| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10599092 | Bioorganic & Medicinal Chemistry Letters | 2005 | 5 Pages |
Abstract
PDI is an enzyme that acts as a chaperone, shufflase, and oxidase during the folding of disulfide-containing proteins. The ability of aromatic thiols to increase the activity of PDI-catalyzed protein folding over that of the standard thiol glutathione (GSH) was measured. 4-Mercaptobenzoic acid (ArSH) increased the activity of PDI by a factor of three.
Related Topics
Physical Sciences and Engineering
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Authors
Jonathan D. Gough, Watson J. Lees,