Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10799905 | Biochimica et Biophysica Acta (BBA) - General Subjects | 2016 | 12 Pages |
Abstract
Accessory domains covalently linked to a PPIase domain supply an additional layer of control to the catalysis of prolyl isomerization in specific client proteins. Understanding these control mechanisms will provide new insights into the physiological mode of action of the multidomain PPIases and their ability to form therapeutic targets. This article is part of a Special Issue entitled Proline-directed Foldases: Cell Signaling Catalysts and Drug Targets.
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Authors
Cordelia Schiene-Fischer,