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    Diversity Does Make a Difference: Fibroblast Growth Factor - HeparinInteractions

    Author
    Faham, S.; Linhardt, Robert J.; Rees, D.C.
    ORCID
    https://orcid.org/0000-0003-2219-5833
    Thumbnail
    Other Contributors
    Date Issued
    1998
    Subject
    Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
    Degree
    Terms of Use
    In Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/;
    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.
    Metadata
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    URI
    https://doi.org/10.1016/S0959-440X(98)80147-4; https://hdl.handle.net/20.500.13015/5889
    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.;
    Description
    Current Opinions in Structural Biology, 8, 578-586; Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
    Department
    The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
    Relationships
    The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; https://harc.rpi.edu/;
    Access
    https://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/S0959-440X(98)80147-4;
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    • Linhardt Research Labs Papers

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