| Literature DB >> 9613830 |
L Kinsella1, H L Chen, J A Smith, P S Rudland, D G Fernig.
Abstract
We have examined structure-function relationships that have been proposed to account for the heparin-binding properties of basic fibroblast growth factor and its receptor, FGFR-1, using synthetic peptides, DNA synthesis assays and binding assays in a resonant mirror biosensor. The results suggest that the interaction of FGFR-1 with heparin may not be physiologically relevant and that the site of interaction of the polysaccharide on bFGF is more complex than has been anticipated.Entities:
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Year: 1998 PMID: 9613830 DOI: 10.1023/a:1006986104865
Source DB: PubMed Journal: Glycoconj J ISSN: 0282-0080 Impact factor: 2.916