Cardiff University | Prifysgol Caerdydd ORCA
Online Research @ Cardiff 
WelshClear Cookie - decide language by browser settings

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

Full text not available from this repository.

Abstract

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
URI: http://orca.cf.ac.uk/id/eprint/56920

Citation Data

Cited 11 times in Google Scholar. View in Google Scholar

Cited 31 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item Edit Item