Pub. Date : 2017 Apr 13
PMID : 28264989
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | With respect to the inhibitor profile, we found that ADAM9 was inhibited by the hydroxamate-based metalloprotease inhibitors marimastat, TAPI-2, BB94, GM6001 and GW280264X, and by 10 nM of the tissue inhibitor of metalloproteinases (TIMP)-3, but not by up to 20 nM of TIMP-1 or -2. | hydroxamate | ADAM metallopeptidase domain 9 | Homo sapiens |
| 2 | Additionally, we screened a non-hydroxamate small-molecule library for novel ADAM9 inhibitors and identified four compounds that selectively inhibited ADAM9-dependent proteolysis over ADAM10- or ADAM17-dependent processing. | hydroxamate | ADAM metallopeptidase domain 9 | Homo sapiens |
| 3 | Additionally, we screened a non-hydroxamate small-molecule library for novel ADAM9 inhibitors and identified four compounds that selectively inhibited ADAM9-dependent proteolysis over ADAM10- or ADAM17-dependent processing. | hydroxamate | ADAM metallopeptidase domain 9 | Homo sapiens |
| 4 | The identification of novel non-hydroxamate inhibitors of ADAM9 could provide the basis for designing more selective compounds that block the contribution of ADAM9 to pathological neovascularization and cancer. | hydroxamate | ADAM metallopeptidase domain 9 | Homo sapiens |
| 5 | The identification of novel non-hydroxamate inhibitors of ADAM9 could provide the basis for designing more selective compounds that block the contribution of ADAM9 to pathological neovascularization and cancer. | hydroxamate | ADAM metallopeptidase domain 9 | Homo sapiens |