Freedman, Robert B. and Hirst, Timothy R. and Tuite, Mick F. (1994) Protein Disulfide-Isomerase Build Bridges in Protein-Folding. Trends in Biochemical Sciences, 19 (8). pp. 331-336. ISSN 0968-0004. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)
Protein disulphide isomerase (PDI) has been known for many years to assist in the folding of proteins containing disulphide bonds, but the exact mechanism by which it achieves this is only now becoming clear. The active site of PDI closely resembles that of the redox protein thioredoxin, and cDNA cloning has revealed a superfamily of proteins with related active-site sequences, in organisms ranging from bacteria to higher animals and plants. Recent mutagenesis studies are now helping to unravel the catalytic mechanism of PDI, and work in yeast and other systems is clarifying the physiological roles of the multiple PDI-related proteins.
|Subjects:||Q Science > QP Physiology (Living systems) > QP517 Biochemistry|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||P. Ogbuji|
|Date Deposited:||05 Oct 2009 08:31|
|Last Modified:||10 Jun 2014 12:57|
|Resource URI:||https://kar.kent.ac.uk/id/eprint/20204 (The current URI for this page, for reference purposes)|