Snake venom metalloproteinases (SVMPs) represent a diverse group of multi-domain
proteins with several biological activities such as the ability to induce hemorrhage …

Nature endowed snakes with a lethal secretion known as venom, which has been fine-tuned
over millions of years of evolution. Snakes utilize venom to subdue their prey and to survive …

The Handbook of Venoms and Toxins of Reptiles offers" one-stop shop**" to all biologists,
biochemists, toxicologists, physicians, clinicians, and epidemiologists, and informed …

Metalloproteinases are among the most abundant toxins in many Viperidae venoms. Snake
venom metalloproteinases (SVMPs) are the primary factors responsible for hemorrhage and …

Disintegrins are small cysteine-rich proteins found in a variety of snake venom. These
proteins selectively modulate integrin function, heterodimeric receptors involved in cell-cell …

Disintegrins, a family of polypeptides released in the venoms of viperid snakes (vipers and
rattlesnakes) by the proteolytic processing of multidomain metalloproteinases, selectively …

Lebein, is an heterodimeric disintegrin isolated from Macrovipera lebetina snake venom that
was previously characterized as an inhibitor of ADP‐induced platelet aggregation. In this …

Disulfide-rich domains are small protein domains whose global folds are stabilized primarily
by the formation of disulfide bonds and, to a much lesser extent, by secondary structure and …

Angiogenesis is the fundamental process by which new blood vessels are formed. Extensive
research has shown that this event can be co-opted by tumors to ensure their growth …

Disintegrins are small peptides possessing a tripeptide motif capable of binding to integrins.
These were first isolated from viper venoms and are now also found in many other …