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• W2034000077 endingPage "568" @default.
• W2034000077 startingPage "559" @default.
• W2034000077 abstract "Cathepsin F is a lysosomal cysteine protease of the papain family, and likely plays a regulatory role in processing the invariant chain that is associated with the major histocompatibility complex (MHC) class II. Evidence suggests that inhibiting cathepsin F activity will block MHC class II processing in macrophages. Consequently, inhibitors of this enzyme may be useful in treating certain diseases that involve an inappropriate or excessive immune response. We have determined the 1.7 Å structure of the mature domain of human cathepsin F associated with an irreversible vinyl sulfone inhibitor. This structure provides a basis for understanding cathepsin F's substrate specificity, and suggests ways of identifying potent and selective inhibitors of this enzyme." @default.
• W2034000077 created "2016-06-24" @default.
• W2034000077 creator A5025021180 @default.
• W2034000077 creator A5036811529 @default.
• W2034000077 creator A5073292373 @default.
• W2034000077 date "2002-09-01" @default.
• W2034000077 modified "2023-10-12" @default.
• W2034000077 title "The Crystal Structure of Human Cathepsin F and Its Implications for the Development of Novel Immunomodulators" @default.
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• W2034000077 doi "https://doi.org/10.1016/s0022-2836(02)00780-5" @default.
• W2034000077 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12225749" @default.
• W2034000077 hasPublicationYear "2002" @default.
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