메뉴 건너뛰기




Volumn 96, Issue 4, 2015, Pages 203-231

Fell-Muir Lecture: Heparan sulphate and the art of cell regulation: A polymer chain conducts the protein orchestra

Author keywords

Glycosaminoglycan; Heparan sulphate; Heparan sulphate heparin

Indexed keywords

ANGIOGENIC FACTOR; COLLAGEN ALPHA4V; COLLAGEN DERIVATIVE; COLLAGEN Q; COLLAGEN TYPE 1; COLLAGEN TYPE 5; COLLAGEN TYPE 9; FIBRILLIN; FIBROBLAST GROWTH FACTOR; FIBRONECTIN; HEPARAN SULFATE; INTERLEUKIN 8; MIP1 ALPHA; MORPHOGEN; NEUROPILIN; NEUROTROPHIC FACTOR; PLEIOTROPHIN; RECEPTOR; SCATTER FACTOR; SONIC HEDGEHOG PROTEIN; STROMAL CELL DERIVED FACTOR 1; STROMAL CELL DERIVED FACTOR 1ALPHA; STROMAL CELL DERIVED FACTOR 1GAMMA; THROMBOCYTE FACTOR 4; UNCLASSIFIED DRUG; VASCULOTROPIN; VASCULOTROPIN RECEPTOR;

EID: 84939607385     PISSN: 09599673     EISSN: 13652613     Source Type: Journal    
DOI: 10.1111/iep.12135     Document Type: Article
Times cited : (87)

References (231)
  • 1
    • 0041671071 scopus 로고    scopus 로고
    • Qsulf1 remodels the 6-O sulfation states of cell surface heparan sulfate proteoglycans to promote Wnt signaling
    • Ai X., Do A.T., Lozynska O., Kusche-Gullberg M., Lindahl U. & Emerson C.P. (2003) Qsulf1 remodels the 6-O sulfation states of cell surface heparan sulfate proteoglycans to promote Wnt signaling. J. Cell Biol. 162, 341-351.
    • (2003) J. Cell Biol. , vol.162 , pp. 341-351
    • Ai, X.1    Do, A.T.2    Lozynska, O.3    Kusche-Gullberg, M.4    Lindahl, U.5    Emerson, C.P.6
  • 2
    • 35548943609 scopus 로고    scopus 로고
    • SULF1 and SULF2 regulate heparan sulfate-mediated GDNF signaling for esophageal innervation
    • Ai X., Kitazawa T., Do A.T., Kusche-Gullberg M., Labosky P.A. & Emerson C.P. Jr (2007) SULF1 and SULF2 regulate heparan sulfate-mediated GDNF signaling for esophageal innervation. Development 134, 3327-3338.
    • (2007) Development , vol.134 , pp. 3327-3338
    • Ai, X.1    Kitazawa, T.2    Do, A.T.3    Kusche-Gullberg, M.4    Labosky, P.A.5    Emerson, C.P.6
  • 3
    • 34249035860 scopus 로고    scopus 로고
    • The major determinant of the heparin binding of glial cell-line-derived neurotrophic factor is near the N-terminus and is dispensable for receptor binding
    • Alfano I., Vora P., Mummery R., Mulloy B. & Rider C. (2007) The major determinant of the heparin binding of glial cell-line-derived neurotrophic factor is near the N-terminus and is dispensable for receptor binding. Biochem. J. 404, 131-140.
    • (2007) Biochem. J. , vol.404 , pp. 131-140
    • Alfano, I.1    Vora, P.2    Mummery, R.3    Mulloy, B.4    Rider, C.5
  • 4
    • 0242677706 scopus 로고    scopus 로고
    • Spatial and temporal expression of heparan sulfate in mouse development regulates FGF and FGF receptor assembly
    • Allen B.L. & Rapraeger A.C. (2003) Spatial and temporal expression of heparan sulfate in mouse development regulates FGF and FGF receptor assembly. J. Cell Biol. 163, 637-648.
    • (2003) J. Cell Biol. , vol.163 , pp. 637-648
    • Allen, B.L.1    Rapraeger, A.C.2
  • 5
    • 0035956435 scopus 로고    scopus 로고
    • Role of heparan sulfate as a tissue-specific regulator of FGF-4 and FGF receptor recognition
    • Allen B.L., Filla M.S. & Rapraeger A.C. (2003) Role of heparan sulfate as a tissue-specific regulator of FGF-4 and FGF receptor recognition. J. Cell Biol. 155, 845-858.
    • (2003) J. Cell Biol. , vol.155 , pp. 845-858
    • Allen, B.L.1    Filla, M.S.2    Rapraeger, A.C.3
  • 6
    • 70350029643 scopus 로고    scopus 로고
    • Extra-embryonic syndecan 2 regulates organ primordia migration and fibrillogenesis throughout the zebrafish embryo
    • Arrington C.B. & Yost H.J. (2009) Extra-embryonic syndecan 2 regulates organ primordia migration and fibrillogenesis throughout the zebrafish embryo. Development 136, 3143-3152.
    • (2009) Development , vol.136 , pp. 3143-3152
    • Arrington, C.B.1    Yost, H.J.2
  • 7
    • 0031561123 scopus 로고    scopus 로고
    • Identification of heparin-binding sites in midkine and their role in neurite-promotion
    • Asai T., Watanabe K., Ichihara-Tanaka K. et al. (1997) Identification of heparin-binding sites in midkine and their role in neurite-promotion. Biochem. Biophys. Res. Commun. 236, 66-70.
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 66-70
    • Asai, T.1    Watanabe, K.2    Ichihara-Tanaka, K.3
  • 8
    • 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. (2004) Characterization of growth factor-binding structures in heparin/heparan sulfate using an octasaccharide library. J. Biol. Chem. 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
  • 9
    • 24744454378 scopus 로고    scopus 로고
    • Heparin regulates VEGF165-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. (2005) Heparin regulates VEGF165-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. 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
  • 10
    • 77951896697 scopus 로고    scopus 로고
    • The long-range activity of hedgehog is regulated in the apical extracellular space by the glypican dally and the hydrolase notum
    • Ayers K.L., Gallet A., Staccini-Lavenant L. & Thérond L.P. (2010) The long-range activity of hedgehog is regulated in the apical extracellular space by the glypican dally and the hydrolase notum. Dev. Cell 18, 605-620.
    • (2010) Dev. Cell , vol.18 , pp. 605-620
    • Ayers, K.L.1    Gallet, A.2    Staccini-Lavenant, L.3    Thérond, L.P.4
  • 11
    • 0033964411 scopus 로고    scopus 로고
    • The GDNF family ligands and receptors - implications for neural development
    • Baloh R., Enomoto H., Johnson E. & Milbrandt J. (2000) The GDNF family ligands and receptors - implications for neural development. Curr. Opin. Neurobiol. 10, 103-110.
    • (2000) Curr. Opin. Neurobiol. , vol.10 , pp. 103-110
    • Baloh, R.1    Enomoto, H.2    Johnson, E.3    Milbrandt, J.4
  • 12
    • 0025900908 scopus 로고
    • Localization of the major heparin-binding site in fibronectin
    • Barkalow F.J. & Schwarzbauer J.E. (1991) Localization of the major heparin-binding site in fibronectin. J. Biol. Chem. 266, 7812-7818.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7812-7818
    • Barkalow, F.J.1    Schwarzbauer, J.E.2
  • 13
    • 0036903815 scopus 로고    scopus 로고
    • Signalling by glial cell line-derived neurotrophic factor (GDNF) requires heparan sulfate glycosaminoglycan
    • Barnett M.W., Fisher C.E., Perona-Wright G. & Davies J.A. (2002) Signalling by glial cell line-derived neurotrophic factor (GDNF) requires heparan sulfate glycosaminoglycan. J. Cell Sci. 115, 4495-4503.
    • (2002) J. Cell Sci. , vol.115 , pp. 4495-4503
    • Barnett, M.W.1    Fisher, C.E.2    Perona-Wright, G.3    Davies, J.A.4
  • 14
    • 34249001458 scopus 로고    scopus 로고
    • Cell adhesion to fibrillin-1: identification of an Arg-Gly-Asp-dependent synergy region and a heparin-binding site that regulates focal adhesion formation
    • Bax D.V., Mahalingham Y., Cain S. et al. (2007) Cell adhesion to fibrillin-1: identification of an Arg-Gly-Asp-dependent synergy region and a heparin-binding site that regulates focal adhesion formation. J. Cell Sci. 120, 1383-1392.
    • (2007) J. Cell Sci. , vol.120 , pp. 1383-1392
    • Bax, D.V.1    Mahalingham, Y.2    Cain, S.3
  • 15
    • 61649100307 scopus 로고    scopus 로고
    • The FGF family: biology, pathophysiology and therapy
    • Beenken A. & Mohammadi M. (2009) The FGF family: biology, pathophysiology and therapy. Nat. Rev. Drug Discovery 8, 235-253.
    • (2009) Nat. Rev. Drug Discovery , vol.8 , pp. 235-253
    • Beenken, A.1    Mohammadi, M.2
  • 16
    • 78651309004 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycan syndecan-3 is a novel receptor for GDNF, neurturin, and artemin
    • Bespalov M.M., Sidorova Y.A., Tumova S. et al. (2011) Heparan sulfate proteoglycan syndecan-3 is a novel receptor for GDNF, neurturin, and artemin. J. Cell Biol. 192, 153-169.
    • (2011) J. Cell Biol. , vol.192 , pp. 153-169
    • Bespalov, M.M.1    Sidorova, Y.A.2    Tumova, S.3
  • 18
    • 79951956048 scopus 로고    scopus 로고
    • Bioactive synthetic heparan sulfate and heparin derivatives: from long fragments mimetics to chimeras
    • Bonnaffé 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
    • Bonnaffé, D.1
  • 19
    • 0022240874 scopus 로고
    • Anchorage of collagen-tailed acetylcholinesterase to the extracellular matrix is mediated by heparan sulfate proteoglycans
    • Brandan E., Maldonado M., Garrido J. & Inestrosa N.C. (1985) Anchorage of collagen-tailed acetylcholinesterase to the extracellular matrix is mediated by heparan sulfate proteoglycans. J. Cell Biol. 101, 985-992.
    • (1985) J. Cell Biol. , vol.101 , pp. 985-992
    • Brandan, E.1    Maldonado, M.2    Garrido, J.3    Inestrosa, N.C.4
  • 20
    • 84876372433 scopus 로고    scopus 로고
    • Cooperative heparin-mediated oligomerization of fibroblast growth factor-1 (FGF1) precedes recruitment of FGFR2 to ternary complexes
    • Brown A., Robinson C.J., Gallagher J.T. & Blundell T.L. (2013) Cooperative heparin-mediated oligomerization of fibroblast growth factor-1 (FGF1) precedes recruitment of FGFR2 to ternary complexes. Biophys. J. 104, 1720-1730.
    • (2013) Biophys. J. , vol.104 , pp. 1720-1730
    • Brown, A.1    Robinson, C.J.2    Gallagher, J.T.3    Blundell, T.L.4
  • 21
    • 0036323505 scopus 로고    scopus 로고
    • Heparan sulfate depletion within pulmonary fibroblasts: implications for elastogenesis and repair
    • Buczek-Thomas J.A., Chu C.L., Rich C.B., Stone P.J., Foster J.A. & Nugent M.A. (2002) Heparan sulfate depletion within pulmonary fibroblasts: implications for elastogenesis and repair. J. Cell. Physiol. 192, 294-303.
    • (2002) J. Cell. Physiol. , vol.192 , pp. 294-303
    • Buczek-Thomas, J.A.1    Chu, C.L.2    Rich, C.B.3    Stone, P.J.4    Foster, J.A.5    Nugent, M.A.6
  • 22
    • 0032526145 scopus 로고    scopus 로고
    • Renal agenesis in mice homozygous for a gene trap mutation in the gene encoding heparan sulfate 2-sulfotransferase
    • Bullock S., Fletcher J., Beddington R. & Wilson V. (1998) Renal agenesis in mice homozygous for a gene trap mutation in the gene encoding heparan sulfate 2-sulfotransferase. Genes Dev. 12, 1894-1906.
    • (1998) Genes Dev. , vol.12 , pp. 1894-1906
    • Bullock, S.1    Fletcher, J.2    Beddington, R.3    Wilson, V.4
  • 23
    • 33751187897 scopus 로고    scopus 로고
    • The molecular diversity of glycosaminoglycans shapes animal development
    • Bulow H.E. & Hobert O. (2006) The molecular diversity of glycosaminoglycans shapes animal development. Annu. Rev. Cell Dev. Biol. 22, 375-407.
    • (2006) Annu. Rev. Cell Dev. Biol. , vol.22 , pp. 375-407
    • Bulow, H.E.1    Hobert, O.2
  • 24
    • 0029120352 scopus 로고
    • Heparin binding by fibronectin module III-13 involves six discontinuous basic residues brought together to form a cationic cradle
    • Busby T.F., Argraves W.S., Brew S.A., Pechik I., Gilliland G.L., Ingham K.C. (1995) Heparin binding by fibronectin module III-13 involves six discontinuous basic residues brought together to form a cationic cradle. J. Biol. Chem. 270, 18558-18562.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18558-18562
    • Busby, T.F.1    Argraves, W.S.2    Brew, S.A.3    Pechik, I.4    Gilliland, G.L.5    Ingham, K.C.6
  • 25
    • 24044522531 scopus 로고    scopus 로고
    • Fibrillin-1 interactions with heparin. Implications for microfibril and elastic fiber assembly
    • Cain S.A., Baldock C., Gallagher J.T. et al. (2005) Fibrillin-1 interactions with heparin. Implications for microfibril and elastic fiber assembly. J. Biol. Chem. 280, 30526-30537.
    • (2005) J. Biol. Chem. , vol.280 , pp. 30526-30537
    • Cain, S.A.1    Baldock, C.2    Gallagher, J.T.3
  • 26
    • 55249108724 scopus 로고    scopus 로고
    • Heparan sulfate regulates fibrillin-1 N- and C-terminal interactions
    • Cain S.A., Baldwin A.K., Mahalingham Y. et al. (2008) Heparan sulfate regulates fibrillin-1 N- and C-terminal interactions. J. Biol. Chem. 283, 27017-27027.
    • (2008) J. Biol. Chem. , vol.283 , pp. 27017-27027
    • Cain, S.A.1    Baldwin, A.K.2    Mahalingham, Y.3
  • 27
    • 84868306933 scopus 로고    scopus 로고
    • Fibrillin-1 mutations causing Weill-Marchesani syndrome and acromicric and geleophysic dysplasias disrupt heparan sulfate interactions
    • Cain S.A., McGovern A., Baldwin A., Baldock C., Kielty C.M. (2012) Fibrillin-1 mutations causing Weill-Marchesani syndrome and acromicric and geleophysic dysplasias disrupt heparan sulfate interactions. PLoS ONE 7, e48634.
    • (2012) PLoS ONE , vol.7 , pp. e48634
    • Cain, S.A.1    McGovern, A.2    Baldwin, A.3    Baldock, C.4    Kielty, C.M.5
  • 29
    • 0024584913 scopus 로고
    • Molecular modelling of protein-glycosaminoglycan interactions
    • Cardin A.D. & Weintraub H.J.R. (1989) Molecular modelling of protein-glycosaminoglycan interactions. Atherosclerosis 9, 21-32.
    • (1989) Atherosclerosis , vol.9 , pp. 21-32
    • Cardin, A.D.1    Weintraub, H.J.R.2
  • 30
    • 0030345443 scopus 로고    scopus 로고
    • N-syndecan: structure and function of a transmembrane heparan sulfate proteoglycan
    • Carey D.J. (1996) N-syndecan: structure and function of a transmembrane heparan sulfate proteoglycan. Perspect. Dev. Neurobiol. 3, 331-346.
    • (1996) Perspect. Dev. Neurobiol. , vol.3 , pp. 331-346
    • Carey, D.J.1
  • 31
    • 2542487390 scopus 로고    scopus 로고
    • MuSK is required for anchoring acetylcholinesterase at the neuromuscular junction
    • Cartaud A., Strochlic L., Guerra M. et al. (2004) MuSK is required for anchoring acetylcholinesterase at the neuromuscular junction. J. Cell Biol. 165, 505-515.
    • (2004) J. Cell Biol. , vol.165 , pp. 505-515
    • Cartaud, A.1    Strochlic, L.2    Guerra, M.3
  • 32
    • 0035707396 scopus 로고    scopus 로고
    • Structure and biological interactions of heparin and heparan sulfate
    • Casu B. & Lindahl U. (2001) Structure and biological interactions of heparin and heparan sulfate. Adv. Carbohydr. Chem. Biochem. 57, 159-206.
    • (2001) Adv. Carbohydr. Chem. Biochem. , vol.57 , pp. 159-206
    • Casu, B.1    Lindahl, U.2
  • 33
    • 84856226327 scopus 로고    scopus 로고
    • Fell-Muir Lecture: Chondroitin sulphate glycosaminoglycans: fun for some and confusion for others
    • Caterson B. (2012) Fell-Muir Lecture: Chondroitin sulphate glycosaminoglycans: fun for some and confusion for others. Int. J. Exp. Pathol. 93, 1-10.
    • (2012) Int. J. Exp. Pathol. , vol.93 , pp. 1-10
    • Caterson, B.1
  • 34
    • 41949105981 scopus 로고    scopus 로고
    • Interactions of hepatocyte growth factor/scatter factor with various glycosaminoglycans reveal an important interplay between the presence of iduronate and sulphate density
    • Catlow K.R., Deakin J.A., Wei Z. et al. (2008) Interactions of hepatocyte growth factor/scatter factor with various glycosaminoglycans reveal an important interplay between the presence of iduronate and sulphate density. J. Biol. Chem. 283, 5235-5248.
    • (2008) J. Biol. Chem. , vol.283 , pp. 5235-5248
    • Catlow, K.R.1    Deakin, J.A.2    Wei, Z.3
  • 35
    • 84455173121 scopus 로고    scopus 로고
    • Two distinct sites in sonic Hedgehog combine for heparan sulfate interactions and cell signalling functions
    • Chang S.C., Mulloy B., Magee A.I. & Couchman J.R. (2011) Two distinct sites in sonic Hedgehog combine for heparan sulfate interactions and cell signalling functions. J. Biol. Chem. 286, 44391-44402.
    • (2011) J. Biol. Chem. , vol.286 , pp. 44391-44402
    • Chang, S.C.1    Mulloy, B.2    Magee, A.I.3    Couchman, J.R.4
  • 36
    • 0029948752 scopus 로고    scopus 로고
    • Schwann cells secrete a novel collagen-like adhesive protein that binds N-syndecan
    • Chernousov M.A., Stahl R.C. & Carey D.J. (1996) Schwann cells secrete a novel collagen-like adhesive protein that binds N-syndecan. J. Biol. Chem. 271, 3844-13853.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3844-13853
    • Chernousov, M.A.1    Stahl, R.C.2    Carey, D.J.3
  • 37
    • 0035882520 scopus 로고    scopus 로고
    • Schwann cell type V collagen inhibits axonal outgrowth and promotes Schwann cell migration via distinct adhesive activities of the collagen and noncollagen domains
    • Chernousov M.A., Stahl R.C. & Carey D.J. (2001) Schwann cell type V collagen inhibits axonal outgrowth and promotes Schwann cell migration via distinct adhesive activities of the collagen and noncollagen domains. J. Neurosci. 21, 6125-6135.
    • (2001) J. Neurosci. , vol.21 , pp. 6125-6135
    • Chernousov, M.A.1    Stahl, R.C.2    Carey, D.J.3
  • 38
    • 79952107602 scopus 로고    scopus 로고
    • Syndecans as cell surface receptors: unique structure equates with functional diversity
    • Choi Y., Chung H., Jung H., Couchman J.R. & Oh E.S. (2011) Syndecans as cell surface receptors: unique structure equates with functional diversity. Matrix Biol. 30, 93-99.
    • (2011) Matrix Biol. , vol.30 , pp. 93-99
    • Choi, Y.1    Chung, H.2    Jung, H.3    Couchman, J.R.4    Oh, E.S.5
  • 39
    • 77954179353 scopus 로고    scopus 로고
    • Heparan sulfate-dependent signalling of fibroblast growth factor 18 by chondrocyte-derived perlecan
    • Chuang C.Y., Lord M.S., Melrose J. et al. (2010) Heparan sulfate-dependent signalling of fibroblast growth factor 18 by chondrocyte-derived perlecan. Biochemistry 49, 5524-5532.
    • (2010) Biochemistry , vol.49 , pp. 5524-5532
    • Chuang, C.Y.1    Lord, M.S.2    Melrose, J.3
  • 41
    • 78049404922 scopus 로고    scopus 로고
    • Transmembrane signalling proteoglycans
    • Couchman J.R. (2010) Transmembrane signalling proteoglycans. Annu. Rev. Cell Dev. Biol. 26, 89-114.
    • (2010) Annu. Rev. Cell Dev. Biol. , vol.26 , pp. 89-114
    • Couchman, J.R.1
  • 42
    • 84873029601 scopus 로고    scopus 로고
    • An introduction to proteoglycans and their localisation
    • Couchman J.R. & Pataki C.A. (2012) An introduction to proteoglycans and their localisation. J. Histochem. Cytochem. 60, 885-897.
    • (2012) J. Histochem. Cytochem. , vol.60 , pp. 885-897
    • Couchman, J.R.1    Pataki, C.A.2
  • 43
    • 77956289296 scopus 로고    scopus 로고
    • Inhibition of chemokine-glycosaminoglycan interactions in donor tissue reduces mouse allograft vasculopathy and transplant rejection
    • Dai E., Liu L.Y., Wang H. et al. (2010) Inhibition of chemokine-glycosaminoglycan interactions in donor tissue reduces mouse allograft vasculopathy and transplant rejection. PLoS ONE 6, 5.
    • (2010) PLoS ONE , vol.6 , pp. 5
    • Dai, E.1    Liu, L.Y.2    Wang, H.3
  • 44
    • 0346121461 scopus 로고    scopus 로고
    • Structural determinants of heparan sulfate modulation of GDNF signalling
    • Davies J.A., Yates E.A. & Turnbull J.E. (2003) Structural determinants of heparan sulfate modulation of GDNF signalling. Growth Factors 21, 109-119.
    • (2003) Growth Factors , vol.21 , pp. 109-119
    • Davies, J.A.1    Yates, E.A.2    Turnbull, J.E.3
  • 45
    • 65249134463 scopus 로고    scopus 로고
    • The binding properties of minimal oligosaccharides reveal a common heparan sulfate/dermatan sulfate-binding site in hepatocyte growth factor/scatter factor that can accommodate a wide variety of sulfation patterns
    • Deakin J.D., Blaum B.S., Gallagher J.T., Uhrin D. & Lyon M. (2008) The binding properties of minimal oligosaccharides reveal a common heparan sulfate/dermatan sulfate-binding site in hepatocyte growth factor/scatter factor that can accommodate a wide variety of sulfation patterns. J. Biol. Chem. 284, 6311-6321.
    • (2008) J. Biol. Chem. , vol.284 , pp. 6311-6321
    • Deakin, J.D.1    Blaum, B.S.2    Gallagher, J.T.3    Uhrin, D.4    Lyon, M.5
  • 46
    • 79955748614 scopus 로고    scopus 로고
    • Novel contact-dependent bone morphogenetic protein (BMP) signalling mediated by heparan sulfate proteoglycans
    • Dejima K., Kanai M.I., Akiyama T., Levings D.C., Nakato H. (2011) Novel contact-dependent bone morphogenetic protein (BMP) signalling mediated by heparan sulfate proteoglycans. J. Biol. Chem. 286, 17103-17111.
    • (2011) J. Biol. Chem. , vol.286 , pp. 17103-17111
    • Dejima, K.1    Kanai, M.I.2    Akiyama, T.3    Levings, D.C.4    Nakato, H.5
  • 48
    • 0034703006 scopus 로고    scopus 로고
    • Unraveling the amino acid sequence crucial for heparin binding to collagen V
    • Delacoux F., Fichard A., Cogne S., Garrone R. & Ruggiero F. (2000) Unraveling the amino acid sequence crucial for heparin binding to collagen V. J. Biol. Chem. 275, 29377-29382.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29377-29382
    • Delacoux, F.1    Fichard, A.2    Cogne, S.3    Garrone, R.4    Ruggiero, F.5
  • 49
    • 0037023784 scopus 로고    scopus 로고
    • Hepatocyte growth factor/scatter factor binds to small heparin-derived oligosaccharides and stimulates proliferation of human HaCaT cells
    • Delehedde M., Lyon M., Vidyasagar R., McDonnell T.J. & Fernig D. (2002) Hepatocyte growth factor/scatter factor binds to small heparin-derived oligosaccharides and stimulates proliferation of human HaCaT cells. J. Biol. Chem. 277, 12456-12462.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12456-12462
    • Delehedde, M.1    Lyon, M.2    Vidyasagar, R.3    McDonnell, T.J.4    Fernig, D.5
  • 50
    • 0037931520 scopus 로고    scopus 로고
    • Two different heparin-binding domains in the triple-helical domain of colq, the collagen tail subunit of synaptic acetylcholinesterase
    • Deprez P., Inestrosa N.C. & Krejci E. (2003) Two different heparin-binding domains in the triple-helical domain of colq, the collagen tail subunit of synaptic acetylcholinesterase. J. Biol. Chem. 278, 23233-23242.
    • (2003) J. Biol. Chem. , vol.278 , pp. 23233-23242
    • Deprez, P.1    Inestrosa, N.C.2    Krejci, E.3
  • 51
    • 0035979765 scopus 로고    scopus 로고
    • Regulation of Wnt signaling and embryo patterning by an extracellular sulfatase
    • Dhoot G.K., Gustafsson M.K., Ai X., Sun W., Standiford D.M. & Emerson C.P. (2001) Regulation of Wnt signaling and embryo patterning by an extracellular sulfatase. Science 293, 1663-1666.
    • (2001) Science , vol.293 , pp. 1663-1666
    • Dhoot, G.K.1    Gustafsson, M.K.2    Ai, X.3    Sun, W.4    Standiford, D.M.5    Emerson, C.P.6
  • 52
    • 70450242729 scopus 로고    scopus 로고
    • Heparan sulfate and transglutaminase activity are required for the formation of covalently cross-linked hedgehog oligomers
    • Dierker T., Dreier R., Migone M., Hamer S. & Grobe K. (2009a) Heparan sulfate and transglutaminase activity are required for the formation of covalently cross-linked hedgehog oligomers. J. Biol. Chem. 284, 32562-32571.
    • (2009) J. Biol. Chem. , vol.284 , pp. 32562-32571
    • Dierker, T.1    Dreier, R.2    Migone, M.3    Hamer, S.4    Grobe, K.5
  • 53
    • 65549150886 scopus 로고    scopus 로고
    • Heparan sulfate-modulated, metalloprotease-mediated sonic hedgehog release from producing cells
    • Dierker T., Dreier R., Petersen A., Bordych C. & Grobe K. (2009b) Heparan sulfate-modulated, metalloprotease-mediated sonic hedgehog release from producing cells. J. Biol. Chem. 284, 8013-8022.
    • (2009) J. Biol. Chem. , vol.284 , pp. 8013-8022
    • Dierker, T.1    Dreier, R.2    Petersen, A.3    Bordych, C.4    Grobe, K.5
  • 54
    • 0032566048 scopus 로고    scopus 로고
    • Structure of a heparin-linked biologically-active dimer of fibroblast growth factor
    • DiGabriele A.D., Lax I., Chen D.I. et al. (1998) Structure of a heparin-linked biologically-active dimer of fibroblast growth factor. Nature 393, 812-817.
    • (1998) Nature , vol.393 , pp. 812-817
    • DiGabriele, A.D.1    Lax, I.2    Chen, D.I.3
  • 55
    • 84864472945 scopus 로고    scopus 로고
    • Transport of fibroblast growth factor 2 in the pericellular matrix is controlled by the spatial distribution of its binding sites in heparan sulfate
    • Duchesne L., Octeau V., Bearon R.N. et al. (2012) Transport of fibroblast growth factor 2 in the pericellular matrix is controlled by the spatial distribution of its binding sites in heparan sulfate. PLoS Biol. 10, e1001361.
    • (2012) PLoS Biol. , vol.10
    • Duchesne, L.1    Octeau, V.2    Bearon, R.N.3
  • 56
    • 0036510538 scopus 로고    scopus 로고
    • Schwann cell adhesion to a novel heparan sulfate binding site in the N-terminal domain of α4 type V collagen is mediated by syndecan-3
    • Erdman R., Stahl R.C., Rothblum K., Chernousov M.A. & Carey D.J. (2002) Schwann cell adhesion to a novel heparan sulfate binding site in the N-terminal domain of α4 type V collagen is mediated by syndecan-3. J. Biol. Chem. 277, 7619-7625.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7619-7625
    • Erdman, R.1    Stahl, R.C.2    Rothblum, K.3    Chernousov, M.A.4    Carey, D.J.5
  • 57
    • 0034947648 scopus 로고    scopus 로고
    • Molecular diversity of heparan sulfate
    • Esko J.D. & Lindahl U. (2001) Molecular diversity of heparan sulfate. J. Clin. Invest. 108, 169-173.
    • (2001) J. Clin. Invest. , vol.108 , pp. 169-173
    • Esko, J.D.1    Lindahl, U.2
  • 58
    • 0029866647 scopus 로고    scopus 로고
    • Heparin structure and interactions with basic fibroblast growth factor
    • Faham S., Hileman R.E., Fromm J.R., Linhardt R.J. & Rees D.C. (1996) Heparin structure and interactions with basic fibroblast growth factor. Science 271, 1116-1120.
    • (1996) Science , vol.271 , pp. 1116-1120
    • Faham, S.1    Hileman, R.E.2    Fromm, J.R.3    Linhardt, R.J.4    Rees, D.C.5
  • 59
    • 22444440486 scopus 로고    scopus 로고
    • Structural model of the amino propeptide of collagen XI α1 chain with similarity to the LNS domains
    • Fallahi A., Kroll B., Warner L.R. & Oxford R.J. (2005) Structural model of the amino propeptide of collagen XI α1 chain with similarity to the LNS domains. Protein Sci. 14, 1526-1537.
    • (2005) Protein Sci. , vol.14 , pp. 1526-1537
    • Fallahi, A.1    Kroll, B.2    Warner, L.R.3    Oxford, R.J.4
  • 60
    • 79959552141 scopus 로고    scopus 로고
    • Dual roles of the Cardin-Weintraub motif in multimeric Sonic hedgehog
    • Farshi P., Ohlig F., Pickhinke U. et al. (2011) Dual roles of the Cardin-Weintraub motif in multimeric Sonic hedgehog. J. Biol. Chem. 286, 23608-23619.
    • (2011) J. Biol. Chem. , vol.286 , pp. 23608-23619
    • Farshi, P.1    Ohlig, F.2    Pickhinke, U.3
  • 61
    • 4143136640 scopus 로고    scopus 로고
    • Vascular endothelial growth factor: basic science and clinical progress
    • Ferrara N. (2004) Vascular endothelial growth factor: basic science and clinical progress. Endocr. Rev. 25, 581-611.
    • (2004) Endocr. Rev. , vol.25 , pp. 581-611
    • Ferrara, N.1
  • 62
    • 84867827672 scopus 로고    scopus 로고
    • Endothelial heparan sulfate 6-O-sulfation levels regulate angiogenic responses of endothelial cells to fibroblast growth factor 2 and vascular endothelial growth factor
    • Ferreras C., Rushton G., Cole G.L. et al. (2012) Endothelial heparan sulfate 6-O-sulfation levels regulate angiogenic responses of endothelial cells to fibroblast growth factor 2 and vascular endothelial growth factor. J. Biol. Chem. 287, 36132-36146.
    • (2012) J. Biol. Chem. , vol.287 , pp. 36132-36146
    • Ferreras, C.1    Rushton, G.2    Cole, G.L.3
  • 63
    • 84901462346 scopus 로고    scopus 로고
    • The role of glypicans in Hedgehog signalling
    • Filmus J. & Capurro M. (2014) The role of glypicans in Hedgehog signalling. Matrix Biol. 35, 248-252.
    • (2014) Matrix Biol. , vol.35 , pp. 248-252
    • Filmus, J.1    Capurro, M.2
  • 64
    • 33745475107 scopus 로고    scopus 로고
    • Computational approaches to the identification of heparin binding sites on the surfaces of proteins
    • Forster M. & Mulloy B. (2006) Computational approaches to the identification of heparin binding sites on the surfaces of proteins. Biochem. Soc. Trans. 34, 431-434.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 431-434
    • Forster, M.1    Mulloy, B.2
  • 65
    • 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. (2009) Characterization of the human sulfatase Sulf1 and its high affinity heparin/heparan sulfate interaction domain. J. Biol. Chem. 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
  • 66
    • 0028832566 scopus 로고
    • Differences in the interaction of heparin with arginine and lysine and the importance of these basic amino acids in the binding of heparin to acidic fibroblast growth factor
    • Fromm J.R., Hileman R.E., Caldwell E.E.O., Weiler J.M. & Linhardt R.J. (1995) Differences in the interaction of heparin with arginine and lysine and the importance of these basic amino acids in the binding of heparin to acidic fibroblast growth factor. Arch Biochem Biophys 323, 279-287.
    • (1995) Arch Biochem Biophys , vol.323 , pp. 279-287
    • Fromm, J.R.1    Hileman, R.E.2    Caldwell, E.E.O.3    Weiler, J.M.4    Linhardt, R.J.5
  • 67
    • 34248229139 scopus 로고    scopus 로고
    • Genetic alteration of endothelial heparan sulfate selectively inhibits tumour angiogenesis
    • Fuster M.M., Wang L., Castagnola J. et al. (2007) Genetic alteration of endothelial heparan sulfate selectively inhibits tumour angiogenesis. J. Cell Biol. 177, 539-549.
    • (2007) J. Cell Biol. , vol.177 , pp. 539-549
    • Fuster, M.M.1    Wang, L.2    Castagnola, J.3
  • 68
    • 0034907578 scopus 로고    scopus 로고
    • Heparan sulfate: growth control with a restricted sequence menu
    • Gallagher J.T. (2001) Heparan sulfate: growth control with a restricted sequence menu. J. Clin. Invest. 108, 357-361.
    • (2001) J. Clin. Invest. , vol.108 , pp. 357-361
    • Gallagher, J.T.1
  • 69
    • 0001106533 scopus 로고    scopus 로고
    • Heparan sulphate. Molecular structure and interactions with growth factors and morphogens
    • In: (ed. R.V. Iozzo), New York, NY - Basel: Marcel Dekker Inc.
    • Gallagher J.T., Lyon M. (2000) Heparan sulphate. Molecular structure and interactions with growth factors and morphogens. In: Proteoglycans; Structure, Biology and Molecular Interactions, pp. 27-60 (ed. R.V. Iozzo ), New York, NY - Basel: Marcel Dekker Inc.
    • (2000) Proteoglycans; Structure, Biology and Molecular Interactions , pp. 27-60
    • Gallagher, J.T.1    Lyon, M.2
  • 70
    • 0022384993 scopus 로고
    • Molecular distinctions between heparan sulphate and heparin. Analysis of sulphation patterns indicates that heparan sulphate and heparin are separate families of N-sulphated polysaccharides
    • Gallagher 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 of N-sulphated polysaccharides. Biochem. J. 23, 665-674.
    • (1985) Biochem. J. , vol.23 , pp. 665-674
    • Gallagher, J.T.1    Walker, A.2
  • 71
    • 0036111641 scopus 로고    scopus 로고
    • HSPG modification by the secreted enzyme Notum shapes the Wingless morphogen gradient
    • Giraldez A.J., Copley R.R. & Cohen S.M. (2002) HSPG modification by the secreted enzyme Notum shapes the Wingless morphogen gradient. Dev. Cell 2, 667-676.
    • (2002) Dev. Cell , vol.2 , pp. 667-676
    • Giraldez, A.J.1    Copley, R.R.2    Cohen, S.M.3
  • 72
    • 84875421249 scopus 로고    scopus 로고
    • Exploring mechanisms of FGF signalling through the lens of structural biology
    • Goetz R. & Mohammadi M. (2013) Exploring mechanisms of FGF signalling through the lens of structural biology. Nat. Rev. Mol. Cell Biol. 14, 166-180.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 166-180
    • Goetz, R.1    Mohammadi, M.2
  • 73
    • 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. et al. (2001) Different affinities of glycosaminoglycan oligosaccharides for monomeric and dimeric interleukin-8: a model for chemokine regulation at inflammatory sites. Biochemistry 41, 1640-1646.
    • (2001) Biochemistry , vol.41 , pp. 1640-1646
    • Goger, B.1    Halden, Y.2    Rek, A.3
  • 74
    • 45149083078 scopus 로고    scopus 로고
    • Evidence that heparin saccharides promote FGF2 mitogenesis through two distinct mechanisms
    • Goodger S.J., Robinson C.J., Murphy K.J. et al. (2008) Evidence that heparin saccharides promote FGF2 mitogenesis through two distinct mechanisms. J. Biol. Chem. 283, 13001-13008.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13001-13008
    • Goodger, S.J.1    Robinson, C.J.2    Murphy, K.J.3
  • 75
    • 75349091269 scopus 로고    scopus 로고
    • Structure-function analysis of VEGF receptor activation and the role of co-receptors in angiogenic signalling
    • Grünewald F.S., Prota A.E., Giese A. & Ballmer-Hofer K. (2010) Structure-function analysis of VEGF receptor activation and the role of co-receptors in angiogenic signalling. Biochim. Biophys. Acta 1804, 567-580.
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 567-580
    • Grünewald, F.S.1    Prota, A.E.2    Giese, A.3    Ballmer-Hofer, K.4
  • 76
    • 18444362115 scopus 로고    scopus 로고
    • Minimal heparin/heparan sulfate sequences for binding to fibroblast growth factor-1
    • Guerrini M., Agulles T., Bisio A. et al. (2002) Minimal heparin/heparan sulfate sequences for binding to fibroblast growth factor-1. Biochem. Biophys. Res. Commun. 292, 222-230.
    • (2002) Biochem. Biophys. Res. Commun. , vol.292 , pp. 222-230
    • Guerrini, M.1    Agulles, T.2    Bisio, A.3
  • 77
    • 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. (1993) Activating and inhibitory heparin sequences for FGF-2 (basic FGF). Distinct requirements for FGF-1, FGF-2, and FGF-4. J. Biol. Chem. 268, 23906-23914.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23906-23914
    • Guimond, S.1    Maccarana, M.2    Olwin, B.B.3    Lindahl, U.4    Rapraeger, A.C.5
  • 78
    • 0026709214 scopus 로고
    • Structure of a heparan sulphate oligosaccharide that binds to basic fibroblast growth factor
    • Habuchi H., Suzuki S., Saito T. et al. (1992) Structure of a heparan sulphate oligosaccharide that binds to basic fibroblast growth factor. Biochem. J. 285, 805-813.
    • (1992) Biochem. J. , vol.285 , pp. 805-813
    • Habuchi, H.1    Suzuki, S.2    Saito, T.3
  • 79
    • 22244448718 scopus 로고    scopus 로고
    • Regulation of protein function by glycosaminoglycans - as exemplified by chemokines
    • Handel T.M., Johnson Z., Crown S.E., Lau E.K. & Proudfoot A.E. (2005) Regulation of protein function by glycosaminoglycans - as exemplified by chemokines. Annu. Rev. Biochem. 74, 385-410.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 385-410
    • Handel, T.M.1    Johnson, Z.2    Crown, S.E.3    Lau, E.K.4    Proudfoot, A.E.5
  • 80
    • 13144295030 scopus 로고    scopus 로고
    • Engineered mutants of HGF/SF with reduced binding to heparan sulphate proteoglycans, decreased clearance and enhanced activity in vivo
    • Hartmann G., Prospero T., Brinkmann V. et al. (1998) Engineered mutants of HGF/SF with reduced binding to heparan sulphate proteoglycans, decreased clearance and enhanced activity in vivo. Curr. Biol. 8, 125-134.
    • (1998) Curr. Biol. , vol.8 , pp. 125-134
    • Hartmann, G.1    Prospero, T.2    Brinkmann, V.3
  • 81
    • 0032006909 scopus 로고    scopus 로고
    • Glycosaminoglycan-protein interactions: definition of consensus sites in glycosaminoglycan binding regions
    • Hileman R.E., Fromm J.R., Weiler J.M. & Linhardt R.J. (1998) Glycosaminoglycan-protein interactions: definition of consensus sites in glycosaminoglycan binding regions. 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
  • 82
    • 79953199422 scopus 로고    scopus 로고
    • Influencing hematopoietic differentiation of mouse embryonic stem cells using soluble heparin and heparan sulfate saccharides
    • Holley R.J., Pickford C.E., Rushton G. et al. (2011) Influencing hematopoietic differentiation of mouse embryonic stem cells using soluble heparin and heparan sulfate saccharides. J. Biol. Chem. 286, 6241-6252.
    • (2011) J. Biol. Chem. , vol.286 , pp. 6241-6252
    • Holley, R.J.1    Pickford, C.E.2    Rushton, G.3
  • 83
    • 33847152551 scopus 로고    scopus 로고
    • Insights into the structure/function of hepatocyte growth factor/scatter factor from studies with individual domains
    • Holmes O., Pillozzi S., Deakin J.A. et al. (2007) Insights into the structure/function of hepatocyte growth factor/scatter factor from studies with individual domains. J. Mol. Biol. 367, 395-408.
    • (2007) J. Mol. Biol. , vol.367 , pp. 395-408
    • Holmes, O.1    Pillozzi, S.2    Deakin, J.A.3
  • 84
    • 33845418128 scopus 로고    scopus 로고
    • On the role of glypicans in the process of morphogen gradient formation
    • Hufnagel L., Kreuger J., Cohen M.C. & Shraiman B.I. (2006) On the role of glypicans in the process of morphogen gradient formation. Dev. Biol. 300, 512-522.
    • (2006) Dev. Biol. , vol.300 , pp. 512-522
    • Hufnagel, L.1    Kreuger, J.2    Cohen, M.C.3    Shraiman, B.I.4
  • 85
    • 0030663341 scopus 로고    scopus 로고
    • Solution structure of midkine, a new heparin-binding growth factor
    • Iwasaki W., Nagata K., Hatanaka H. et al. (1997) Solution structure of midkine, a new heparin-binding growth factor. EMBO J. 16, 6936-6946.
    • (1997) EMBO J. , vol.16 , pp. 6936-6946
    • Iwasaki, W.1    Nagata, K.2    Hatanaka, H.3
  • 87
    • 84878566210 scopus 로고    scopus 로고
    • The heparin-binding growth factor midkine: the biological activities and candidate receptors
    • Kadomatsu K., Kishida S. & Tsubota S. (2013) The heparin-binding growth factor midkine: the biological activities and candidate receptors. J. Biochem. 153, 511-521.
    • (2013) J. Biochem. , vol.153 , pp. 511-521
    • Kadomatsu, K.1    Kishida, S.2    Tsubota, S.3
  • 88
    • 84924651313 scopus 로고    scopus 로고
    • Notum deacylates Wnt proteins to suppress signalling activity
    • Kakugawa S., Langton P.F., Zebisch M. et al. (2015) Notum deacylates Wnt proteins to suppress signalling activity. Nature 519, 187-192.
    • (2015) Nature , vol.519 , pp. 187-192
    • Kakugawa, S.1    Langton, P.F.2    Zebisch, M.3
  • 89
    • 0029999681 scopus 로고    scopus 로고
    • Midkine, a heparin-binding growth/differentiation factor, exhibits nerve cell adhesion and guidance activity for neurite outgrowth in vitro
    • Kaneda N., Talukder A.H., Nishiyama H., Koizumi S. & Muramatsu T. (1996) Midkine, a heparin-binding growth/differentiation factor, exhibits nerve cell adhesion and guidance activity for neurite outgrowth in vitro. J. Biochem. 119, 1150-1156.
    • (1996) J. Biochem. , vol.119 , pp. 1150-1156
    • Kaneda, N.1    Talukder, A.H.2    Nishiyama, H.3    Koizumi, S.4    Muramatsu, T.5
  • 90
    • 33745443328 scopus 로고    scopus 로고
    • Signalling by HGF/SF and Met: the role of heparin sulphate co-receptors
    • Kemp L.E., Mulloy B. & Gherardi E. (2006) Signalling by HGF/SF and Met: the role of heparin sulphate co-receptors. Biochem. Soc. Trans. 34, 414-417.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 414-417
    • Kemp, L.E.1    Mulloy, B.2    Gherardi, E.3
  • 92
    • 0040735688 scopus 로고    scopus 로고
    • Heparin-binding growth-associated molecule contains two heparin-binding β-sheet domains that are homologous to the thrombospondin type I repeat
    • Kilpeläinen I., Kaksonen M., Kinnunen T. et al. (2000) Heparin-binding growth-associated molecule contains two heparin-binding β-sheet domains that are homologous to the thrombospondin type I repeat. J. Biol. Chem. 275, 13564-13570.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13564-13570
    • Kilpeläinen, I.1    Kaksonen, M.2    Kinnunen, T.3
  • 93
    • 1642442637 scopus 로고    scopus 로고
    • C-terminal and heparin-binding domains of collagenic tail subunit are both essential for anchoring acetylcholinesterase at the synapse
    • Kimbell L.M., Ohno K., Engel A.G. & Rotundo R.L. (2004) C-terminal and heparin-binding domains of collagenic tail subunit are both essential for anchoring acetylcholinesterase at the synapse. J. Biol. Chem. 279, 10997-11005.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10997-11005
    • Kimbell, L.M.1    Ohno, K.2    Engel, A.G.3    Rotundo, R.L.4
  • 94
    • 0030050980 scopus 로고    scopus 로고
    • Neurite outgrowth in brain neurons induced by heparin-binding growth-associated molecule (HB-GAM) depends on the specific interaction of HB-GAM with heparan sulphate
    • Kinnunen T., Nolo R., Maccarana M., Lindahl U. & Rauvala H. (1996) Neurite outgrowth in brain neurons induced by heparin-binding growth-associated molecule (HB-GAM) depends on the specific interaction of HB-GAM with heparan sulphate. J. Biol. Chem. 271, 2243-2248.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2243-2248
    • Kinnunen, T.1    Nolo, R.2    Maccarana, M.3    Lindahl, U.4    Rauvala, H.5
  • 95
    • 0032562591 scopus 로고    scopus 로고
    • Cortactin-src kinase signalling pathway is involved in N-syndecan-dependent neurite outgrowth
    • Kinnunen T., Kaksonen M., Saarinen J., Kalkkinen N., Peng H.B. & Rauvala H. (1998) Cortactin-src kinase signalling pathway is involved in N-syndecan-dependent neurite outgrowth. J. Biol. Chem. 273, 10702-10708.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10702-10708
    • Kinnunen, T.1    Kaksonen, M.2    Saarinen, J.3    Kalkkinen, N.4    Peng, H.B.5    Rauvala, H.6
  • 96
    • 0022001051 scopus 로고
    • Heparan sulfate proteoglycans from mouse mammary epithelial cells. Basal extracellular proteoglycan binds specifically to native type I collagen fibrils
    • Koda J.E., Rapraeger A. & Bernfield M. (1985) Heparan sulfate proteoglycans from mouse mammary epithelial cells. Basal extracellular proteoglycan binds specifically to native type I collagen fibrils. J. Biol. Chem. 260, 8157-8162.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8157-8162
    • Koda, J.E.1    Rapraeger, A.2    Bernfield, M.3
  • 97
    • 0030892080 scopus 로고    scopus 로고
    • Identification of a glycosaminoglycan-binding site in chemokine macrophage inflammatory protein-1α
    • Koopmann W. & Krangel M.S. (1997) Identification of a glycosaminoglycan-binding site in chemokine macrophage inflammatory protein-1α. J. Biol. Chem. 272, 10103-10109.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10103-10109
    • Koopmann, W.1    Krangel, M.S.2
  • 98
    • 0036007121 scopus 로고    scopus 로고
    • Ectodermal syndecan-2 mediates left-right axis formation in migrating mesoderm as a cell-nonautonomous Vg1 cofactor
    • Kramer K.L. & Yost H.J. (2002) Ectodermal syndecan-2 mediates left-right axis formation in migrating mesoderm as a cell-nonautonomous Vg1 cofactor. Dev. Cell 2, 115-124.
    • (2002) Dev. Cell , vol.2 , pp. 115-124
    • Kramer, K.L.1    Yost, H.J.2
  • 99
    • 84873024385 scopus 로고    scopus 로고
    • Heparan sulfate biosynthesis-regulation and variability
    • Kreuger J. & Kjellen L. (2012) Heparan sulfate biosynthesis-regulation and variability. J. Histochem. Cytochem. 60, 898-907.
    • (2012) J. Histochem. Cytochem. , vol.60 , pp. 898-907
    • Kreuger, J.1    Kjellen, L.2
  • 100
    • 0035903106 scopus 로고    scopus 로고
    • Sequence analysis of heparan sulfate epitopes with graded affinities for fibroblast growth factors 1 and 2
    • Kreuger J., Salmivirta M., Sturiale L., Gimenez-Gallego G. & Lindahl U. (2001) Sequence analysis of heparan sulfate epitopes with graded affinities for fibroblast growth factors 1 and 2. J. Biol. Chem. 276, 30744-30752.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30744-30752
    • Kreuger, J.1    Salmivirta, M.2    Sturiale, L.3    Gimenez-Gallego, G.4    Lindahl, U.5
  • 101
    • 33746614761 scopus 로고    scopus 로고
    • Interactions between heparan sulphate and proteins: the concept of specificity
    • Kreuger J., Spillmann D., Li J.P. & Lindahl U. (2006) Interactions between heparan sulphate and proteins: the concept of specificity. J. Cell Biol. 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
  • 102
    • 35148839019 scopus 로고    scopus 로고
    • Molecular mapping and functional characterization of the VEGF164 heparin-binding domain
    • Krilleke D., DeErkenez A., Schubert W. et al. (2007) Molecular mapping and functional characterization of the VEGF164 heparin-binding domain. J. Biol. Chem. 282, 28045-28056.
    • (2007) J. Biol. Chem. , vol.282 , pp. 28045-28056
    • Krilleke, D.1    DeErkenez, A.2    Schubert, W.3
  • 103
    • 70450208952 scopus 로고    scopus 로고
    • The heparin-binding domainconfersdiverse functions of VEGF-A in development and disease:a structure-function study
    • Krilleke D., Ng Y.-S. & Shima D.T. (2009) The heparin-binding domainconfersdiverse functions of VEGF-A in development and disease:a structure-function study. Biochem. Soc. Trans. 37, 1201-1206.
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 1201-1206
    • Krilleke, D.1    Ng, Y.-S.2    Shima, D.T.3
  • 105
    • 42549130865 scopus 로고    scopus 로고
    • The novel CXCL12gamma isoform encodes an unstructured cationic domain which regulates bioactivity and interaction with both glycosaminoglycans and CXCR4
    • Laguri C., Sadir R., Rueda P. et al. (2007) The novel CXCL12gamma 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
  • 106
    • 0031650075 scopus 로고    scopus 로고
    • Proteoglycans: master regulators of molecular encounter?
    • Lander A. (1998) Proteoglycans: master regulators of molecular encounter? Matrix Biol. 17, 465-472.
    • (1998) Matrix Biol. , vol.17 , pp. 465-472
    • Lander, A.1
  • 107
    • 0036080430 scopus 로고    scopus 로고
    • Do morphogen gradients arise by diffusion?
    • Lander A.D., Nie Q. & Wan F.Y. (2002) Do morphogen gradients arise by diffusion? Dev. Cell 2, 785-796.
    • (2002) Dev. Cell , vol.2 , pp. 785-796
    • Lander, A.D.1    Nie, Q.2    Wan, F.Y.3
  • 108
    • 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. et al. (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
  • 109
    • 5644236458 scopus 로고    scopus 로고
    • Heparan sulfate structure in mice with genetically modified heparan sulfate production
    • Ledin J., Staatz W., Li J.P. et al. (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
  • 110
    • 77956239259 scopus 로고    scopus 로고
    • Structure of pleiotrophin- and hepatocyte growth factor-binding sulfated hexasaccharide determined by biochemical and computational approaches
    • Li F., Nandini C.D., Hattori T. et al. (2010) Structure of pleiotrophin- and hepatocyte growth factor-binding sulfated hexasaccharide determined by biochemical and computational approaches. J. Biol. Chem. 285, 27673-27685.
    • (2010) J. Biol. Chem. , vol.285 , pp. 27673-27685
    • Li, F.1    Nandini, C.D.2    Hattori, T.3
  • 111
    • 79951869901 scopus 로고    scopus 로고
    • Glypican-5 stimulates rhabdomyosarcoma cell proliferation by activating Hedgehog signalling
    • Li F., Shi W., Capurro M. & Filmus J. (2011) Glypican-5 stimulates rhabdomyosarcoma cell proliferation by activating Hedgehog signalling. J. Cell Biol. 192, 691-704.
    • (2011) J. Cell Biol. , vol.192 , pp. 691-704
    • Li, F.1    Shi, W.2    Capurro, M.3    Filmus, J.4
  • 112
    • 0035887033 scopus 로고    scopus 로고
    • Crystal structures of NK1-heparin complexes reveal the basis for NK1 activity and enable engineering of potent agonists of the MET receptor
    • Lietha D., Chirgadze D.Y., Mulloy B., Blundell T.L. & Gherardi E. (2001) Crystal structures of NK1-heparin complexes reveal the basis for NK1 activity and enable engineering of potent agonists of the MET receptor. EMBO J. 20, 5543-5555.
    • (2001) EMBO J. , vol.20 , pp. 5543-5555
    • Lietha, D.1    Chirgadze, D.Y.2    Mulloy, B.3    Blundell, T.L.4    Gherardi, E.5
  • 113
    • 12344310615 scopus 로고    scopus 로고
    • Functions of heparan sulfate proteoglycans in cell signaling during development
    • Lin X. (2004) Functions of heparan sulfate proteoglycans in cell signaling during development. Development 131, 6009-6021.
    • (2004) Development , vol.131 , pp. 6009-6021
    • Lin, X.1
  • 114
    • 0034253918 scopus 로고    scopus 로고
    • Role of heparan sulfate proteoglycans in cell-cell signaling in Drosophila
    • Lin X. & Perrimon N. (2000) Role of heparan sulfate proteoglycans in cell-cell signaling in Drosophila. Matrix Biol. 19, 303-307.
    • (2000) Matrix Biol. , vol.19 , pp. 303-307
    • Lin, X.1    Perrimon, N.2
  • 115
    • 0034663225 scopus 로고    scopus 로고
    • Disruption of gastrulation and heparan sulfate biosynthesis in EXT1-deficient mice
    • Lin X., Wei G., Shi Z. et al. (2000) Disruption of gastrulation and heparan sulfate biosynthesis in EXT1-deficient mice. Dev. Biol. 224, 299-311.
    • (2000) Dev. Biol. , vol.224 , pp. 299-311
    • Lin, X.1    Wei, G.2    Shi, Z.3
  • 116
    • 70149088868 scopus 로고    scopus 로고
    • Interactions between heparin sulphate and proteins-design and functional implications
    • Lindahl U. & Li J.P. (2009) Interactions between heparin sulphate 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
  • 118
    • 70349876852 scopus 로고    scopus 로고
    • The molecular basis and functional implications of chemokine interactions with heparan sulphate
    • Lortat-Jacob H. (2009) The molecular basis and functional implications of chemokine interactions with heparan sulphate. Curr. Opin. Struct. Biol. 19, 543-548.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 543-548
    • Lortat-Jacob, H.1
  • 119
    • 0029051004 scopus 로고
    • Molecular organization of the interferon gamma-binding domain in heparan sulphate
    • Lortat-Jacob H., Turnbull J.E. & Grimaud J.A. (1995) Molecular organization of the interferon gamma-binding domain in heparan sulphate. Biochem. J. 310, 497-505.
    • (1995) Biochem. J. , vol.310 , pp. 497-505
    • Lortat-Jacob, H.1    Turnbull, J.E.2    Grimaud, J.A.3
  • 120
    • 0037022280 scopus 로고    scopus 로고
    • Structural diversity of heparan sulfate binding domains in chemokines
    • Lortat-Jacob H., Grosdidier A. & Imberty A. (2002) Structural diversity of heparan sulfate binding domains in chemokines. Proc Natl Acad Sci USA. 99, 1229-1234.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1229-1234
    • Lortat-Jacob, H.1    Grosdidier, A.2    Imberty, A.3
  • 121
    • 33746377014 scopus 로고    scopus 로고
    • Control of fibroblast growth factor (FGF7)- and FGF1-induced mitogenesis and downstream signalling by distinct heparin octasaccharide motifs
    • Luo Y., Ye S., Kan M. & McKeehan W.L. (2006) Control of fibroblast growth factor (FGF7)- and FGF1-induced mitogenesis and downstream signalling by distinct heparin octasaccharide motifs. J. Biol. Chem. 281, 21052-21061.
    • (2006) J. Biol. Chem. , vol.281 , pp. 21052-21061
    • Luo, Y.1    Ye, S.2    Kan, M.3    McKeehan, W.L.4
  • 122
    • 0023137162 scopus 로고
    • Identification of an extended N-acetylated sequence adjacent to the protein-linkage region of heparan sulphate
    • Lyon M., Steward W.P., Hampson I. & Gallagher J.T. (1987) Identification of an extended N-acetylated sequence adjacent to the protein-linkage region of heparan sulphate. Biochem. J. 242, 493-498.
    • (1987) Biochem. J. , vol.242 , pp. 493-498
    • Lyon, M.1    Steward, W.P.2    Hampson, I.3    Gallagher, J.T.4
  • 123
    • 0028346379 scopus 로고
    • Liver heparan sulphate structure: a novel molecular design
    • Lyon M., Deakin J. & Gallagher J.T. (1994) Liver heparan sulphate structure: a novel molecular design. J. Biol. Chem. 269, 11208-11215.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11208-11215
    • Lyon, M.1    Deakin, J.2    Gallagher, J.T.3
  • 124
    • 0034681420 scopus 로고    scopus 로고
    • Elucidation of the structural features of heparan sulfate important for interaction with the Hep-2 domain of fibronectin
    • Lyon M., Rushton G.R., Askari J.A., Humphries M. & Gallagher J.T. (2000) Elucidation of the structural features of heparan sulfate important for interaction with the Hep-2 domain of fibronectin. J. Biol. Chem. 275, 4599-4606.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4599-4606
    • Lyon, M.1    Rushton, G.R.2    Askari, J.A.3    Humphries, M.4    Gallagher, J.T.5
  • 125
    • 0037059771 scopus 로고    scopus 로고
    • The mode of action of heparan and dermatan sulfates in the regulation of hepatocyte growth factor/scatter factor
    • Lyon M., Deakin J. & Gallagher J.T. (2002) The mode of action of heparan and dermatan sulfates in the regulation of hepatocyte growth factor/scatter factor. J. Biol. Chem. 277, 1040-1046.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1040-1046
    • Lyon, M.1    Deakin, J.2    Gallagher, J.T.3
  • 126
    • 6344284887 scopus 로고    scopus 로고
    • The interactions of hepatocyte growth factor/scatter factor and Its NK1 and NK2 variants with glycosaminoglycans using a modified gel mobility shift assay
    • Lyon M., Deakin J.D., Lietha D., Gherardi E. & Gallagher J.T. (2004) The interactions of hepatocyte growth factor/scatter factor and Its NK1 and NK2 variants with glycosaminoglycans using a modified gel mobility shift assay. J. Biol. Chem. 279, 43560-43567.
    • (2004) J. Biol. Chem. , vol.279 , pp. 43560-43567
    • Lyon, M.1    Deakin, J.D.2    Lietha, D.3    Gherardi, E.4    Gallagher, J.T.5
  • 127
    • 0027448951 scopus 로고
    • Minimal sequence in heparin/heparan sulphate required for binding basic fibroblast growth factor
    • Maccarana M., Casu B. & Lindahl U. (1993) Minimal sequence in heparin/heparan sulphate required for binding basic fibroblast growth factor. J. Biol. Chem. 268, 23898-23905.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23898-23905
    • Maccarana, M.1    Casu, B.2    Lindahl, U.3
  • 128
    • 0032514145 scopus 로고    scopus 로고
    • Involvement of receptor-like protein tyrosine phosphatase ζ/RPTPβ and its ligand pleiotrophin/heparin-binding growth-associated molecule (HB-GAM) in neuronal migration
    • Maeda N. & Noda M. (1998) Involvement of receptor-like protein tyrosine phosphatase ζ/RPTPβ and its ligand pleiotrophin/heparin-binding growth-associated molecule (HB-GAM) in neuronal migration. J. Cell Biol. 142, 203-216.
    • (1998) J. Cell Biol. , vol.142 , pp. 203-216
    • Maeda, N.1    Noda, M.2
  • 129
    • 34047257842 scopus 로고    scopus 로고
    • Cellular adhesion responses to the heparin-binding (hepii) domain of fibronectin require heparan sulfate with specific properties
    • Mahalingam Y., Gallagher J.T. & Couchman J.R. (2007) Cellular adhesion responses to the heparin-binding (hepii) domain of fibronectin require heparan sulfate with specific properties. J. Biol. Chem. 282, 3221-3230.
    • (2007) J. Biol. Chem. , vol.282 , pp. 3221-3230
    • Mahalingam, Y.1    Gallagher, J.T.2    Couchman, J.R.3
  • 130
    • 73949157671 scopus 로고    scopus 로고
    • Differential interactions of FGFs with heparan sulfate control gradient formation and branching morphogenesis
    • Makarenkova H.P., Hoffman M.P., Beenken A. et al. (2009) Differential interactions of FGFs with heparan sulfate control gradient formation and branching morphogenesis. Sci. Signal. 2, ra55.
    • (2009) Sci. Signal. , vol.2 , pp. ra55
    • Makarenkova, H.P.1    Hoffman, M.P.2    Beenken, A.3
  • 131
    • 0037025311 scopus 로고    scopus 로고
    • Neuropilin-1 binds vascular endothelial growth factor 165, placenta growth factor-2, and heparin via its b1b2 domain
    • Mamluk R., Gechtman Z., Kutcher M.E., Gasiunas N., Gallagher J.T. & Klagsbrun M. (2002) Neuropilin-1 binds vascular endothelial growth factor 165, placenta growth factor-2, and heparin via its b1b2 domain. J. Biol. Chem. 277, 24818-24825.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24818-24825
    • Mamluk, R.1    Gechtman, Z.2    Kutcher, M.E.3    Gasiunas, N.4    Gallagher, J.T.5    Klagsbrun, M.6
  • 132
    • 84908228669 scopus 로고    scopus 로고
    • Extracellular distribution of diffusible growth factors controlled by heparan sulfate proteoglycans during mammalian embryogenesis
    • Matsuo I. & Kimura-Yoshida C. (2014) Extracellular distribution of diffusible growth factors controlled by heparan sulfate proteoglycans during mammalian embryogenesis. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 369, 20130545.
    • (2014) Philos. Trans. R. Soc. Lond. B. Biol. Sci. , vol.369
    • Matsuo, I.1    Kimura-Yoshida, C.2
  • 133
    • 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. et al. (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
  • 134
    • 0002452569 scopus 로고    scopus 로고
    • Developmental roles and clinical significance of hedgehog signaling
    • McMahon A.P., Ingham P.W. & Tabin C.J. (2003) Developmental roles and clinical significance of hedgehog signaling. Curr. Top. Dev. Biol. 53, 1-114.
    • (2003) Curr. Top. Dev. Biol. , vol.53 , pp. 1-114
    • McMahon, A.P.1    Ingham, P.W.2    Tabin, C.J.3
  • 135
    • 0033603298 scopus 로고    scopus 로고
    • Highly sensitive sequencing of the sulphated domains of heparan sulphate
    • Merry C.L., Lyon M., Deakin J.A., Hopwood J.J. & Gallagher J.T. (1999) Highly sensitive sequencing of the sulphated domains of heparan sulphate. J. Biol. Chem. 274, 18455-18462.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18455-18462
    • Merry, C.L.1    Lyon, M.2    Deakin, J.A.3    Hopwood, J.J.4    Gallagher, J.T.5
  • 136
    • 0035929660 scopus 로고    scopus 로고
    • The molecular phenotype of heparan sulfate in the Hs2st-/-mutant mouse
    • Merry C.L., Bullock S.L., Swan D.C. et al. (2001) The molecular phenotype of heparan sulfate in the Hs2st-/-mutant mouse. J. Biol. Chem. 276, 35429-35434.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35429-35434
    • Merry, C.L.1    Bullock, S.L.2    Swan, D.C.3
  • 137
    • 33748636461 scopus 로고    scopus 로고
    • Heparin-mediated conformational changes in fibronectin expose vascular endothelial growth factor binding sites
    • Mitsi M., Hong Z., Costello C.E. & Nugent M.A. (2006) Heparin-mediated conformational changes in fibronectin expose vascular endothelial growth factor binding sites. Biochemistry 45, 10319-10328.
    • (2006) Biochemistry , vol.45 , pp. 10319-10328
    • Mitsi, M.1    Hong, Z.2    Costello, C.E.3    Nugent, M.A.4
  • 138
    • 44449125309 scopus 로고    scopus 로고
    • The structural plasticity of heparan sulfate NA-domains and hence their role in mediating multivalent interactions is confirmed by high-accuracy 15N-NMR relaxation studies
    • Mobli M., Nilsson M. & Almond A. (2008) The structural plasticity of heparan sulfate NA-domains and hence their role in mediating multivalent interactions is confirmed by high-accuracy 15N-NMR relaxation studies. Glycoconj. J. 25, 401-414.
    • (2008) Glycoconj. J. , vol.25 , pp. 401-414
    • Mobli, M.1    Nilsson, M.2    Almond, A.3
  • 139
    • 18144423534 scopus 로고    scopus 로고
    • Structural basis for fibroblast growth factor receptor activation
    • Mohammadi M., Olsen S.K. & Ibrahimi O.A. (2005) Structural basis for fibroblast growth factor receptor activation. Cytokine Growth Factor Rev. 16, 107-137.
    • (2005) Cytokine Growth Factor Rev. , vol.16 , pp. 107-137
    • Mohammadi, M.1    Olsen, S.K.2    Ibrahimi, O.A.3
  • 140
    • 0035109876 scopus 로고    scopus 로고
    • Identification of a novel heparin-binding site in the alternatively-spliced IICS region of fibronectin: roles of integrins and proteoglycans in cell adhesion to fibronectin splice variants
    • Mostavi-Pour Z., Askari J.A., Whittard J.D. & Humphries M.J. (2001) Identification of a novel heparin-binding site in the alternatively-spliced IICS region of fibronectin: roles of integrins and proteoglycans in cell adhesion to fibronectin splice variants. Matrix Biol. 20, 63-73.
    • (2001) Matrix Biol. , vol.20 , pp. 63-73
    • Mostavi-Pour, Z.1    Askari, J.A.2    Whittard, J.D.3    Humphries, M.J.4
  • 141
    • 31044438562 scopus 로고    scopus 로고
    • The specificity of interactions between proteins and sulfated polysaccharides
    • Mulloy B. (2005) The specificity of interactions between proteins and sulfated polysaccharides. An. Acad. Bras. Ciênc. 77, 651-664.
    • (2005) An. Acad. Bras. Ciênc. , vol.77 , pp. 651-664
    • Mulloy, B.1
  • 142
    • 84861888183 scopus 로고    scopus 로고
    • Structure and physiochemical characterisation of heparin
    • In:(eds R. Lever, B. Mulloy & C.P. Page), Berlin, Heidelberg: Springer Verlag
    • Mulloy B. (2012) Structure and physiochemical characterisation of heparin. In: Heparin - A Century of Progress, pp. 77-98. (eds R. Lever, B. Mulloy & C.P. Page ), Berlin, Heidelberg: Springer Verlag.
    • (2012) Heparin - A Century of Progress , pp. 77-98
    • Mulloy, B.1
  • 143
    • 0033650826 scopus 로고    scopus 로고
    • Conformation and dynamics of heparin and heparan sulfate
    • Mulloy B. & Forster M.J. (2000) Conformation and dynamics of heparin and heparan sulfate. Glycobiology 10, 1147-1156.
    • (2000) Glycobiology , vol.10 , pp. 1147-1156
    • Mulloy, B.1    Forster, M.J.2
  • 144
    • 0035443891 scopus 로고    scopus 로고
    • Order out of complexity - protein structures that interact with heparin
    • Mulloy B. & Linhardt R.J. (2001) Order out of complexity - protein structures that interact with heparin. Curr. Opin. Struct. Biol. 11, 623-628.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 623-628
    • Mulloy, B.1    Linhardt, R.J.2
  • 145
    • 0028129122 scopus 로고
    • Localization of heparin-binding, neurite outgrowth and antigenic regions in midkine molecule
    • Muramatsu H., Inui T., Kimura T. et al. (1994) Localization of heparin-binding, neurite outgrowth and antigenic regions in midkine molecule. Biochem. Biophys. Res. Commun. 203, 1131-1139.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 1131-1139
    • Muramatsu, H.1    Inui, T.2    Kimura, T.3
  • 146
    • 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.R., 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.R.2    Lyon, M.3    Thompson, J.E.4    Roberts, I.S.5    Gallagher, J.T.6
  • 147
    • 79957607304 scopus 로고    scopus 로고
    • Highly sulfated nonreducing end-derived heparan sulfate domains bind fibroblast growth factor-2 with high affinity and are enriched in biologically active fractions
    • Naimy H., Buczek-Thomas J.A., Nugent M.A., Leymarie N. & Zaia J. (2011) Highly sulfated nonreducing end-derived heparan sulfate domains bind fibroblast growth factor-2 with high affinity and are enriched in biologically active fractions. J. Biol. Chem. 286, 19311-19319.
    • (2011) J. Biol. Chem. , vol.286 , pp. 19311-19319
    • Naimy, H.1    Buczek-Thomas, J.A.2    Nugent, M.A.3    Leymarie, N.4    Zaia, J.5
  • 148
    • 84939633461 scopus 로고    scopus 로고
    • In vitro model for hematopoietic progenitor cell homing reveals endothelial heparan sulfate proteoglycans as direct adhesive ligands
    • Netelenbos T., van den Born J., Kessler F.L., Zweegman S., Huijgens P.C. & Dräger A.M. (2003) In vitro model for hematopoietic progenitor cell homing reveals endothelial heparan sulfate proteoglycans as direct adhesive ligands. J. Leukoc. Biol. 72, 353-362.
    • (2003) J. Leukoc. Biol. , vol.72 , pp. 353-362
    • Netelenbos, T.1    van den Born, J.2    Kessler, F.L.3    Zweegman, S.4    Huijgens, P.C.5    Dräger, A.M.6
  • 149
    • 33344467123 scopus 로고    scopus 로고
    • VEGF function in vascular pathogenesis
    • Ng Y.S., Krilleke D. & Shima D.T. (2006) VEGF function in vascular pathogenesis. Exp. Cell Res. 312, 527-537.
    • (2006) Exp. Cell Res. , vol.312 , pp. 527-537
    • Ng, Y.S.1    Krilleke, D.2    Shima, D.T.3
  • 150
    • 79958198050 scopus 로고    scopus 로고
    • Sonic hedgehog shedding results in functional activation of the solubilized protein
    • Ohlig S., Farshi P., Pickhinke U. et al. (2011) Sonic hedgehog shedding results in functional activation of the solubilized protein. Dev. Cell 20, 764-774.
    • (2011) Dev. Cell , vol.20 , pp. 764-774
    • Ohlig, S.1    Farshi, P.2    Pickhinke, U.3
  • 151
    • 84871596524 scopus 로고    scopus 로고
    • An emerging role of Sonic hedgehog shedding as a modulator of heparan sulfate interactions
    • Ohlig S., Pickhinke U., Sirko S. et al. (2012) An emerging role of Sonic hedgehog shedding as a modulator of heparan sulfate interactions. J. Biol. Chem. 287, 43708-43719.
    • (2012) J. Biol. Chem. , vol.287 , pp. 43708-43719
    • Ohlig, S.1    Pickhinke, U.2    Sirko, S.3
  • 152
    • 84875809263 scopus 로고    scopus 로고
    • Specific binding of collagen Q to the neuromuscular junction is exploited to cure congenital myasthenia and to explore bases of myasthenia gravis
    • Ohno K., Ito M., Kawakami Y., Krejci E. & Engel A.G. (2013) Specific binding of collagen Q to the neuromuscular junction is exploited to cure congenital myasthenia and to explore bases of myasthenia gravis. Chem. Biol. Interact. 203, 335-340.
    • (2013) Chem. Biol. Interact. , vol.203 , pp. 335-340
    • Ohno, K.1    Ito, M.2    Kawakami, Y.3    Krejci, E.4    Engel, A.G.5
  • 153
    • 42649106868 scopus 로고    scopus 로고
    • The heparanome and regulation of cell function: structures, functions and challenges
    • Ori A., Wilkinson M.C. & Fernig D.G. (2008) The heparanome and regulation of cell function: structures, functions and challenges. Front Biosci. 13, 4309-4338.
    • (2008) Front Biosci. , vol.13 , pp. 4309-4338
    • Ori, A.1    Wilkinson, M.C.2    Fernig, D.G.3
  • 154
    • 58049218445 scopus 로고    scopus 로고
    • The structure of the glial cell line-derived neurotrophic factor-coreceptor complex: insights into RET signalling and heparin binding
    • Parkash V., Leppänen V.-M., Virtanen H. et al. (2008) The structure of the glial cell line-derived neurotrophic factor-coreceptor complex: insights into RET signalling and heparin binding. J. Biol. Chem. 283, 35164-35172.
    • (2008) J. Biol. Chem. , vol.283 , pp. 35164-35172
    • Parkash, V.1    Leppänen, V.-M.2    Virtanen, H.3
  • 155
    • 44049086666 scopus 로고    scopus 로고
    • Specific heparan sulfate structures modulate FGF10-mediated submandibular gland epithelial morphogenesis and differentiation
    • Patel V.N., Likar K.M., Zisman-Rozen S. et al. (2008) Specific heparan sulfate structures modulate FGF10-mediated submandibular gland epithelial morphogenesis and differentiation. J. Biol. Chem. 283, 9308-9317.
    • (2008) J. Biol. Chem. , vol.283 , pp. 9308-9317
    • Patel, V.N.1    Likar, K.M.2    Zisman-Rozen, S.3
  • 156
    • 0035443744 scopus 로고    scopus 로고
    • Role of heparan sulfate in fibroblast growth factor signalling: a structural view
    • Pellegrini L. (2001) Role of heparan sulfate in fibroblast growth factor signalling: a structural view. Curr. Opin. Struct. Biol. 11, 629-634.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 629-634
    • Pellegrini, L.1
  • 157
    • 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. (2000) Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin. Nature 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
  • 158
    • 0037452728 scopus 로고    scopus 로고
    • Glycosaminoglycan binding and oligomerization are essential for the in vivo activity of certain chemokines
    • Proudfoot A.E., Handel T.M., Johnson Z. et al. (2003) Glycosaminoglycan binding and oligomerization are essential for the in vivo activity of certain chemokines. Proc. Natl Acad. Sci. USA 100, 1885-1890.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 1885-1890
    • Proudfoot, A.E.1    Handel, T.M.2    Johnson, Z.3
  • 159
    • 0032483520 scopus 로고    scopus 로고
    • Heparan sulphate oligosaccharides require 6-O sulphation for promotion of basic fibroblast factor mitogenic activity
    • Pye D., Vives R., Turnbul J.E., Hyde P. & Gallagher J.T. (1998) Heparan sulphate oligosaccharides require 6-O sulphation for promotion of basic fibroblast factor mitogenic activity. J. Biol. Chem. 273, 1183-1192.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1183-1192
    • Pye, D.1    Vives, R.2    Turnbul, J.E.3    Hyde, P.4    Gallagher, J.T.5
  • 160
    • 79954602896 scopus 로고    scopus 로고
    • Lacrimal gland development and Fgf10-Fgfr2b signalling are controlled by 2-O- and 6-O-sulfated heparan sulphate
    • Qu X., Carbe C., Tao C. et al. (2011) Lacrimal gland development and Fgf10-Fgfr2b signalling are controlled by 2-O- and 6-O-sulfated heparan sulphate. J. Biol. Chem. 286, 14435-14444.
    • (2011) J. Biol. Chem. , vol.286 , pp. 14435-14444
    • Qu, X.1    Carbe, C.2    Tao, C.3
  • 161
    • 15744403559 scopus 로고    scopus 로고
    • Structural insights into biological roles of protein-glycosaminoglycan interactions
    • Raman R., Sasisekharan V. & Sasisekharan R. (2005) Structural insights into biological roles of protein-glycosaminoglycan interactions. Chem. Biol. 12, 267-277.
    • (2005) Chem. Biol. , vol.12 , pp. 267-277
    • Raman, R.1    Sasisekharan, V.2    Sasisekharan, R.3
  • 162
    • 79952728727 scopus 로고    scopus 로고
    • Heparanase plays a dual role in driving hepatocyte growth factor (HGF) signaling by enhancing HGF expression and activity
    • Ramani V.C., Yang Y., Ren Y., Nan L. & Sanderson R. (2011) Heparanase plays a dual role in driving hepatocyte growth factor (HGF) signaling by enhancing HGF expression and activity. J. Biol. Chem. 286, 6490-6499.
    • (2011) J. Biol. Chem. , vol.286 , pp. 6490-6499
    • Ramani, V.C.1    Yang, Y.2    Ren, Y.3    Nan, L.4    Sanderson, R.5
  • 163
    • 0025835670 scopus 로고
    • Requirement of heparan sulfate for bFGF-mediated fibroblast growth and myoblast differentiation
    • Rapraeger A.C., Krufka A. & Olwin B.B. (1991) Requirement of heparan sulfate for bFGF-mediated fibroblast growth and myoblast differentiation. Science 252, 1705-1708.
    • (1991) Science , vol.252 , pp. 1705-1708
    • Rapraeger, A.C.1    Krufka, A.2    Olwin, B.B.3
  • 164
    • 0028216755 scopus 로고
    • Isolation of a neuronal cell surface receptor of heparin binding growth-associated molecule (HB-GAM). Identification as N-syndecan (syndecan-3)
    • Raulo E., Chernousov M.A., Carey D.J., Nolo R. & Rauvala H. (1994) Isolation of a neuronal cell surface receptor of heparin binding growth-associated molecule (HB-GAM). Identification as N-syndecan (syndecan-3). J. Biol. Chem. 269, 12999-13004.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12999-13004
    • Raulo, E.1    Chernousov, M.A.2    Carey, D.J.3    Nolo, R.4    Rauvala, H.5
  • 165
    • 0024317792 scopus 로고
    • An 18 kDa heparin-binding protein of developing brain that is distinct from fibroblast growth factors
    • Rauvala H. (1989) An 18 kDa heparin-binding protein of developing brain that is distinct from fibroblast growth factors. EMBO J. 8, 2933-2941.
    • (1989) EMBO J. , vol.8 , pp. 2933-2941
    • Rauvala, H.1
  • 167
    • 33747162038 scopus 로고    scopus 로고
    • Structural requirements for heparin/heparan sulfate binding to type V collagen
    • Ricard-Blum S., Beraud M., Raynal N., Farndale R.W. & Ruggiero F. (2006) Structural requirements for heparin/heparan sulfate binding to type V collagen. J. Biol. Chem. 281, 25195-25204.
    • (2006) J. Biol. Chem. , vol.281 , pp. 25195-25204
    • Ricard-Blum, S.1    Beraud, M.2    Raynal, N.3    Farndale, R.W.4    Ruggiero, F.5
  • 168
    • 0037942791 scopus 로고    scopus 로고
    • The binding of human glial cell line-derived neurotrophic factor to heparin and heparan sulfate: importance of 2-O-sulfate groups and effect on its interaction with its receptor, GFRα1
    • Rickard S.M., Mummery R.S., Mulloy B. & Rider C.C. (2003) The binding of human glial cell line-derived neurotrophic factor to heparin and heparan sulfate: importance of 2-O-sulfate groups and effect on its interaction with its receptor, GFRα1. Glycobiology 13, 419-426.
    • (2003) Glycobiology , vol.13 , pp. 419-426
    • Rickard, S.M.1    Mummery, R.S.2    Mulloy, B.3    Rider, C.C.4
  • 169
    • 33745439051 scopus 로고    scopus 로고
    • Heparin/heparan sulphate binding in the TGF-beta cytokine superfamily
    • Rider C.C. (2006) Heparin/heparan sulphate binding in the TGF-beta cytokine superfamily. Biochem. Soc. Trans. 34, 458-461.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 458-461
    • Rider, C.C.1
  • 170
    • 0035062394 scopus 로고    scopus 로고
    • The splice variants of vascular endothelial growth factor (VEGF) and their receptors
    • Robinson C.R. & Stringer S.E. (2006) The splice variants of vascular endothelial growth factor (VEGF) and their receptors. J. Cell Sci. 114, 853-865.
    • (2006) J. Cell Sci. , vol.114 , pp. 853-865
    • Robinson, C.R.1    Stringer, S.E.2
  • 171
    • 29644438840 scopus 로고    scopus 로고
    • Cooperative dimerization of fibroblast growth factor 1 (FGF1) upon a single heparin saccharide may drive the formation of 2:2:1 FGF1-FGFR2c-heparin ternary complexes
    • Robinson C.J., Harmer N.J., Goodger S.J., Blundell T.L. & Gallagher J.T. (2005) Cooperative dimerization of fibroblast growth factor 1 (FGF1) upon a single heparin saccharide may drive the formation of 2:2:1 FGF1-FGFR2c-heparin ternary complexes. J. Biol. Chem. 280, 42274-42282.
    • (2005) J. Biol. Chem. , vol.280 , pp. 42274-42282
    • Robinson, C.J.1    Harmer, N.J.2    Goodger, S.J.3    Blundell, T.L.4    Gallagher, J.T.5
  • 172
    • 33644977975 scopus 로고    scopus 로고
    • 165 - binding sites within heparan sulphate encompass two highly-sulphated domains and can be liberated by K5lyase
    • 165 - binding sites within heparan sulphate encompass two highly-sulphated domains and can be liberated by K5lyase. J. Biol. Chem. 281, 1731-1740.
    • (2006) J. Biol. Chem. , vol.281 , pp. 1731-1740
    • Robinson, C.R.1    Mulloy, B.2    Gallagher, J.T.3    Stringer, S.E.4
  • 173
    • 0034623075 scopus 로고    scopus 로고
    • Schwann cells synthesize Type V collagen that contains a novel α4 chain: molecular cloning, biochemical characterization, and high affinity heparin binding of α4 (v) collagen
    • Rothblum K., Tyler W.A., Stahl R.C. & Carey D.J. (2000) Schwann cells synthesize Type V collagen that contains a novel α4 chain: molecular cloning, biochemical characterization, and high affinity heparin binding of α4 (v) collagen. J. Biol. Chem. 275, 28208-28215.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28208-28215
    • Rothblum, K.1    Tyler, W.A.2    Stahl, R.C.3    Carey, D.J.4
  • 174
    • 10944226758 scopus 로고    scopus 로고
    • Constitutive release of α4 type V collagen N-terminal domain by Schwann cells and binding to cell surface and extracellular matrix heparan sulfate proteoglycans
    • Rothblum K., Stahl R.C. & Carey D.J. (2004) Constitutive release of α4 type V collagen N-terminal domain by Schwann cells and binding to cell surface and extracellular matrix heparan sulfate proteoglycans. J. Biol. Chem. 279, 51282-51288.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51282-51288
    • Rothblum, K.1    Stahl, R.C.2    Carey, D.J.3
  • 176
    • 0036341998 scopus 로고    scopus 로고
    • Cerebellar proteoglycans regulate sonic hedgehog responses during development
    • Rubin J.B., Choi Y. & Segal R.A. (2002) Cerebellar proteoglycans regulate sonic hedgehog responses during development. Development 129, 2223-2232.
    • (2002) Development , vol.129 , pp. 2223-2232
    • Rubin, J.B.1    Choi, Y.2    Segal, R.A.3
  • 177
    • 84859835237 scopus 로고    scopus 로고
    • A highly efficient tree structure for the biosynthesis of heparan sulfate accounts for the commonly observed disaccharides and suggests a mechanism for domain synthesis
    • Rudd T.R. & Yates E.A. (2012) A highly efficient tree structure for the biosynthesis of heparan sulfate accounts for the commonly observed disaccharides and suggests a mechanism for domain synthesis. Mol. BioSyst. 8, 1499-1506.
    • (2012) Mol. BioSyst. , vol.8 , pp. 1499-1506
    • Rudd, T.R.1    Yates, E.A.2
  • 178
    • 49749117434 scopus 로고    scopus 로고
    • The CXCL12gamma chemokine displays unprecedented structural and functional properties that make it a paradigm of chemoattractant proteins
    • Rueda P., Balabanian K., Lagane B. et al. (2008) The CXCL12gamma chemokine displays unprecedented structural and functional properties that make it a paradigm of chemoattractant proteins. PLoS ONE 3, e2543.
    • (2008) PLoS ONE , vol.3 , pp. e2543
    • Rueda, P.1    Balabanian, K.2    Lagane, B.3
  • 179
    • 84867255818 scopus 로고    scopus 로고
    • Homeostatic and tissue reparation defaults in mice carrying selective genetic invalidation of CXCL12/proteoglycan interactions
    • Rueda P., Richart A., Récalde A. et al. (2012) Homeostatic and tissue reparation defaults in mice carrying selective genetic invalidation of CXCL12/proteoglycan interactions. Circulation 126, 1882-1895.
    • (2012) Circulation , vol.126 , pp. 1882-1895
    • Rueda, P.1    Richart, A.2    Récalde, A.3
  • 180
    • 0037108152 scopus 로고    scopus 로고
    • Spatially restricted patterning cues provided by heparin-binding VEGF-A control blood vessel branching morphogenesis
    • Ruhrberg C., Gerhardt H., Golding M. et al. (2002) Spatially restricted patterning cues provided by heparin-binding VEGF-A control blood vessel branching morphogenesis. Genes Dev. 16, 2684-2698.
    • (2002) Genes Dev. , vol.16 , pp. 2684-2698
    • Ruhrberg, C.1    Gerhardt, H.2    Golding, M.3
  • 181
    • 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. (2001) Characterization of the stromal cell-derived factor-1alpha-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
  • 182
    • 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
  • 183
    • 0028321612 scopus 로고
    • Mapping the heparin-binding sites on type I collagen monomers and fibrils
    • San Antonio J.D., Lander A.D., Karnovski M.J., Slayter H.S. (1994) Mapping the heparin-binding sites on type I collagen monomers and fibrils. J. Cell Biol. 125, 1179-1188.
    • (1994) J. Cell Biol. , vol.125 , pp. 1179-1188
    • San Antonio, J.D.1    Lander, A.D.2    Karnovski, M.J.3    Slayter, H.S.4
  • 184
    • 0033635299 scopus 로고    scopus 로고
    • Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization
    • Schlessinger J., Plotnikov A.N., Ibrahimi O.A. et al. (2000) Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization. Mol. Cell 6, 743-750.
    • (2000) Mol. Cell , vol.6 , pp. 743-750
    • Schlessinger, J.1    Plotnikov, A.N.2    Ibrahimi, O.A.3
  • 186
    • 84878760333 scopus 로고    scopus 로고
    • HSulf sulfatases catalyze processive and oriented 6-O-desulfation of heparan sulfate that differentially regulates fibroblast growth factor activity
    • Seffouh A., Milz F., Przybylski C. et al. (2013) HSulf sulfatases catalyze processive and oriented 6-O-desulfation of heparan sulfate that differentially regulates fibroblast growth factor activity. FASEB J. 27, 2431-2439.
    • (2013) FASEB J. , vol.27 , pp. 2431-2439
    • Seffouh, A.1    Milz, F.2    Przybylski, C.3
  • 187
    • 0035782690 scopus 로고    scopus 로고
    • Genetic dissection of proteoglycan function in Drosophila and C. elegans
    • Selleck S.B. (2001) Genetic dissection of proteoglycan function in Drosophila and C. elegans. Semin. Cell Dev. Biol. 12, 127-134.
    • (2001) Semin. Cell Dev. Biol. , vol.12 , pp. 127-134
    • Selleck, S.B.1
  • 188
    • 77952920276 scopus 로고    scopus 로고
    • Characterization of the chemokine CXCL11-heparin interaction suggests two different affinities for glycosaminoglycans
    • Severin I.C., Gaudry J.P., Johnson Z. et al. (2010) Characterization of the chemokine CXCL11-heparin interaction suggests two different affinities for glycosaminoglycans. J. Biol.Chem. 285, 17713-17724.
    • (2010) J. Biol.Chem. , vol.285 , pp. 17713-17724
    • Severin, I.C.1    Gaudry, J.P.2    Johnson, Z.3
  • 189
    • 76949094151 scopus 로고    scopus 로고
    • Hs2st mediated kidney mesenchyme induction regulates early ureteric bud branching
    • Shah M.M., Sakurai H., Sweeney D.E. et al. (2010) Hs2st mediated kidney mesenchyme induction regulates early ureteric bud branching. Dev. Biol. 339, 354-365.
    • (2010) Dev. Biol. , vol.339 , pp. 354-365
    • Shah, M.M.1    Sakurai, H.2    Sweeney, D.E.3
  • 190
    • 0033559259 scopus 로고    scopus 로고
    • Crystal structure of a heparin-and integrin-binding segment of human fibronectin
    • Sharma A., Askari A.J., Humphries M.J., Jones E.Y. & Stuart D.I. (1999) Crystal structure of a heparin-and integrin-binding segment of human fibronectin. EMBO J. 18, 1468-1479.
    • (1999) EMBO J. , vol.18 , pp. 1468-1479
    • Sharma, A.1    Askari, A.J.2    Humphries, M.J.3    Jones, E.Y.4    Stuart, D.I.5
  • 191
    • 66449127755 scopus 로고    scopus 로고
    • Organ-specific heparan sulphate structural phenotypes
    • Shi X. & Zaia J. (2009) Organ-specific heparan sulphate structural phenotypes. J. Biol. Chem. 284, 11806-11814.
    • (2009) J. Biol. Chem. , vol.284 , pp. 11806-11814
    • Shi, X.1    Zaia, J.2
  • 192
    • 33746320397 scopus 로고    scopus 로고
    • Glycosaminoglycan modification of neuropilin-1 modulates VEGFR2 signaling
    • Shintani Y., Takashima S., Asano Y. et al. (2006) Glycosaminoglycan modification of neuropilin-1 modulates VEGFR2 signaling. EMBO J., 25, 3045-3055.
    • (2006) EMBO J. , vol.25 , pp. 3045-3055
    • Shintani, Y.1    Takashima, S.2    Asano, Y.3
  • 193
    • 84861878700 scopus 로고    scopus 로고
    • Glycosaminoglycan and chemokine/growth factor interactions
    • In: - (eds R. Lever, B. Mulloy, C.P. Page), Berlin, Heidelberg: Springer Verlag.
    • Shute J. (2012) Glycosaminoglycan and chemokine/growth factor interactions. In: Heparin - A Century of Progress, pp. 307-324 (eds R. Lever, B. Mulloy, C.P. Page ), Berlin, Heidelberg: Springer Verlag.
    • (2012) Heparin - A Century of Progress , pp. 307-324
    • Shute, J.1
  • 194
    • 48549084196 scopus 로고    scopus 로고
    • The activities of heparan sulfate and its analogue heparin are dictated by biosynthesis, sequence, and conformation
    • Skidmore M.A., Guimond S.E., Rudd T.R., Fernig D.G., Turnbull J.E. & Yates E.A. (2008) The activities of heparan sulfate and its analogue heparin are dictated by biosynthesis, sequence, and conformation. Connect. Tissue Res. 49, 140-144.
    • (2008) Connect. Tissue Res. , vol.49 , pp. 140-144
    • Skidmore, M.A.1    Guimond, S.E.2    Rudd, T.R.3    Fernig, D.G.4    Turnbull, J.E.5    Yates, E.A.6
  • 195
    • 76049122467 scopus 로고    scopus 로고
    • PDGF-A interactions with fibronectin reveal a critical role for heparan sulfate in directed cell migration during Xenopus gastrulation
    • Smith E.M., Mitsi M. & Nugent M.A. (2009) PDGF-A interactions with fibronectin reveal a critical role for heparan sulfate in directed cell migration during Xenopus gastrulation. PNAS 106, 21683-21688.
    • (2009) PNAS , vol.106 , pp. 21683-21688
    • Smith, E.M.1    Mitsi, M.2    Nugent, M.A.3
  • 196
    • 0032546954 scopus 로고    scopus 로고
    • Defining the interleukin binding domain of heparin sulphate
    • Spillmann D., Witt D. & Lindahl U. (1998) Defining the interleukin binding domain of heparin sulphate. J. Biol. Chem. 273, 15847-15893.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15847-15893
    • Spillmann, D.1    Witt, D.2    Lindahl, U.3
  • 197
    • 77953296953 scopus 로고    scopus 로고
    • Extended N-sulfated domains reside at the nonreducing end of heparan sulfate chains
    • Staples G.O., Shi X. & Zaia J. (2010) Extended N-sulfated domains reside at the nonreducing end of heparan sulfate chains. J. Biol. Chem. 285, 18336-18343.
    • (2010) J. Biol. Chem. , vol.285 , pp. 18336-18343
    • Staples, G.O.1    Shi, X.2    Zaia, J.3
  • 198
    • 84898069475 scopus 로고    scopus 로고
    • Fibroblast growth factor-based signaling through synthetic heparan sulfate blocks copolymers studied using high cell density three-dimensional cell printing
    • Sterner E., Masuko S., Li G. et al. (2014) Fibroblast growth factor-based signaling through synthetic heparan sulfate blocks copolymers studied using high cell density three-dimensional cell printing. J. Biol. Chem. 289, 9754-9765.
    • (2014) J. Biol. Chem. , vol.289 , pp. 9754-9765
    • Sterner, E.1    Masuko, S.2    Li, G.3
  • 199
    • 0030796217 scopus 로고    scopus 로고
    • Specific binding of the chemokine platelet factor 4 to heparan sulfate
    • Stringer S.E. & Gallagher J.T. (1997) Specific binding of the chemokine platelet factor 4 to heparan sulfate. J. Biol. Chem. 272, 20508-20514.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20508-20514
    • Stringer, S.E.1    Gallagher, J.T.2
  • 200
    • 0036721004 scopus 로고    scopus 로고
    • Characterization of the binding site on heparan sulfate for macrophage inflammatory protein 1a
    • Stringer S.E., Forster M.J., Mulloy B., Bishop C.R., Graham G.J. & Gallagher J.T. (2002) Characterization of the binding site on heparan sulfate for macrophage inflammatory protein 1a. Blood 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
  • 201
    • 0037443392 scopus 로고    scopus 로고
    • Identification of an MIP-1α-binding heparan sulfate oligosaccharide that supports long-term in vitro maintenance of human LTC-ICs
    • Stringer S.E., Nelson M.S. & Gupta P. (2003) Identification of an MIP-1α-binding heparan sulfate oligosaccharide that supports long-term in vitro maintenance of human LTC-ICs. Blood 101, 2243-2245.
    • (2003) Blood , vol.101 , pp. 2243-2245
    • Stringer, S.E.1    Nelson, M.S.2    Gupta, P.3
  • 202
    • 0033794318 scopus 로고    scopus 로고
    • Recent advances in the study of the biosynthesis and functions of sulfated glycosaminoglycans
    • Sugahara K. & Kitagawa H. (2000) Recent advances in the study of the biosynthesis and functions of sulfated glycosaminoglycans. Curr. Opin. Struct. Biol. 10, 518-527.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 518-527
    • Sugahara, K.1    Kitagawa, H.2
  • 203
    • 44849135267 scopus 로고    scopus 로고
    • 6-O-sulfation of heparan sulfate differentially regulates various FGFs-dependent signalling in culture
    • Sugaya N., Habuchi H., Nagai N., Ashikari-Hada S. & Kimata K. (2008) 6-O-sulfation of heparan sulfate differentially regulates various FGFs-dependent signalling in culture. J. Biol. Chem. 283, 10366-10376.
    • (2008) J. Biol. Chem. , vol.283 , pp. 10366-10376
    • Sugaya, N.1    Habuchi, H.2    Nagai, N.3    Ashikari-Hada, S.4    Kimata, K.5
  • 204
    • 0032560482 scopus 로고    scopus 로고
    • Defining the domains of type I collagen involved in heparin-binding and endothelial tube formation
    • Sweeney S.M., Guy C.A., Fields G.B. & San Antonio J.D. (1998) Defining the domains of type I collagen involved in heparin-binding and endothelial tube formation. Proc. Natl Acad. Sci. USA 90, 7275-7280.
    • (1998) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7275-7280
    • Sweeney, S.M.1    Guy, C.A.2    Fields, G.B.3    San Antonio, J.D.4
  • 205
    • 0035929624 scopus 로고    scopus 로고
    • Interactions of fibrillin-1 with heparin/heparan sulphate: implications for microfibrillar assembly
    • Tiedemann K., Bätge B., Muller P.K. & Reinhardt D.P. (2001) Interactions of fibrillin-1 with heparin/heparan sulphate: implications for microfibrillar assembly. J. Biol. Chem. 276, 36035-36042.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36035-36042
    • Tiedemann, K.1    Bätge, B.2    Muller, P.K.3    Reinhardt, D.P.4
  • 206
    • 48449091794 scopus 로고    scopus 로고
    • Glycosaminoglycan-mediated coacervation of tropoelastin abolishes the critical concentration, accelerates coacervate formation, and facilitates spherule fusion: implications for tropoelastin microassembly
    • Tu Y. & Weiss A.S. (2008) Glycosaminoglycan-mediated coacervation of tropoelastin abolishes the critical concentration, accelerates coacervate formation, and facilitates spherule fusion: implications for tropoelastin microassembly. Biomacromolecules 9, 1739-1744.
    • (2008) Biomacromolecules , vol.9 , pp. 1739-1744
    • Tu, Y.1    Weiss, A.S.2
  • 207
    • 0025186852 scopus 로고
    • Molecular organization of heparan sulphate from human skin fibroblasts
    • Turnbull J.E. & Gallagher J.T. (1990) Molecular organization of heparan sulphate from human skin fibroblasts. Biochem. J. 265, 715-724.
    • (1990) Biochem. J. , vol.265 , pp. 715-724
    • Turnbull, J.E.1    Gallagher, J.T.2
  • 208
    • 0026016084 scopus 로고
    • Distribution of iduronate 2-sulphate residues in heparan sulphate. Evidence for an ordered polymeric structure
    • Turnbull J.E. & Gallagher J.T. (1991) Distribution of iduronate 2-sulphate residues in heparan sulphate. Evidence for an ordered polymeric structure. Biochem. J. 273, 553-559.
    • (1991) Biochem. J. , vol.273 , pp. 553-559
    • Turnbull, J.E.1    Gallagher, J.T.2
  • 209
    • 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. (1992) Identification of the basic fibroblast growth factor binding sequence in fibroblast heparan sulfate. J. Biol. Chem. 267, 10337-10341.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10337-10341
    • Turnbull, J.E.1    Fernig, D.G.2    Ke, Y.3    Wilkinson, M.C.4    Gallagher, J.T.5
  • 210
    • 77951818493 scopus 로고    scopus 로고
    • Differential scanning fluorimetry measurement of protein stability changes upon binding to glycosaminoglycans: a screening test for binding specificity
    • Uniewicz K.A., Ori A., Xu R. et al. (2010) Differential scanning fluorimetry measurement of protein stability changes upon binding to glycosaminoglycans: a screening test for binding specificity. Anal. Chem. 82, 3796-3802.
    • (2010) Anal. Chem. , vol.82 , pp. 3796-3802
    • Uniewicz, K.A.1    Ori, A.2    Xu, R.3
  • 212
    • 0035895985 scopus 로고    scopus 로고
    • Characterization of type XI collagen-glycosaminoglycan interactions
    • Vaughan-Thomas A., Young R.D., Phillips A.C. & Duance V.C. (2001) Characterization of type XI collagen-glycosaminoglycan interactions. J. Biol. Chem. 276, 5303-5309.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5303-5309
    • Vaughan-Thomas, A.1    Young, R.D.2    Phillips, A.C.3    Duance, V.C.4
  • 213
    • 0037126683 scopus 로고    scopus 로고
    • A kinetics and modelling study of RANTES (9-68) binding to heparin reveals a mechanism of cooperative oligomerization
    • Vives R.R., Sadir R., Imberty A., Rencurosi A. & Lortat-Jacob H. (2002) A kinetics and modelling 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
    • Vives, R.R.1    Sadir, R.2    Imberty, A.3    Rencurosi, A.4    Lortat-Jacob, H.5
  • 214
    • 1242272044 scopus 로고    scopus 로고
    • Domain-specific modification of heparan sulfate by Qsulf1 modulates the binding of the bone morphogenetic protein antagonist noggin
    • Viviano B.L., Paine-Saunders S., Gasiunas N., Gallagher J.T. & Saunders S. (2004) Domain-specific modification of heparan sulfate by Qsulf1 modulates the binding of the bone morphogenetic protein antagonist noggin. J. Biol. Chem. 279, 5604-5611.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5604-5611
    • Viviano, B.L.1    Paine-Saunders, S.2    Gasiunas, N.3    Gallagher, J.T.4    Saunders, S.5
  • 215
    • 45449112808 scopus 로고    scopus 로고
    • Nanoscale organization of hedgehog is essential for long-range signalling
    • Vyas N., Goswami D., Manonmani A. et al. (2008) Nanoscale organization of hedgehog is essential for long-range signalling. Cell 133, 1214-1227.
    • (2008) Cell , vol.133 , pp. 1214-1227
    • Vyas, N.1    Goswami, D.2    Manonmani, A.3
  • 216
    • 0029846488 scopus 로고    scopus 로고
    • Structural domains of heparan sulphate for specific recognition of the C-terminal heparin-binding domain of human plasma fibronectin (HEP II)
    • Walker A. & Gallagher J.T. (1996) Structural domains of heparan sulphate for specific recognition of the C-terminal heparin-binding domain of human plasma fibronectin (HEP II). Biochem. J. 317, 871-877.
    • (1996) Biochem. J. , vol.317 , pp. 871-877
    • Walker, A.1    Gallagher, J.T.2
  • 217
    • 0028039867 scopus 로고
    • Specific heparan sulfate saccharides mediate the activity of basic fibroblast growth factor
    • Walker A., Turnbull J.E. & Gallagher J.T. (1994) Specific heparan sulfate saccharides mediate the activity of basic fibroblast growth factor. J. Biol. Chem. 269, 931-935.
    • (1994) J. Biol. Chem. , vol.269 , pp. 931-935
    • Walker, A.1    Turnbull, J.E.2    Gallagher, J.T.3
  • 218
    • 33846005181 scopus 로고    scopus 로고
    • Isoform-specific heparan sulfate binding within the amino-terminal noncollagenous domain of collagen α1 (XI)
    • Warner L.R., Brown R.J., Yingst S.M.C. & Oxford J.T. (2006) Isoform-specific heparan sulfate binding within the amino-terminal noncollagenous domain of collagen α1 (XI). J. Biol. Chem. 281, 39507-39516.
    • (2006) J. Biol. Chem. , vol.281 , pp. 39507-39516
    • Warner, L.R.1    Brown, R.J.2    Yingst, S.M.C.3    Oxford, J.T.4
  • 219
    • 84885348475 scopus 로고    scopus 로고
    • Structural insights into proteoglycan-shaped Hedgehog signalling
    • Whalen D.M., Malinauskas T., Gilbert R.J.C. & Siebold C. (2013) Structural insights into proteoglycan-shaped Hedgehog signalling. PNAS 110, 16420-16425.
    • (2013) PNAS , vol.110 , pp. 16420-16425
    • Whalen, D.M.1    Malinauskas, T.2    Gilbert, R.J.C.3    Siebold, C.4
  • 221
    • 84902215812 scopus 로고    scopus 로고
    • Demystifying heparan sulfate-protein interactions
    • Xu D. & Esko J.D. (2014) Demystifying heparan sulfate-protein interactions. Annu. Rev. Biochem. 83, 129-157.
    • (2014) Annu. Rev. Biochem. , vol.83 , pp. 129-157
    • Xu, D.1    Esko, J.D.2
  • 222
    • 78650939979 scopus 로고    scopus 로고
    • Heparan sulfate regulates VEGF165- and VEGF121-mediated vascular hyperpermeability
    • Xu D., Fuster M.M., Lawrence R. & Esko J.D. (2011) Heparan sulfate regulates VEGF165- and VEGF121-mediated vascular hyperpermeability. J. Biol. Chem. 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
  • 223
    • 84869204033 scopus 로고    scopus 로고
    • Diversification of the structural determinants of fibroblast growth factor-heparin interactions: implications for binding specificity
    • Xu R., Ori A., Rudd T.R. et al. (2012a) Diversification of the structural determinants of fibroblast growth factor-heparin interactions: implications for binding specificity. J. Biol. Chem. 287, 40061-40073.
    • (2012) J. Biol. Chem. , vol.287 , pp. 40061-40073
    • Xu, R.1    Ori, A.2    Rudd, T.R.3
  • 224
    • 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. (2012b) 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
  • 225
    • 77954055939 scopus 로고    scopus 로고
    • Shaping morphogen gradients by proteoglycans
    • Yan D. & Lin X. (2009) Shaping morphogen gradients by proteoglycans. Cold. Spring. Harb. Perspect. Biol. 1, a002493.
    • (2009) Cold. Spring. Harb. Perspect. Biol. , vol.1 , pp. a002493
    • Yan, D.1    Lin, X.2
  • 226
    • 0025976838 scopus 로고
    • Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor
    • Yayon A., Klagsbrun M., Esko J.D., Leder P. & Ornitz D.M. (1991) Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor. Cell 64, 841-848.
    • (1991) Cell , vol.64 , pp. 841-848
    • Yayon, A.1    Klagsbrun, M.2    Esko, J.D.3    Leder, P.4    Ornitz, D.M.5
  • 227
    • 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. et al. (2005) Chemokine-glycosaminoglycan binding: specificity for CCR2 ligand binding to highly sulfated oligosaccharides using FTICR mass spectrometry. J. Biol. Chem. 280, 32200-32208.
    • (2005) J. Biol. Chem. , vol.280 , pp. 32200-32208
    • Yu, Y.1    Sweeney, M.D.2    Saad, O.M.3
  • 228
  • 229
    • 0032518610 scopus 로고    scopus 로고
    • The solution structure of the N-terminal domain of hepatocyte growth factor reveals a potential heparin-binding site
    • Zhou H., Mazzulla M.J., Kaufman J.D. et al. (1998) The solution structure of the N-terminal domain of hepatocyte growth factor reveals a potential heparin-binding site. Structure 6, 109-116.
    • (1998) Structure , vol.6 , pp. 109-116
    • Zhou, H.1    Mazzulla, M.J.2    Kaufman, J.D.3
  • 230
    • 0029034348 scopus 로고
    • Sulfated oligosaccharides promote hepatocyte growth factor association and govern its mitogenic activity
    • Zioncheck T.F., Richardson L., Liu J. et al. (1995) Sulfated oligosaccharides promote hepatocyte growth factor association and govern its mitogenic activity. J. Biol. Chem. 270, 16871-16878.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16871-16878
    • Zioncheck, T.F.1    Richardson, L.2    Liu, J.3
  • 231
    • 0037234754 scopus 로고    scopus 로고
    • Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor
    • Zou P., Zou K., Muramatsu H. et al. (2003) Glycosaminoglycan structures required for strong binding to midkine, a heparin-binding growth factor. Glycobiology 13, 35-42.
    • (2003) Glycobiology , vol.13 , pp. 35-42
    • Zou, P.1    Zou, K.2    Muramatsu, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.