| Structural highlights
Function
[CATS_HUMAN] Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.
Publication Abstract from PubMed
6-Phenyl-1H-imidazo[4,5-c]pyridine-4-carbonitrile analogues were identified as potent and selective cathepsin S inhibitor against both purified enzyme and in human JY cell based cellular assays. This core has a very stable thio-trapping nitrile war-head in comparison with the well reported pyrimidine-2-carbonitrile cysteine cathepsin inhibitors. Compound 47 is also very potent in in vivo mouse spleenic Lip10 accumulation assays.
6-Phenyl-1H-imidazo[4,5-c]pyridine-4-carbonitrile as cathepsin S inhibitors.,Cai J, Baugh M, Black D, Long C, Jonathan Bennett D, Dempster M, Fradera X, Gillespie J, Andrews F, Boucharens S, Bruin J, Cameron KS, Cumming I, Hamilton W, Jones PS, Kaptein A, Kinghorn E, Maidment M, Martin I, Mitchell A, Rankovic Z, Robinson J, Scullion P, Uitdehaag JC, Vink P, Westwood P, van Zeeland M, van Berkom L, Bastiani M, Meulemans T Bioorg Med Chem Lett. 2010 Aug 1;20(15):4350-4. Epub 2010 Jun 17. PMID:20598883[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cai J, Baugh M, Black D, Long C, Jonathan Bennett D, Dempster M, Fradera X, Gillespie J, Andrews F, Boucharens S, Bruin J, Cameron KS, Cumming I, Hamilton W, Jones PS, Kaptein A, Kinghorn E, Maidment M, Martin I, Mitchell A, Rankovic Z, Robinson J, Scullion P, Uitdehaag JC, Vink P, Westwood P, van Zeeland M, van Berkom L, Bastiani M, Meulemans T. 6-Phenyl-1H-imidazo[4,5-c]pyridine-4-carbonitrile as cathepsin S inhibitors. Bioorg Med Chem Lett. 2010 Aug 1;20(15):4350-4. Epub 2010 Jun 17. PMID:20598883 doi:10.1016/j.bmcl.2010.06.072
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