Hauske, Patrick, Ottmann, Christian, Meltzer, Michael, Ehrmann, Michael ORCID: https://orcid.org/0000-0002-1927-260X and Kaiser, Markus 2008. Allosteric regulation of proteases. Chembiochem 9 (18) , pp. 2920-2928. 10.1002/cbic.200800528 |
Official URL: http://dx.doi.org/10.1002/cbic.200800528
Abstract
Allostery is a basic principle of control of enzymatic activities based on the interaction of a protein or small molecule at a site distinct from an enzyme's active center. Allosteric modulators represent an alternative approach to the design and synthesis of small-molecule activators or inhibitors of proteases and are therefore of wide interest for medicinal chemistry. The structural bases of some proteinaceous and small-molecule allosteric protease regulators have already been elucidated, indicating a general mechanism that might be exploitable for future rational design of small-molecule effectors
Item Type: | Article |
---|---|
Date Type: | Publication |
Status: | Published |
Schools: | Biosciences |
Subjects: | Q Science > QD Chemistry Q Science > QP Physiology |
Publisher: | Wiley-Blackwell |
ISSN: | 1439-4227 |
Last Modified: | 25 Oct 2022 09:15 |
URI: | https://orca.cardiff.ac.uk/id/eprint/57791 |
Citation Data
Cited 68 times in Scopus. View in Scopus. Powered By Scopus® Data
Actions (repository staff only)
Edit Item |