Characterization of the glutathione‐dependent reduction of the peroxiredoxin 5 homolog PfAOP from Plasmodium falciparum
Author:
Affiliation:
1. Faculty of Chemistry TU Kaiserslautern Kaiserslautern Germany
Funder
Deutsche Forschungsgemeinschaft
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.4290
Reference36 articles.
1. Multiple Functions and Regulation of Mammalian Peroxiredoxins
2. Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling
3. Enzymatic control of cysteinyl thiol switches in proteins
4. The Conundrum of Hydrogen Peroxide Signaling and the Emerging Role of Peroxiredoxins as Redox Relay Hubs
5. Structure-based Insights into the Catalytic Power and Conformational Dexterity of Peroxiredoxins
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1. Tsa1 is the dominant peroxide scavenger and a source of H2O2-dependent GSSG production in yeast;2024-07-03
2. Deciphering the mechanism of glutaredoxin-catalyzed roGFP2 redox sensing reveals a ternary complex with glutathione for protein disulfide reduction;Nature Communications;2024-02-26
3. Glutathione kinetically outcompetes reactions between dimedone and a cyclic sulfenamide or physiological sulfenic acids;Free Radical Biology and Medicine;2023-11
4. Substrate Promiscuity and Hyperoxidation Susceptibility as Potential Driving Forces for the Co-evolution of Prx5-Type and Prx6-Type 1-Cys Peroxiredoxin Mechanisms;ACS Catalysis;2023-02-28
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