EC Number   |
Inhibitors |
Structure  |
|---|
   3.4.22.27 | more |
inhibitory potential in vivo on Ii degradation in JY cells |
 |
| 3.4.22.27 | more |
analysis of inhibition mechanisms and binding to the active site; design and synthesis of arylaminoethyl amides as noncovalent inhibitors of cathepsin S, overview |
|
| 3.4.22.27 | more |
diverse arylaminoethyl amides as noncovalent inhibitors of cathepsin S with IC50 in the nanomolar range, optimization of P1 and N-aryl, binding specificities of positions P1 and P2, and of subsite S1, overview |
|
| 3.4.22.27 | more |
synthesis and evaluation of heterocyclic arylaminoethyl amides as noncovalent inhibitors of cathepsin S, binding specificities of positions P1-P3 and of subsite S3, overview |
|
| 3.4.22.27 | more |
synthesis and inhibitory effects of diverse arylaminoethyl carbamate inhibitors possessing a substrate peptidomimetic scaffold, structue-activity relationship, pharmacokinetics, overview |
|
| 3.4.22.27 | more |
reversible inhibition by a dipeptide-nitrile inhibitor |
|
| 3.4.22.27 | more |
no inhibition by proteasome inhibitors |
|
| 3.4.22.27 | more |
effect of cathepsin S inhibition on bronchoalveolar lavage fluid cytokines: inhibition reduces ozone-induced interleukin-6 levels at 3 h and 20-24 h and TNF-alpha levels are inhibited at 20-24 h |
|
| 3.4.22.27 | more |
design and synthesis of a near-infrared quenched activity-based probes (qABP) that selectively target cathepsin S which is highly expressed in immune cells, green-fluorescent pan-reactive cysteine cathepsin qABP in dual color labeling studies in bone marrow-derived immune cells, and identification of vesicles containing exclusively cathepsin S activity, method optimization and evaluation, overview. The high degree of selectivity is retained both in vitro and in vivo |
|
| 3.4.22.27 | Triton X-100 |
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