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Issue 6, 2011
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Isothiazolones; thiol-reactive inhibitors of cysteine protease cathepsin B and histone acetyltransferase PCAF

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Abstract

Isothiazolones and 5-chloroisothiazolones react chemoselectively with thiols by cleavage of the weak nitrogen–sulfur bond to form disulfides. They show selectivity for inhibition of the thiol-dependent cysteine protease cathepsin B and the histone acetyltransferase p300/CBP associated factor (PCAF) based on their substitution pattern. Furthermore, enzyme kinetics and mass spectroscopy indicate covalent binding of a 5-chloroisothiazolone to cathepsin B, which demonstrates their potential utility as probes for activity-based protein profiling.

Graphical abstract: Isothiazolones; thiol-reactive inhibitors of cysteine protease cathepsin B and histone acetyltransferase PCAF

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Publication details

The article was received on 21 Jul 2010, accepted on 08 Dec 2010 and first published on 25 Jan 2011


Article type: Paper
DOI: 10.1039/C0OB00464B
Citation: Org. Biomol. Chem., 2011,9, 1817-1822

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    Isothiazolones; thiol-reactive inhibitors of cysteine protease cathepsin B and histone acetyltransferase PCAF

    R. Wisastra, M. Ghizzoni, H. Maarsingh, A. J. Minnaard, H. J. Haisma and F. J. Dekker, Org. Biomol. Chem., 2011, 9, 1817
    DOI: 10.1039/C0OB00464B

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