References
- Aslund, F., Zheng, M., Beckwith, J., and Storz, G. (1999). Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status. Proc. Natl. Acad. Sci. USA 96, 6161-6165. https://doi.org/10.1073/pnas.96.11.6161
- Barata, A.G., and Dick, T.P. (2013). In vivo imaging of H2O2 production in Drosophila. Methods Enzymol. 526, 61-82. https://doi.org/10.1016/B978-0-12-405883-5.00004-1
- Barranco-Medina, S., Lazaro, J.J., and Dietz, K.J. (2009). The oligomeric conformation of peroxiredoxins links redox state to function. FEBS Lett. 583, 1809-1816. https://doi.org/10.1016/j.febslet.2009.05.029
- Bilan, D., and Belousov, V. (2015). HyPer family probes: state of the art. Antioxid. Redox Signal. [Epub ahead of Print] doi:10.1089/ars.2015.6586.
- Cao, Z., Bhella, D., and Lindsay, J.G. (2007). Reconstitution of the mitochondrial PrxIII antioxidant defence pathway: general properties and factors affecting PrxIII activity and oligomeric state. J. Mol. Biol. 372, 1022-1033. https://doi.org/10.1016/j.jmb.2007.07.018
- Chae, H.Z., Oubrahim, H., Park, J.W., Rhee, S.G., and Chock, P.B. (2012). Protein glutathionylation in the regulation of peroxiredoxins:a family of thiol-specific peroxidases that function as antioxidants, molecular chaperones, and signal modulators. Antioxid. Redox Signal. 16, 506-523. https://doi.org/10.1089/ars.2011.4260
- Chang, T.S., Jeong, W., Choi, S.Y., Yu, S., Kang, S.W., and Rhee, S.G. (2002). Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation. J. Biol. Chem. 277, 25370-25376. https://doi.org/10.1074/jbc.M110432200
- Cox, A.G., Pullar, J.M., Hughes, G., Ledgerwood, E.C., and Hampton, M.B. (2008). Oxidation of mitochondrial peroxiredoxin 3 during the initiation of receptor-mediated apoptosis. Free Rad. Biol. Med. 44, 1001-1009. https://doi.org/10.1016/j.freeradbiomed.2007.11.017
- Cox, A.G., Winterbourn, C.C., and Hampton, M.B. (2010). Measuring the redox state of cellular peroxiredoxins by immunoblotting. Methods Enzymol. 474, 51-66. https://doi.org/10.1016/S0076-6879(10)74004-0
- Delaunay, A., Pflieger, D., Barrault, M.B., Vinh, J. and Toledano, M.B. (2002). A thiol peroxidase is an H2O2 receptor and redoxtransducer in gene activation. Cell 111, 471-481. https://doi.org/10.1016/S0092-8674(02)01048-6
- Ermakova, Y.G., Bilan, D.S., Matlashov, M.E., Mishina, N.M., Markvicheva, K.N., Subach, O.M., Subach, F.V., Bogeski, I., Hoth, M., Enikolopov, G., et al. (2014). Red fluorescent genetically encoded indicator for intracellular hydrogen peroxide. Nat. Commun. 5, 5222. https://doi.org/10.1038/ncomms6222
- Ezerina, D., Morgan, B. and Dick, T.P. (2014) Imaging dynamic redox processes with genetically encoded probes. J. Mol. Cell. Cardiol. 73, 43-49. https://doi.org/10.1016/j.yjmcc.2013.12.023
- Hall, A., Nelson, K., Poole, L.B., and Karplus, P.A. (2011). Structurebased insights into the catalytic power and conformational dexterity of peroxiredoxins. Antioxid. Redox Signal. 15, 795-815. https://doi.org/10.1089/ars.2010.3624
- Hall, A., Sankaran, B., Poole, L.B., and Karplus, P.A. (2009). Structural changes common to catalysis in the Tpx peroxiredoxin subfamily. J. Mol. Biol. 393, 867-881. https://doi.org/10.1016/j.jmb.2009.08.040
- Jang, H.H., Kim, S.Y., Park, S.K., Jeon, H.S., Lee, Y.M., Jung, J.H., Lee, S.Y., Chae, H.B., Jung, Y.J., Lee, K.O., et al. (2006). Phosphorylation and concomitant structural changes in human 2-Cys peroxiredoxin isotype I differentially regulate its peroxidase and molecular chaperone functions. FEBS Lett. 580, 351-355. https://doi.org/10.1016/j.febslet.2005.12.030
- Konig, J., Galliardt, H., Jutte, P., Schaper, S., Dittmann, L., and Dietz, K.J. (2013). The conformational bases for the two functionalities of 2-Cysteine peroxiredoxins as peroxidase and chaperone. J. Exp. Bot. 64, 3483-3497. https://doi.org/10.1093/jxb/ert184
- Koo, K.H., Lee, S., Jeong, S.Y., Kim, E.T., Kim, H.J., Kim, K., Song, K., and Chae, H.Z. (2002). Regulation of thioredoxin peroxidase activity by C-terminal truncation. Arch. Biochem. Biophys. 397, 312-318. https://doi.org/10.1006/abbi.2001.2700
- Kumar, V., Kitaeff, N., Hampton, M.B., Cannell, M.B., and Winterbourn, C.C. (2009). Reversible oxidation of mitochondrial peroxiredoxin 3 in mouse heart subjected to ischemia and reperfusion. FEBS Lett. 583, 997-1000. https://doi.org/10.1016/j.febslet.2009.02.018
- Moon, J.C., Kim, G.M., Kim, E.K., Lee, H.N., Ha, B., Lee, S.Y., and Jang, H.H. (2013). Reversal of 2-Cys peroxiredoxin oligomerization by sulfiredoxin. Biochem. Biophys. Res. Commun. 432, 291-295. https://doi.org/10.1016/j.bbrc.2013.01.114
- Muthuramalingam, M., Seidel, T., Laxa, M., Nunes de Miranda, S.M., Gartner, F., Stroher, E., Kandlbinder, A., and Dietz, K.J. (2009). Multiple redox and non-redox interactions define 2-Cys peroxiredoxin as a regulatory hub in the chloroplast. Mol. Plant 2, 1273-1288. https://doi.org/10.1093/mp/ssp089
- Nelson, K.J., Parsonage, D., Karplus, P.A., and Poole, L.B. (2013). Evaluating peroxiredoxin sensitivity toward inactivation by peroxide substrates. Method Enzymol. 527, 21-40. https://doi.org/10.1016/B978-0-12-405882-8.00002-7
- Noichri, Y., Palais, G., Ruby, V., D'Autreaux, B., Delaunay-Moisan, A., Nystrom, T., Molin, M., and Toledano, M.B. (2015). In vivo parameters influencing 2-Cys Prx oligomerization: The role of enzyme sulfinylation. Redox Biol. 6, 326-333. https://doi.org/10.1016/j.redox.2015.08.011
- Parsonage, D., Youngblood, D.S., Sarma, G.N., Wood, Z.A., Karplus, P.A., and Poole, L.B. (2005). Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin. Biochemistry 44, 10583-10592. https://doi.org/10.1021/bi050448i
- Parsonage, D., Karplus, P.A., and Poole, L.B. (2008). Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin. Proc. Natl. Acad. Sci. USA 105, 8209-8214. https://doi.org/10.1073/pnas.0708308105
- Perkins, A., Poole, L.B., and Karplus, P.A. (2014). Tuning of peroxiredoxin catalysis for various physiological roles. Biochemistry 53, 7693-7705. https://doi.org/10.1021/bi5013222
- Perkins, A., Nelson, K.J., Parsonage, D., Poole, L.B., and Karplus, P.A. (2015). Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling. Trends Biochem. Sci. 40, 435-445. https://doi.org/10.1016/j.tibs.2015.05.001
- Poynton, R.A., and Hampton, M.B. (2014). Peroxiredoxins as biomarkers of oxidative stress. Biochimica Biophys. Acta 1840, 906-912. https://doi.org/10.1016/j.bbagen.2013.08.001
- Qu, D., Rashidian, J., Mount, M.P., Aleyasin, H., Parsanejad, M., Lira, A., Haque, E., Zhang, Y., Callaghan, S., Daigle, M., et al. (2007). Role of Cdk5-mediated phosphorylation of Prx2 in MPTP toxicity and Parkinson's disease. Neuron 55, 37-52. https://doi.org/10.1016/j.neuron.2007.05.033
- Randall, L.M., Manta, B., Hugo, M., Gil, M., Batthyany, C., Trujillo, M., Poole, L.B., and Denicola, A. (2014). Nitration transforms a sensitive peroxiredoxin 2 into a more active and robust peroxidase. J. Biol. Chem. 289, 15536-15543. https://doi.org/10.1074/jbc.M113.539213
- Rhee, S.G., and Woo, H.A. (2011). Multiple functions of peroxiredoxins:peroxidases, sensors and regulators of the intracellular messenger H(2)O(2), and protein chaperones. Antioxid. Redox Signal. 15, 781-794. https://doi.org/10.1089/ars.2010.3393
- Rhee, S.G., Woo, H.A., Kil, I.S., and Bae, S.H. (2012). Peroxiredoxin Functions as a Peroxidase and a Regulator and Sensor of Local Peroxides. J. Biol. Chem. 287, 4403-4410. https://doi.org/10.1074/jbc.R111.283432
- Sayed, A.A., and Williams, D.L. (2004). Biochemical characterization of 2-Cys peroxiredoxins from Schistosoma mansoni. J. Biol. Chem. 279, 26159-26166. https://doi.org/10.1074/jbc.M401748200
- Schwarzlander, M., Dick, T.P., Meyer, A.J., and Morgan, B. (2015). Dissecting redox biology using fluorescent protein sensors. Antioxid. Redox Signal. [Epub ahead of print]. dio:10.1089/ars.2015.6266
- Seidel, T., Seefeldt, B., Sauer, M., and Dietz, K.J. (2010). In vivo analysis of the 2-Cys peroxiredoxin oligomeric state by two-step FRET. J. Biotechnol. 149, 272-279. https://doi.org/10.1016/j.jbiotec.2010.06.016
- Seo, J.H., Lim, J.C., Lee, D.Y., Kim, K.S., Piszczek, G., Nam, H.W., Kim, Y.S., Ahn, T., Yun, C.H., Kim, K., et al. (2009). Novel protective mechanism against irreversible hyperoxidation of peroxiredoxin: Nalpha-terminal acetylation of human peroxiredoxin II. J. Biol. Chem. 284, 13455-13465. https://doi.org/10.1074/jbc.M900641200
- Sobotta, M.C., Barata, A.G., Schmidt, U., Mueller, S., Millonig, G., and Dick, T.P. (2013). Exposing cells to H2O2: a quantitative comparison between continuous low-dose and one-time highdose treatments. Free Rad. Biol. Med. 60, 325-335. https://doi.org/10.1016/j.freeradbiomed.2013.02.017
- Sobotta, M.C., Liou, W., Stocker, S., Talwar, D., Oehler, M., Ruppert, T., Scharf, A.N., and Dick, T.P. (2015). Peroxiredoxin-2 and STAT3 form a redox relay for H2O2 signaling. Nat. Chem. Biol. 11, 64-70. https://doi.org/10.1038/nchembio.1695
- Tarrago, L., Peterfi, Z., Lee, B.C., Michel, T., and Gladyshev, V.N. (2015). Monitoring methionine sulfoxide with stereospecific mechanism-based fluorescent sensors. Nat. Chem. Biol. 11, 332-338. https://doi.org/10.1038/nchembio.1787
- Teixeira, F., Castro, H., Cruz, T., Tse, E., Koldewey, P., Southworth, D.R., Tomas, A.M., and Jakob, U. (2015). Mitochondrial peroxiredoxin functions as crucial chaperone reservoir in Leishmania infantum. Proc. Natl. Acad. Sci. USA 112, E616-624. https://doi.org/10.1073/pnas.1419682112
- Trujillo, M., Clippe, A., Manta, B., Ferrer-Sueta, G., Smeets, A., Declercq, J.P., Knoops, B., and Radi, R. (2007). Pre-steady state kinetic characterization of human peroxiredoxin 5: taking advantage of Trp84 fluorescence increase upon oxidation. Arch. Biochem. Biophys. 467, 95-106. https://doi.org/10.1016/j.abb.2007.08.008
- Wang, X., Wang, L.K., Wang, X., Sun, F., and Wang, C.C. (2012). Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4. Biochem. J. 441, 113-118. https://doi.org/10.1042/BJ20110380
- Winterbourn, C.C. (2013). The biological chemistry of hydrogen peroxide. Methods Enzymol. 528, 3-25. https://doi.org/10.1016/B978-0-12-405881-1.00001-X
- Wood, Z.A., Poole, L.B., and Karplus, P.A. (2003). Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300, 650-653. https://doi.org/10.1126/science.1080405
- Zhao, Y., Araki, S., Wu, J., Teramoto, T., Chang, Y.F., Nakano, M., Abdelfattah, A.S., Fujiwara, M., Ishihara, T., Nagai, T., et al. (2011). An expanded palette of genetically encoded Ca(2)(+) indicators. Science 333, 1888-1891. https://doi.org/10.1126/science.1208592
- Zykova, T.A., Zhu, F., Vakorina, T.I., Zhang, J., Higgins, L.A., Urusova, D.V., Bode, A.M., and Dong, Z. (2010). T-LAK cell-originated protein kinase (TOPK) phosphorylation of Prx1 at Ser-32 prevents UVB-induced apoptosis in RPMI7951 melanoma cells through the regulation of Prx1 peroxidase activity. J. Biol. Chem. 285, 29138-29146. https://doi.org/10.1074/jbc.M110.135905
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