Nanotransducers in cellular redox signaling: modification of thiols by reactive oxygen and nitrogen species
Abstract
The control of signal transduction involves post-translational modification of proteins at key amino acids. Cysteine residues are important in the control of 'redox' cell-signaling pathways, as thiol chemistry offers the possibility of modification by structurally diverse species, including those derived from oxidized lipids, peroxides or nitric oxide. An important and provocative study of the modification of thiols in the transcription factor OxyR recently extended this hypothesis. The findings offer the enticing possibility that the cell can distinguish between different degrees of oxidant and nitrosative exposure by modification at a single site on a signaling molecule.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Mitochondrial proteins are also subject to attack by ROS.
“Mitochondrial proteins are also subject to attack by ROS (88, 121, 157, 257, 318).”
From Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function (2009) · cites this paper as [88]
Cites
Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855 · see citing works
Schafer, F. Q., & Buettner, G. R. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00480-4 · Cited by 4,587 · see citing works
Lipton, S. A., Choi, Y.-B., Pan, Z.-H., Lei, S. Z., Chen, H.-S. V., Sucher, N. J., Loscalzo, J., Singel, D. J., & Stamler, J. S. (1993) · Nature · doi:10.1038/364626a0 · Cited by 2,433 · see citing works
Activation of the OxyR Transcription Factor by Reversible Disulfide Bond Formation
Zheng, M., Åslund, F., & Storz, G. (1998) · Science · doi:10.1126/science.279.5357.1718 · Cited by 1,197 · see citing works
Stone, J. R., & Marletta, M. A. (1994) · Biochemistry · doi:10.1021/bi00184a036 · Cited by 647 · see citing works
Structural Basis of the Redox Switch in the OxyR Transcription Factor
Choi, H., Kim, S.-J., Mukhopadhyay, P., Cho, S., Woo, J.-R., Storz, G., & Ryu, S.-E. (2001) · Cell · doi:10.1016/s0092-8674(01)00300-2 · Cited by 560 · see citing works
Nitric oxide and iron proteins
Cooper, C. E. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00021-3 · Cited by 510 · see citing works
Self-citationA Molecular Redox Switch on p21
Lander, H. M., Hajjar, D. P., Hempstead, B. L., Mirza, U. A., Chait, B. T., Campbell, S. L., & Quilliam, L. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.7.4323 · Cited by 488 · see citing works
Kim, S. O., Merchant, K., Nudelman, R., Beyer, W. F., Keng, T., DeAngelo, J. D., Hausladen, A., & Stamler, J. S. (2002) · Cell · doi:10.1016/s0092-8674(02)00723-7 · Cited by 481 · see citing works
Redox-operated genetic switches: the SoxR and OxyR transcription factors
Pomposiello, P. J., & Demple, B. (2001) · Trends in biotechnology · doi:10.1016/s0167-7799(00)01542-0 · Cited by 403 · see citing works
Control of pRB phosphorylation
Mittnacht, S. (1998) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(98)80057-9 · Cited by 385 · see citing works
Nitrosative Stress: Activation of the Transcription Factor OxyR
Hausladen, A., Privalle, C. T., Keng, T., DeAngelo, J., & Stamler, J. S. (1996) · Cell · doi:10.1016/s0092-8674(00)80147-6 · Cited by 359 · see citing works
Kullik, I., Tolédano, M. B., Tartaglia, L. A., & Storz, G. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.5.1275-1284.1995 · Cited by 245 · see citing works
Nitric oxide and cytochrome oxidase: substrate, inhibitor or effector?
Cooper, C. E. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)02035-7 · Cited by 223 · see citing works
Self-citationRegulation of protein phosphatase 2A by hydrogen peroxide and glutathionylation.
Rao, R., & Clayton, L. (2002) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/s0006-291x(02)00268-1 · Cited by 172 · see citing works
Redox signalling in the chloroplast: structure of oxidized pea fructose‐1,6‐bisphosphate phosphatase
Chiadmi, M., Navaza, A., Myroslawa Miginiac-maslow, B., Jacquot, J., & Cherfils, J. (1999) · The EMBO Journal · doi:10.1093/emboj/18.23.6809 · Cited by 146 · see citing works
Brookes, P., & Darley-Usmar, V. M. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00805-x · Cited by 137 · see citing works
Self-citationStorz, G., Tartaglia, L. A., & Ames, B. N. (1990) · Antonie van Leeuwenhoek · doi:10.1007/bf00548927 · Cited by 120 · see citing works
Mechanisms of Cell Signaling by Nitric Oxide and Peroxynitrite: From Mitochondria to MAP Kinases
Levonen, A., Patel, R. P., Brookes, P. S., Go, Y., Jo, H., Parthasarathy, S., Anderson, P. G., & Darley-Usmar, V. M. (2001) · Antioxidants and Redox Signaling · doi:10.1089/152308601300185188 · Cited by 112 · see citing works
Self-citationRepression of photosynthesis gene expression by formation of a disulfide bond in CrtJ
Masuda, S., Dong, C., Swem, D. L., Setterdahl, A. T., Knaff, D. B., & Bauer, C. E. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.102013099 · Cited by 82 · see citing works
Demple, B. (1998) · Science · doi:10.1126/science.279.5357.1655 · Cited by 66 · see citing works
Design of Metabolic Control for Large Flux Changes
Thomas, S., & Fell, D. A. (1996) · Journal of Theoretical Biology · doi:10.1006/jtbi.1996.0166 · Cited by 44 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
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
Bacterial mercury resistance from atoms to ecosystems
Barkay, T., Miller, S. M., & Summers, A. O. (2003) · FEMS Microbiology Reviews · doi:10.1016/s0168-6445(03)00046-9 · Cited by 1,054 · see citing works
Nitric oxide signalling in plants
Neill, S. J., Desikan, R., & Hancock, J. T. (2003) · New Phytologist · doi:10.1046/j.1469-8137.2003.00804.x · Cited by 872 · see citing works
Protein Sulfenic Acids in Redox Signaling
Poole, L. B., Karplus, P. A., & Claiborne, A. (2004) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.44.101802.121735 · Cited by 598 · see citing works
Nitric oxide, cell bioenergetics and neurodegeneration
Moncada, S., & Bolaños, J. P. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03988.x · Cited by 556 · see citing works
ABA, hydrogen peroxide and nitric oxide signalling in stomatal guard cells
Desikan, R. (2003) · Journal of Experimental Botany · doi:10.1093/jxb/erh033 · Cited by 518 · see citing works
The thioredoxin system—From science to clinic
Gromer, S., Urig, S., & Becker, K. (2003) · Medicinal Research Reviews · doi:10.1002/med.10051 · Cited by 482 · see citing works
Stowe, D. F., & Camara, A. K. S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2331 · Cited by 471 · see citing works
Ball, L., Accotto, G. P., Bechtold, U., Creissen, G. P., Funck, D., Jiménez, A., Kular, B., Leyland, N., Mejía-Carranza, J., Reynolds, H. V., et al. (2004) · The Plant Cell · doi:10.1105/tpc.104.022608 · Cited by 437 · see citing works
Redox-Dependent Transcriptional Regulation
Liu, H., Colavitti, R., Rovira, I. I., & Finkel, T. (2005) · Circulation Research · doi:10.1161/01.res.0000188210.72062.10 · Cited by 427 · see citing works
Cortese-Krott, M. M., Koning, A. M., Kuhnle, G., Nagy, P., Bianco, C. L., Pasch, A., Wink, D. A., Fukuto, J. M., Jackson, A. A., van Goor, H., et al. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7083 · Cited by 363 · see citing works
Perraud, A.-L., Takanishi, C. L., Shen, B. W., Kang, S. J., Smith, M., Schmitz, C., Knowles, H. M., Ferraris, D. V., Li, W., Zhang, J., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411446200 · Cited by 358 · see citing works
Glutathione, photosynthesis and the redox regulation of stress-responsive gene expression
Mullineaux, P. M., & Rausch, T. (2005) · Photosynthesis Research · doi:10.1007/s11120-005-8811-8 · Cited by 344 · see citing works
Dranka, B. P., Hill, B. G., & Darley-Usmar, V. M. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.01.015 · Cited by 329 · see citing works
Self-citationGuard‐cell signalling for hydrogen peroxide and abscisic acid
Wang, P., & Song, C. (2008) · New Phytologist · doi:10.1111/j.1469-8137.2008.02431.x · Cited by 325 · see citing works
Free Radicals, Mitochondria, and Oxidized Lipids
Gutiérrez, J., Ballinger, S. W., Darley-Usmar, V. M., & Landar, A. L. (2006) · Circulation Research · doi:10.1161/01.res.0000248212.86638.e9 · Cited by 319 · see citing works
Self-citationCell signalling by reactive lipid species: new concepts and molecular mechanisms
Higdon, A. N., Diers, A. R., Oh, J. Y., Landar, A. L., & Darley-Usmar, V. M. (2012) · Biochemical Journal · doi:10.1042/bj20111752 · Cited by 320 · see citing works
Self-citationWhat Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology
Hill, B. G., Dranka, B. P., Bailey, S. M., Lancaster, J. R., & Darley-Usmar, V. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.101618 · Cited by 310 · see citing works
Self-citationRegulation of sperm function by reactive oxygen species
Ford, W. C. L. (2004) · Human Reproduction Update · doi:10.1093/humupd/dmh034 · Cited by 305 · see citing works
Thiol-Based Regulatory Switches
Paget, M. S. B., & Buttner, M. J. (2003) · Annual Review of Genetics · doi:10.1146/annurev.genet.37.110801.142538 · Cited by 294 · see citing works
Sulfur Assimilation and the Role of Sulfur in Plant Metabolism: A Survey
Droux, M. (2004) · Photosynthesis Research · doi:10.1023/b:pres.0000017196.95499.11 · Cited by 262 · see citing works
Glutathione homeostasis and redox-regulation by sulfhydryl groups
Meyer, A. J., & Hell, R. (2005) · Photosynthesis Research · doi:10.1007/s11120-005-8425-1 · Cited by 261 · see citing works
Levonen, A., Hill, B. G., Kansanen, E., Zhang, J., & Darley-Usmar, V. M. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.025 · Cited by 232 · see citing works
Self-citationReactive Oxygen Species and Boar Sperm Function1
Awda, B. J., Mackenzie-Bell, M., & Buhr, M. M. (2009) · Biology of Reproduction · doi:10.1095/biolreprod.109.076471 · Cited by 228 · see citing works
Vascular Oxidant Stress and Inflammation in Hyperhomocysteinemia
Papatheodorou, L., & Weiss, N. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1750 · Cited by 223 · see citing works
Regulators of bacterial responses to nitric oxide
Spiro, S. (2007) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2006.00061.x · Cited by 208 · see citing works
Hancock, J. T., Henson, D., Nyirenda, M., Desikan, R., Harrison, J., Lewis, M., Hughes, J., & Neill, S. J. (2005) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2005.07.012 · Cited by 206 · see citing works
A Role for ETR1 in Hydrogen Peroxide Signaling in Stomatal Guard Cells
Desikan, R., Hancock, J. T., Bright, J., Harrison, J., Weir, I. S., Hooley, R., & Neill, S. J. (2005) · PLANT PHYSIOLOGY · doi:10.1104/pp.104.056994 · Cited by 204 · see citing works
Cheng, M., Ko, K., Chang, W., Kuo, W., Chen, G., & Lin, T. (2015) · The Plant Journal · doi:10.1111/tpj.12940 · Cited by 200 · see citing works
Hidalgo, C., Sánchez, G., Barrientos, G. C., & Aracena-Parks, P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600451200 · Cited by 196 · see citing works
The Redox Activity of Hemoglobins: From Physiologic Functions to Pathologic Mechanisms
Reeder, B. J. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2974 · Cited by 189 · see citing works
Myeloperoxidase: An Oxidative Pathway for Generating Dysfunctional High-Density Lipoprotein
Shao, B., Oda, M. N., Oram, J. F., & Heinecke, J. W. (2009) · Chemical Research in Toxicology · doi:10.1021/tx9003775 · Cited by 185 · see citing works
Shao, B., Pennathur, S., & Heinecke, J. W. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.337345 · Cited by 170 · see citing works
The Evolving Understanding of the Contribution of Lipid Metabolism to Diabetic Kidney Disease
Stadler, K., Goldberg, I. J., & Susztak, K. (2015) · Current Diabetes Reports · doi:10.1007/s11892-015-0611-8 · Cited by 165 · see citing works
Synthesis of the sulfur amino acids: cysteine and methionine
Wirtz, M., & Droux, M. (2005) · Photosynthesis Research · doi:10.1007/s11120-005-8810-9 · Cited by 165 · see citing works
Doing the unexpected: proteins involved in hydrogen peroxide perception
Hancock, J. T. (2006) · Journal of Experimental Botany · doi:10.1093/jxb/erj180 · Cited by 162 · see citing works
Microbial H2O2 sensors as archetypical redox signaling modules
Tolédano, M. B., Delaunay, A., Monceau, L., & Tacnet, F. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.05.005 · Cited by 152 · see citing works
Recent Insights into the Mitochondrial Role in Autophagy and Its Regulation by Oxidative Stress
Agujetas, V. R., de Dios, C., Pinilla, L. L., Marı́, M., Morales, A., & Colell, A. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/3809308 · Cited by 149 · see citing works
ROS perception in Arabidopsis thaliana: the ozone‐induced calcium response
Evans, N. H., McAinsh, M. R., Hetherington, A. M., & Knight, M. R. (2005) · The Plant Journal · doi:10.1111/j.1365-313x.2004.02325.x · Cited by 143 · see citing works
Oxidative stress-induced apoptosis and autophagy: Balancing the contrary forces in spermatogenesis
Sharma, P., Kaushal, N., Saleth, L. R., Ghavami, S., Dhingra, S., & Kaur, P. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2023.166742 · Cited by 142 · see citing works
Cytoprotection against Oxidative Stress and the Regulation of Glutathione Synthesis
Dickinson, D. A., Moellering, D. R., Iles, K. E., Patel, R. P., Levonen, A., Wigley, A. F., Darley-Usmar, V. M., & Forman, H. J. (2003) · Biological Chemistry · doi:10.1515/bc.2003.061 · Cited by 141 · see citing works
Self-citationThe Histidine Kinase AHK5 Integrates Endogenous and Environmental Signals in Arabidopsis Guard Cells
Desikan, R., Horák, J., Chaban, C., Mira‐Rodado, V., Witthöft, J., Elgass, K., Grefen, C., Cheung, M., Meixner, A. J., Hooley, R., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002491 · Cited by 140 · see citing works
The Disulfide Proteome and Other Reactive Cysteine Proteomes: Analysis and Functional Significance
Lindahl, M., Mata-Cabana, A., & Kieselbach, T. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3551 · Cited by 141 · see citing works
Eccleston, H. B., Andringa, K. K., Betancourt, A. M., King, A. L., Mantena, S. K., Swain, T. M., Tinsley, H. N., Nolte, R. N., Nagy, T. R., Abrams, G. A., et al. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3395 · Cited by 133 · see citing works
Cell signalling by oxidized lipids and the role of reactive oxygen species in the endothelium
Zmijewski, J. W., Landar, A., Watanabe, N., Dickinson, D. A., Noguchi, N., & Darley-Usmar, V. M. (2005) · Biochemical Society Transactions · doi:10.1042/bst20051385 · Cited by 112 · see citing works
Self-citationCrawford, J. H., Chacko, B. K., Pruitt, H. M., Piknova, B., Hogg, N., & Patel, R. P. (2004) · Blood · doi:10.1182/blood-2004-03-0880 · Cited by 111 · see citing works
Self-citationFormation, Reactivity, and Detection of Protein Sulfenic Acids
Kettenhofen, N. J., & Wood, M. J. A. (2010) · Chemical Research in Toxicology · doi:10.1021/tx100237w · Cited by 110 · see citing works
Sulfur in Plants An Ecological Perspective
Hawkesford, M. J., & Kok, L. J. D. (2007) · Plant ecophysiology · doi:10.1007/978-1-4020-5887-5 · Cited by 108 · see citing works
Buettner, G. R., Wagner, B. A., & Rodgers, V. G. J. (2011) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-011-9320-3 · Cited by 101 · see citing works
Wohlgemuth, S. E., Calvani, R., & Marzetti, E. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.03.007 · Cited by 97 · see citing works
Olsson, M. G., Allhorn, M., Bülow, L., Hansson, S. R., Ley, D., Olsson, M. L., Schmidtchen, A., & Åkerström, B. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4282 · Cited by 96 · see citing works
Rose, S., Melnyk, S., Trusty, T. A., Pavliv, O., Seidel, L., Li, J., Nick, T. G., & James, S. J. (2011) · Autism Research and Treatment · doi:10.1155/2012/986519 · Cited by 93 · see citing works
Linking protein oxidation to environmental pollutants: Redox proteomic approaches
Braconi, D., Bernardini, G., & Santucci, A. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.06.029 · Cited by 92 · see citing works
Redox Control of Neural Function: Background, Mechanisms, and Significance
Maher, P. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1941 · Cited by 99 · see citing works
Zinc Center as Redox Switch—New Function for an Old Motif
Ilbert, M., Graf, P. C. F., & Jakob, U. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.835 · Cited by 88 · see citing works
GTPases and reactive oxygen species: switches for killing and signaling
Werner, E. (2003) · Journal of Cell Science · doi:10.1242/jcs.00937 · Cited by 92 · see citing works
Dissecting the role of redox signaling in neuronal development
Bórquez, D. A., Urrutia, P. J., Wilson, C., van Zundert, B., Núñez, M. T., & González-Billault, C. E. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13581 · Cited by 86 · see citing works
Shao, B. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2011.11.011 · Cited by 83 · see citing works
Redox Regulation in Amyotrophic Lateral Sclerosis
Parakh, S., Spencer, D. M. S., Halloran, M. A., Soo, K. Y., & Atkin, J. D. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/408681 · Cited by 80 · see citing works
Signaling and Communication in Plants
Mugnai, S. (2011) · Frontiers in artificial intelligence and applications · doi:10.3233/978-1-60750-972-1-205 · Cited by 80 · see citing works
Mechanisms of the interaction of nitroxyl with mitochondria
SHIVA, S., CRAWFORD, J. H., RAMACHANDRAN, A., CEASER, E. K., HILLSON, T., BROOKES, P. S., PATEL, R. P., & DARLEY-USMAR, V. M. (2004) · Biochemical Journal · doi:10.1042/bj20031758 · Cited by 78 · see citing works
Self-citationOxidative Stress in ESRD Patients on Dialysis and the Risk of Cardiovascular Diseases
Rysz, J., Franczyk, B., Ławiński, J., & Gluba-Brzózka, A. (2020) · Antioxidants · doi:10.3390/antiox9111079 · Cited by 75 · see citing works
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 · see citing works
Erdal, S., & Türk, H. (2016) · Environmental and Experimental Botany · doi:10.1016/j.envexpbot.2016.08.014 · Cited by 73 · see citing works
Redox Capacitor to Establish Bio‐Device Redox‐Connectivity
Kim, E., Liu, Y., Bentley, W. E., & Payne, G. F. (2012) · Advanced Functional Materials · doi:10.1002/adfm.201101946 · Cited by 68 · see citing works
Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin
Mata‐Cabana, A., Florencio, F. J., & Lindahl, M. (2007) · PROTEOMICS · doi:10.1002/pmic.200700410 · Cited by 65 · see citing works
The emerging role of cardiovascular risk factor-induced mitochondrial dysfunction in atherogenesis
Puddu, P., Puddu, G. M., Cravero, E., Pascalis, S. D., & Muscari, A. (2009) · Journal of Biomedical Science · doi:10.1186/1423-0127-16-112 · Cited by 65 · see citing works
Martirosyan, A., Leonard, S. S., Shi, X., Griffith, B. N., Gannett, P. M., & Strobl, J. S. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.105.096891 · Cited by 62 · see citing works
Thioredoxin-mediated redox regulation of resistance to endocrine therapy in breast cancer
Penney, R. B., & Roy, D. (2013) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2013.02.005 · Cited by 60 · see citing works
Cellular Oxidative Processes in Relation to Renal Disease
WARDLE, E. N. (2005) · American Journal of Nephrology · doi:10.1159/000083477 · Cited by 60 · see citing works
Bailey, S. M., Mantena, S. K., Millender-Swain, T., Çakır, Y., Jhala, N. C., Chhieng, D., Pinkerton, K. E., & Ballinger, S. W. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.01.003 · Cited by 58 · see citing works
Reactive Oxygen Species as Signalling Molecules
Desikan, R., Hancock, J. T., & Neill, S. J. (2005) · doi:10.1002/9780470988565.ch7 · Cited by 58 · see citing works
Neuroprotective Effect of Sulfhydryl Reduction in a Rat Optic Nerve Crush Model
Swanson, K. I., Schlieve, C. R., Lieven, C. J., & Levin, L. A. (2005) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.05-0155 · Cited by 54 · see citing works
Control of Primary Metabolism in Plants
(2006) · Blackwell Publishing Ltd eBooks · doi:10.1002/9780470988640 · Cited by 55 · see citing works
Affinity of S100A1 protein for calcium increases dramatically upon glutathionylation
Goch, G., Vdovenko, S., Kozłowska, H., & Bierzyński, A. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04680.x · Cited by 52 · see citing works
The electrophile responsive proteome: Integrating proteomics and lipidomics with cellular function
Higdon, A. N., Landar, A., Barnes, S., & Darley-Usmar, V. M. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4523 · Cited by 51 · see citing works
Self-citationAndringa, K. K., Bajt, M. L., Jaeschke, H., & Bailey, S. M. (2008) · Toxicology Letters · doi:10.1016/j.toxlet.2008.01.010 · Cited by 51 · see citing works
Lebreton, S., Graciet, E., & Gontero, B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213096200 · Cited by 51 · see citing works
Skin Redox Balance Maintenance: The Need for an Nrf2-Activator Delivery System
Ben-Yehuda Greenwald, M., Ben-Sasson, S., Bianco-Peled, H., & Kohen, R. (2016) · Cosmetics · doi:10.3390/cosmetics3010001 · Cited by 49 · see citing works
Sensing and Responding to UV-A in Cyanobacteria
Moon, Y., Kim, S. J., & Chung, Y. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms131216303 · Cited by 49 · see citing works
Almeida, Á., Cidad, P., Delgado‐Esteban, M., Fernández, E., Garcı́a-Nogales, P., & Bolaños, J. P. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20281 · Cited by 49 · see citing works
Lancaster, J. R. (2008) · Nitric Oxide · doi:10.1016/j.niox.2008.04.028 · Cited by 48 · see citing works
Corti, A., Paolicchi, A., Franzini, M., Dominici, S., Casini, A., & Alfonso Pompella, C. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.911 · Cited by 47 · see citing works
CorE from Myxococcus xanthus Is a Copper-Dependent RNA Polymerase Sigma Factor
Gómez‐Santos, N., Pérez, J., Sánchez‐Sutil, M. C., Moraleda‐Muñoz, A., & Muñoz‐Dorado, J. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002106 · Cited by 47 · see citing works
Liu, Y., Zheng, J., Ge, L., Tang, H., Hu, J., Li, X., Wang, X., Zhang, Y., & Shi, Q. (2024) · Scientia Horticulturae · doi:10.1016/j.scienta.2024.112911 · Cited by 45 · see citing works
King, A. L., Mantena, S. K., Andringa, K. K., Millender-Swain, T., Dunham‐Snary, K. J., Oliva, C. R., Griguer, C. E., & Bailey, S. M. (2016) · Redox Biology · doi:10.1016/j.redox.2016.08.005 · Cited by 45 · see citing works
Landar, A. L., Oh, J., Giles, N. M., Isom, A., KIRK, M. C., Barnes, S., & Darley-Usmar, V. M. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.08.046 · Cited by 45 · see citing works
Self-citationDesikan, R., Hancock, J. T., & Neill, S. J. (2003) · Topics in current genetics · doi:10.1007/978-3-540-39402-0_6 · Cited by 45 · see citing works
Non-reductive modulation of chloroplast fructose-1,6-bisphosphatase by 2-Cys peroxiredoxin
Caporaletti, D., D’Alessio, A. C., Rodriguez-Suarez, R. J., Senn, A. M., Duek, P. D., & Wolosiuk, R. A. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.02.013 · Cited by 43 · see citing works
Frenay, A.-R. S., de Borst, M. H., Bachtler, M., Tschopp, N., Velde‐Keyzer, C. A. T., van den Berg, E., Bakker, S. J. L., Feelisch, M., Pasch, A., & van Goor, H. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.08.024 · Cited by 42 · see citing works
Liu, D., Shan, Y., Valluru, L., & Bao, F. (2013) · BMC Neuroscience · doi:10.1186/1471-2202-14-23 · Cited by 42 · see citing works
Fedorova, M., Kuleva, N., & Hoffmann, R. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.09.011 · Cited by 41 · see citing works
Cumpstey, A. F., Clark, A. D., Santolini, J., Jackson, A. A., & Feelisch, M. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0017 · Cited by 40 · see citing works
Role of Reversible, Thioredoxin-Sensitive Oxidative Protein Modifications in Cardiac Myocytes
Kuster, G. M., Siwik, D. A., Pimentel, D. R., & Colucci, W. S. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.2153 · Cited by 40 · see citing works
The Structure of the Organic Hydroperoxide Resistance Protein from Deinococcus radiodurans
Meunier-Jamin, C., Kapp, U., Leonard, G. A., & McSweeney, S. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312983200 · Cited by 38 · see citing works
Role of Exogenous Glutathione in Alleviating Abiotic Stress in Maize (Zea mays L.)
Pei, L., Che, R., He, L., Gao, X., Li, W., & Li, H. (2018) · Journal of Plant Growth Regulation · doi:10.1007/s00344-018-9832-9 · Cited by 37 · see citing works
N-acetyl-l-cysteine fosters inactivation and transfer to endolysosomes of c-Src
Krasnowska, E. K., Pittaluga, E., Brunati, A. M., Brunelli, R., Costa, G., Spirito, M. D., Serafino, A., Ursini, F., & Parasassi, T. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.09.012 · Cited by 35 · see citing works
Systems redox biology in health and disease
Feelisch, M., Cortese-Krott, M. M., Santolini, J., Wootton, S. A., & Jackson, A. A. (2022) · EXCLI journal · doi:10.17179/excli2022-4793 · Cited by 33 · see citing works
The chemical biology of nitric oxide — an outsider's reflections about its role in osteoarthritis
Feelisch, M. (2008) · Osteoarthritis and Cartilage · doi:10.1016/s1063-4584(08)60007-2 · Cited by 31 · see citing works
ATP‐dependent modulation and autophosphorylation of rapeseed 2‐Cys peroxiredoxin
Arán, M., Caporaletti, D., Senn, A. M., Téllez-Iñón, M. T., Girotti, M. R., Llera, A. S., & Wolosiuk, R. A. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06299.x · Cited by 30 · see citing works
- Authors
- Cooper, C. E., Patel, R. P., Brookes, P. S., & Darley-Usmar, V. M.
- Affiliations
- University of Essex (GB)
- University of Alabama at Birmingham (US)
- Corresponding author
- Darley-Usmar, Victor M.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2002-10
- Volume
- 27
- Issue
- 10
- Pages
- 489-492
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W1999952146
- Cited by
- 180
- References
- 22
- Citations by year
- 2024: 3 · 2023: 2 · 2022: 4 · 2021: 1 · 2020: 4 · 2019: 5 · 2018: 3 · 2017: 5 · 2016: 8 · 2015: 5 · 2014: 9 · 2013: 6 · 2012: 11
- FWCI
- 5.06
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Biochemical Sciences (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- redox signaling, nanotransducers, thiol modification, cysteine residues, reactive oxygen species, reactive nitrogen species, nitrosative stress, OxyR, post-translational modification, protein oxidation, nitrosylation, oxidized lipids, peroxides, nitric oxide
- MeSH terms
- Animals, Cysteine, Escherichia coli, Oxidation-Reduction, Protein Processing, Post-Translational, Proteins, Sulfhydryl Compounds, Signal Transduction, Reactive Oxygen Species, Reactive Nitrogen Species
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review