Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

Altschul, S. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.17.3389 · Cited by 73,302 · see citing works

Structure, mechanism and regulation of peroxiredoxins

Wood, Z. A., Schröder, E., Harris, J. R., & Poole, L. B. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)00003-8 · Cited by 2,546 · see citing works

Strategies of antioxidant defense

SIES, H. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb18025.x · Cited by 1,976 · see citing works

Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine).

Griffith, O. W., & Meister, A. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35980-5 · Cited by 1,683 · see citing works

Enhanced genome annotation using structural profiles in the program 3D-PSSM 1 1Edited by J. Thornton

Kelley, L. A., MacCallum, R. M., & Sternberg, M. J. E. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3741 · Cited by 1,462 · see citing works

Oxidant signals and oxidative stress

Finkel, T. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00002-4 · Cited by 1,393 · see citing works

Peroxiredoxin Evolution and the Regulation of Hydrogen Peroxide Signaling

Wood, Z. A., Poole, L. B., & Karplus, P. A. (2003) · Science · doi:10.1126/science.1080405 · Cited by 1,369 · see citing works

A workbench for multiple alignment construction and analysis

Schuler, G. D., Altschul, S. F., & Lipman, D. J. (1991) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340090304 · Cited by 985 · see citing works

ATP-dependent reduction of cysteine–sulphinic acid by S. cerevisiae sulphiredoxin

Biteau, B., Labarre, J., & Tolédano, M. B. (2003) · Nature · doi:10.1038/nature02075 · Cited by 970 · see citing works

Thioredoxin-dependent peroxide reductase from yeast.

Chae, H. Z., Chung, S., & Rhee, S. G. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47038-x · Cited by 960 · see citing works

Alkyl Hydroperoxide Reductase Is the Primary Scavenger of Endogenous Hydrogen Peroxide in Escherichia coli

Seaver, L. C., & Imlay, J. A. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.24.7173-7181.2001 · Cited by 797 · see citing works

Peroxynitrite reductase activity of bacterial peroxiredoxins

Bryk, R., Griffin, P. R., & Nathan, C. (2000) · Nature · doi:10.1038/35025109 · Cited by 679 · see citing works

Reversing the Inactivation of Peroxiredoxins Caused by Cysteine Sulfinic Acid Formation

Woo, H. A., Chae, H. Z., Hwang, S. C., Yang, K., Kang, S. W., Kim, K., & Rhee, S. G. (2003) · Science · doi:10.1126/science.1080273 · Cited by 558 · see citing works

Inactivation of Human Peroxiredoxin I during Catalysis as the Result of the Oxidation of the Catalytic Site Cysteine to Cysteine-sulfinic Acid

Yang, K.-S., Kang, S. W., Woo, H. A., Hwang, S. C., Chae, H. Z., Kim, K., & Rhee, S. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206626200 · Cited by 458 · see citing works

Metabolic Enzymes of Mycobacteria Linked to Antioxidant Defense by a Thioredoxin-Like Protein

Bryk, R., Lima, C. D., Erdjument‐Bromage, H., Tempst, P., & Nathan, C. (2002) · Science · doi:10.1126/science.1067798 · Cited by 400 · see citing works

Proteomics Analysis of Cellular Response to Oxidative Stress

Rabilloud, T., Heller, M., Gasnier, F., Luche, S., Rey, C., Aebersold, R., Benahmed, M., Louisot, P., & Lunardi, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106585200 · Cited by 393 · see citing works

Identification of a novel stress-responsive gene Hi95 involved in regulation of cell viability

Budanov, A. V., Shoshani, T., Faerman, A., Zelin, E., Kamer, I., Kalinski, H., Gorodin, S., Fishman, A., Chajut, A., Einat, P., et al. (2002) · Oncogene · doi:10.1038/sj.onc.1205877 · Cited by 363 · see citing works

Dimerization of thiol-specific antioxidant and the essential role of cysteine 47.

Chae, H. Z., Uhm, T.-B., & Rhee, S. G. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.15.7022 · Cited by 309 · see citing works

PA26, a novel target of the p53 tumor suppressor and member of the GADD family of DNA damage and growth arrest inducible genes

Velasco-Miguel, S., Buckbinder, L., Jean, P., Gelbert, L., Talbott, R. L., Laidlaw, J. L., Seizinger, B. R., & Kley, N. (1999) · Oncogene · doi:10.1038/sj.onc.1202274 · Cited by 249 · see citing works

Alkyl Hydroperoxide Reductase Subunit C (AhpC) Protects Bacterial and Human Cells against Reactive Nitrogen Intermediates

Chen, L., Xie, Q. W., & Nathan, C. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80079-9 · Cited by 222 · see citing works

Mammalian Thioredoxin Reductase Is Irreversibly Inhibited by Dinitrohalobenzenes by Alkylation of Both the Redox Active Selenocysteine and Its Neighboring Cysteine Residue

Nordberg, J., Zhong, L., Holmgren, A., & Arnér, E. S. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.18.10835 · Cited by 200 · see citing works

Cooperation of Yeast Peroxiredoxins Tsa1p and Tsa2p in the Cellular Defense against Oxidative and Nitrosative Stress

Wong, C., Zhou, Y., Ng, R. W. M., Kung, H., & Jin, D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106846200 · Cited by 174 · see citing works

Regeneration of Peroxiredoxins during Recovery after Oxidative Stress

Chevallet, M., Wagner, E., Luche, S., DORSSELAER, A. V., Leize‐Wagner, E., & Rabilloud, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305161200 · Cited by 153 · see citing works

An Overoxidation Journey with a Return Ticket

Georgiou, G. N., & Masip, L. (2003) · Science · doi:10.1126/science.1084976 · Cited by 122 · see citing works

Variants of peroxiredoxins expression in response to hydroperoxide stress

Mitsumoto, A., Takanezawa, Y., Okawa, K., Iwamatsu, A., & Nakagawa, Y. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00503-7 · Cited by 119 · see citing works

PA26 is a candidate gene for heterotaxia in humans: identification of a novel PA26-related gene family in human and mouse

Peeters, H., Debeer, P., Bairoch, A., Wilquet, V., Huysmans, C., Parthoens, E., Fryns, J. P., Gewillig, M. H. M. L., Nakamura, Y., Niikawa, N., et al. (2003) · Human Genetics · doi:10.1007/s00439-003-0917-5 · Cited by 117 · see citing works

Role of Peroxidoxins in Leishmania chagasiSurvival

Barr, S. D., & Gedamu, L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212990200 · Cited by 110 · see citing works

The Crystal Structure of Mycobacterium tuberculosisAlkylhydroperoxidase AhpD, a Potential Target for Antitubercular Drug Design

Nunn, C. M., Djordjević, S., Hillas, P. J., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200864200 · Cited by 43 · see citing works

The Mechanism of Mycobacterium tuberculosis Alkylhydroperoxidase AhpD as Defined by Mutagenesis, Crystallography, and Kinetics

Koshkin, A., Nunn, C. M., Djordjević, S., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303747200 · Cited by 43 · see citing works

ROS function in redox signaling and oxidative stress

Schieber, M., & Chandel, N. S. (2014) · Current Biology · doi:10.1016/j.cub.2014.03.034 · Cited by 6,931 · see citing works

Regulation of cancer cell metabolism

Cairns, R. A., Harris, I. S., & Mak, T. W. (2011) · Nature Reviews Cancer · doi:10.1038/nrc2981 · Cited by 4,744 · see citing works

ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis

D'Autréaux, B., & Toledano, M. B. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2256 · Cited by 3,642 · see citing works

TIGAR, a p53-Inducible Regulator of Glycolysis and Apoptosis

Bensaad, K., Tsuruta, A., Selak, M. A., Vidal, M. N. C., Nakano, K., Bartrons, R., Gottlieb, E., & Vousden, K. H. (2006) · Cell · doi:10.1016/j.cell.2006.05.036 · Cited by 2,019 · see citing works

Synaptic versus extrasynaptic NMDA receptor signalling: implications for neurodegenerative disorders

Hardingham, G. E., & Bading, H. (2010) · Nature Reviews Neuroscience · doi:10.1038/nrn2911 · Cited by 1,644 · see citing works

Hydrogen peroxide sensing and signaling

Veal, E. A., Day, A. M., & Morgan, B. A. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.03.016 · Cited by 1,604 · see citing works

Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling.

Lee, J., Giordano, S., & Zhang, J. (2012) · Biochemical Journal · doi:10.1042/bj20111451 · Cited by 1,438 · see citing works

p53 Target Genes Sestrin1 and Sestrin2 Connect Genotoxic Stress and mTOR Signaling

Budanov, A. V., & Karin, M. (2008) · Cell · doi:10.1016/j.cell.2008.06.028 · Cited by 1,326 · see citing works

The Control of the Metabolic Switch in Cancers by Oncogenes and Tumor Suppressor Genes

Levine, A. J., & Puzio-Kuter, A. M. (2010) · Science · doi:10.1126/science.1193494 · Cited by 1,243 · see citing works

Autophagy in malignant transformation and cancer progression

Galluzzi, L., Pietrocola, F., Bravo‐San Pedro, J. M., Amaravadi, R. K., Baehrecke, E. H., Cecconi, F., Codogno, P., Debnath, J., Gewirtz, D. A., Karantza, V., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201490784 · Cited by 1,182 · see citing works

Serine starvation induces stress and p53-dependent metabolic remodelling in cancer cells

Maddocks, O. D. K., Berkers, C. R., Mason, S. M., Zheng, L., Blyth, K., Gottlieb, E., & Vousden, K. H. (2013) · Nature · doi:10.1038/nature11743 · Cited by 1,007 · see citing works

p53 and metabolism

Vousden, K. H., & Ryan, K. M. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2715 · Cited by 959 · see citing works

ROS Generation and Antioxidant Defense Systems in Normal and Malignant Cells

Snezhkina, A. V., Kudryavtseva, A. V., Kardymon, O. L., Savvateeva, M. V., Melnikova, N. V., Krasnov, G. S., & Dmitriev, A. A. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/6175804 · Cited by 934 · see citing works

The CASTOR Proteins Are Arginine Sensors for the mTORC1 Pathway

Chantranupong, L., Scaria, S. M., Saxton, R. A., Gygi, M. P., Shen, K., Wyant, G. A., Wang, T., Harper, J. W., Gygi, S. P., & Sabatini, D. M. (2016) · Cell · doi:10.1016/j.cell.2016.02.035 · Cited by 843 · see citing works

Glutaminase 2, a novel p53 target gene regulating energy metabolism and antioxidant function

Hu, W., Zhang, C., Wu, R., Sun, Y., Levine, A., & Feng, Z. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1001006107 · Cited by 862 · see citing works

Redox-based regulation of signal transduction: principles, pitfalls, and promises

Janssen-Heininger, Y. M. W., Mossman, B. T., Heintz, N. H., Forman, H. J., Kalyanaraman, B., Finkel, T., Stamler, J. S., Rhee, S. G., & van der Vliet, A. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.011 · Cited by 784 · see citing works

Akt Determines Replicative Senescence and Oxidative or Oncogenic Premature Senescence and Sensitizes Cells to Oxidative Apoptosis

Nogueira, V., Park, Y., Chen, C.-C., Xu, P.-Z., Chen, M.-L., Tonic, I., Unterman, T., & Hay, N. (2008) · Cancer Cell · doi:10.1016/j.ccr.2008.11.003 · Cited by 780 · see citing works

Acetylation of the p53 DNA-binding domain regulates apoptosis induction.

Sykes, S. M., Mellert, H. S., Holbert, M. A., Li, K., Marmorstein, R., Lane, W. S., & McMahon, S. B. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.11.026 · Cited by 752 · see citing works

Phosphate-activated glutaminase (GLS2), a p53-inducible regulator of glutamine metabolism and reactive oxygen species

Suzuki, S., Tanaka, T., Poyurovsky, M. V., Nagano, H., Mayama, T., Ohkubo, S., Lokshin, M., Hosokawa, H., Nakayama, T., Suzuki, Y., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002459107 · Cited by 705 · see citing works

Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors

Kwon, J., Lee, S.-R., Yang, K.-S., Ahn, Y., Kim, Y. J., Stadtman, E. R., & Rhee, S. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407396101 · Cited by 631 · see citing works

Sestrin as a feedback inhibitor of TOR that prevents age-related pathologies

Lee, J. H., Budanov, A. V., Park, E. J., Birse, R., Kim, T. E., Perkins, G. A., Ocorr, K., Ellisman, M. H., Bodmer, R., Bier, E., et al. (2010) · Science · doi:10.1126/science.1182228 · Cited by 570 · see citing works

ROS in Cancer: The Burning Question

Chio, I. I. C., & Tuveson, D. A. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.03.004 · Cited by 532 · see citing works

Coping with stress: multiple ways to activate p53

Horn, H. F., & Vousden, K. H. (2007) · Oncogene · doi:10.1038/sj.onc.1210263 · Cited by 522 · see citing works

Synaptic NMDA receptor activity boosts intrinsic antioxidant defenses

Papadia, S., Soriano, F. X., Léveillé, F., Martel, M.-A., Dakin, K. A., Hansen, H. H., Kaindl, A., Sifringer, M., Fowler, J., Stefovska, V., et al. (2008) · Nature Neuroscience · doi:10.1038/nn2071 · Cited by 498 · see citing works

Sestrins activate Nrf2 by promoting p62-dependent autophagic degradation of Keap1 and prevent oxidative liver damage

Bae, S. H., Sung, S. H., Oh, S. Y., Lim, J. M., Lee, S. K., Park, Y. N., Lee, H. E., Kang, D., & Rhee, S. G. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2012.12.002 · Cited by 492 · see citing works

Mitochondrial Uncoupling: A Key Controller of Biological Processes in Physiology and Diseases

Demine, S., Renard, P., & Arnould, T. (2019) · Cells · doi:10.3390/cells8080795 · Cited by 476 · see citing works

The Sestrins Interact with GATOR2 to Negatively Regulate the Amino-Acid-Sensing Pathway Upstream of mTORC1

Chantranupong, L., Wolfson, R. L., Orozco, J. M., Saxton, R. A., Scaria, S. M., Bar-Peled, L., Spooner, E., Isasa, M., Gygi, S. P., & Sabatini, D. M. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.09.014 · Cited by 466 · see citing works

Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway

Saxton, R. A., Knockenhauer, K. E., Wolfson, R. L., Chantranupong, L., Pacold, M. E., Wang, T., Schwartz, T. U., & Sabatini, D. M. (2016) · Science · doi:10.1126/science.aad2087 · Cited by 457 · see citing works

Delayed ageing through damage protection by the Arf/p53 pathway

Matheu, A., Maraver, A., Klatt, P., Flores, I., Garcia-Cao, I., Borras, C., Flores, J. M., Viña, J., Blasco, M. A., & Serrano, M. (2007) · Nature · doi:10.1038/nature05949 · Cited by 466 · see citing works

Multiple Functions of Peroxiredoxins: Peroxidases, Sensors and Regulators of the Intracellular Messenger H ₂ O ₂ , and Protein Chaperones

Rhee, S. G., & Woo, H. A. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3393 · Cited by 463 · see citing works

Dynamic redox control of NF-κB through glutaredoxin-regulated S-glutathionylation of inhibitory κB kinase β

Reynaert, N. L., van der Vliet, A., Guala, A. S., McGovern, T., Hristova, M., Pantano, C., Heintz, N. H., Heim, J., Ho, Y.-S., Matthews, D. E., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603290103 · Cited by 442 · see citing works

Characterization of Mammalian Sulfiredoxin and Its Reactivation of Hyperoxidized Peroxiredoxin through Reduction of Cysteine Sulfinic Acid in the Active Site to Cysteine

Chang, T.-S., Jeong, W., Woo, H. A., Lee, S. M., Park, S., & Rhee, S. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409482200 · Cited by 388 · see citing works

Sestrins inhibit mTORC1 kinase activation through the GATOR complex

Parmigiani, A., Nourbakhsh, A., Ding, B., Wang, W., Kim, Y. C., Akopiants, K., Guan, K.-L., Karin, M., & Budanov, A. V. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.10.019 · Cited by 336 · see citing works

Mechanisms of Ascorbate-Induced Cytotoxicity in Pancreatic Cancer

Du, J., Martin, S. M., Levine, M., Wagner, B. A., Buettner, G. R., Wang, S.-H., Taghiyev, A. F., Du, C., Knudson, C. M., & Cullen, J. J. (2010) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-09-1713 · Cited by 316 · see citing works

Maintenance of metabolic homeostasis by Sestrin2 and Sestrin3

Lee, J. H., Budanov, A. V., Talukdar, S., Park, E. J., Park, H. L., Park, H.-W., Bandyopadhyay, G., Li, N., Aghajan, M., Jang, I., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.08.004 · Cited by 295 · see citing works

The Role of p53 in Metabolic Regulation

Puzio-Kuter, A. M. (2011) · Genes & Cancer · doi:10.1177/1947601911409738 · Cited by 273 · see citing works

Sestrins function as guanine nucleotide dissociation inhibitors for Rag GTPases to control mTORC1 signaling

Peng, M., Yin, N., & Li, M. O. (2014) · Cell · doi:10.1016/j.cell.2014.08.038 · Cited by 220 · see citing works

Stressin’ Sestrins take an aging fight

Budanov, A. V., Lee, J. H., & Karin, M. (2010) · EMBO Molecular Medicine · doi:10.1002/emmm.201000097 · Cited by 208 · see citing works

Regulation of AIF expression by p53

Stambolsky, P., Weisz, L., Shats, I., Klein, Y., Goldfinger, N., Oren, M., & Rotter, V (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401965 · Cited by 194 · see citing works

Sestrin prevents atrophy of disused and aging muscles by integrating anabolic and catabolic signals

Segalés, J., Perdiguero, E., Serrano, A. L., Sousa-Victor, P., Ortet, L., Jardí, M., Budanov, A. V., Garcia-Prat, L., Sandri, M., Thomson, D. M., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-13832-9 · Cited by 153 · see citing works

The role of tumor suppressor p53 in the antioxidant defense and metabolism

Budanov, A. V. (2014) · Subcellular Biochemistry · doi:10.1007/978-94-017-9211-0_18 · Cited by 157 · see citing works

Calcium signaling alterations, oxidative stress, and autophagy in aging

Ureshino, R. P., Rocha, K. K., Lopes, G. S., Bincoletto, C., & Smaili, S. S. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5777 · Cited by 143 · see citing works

The antioxidant function of sestrins is mediated by promotion of autophagic degradation of Keap1 and Nrf2 activation and by inhibition of mTORC1

Rhee, S. G., & Bae, S. H. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.007 · Cited by 141 · see citing works

Forkhead Box O as a Sensor, Mediator, and Regulator of Redox Signaling

de Keizer, P. L. J., Burgering, B. M. T., & Dansen, T. B. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3403 · Cited by 131 · see citing works

Regulation of nucleotide metabolism by mutant p53 contributes to its gain-of-function activities

Kollareddy, M., Dimitrova, E., Vallabhaneni, K. C., Chan, A., Le, T., Chauhan, K. M., Carrero, Z. I., Ramakrishnan, G., Watabe, K., Haupt, Y., et al. (2015) · Nature Communications · doi:10.1038/ncomms8389 · Cited by 127 · see citing works

Sestrin 3 protein enhances hepatic insulin sensitivity by direct activation of the mTORC2-Akt signaling

Tao, R., Xiong, X., Liangpunsakul, S., & Dong, X. C. (2015) · Diabetes · doi:10.2337/db14-0539 · Cited by 96 · see citing works

A distinct p53 target gene set predicts for response to the selective p53–HDM2 inhibitor NVP-CGM097

Jeay, S., Gaulis, S., Ferretti, S., Bitter, H., Ito, M., Valat, T., Murakami, M., Ruetz, S., Guthy, D. A., Rynn, C., et al. (2015) · eLife · doi:10.7554/elife.06498 · Cited by 85 · see citing works

P53 coordinates decidual sestrin 2/AMPK/mTORC1 signaling to govern parturition timing

Deng, W., Cha, J., Yuan, J., Haraguchi, H., Bartos, A., Leishman, E., Viollet, B., Bradshaw, H. B., Hirota, Y., & Dey, S. K. (2016) · Journal of Clinical Investigation · doi:10.1172/jci87715 · Cited by 85 · see citing works

Sestrin2 protects dopaminergic cells against rotenone toxicity through AMPK-Dependent autophagy activation

Hou, Y.-S., Guan, J.-J., Xu, H.-D., Wu, F., Sheng, R., & Qin, Z.-H. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00285-15 · Cited by 87 · see citing works

Resveratrol inhibits LXRα-dependent hepatic lipogenesis through novel antioxidant Sestrin2 gene induction

Jin, S. H., Yang, J. H., Shin, B. Y., Seo, K., Shin, S. M., Cho, I. J., & Ki, S. H. (2013) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2013.04.023 · Cited by 83 · see citing works

Regulation of Metabolic Activity by p53

Flöter, J., Kaymak, I., & Schulze, A. (2017) · Metabolites · doi:10.3390/metabo7020021 · Cited by 81 · see citing works

AMPK signaling in skeletal muscle during exercise: Role of reactive oxygen and nitrogen species

Morales-Alamo, D., & Calbet, J. A. L. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.01.012 · Cited by 72 · see citing works

CNS Peroxiredoxins and Their Regulation in Health and Disease

Bell, K. F. S., & Hardingham, G. E. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3567 · Cited by 71 · see citing works

Recent insights into the biological functions of sestrins in health and disease

Wang, M., Xu, Y., Liu, J., Ye, J., Yuan, W., Jiang, H., Wang, Z., Jiang, H., & Wan, J. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000484060 · Cited by 67 · see citing works

Sestrin2 Protein Positively Regulates AKT Enzyme Signaling and Survival in Human Squamous Cell Carcinoma and Melanoma Cells

Zhao, B., Shah, P., Budanov, A. V., Qiang, L., Ming, M., Aplin, A., Sims, D. M., & He, Y.-Y. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.595397 · Cited by 61 · see citing works

Lymphocytes from rheumatoid arthritis patients have elevated levels of intracellular peroxiredoxin 2, and a greater frequency of cells with exofacial peroxiredoxin 2, compared with healthy human lymphocytes

Szabó-Taylor, K. É., Eggleton, P., Turner, C. A. L., Faro, M. L. L., Tarr, J. M., Tóth, S., Whiteman, M., Haigh, R. C., Littlechild, J. A., & Winyard, P. G. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.04.016 · Cited by 45 · see citing works

Distinct Role of Sesn2 in Response to UVB‐Induced DNA Damage and UVA‐Induced Oxidative Stress in Melanocytes

Zhao, B., Shah, P., Qiang, L., He, T., Budanov, A., & He, Y. (2017) · Photochemistry and Photobiology · doi:10.1111/php.12624 · Cited by 44 · see citing works

Minocycline Inhibits ICAD Degradation and the NF-ΚB Activation Induced by 6-OHDA in PC12 Cells

Jiang, B.-P., Le, L., Xu, L.-J., & Xiao, P.-G. (2014) · Brain Research · doi:10.1016/j.brainres.2014.08.001 · Cited by 19 · see citing works

Lack of p53 Affects the Expression of Several Brain Mitochondrial Proteins: Insights from Proteomics into Important Pathways Regulated by p53

Fiorini, A., Sultana, R., Barone, E., Cenini, G., Perluigi, M., Mancuso, C., Cai, J., Klein, J. B., St. Clair, D., & Butterfield, D. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049846 · Cited by 16 · see citing works

Spectrophotometric determination of hydrogen peroxide: catalase activity and rates of hydrogen peroxide removal by erythrocytes

Masuoka, N., Wakimoto, M., UBUKA, T., & Nakano, T. (1996) · Clinica Chimica Acta · doi:10.1016/0009-8981(96)06374-7 · Cited by 56 · see citing works

Regulation of Protein Synthesis by Hydrogen Peroxide in Crowns of Winter Wheat

Matsuda, Y., Okuda, T., & Sagisaka, S. (1994) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.58.906 · Cited by 21 · see citing works

Self-Decomposition Characteristic of Concentrated Hydrogen Peroxide with Temperature and Stabilizer

Chung, S.-M., An, S., & Kwon, S. (2009) · Journal of the Korean Society of Propulsion Engineers · Cited by 1 · see citing works

Microbicidal activity of N-chlorotaurine in combination with hydrogen peroxide

Mustedanagic, J., Ximenes, V. F., & Nagl, M. (2017) · AMB Express · doi:10.1186/s13568-017-0404-3 · Cited by 5 · see citing works

Influence of Hydrogen Peroxide on COD in Wastewater

Barlin, S. (2003) · Environment Protection In Petrochemical Industry