Biol. Transl. Sci. 115, 375-420.
    • (2013) Prog. Mol. Biol. Transl. Sci , vol.115 , pp. 375-420
    • Stephens, B.1    Handel, T.M.2
  • 27
    • 0026333179 scopus 로고
    • Structure-activity relationships of interleukin-8 determined using chemically synthesized analogs. Critical role of NH2-terminal residues and evidence for uncoupling of neutrophil chemotaxis, exocytosis, and receptor binding activities
    • Clark-Lewis, I., Schumacher, C., Baggiolini, M., Moser, B. (1991) Structure-activity relationships of interleukin-8 determined using chemically synthesized analogs. Critical role of NH2-terminal residues and evidence for uncoupling of neutrophil chemotaxis, exocytosis, and receptor binding activities. J. Biol. Chem. 266, 23128-23134.
    • (1991) J. Biol. Chem , vol.266 , pp. 23128-23134
    • Clark-Lewis, I.1    Schumacher, C.2    Baggiolini, M.3    Moser, B.4
  • 29
    • 84919360392 scopus 로고    scopus 로고
    • Stoichiometry and geometry of the CXC chemokine receptor 4 complex with CXC ligand 12: Molecular modeling and experimental validation
    • Kufareva, I., Stephens, B. S., Holden, L. G., Qin, L., Zhao, C., Kawamura, T., Abagyan, R., Handel, T. M. (2014) Stoichiometry and geometry of the CXC chemokine receptor 4 complex with CXC ligand 12: molecular modeling and experimental validation. Proc. Natl. Acad. Sci. U.S.A. 111, E5363-E5372.
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111
    • Kufareva, I.1    Stephens, B.S.2    Holden, L.G.3    Qin, L.4    Zhao, C.5    Kawamura, T.6    Abagyan, R.7    Handel, T.M.8
  • 31
    • 0033081379 scopus 로고    scopus 로고
    • Structure of a CXC chemokine-receptor fragment in complex with interleukin-8
    • Skelton, N.J., Quan, C., Reilly, D., Lowman, H. (1999) Structure of a CXC chemokine-receptor fragment in complex with interleukin-8. Structure 7, 157-168.
    • (1999) Structure , vol.7 , pp. 157-168
    • Skelton, N.J.1    Quan, C.2    Reilly, D.3    Lowman, H.4
  • 35
    • 84895123623 scopus 로고    scopus 로고
    • The structural role of receptor tyrosine sulfation in chemokine recognition
    • Ludeman, J. P., Stone, M. J. (2014) The structural role of receptor tyrosine sulfation in chemokine recognition. Br. J. Pharmacol. 171, 1167-1179.
    • (2014) Br. J. Pharmacol , vol.171 , pp. 1167-1179
    • Ludeman, J.P.1    Stone, M.J.2
  • 36
    • 0032006909 scopus 로고    scopus 로고
    • Glycosaminoglycan-protein interactions: Definition of consensus sites in glycosaminoglycan binding proteins
    • Hileman, R. E., Fromm, J. R., Weiler, J. M., Linhardt, R. J. (1998) Glycosaminoglycan-protein interactions: definition of consensus sites in glycosaminoglycan binding proteins. Bioessays 20, 156-167.
    • (1998) Bioessays , vol.20 , pp. 156-167
    • Hileman, R.E.1    Fromm, J.R.2    Weiler, J.M.3    Linhardt, R.J.4
  • 37
    • 84949492234 scopus 로고    scopus 로고
    • A simple method for discovering druggable, specific glycosaminoglycan-protein systems: Elucidation of key principles from heparin/heparan sulfate-binding proteins
    • Sarkar, A., Desai, U. R. (2015) A simple method for discovering druggable, specific glycosaminoglycan-protein systems: elucidation of key principles from heparin/heparan sulfate-binding proteins. PLoS One 10, e0141127.
    • (2015) Plos One , vol.10
    • Sarkar, A.1    Desai, U.R.2
  • 38
    • 84883318589 scopus 로고    scopus 로고
    • Molecular basis of glycosaminoglycan heparin binding to the chemokine CXCL1 dimer
    • Poluri, K. M., Joseph, P. R., Sawant, K. V., Rajarathnam, K. (2013) Molecular basis of glycosaminoglycan heparin binding to the chemokine CXCL1 dimer. J. Biol. Chem. 288, 25143-25153.
    • (2013) J. Biol. Chem , vol.288 , pp. 25143-25153
    • Poluri, K.M.1    Joseph, P.R.2    Sawant, K.V.3    Rajarathnam, K.4
  • 40
    • 0029610823 scopus 로고
    • Heparin binding to platelet factor-4—an NMR and site-directed mutagenesis study: Arginine residues are crucial for binding
    • Mayo, K. H., Ilyina, E., Roongta, V., Dundas, M., Joseph, J., Lai, C. K., Maione, T., Daly, T. J. (1995) Heparin binding to platelet factor-4—an NMR and site-directed mutagenesis study: arginine residues are crucial for binding. Biochem. J. 312, 357-365.
    • (1995) Biochem. J , vol.312 , pp. 357-365
    • Mayo, K.H.1    Ilyina, E.2    Roongta, V.3    Dundas, M.4    Joseph, J.5    Lai, C.K.6    Maione, T.7    Daly, T.J.8
  • 42
    • 0038608022 scopus 로고    scopus 로고
    • CXCR3 and heparin binding sites of the chemokine IP-10 (CXCL10)
    • Campanella, G. S., Lee, E. M., Sun, J., Luster, A. D. (2003) CXCR3 and heparin binding sites of the chemokine IP-10 (CXCL10). J. Biol. Chem. 278, 17066-17074.
    • (2003) J. Biol. Chem , vol.278 , pp. 17066-17074
    • Campanella, G.S.1    Lee, E.M.2    Sun, J.3    Luster, A.D.4
  • 44
    • 1842477451 scopus 로고    scopus 로고
    • Identification and characterization of a glycosaminoglycan recognition element of the C chemokine lymphotactin
    • Peterson, F. C., Elgin, E. S., Nelson, T. J., Zhang, F., Hoeger, T. J., Linhardt, R. J., Volkman, B. F. (2004) Identification and characterization of a glycosaminoglycan recognition element of the C chemokine lymphotactin. J. Biol. Chem. 279, 12598-12604.
    • (2004) J. Biol. Chem , vol.279 , pp. 12598-12604
    • Peterson, F.C.1    Elgin, E.S.2    Nelson, T.J.3    Zhang, F.4    Hoeger, T.J.5    Linhardt, R.J.6    Volkman, B.F.7
  • 46
    • 42549130865 scopus 로고    scopus 로고
    • The novel CXCL12g isoform encodes an unstructured cationic domain which regulates bioactivity and interaction with both glycosaminoglycans and CXCR4
    • Laguri, C., Sadir, R., Rueda, P., Baleux, F., Gans, P., Arenzana-Seisdedos, F., Lortat-Jacob, H. (2007) The novel CXCL12g isoform encodes an unstructured cationic domain which regulates bioactivity and interaction with both glycosaminoglycans and CXCR4. PLoS One 2, e1110.
    • (2007) Plos One , vol.2
    • Laguri, C.1    Sadir, R.2    Rueda, P.3    Baleux, F.4    Gans, P.5    Arenzana-Seisdedos, F.6    Lortat-Jacob, H.7
  • 47
    • 0035896615 scopus 로고    scopus 로고
    • Characterization of the stromal cell-derived factor-1a-heparin complex
    • Sadir, R., Baleux, F., Grosdidier, A., Imberty, A., Lortat-Jacob, H. (2001) Characterization of the stromal cell-derived factor-1a-heparin complex. J. Biol. Chem. 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
  • 48
    • 0030892080 scopus 로고    scopus 로고
    • Identification of a glycosaminoglycan-binding site in chemokine macrophage inflammatory protein-1a
    • Koopmann, W., Krangel, M. S. (1997) Identification of a glycosaminoglycan-binding site in chemokine macrophage inflammatory protein-1a. J. Biol. Chem. 272, 10103-10109.
    • (1997) J. Biol. Chem , vol.272 , pp. 10103-10109
    • Koopmann, W.1    Krangel, M.S.2
  • 49
    • 0035942317 scopus 로고    scopus 로고
    • Importance of basic residues and quaternary structure in the function of MIP-1b: CCR5 binding and cell surface sugar interactions
    • Laurence, J. S., Blanpain, C., De Leener, A., Parmentier, M., LiWang, P. J. (2001) Importance of basic residues and quaternary structure in the function of MIP-1b: CCR5 binding and cell surface sugar interactions. Biochemistry 40, 4990-4999.
    • (2001) Biochemistry , vol.40 , pp. 4990-4999
    • Laurence, J.S.1    Blanpain, C.2    De Leener, A.3    Parmentier, M.4    Liwang, P.J.5
  • 52
    • 84881503494 scopus 로고    scopus 로고
    • CCL18 exhibits a regulatory role through inhibition of receptor and glycosaminoglycan binding
    • Krohn, S. C., Bonvin, P., Proudfoot, A. E. (2013) CCL18 exhibits a regulatory role through inhibition of receptor and glycosaminoglycan binding. PLoS One 8, e72321.
    • (2013) Plos One , vol.8
    • Krohn, S.C.1    Bonvin, P.2    Proudfoot, A.E.3
  • 53
    • 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. (2004) Identification of the glycosaminoglycan binding site of the CC chemokine, MCP-1: implications for structure and function in vivo. J. Biol. Chem. 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
  • 54
    • 84901450371 scopus 로고    scopus 로고
    • Multiple glycosaminoglycan-binding epitopes of monocyte chemoattractant protein-3/CCL7 enable it to function as a non-oligomerizing chemokine
    • Salanga, C. L., Dyer, D. P., Kiselar, J. G., Gupta, S., Chance, M. R., Handel, T. M. (2014) Multiple glycosaminoglycan-binding epitopes of monocyte chemoattractant protein-3/CCL7 enable it to function as a non-oligomerizing chemokine. J. Biol. Chem. 289, 14896-14912.
    • (2014) J. Biol. Chem , vol.289 , pp. 14896-14912
    • Salanga, C.L.1    Dyer, D.P.2    Kiselar, J.G.3    Gupta, S.4    Chance, M.R.5    Handel, T.M.6
  • 55
    • 0032491615 scopus 로고    scopus 로고
    • Lysine 58 and histidine 66 at the C-terminal a-helix of monocyte chemoattractant protein-1 are essential for glycosaminoglycan binding
    • Chakravarty, L., Rogers, L., Quach, T., Breckenridge, S., Kolattukudy, P. E. (1998) Lysine 58 and histidine 66 at the C-terminal a-helix of monocyte chemoattractant protein-1 are essential for glycosaminoglycan binding. J. Biol. Chem. 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
  • 56
    • 0034725586 scopus 로고    scopus 로고
    • The crystal structure of the chemokine domain of fractalkine shows a novel quaternary arrangement
    • Hoover, D. M., Mizoue, L. S., Handel, T. M., Lubkowski, J. (2000) The crystal structure of the chemokine domain of fractalkine shows a novel quaternary arrangement. J. Biol. Chem. 275, 23187-23193.
    • (2000) J. Biol. Chem , vol.275 , pp. 23187-23193
    • Hoover, D.M.1    Mizoue, L.S.2    Handel, T.M.3    Lubkowski, J.4
  • 57
    • 84940772260 scopus 로고    scopus 로고
    • The positively charged COOH-terminal glycosaminoglycan binding CXCL9(74-103) peptide inhibits CXCL8-induced neutrophil extravasation and monosodium urate crystalinduced gout in mice
    • Vanheule, V., Janssens, R., Boff, D., Kitic, N., Berghmans, N., Ronsse, I., Kungl, A. J., Amaral, F. A., Teixeira, M. M., Van Damme, J., Proost, P., Mortier, A. (2015) The positively charged COOH-terminal glycosaminoglycan binding CXCL9(74-103) peptide inhibits CXCL8-induced neutrophil extravasation and monosodium urate crystalinduced gout in mice. J. Biol. Chem. 290, 21292-21304.
    • (2015) J. Biol. Chem , vol.290 , pp. 21292-21304
    • Vanheule, V.1    Janssens, R.2    Boff, D.3    Kitic, N.4    Berghmans, N.5    Ronsse, I.6    Kungl, A.J.7    Amaral, F.A.8    Teixeira, M.M.9    Van Damme, J.10    Proost, P.11    Mortier, A.12
  • 59
    • 0034327691 scopus 로고    scopus 로고
    • Monocyte chemotactic protein-1 receptor CCR2B is a glycoprotein that has tyrosine sulfation in a conserved extracellular N-terminal region
    • Preobrazhensky, A. A., Dragan, S., Kawano, T., Gavrilin, M. A., Gulina, I. V., Chakravarty, L., Kolattukudy, P. E. (2000) Monocyte chemotactic protein-1 receptor CCR2B is a glycoprotein that has tyrosine sulfation in a conserved extracellular N-terminal region. J. Immunol. 165, 5295-5303.
    • (2000) J. Immunol , vol.165 , pp. 5295-5303
    • Preobrazhensky, A.A.1    Dragan, S.2    Kawano, T.3    Gavrilin, M.A.4    Gulina, I.V.5    Chakravarty, L.6    Kolattukudy, P.E.7
  • 60
    • 84875988747 scopus 로고    scopus 로고
    • Tyrosine sulfation of chemokine receptor CCR2 enhances interactions with both monomeric and dimeric forms of the chemokine monocyte chemoattractant protein-1 (MCP-1)
    • Tan, J. H., Ludeman, J. P., Wedderburn, J., Canals, M., Hall, P., Butler, S. J., Taleski, D., Christopoulos, A., Hickey, M. J., Payne, R. J., Stone, M. J. (2013) Tyrosine sulfation of chemokine receptor CCR2 enhances interactions with both monomeric and dimeric forms of the chemokine monocyte chemoattractant protein-1 (MCP-1). J. Biol. Chem. 288, 10024-10034.
    • (2013) J. Biol. Chem , vol.288 , pp. 10024-10034
    • Tan, J.H.1    Ludeman, J.P.2    Wedderburn, J.3    Canals, M.4    Hall, P.5    Butler, S.J.6    Taleski, D.7    Christopoulos, A.8    Hickey, M.J.9    Payne, R.J.10    Stone, M.J.11
  • 62
    • 2442494318 scopus 로고    scopus 로고
    • Analysis of post-translational CCR8 modifications and their influence on receptor activity
    • Gutièrrez, J., Kremer, L., Zaballos, A., Goya, I., Martìnez, C., Márquez, G. (2004) Analysis of post-translational CCR8 modifications and their influence on receptor activity. J. Biol. Chem. 279, 14726-14733.
    • (2004) J. Biol. Chem , vol.279 , pp. 14726-14733
    • Gutièrrez, J.1    Kremer, L.2    Zaballos, A.3    Goya, I.4    Martìnez, C.5    Márquez, G.6
  • 63
    • 33746505443 scopus 로고    scopus 로고
    • CXCR3 requires tyrosine sulfation for ligand binding and a second extracellular loop arginine residue for ligand-induced chemotaxis
    • Colvin, R. A., Campanella, G. S., Manice, L. A., Luster, A. D. (2006) CXCR3 requires tyrosine sulfation for ligand binding and a second extracellular loop arginine residue for ligand-induced chemotaxis. Mol. Cell. Biol. 26, 5838-5849.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 5838-5849
    • Colvin, R.A.1    Campanella, G.S.2    Manice, L.A.3    Luster, A.D.4
  • 64
    • 0037119426 scopus 로고    scopus 로고
    • The role of post-translational modifications of the CXCR4 amino terminus in stromal-derived factor 1 alpha association and HIV-1 entry
    • Farzan, M., Babcock, G. J., Vasilieva, N., Wright, P. L., Kiprilov, E., Mirzabekov, T., Choe, H. (2002) The role of post-translational modifications of the CXCR4 amino terminus in stromal-derived factor 1 alpha association and HIV-1 entry. J. Biol. Chem. 277, 29484-29489.
    • (2002) J. Biol. Chem , vol.277 , pp. 29484-29489
    • Farzan, M.1    Babcock, G.J.2    Vasilieva, N.3    Wright, P.L.4    Kiprilov, E.5    Mirzabekov, T.6    Choe, H.7
  • 65
    • 0037204744 scopus 로고    scopus 로고
    • CX3CR1 tyrosine sulfation enhances fractalkine-induced cell adhesion
    • Fong, A. M., Alam, S. M., Imai, T., Haribabu, B., Patel, D. D. (2002) CX3CR1 tyrosine sulfation enhances fractalkine-induced cell adhesion. J. Biol. Chem. 277, 19418-19423.
    • (2002) J. Biol. Chem , vol.277 , pp. 19418-19423
    • Fong, A.M.1    Alam, S.M.2    Imai, T.3    Haribabu, B.4    Patel, D.D.5
  • 66
    • 20044390745 scopus 로고    scopus 로고
    • Sulphated tyrosines mediate association of chemokines and Plasmodium vivax Duffy binding protein with the Duffy antigen/receptor for chemokines (DARC). Mol
    • Choe, H., Moore, M. J., Owens, C. M., Wright, P. L., Vasilieva, N., Li, W., Singh, A. P., Shakri, R., Chitnis, C. E., Farzan, M. (2005) Sulphated tyrosines mediate association of chemokines and Plasmodium vivax Duffy binding protein with the Duffy antigen/receptor for chemokines (DARC). Mol. Microbiol. 55, 1413-1422.
    • (2005) Microbiol , vol.55 , pp. 1413-1422
    • Choe, H.1    Moore, M.J.2    Owens, C.M.3    Wright, P.L.4    Vasilieva, N.5    Li, W.6    Singh, A.P.7    Shakri, R.8    Chitnis, C.E.9    Farzan, M.10
  • 67
    • 33644804663 scopus 로고    scopus 로고
    • Discovery of a sulfated tetrapeptide that binds to vascular endothelial growth factor
    • Maynard, H. D., Hubbell, J. A. (2005) Discovery of a sulfated tetrapeptide that binds to vascular endothelial growth factor. Acta Biomater. 1, 451-459.
    • (2005) Acta Biomater , vol.1 , pp. 451-459
    • Maynard, H.D.1    Hubbell, J.A.2
  • 68
    • 84856370035 scopus 로고    scopus 로고
    • A synthetic heparan sulfate-mimetic peptide conjugated to a mini CD4 displays very high anti- HIV-1 activity independently of coreceptor usage
    • Connell, B. J., Baleux, F., Coic, Y. M., Clayette, P., Bonnaffè, D., Lortat-Jacob, H. (2012) A synthetic heparan sulfate-mimetic peptide conjugated to a mini CD4 displays very high anti- HIV-1 activity independently of coreceptor usage. Chem. Biol. 19, 131-139.
    • (2012) Chem. Biol , vol.19 , pp. 131-139
    • Connell, B.J.1    Baleux, F.2    Coic, Y.M.3    Clayette, P.4    Bonnaffè, D.5    Lortat-Jacob, H.6
  • 70
    • 77956874062 scopus 로고    scopus 로고
    • A competitive binding study of chemokine, sulfated receptor, and glycosaminoglycan interactions by nano-electrospray ionization mass spectrometry
    • Jen, C. H., Leary, J. A. (2010) A competitive binding study of chemokine, sulfated receptor, and glycosaminoglycan interactions by nano-electrospray ionization mass spectrometry. Anal. Biochem. 407, 134-140.
    • (2010) Anal. Biochem , vol.407 , pp. 134-140
    • Jen, C.H.1    Leary, J.A.2
  • 71
    • 33845767989 scopus 로고    scopus 로고
    • Recognition of RANTES by extracellular parts of the CCR5 receptor
    • Duma, L., Häussinger, D., Rogowski, M., Lusso, P., Grzesiek, S. (2007) Recognition of RANTES by extracellular parts of the CCR5 receptor. J. Mol. Biol. 365, 1063-1075.
    • (2007) J. Mol. Biol , vol.365 , pp. 1063-1075
    • Duma, L.1    Häussinger, D.2    Rogowski, M.3    Lusso, P.4    Grzesiek, S.5
  • 73
    • 0033613247 scopus 로고    scopus 로고
    • Glycosaminoglycans interact selectively with chemokines and modulate receptor binding and cellular responses
    • Kuschert, G. S., Coulin, F., Power, C. A., Proudfoot, A. E., Hubbard, R. E., Hoogewerf, A. J., Wells, T. N. (1999) Glycosaminoglycans interact selectively with chemokines and modulate receptor binding and cellular responses. Biochemistry 38, 12959-12968.
    • (1999) Biochemistry , vol.38 , pp. 12959-12968
    • Kuschert, G.S.1    Coulin, F.2    Power, C.A.3    Proudfoot, A.E.4    Hubbard, R.E.5    Hoogewerf, A.J.6    Wells, T.N.7
  • 74
    • 57049126122 scopus 로고    scopus 로고
    • Sulfated oligosaccharides (Heparin and fucoidan) binding and dimerization of stromal cell-derived factor-1 (SDF-1/CXCL 12) are coupled as evidenced by affinity CE-MS analysis
    • Fermas, S., Gonnet, F., Sutton, A., Charnaux, N., Mulloy, B., Du, Y., Baleux, F., Daniel, R. (2008) Sulfated oligosaccharides (heparin and fucoidan) binding and dimerization of stromal cell-derived factor-1 (SDF-1/CXCL 12) are coupled as evidenced by affinity CE-MS analysis. Glycobiology 18, 1054-1064.
    • (2008) Glycobiology , vol.18 , pp. 1054-1064
    • Fermas, S.1    Gonnet, F.2    Sutton, A.3    Charnaux, N.4    Mulloy, B.5    Du, Y.6    Baleux, F.7    Daniel, R.8
  • 75
    • 1542376200 scopus 로고    scopus 로고
    • A structural and dynamic model for the interaction of interleukin-8 and glycosaminoglycans: Support from isothermal fluorescence titrations
    • Krieger, E., Geretti, E., Brandner, B., Goger, B., Wells, T. N., Kungl, A. J. (2004) A structural and dynamic model for the interaction of interleukin-8 and glycosaminoglycans: support from isothermal fluorescence titrations. Proteins 54, 768-775.
    • (2004) Proteins , vol.54 , pp. 768-775
    • Krieger, E.1    Geretti, E.2    Brandner, B.3    Goger, B.4    Wells, T.N.5    Kungl, A.J.6
  • 76
    • 84880921570 scopus 로고    scopus 로고
    • Interaction of chondroitin sulfate and dermatan sulfate from various biological sources with heparin-binding growth factors and cytokines
    • Mizumoto, S., Fongmoon, D., Sugahara, K. (2013) Interaction of chondroitin sulfate and dermatan sulfate from various biological sources with heparin-binding growth factors and cytokines. Glycoconj. J. 30, 619-632.
    • (2013) Glycoconj. J , vol.30 , pp. 619-632
    • Mizumoto, S.1    Fongmoon, D.2    Sugahara, K.3
  • 77
    • 78449271616 scopus 로고    scopus 로고
    • Desorption electrospray ionization mass spectrometry of glycosaminoglycans and their protein noncovalent complex
    • Przybylski, C., Gonnet, F., Hersant, Y., Bonnaffè, D., Lortat-Jacob, H., Daniel, R. (2010) Desorption electrospray ionization mass spectrometry of glycosaminoglycans and their protein noncovalent complex. Anal. Chem. 82, 9225-9233.
    • (2010) Anal. Chem , vol.82 , pp. 9225-9233
    • Przybylski, C.1    Gonnet, F.2    Hersant, Y.3    Bonnaffè, D.4    Lortat-Jacob, H.5    Daniel, R.6
  • 78
    • 84875451109 scopus 로고    scopus 로고
    • Differentiation of CC vs CXC chemokine dimers with GAG octasaccharide binding partners: An ion mobility mass spectrometry approach
    • Seo, Y., Andaya, A., Bleiholder, C., Leary, J. A. (2013) Differentiation of CC vs CXC chemokine dimers with GAG octasaccharide binding partners: an ion mobility mass spectrometry approach. J. Am. Chem. Soc. 135, 4325-4332.
    • (2013) J. Am. Chem. Soc , vol.135 , pp. 4325-4332
    • Seo, Y.1    Aya, A.2    Bleiholder, C.3    Leary, J.A.4
  • 79
    • 84920792489 scopus 로고    scopus 로고
    • Heparin-Binding Proteins (Chemokines and Defensins) and their complexes with glycosaminoglycans from the solution NMR perspective
    • Pomin, V. H. (2014) Heparin-Binding Proteins (Chemokines and Defensins) and their complexes with glycosaminoglycans from the solution NMR perspective. Curr. Protein Pept. Sci. 15, 738-744.
    • (2014) Curr. Protein Pept. Sci , vol.15 , pp. 738-744
    • Pomin, V.H.1
  • 80
    • 0037126683 scopus 로고    scopus 로고
    • A kinetics and modeling study of RANTES(9-68) binding to heparin reveals a mechanism of cooperative oligomerization
    • Vivès, R. R., Sadir, R., Imberty, A., Rencurosi, A., Lortat-Jacob, H. (2002) A kinetics and modeling study of RANTES(9-68) binding to heparin reveals a mechanism of cooperative oligomerization. Biochemistry 41, 14779-14789.
    • (2002) Biochemistry , vol.41 , pp. 14779-14789
    • Vivès, R.R.1    Sadir, R.2    Imberty, A.3    Rencurosi, A.4    Lortat-Jacob, H.5
  • 83
    • 84905723835 scopus 로고    scopus 로고
    • Well-defined biomimetic surfaces to characterize glycosaminoglycan-mediated interactions on the molecular, supramolecular and cellular levels
    • Migliorini, E., Thakar, D., Sadir, R., Pleiner, T., Baleux, F., Lortat-Jacob, H., Coche-Guerente, L., Richter, R. P. (2014) Well-defined biomimetic surfaces to characterize glycosaminoglycan-mediated interactions on the molecular, supramolecular and cellular levels. Biomaterials 35, 8903-8915.
    • (2014) Biomaterials , vol.35 , pp. 8903-8915
    • Migliorini, E.1    Thakar, D.2    Sadir, R.3    Pleiner, T.4    Baleux, F.5    Lortat-Jacob, H.6    Coche-Guerente, L.7    Richter, R.P.8
  • 84
    • 84863207545 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry: Are we out of the quicksand
    • Iacob, R. E., Engen, J. R. (2012) Hydrogen exchange mass spectrometry: are we out of the quicksand? J. Am. Soc. Mass Spectrom. 23, 1003-1010.
    • (2012) J. Am. Soc. Mass Spectrom , vol.23 , pp. 1003-1010
    • Iacob, R.E.1    Engen, J.R.2
  • 86
    • 84930677017 scopus 로고    scopus 로고
    • Current structural biology of the heparin interactome
    • Pomin, V. H., Mulloy, B. (2015) Current structural biology of the heparin interactome. Curr. Opin. Struct. Biol. 34, 17-25.
    • (2015) Curr. Opin. Struct. Biol , vol.34 , pp. 17-25
    • Pomin, V.H.1    Mulloy, B.2
  • 87
    • 84936756671 scopus 로고    scopus 로고
    • NMR characterization of the electrostatic interaction of the basic residues in HDGF and FGF2 during heparin binding
    • Chiu, L. Y., Hung, K. W., Tjong, S. C., Chiang, Y. W., Sue, S. C. (2014) NMR characterization of the electrostatic interaction of the basic residues in HDGF and FGF2 during heparin binding. Biochim. Biophys. Acta 1844, 1851-1859.
    • (2014) Biochim. Biophys. Acta , vol.1844 , pp. 1851-1859
    • Chiu, L.Y.1    Hung, K.W.2    Tjong, S.C.3    Chiang, Y.W.4    Sue, S.C.5
  • 90
    • 0034609536 scopus 로고    scopus 로고
    • Structural diversity of N-sulfated heparan sulfate domains: Distinct modes of glucuronyl C5 epimerization, iduronic acid 2-O-sulfation, and glucosamine 6-Osulfation
    • Safaiyan, F., Lindahl, U., Salmivirta, M. (2000) Structural diversity of N-sulfated heparan sulfate domains: distinct modes of glucuronyl C5 epimerization, iduronic acid 2-O-sulfation, and glucosamine 6-Osulfation. Biochemistry 39, 10823-10830.
    • (2000) Biochemistry , vol.39 , pp. 10823-10830
    • Safaiyan, F.1    Lindahl, U.2    Salmivirta, M.3
  • 91
    • 3042690685 scopus 로고    scopus 로고
    • A new model for the domain structure of heparan sulfate based on the novel specificity of K5 lyase
    • Murphy, K. J., Merry, C. L., Lyon, M., Thompson, J. E., Roberts, I. S., Gallagher, J. T. (2004) A new model for the domain structure of heparan sulfate based on the novel specificity of K5 lyase. J. Biol. Chem. 279, 27239-27245.
    • (2004) J. Biol. Chem , vol.279 , pp. 27239-27245
    • Murphy, K.J.1    Merry, C.L.2    Lyon, M.3    Thompson, J.E.4    Roberts, I.S.5    Gallagher, J.T.6
  • 92
    • 84936883573 scopus 로고    scopus 로고
    • Molecular interactions between chondroitin-dermatan sulfate and growth factors/receptors/matrix proteins
    • Mizumoto, S., Yamada, S., Sugahara, K. (2015) Molecular interactions between chondroitin-dermatan sulfate and growth factors/receptors/matrix proteins. Curr. Opin. Struct. Biol. 34, 35-42.
    • (2015) Curr. Opin. Struct. Biol , vol.34 , pp. 35-42
    • Mizumoto, S.1    Yamada, S.2    Sugahara, K.3
  • 93
    • 5644236458 scopus 로고    scopus 로고
    • Heparan sulfate structure in mice with genetically modified heparan sulfate production
    • Ledin, J., Staatz, W., Li, J. P., Götte, M., Selleck, S., Kjellèn, L., Spillmann, D. (2004) Heparan sulfate structure in mice with genetically modified heparan sulfate production. J. Biol. Chem. 279, 42732-42741.
    • (2004) J. Biol. Chem , vol.279 , pp. 42732-42741
    • Ledin, J.1    Staatz, W.2    Li, J.P.3    Götte, M.4    Selleck, S.5    Kjellèn, L.6    Spillmann, D.7
  • 94
    • 84872523789 scopus 로고    scopus 로고
    • Age-related impairment of endothelial progenitor cell migration correlates with structural alterations of heparan sulfate proteoglycans
    • Williamson, K. A., Hamilton, A., Reynolds, J. A., Sipos, P., Crocker, I., Stringer, S. E., Alexander, Y. M. (2013) Age-related impairment of endothelial progenitor cell migration correlates with structural alterations of heparan sulfate proteoglycans. Aging Cell 12, 139-147.
    • (2013) Aging Cell , vol.12 , pp. 139-147
    • Williamson, K.A.1    Hamilton, A.2    Reynolds, J.A.3    Sipos, P.4    Crocker, I.5    Stringer, S.E.6    Alexander, Y.M.7
  • 95
    • 0032577484 scopus 로고    scopus 로고
    • Age-dependent modulation of heparan sulfate structure and function
    • Feyzi, E., Saldeen, T., Larsson, E., Lindahl, U., Salmivirta, M. (1998) Age-dependent modulation of heparan sulfate structure and function. J. Biol. Chem. 273, 13395-13398.
    • (1998) J. Biol. Chem , vol.273 , pp. 13395-13398
    • Feyzi, E.1    Saldeen, T.2    Larsson, E.3    Lindahl, U.4    Salmivirta, M.5
  • 97
    • 66449127755 scopus 로고    scopus 로고
    • Organ-specific heparan sulfate structural phenotypes
    • Shi, X., Zaia, J. (2009) Organ-specific heparan sulfate structural phenotypes. J. Biol. Chem. 284, 11806-11814.
    • (2009) J. Biol. Chem , vol.284 , pp. 11806-11814
    • Shi, X.1    Zaia, J.2
  • 98
    • 84877712933 scopus 로고    scopus 로고
    • Comparative glycomics of leukocyte glycosaminoglycans
    • Shao, C., Shi, X., White, M., Huang, Y., Hartshorn, K., Zaia, J. (2013) Comparative glycomics of leukocyte glycosaminoglycans. FEBS J. 280, 2447-2461.
    • (2013) FEBS J , vol.280 , pp. 2447-2461
    • Shao, C.1    Shi, X.2    White, M.3    Huang, Y.4    Hartshorn, K.5    Zaia, J.6
  • 101
    • 84899881420 scopus 로고    scopus 로고
    • Blood vessels pattern heparan sulfate gradients between their apical and basolateral aspects
    • Stoler-Barak, L., Moussion, C., Shezen, E., Hatzav, M., Sixt, M., Alon, R. (2014) Blood vessels pattern heparan sulfate gradients between their apical and basolateral aspects. PLoS One 9, e85699.
    • (2014) Plos One , vol.9
    • Stoler-Barak, L.1    Moussion, C.2    Shezen, E.3    Hatzav, M.4    Sixt, M.5    Alon, R.6
  • 104
    • 84873024385 scopus 로고    scopus 로고
    • Heparan sulfate biosynthesis: Regulation and variability
    • Kreuger, J., Kjellèn, L. (2012) Heparan sulfate biosynthesis: regulation and variability. J. Histochem. Cytochem. 60, 898-907.
    • (2012) J. Histochem. Cytochem , vol.60 , pp. 898-907
    • Kreuger, J.1    Kjellèn, L.2
  • 105
    • 84941053190 scopus 로고    scopus 로고
    • Profiling sulfation/epimerization pattern of full-length heparan sulfate by NMR following cell culture 13C-glucose metabolic labeling
    • Pegeot, M., Sadir, R., Eriksson, I., Kjellèn, L., Simorre, J. P., Gans, P., Lortat-Jacob, H. (2015) Profiling sulfation/epimerization pattern of full-length heparan sulfate by NMR following cell culture 13C-glucose metabolic labeling. Glycobiology 25, 151-156.
    • (2015) Glycobiology , vol.25 , pp. 151-156
    • Pegeot, M.1    Sadir, R.2    Eriksson, I.3    Kjellèn, L.4    Simorre, J.P.5    Gans, P.6    Lortat-Jacob, H.7
  • 106
    • 84928391846 scopus 로고    scopus 로고
    • C5-epimerase and 2-O-sulfotransferase associate in vitro to generate contiguous epimerized and 2-O-sulfated heparan sulfate domains
    • Prèchoux, A., Halimi, C., Simorre, J. P., Lortat-Jacob, H., Laguri, C. (2015) C5-epimerase and 2-O-sulfotransferase associate in vitro to generate contiguous epimerized and 2-O-sulfated heparan sulfate domains. ACS Chem. Biol. 10, 1064-1071.
    • (2015) ACS Chem. Biol , vol.10 , pp. 1064-1071
    • Prèchoux, A.1    Halimi, C.2    Simorre, J.P.3    Lortat-Jacob, H.4    Laguri, C.5
  • 109
    • 34548472635 scopus 로고    scopus 로고
    • CCR2 chemokines bind selectively to acetylated heparan sulfate octasaccharides
    • Schenauer, M. R., Yu, Y., Sweeney, M. D., Leary, J. A. (2007) CCR2 chemokines bind selectively to acetylated heparan sulfate octasaccharides. J. Biol. Chem. 282, 25182-25188.
    • (2007) J. Biol. Chem , vol.282 , pp. 25182-25188
    • Schenauer, M.R.1    Yu, Y.2    Sweeney, M.D.3    Leary, J.A.4
  • 111
    • 84928675605 scopus 로고    scopus 로고
    • Modular synthesis of heparin-related tetra-, hexaand octasaccharides with differential O-6 protections: Programming for regiodefined 6-O-modifications
    • Baráth, M., Hansen, S. U., Dalton, C. E., Jayson, G. C., Miller, G. J., Gardiner, J. M. (2015) Modular synthesis of heparin-related tetra-, hexaand octasaccharides with differential O-6 protections: programming for regiodefined 6-O-modifications. Molecules 20, 6167-6180.
    • (2015) Molecules , vol.20 , pp. 6167-6180
    • Baráth, M.1    Hansen, S.U.2    Dalton, C.E.3    Jayson, G.C.4    Miller, G.J.5    Gardiner, J.M.6
  • 112
    • 79951956048 scopus 로고    scopus 로고
    • Bioactive synthetic heparan sulfate and heparin derivatives: From long fragments mimetics to chimeras
    • Bonnaffè, D. (2011) Bioactive synthetic heparan sulfate and heparin derivatives: from long fragments mimetics to chimeras. C. R. Chim. 14, 59-73.
    • (2011) C. R. Chim , vol.14 , pp. 59-73
    • Bonnaffè, D.1
  • 113
    • 42449137538 scopus 로고    scopus 로고
    • Mixture synthesis and “charge tagging” based demixing: An efficient strategy for the preparation of heparan sulfate libraries
    • Dilhas, A., Lucas, R., Loureiro-Morais, L., Hersant, Y., Bonnaffè, D. (2008) Mixture synthesis and “charge tagging” based demixing: an efficient strategy for the preparation of heparan sulfate libraries. J. Comb. Chem. 10, 166-169.
    • (2008) J. Comb. Chem , vol.10 , pp. 166-169
    • Dilhas, A.1    Lucas, R.2    Loureiro-Morais, L.3    Hersant, Y.4    Bonnaffè, D.5
  • 114
    • 33846183585 scopus 로고    scopus 로고
    • Synthesis of 48 disaccharide building blocks for the assembly of a heparin and heparan sulfate oligosaccharide library
    • Lu, L. D., Shie, C. R., Kulkarni, S. S., Pan, G. R., Lu, X. A., Hung, S. C. (2006) Synthesis of 48 disaccharide building blocks for the assembly of a heparin and heparan sulfate oligosaccharide library. Org. Lett. 8, 5995-5998.
    • (2006) Org. Lett , vol.8 , pp. 5995-5998
    • Lu, L.D.1    Shie, C.R.2    Kulkarni, S.S.3    Pan, G.R.4    Lu, X.A.5    Hung, S.C.6
  • 115
    • 84890171360 scopus 로고    scopus 로고
    • Synthetic heparin and heparan sulfate oligosaccharides and their protein interactions
    • Zulueta, M. M., Lin, S. Y., Hu, Y. P., Hung, S. C. (2013) Synthetic heparin and heparan sulfate oligosaccharides and their protein interactions. Curr. Opin. Chem. Biol. 17, 1023-1029.
    • (2013) Curr. Opin. Chem. Biol , vol.17 , pp. 1023-1029
    • Zulueta, M.M.1    Lin, S.Y.2    Hu, Y.P.3    Hung, S.C.4
  • 117
    • 84890150079 scopus 로고    scopus 로고
    • Synthetic probes of glycosaminoglycan function
    • Griffin, M. E., Hsieh-Wilson, L. C. (2013) Synthetic probes of glycosaminoglycan function. Curr. Opin. Chem. Biol. 17, 1014-1022.
    • (2013) Curr. Opin. Chem. Biol , vol.17 , pp. 1014-1022
    • Griffin, M.E.1    Hsieh-Wilson, L.C.2
  • 118
    • 84918813942 scopus 로고    scopus 로고
    • Stereocontrolled preparation of biotinylated chondroitin sulfate E di-, tetra-, and hexasaccharide conjugates
    • Jacquinet, J. C., Lopin-Bon, C. (2015) Stereocontrolled preparation of biotinylated chondroitin sulfate E di-, tetra-, and hexasaccharide conjugates. Carbohydr. Res. 402, 35-43.
    • (2015) Carbohydr. Res , vol.402 , pp. 35-43
    • Jacquinet, J.C.1    Lopin-Bon, C.2
  • 119
    • 70349268369 scopus 로고    scopus 로고
    • From polymer to sizedefined oligomers: A highly divergent and stereocontrolled construction of chondroitin sulfate A, C, D, E, K, L, and M oligomers from a single precursor, part 2
    • Jacquinet, J. C., Lopin-Bon, C., Vibert, A. (2009) From polymer to sizedefined oligomers: a highly divergent and stereocontrolled construction of chondroitin sulfate A, C, D, E, K, L, and M oligomers from a single precursor, part 2. Chemistry 15, 9579-9595.
    • (2009) Chemistry , vol.15 , pp. 9579-9595
    • Jacquinet, J.C.1    Lopin-Bon, C.2    Vibert, A.3
  • 120
    • 84925180385 scopus 로고    scopus 로고
    • Synthesis of a chondroitin sulfate disaccharide library and a GAG-binding protein interaction analysis
    • Wakao, M., Obata, R., Miyachi, K., Kaitsubata, Y., Kondo, T., Sakami, C., Suda, Y. (2015) Synthesis of a chondroitin sulfate disaccharide library and a GAG-binding protein interaction analysis. Bioorg. Med. Chem. Lett. 25, 1407-1411.
    • (2015) Bioorg. Med. Chem. Lett , vol.25 , pp. 1407-1411
    • Wakao, M.1    Obata, R.2    Miyachi, K.3    Kaitsubata, Y.4    Kondo, T.5    Sakami, C.6    Suda, Y.7
  • 121
    • 84910051456 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of heparan sulfate and heparin
    • Liu, J., Linhardt, R. J. (2014) Chemoenzymatic synthesis of heparan sulfate and heparin. Nat. Prod. Rep. 31, 1676-1685.
    • (2014) Nat. Prod. Rep , vol.31 , pp. 1676-1685
    • Liu, J.1    Linhardt, R.J.2
  • 122
    • 84880572555 scopus 로고    scopus 로고
    • Use of biosynthetic enzymes in heparin and heparan sulfate synthesis
    • Chappell, E. P., Liu, J. (2013) Use of biosynthetic enzymes in heparin and heparan sulfate synthesis. Bioorg. Med. Chem. 21, 4786-4792.
    • (2013) Bioorg. Med. Chem , vol.21 , pp. 4786-4792
    • Chappell, E.P.1    Liu, J.2
  • 124
    • 83255165450 scopus 로고    scopus 로고
    • Directing the biological activities of heparan sulfate oligosaccharides using a chemoenzymatic approach
    • Xu, Y., Wang, Z., Liu, R., Bridges, A. S., Huang, X., Liu, J. (2012) Directing the biological activities of heparan sulfate oligosaccharides using a chemoenzymatic approach. Glycobiology 22, 96-106.
    • (2012) Glycobiology , vol.22 , pp. 96-106
    • Xu, Y.1    Wang, Z.2    Liu, R.3    Bridges, A.S.4    Huang, X.5    Liu, J.6
  • 126
    • 84940434871 scopus 로고    scopus 로고
    • Synthetic heparan sulfate dodecasaccharides reveal single sulfation site interconverts CXCL8 and CXCL12 chemokine biology
    • Jayson, G. C., Hansen, S. U., Miller, G. J., Cole, C. L., Rushton, G., Avizienyte, E., Gardiner, J. M. (2015) Synthetic heparan sulfate dodecasaccharides reveal single sulfation site interconverts CXCL8 and CXCL12 chemokine biology. Chem. Commun. 51, 13846-13849.
    • (2015) Chem. Commun , vol.51 , pp. 13846-13849
    • Jayson, G.C.1    Hansen, S.U.2    Miller, G.J.3    Cole, C.L.4    Rushton, G.5    Avizienyte, E.6    Gardiner, J.M.7
  • 127
    • 3042786282 scopus 로고    scopus 로고
    • Oligosaccharide microarrays to decipher the glyco code
    • Feizi, T., Chai, W. (2004) Oligosaccharide microarrays to decipher the glyco code. Nat. Rev. Mol. Cell Biol. 5, 582-588.
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 582-588
    • Feizi, T.1    Chai, W.2
  • 128
    • 0036788485 scopus 로고    scopus 로고
    • Oligosaccharide microarrays for high-throughput detection and specificity assignments of carbohydrate-protein interactions
    • Fukui, S., Feizi, T., Galustian, C., Lawson, A. M., Chai, W. (2002) Oligosaccharide microarrays for high-throughput detection and specificity assignments of carbohydrate-protein interactions. Nat. Biotechnol. 20, 1011-1017.
    • (2002) Nat. Biotechnol , vol.20 , pp. 1011-1017
    • Fukui, S.1    Feizi, T.2    Galustian, C.3    Lawson, A.M.4    Chai, W.5
  • 129
    • 42949108680 scopus 로고    scopus 로고
    • Polypyrrole oligosaccharide array and surface plasmon resonance imaging for the measurement of glycosaminoglycan binding interactions
    • Mercey, E., Sadir, R., Maillart, E., Roget, A., Baleux, F., Lortat-Jacob, H., Livache, T. (2008) Polypyrrole oligosaccharide array and surface plasmon resonance imaging for the measurement of glycosaminoglycan binding interactions. Anal. Chem. 80, 3476-3482.
    • (2008) Anal. Chem , vol.80 , pp. 3476-3482
    • Mercey, E.1    Sadir, R.2    Maillart, E.3    Roget, A.4    Baleux, F.5    Lortat-Jacob, H.6    Livache, T.7
  • 131
    • 84930384439 scopus 로고    scopus 로고
    • Interactions of the chemokine CCL5/RANTES with medium-sized chondroitin sulfate ligands
    • Deshauer, C., Morgan, A. M., Ryan, E. O., Handel, T. M., Prestegard, J. H., Wang, X. (2015) Interactions of the chemokine CCL5/RANTES with medium-sized chondroitin sulfate ligands. Structure 23, 1066-1077.
    • (2015) Structure , vol.23 , pp. 1066-1077
    • Deshauer, C.1    Morgan, A.M.2    Ryan, E.O.3    Handel, T.M.4    Prestegard, J.H.5    Wang, X.6
  • 132
    • 79959504815 scopus 로고    scopus 로고
    • 13C-labeled heparan sulfate analogue as a tool to study protein/heparan sulfate interactions by NMR spectroscopy: Application to the CXCL12a chemokine
    • Laguri, C., Sapay, N., Simorre, J. P., Brutscher, B., Imberty, A., Gans, P., Lortat-Jacob, H. (2011) 13C-labeled heparan sulfate analogue as a tool to study protein/heparan sulfate interactions by NMR spectroscopy: application to the CXCL12a chemokine. J. Am. Chem. Soc. 133, 9642-9645.
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 9642-9645
    • Laguri, C.1    Sapay, N.2    Simorre, J.P.3    Brutscher, B.4    Imberty, A.5    Gans, P.6    Lortat-Jacob, H.7
  • 133
    • 0035895930 scopus 로고    scopus 로고
    • Versican interacts with chemokines and modulates cellular responses
    • Hirose, J., Kawashima, H., Yoshie, O., Tashiro, K., Miyasaka, M. (2001) Versican interacts with chemokines and modulates cellular responses. J. Biol. Chem. 276, 5228-5234.
    • (2001) J. Biol. Chem , vol.276 , pp. 5228-5234
    • Hirose, J.1    Kawashima, H.2    Yoshie, O.3    Tashiro, K.4    Miyasaka, M.5
  • 134
    • 0037014569 scopus 로고    scopus 로고
    • Chondroitin sulfate B exerts its inhibitory effect on secondary lymphoid tissue chemokine (SLC) by binding to the C-terminus of SLC
    • Hirose, J., Kawashima, H., Swope Willis, M., Springer, T. A., Hasegawa, H., Yoshie, O., Miyasaka, M. (2002) Chondroitin sulfate B exerts its inhibitory effect on secondary lymphoid tissue chemokine (SLC) by binding to the C-terminus of SLC. Biochim. Biophys. Acta 1571, 219-224.
    • (2002) Biochim. Biophys. Acta , vol.1571 , pp. 219-224
    • Hirose, J.1    Kawashima, H.2    Swope Willis, M.3    Springer, T.A.4    Hasegawa, H.5    Yoshie, O.6    Miyasaka, M.7
  • 135
  • 136
    • 34248168879 scopus 로고    scopus 로고
    • Structural and functional basis of CXCL12 (Stromal cellderived factor-1a) binding to heparin
    • Murphy, J. W., Cho, Y., Sachpatzidis, A., Fan, C., Hodsdon, M. E., Lolis, E. (2007) Structural and functional basis of CXCL12 (stromal cellderived factor-1a) binding to heparin. J. Biol. Chem. 282, 10018-10027.
    • (2007) J. Biol. Chem , vol.282 , pp. 10018-10027
    • Murphy, J.W.1    Cho, Y.2    Sachpatzidis, A.3    Fan, C.4    Hodsdon, M.E.5    Lolis, E.6
  • 138
    • 84945917798 scopus 로고    scopus 로고
    • Solution NMR characterization of chemokine CXCL8/IL-8 monomer and dimer binding to glycosaminoglycans: Structural plasticity mediates differential binding interactions
    • Joseph, P. R., Mosier, P. D., Desai, U. R., Rajarathnam, K. (2015) Solution NMR characterization of chemokine CXCL8/IL-8 monomer and dimer binding to glycosaminoglycans: structural plasticity mediates differential binding interactions. Biochem. J. 472, 121-133.
    • (2015) Biochem. J. , vol.472 , pp. 121-133
    • Joseph, P.R.1    Mosier, P.D.2    Desai, U.R.3    Rajarathnam, K.4
  • 140
    • 84856995936 scopus 로고    scopus 로고
    • Mechanisms regulating the secretion of the promalignancy chemokine CCL5 by breast tumor cells: CCL5’s 40s loop and intracellular glycosaminoglycans
    • Soria, G., Lebel-Haziv, Y., Ehrlich, M., Meshel, T., Suez, A., Avezov, E., Rozenberg, P., Ben-Baruch, A. (2012) Mechanisms regulating the secretion of the promalignancy chemokine CCL5 by breast tumor cells: CCL5’s 40s loop and intracellular glycosaminoglycans. Neoplasia 14, 1-19.
    • (2012) Neoplasia , vol.14 , pp. 1-19
    • Soria, G.1    Lebel-Haziv, Y.2    Ehrlich, M.3    Meshel, T.4    Suez, A.5    Avezov, E.6    Rozenberg, P.7    Ben-Baruch, A.8
  • 141
    • 84928209378 scopus 로고    scopus 로고
    • Breast cancer: Coordinated regulation of CCL2 secretion by intracellular glycosaminoglycans and chemokine motifs
    • Lebel-Haziv, Y., Meshel, T., Soria, G., Yeheskel, A., Mamon, E., Ben-Baruch, A. (2014) Breast cancer: coordinated regulation of CCL2 secretion by intracellular glycosaminoglycans and chemokine motifs. Neoplasia 16, 723-740.
    • (2014) Neoplasia , vol.16 , pp. 723-740
    • Lebel-Haziv, Y.1    Meshel, T.2    Soria, G.3    Yeheskel, A.4    Mamon, E.5    Ben-Baruch, A.6
  • 142
    • 78951484487 scopus 로고    scopus 로고
    • Serglycin is a major proteoglycan in polarized human endothelial cells and is implicated in the secretion of the chemokine GROa/CXCL1
    • Meen, A. J., Øynebråten, I., Reine, T. M., Duelli, A., Svennevig, K., Pejler, G., Jenssen, T., Kolset, S. O. (2011) Serglycin is a major proteoglycan in polarized human endothelial cells and is implicated in the secretion of the chemokine GROa/CXCL1. J. Biol. Chem. 286, 2636-2647.
    • (2011) J. Biol. Chem , vol.286 , pp. 2636-2647
    • Meen, A.J.1    Øynebråten, I.2    Reine, T.M.3    Duelli, A.4    Svennevig, K.5    Pejler, G.6    Jenssen, T.7    Kolset, S.O.8
  • 143
    • 0035127893 scopus 로고    scopus 로고
    • Disaccharides derived from heparin or heparan sulfate regulate IL-8 and IL-1b secretion by intestinal epithelial cells
    • Chowers, Y., Lider, O., Schor, H., Barshack, I., Tal, R., Ariel, A., Bar-Meir, S., Cohen, I. R., Cahalon, L. (2001) Disaccharides derived from heparin or heparan sulfate regulate IL-8 and IL-1b secretion by intestinal epithelial cells. Gastroenterology 120, 449-459.
    • (2001) Gastroenterology , vol.120 , pp. 449-459
    • Chowers, Y.1    Lider, O.2    Schor, H.3    Barshack, I.4    Tal, R.5    Ariel, A.6    Bar-Meir, S.7    Cohen, I.R.8    Cahalon, L.9
  • 147
    • 79952102426 scopus 로고    scopus 로고
    • Effect of posttranslational processing on the in vitro and in vivo activity of chemokines
    • Mortier, A., Gouwy, M., Van Damme, J., Proost, P. (2011) Effect of posttranslational processing on the in vitro and in vivo activity of chemokines. Exp. Cell Res. 317, 642-654.
    • (2011) Exp. Cell Res , vol.317 , pp. 642-654
    • Mortier, A.1    Gouwy, M.2    Van Damme, J.3    Proost, P.4
  • 148
    • 84857287661 scopus 로고    scopus 로고
    • Biochemical analysis of matrix metalloproteinase activation of chemokines CCL15 and CCL23 and increased glycosaminoglycan binding of CCL16
    • Starr, A. E., Dufour, A., Maier, J., Overall, C. M. (2012) Biochemical analysis of matrix metalloproteinase activation of chemokines CCL15 and CCL23 and increased glycosaminoglycan binding of CCL16. J. Biol. Chem. 287, 5848-5860.
    • (2012) J. Biol. Chem , vol.287 , pp. 5848-5860
    • Starr, A.E.1    Dufour, A.2    Maier, J.3    Overall, C.M.4
  • 149
    • 0142254121 scopus 로고    scopus 로고
    • Regulation of the immune response by the interaction of chemokines and proteases
    • Struyf, S., Proost, P., Van Damme, J. (2003) Regulation of the immune response by the interaction of chemokines and proteases. Adv. Immunol. 81, 1-44.
    • (2003) Adv. Immunol , vol.81 , pp. 1-44
    • Struyf, S.1    Proost, P.2    Van Damme, J.3
  • 150
    • 43049107148 scopus 로고    scopus 로고
    • Proteolytic processing of chemokines: Implications in physiological and pathological conditions
    • Wolf, M., Albrecht, S., Märki, C. (2008) Proteolytic processing of chemokines: implications in physiological and pathological conditions. Int. J. Biochem. Cell Biol. 40, 1185-1198.
    • (2008) Int. J. Biochem. Cell Biol , vol.40 , pp. 1185-1198
    • Wolf, M.1    Albrecht, S.2    Märki, C.3
  • 151
    • 84930644133 scopus 로고    scopus 로고
    • Cysteine Cathepsins Activate ELR Chemokines and Inactivate Non-ELR Chemokines
    • Repnik, U., Starr, A. E., Overall, C. M., Turk, B. (2015) Cysteine Cathepsins Activate ELR Chemokines and Inactivate Non-ELR Chemokines. J. Biol. Chem. 290, 13800-13811.
    • (2015) J. Biol. Chem , vol.290 , pp. 13800-13811
    • Repnik, U.1    Starr, A.E.2    Overall, C.M.3    Turk, B.4
  • 152
    • 34447508446 scopus 로고    scopus 로고
    • Eotaxin selectively binds heparin: An interaction that protects eotaxin from proteolysis and potentiates chemotactic activity in vivo
    • Ellyard, J. I., Simson, L., Bezos, A., Johnston, K., Freeman, C., Parish, C. R. (2007) Eotaxin selectively binds heparin: an interaction that protects eotaxin from proteolysis and potentiates chemotactic activity in vivo. J. Biol. Chem. 282, 15238-15247.
    • (2007) J. Biol. Chem , vol.282 , pp. 15238-15247
    • Ellyard, J.I.1    Simson, L.2    Bezos, A.3    Johnston, K.4    Freeman, C.5    Parish, C.R.6
  • 153
    • 6344284808 scopus 로고    scopus 로고
    • Heparan sulfate/heparin oligosaccharides protect stromal cell-derived factor-1 (SDF-1)/CXCL12 against proteolysis induced by CD26/dipeptidyl peptidase IV
    • Sadir, R., Imberty, A., Baleux, F., Lortat-Jacob, H. (2004) Heparan sulfate/heparin oligosaccharides protect stromal cell-derived factor-1 (SDF-1)/CXCL12 against proteolysis induced by CD26/dipeptidyl peptidase IV. J. Biol. Chem. 279, 43854-43860.
    • (2004) J. Biol. Chem , vol.279 , pp. 43854-43860
    • Sadir, R.1    Imberty, A.2    Baleux, F.3    Lortat-Jacob, H.4
  • 155
    • 18744383614 scopus 로고    scopus 로고
    • Matrilysin shedding of syndecan-1 regulates chemokine mobilization and transepithelial efflux of neutrophils in acute lung injury
    • Li, Q., Park, P. W., Wilson, C. L., Parks, W. C. (2002) Matrilysin shedding of syndecan-1 regulates chemokine mobilization and transepithelial efflux of neutrophils in acute lung injury. Cell 111, 635-646.
    • (2002) Cell , vol.111 , pp. 635-646
    • Li, Q.1    Park, P.W.2    Wilson, C.L.3    Parks, W.C.4
  • 156
    • 84871326579 scopus 로고    scopus 로고
    • Inflammatory chemokines direct and restrict leukocyte migration within live tissues as glycan-bound gradients
    • Sarris, M., Masson, J. B., Maurin, D., Van der Aa, L. M., Boudinot, P., Lortat-Jacob, H., Herbomel, P. (2012) Inflammatory chemokines direct and restrict leukocyte migration within live tissues as glycan-bound gradients. Curr. Biol. 22, 2375-2382.
    • (2012) Curr. Biol , vol.22 , pp. 2375-2382
    • Sarris, M.1    Masson, J.B.2    Maurin, D.3    Van Der Aa, L.M.4    Boudinot, P.5    Lortat-Jacob, H.6    Herbomel, P.7
  • 158
    • 84882908901 scopus 로고    scopus 로고
    • Mechanical guidance of cell migration: Lessons from chemotaxis
    • Roca-Cusachs, P., Sunyer, R., Trepat, X. (2013) Mechanical guidance of cell migration: lessons from chemotaxis. Curr. Opin. Cell Biol. 25, 543-549.
    • (2013) Curr. Opin. Cell Biol , vol.25 , pp. 543-549
    • Roca-Cusachs, P.1    Sunyer, R.2    Trepat, X.3
  • 159
    • 84922287672 scopus 로고    scopus 로고
    • Extracellular matrix assembly: A multiscale deconstruction
    • Mouw, J. K., Ou, G., Weaver, V. M. (2014) Extracellular matrix assembly: a multiscale deconstruction. Nat. Rev. Mol. Cell Biol. 15, 771-785.
    • (2014) Nat. Rev. Mol. Cell Biol , vol.15 , pp. 771-785
    • Mouw, J.K.1    Ou, G.2    Weaver, V.M.3
  • 161
    • 70350528813 scopus 로고    scopus 로고
    • Anti-inflammatory therapy by intravenous delivery of non-heparan sulfate-binding CXCL12
    • O’Boyle, G., Mellor, P., Kirby, J. A., Ali, S. (2009) Anti-inflammatory therapy by intravenous delivery of non-heparan sulfate-binding CXCL12. FASEB J. 23, 3906-3916.
    • (2009) FASEB J , vol.23 , pp. 3906-3916
    • O’Boyle, G.1    Mellor, P.2    Kirby, J.A.3    Ali, S.4
  • 162
    • 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. (2002) Sulfated polysaccharides increase plasma levels of SDF-1 in monkeys and mice: involvement in mobilization of stem/progenitor cells. Blood 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
  • 164
    • 84879636340 scopus 로고    scopus 로고
    • Role of high endothelial venule-expressed heparan sulfate in chemokine presentation and lymphocyte homing
    • Tsuboi, K., Hirakawa, J., Seki, E., Imai, Y., Yamaguchi, Y., Fukuda, M., Kawashima, H. (2013) Role of high endothelial venule-expressed heparan sulfate in chemokine presentation and lymphocyte homing. J. Immunol. 191, 448-455.
    • (2013) J. Immunol , vol.191 , pp. 448-455
    • Tsuboi, K.1    Hirakawa, J.2    Seki, E.3    Imai, Y.4    Yamaguchi, Y.5    Fukuda, M.6    Kawashima, H.7
  • 165
    • 24944451114 scopus 로고    scopus 로고
    • Endothelial heparan sulfate deficiency impairs L-selectin- and chemokine-mediated neutrophil trafficking during inflammatory responses
    • Wang, L., Fuster, M., Sriramarao, P., Esko, J. D. (2005) Endothelial heparan sulfate deficiency impairs L-selectin- and chemokine-mediated neutrophil trafficking during inflammatory responses. Nat. Immunol. 6, 902-910.
    • (2005) Nat. Immunol , vol.6 , pp. 902-910
    • Wang, L.1    Fuster, M.2    Sriramarao, P.3    Esko, J.D.4
  • 167
    • 79955979240 scopus 로고    scopus 로고
    • Evolution of glycosaminoglycans: Comparative biochemical study
    • Yamada, S., Sugahara, K., Ozbek, S. (2011) Evolution of glycosaminoglycans: Comparative biochemical study. Commun. Integr. Biol. 4, 150-158.
    • (2011) Commun. Integr. Biol , vol.4 , pp. 150-158
    • Yamada, S.1    Sugahara, K.2    Ozbek, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.