The structures of snake venom metalloproteases (SVMPs) are proposed to be useful models
to understand the structural and functional relationship of ADAM (a disintegrin and …

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

AaHIV, a P-III-type snake venom metalloproteinase (SVMP), consists of metalloproteinase/
disintegrin/cysteine-rich (MDC) domains and is homologous to a disintegrin and …

A disintegrin and metalloproteinase (ADAM) family proteins constitute a major class of
membrane-anchored multidomain proteinases that are responsible for the shedding of cell …

Snake venom disintegrins represent a family of RGD (Arg-Gly-Asp) or KGD (Lys-Gly-Asp)-
containing proteins which have been reported to be unique and potentially useful tools not …

A disintegrin and metalloproteinase (ADAM) family of proteins constitutes a major class of
mammalian membrane-bound sheddases that are responsible for the processing of cell …

ADAMs (ad isintegrin a nd m etalloproteinase) are sheddases possessing extracellular m
etalloproteinase/d isintegrin/c ysteine‐rich (MDC) domains. ADAMs uniquely display both …

Snake venom metalloproteinases (SVMPs) are members of the Reprolysin family of
metalloproteinases to which the ADAM (a disintegrin and metalloproteinase) proteins also …

A new metalloproteinase–disintegrin, named Jerdonitin, was purified from Trimeresurus
jerdonii venom with a molecular weight of 36kDa on SDS–PAGE. It dose-dependently …

Snake venom metalloproteinases (SVMPs) are zinc-dependent enzymes responsible for
most symptoms of human envenoming. Like matrix metalloproteinases (MMPs) and a …