Literature summary for 3.4.22.27 extracted from

Alper, P.B.; Liu, H.; Chatterjee, A.K.; Nguyen, K.T.; Tully, D.C.; Tumanut, C.; Li, J.; Harris, J.L.; Tuntland, T.; Chang, J.; Gordon, P.; Hollenbeck, T.; Karanewsky, D.S.
Arylaminoethyl amides as noncovalent inhibitors of cathepsin S. Part 2: optimization of P1 and N-aryl (2006), Bioorg. Med. Chem. Lett., 16, 1486-1490.

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Application

Application	Comment	Organism
pharmacology	the enzyme might be a good target for development of inhibitors in treatment of collagen-induced arthritis and autoimmune myasthenia gravis	Mus musculus

Protein Variants

Protein Variants	Comment	Organism
additional information	cathepsin S-deficient mutant mice show impaired degradation of the invariant chain in antigen presenting cells alng with resistance to collagen-induced arthritis and autoimmune myasthenia gravis	Mus musculus

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	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	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	-	-	-

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Release 2023.1 (January 2023)