Myeloid and erythroid nuclear termination stage-specific protein (MENT) is a member of the serpin family of protease inhibitors, and participates in DNA and chromatin condensation.[1] Alongside its ability to condense chromatin, MENT is also an effective inhibitor of the proteases cathepsin K, cathepsin L, and cathepsin V, all of which are cysteine proteases.[2] As such, although MENT is structurally classified as a member of the serpin family, it is functionally termed a "cross-class inhibitor," as it is a cysteine rather than a serine protease inhibitor.
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- ^ McGowan S, Buckle AM, Irving JA, et al. (July 2006). "X-ray crystal structure of MENT: evidence for functional loop-sheet polymers in chromatin condensation". EMBO J. 25 (13): 3144–55. doi:10.1038/sj.emboj.7601201. PMC 1500978. PMID 16810322.
- ^ Irving JA, Shushanov SS, Pike RN, et al. (April 2002). "Inhibitory activity of a heterochromatin-associated serpin (MENT) against papain-like cysteine proteinases affects chromatin structure and blocks cell proliferation". J. Biol. Chem. 277 (15): 13192–201. doi:10.1074/jbc.M108460200. PMID 11821386.
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