Clausen, Tim, Southan, Chris and Ehrmann, Michael ORCID: https://orcid.org/0000-0002-1927-260X 2002. The HtrA family of proteases: implications for protein composition and cell fate. Molecular Cell 10 (3) , pp. 443-455. 10.1016/S1097-2765(02)00658-5 |
Official URL: http://dx.doi.org/10.1016/S1097-2765(02)00658-5
Abstract
Cells precisely monitor the concentration and functionality of each protein for optimal performance. Protein quality control involves molecular chaperones, folding catalysts, and proteases that are often heat shock proteins. One quality control factor is HtrA, one of a new class of oligomeric serine proteases. The defining feature of the HtrA family is the combination of a catalytic domain with at least one C-terminal PDZ domain. Here, we discuss the properties and roles of this ATP-independent protease chaperone system in protein metabolism and cell fate.
Item Type: | Article |
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Date Type: | Publication |
Status: | Published |
Schools: | Biosciences |
Publisher: | Cell Press |
ISSN: | 1097-2765 |
Last Modified: | 27 Oct 2022 08:46 |
URI: | https://orca.cardiff.ac.uk/id/eprint/63338 |
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