Human cathepsin X: a cysteine protease with unique carboxypeptidase activity.Naegler D.K., Zhang R., Tam W., Sulea T., Purisima E.O., Menard R.View abstractCited forFUNCTION, CATALYTIC ACTIVITYCategoryFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiochemistry 38:12648-12654 (1999)Cited in1
Crystal structure of human procathepsin X: a cysteine protease with the proregion covalently linked to the active site cysteine.Sivaraman J., Nagler D.K., Zhang R., Menard R., Cygler M.View abstractCited forX-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 27-303, ACTIVITY REGULATION, DISULFIDE BONDS, ACTIVE SITECategoriesFunction, PTM / Processing, StructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Mol. Biol. 295:939-951 (2000)Cited in1
Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease.Guncar G., Klemencic I., Turk B., Turk V., Karaoglanovic-Carmona A., Juliano L., Turk D.View abstractCited forX-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS), DISULFIDE BONDS, ACTIVE SITECategoriesPTM / Processing, Function, StructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCStructure 8:305-313 (2000)Cited in1