Diversity Does Make a Difference: Fibroblast Growth Factor - HeparinInteractions

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Authors
Faham, S.
Linhardt, Robert J.
Rees, D.C.
Issue Date
1998
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Article
Language
ENG
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Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
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Abstract
Fibroblast growth factors (FGFs) are members of a protein family with a broad range of biological activities. The best characterized FGFs interact with two distinct extracellular receptors — a transmembrane tyrosine kinase FGF receptor (FGFR) and a heparan sulfate-related proteoglycan of the extracellular matrix. These components form a FGF—FGFR—proteoglycan complex that activates the FGF-mediated signal transduction process through FGFR dimerization. Recent crystal structure determinations of FGF—heparin complexes have provided insights into both the interactions between these components and the role of heparin-like proteoglycans in FGF function. Future advances in this field will benefit enormously from an ability to specifically prepare homogenous heparin-based oligosaccharides of defined sequence for use in biochemical and structural studies of FGF and many other systems.
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Current Opinions in Structural Biology, 8, 578-586
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Full Citation
Diversity Does Make a Difference: Fibroblast Growth Factor - HeparinInteractions, S. Faham, R.J. Linhardt, D.C. Rees, Current Opinionsin Structural Biology, 8, 578-586 1998.
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