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EMBO Press, EMBO Reports, 1(6), p. 28-32, 2005

DOI: 10.1038/sj.embor.7400311

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The human protein disulphide isomerase family: substrate interactions and functional properties

Journal article published in 2005 by Lars Ellgaard ORCID, Lloyd W. Ruddock
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

The process of disulphide bond formation in the endoplasmic reticulum of eukaryotic cells was one of the first mechanisms of catalysed protein folding to be discovered. Protein disulphide isomerase (PDI) is now known to catalyse all of the reactions that are involved in native disulphide bond formation, but despite more than 40 years of study, its mechanism of action is still not fully understood. This review discusses recent advances in our understanding of the human PDI family of enzymes and focuses on their functional properties, substrate interactions and some recently identified family members.