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CHN2 — ERVK-6

Text-mined interactions from Literome

Yong et al., Mol Biochem Parasitol 2000 : Here, we describe the properties of a phenotypically stable T. cruzi cell line ( R-Dm28 ) that displays increased resistance to Z- ( SBz ) Cys-Phe-CHN2 , an irreversible cysteine-proteinase inhibitor which preferentially inactivates cathepsin L-like enzymes
Baricos et al., Arch Biochem Biophys 1991 (Disease Models, Animal...) : Administration of Z-Phe-Tyr ( O-t-butyl ) CHN2 , a specific, irreversible cysteine proteinase inhibitor with a high degree of selectivity toward cathepsin L, also caused a reduction in anti-GBM antibody induced proteinuria ( 90 +/- 18 mg/24 h, N = 6, P less than 0.05 )
Björck et al., Nature 1989 : The cysteine proteinase produced by group A streptococci was isolated and found to be inhibited by Z-LVG-CHN2 ; moreover, excess proteinase relieved the growth inhibition caused by the peptide derivative, suggesting that the antibacterial activity of Z-LVG-CHN2 is due to inhibition of this cysteine proteinase
Debari et al., Calcif Tissue Int 1995 (Bone Resorption...) : Mouse bone marrow cell derived osteoclasts were suspended on dentine slices and cultured for 48 hours in the presence of either E-64 ( a generalized cysteine proteinase inhibitor ) or Z-Phe-Phe-CHN2 ( a selective cathepsin L inhibitor )