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All rights reserved. http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Large Corpus Document http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RAwUYnqXaRgpofXfHo0o0HHu574MNvUl2Aabb-hT77wts#_6 http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/pav/version 20131211 http://www.tkuhn.ch/bel2nanopub/RAwUYnqXaRgpofXfHo0o0HHu574MNvUl2Aabb-hT77wts#_5 http://www.w3.org/ns/prov#value Gangliosides bind FGF1, FGF2, and FGF4 via negatively charged Neu-Ac residues [147,148]. In the extracellular environment, gangliosides compete with free heparin for the binding to the growth factor. On endothelial cells, free gangliosides prevent the binding of FGF2 to FGFRs and HSPGs, thus inhibiting FGF2-mediated cell proliferation [147]. Ganglioside GM1 is expressed on the endothelial cell surface and binds FGF2 with an affinity that is significantly higher than that of its free counterpart (Table 1). 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