Nicholas W. Shworak

TL;DR: It is shown that heparan sulfate modified by a subset of the multiple D-glucosaminyl 3-O-sulfotransferase isoforms provides sites for the binding of a third viral glycoprotein, gD, and for initiation of HSV-1 entry.

TL;DR: The current state of knowledge about the structure and the biosynthesis of HSPGs are outlined as well as interactions of these components with growth factors, enzymes, and protease inhibitors are described to provide a conceptual framework for elucidating the roles of H SPGs in other biologic systems.

TL;DR: The reiteration and conservation of the3-OST sulfotransferase domain suggest that this structure is a self-contained functional unit, and the extensive number of 3OST genes with diverse expression patterns of multiple transcripts suggests that the novel 3-OST enzymes, like 3-ost-1, regulate important biologic properties of heparan sulfate proteoglycans.

TL;DR: Genetic evidence is provided for the critical role of the diaphragms in fenestrated capillaries in the maintenance of blood composition by deletion of the PV1-encoding Plvap gene in mice.

TL;DR: The primary sequences of internal peptides obtained from HSPGinact core proteins and the NH2-terminal sequence analyses demonstrate that the 30-kDa component is a previously unidentified species, designated as ryudocan, which is the rat homolog of syndecan.