期刊
FEBS LETTERS
卷 583, 期 12, 页码 1809-1816出版社
WILEY
DOI: 10.1016/j.febslet.2009.05.029
关键词
Protein oligomerization; Peroxiredoxin; Sulfiredoxin; Chaperone activity; Dithiothreitol
资金
- Deutsche Forschungsgemeinschaft [Di346]
Protein-protein associations, i.e. formation of permanent or transient protein complexes, are essential for protein functionality and regulation within the cellular context. Peroxiredoxins (Prx) undergo major redox-dependent conformational changes and the dynamics are linked to functional switches. While a large number of investigations have addressed the principles and functions of Prx oligomerization, understanding of the diverse in vivo roles of this conserved redox-dependent feature of Prx is slowly emerging. The review summarizes studies on Prx oligomerization, its tight connection to the redox state, and the knowledge and hypotheses on its physiological function in the cell as peroxidase, chaperone, binding partner, enzyme activator and/or redox sensor. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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