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Issue 76, 2013
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Virtual screening and experimental validation reveal novel small-molecule inhibitors of 14-3-3 proteinprotein interactions

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Abstract

We report first non-covalent and exclusively extracellular inhibitors of 14-3-3 proteinprotein interactions identified by virtual screening. Optimization by crystal structure analysis and in vitro binding assays yielded compounds capable of disrupting the interaction of 14-3-3σ with aminopeptidase N in a cellular assay.

Graphical abstract: Virtual screening and experimental validation reveal novel small-molecule inhibitors of 14-3-3 protein–protein interactions

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Publication details

The article was received on 19 Jun 2013, accepted on 24 Jul 2013 and first published on 25 Jul 2013


Article type: Communication
DOI: 10.1039/C3CC44612C
Citation: Chem. Commun., 2013,49, 8468-8470
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    Virtual screening and experimental validation reveal novel small-molecule inhibitors of 14-3-3 proteinprotein interactions

    P. Thiel, L. Röglin, N. Meissner, S. Hennig, O. Kohlbacher and C. Ottmann, Chem. Commun., 2013, 49, 8468
    DOI: 10.1039/C3CC44612C

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