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Robert Friesel
Researcher at Maine Medical Center
Publications - 90
Citations - 7002
Robert Friesel is an academic researcher from Maine Medical Center. The author has contributed to research in topics: Fibroblast growth factor & Signal transduction. The author has an hindex of 40, co-authored 88 publications receiving 6733 citations. Previous affiliations of Robert Friesel include Baylor College of Medicine & American Red Cross.
Papers
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Journal ArticleDOI
Molecular mechanisms of angiogenesis: fibroblast growth factor signal transduction.
Robert Friesel,Thomas Maciag +1 more
TL;DR: Recent insights into the pathways used for the regulation of FGF secretion and cellular trafficking as well as signaling by FGFRs are described.
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Heparin binds endothelial cell growth factor, the principal endothelial cell mitogen in bovine brain
TL;DR: Data indicate that ECGF is the principal mitogen for endothelial cells from bovine brain, that heparin affinity chromatography may be used to purify and concentrate ECGF, and that the affinity of ECGF forHeparin may have structural and perhaps biological significance.
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Identification of Sef, a novel modulator of FGF signalling.
TL;DR: The identification of a novel modulator of FGF signal transduction, sef, isolated from a zebrafish embryo library through an in situ hybridization screen is reported, suggesting that Sef is required to limit FGF signalling during development.
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The Role of Fibroblast Growth Factors in Tumor Growth
Murray Korc,Robert Friesel +1 more
TL;DR: FGF has the potential to overcome chemotherapy resistance highlighting that chemotherapy may be more effective when used in combination with FGF inhibitor therapy and FGFRs have variable activity in promoting angiogenesis.
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Interaction of endothelial cell growth factor with heparin: characterization by receptor and antibody recognition.
Alain B. Schreiber,John Kenney,William J. Kowalski,Robert Friesel,Tevie Mehlman,Thomas Maciag +5 more
TL;DR: The data suggest that the association between heparin and ECGF induces a conformational change in the polypeptide that increases or stabilizes the biological activity of the mitogen.