Keywordssnake venom; viperids; metalloproteinases; hemorrhage; capillary vessels; basement membrane; type IV collagen; ADAM; disintegrin; SVMP; snake venom; metalloproteinase; disintegrin; ADAM; ADAMTS; MDC; reprolysin; adamalysin; shedding; crystal structure; snake venom; metalloproteinase; post-translational processing; enzyme inhibitor; hemorrhage; Snake venom toxin multi-gene family; snake venom metalloproteinase; genomic organization of SVMP genes; PII-SVMP; PI-SVMP; gene duplication; intronic retroelements; intronization; cross-linking; hydrogen/deuterium exchange; mass spectrometry; metalloendopeptidase inhibitor; modeling; natural immunity; natural resistance; snake venom; structure; therapeutic application; procoagulant; anticoagulant; factor X activator; prothrombin activator; platelet aggregation; fibrinolytic; exosites in enzymes; allosteric sites; snake venom metalloproteinases; PII SVMP homologues; disintegrin domain; zinc-binding motif; hemorrhagic activity; platelet aggregation; proteinase activity; proteomics; exudate; extracellular matrix; basement membrane; hemorrhage; snake venom metalloproteinases; FACITs; snake venom metalloproteinases (SVMPs); TLR4; damage associated molecular pattern molecules (DAMPs); exudate; increased vascular permeability; snake; genome; genomics; king cobra; reptile; Malayan pit viper; snake venom metalloproteinases; snake venom metalloproteinase inhibitors; Russell’s viper; viper venom; n/a
