Mark C. Wilkinson

This study characterizes recombinant disintegrins from Echis species, showing distinct inhibitory effects on platelet aggregation and endothelial cell migration.

This study investigates the roles of disintegrin-like and cysteine-rich domains in substrate recognition and catalytic activity of PIII snake venom metalloproteinases using recombinant variants and functional assays.

The paper develops a method to produce and activate purified snake venom metalloproteinases (SVMPs) using recombinant zymogens, enabling detailed biochemical and functional analysis.

This study identifies snake venom metalloproteinases (SVMPs) as the main cytotoxic agents in two African viper venoms and shows EDTA can inhibit their effects.

The paper characterizes two distinct serine protease groups in puff adder venom, revealing novel gelatinase activity and structural insights into their substrate specificity and functional roles.

This paper develops DC-174, an oral small molecule that inhibits snake venom metalloproteinases and shows efficacy in a mouse model of envenoming.

This study compares venom variation in Bitis arietans across three regions using transcriptomics, chromatography, and functional assays, finding substantial toxin variation but no major impact on antivenom efficacy.

This study characterizes the diversity and bioactivity of venom metalloproteases in puff adders, identifying distinct forms with varying enzymatic activities and proposing a new nomenclature for the dominant SVMPs.