Myeloid and erythroid nuclear termination stage-specific protein
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. 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. 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.
- 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.
|This protein-related article is a stub. You can help Wikipedia by expanding it.|