EC Number   |
Inhibitors |
Structure  |
|---|
   1.14.11.29 | more |
the peptide inhibitors consist of amino acids identical to those in the CODD556-575 except the 564 proline residue, and target the C-terminal oxygen-dependent degradation domain binding site in the PHD2 active pocket. Specific inhibition of PHD2, no inhibition of FIH, EC 1.14.11.30 |
 |
| 1.14.11.29 | more |
temporal dynamics of hydroxylase inhibition, overview |
|
| 1.14.11.29 | more |
polynitrogen compound as HIF-1alpha PHD3 inhibitors, the metal complexes of these polynitrogen compounds cannot inhibit the catalytical activity of PHD3, overview. The inhibitory mechanism of PHD3 activity by polynitrogen compounds is due to their binding to iron to form stable coordination complexes |
|
| 1.14.11.29 | more |
screening of iron chelators pyridines, hydroxypyrones/hydroxypyridinones, and catechols as inhibitors for PHD2, analysis of selectivity of the inhibitors for PHD2 compared to FIH, EC 1.14.11.30. Ligand binding kinetics and structural analysis, overview. Representative inhibitors bind to the metal center in PHD2 as an 2-oxoglutarate mimic |
|
| 1.14.11.29 | more |
inhibition of the recombinant human PHD3 activity by tetraazamacrocycles, overview |
|
| 1.14.11.29 | more |
compounds with a 3-carbamoylpropanoic acids-containing benzoxazole moiety are inhibitors of PHD-2. However, neither the acids nor their respective ethyl esters upregulate HIF-1alpha levels in cells |
|
| 1.14.11.29 | Mn2+ |
- |
  |
| 1.14.11.29 | Zn2+ |
- |
|
| 1.14.11.29 | Cu2+ |
binding analysis |
|
| 1.14.11.29 | Cu2+ |
- |
|
