EC Number   |
Title |
Organism |
|---|
   3.4.23.22 | Active site mapping of an aspartic protease by multiple fragment crystal structures versatile warheads to address a catalytic dyad |
Cryphonectria parasitica |
| 3.4.23.22 | Design and synthesis of bioisosteres of acylhydrazones as stable inhibitors of the aspartic protease endothiapepsin |
Cryphonectria parasitica |
| 3.4.23.22 | Experimental active-site mapping by fragments hot spots remote from the catalytic center of endothiapepsin |
Cryphonectria parasitica |
| 3.4.23.22 | Fragment growing exploiting dynamic combinatorial chemistry of inhibitors of the aspartic protease endothiapepsin |
Cryphonectria parasitica |
| 3.4.23.22 | Fragment linking and optimization of inhibitors of the aspartic protease endothiapepsin fragment-based drug design facilitated by dynamic combinatorial chemistry |
Cryphonectria parasitica |
| 3.4.23.22 | Fragment-based drug design facilitated by protein-templated click chemistry fragment linking and optimization of inhibitors of the aspartic protease endothiapepsin |
Cryphonectria parasitica |
| 3.4.23.22 | Structure-based optimization of inhibitors of the aspartic protease endothiapepsin |
Cryphonectria parasitica |
| 3.4.23.22 | A neutron Laue diffraction study of endothiapepsin: implications for the aspartic proteinase mechanism |
Endothia sp. |
| 3.4.23.22 | A preliminary neutron Laue diffraction study of the aspartic proteinase endothiapepsin |
Endothia sp. |
| 3.4.23.22 | A small nonrule of 3 compatible fragment library provides high hit rate of endothiapepsin crystal structures with various fragment chemotypes |
Cryphonectria parasitica |
