R
Ronald E. Hileman
Researcher at University of Iowa
Publications - 28
Citations - 3837
Ronald E. Hileman is an academic researcher from University of Iowa. The author has contributed to research in topics: Heparan sulfate & Heparin. The author has an hindex of 21, co-authored 28 publications receiving 3698 citations. Previous affiliations of Ronald E. Hileman include University of Nebraska–Lincoln.
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Journal ArticleDOI
Dengue virus infectivity depends on envelope protein binding to target cell heparan sulfate
Yaping Chen,Terry Maguire,Ronald E. Hileman,Jonathan R. Fromm,Jeffrey D. Esko,Robert J. Linhardt,Rory M. Marks +6 more
TL;DR: Heparin, highly sulfated heparan sulfate, and the polysulfonate pharmaceutical Suramin effectively prevented dengue virus infection of target cells, indicating that the envelope protein-target cell receptor interaction is a critical determinant of infectivity.
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Heparin structure and interactions with basic fibroblast growth factor.
TL;DR: No significant conformational change in bFGF occurred upon heparin oligosaccharide binding, which suggests that heparIn primarily serves to juxtapose components of the FGF signal transduction pathway.
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Glycosaminoglycan‐protein interactions: definition of consensus sites in glycosaminoglycan binding proteins
TL;DR: A new consensus sequence TXXBXXTBXXXTBB is described, where turns bring basic interacting amino acid residues into proximity, indicating that protein‐GAG interactions play a prominent role in cell‐cell interaction and cell growth.
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Differences in the Interaction of Heparin with Arginine and Lysine and the Importance of these Basic Amino Acids in the Binding of Heparin to Acidic Fibroblast Growth Factor
Jonathan R. Fromm,Ronald E. Hileman,Elizabeth E.O. Caldwell,John M. Weiler,Robert J. Linhardt +4 more
TL;DR: It is suggested that the greater affinity of the guanidino cation for sulfate in GAGs is probably due to stronger hydrogen bonding and a more exothermic electrostatic interaction, which can be rationalized by soft acid, soft base concepts.
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Structural differences and the presence of unsubstituted amino groups in heparan sulphates from different tissues and species.
Toshihiko Toida,Hisao Yoshida,Hidenao Toyoda,Ichiro Koshiishi,Toshio Imanari,Ronald E. Hileman,Jonathan R. Fromm,Robert J. Linhardt +7 more
TL;DR: A comparison of heparan sulphate chains isolated from various porcine and bovine tissues is presented to suggest that structural differences may play a role in important biological events controlled by heparin sulphate in different tissues.