EC Number   |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
|---|
   3.4.24.42 | 31270 |
Primary structure of a hemorrhagic metalloproteinase, HT-2, isolated from the venom of Crotalus ruber ruber |
J. Biochem. |
108 |
711-719 |
1990 |
Crotalus ruber ruber |
2081731 |
| 3.4.24.42 | 667447 |
Structural features of the reprolysin atrolysin C and tissue inhibitors of metalloproteinases (TIMPs) interaction |
Biochem. Biophys. Res. Commun. |
347 |
641-648 |
2006 |
Crotalus atrox |
16842758 |
| 3.4.24.42 | 31269 |
Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d) |
Proc. Natl. Acad. Sci. USA |
91 |
8447-8451 |
1994 |
Crotalus atrox |
8078901 |
| 3.4.24.42 | 31260 |
Studies on the mechanism of hemorrhage production by five proteolytic hemorrhagic toxins from Crotalus atrox venom |
Biol. Chem. Hoppe-Seyler |
369 |
121-129 |
1988 |
Crotalus atrox |
3060135 |
| 3.4.24.42 | 31265 |
Substrate specificities and inhibition of two hemorrhagic zinc proteases Ht-c and Ht-d from Crotalus atrox venom |
Eur. J. Biochem. |
156 |
65-72 |
1986 |
Crotalus atrox |
3514216 |
| 3.4.24.42 | 651912 |
The interglobular domain of cartilage aggrecan is cleaved by hemorrhagic metalloproteinase HT-d (atrolysin C) at the matrix metalloproteinase and aggrecanase sites |
J. Biol. Chem. |
273 |
5846-5850 |
1998 |
Crotalus atrox |
9488721 |
