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Protein folding and disulfide bond formation in the eukaryotic cell.

Benham, A.M.

Authors



Abstract

The endoplasmic reticulum (ER) plays a critical role as a compartment for protein folding in eukaryotic cells. Defects in protein folding contribute to a growing list of diseases, and advances in our understanding of the molecular details of protein folding are helping to provide more efficient ways of producing recombinant proteins for industrial and medicinal use. Moreover, research performed in recent years has shown the importance of the ER as a signalling compartment that contributes to overall cellular homeostasis. Hamlet’s castle provided a stunning backdrop for the latest European network meeting to discuss this subject matter in Elsinore, Denmark, from 3 to 5 June 2009. Organized by researchers at the Department of Biology, University of Copenhagen, the meeting featured 20 talks by both established names and younger scientists, focusing on topics such as oxidative protein folding and maturation (in particular in the ER, but also in other compartments), cellular redox regulation, ER-associated degradation, and the unfolded protein response. Exciting new advances were presented, and the intimate setting with about 50 participants provided an excellent opportunity to discuss current key questions in the field.

Citation

Benham, A. (2009). Protein folding and disulfide bond formation in the eukaryotic cell. The FEBS Journal, 276(23), 6905-11. https://doi.org/10.1111/j.1742-4658.2009.07409.x

Journal Article Type Article
Publication Date 2009-12
Deposit Date May 14, 2010
Journal FEBS Journal
Print ISSN 1742-464X
Publisher Wiley
Peer Reviewed Peer Reviewed
Volume 276
Issue 23
Pages 6905-11
DOI https://doi.org/10.1111/j.1742-4658.2009.07409.x
Keywords Haperone, Endoplasmic reticulum, Mitochondria, Protein disulfide isomerase, Protein folding, Redox regulation.