10 research outputs found

    Biomolecular Recognition of Methylated Histones

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    Lysine and arginine methylations are among the most abundant posttranslational modifications found on histone proteins. The recognition of methylated lysine and arginine residues by epigenetic reader proteins provides an important molecular requirement for regulation of human genes. Recent structural and mechanistic studies importantly advanced our basic understanding of biomolecular recognition of methylated histones by diverse classes of epigenetic readers. In this chapter, we describe chemical biological studies on the recognition of methylated histones by the aromatic cage-containing reader proteins.</p

    Exploiting non-covalent π interactions for catalyst design

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    Molecular recognition, binding and catalysis are often mediated by non-covalent interactions involving aromatic functional groups. Although the relative complexity of these so-called π interactions has made them challenging to study, theory and modelling have now reached the stage at which we can explain their physical origins and obtain reliable insight into their effects on molecular binding and chemical transformations. This offers opportunities for the rational manipulation of these complex non-covalent interactions and their direct incorporation into the design of small-molecule catalysts and enzymes

    Critical roles of non-histone protein lysine methylation in human tumorigenesis

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