Assay ID | Title | Year | Journal | Article |
AID314754 | Inhibition of carbonic anhydrase 9 catalytic domain assessed as residual activity at 2.5 mM | 2008 | Bioorganic & medicinal chemistry letters, Mar-15, Volume: 18, Issue:6
| Carbonic anhydrase inhibitors: the very weak inhibitors dithiothreitol, beta-mercaptoethanol, tris(carboxyethyl)phosphine and threitol interfere with the binding of sulfonamides to isozymes II and IX. |
AID314748 | Inhibition of carbonic anhydrase 9 catalytic domain assessed as residual activity at 0.1 mM | 2008 | Bioorganic & medicinal chemistry letters, Mar-15, Volume: 18, Issue:6
| Carbonic anhydrase inhibitors: the very weak inhibitors dithiothreitol, beta-mercaptoethanol, tris(carboxyethyl)phosphine and threitol interfere with the binding of sulfonamides to isozymes II and IX. |
AID314744 | Inhibition of carbonic anhydrase 2 assessed as residual activity at 0.01 mM | 2008 | Bioorganic & medicinal chemistry letters, Mar-15, Volume: 18, Issue:6
| Carbonic anhydrase inhibitors: the very weak inhibitors dithiothreitol, beta-mercaptoethanol, tris(carboxyethyl)phosphine and threitol interfere with the binding of sulfonamides to isozymes II and IX. |
AID314741 | Inhibition of carbonic anhydrase 2 assessed as residual activity at 0.001 mM | 2008 | Bioorganic & medicinal chemistry letters, Mar-15, Volume: 18, Issue:6
| Carbonic anhydrase inhibitors: the very weak inhibitors dithiothreitol, beta-mercaptoethanol, tris(carboxyethyl)phosphine and threitol interfere with the binding of sulfonamides to isozymes II and IX. |
AID314755 | Inhibition of carbonic anhydrase 9 assessed as residual activity at 2.5 mM | 2008 | Bioorganic & medicinal chemistry letters, Mar-15, Volume: 18, Issue:6
| Carbonic anhydrase inhibitors: the very weak inhibitors dithiothreitol, beta-mercaptoethanol, tris(carboxyethyl)phosphine and threitol interfere with the binding of sulfonamides to isozymes II and IX. |
AID314758 | Inhibition of carbonic anhydrase 9 assessed as residual activity at 10 mM | 2008 | Bioorganic & medicinal chemistry letters, Mar-15, Volume: 18, Issue:6
| Carbonic anhydrase inhibitors: the very weak inhibitors dithiothreitol, beta-mercaptoethanol, tris(carboxyethyl)phosphine and threitol interfere with the binding of sulfonamides to isozymes II and IX. |
AID314746 | Inhibition of carbonic anhydrase 9 assessed as residual activity at 0.01 mM | 2008 | Bioorganic & medicinal chemistry letters, Mar-15, Volume: 18, Issue:6
| Carbonic anhydrase inhibitors: the very weak inhibitors dithiothreitol, beta-mercaptoethanol, tris(carboxyethyl)phosphine and threitol interfere with the binding of sulfonamides to isozymes II and IX. |
AID314751 | Inhibition of carbonic anhydrase 9 catalytic domain assessed as residual activity at 1.0 mM | 2008 | Bioorganic & medicinal chemistry letters, Mar-15, Volume: 18, Issue:6
| Carbonic anhydrase inhibitors: the very weak inhibitors dithiothreitol, beta-mercaptoethanol, tris(carboxyethyl)phosphine and threitol interfere with the binding of sulfonamides to isozymes II and IX. |
AID314747 | Inhibition of carbonic anhydrase 2 assessed as residual activity at 0.1 mM | 2008 | Bioorganic & medicinal chemistry letters, Mar-15, Volume: 18, Issue:6
| Carbonic anhydrase inhibitors: the very weak inhibitors dithiothreitol, beta-mercaptoethanol, tris(carboxyethyl)phosphine and threitol interfere with the binding of sulfonamides to isozymes II and IX. |
AID314749 | Inhibition of carbonic anhydrase 9 assessed as residual activity at 0.1 mM | 2008 | Bioorganic & medicinal chemistry letters, Mar-15, Volume: 18, Issue:6
| Carbonic anhydrase inhibitors: the very weak inhibitors dithiothreitol, beta-mercaptoethanol, tris(carboxyethyl)phosphine and threitol interfere with the binding of sulfonamides to isozymes II and IX. |
AID314743 | Inhibition of carbonic anhydrase 9 assessed as residual activity at 0.001 mM | 2008 | Bioorganic & medicinal chemistry letters, Mar-15, Volume: 18, Issue:6
| Carbonic anhydrase inhibitors: the very weak inhibitors dithiothreitol, beta-mercaptoethanol, tris(carboxyethyl)phosphine and threitol interfere with the binding of sulfonamides to isozymes II and IX. |
AID314745 | Inhibition of carbonic anhydrase 9 catalytic domain assessed as residual activity at 0.01 mM | 2008 | Bioorganic & medicinal chemistry letters, Mar-15, Volume: 18, Issue:6
| Carbonic anhydrase inhibitors: the very weak inhibitors dithiothreitol, beta-mercaptoethanol, tris(carboxyethyl)phosphine and threitol interfere with the binding of sulfonamides to isozymes II and IX. |
AID314742 | Inhibition of carbonic anhydrase 9 catalytic domain assessed as residual activity at 0.001 mM | 2008 | Bioorganic & medicinal chemistry letters, Mar-15, Volume: 18, Issue:6
| Carbonic anhydrase inhibitors: the very weak inhibitors dithiothreitol, beta-mercaptoethanol, tris(carboxyethyl)phosphine and threitol interfere with the binding of sulfonamides to isozymes II and IX. |
AID314756 | Inhibition of carbonic anhydrase 2 assessed as residual activity at 10 mM | 2008 | Bioorganic & medicinal chemistry letters, Mar-15, Volume: 18, Issue:6
| Carbonic anhydrase inhibitors: the very weak inhibitors dithiothreitol, beta-mercaptoethanol, tris(carboxyethyl)phosphine and threitol interfere with the binding of sulfonamides to isozymes II and IX. |
AID314750 | Inhibition of carbonic anhydrase 2 assessed as residual activity at 1.0 mM | 2008 | Bioorganic & medicinal chemistry letters, Mar-15, Volume: 18, Issue:6
| Carbonic anhydrase inhibitors: the very weak inhibitors dithiothreitol, beta-mercaptoethanol, tris(carboxyethyl)phosphine and threitol interfere with the binding of sulfonamides to isozymes II and IX. |
AID314753 | Inhibition of carbonic anhydrase 2 assessed as residual activity at 2.5 mM | 2008 | Bioorganic & medicinal chemistry letters, Mar-15, Volume: 18, Issue:6
| Carbonic anhydrase inhibitors: the very weak inhibitors dithiothreitol, beta-mercaptoethanol, tris(carboxyethyl)phosphine and threitol interfere with the binding of sulfonamides to isozymes II and IX. |
AID314757 | Inhibition of carbonic anhydrase 9 catalytic domain assessed as residual activity at 10 mM | 2008 | Bioorganic & medicinal chemistry letters, Mar-15, Volume: 18, Issue:6
| Carbonic anhydrase inhibitors: the very weak inhibitors dithiothreitol, beta-mercaptoethanol, tris(carboxyethyl)phosphine and threitol interfere with the binding of sulfonamides to isozymes II and IX. |
AID314752 | Inhibition of carbonic anhydrase 9 assessed as residual activity at 1.0 mM | 2008 | Bioorganic & medicinal chemistry letters, Mar-15, Volume: 18, Issue:6
| Carbonic anhydrase inhibitors: the very weak inhibitors dithiothreitol, beta-mercaptoethanol, tris(carboxyethyl)phosphine and threitol interfere with the binding of sulfonamides to isozymes II and IX. |
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023] |