Proteomics Analysis of Cellular Response to Oxidative Stress

Strategies of antioxidant defense

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

Thioredoxin-dependent peroxide reductase from yeast.

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Mammalian Peroxiredoxin Isoforms Can Reduce Hydrogen Peroxide Generated in Response to Growth Factors and Tumor Necrosis Factor-α

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The H2O2 Stimulon in Saccharomyces cerevisiae

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Improvement of the solubilization of proteins in two‐dimensional electrophoresis with immobilized pH gradients

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Regulatory Role for a Novel Human Thioredoxin Peroxidase in NF-κB Activation

Jin, D., Chae, H. Z., Rhee, S. G., & Jeang, K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.49.30952 · Cited by 412

Differential regulation of antioxidant enzymes in response to oxidants.

Shull, S., Heintz, N. H., Periasamy, M., Manohar, M., Janssen, Y. M., Marsh, J. P., & Mossman, B. T. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54242-3 · Cited by 403

Cloning and Expression of a Novel Mammalian Thioredoxin

Spyrou, G., Enmark, E., Miranda‐Vizuete, A., & Gustafsson, J.-Α. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.5.2936 · Cited by 399

Crystal structure of a novel human peroxidase enzyme at 2.0 Å resolution

Choi, H., Kang, S. W., Yang, C., Rhee, S. G., & Ryu, S.-E. (1998) · Nature Structural Biology · doi:10.1038/nsb0598-400 · Cited by 382

Thioredoxin Peroxidase Is a Novel Inhibitor of Apoptosis with a Mechanism Distinct from That of Bcl-2

Zhang, P., Liu, B., Kang, S. W., Seo, M. S., Rhee, S. G., & Obeid, L. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.49.30615 · Cited by 370

A proteomic approach to identify early molecular targets of oxidative stress in human epithelial lens cells

Paron, I., D'Elia, A. V., DˈAmbrosio, C., Scaloni, A., D’Aurizio, F., Prescott, A. R., Damante, G., & Tell, G. (2004) · Biochemical Journal · doi:10.1042/bj20031190 · Cited by 97

Measuring the Redox State of Cellular Peroxiredoxins by Immunoblotting

Cox, A. G., Winterbourn, C. C., & Hampton, M. B. (2010) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(10)74004-0 · Cited by 96

Sestrin 2 Is Not a Reductase for Cysteine Sulfinic Acid of Peroxiredoxins

Woo, H. A., Bae, S. H., Park, S., & Rhee, S. G. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2360 · Cited by 101

Substrate Specificity, Localization, and Essential Role of the Glutathione Peroxidase-type Tryparedoxin Peroxidases in Trypanosoma brucei

Schlecker, T., Schmidt, A., Dirdjaja, N., Voncken, F. G. J., CLAYTON, C. E., & Krauth‐Siegel, R. L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413338200 · Cited by 98

Oxidative stress triggers thiol oxidation in the glyceraldehyde‐3‐phosphate dehydrogenase of Staphylococcus aureus

Weber, H., Engelmann, S., Becher, D., & Hecker, M. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.03971.x · Cited by 93

Towards a comprehensive understanding of Bacillus subtilis cell physiology by physiological proteomics

Hecker, M., & Völker, U. (2004) · PROTEOMICS · doi:10.1002/pmic.200401017 · Cited by 93

A bibliometric analysis of research on proteomics in Science Citation Index Expanded

Tan, J., Fu, H., & Ho, Y. (2013) · Scientometrics · doi:10.1007/s11192-013-1125-2 · Cited by 100

Differential Kinetics of Two-Cysteine Peroxiredoxin Disulfide Formation Reveal a Novel Model for Peroxide Sensing

Portillo‐Ledesma, S., Randall, L. M., Parsonage, D., Rizza, J. D., Karplus, P. A., Poole, L. B., Denicola, A., & Ferrer‐Sueta, G. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00188 · Cited by 92

Role of peroxiredoxin2 downregulation in recurrent miscarriage through regulation of trophoblast proliferation and apoptosis

Wu, F., Tian, F., Zeng, W., Liu, X., Fan, J., Lin, Y. C., & Zhang, Y. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.301 · Cited by 87

Nanoisozymes: Crystal‐Facet‐Dependent Enzyme‐Mimetic Activity of V2O5 Nanomaterials

Ghosh, S., Roy, P., Karmodak, N., Jemmis, E. D., & Mugesh, G. (2018) · Angewandte Chemie · doi:10.1002/ange.201800681 · Cited by 87

Impaired homeostasis and phenotypic abnormalities in Prdx6−/−mice lens epithelial cells by reactive oxygen species: increased expression and activation of TGFβ

Fatma, N., Kubo, E., Sharma, P., Beier, D. R., & Singh, D. P. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401597 · Cited by 90

The sulfiredoxin–peroxiredoxin (Srx–Prx) axis in cell signal transduction and cancer development

Mishra, M., Jiang, H., Wu, L., Chawsheen, H. A., & Wei, Q. (2015) · Cancer Letters · doi:10.1016/j.canlet.2015.07.002 · Cited by 90

Oxidative stress and counteracting mechanisms in hormone receptor positive, triple-negative and basal-like breast carcinomas

Karihtala, P., Kauppila, S., Soini, Y., & Arja-Jukkola-Vuorinen (2011) · BMC Cancer · doi:10.1186/1471-2407-11-262 · Cited by 87

Localized redox relays as a privileged mode of cytoplasmic hydrogen peroxide signaling

Travasso, R. D. M., dos Aidos, F. S., Bayani, A., Abranches, P., & Salvador, A. (2017) · Redox Biology · doi:10.1016/j.redox.2017.01.003 · Cited by 89

The role of protein quality control in mitochondrial protein homeostasis under oxidative stress

Bender, T., Leidhold, C., Ruppert, T., Franken, S., & Voos, W. (2010) · PROTEOMICS · doi:10.1002/pmic.200800619 · Cited by 86

Peroxiredoxin 1 Interacts with Androgen Receptor and Enhances Its Transactivation

Park, S., Yu, X., Ip, C. C. Y., Mohler, J. L., Bogner, P. N., & Park, Y. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-0651 · Cited by 81

Fluorescence thiol modification assay: oxidatively modified proteins in Bacillus subtilis

Hochgräfe, F., Mostertz, J., Albrecht, D., & Hecker, M. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04845.x · Cited by 81

Proteomics of immune-challenged Drosophila melanogaster larvae hemolymph

Guedes, S. D. M., Vitorino, R. M. P., Domingues, R., Tomer, K. B., Correia, A. J. F., Amado, F. M. L., & Domingues, P. M. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.12.135 · Cited by 80

Something Old, Something New, Something Borrowed; How the Thermoacidophilic Archaeon Sulfolobus solfataricus Responds to Oxidative Stress

Maaty, W. S. A., Wiedenheft, B., Tarlykov, P., Schaff, N., Heinemann, J. V., Robison-Cox, J., Valenzuela, J. J., Dougherty, A., Blum, P., Lawrence, C. M., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006964 · Cited by 78

Nanoparticle-induced oxidation of corona proteins initiates an oxidative stress response in cells

Jayaram, D. T., Runa, S., Kemp, M. L., & Payne, C. K. (2017) · Nanoscale · doi:10.1039/c6nr09500c · Cited by 77

Measurement of Peroxiredoxin Activity

Nelson, K. J., & Parsonage, D. (2011) · Current Protocols in Toxicology · doi:10.1002/0471140856.tx0710s49 · Cited by 78

Oxidative stress modulates heme synthesis and induces peroxiredoxin-2 as a novel cytoprotective response in -thalassemic erythropoiesis

Franceschi, L. D., Bertoldi, M., Falco, L. D., Franco, S. S., Ronzoni, L., Turrini, F., Colancecco, A., Camaschella, C., Cappellini, M. D., & Iolascon, A. (2011) · Haematologica · doi:10.3324/haematol.2011.043612 · Cited by 77

Loss of PKC-δ alters cardiac metabolism

Mayr, M., Chung, Y., Mayr, U., McGregor, E., Troy, H., Baier, G., Leitges, M., Dunn, M. J., Griffiths, J. R., & Xu, Q. (2004) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00877.2003 · Cited by 77

SIRT2 Deacetylates and Inhibits the Peroxidase Activity of Peroxiredoxin-1 to Sensitize Breast Cancer Cells to Oxidant Stress-Inducing Agents

Fiskus, W. C., Coothankandaswamy, V., Chen, J., Ma, H., Ha, K., Saenz, D. T., Krieger, S., Mill, C. P., Sun, B., Huang, P., et al. (2016) · Cancer Research · doi:10.1158/0008-5472.can-16-0126 · Cited by 77

Novel hyperoxidation resistance motifs in 2-Cys peroxiredoxins

Bolduc, J. A., Nelson, K. J., Haynes, A. C., Lee, J., Reisz, J. A., Graff, A. H., Clodfelter, J. E., Parsonage, D., Poole, L. B., Furdui, C. M., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.001690 · Cited by 79

Typical 2‐Cys peroxiredoxins – modulation by covalent transformations and noncovalent interactions

Arán, M., Ferrero, D. S., Pagano, E. A., & Wolosiuk, R. A. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.06984.x · Cited by 74

What Room for Two-Dimensional Gel-Based Proteomics in a Shotgun Proteomics World?

Marcus, K., Lelong, C., & Rabilloud, T. (2020) · Proteomes · doi:10.3390/proteomes8030017 · Cited by 75

Hexameric oligomerization of mitochondrial peroxiredoxin PrxIIF and formation of an ultrahigh affinity complex with its electron donor thioredoxin Trx-o

Barranco-Medina, S., Krell, T., Bernier-Villamor, L., Sevilla, F., Lázaro, J. J., & Dietz, K. (2008) · Journal of Experimental Botany · doi:10.1093/jxb/ern177 · Cited by 70

Two-dimensional differential in-gel electrophoresis–based proteomics of male gametes in relation to oxidative stress

Hamada, A., Sharma, R. K., du Plessis, S. S., Willard, B. B., Yadav, S. P., Sabanegh, E., & Agarwal, A. K. (2013) · Fertility and Sterility · doi:10.1016/j.fertnstert.2012.11.046 · Cited by 70

Proteomic profiling for cancer progression: Differential display analysis for the expression of intracellular proteins between regressive and progressive cancer cell lines

Hayashi, E., Kuramitsu, Y., Okada, F., Fujimoto, M., Zhang, X., Kobayashi, M., Iizuka, N., Ueyama, Y., & Nakamura, K. (2005) · PROTEOMICS · doi:10.1002/pmic.200401132 · Cited by 69

A parallel proteomic and metabolomic analysis of the hydrogen peroxide‐ and Sty1p‐dependent stress response in Schizosaccharomyces pombe

Weeks, M. E., Sinclair, J., Butt, A., Chung, Y., Worthington, J. L., Wilkinson, C. R. M., Griffiths, J. R., Jones, N., Waterfield, M. D., & Timms, J. F. (2006) · PROTEOMICS · doi:10.1002/pmic.200500741 · Cited by 68

Differential Proteomic Analysis of Arabidopsis thaliana Genotypes Exhibiting Resistance or Susceptibility to the Insect Herbivore, Plutella xylostella

Collins, R. M., Afzal, M., Ward, D. A., Prescott, M. C., Sait, S. M., Rees, H. H., & Tomsett, A. B. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010103 · Cited by 67

Oxidative proteome modifications target specific cellular pathways during oxidative stress, cellular senescence and aging

Baraibar, M. A., & Friguet, B. (2012) · Experimental Gerontology · doi:10.1016/j.exger.2012.10.007 · Cited by 66

Mitochondrial Peroxiredoxin III is a Potential Target for Cancer Therapy

Song, I.-S., Kim, H.-K., Jeong, S.-H., Lee, S., Kim, N., Rhee, B. D., Ko, K. S., & Han, J. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12107163 · Cited by 67

Dual Role of Peroxiredoxin I in Macrophage-derived Foam Cells

Conway, J., & Kinter, M. T. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605026200 · Cited by 66

Global Investigation of p53-induced Apoptosis Through Quantitative Proteomic Profiling Using Comparative Amino Acid-coded Tagging

Gu, S., Liu, Z., Pan, S., Jiang, Z., Lu, H., Amit, O., Bradbury, E. M., Hu, C. A., & Chen, X. (2004) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400033-mcp200 · Cited by 66

Antioxidant defense in hibernation: Cloning and expression of peroxiredoxins from hibernating ground squirrels, Spermophilus tridecemlineatus

Morin, P., & Storey, K. B. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.01.035 · Cited by 65

Expression and regulation of peroxiredoxin 5 in human osteoarthritis

Wang, M.-X., Wei, A., Yuan, J. J., Trickett, A. E., Knoops, B., & Murrell, G. A. C. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03511-1 · Cited by 65

IDH2 deficiency increases the liver susceptibility to ischemia-reperfusion injury via increased mitochondrial oxidative injury

Han, S. J., Choi, H. S., Kim, J. I., Park, J., & Park, K. M. (2017) · Redox Biology · doi:10.1016/j.redox.2017.09.003 · Cited by 64

Sulfiredoxin Protein Is Critical for Redox Balance and Survival of Cells Exposed to Low Steady-state Levels of H2O2*

Baek, J. Y., Han, S. H., Sung, S. H., Lee, H. E., Kim, Y., Noh, Y. H., Bae, S. H., Rhee, S. G., & Chang, T. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.316711 · Cited by 64

Overoxidation of peroxiredoxins as an immediate and sensitive marker of oxidative stress in HepG2 cells and its application to the redox effects induced by ischemia/reperfusion in human liver

Cesaratto, L., Vascotto, C., DˈAmbrosio, C., Scaloni, A., Baccarani, U., Paron, I., Damante, G., Calligaris, S. D., Quadrifoglio, F., Tiribelli, C., et al. (2005) · Free Radical Research · doi:10.1080/10715760400029603 · Cited by 63

Nitrosative Stress Induces Peroxiredoxin 1 Ubiquitination During Ischemic Insult via E6AP Activation in Endothelial Cells Both In Vitro and In Vivo

Tao, R., Wang, H., Hong, L.-J., Huang, J.-Y., Lu, Y., Liao, M.-H., Ye, W., Lu, N., Zhu, D.-Y., Huang, Q., et al. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5381 · Cited by 61

Peroxiredoxin-2 expression is increased in β-thalassemic mouse red cells but is displaced from the membrane as a marker of oxidative stress

Mattè, A., Low, P. S., Turrini, F., Bertoldi, M., Campanella, M. E., Spano, D., Pantaleo, A., Siciliano, A., & Franceschi, L. D. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.05.003 · Cited by 60

Oxidative stress-induced antioxidant enzyme expression is an early phenomenon in ovarian carcinogenesis

Pylväs-Eerola, M., Puistola, U., Kauppila, S., Soini, Y., & Karihtala, P. (2010) · European Journal of Cancer · doi:10.1016/j.ejca.2010.02.006 · Cited by 61

Differential appearance of isoforms and cultivar variation in protein temporal profiles revealed in the maturing barley grain proteome

Finnie, C., Bak‐Jensen, K. S., Laugesen, S., Roepstorff, P., & Svensson, B. (2005) · Plant Science · doi:10.1016/j.plantsci.2005.11.012 · Cited by 60

Activity assay of mammalian 2-cys peroxiredoxins using yeast thioredoxin reductase system

Kim, J.-A., Park, S., Kim, K., Rhee, S. G., & Kang, S. W. (2004) · Analytical Biochemistry · doi:10.1016/j.ab.2004.12.008 · Cited by 62

Accumulation of overoxidized Peroxiredoxin III in aged rat liver mitochondria

Musicco, C., Capelli, V., Pesce, V., Timperio, A. M., Calvani, M., Mosconi, L., Zolla, L., Cantatore, P., & Gadaleta, M. N. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.03.002 · Cited by 60

Structural Basis for the Retroreduction of Inactivated Peroxiredoxins by Human Sulfiredoxin,

Jönsson, T. J., Murray, M. S., Johnson, L. C., Poole, L. B., & Lowther, W. T. (2005) · Biochemistry · doi:10.1021/bi050131i · Cited by 62

Two-dimensional gel electrophoresis in bacterial proteomics

Curreem, S. O. T., Watt, R. M., Lau, S. K. P., & Woo, P. C. Y. (2012) · Protein & Cell · doi:10.1007/s13238-012-2034-5 · Cited by 58

Mitochondrial H2O2 signaling is controlled by the concerted action of peroxiredoxin III and sulfiredoxin: Linking mitochondrial function to circadian rhythm

Rhee, S. G., & Kil, I. S. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.10.011 · Cited by 58

A mosquito 2-Cys peroxiredoxin protects against nitrosative and oxidative stresses associated with malaria parasite infection

Peterson, T. M. L., & Luckhart, S. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.10.059 · Cited by 58

Cloning and characterization of a 2-Cys peroxiredoxin from Pisum sativum

Bernier-Villamor, L. (2004) · Journal of Experimental Botany · doi:10.1093/jxb/erh238 · Cited by 57

Comparative proteomic analysis using samples obtained with laser microdissection and saturation dye labelling

Wilson, K. E., Marouga, R., Prime, J. E., Pashby, D. P., Orange, P. R., Crosier, S., Keith, A. B., Lathe, R., Mullins, J. J., Estibeiro, P., et al. (2005) · PROTEOMICS · doi:10.1002/pmic.200401255 · Cited by 55

Upregulation of Mitochondrial Gene Expression in PBMC from Convalescent SARS Patients

SHAO, H., Lan, D., Duan, Z., Liu, Z., MIN, J., Zhang, L., Huang, J., Su, J., Chen, S., & Xu, A. (2006) · Journal of Clinical Immunology · doi:10.1007/s10875-006-9046-y · Cited by 53

Induction of Sulfiredoxin via an Nrf2-Dependent Pathway and Hyperoxidation of Peroxiredoxin III in the Lungs of Mice Exposed to Hyperoxia

Bae, S. H., Woo, H. A., Sung, S. H., Lee, H. E., Lee, S. K., Kil, I. S., & Rhee, S. G. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2325 · Cited by 57

Redox Regulation of Lipopolysaccharide-mediated Sulfiredoxin Induction, Which Depends on Both AP-1 and Nrf2

Kim, H., Jung, Y., Shin, B. S., Kim, H., Song, H., Bae, S. H., Rhee, S. G., & Jeong, W. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.126839 · Cited by 56

An unexplored role for Peroxiredoxin in exercise-induced redox signalling?

Wadley, A. J., Aldred, S., & Coles, S. (2015) · Redox Biology · doi:10.1016/j.redox.2015.10.003 · Cited by 55

Thiol oxidation of cell signaling proteins: Controlling an apoptotic equilibrium

Cross, J. V., & Templeton, D. J. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20202 · Cited by 54

Oxidative stress-induced proteome alterations target different cellular pathways in human myoblasts

Baraibar, M. A., Hyzewicz, J., Rogowska-Wrzesińska, A., Ladouce, R., Roepstorff, P., Mouly, V., & Friguet, B. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.06.032 · Cited by 53

Phagocytosis of nano-sized titanium dioxide triggers changes in protein acetylation

Sund, J., Palomäki, J., Ahonen, N., Savolainen, K., Alenius, H. T., & Puustinen, A. (2014) · Journal of Proteomics · doi:10.1016/j.jprot.2014.06.011 · Cited by 53

Hyperoxidized peroxiredoxin 2 interacts with the protein disulfide- isomerase ERp46

Pace, P., Peskin, A. V., Han, M., Hampton, M. B., & Winterbourn, C. C. (2013) · Biochemical Journal · doi:10.1042/bj20130030 · Cited by 53

Hydrogen sulfide-producing cystathionine γ-lyase is critical in the progression of kidney fibrosis

Han, S. J., Noh, M. R., Jung, J.-M., Ishii, I., Yoo, J., Kim, J. I., & Park, K. M. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.08.017 · Cited by 53

The biological role of peroxiredoxins in innate immune responses of aquatic invertebrates

Abbas, M. N., Kausar, S., & Cui, H. (2019) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2019.03.062 · Cited by 53

Mitochondrial Bioenergetics at the Onset of Drug Resistance in Hematological Malignancies: An Overview

Barbato, A., Scandura, G., Puglisi, F., Cambria, D., Spina, E. L., Palumbo, G. A., Lazzarino, G., Tibullo, D., Raimondo, F. D., Giallongo, C., et al. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.604143 · Cited by 53

Proteomics-based identification of plasma biomarkers in oral squamous cell carcinoma

Tung, C., Lin, S., Chou, H., Chen, Y., Lin, H.-C., Tung, C.-L., Huang, K.-J., Chen, Y., Lee, Y., & Chan, H. (2012) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2012.11.017 · Cited by 52

Proteomic Analysis of Oxidative Stress-Responsive Proteins in Human Pneumocytes: Insight into the Regulation of DJ-1 Expression

Duan, X., Kelsen, S. G., & Merali, S. (2008) · Journal of Proteome Research · doi:10.1021/pr800295j · Cited by 52

Proteomic changes to the sarcoplasmic fraction of predominantly red or white muscle following acute heat stress

Cruzen, S. M., Pearce, S., Baumgard, L. H., Gabler, N. K., Huff-Lonergan, E. J., & Lonergan, S. M. (2015) · Journal of Proteomics · doi:10.1016/j.jprot.2015.07.032 · Cited by 51

Mapping protein cysteine sulfonic acid modifications with specific enrichment and mass spectrometry: An integrated approach to explore the cysteine oxidation

Chang, Y., Huang, C., Lin, C., Chang, H., & Wu, C. (2010) · PROTEOMICS · doi:10.1002/pmic.200900850 · Cited by 51

Peroxiredoxin 5 Expression in the Human Thyroid Gland

Gérard, A.-C., Many, M., Daumerie, C., Knoops, B., & Colin, I. M. (2005) · Thyroid · doi:10.1089/thy.2005.15.205 · Cited by 51

Cardiac peroxiredoxins undergo complex modifications during cardiac oxidant stress

Schröder, E., Brennan, J. P., & Eaton, P. (2008) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00017.2008 · Cited by 52

Peroxiredoxin III and Sulfiredoxin Together Protect Mice from Pyrazole-Induced Oxidative Liver Injury

Bae, S. H., Sung, S. H., Lee, H., Kang, H. T., Lee, S. K., Oh, S. Y., Woo, H. A., Kil, I. S., & Rhee, S. G. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4334 · Cited by 50

High Expression of Antioxidant Proteins in Dendritic Cells

Rivollier, A., Perrin‐Cocon, L., Luche, S., Diemer, H., Strub, J., Hanau, D., DORSSELAER, A. V., Lotteau, V., Rabourdin‐Combe, C., Rabilloud, T., et al. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m500262-mcp200 · Cited by 50

IDENTIFICATION OF OXIDATIVE STRESS-RELATED PROTEINS FOR PREDICTIVE SCREENING OF HEPATOTOXICITY USING A PROTEOMIC APPROACH

Yamamoto, T., Kikkawa, R., Yamada, H., & Horii, I. (2005) · The Journal of Toxicological Sciences · doi:10.2131/jts.30.213 · Cited by 50

Expression and modification proteomics during skeletal muscle ageing

Baraibar, M. A., Gueugneau, M., Duguez, S., Butler-Browne, G. S., Béchet, D., & Friguet, B. (2013) · Biogerontology · doi:10.1007/s10522-013-9426-7 · Cited by 49

Peroxiredoxin-1 from Schistosoma japonicum functions as a scavenger against hydrogen peroxide but not nitric oxide

Kumagai, T., Osada, Y., Ohta, N., & Kanazawa, T. (2008) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2008.11.002 · Cited by 49

Degradation of Redox-Sensitive Proteins including Peroxiredoxins and DJ-1 is Promoted by Oxidation-induced Conformational Changes and Ubiquitination

Song, I.-K., Lee, J., Cho, J., Jeong, J., Shin, D. H., & Lee, K. (2016) · Scientific Reports · doi:10.1038/srep34432 · Cited by 50

Loss of Lon1 in Arabidopsis Changes the Mitochondrial Proteome Leading to Altered Metabolite Profiles and Growth Retardation without an Accumulation of Oxidative Damage

Solheim, C., Li, L., Hatzopoulos, P., & Millar, A. H. (2012) · PLANT PHYSIOLOGY · doi:10.1104/pp.112.203711 · Cited by 48

Phorbol Ester-dependent Activation of Peroxiredoxin I Gene Expression via a Protein Kinase C, Ras, p38 Mitogen-activated Protein Kinase Signaling Pathway*

Hess, A., Wijayanti, N., Neuschäfer-Rube, A. P., Katz, N., Kietzmann, T., & Immenschuh, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307871200 · Cited by 49

Detecting oxidative post-translational modifications in proteins

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