Organocatalysts of oxidative protein folding inspired by protein disulfide isomerase
Author:
Affiliation:
1. Department of Chemistry
2. University of Wisconsin–Madison
3. Madison, USA
4. Molecular & Cellular Pharmacology Graduate Training Program
5. Department of Biochemistry
Abstract
Organocatalysts derived from ethylenetriamine and containing a hydrophobic moiety effect the isomerization of non-native protein disulfide bonds to native ones.
Funder
Pharmaceutical Research and Manufacturers of America Foundation
National Institutes of Health
Publisher
Royal Society of Chemistry (RSC)
Subject
Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2014/OB/C4OB01738B
Reference70 articles.
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2. Oxidative Folding of Peptides and Proteins , ed. J. Buchner and L. Moroder , The Royal Society of Chemistry , Cambridge, UK , 2009
3. The Disulfide Proteome and Other Reactive Cysteine Proteomes: Analysis and Functional Significance
4. Forming disulfides in the endoplasmic reticulum
5. Principles that Govern the Folding of Protein Chains
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