Protein disulphide bonds-biochemistry, biotechnology and biomedical impact
A Biochemical Society Scientific Meeting
The majority of proteins secreted by eukaryotic cells are subject to an array of post-translational modifications including intra- and inter-chain disulphide bonds. The pathway of synthesis and export of secreted proteins has been actively researched for over half a century. Fundamental enzymology and protein science continues on the mechanisms of disulphide bond formation alongside work with a more cell biological perspective on the oxidative protein folding pathway in the endoplasmic reticulum and its interaction with the secretory and protein degradation pathways.
This meeting brought together the communities working on the biochemistry and cell biology of the oxidative protein folding pathway, cell manipulation for production of high-value, disulphide-bonded protein products, and the contribution of protein misfolding to human disease, highlighting recent advances and to stimulate new research. In so doing we also celebrated the work of Robert Freedman, a pioneer in this field.
View full programme here.
Oral communication slots were available at this meeting. All attendees, particularly researchers in the early stages of their career, were invited to submit a poster abstract for consideration as an oral communication.
Student Bursaries are available for this meeting.
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Topics covered in this meeting were invited to submit to our journal, Biochemical Society Transactions, or other publication published by Portland Press, the wholly-owned trading subsidiary of the Biochemical Society.