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Diversity of allosteric regulation in proteases

Merdanovic, Melisa, Mönig, Timon, Ehrmann, Michael and Kaiser, Markus 2013. Diversity of allosteric regulation in proteases. ACS Chemical Biology 8 (1) , pp. 19-26. 10.1021/cb3005935

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Allostery is a fundamental regulatory mechanism that is based on a functional modulation of a site by a distant site. Allosteric regulation can be triggered by binding of diverse allosteric effectors, ranging from small molecules to macromolecules, and is therefore offering promising opportunities for functional modulation in a wide range of applications including the development of chemical probes or drug discovery. Here, we provide an overview of key classes of allosteric protease effectors, their corresponding molecular mechanisms, and their practical implications.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Subjects: Q Science > QD Chemistry
Q Science > QP Physiology
Publisher: American Chemical Society
ISSN: 1554-8929
Last Modified: 04 Jun 2017 06:10

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