The oligomeric conformation of peroxiredoxins links redox state to function

Barranco-Medina S, Lazaro J-J, Dietz K-J (2009)
FEBS LETTERS 583(12): 1809-1816.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Autor/in
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Abstract / Bemerkung
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.
Stichworte
Protein oligomerization; Sulfiredoxin; Chaperone; activity; Dithiothreitol; Peroxiredoxin
Erscheinungsjahr
2009
Zeitschriftentitel
FEBS LETTERS
Band
583
Ausgabe
12
Seite(n)
1809-1816
ISSN
0014-5793
Page URI
https://pub.uni-bielefeld.de/record/1591737

Zitieren

Barranco-Medina S, Lazaro J-J, Dietz K-J. The oligomeric conformation of peroxiredoxins links redox state to function. FEBS LETTERS. 2009;583(12):1809-1816.
Barranco-Medina, S., Lazaro, J. - J., & Dietz, K. - J. (2009). The oligomeric conformation of peroxiredoxins links redox state to function. FEBS LETTERS, 583(12), 1809-1816. doi:10.1016/j.febslet.2009.05.029
Barranco-Medina, S., Lazaro, J. - J., and Dietz, K. - J. (2009). The oligomeric conformation of peroxiredoxins links redox state to function. FEBS LETTERS 583, 1809-1816.
Barranco-Medina, S., Lazaro, J.-J., & Dietz, K.-J., 2009. The oligomeric conformation of peroxiredoxins links redox state to function. FEBS LETTERS, 583(12), p 1809-1816.
S. Barranco-Medina, J.-J. Lazaro, and K.-J. Dietz, “The oligomeric conformation of peroxiredoxins links redox state to function”, FEBS LETTERS, vol. 583, 2009, pp. 1809-1816.
Barranco-Medina, S., Lazaro, J.-J., Dietz, K.-J.: The oligomeric conformation of peroxiredoxins links redox state to function. FEBS LETTERS. 583, 1809-1816 (2009).
Barranco-Medina, Sergio, Lazaro, Juan-Jose, and Dietz, Karl-Josef. “The oligomeric conformation of peroxiredoxins links redox state to function”. FEBS LETTERS 583.12 (2009): 1809-1816.

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