EC Number |
Title |
Organism |
---|
3.4.24.42 | Amino acid sequence of a Crotalus atrox venom metalloproteinase which cleaves type IV collagen and gelatin |
Crotalus atrox |
3.4.24.42 | Atrolysin C |
Crotalus atrox |
3.4.24.42 | Atrolysins: metalloproteinases from Crotalus atrox venom |
Crotalus atrox |
3.4.24.42 | Biochemical characterization of hemorrhagic toxins with fibrinogenase activity isolated from Crotalus ruber ruber venom |
Crotalus ruber ruber |
3.4.24.42 | Characterization of two hemorrhagic zinc proteinases, toxin c and toxin d, from western diamondback rattlesnake (Crotalus atrox) venom |
Crotalus atrox |
3.4.24.42 | Comparative analysis of the catalytic domain of hemorrhagic and non-hemorrhagic snake venom metallopeptidases using bioinformatic tools |
Crotalus atrox |
3.4.24.42 | Hemorrhagic toxins from Western diamondback rattlesnake (Crotalus atrox) venom: isolation and characterization of five toxins and the role of zinc in hemorrhagic toxin e |
Crotalus atrox |
3.4.24.42 | Interaction of the cysteine-rich domain of snake venom metalloproteinases with the A1 domain of von Willebrand factor promotes site-specific proteolysis of von Willebrand factor and inhibition of von Willebrand factor-mediated platelet aggregation |
Crotalus atrox |
3.4.24.42 | Molecular models of the Mojave rattlesnake (Crotalus scutulatus scutulatus) venom metalloproteinases reveal a structural basis for differences in hemorrhagic activities |
Crotalus scutulatus scutulatus |
3.4.24.42 | Molecular models of the Mojave rattlesnake (Crotalus scutulatus scutulatus) venom metalloproteinases reveal a structural basis for differences in hemorrhagic activities |
Crotalus atrox |