B
Benito Casu
Researcher at Massachusetts Institute of Technology
Publications - 89
Citations - 7088
Benito Casu is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Heparin & Heparan sulfate. The author has an hindex of 40, co-authored 89 publications receiving 6804 citations. Previous affiliations of Benito Casu include Federal University of Rio Grande do Norte & University of Brescia.
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Journal ArticleDOI
Structure-activity relationship in heparin : a synthetic pentasaccharide with high affinity for antithrombin III and eliciting high anti-factor Xa activity
TL;DR: Results confirm that the synthetic pentasaccharide with the above structure corresponds to the actual minimal sequence required in heparin for binding to AT-III.
Journal ArticleDOI
Oversulfated chondroitin sulfate is a contaminant in heparin associated with adverse clinical events.
Marco Guerrini,Daniela Beccati,Zachary Shriver,Annamaria Naggi,Karthik Viswanathan,Antonella Bisio,Ishan Capila,Jonathan C. Lansing,Sara Guglieri,Blair A. Fraser,Ali Al-Hakim,Nur Sibel Gunay,Zhenqing Zhang,Luke Robinson,Lucinda F. Buhse,Moheb Nasr,Janet Woodcock,Robert Langer,Ganesh Venkataraman,Robert J. Linhardt,Benito Casu,Giangiacomo Torri,Ram Sasisekharan +22 more
TL;DR: Through detailed structural analysis, the contaminant was found to contain a disaccharide repeat unit of glucuronic acid linked β1→3 to a β-N-acetylgalactosamine, indicative of an allergic-type reaction.
Book ChapterDOI
Structure and biological activity of heparin
TL;DR: The structure and biological activity of heparin are described, being an alternating copolymer of a hexosamine and an alduronic acid, and the repeating disaccharide units constituting the largest fraction of the most common GAG are elaborated in the chapter.
Book ChapterDOI
Structure and biological interactions of heparin and heparan sulfate.
Benito Casu,Ulf Lindahl +1 more
TL;DR: This chapter discusses the structural aspects and structure–activity relationships of heparin/heparan sulfate (HS), and the molecular mechanism behind the anticoagulant/antithrombotic effects.
Journal ArticleDOI
Heparanase: structure, biological functions, and inhibition by heparin-derived mimetics of heparan sulfate.
TL;DR: Heparanase upregulation correlates with increased tumor vascularity and poor postoperative survival of cancer patients, and the unexpected identification of a single functional heparanase is suggested that the enzyme is a promising target for anti-cancer and anti-inflammatory drug development.