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- Luke Carroll, Kelly Gardiner, Marta Ignasiak, Jeppe Holmehave, Shingo Shimodaira, Thomas Breitenbach, Michio Iwaoka, Peter R. Ogilby, David I. Pattison, Michael J. Davies. Interaction kinetics of selenium-containing compounds with oxidants. Free Radical Biology and Medicine 2020;155:58

- Aristidis S. Veskoukis, Vassilis Paschalis, Antonios Kyparos, Michalis G. Nikolaidis. Administration of exercise-conditioned plasma alters muscle catalase kinetics in rat: An argument for in vivo-like Km instead of in vitro-like Vmax. Redox Biology 2018;15:375

- María Inés De Armas, Romina Esteves, Nicolás Viera, Aníbal M. Reyes, Mauricio Mastrogiovanni, Thiago G.P. Alegria, Luis E.S. Netto, Verónica Tórtora, Rafael Radi, Madia Trujillo. Rapid peroxynitrite reduction by human peroxiredoxin 3: Implications for the fate of oxidants in mitochondria. Free Radical Biology and Medicine 2019;130:369

- Austin McGinnis, Vladimir I. Klichko, William C. Orr, Svetlana N. Radyuk. Hyperoxidation of Peroxiredoxins and Effects on Physiology of Drosophila. Antioxidants 2021;10:606

- N. T. Moldogazieva, I. M. Mokhosoev, N. B. Feldman, S. V. Lutsenko. ROS and RNS signalling: adaptive redox switches through oxidative/nitrosative protein modifications. Free Radical Research 2018;52:507

- Kathrin Ulrich, Ursula Jakob. The role of thiols in antioxidant systems. Free Radical Biology and Medicine 2019;140:14

- James West, Trevor Roston, Joseph David, Kristin Allan, Matthew Loberg. Piecing Together How Peroxiredoxins Maintain Genomic Stability. Antioxidants 2018;7:177

- Petr Ježek, Blanka Holendová, Lydie Plecitá-Hlavatá. Redox Signaling from Mitochondria: Signal Propagation and Its Targets. Biomolecules 2020;10:93

- Mars G. Sharapov, Sergey V. Gudkov, Vadim Z. Lankin. Hydroperoxide-Reducing Enzymes in the Regulation of Free-Radical Processes. Biochemistry Moscow 2021;86:1256

- Alexander V. Peskin, Flávia C. Meotti, Luiz F. de Souza, Robert F. Anderson, Christine C. Winterbourn, Armindo Salvador. Intra-dimer cooperativity between the active site cysteines during the oxidation of peroxiredoxin 2. Free Radical Biology and Medicine 2020;158:115

- Sarah Stöcker, Koen Van Laer, Ana Mijuskovic, Tobias P. Dick. The Conundrum of Hydrogen Peroxide Signaling and the Emerging Role of Peroxiredoxins as Redox Relay Hubs. Antioxidants & Redox Signaling 2018;28:558

- Valesca Anschau, Gerardo Ferrer-Sueta, Rogerio Luis Aleixo-Silva, Renata Bannitz Fernandes, Carlos A. Tairum, Celisa Caldana Costa Tonoli, Mario Tyago Murakami, Marcos Antonio de Oliveira, Luis Eduardo Soares Netto. Reduction of sulfenic acids by ascorbate in proteins, connecting thiol-dependent to alternative redox pathways. Free Radical Biology and Medicine 2020;156:207

- Evan A. Elko, Brian Cunniff, David J. Seward, Shi Biao Chia, Reem Aboushousha, Cheryl van de Wetering, Jos van der Velden, Allison Manuel, Arti Shukla, Nicholas H. Heintz, Vikas Anathy, Albert van der Vliet, Yvonne M.W. Janssen-Heininger. Peroxiredoxins and Beyond; Redox Systems Regulating Lung Physiology and Disease. Antioxidants & Redox Signaling 2019;31:1070

- José Rafael Pedrajas, José Antonio Bárcena. Antioxidants and Antioxidant Enzymes in Higher Plants. 2019.

- Larissa A.C. Carvalho, Daniela R. Truzzi, Thamiris S. Fallani, Simone V. Alves, José Carlos Toledo, Ohara Augusto, Luís E.S. Netto, Flavia C. Meotti. Urate hydroperoxide oxidizes human peroxiredoxin 1 and peroxiredoxin 2. Journal of Biological Chemistry 2017;292:8705

- Tom E. Forshaw, Julie A. Reisz, Kimberly J. Nelson, Rajesh Gumpena, J. Reed Lawson, Thomas J. Jönsson, Hanzhi Wu, Jill E. Clodfelter, Lynnette C. Johnson, Cristina M. Furdui, W. Todd Lowther. Specificity of Human Sulfiredoxin for Reductant and Peroxiredoxin Oligomeric State. Antioxidants 2021;10:946

- М.Г. Шарапов, С.В. Гудков, В.З. Ланкин. Гидропероксид-восстанавливающие ферментные системы в регуляции свободнорадикальных процессов. БМ 2021;86:1479

- A.В. Пескин, К.С. Уинтерборн. Загадка 2-Cys-пероксиредоксинов: какова их роль в клетке?. БМ 2021;86:100

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- Deepti Talwar, Tobias P. Dick. Redox Chemistry and Biology of Thiols. 2020.

- Alexander V. Peskin, Christine C. Winterbourn. The Enigma of 2-Cys Peroxiredoxins: What Are Their Roles?. Biochemistry Moscow 2021;86:84

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- Rakesh Kumar, Ashu Mohammad, Reena V. Saini, Anterpreet Chahal, Chi-Ming Wong, Deepak Sharma, Sukhvir Kaur, Vikas Kumar, Christine C. Winterbourn, Adesh K. Saini. Deciphering the in vivo redox behavior of human peroxiredoxins I and II by expressing in budding yeast. Free Radical Biology and Medicine 2019;145:321

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- Mars G. Sharapov, Sergey V. Gudkov. Peroxiredoxin 1 - Multifunctional antioxidant enzyme, protects from oxidative damages and increases the survival rate of mice exposed to total body irradiation. Archives of Biochemistry and Biophysics 2021;697:108671

- Svetlana N. Radyuk, William C. Orr. The Multifaceted Impact of Peroxiredoxins on Aging and Disease. Antioxidants & Redox Signaling 2018;29:1293

- Sarah Stöcker, Michael Maurer, Thomas Ruppert, Tobias P Dick. A role for 2-Cys peroxiredoxins in facilitating cytosolic protein thiol oxidation. Nat Chem Biol 2018;14:148

- Ulla G. Knaus. Reactive Oxygen Species. 2018.

- N. Amy Yewdall, Alexander V. Peskin, Mark B. Hampton, David C. Goldstone, F. Grant Pearce, Juliet A. Gerrard. Quaternary structure influences the peroxidase activity of peroxiredoxin 3. Biochemical and Biophysical Research Communications 2018;497:558
