Assay ID | Title | Year | Journal | Article |
AID390500 | Inhibition of caspase-like activity of rabbit 20S proteasome | 2008 | Journal of medicinal chemistry, Nov-13, Volume: 51, Issue:21
| Leaving groups prolong the duration of 20S proteasome inhibition and enhance the potency of salinosporamides. |
AID390499 | Inhibition of trypsin-like activity of rabbit 20S proteasome | 2008 | Journal of medicinal chemistry, Nov-13, Volume: 51, Issue:21
| Leaving groups prolong the duration of 20S proteasome inhibition and enhance the potency of salinosporamides. |
AID390498 | Inhibition of chymotrypsin-like activity of rabbit 20S proteasome | 2008 | Journal of medicinal chemistry, Nov-13, Volume: 51, Issue:21
| Leaving groups prolong the duration of 20S proteasome inhibition and enhance the potency of salinosporamides. |
AID390497 | Stability in 20 mM HEPES buffer assessed as beta-lactone hydrolysis rate at pH 7.3 at 27 degC | 2008 | Journal of medicinal chemistry, Nov-13, Volume: 51, Issue:21
| Leaving groups prolong the duration of 20S proteasome inhibition and enhance the potency of salinosporamides. |
AID390507 | Inhibition of chymotrypsin-like activity of rabbit 20S proteasome assessed as enzyme activity recovery 24 hrs after dialysis | 2008 | Journal of medicinal chemistry, Nov-13, Volume: 51, Issue:21
| Leaving groups prolong the duration of 20S proteasome inhibition and enhance the potency of salinosporamides. |
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023] |