A key role for mitochondria in endothelial signaling by plasma cysteine/cystine redox potential

Function and interactions of integrins

van der Flier, A., & Sonnenberg, A. (2001) · Cell and Tissue Research · doi:10.1007/s004410100417 · Cited by 1,043 · see citing works

Endothelial cell superoxide generation: regulation and relevance for cardiovascular pathophysiology

Li, J.-M., & Shah, A. M. (2004) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00124.2004 · Cited by 773 · see citing works

Molecular Mechanisms of Angiotensin II–Mediated Mitochondrial Dysfunction: Linking Mitochondrial Oxidative Damage and Vascular Endothelial Dysfunction

Doughan, A. K., Harrison, D. G., & Dikalov, S. I. (2008) · Circulation Research · doi:10.1161/circresaha.107.162800 · Cited by 710 · see citing works

Redox compartmentalization in eukaryotic cells.

Go, Y., & Jones, D. P. (2008) · Biochimica et Biophysica Acta · doi:10.1016/j.bbagen.2008.01.011 · Cited by 635 · see citing works

Glutathione in Human Plasma: Decline in Association with Aging, Age-Related Macular Degeneration, and Diabetes

Samiec, P. S., Drews‐Botsch, C., Flagg, E. W., Kurtz, J. C., Sternberg, P., Reed, R. L., & Jones, D. P. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00286-4 · Cited by 493 · see citing works

Mitochondrial reactive oxygen species-mediated signaling in endothelial cells

Zhang, D. X., & Gutterman, D. D. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01283.2006 · Cited by 432 · see citing works

Redox analysis of human plasma allows separation of pro-oxidant events of aging from decline in antioxidant defenses

Jones, D. P., Mody, V. C., Carlson, J. L., Lynn, M. J., & Sternberg, P. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01040-7 · Cited by 392 · see citing works

Mitochondrial Sources of H 2 O 2 Generation Play a Key Role in Flow-Mediated Dilation in Human Coronary Resistance Arteries

Liu, Y., Zhao, H., Li, H., Kalyanaraman, B., Nicolosi, A. C., & Gutterman, D. D. (2003) · Circulation Research · doi:10.1161/01.res.0000091261.19387.ae · Cited by 323 · see citing works

Redox Potential of Human Thioredoxin 1 and Identification of a Second Dithiol/Disulfide Motif

Watson, W. H., Pohl, J., Montfort, W. R., Stuchlik, O., Reed, M. S., Powis, G., & Jones, D. P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211107200 · Cited by 293 · see citing works

The relationship between mitochondrial shape and function and the cytoskeleton

Anesti, V., & Scorrano, L. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.04.013 · Cited by 286 · see citing works

Role of NAD(P)H Oxidase- and Mitochondria-Derived Reactive Oxygen Species in Cardioprotection of Ischemic Reperfusion Injury by Angiotensin II

Kimura, S., Zhang, G.-X., Nishiyama, A., Shokoji, T., Yao, L., Fan, Y.-Y., Rahman, M., Suzuki, T., Maeta, H., & Abe, Y. (2005) · Hypertension · doi:10.1161/01.hyp.0000163462.98381.7f · Cited by 264 · see citing works

Differential oxidation of thioredoxin-1, thioredoxin-2, and glutathione by metal ions*

Hansen, J. M., Zhang, H., & Jones, D. P. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.09.023 · Cited by 248 · see citing works

A Simple Method of Isolating Mouse Aortic Endothelial Cells

Kobayashi, M., Inoue, K., Warabi, E., Minami, T., & Kodama, T. (2005) · Journal of Atherosclerosis and Thrombosis · doi:10.5551/jat.12.138 · Cited by 238 · see citing works

The Relationship Between Plasma Levels of Oxidized and Reduced Thiols and Early Atherosclerosis in Healthy Adults

Ashfaq, S., Abramson, J. L., Jones, D. P., Rhodes, S. D., Weintraub, W. S., Hooper, W. C., Vaccarino, V., Harrison, D. G., & Quyyumi, A. A. (2006) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2005.09.063 · Cited by 227 · see citing works

Manganese superoxide dismutase and aldehyde dehydrogenase deficiency increase mitochondrial oxidative stress and aggravate age-dependent vascular dysfunction

Wenzel, P., Schuhmacher, S., Kienhöfer, J., Müller, J., Hortmann, M., Oelze, M., Schulz, E., Treiber, N., Kawamoto, T., Scharffetter-Kochanek, K., et al. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn182 · Cited by 207 · see citing works

Estrogen-Induced Mitochondrial Reactive Oxygen Species as Signal-Transducing Messengers

Felty, Q. H., Xiong, W., Sun, D., Sarkar, S., Singh, K. P., Parkash, J., & Roy, D. (2005) · Biochemistry · doi:10.1021/bi047629p · Cited by 199 · see citing works

Oxidation of glutathione and cysteine in human plasma associated with smoking

Moriarty, S. E., Shah, J. H., Lynn, M., Jiang, S., Openo, K., Jones, D. P., & Sternberg, P. (2003) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2003.09.006 · Cited by 193 · see citing works

Isotope-Coded Affinity Tag (ICAT) Approach to Redox Proteomics: Identification and Quantitation of Oxidant-Sensitive Cysteine Thiols in Complex Protein Mixtures

Sethuraman, M., McComb, M. E., Huang, H., Huang, S., Heibeck, T. H., Costello, C. E., & Cohen, R. A. (2004) · Journal of Proteome Research · doi:10.1021/pr049887e · Cited by 177 · see citing works

Redox Changes of Cultured Endothelial Cells and Actin Dynamics

Moldovan, L., Moldovan, N. I., Sohn, R. H., Parikh, S. A., & Goldschmidt‐Clermont, P. J. (2000) · Circulation Research · doi:10.1161/01.res.86.5.549 · Cited by 176 · see citing works

Electrostatic influence of local cysteine environments on disulfide exchange kinetics

Snyder, G. H., Cennerazzo, M. J., Karalis, A. J., & Locey, D. (1981) · Biochemistry · doi:10.1021/bi00526a001 · Cited by 169 · see citing works

Overexpressed Human Mitochondrial Thioredoxin Confers Resistance to Oxidant-induced Apoptosis in Human Osteosarcoma Cells*

Chen, Y., Cai, J.-Y., Murphy, T., & Jones, D. P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202026200 · Cited by 166 · see citing works

Association of Mitochondria with Plectin and Desmin Intermediate Filaments in Striated Muscle

Reipert, S. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4626 · Cited by 157 · see citing works

Compartmental oxidation of thiol–disulphide redox couples during epidermal growth factor signalling

Halvey, P. J., Watson, W. H., Hansen, J. M., Go, Y., Afshin Samali, A., & Jones, D. P. (2005) · Biochemical Journal · doi:10.1042/bj20041829 · Cited by 156 · see citing works

Intracellular Proatherogenic Events and Cell Adhesion Modulated by Extracellular Thiol/Disulfide Redox State

Go, Y., & Jones, D. P. (2005) · Circulation · doi:10.1161/circulationaha.104.515155 · Cited by 153 · see citing works

Endothelial‐specific expression of mitochondrial thioredoxin improves endothelial cell function and reduces atherosclerotic lesions

Zhang, H., Luo, Y., Zhang, W., He, Y., Dai, S., Zhang, R., Huang, Y., Bernatchez, P., Giordano, F. J., Shadel, G., et al. (2007) · American Journal of Pathology · doi:10.2353/ajpath.2007.060960 · Cited by 145 · see citing works

Extracellular thiol/disulfide redox state affects proliferation rate in a human colon carcinoma (Caco2) cell line

Jonas, C. R., Ziegler, T. R., Gu, L. I. H., & Jones, D. P. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01081-x · Cited by 134 · see citing works

Glutathione availability modulates alveolar macrophage function in the chronic ethanol-fed rat

Brown, L. A. S., Ping, X., Harris, F. L., & Gauthier, T. W. (2006) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00346.2006 · Cited by 106 · see citing works

Oxidant-Induced Apoptosis in Human Retinal Pigment Epithelial Cells: Dependence on Extracellular Redox State

Jiang, S., Moriarty-Craige, S. E., Orr, M. L., Cai, J., Sternberg, P., & Jones, D. P. (2005) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.04-0949 · Cited by 106 · see citing works

Mitochondrial thioredoxin in regulation of oxidant‐induced cell death

Chen, Y., Cai, J., & Jones, D. P. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.11.007 · Cited by 92 · see citing works

Mitochondrial Dysfunction as an Initiating Event in Atherogenesis: A Plausible Hypothesis

Puddu, P., Puddu, G. M., Galletti, L., Cravero, E., & Muscari, A. (2005) · Cardiology · doi:10.1159/000083440 · Cited by 87 · see citing works

Endothelial Function and Aminothiol Biomarkers of Oxidative Stress in Healthy Adults

Ashfaq, S., Abramson, J. L., Jones, D. P., Rhodes, S. D., Weintraub, W. S., Hooper, W. C., Vaccarino, V., Alexander, R. W., Harrison, D. G., & Quyyumi, A. A. (2008) · Hypertension · doi:10.1161/hypertensionaha.107.097386 · Cited by 84 · see citing works

Oxidation of Plasma Cysteine/Cystine Redox State in Endotoxin-Induced Lung Injury

Iyer, S. S., Jones, D. P., Brigham, K. L., & Rojas, M. (2008) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2007-0447oc · Cited by 57 · see citing works

Plasma cystine concentration and redox state in aging and physical exercise

Hildebrandt, W., Kinscherf, R., Hauer, K. A., Holm, E., & Dröge, W. (2002) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(02)00013-1 · Cited by 57 · see citing works

Identification of thioredoxin-2 as a regulator of the mitochondrial permeability transition.

He, M., Cai, J.-Y., Go, Y., Johnson, J. M., Martin, W. D., Hansen, J. M., & Jones, D. P. (2008) · Toxicological Sciences · doi:10.1093/toxsci/kfn116 · Cited by 48 · see citing works

Quantification of Redox Conditions in the Nucleus

Go, Y., Pohl, J., & Jones, D. P. (2008) · Methods in molecular biology · doi:10.1007/978-1-60327-461-6_17 · Cited by 45 · see citing works

“Lumen digestion” technique for isolation of aortic endothelial cells from heme oxygenase-1 knockout mice

Chen, S., Segal, M. S., & Agarwal, A. (2004) · BioTechniques · doi:10.2144/04371st05 · Cited by 29 · see citing works

Cell Biology of Ischemia/Reperfusion Injury

Kalogeris, T. J., Baines, C. P., Krenz, M., & Korthuis, R. J. (2012) · International review of cytology · doi:10.1016/b978-0-12-394309-5.00006-7 · Cited by 2,207 · see citing works

Neutrophil extracellular traps enriched in oxidized mitochondrial DNA are interferogenic and contribute to lupus-like disease

Lood, C., Blanco, L. P., Purmalek, M. M., Carmona-Rivera, C., De Ravin, S. S., Smith, C. K., Malech, H. L., Ledbetter, J. A., Elkon, K. B., & Kaplan, M. J. (2016) · Nature Medicine · doi:10.1038/nm.4027 · Cited by 1,570 · see citing works

Reactive oxygen species in health and disease

Alfadda, A. A., & Sallam, R. M. (2012) · Journal of Biomedicine and Biotechnology · doi:10.1155/2012/936486 · Cited by 824 · see citing works

Ischemia/Reperfusion

Kalogeris, T. J., Baines, C. P., Krenz, M., & Korthuis, R. J. (2016) · Comprehensive physiology · doi:10.1002/cphy.c160006 · Cited by 841 · see citing works

Redox regulation of mitochondrial function

Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588 · see citing works

Cysteine/cystine redox signaling in cardiovascular disease

Go, Y.-M., & Jones, D. P. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.11.029 · Cited by 447 · see citing works

The cysteine proteome

Go, Y., Chandler, J. D., & Jones, D. P. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.03.022 · Cited by 343 · see citing works

Banting Lecture 2011

Corkey, B. E. (2011) · Diabetes · doi:10.2337/db11-1483 · Cited by 285 · see citing works

The redox proteome

Go, Y.-M., & Jones, D. P. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.464131 · Cited by 260 · see citing works

Redox compartmentalization and cellular stress

Jones, D. P., & Go, Y.-M. (2010) · Diabetes Obesity and Metabolism · doi:10.1111/j.1463-1326.2010.01266.x · Cited by 246 · see citing works

Thiol/disulfide redox states in signaling and sensing

Go, Y.-M., & Jones, D. P. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.764840 · Cited by 241 · see citing works

The fairytale of the GSSG/GSH redox potential

Flohé, L. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.10.020 · Cited by 239 · see citing works

Reactive oxygen species and redox compartmentalization

Kaludercic, N., Deshwal, S., & Lisa, F. D. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00285 · Cited by 213 · see citing works

Antioxidant Therapeutic Strategies for Cardiovascular Conditions Associated with Oxidative Stress

Farías, J. G., Molina, V. M., Carrasco, R. A., Zepeda, A. B., Figueroa, E., Letelier, P. J., & Castillo, R. L. (2017) · Nutrients · doi:10.3390/nu9090966 · Cited by 195 · see citing works

Impaired Redox Signaling and Antioxidant Gene Expression in Endothelial Cells in Diabetes: A Role for Mitochondria and the Nuclear Factor-E2-Related Factor 2-Kelch-Like ECH-Associated Protein 1 Defense Pathway

Cheng, X., Siow, R. C. M., & Mann, G. E. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3283 · Cited by 178 · see citing works

Redox theory of aging: implications for health and disease

Go, Y., & Jones, D. P. (2017) · Clinical Science · doi:10.1042/cs20160897 · Cited by 173 · see citing works

Extracellular SOD-Derived H2O2 Promotes VEGF Signaling in Caveolae/Lipid Rafts and Post-Ischemic Angiogenesis in Mice

Oshikawa, J., Urao, N., Kim, H. W., Kaplan, N., Razvi, M., McKinney, R. D., Poole, L. B., Fukai, T., & Ushio‐Fukai, M. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010189 · Cited by 160 · see citing works

Redox sensing: orthogonal control in cell cycle and apoptosis signalling

Jones, D. P. (2010) · Journal of Internal Medicine · doi:10.1111/j.1365-2796.2010.02268.x · Cited by 153 · see citing works

Activity-Based Sensing for Site-Specific Proteomic Analysis of Cysteine Oxidation

Shi, Y., & Carroll, K. S. (2019) · Accounts of Chemical Research · doi:10.1021/acs.accounts.9b00562 · Cited by 145 · see citing works

Oxidative stress in asthma: Part of the puzzle

Şahiner, Ü. M., Birben, E., ERZURUM, S. C., Saçkesen, C., & Kalaycı, Ö. (2018) · Pediatric Allergy and Immunology · doi:10.1111/pai.12965 · Cited by 145 · see citing works

Endoplasmic Reticulum Stress and the Unfolded Protein Response in Cerebral Ischemia/Reperfusion Injury

Wang, L., Liu, Y., Zhang, X., Ye, Y., Xiong, X., Zhang, S., Gu, L., Jian, Z., & Wang, H. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.864426 · Cited by 121 · see citing works

Dietary isoflavones and vascular protection: Activation of cellular antioxidant defenses by SERMs or hormesis?

Siow, R. C. M., & Mann, G. E. (2010) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2010.09.003 · Cited by 119 · see citing works

Ischemia/Reperfusion

Kalogeris, T. J., Baines, C. P., Krenz, M., & Korthuis, R. J. (2017) · Comprehensive physiology · doi:10.1002/j.2040-4603.2017.tb00741.x · Cited by 115 · see citing works

Manganese superoxide dismutase (SOD2): is there a center in the universe of mitochondrial redox signaling?

Zou, X., Ratti, B. A., O’Brien, J., Lautenschlager, S. O., Gius, D. R., Bonini, M. G., & Zhu, Y. (2017) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-017-9718-8 · Cited by 112 · see citing works

Reactive species and mitochondrial dysfunction: Mechanistic significance of 4‐hydroxynonenal

Roede, J. R., & Jones, D. P. (2010) · Environmental and Molecular Mutagenesis · doi:10.1002/em.20553 · Cited by 111 · see citing works

Integrated Redox Proteomics and Metabolomics of Mitochondria to Identify Mechanisms of Cd Toxicity

Go, Y., Roede, J. R., Orr, M. C., Liang, Y., & Jones, D. P. (2014) · Toxicological Sciences · doi:10.1093/toxsci/kfu018 · Cited by 98 · see citing works

Intracellular and Extracellular Redox Status and Free Radical Generation in Primary Immune Cells from Children with Autism

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

Selective Targeting of the Cysteine Proteome by Thioredoxin and Glutathione Redox Systems

Go, Y., Roede, J. R., Walker, D. I., Duong, D. M., Seyfried, N. T., Orr, M. L., Liang, Y., Pennell, K. D., & Jones, D. P. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.030437 · Cited by 93 · see citing works

Mapping the cysteine proteome: analysis of redox-sensing thiols

Jones, D. P., & Go, Y. (2011) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2010.12.014 · Cited by 89 · see citing works

Redox signaling and histone acetylation in acute pancreatitis

Escobar, J., Pereda, J., López‐Rodas, G., & Sastre, J. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.11.009 · Cited by 84 · see citing works

Redox regulation of protein damage in plasma

Griffiths, H. R., Dias, I. H. K., Willetts, R. S., & Devitt, A. (2014) · Redox Biology · doi:10.1016/j.redox.2014.01.010 · Cited by 84 · see citing works

Oxidative toxicology of bleomycin: Role of the extracellular redox environment

Allawzi, A. M., Elajaili, H. B., Redente, E. F., & Nozik‐Grayck, E. (2018) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2018.08.001 · Cited by 83 · see citing works

Mechanisms of Pathogenesis in Drug Hepatotoxicity Putting the Stress on Mitochondria

Jones, D. P., Lemasters, J. J., Han, D., Boelsterli, U. A., & Kaplowitz, N. (2010) · Molecular Interventions · doi:10.1124/mi.10.2.7 · Cited by 81 · see citing works

Dietary sulfur amino acid effects on fasting plasma cysteine/cystine redox potential in humans

Jones, D. P., Park, Y. H., Gletsu-Miller, N. A., Liang, Y., Yu, T., Accardi, C. J., & Ziegler, T. R. (2010) · Nutrition · doi:10.1016/j.nut.2010.01.014 · Cited by 81 · see citing works

The Synthesis of a 2D Ultra‐Large Protein Supramolecular Nanofilm by Chemoselective Thiol–Disulfide Exchange and its Emergent Functions

Xu, Y., Liu, Y., Hu, X., Qin, R., Su, H., Li, J., & Yang, P. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201912848 · Cited by 80 · see citing works

Controlling the Structure and Function of Protein Thin Films through Amyloid-like Aggregation

Liu, Y., Tao, F., Miao, S., & Yang, P. (2021) · Accounts of Chemical Research · doi:10.1021/acs.accounts.1c00231 · Cited by 80 · see citing works

Disulfide stress: a novel type of oxidative stress in acute pancreatitis

Moreno, M. L., Escobar, J., Izquierdo-Álvarez, A., Gil, A., Pérez, S., Pereda, J., Zapico, I., Vento, M., Sabater-Orti, L., Marina, A., et al. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.01.009 · Cited by 77 · see citing works

Low-dose cadmium disrupts mitochondrial citric acid cycle and lipid metabolism in mouse lung

Hu, X. Y., Chandler, J. D., Park, S., Liu, K., Fernandes, J., Orr, M. C., Smith, M. R., Ma, C., Kang, S., Uppal, K., et al. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.12.005 · Cited by 75 · see citing works

The Redox Communication Network as a Regulator of Metabolism

Corkey, B. E., & Deeney, J. T. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.567796 · Cited by 70 · see citing works

Clinical and nutritional benefits of cysteine-enriched protein supplements

McPherson, R. A., & Hardy, G. (2011) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e32834c1780 · Cited by 68 · see citing works

Quantitative proteomic characterization of redox-dependent post-translational modifications on protein cysteines

Duan, J., Gaffrey, M. J., & Qian, W. (2017) · Molecular BioSystems · doi:10.1039/c6mb00861e · Cited by 67 · see citing works

Redox balance in Cystic Fibrosis

Ziady, A. G., & Hansen, J. M. (2014) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.03.006 · Cited by 64 · see citing works

Histone Deacetylase Inhibitors Promote Mitochondrial Reactive Oxygen Species Production and Bacterial Clearance by Human Macrophages

Ariffin, J. K., Gupta, K. D., Kapétanovic, R., Iyer, A., Reid, R. C., Fairlie, D. P., & Sweet, M. J. (2015) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01876-15 · Cited by 63 · see citing works

From the Cover: Manganese Stimulates Mitochondrial H2O2Production in SH-SY5Y Human Neuroblastoma Cells Over Physiologic as well as Toxicologic Range

Fernandes, J., Li, H., Bijli, K. M., Chandler, J. D., Orr, M. L., Hu, X. Y., Jones, D. P., & Go, Y. (2016) · Toxicological Sciences · doi:10.1093/toxsci/kfw196 · Cited by 63 · see citing works

Metabolomics‐guided insights on bariatric surgery versus behavioral interventions for weight loss

Tulipani, S., Griffin, J., Palau‐Rodriguez, M., Cubillos, L. X. M., Bernal-López, M. R., Tinahones, F. J., Corkey, B. E., & Andrés‐Lacueva, C. (2016) · Obesity · doi:10.1002/oby.21686 · Cited by 61 · see citing works

Glutathione attenuates ethanol-induced alveolar macrophage oxidative stress and dysfunction by downregulating NADPH oxidases

Yeligar, S. M., Harris, F. L., Hart, C. M., & Brown, L. A. S. (2014) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00159.2013 · Cited by 60 · see citing works

The mitochondrial paradigm for cardiovascular disease susceptibility and cellular function: a complementary concept to Mendelian genetics

Krzywanski, D. M., Moellering, D. R., Fetterman, J. L., Dunham‐Snary, K. J., Sammy, M. J., & Ballinger, S. W. (2011) · Laboratory Investigation · doi:10.1038/labinvest.2011.95 · Cited by 60 · see citing works

Redox Systems Biology of Nutrition and Oxidative Stress

Dennis, K. K., Go, Y., & Jones, D. P. (2018) · Journal of Nutrition · doi:10.1093/jn/nxy306 · Cited by 60 · see citing works

Actin cytoskeleton redox proteome oxidation by cadmium

Go, Y., Orr, M. C., & Jones, D. P. (2013) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00203.2013 · Cited by 54 · see citing works

Protein Fold Classification with Backbone Torsional Characters Using Multi- Class Linear Discriminant Analysis

Go, Y. (2011) · Journal of Proteomics & Bioinformatics · doi:10.4172/jpb.1000190 · Cited by 52 · see citing works

Increased Nuclear Thioredoxin-1 Potentiates Cadmium-Induced Cytotoxicity

Go, Y., Orr, M. C., & Jones, D. P. (2012) · Toxicological Sciences · doi:10.1093/toxsci/kfs271 · Cited by 52 · see citing works

Engineered nanomaterials and oxidative stress: Current understanding and future challenges

Mendoza, R. P., & Brown, J. M. (2018) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2018.09.001 · Cited by 49 · see citing works

MPTP activates ASK1–p38 MAPK signaling pathway through TNF-dependent Trx1 oxidation in parkinsonism mouse model

Ray, A., Sehgal, N., Karunakaran, S., Rangarajan, G., & Ravindranath, V. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.041 · Cited by 50 · see citing works

The Extracellular Redox State Modulates Mitochondrial Function, Gluconeogenesis, and Glycogen Synthesis in Murine Hepatocytes

Nocito, L., Kleckner, A. S., Yoo, E. J., Jones, A. R., Liesa, M., & Corkey, B. E. (2015) · PLoS ONE · doi:10.1371/journal.pone.0122818 · Cited by 44 · see citing works

Dose-Related Alterations of Carbon Nanoparticles in Mammalian Cells Detected Using Biospectroscopy: Potential for Real-World Effects

Li, J., Strong, R. J., Trevisan, J., Fogarty, S. W., Fullwood, N. J., Jones, K. C., & Martin, F. L. (2013) · Environmental Science & Technology · doi:10.1021/es4017848 · Cited by 44 · see citing works

Biomarkers of oxidative stress study VI. Endogenous plasma antioxidants fail as useful biomarkers of endotoxin-induced oxidative stress

Kadiiska, M. B., Peddada, S. D., Herbert, R. A., Basu, S., Hensley, K., Jones, D. P., Hatch, G. E., & Mason, R. P. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.01.006 · Cited by 42 · see citing works

Oxidation of Plasma Cysteine/Cystine and GSH/GSSG Redox Potentials by Acetaminophen and Sulfur Amino Acid Insufficiency in Humans

Mannery, Y. O., Ziegler, T. R., Park, Y. H., & Jones, D. P. (2010) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.110.166421 · Cited by 40 · see citing works

Redox Reactivity of Cerium Oxide Nanoparticles Induces the Formation of Disulfide Bridges in Thiol-Containing Biomolecules

Rollin-Genetet, F., Seidel, C., Artells, E., Auffan, M., Thiéry, A., & Vidaud, C. (2015) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.5b00319 · Cited by 39 · see citing works

Metabolic master regulators: sharing information among multiple systems

Corkey, B. E., & Shirihai, O. S. (2012) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2012.07.006 · Cited by 38 · see citing works

Disturbed Flow Enhances Inflammatory Signaling and Atherogenesis by Increasing Thioredoxin-1 Level in Endothelial Cell Nuclei

Go, Y., Son, D. J., Park, H., Orr, M. L., Li, H., Takabe, W., Kumar, S., Kang, D. W., Kim, C. W., Jo, H., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0108346 · Cited by 38 · see citing works

Cardiac Ischemia/Reperfusion Injury: The Beneficial Effects of Exercise

Borges, J. P., & Verdoorn, K. D. S. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-4307-9_10 · Cited by 37 · see citing works

Increased Inflammatory Signaling and Lethality of Influenza H1N1 by Nuclear Thioredoxin-1

Go, Y., Kang, S.-M., Roede, J. R., Orr, M. L., & Jones, D. P. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018918 · Cited by 34 · see citing works

Minimizing Ischemia Reperfusion Injury in Xenotransplantation

Patel, P. M., Connolly, M. R., Coe, T. M., Calhoun, A., Pollok, F., Markmann, J. F., Burdorf, L., Azimzadeh, A. M., Madsen, J. C., & Pierson, R. N. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.681504 · Cited by 33 · see citing works

Maternal metabolic profile predicts high or low risk of an autism pregnancy outcome

Hollowood-Jones, K., Melnyk, S., Pavliv, O., Evans, T. T., Sides, A., Schmidt, R. J., Hertz‐Picciotto, I., Elms, W., Guerrero, E. E., Krüger, U., et al. (2018) · Research in Autism · doi:10.1016/j.rasd.2018.09.003 · Cited by 29 · see citing works

From Top-Down to Bottom-Up: Computational Modeling Approaches for Cellular Redoxin Networks

Pillay, C. S., Hofmeyr, J. S., Mashamaite, L. N., & Rohwer, J. M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4771 · Cited by 28 · see citing works

Characterization of plasma thiol redox potential in a common marmoset model of aging

Roede, J. R., Uppal, K., Liang, Y., Promislow, D., Wachtman, L. M., & Jones, D. P. (2013) · Redox Biology · doi:10.1016/j.redox.2013.06.003 · Cited by 26 · see citing works

ROS Compartmentalization in Plant Cells Under Abiotic Stress Condition

Gautam, V., Kaur, R., Kohli, S. K., Verma, V., Kaur, P., Singh, R. J., Saini, P., Arora, S., Thukral, A. K., Karpets, Y. V., et al. (2017) · Springer eBooks · doi:10.1007/978-981-10-5254-5_4 · Cited by 26 · see citing works

Redox Clamp Model for Study of Extracellular Thiols and Disulfides in Redox Signaling

Go, Y., & Jones, D. P. (2010) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(10)74010-6 · Cited by 22 · see citing works

Extracellular cysteine (Cys)/cystine (CySS) redox regulates metabotropic glutamate receptor 5 activity

Zhu, J. W., Yuan, J. F., Yang, H. M., Wang, S. T., Zhang, C. G., Sun, L., Yang, H. M., & Zhang, H. (2011) · Biochimie · doi:10.1016/j.biochi.2011.09.013 · Cited by 18 · see citing works

Comparative Expression Profiling of Distinct T Cell Subsets Undergoing Oxidative Stress

Lichtenfels, R., Mougiakakos, D., Johansson, C. C., Dressler, S. P., Recktenwald, C. V., Kiessling, R. W., & Seliger, B. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041345 · Cited by 18 · see citing works

Redox States of Protein Cysteines in Pathways of Protein Turnover and Cytoskeleton Dynamics Are Changed with Aging and Reversed by Slc7a11 Restoration in Mouse Lung Fibroblasts

Zheng, Y., Merchant, M. L., Burke, T. J., Ritzenthaler, J. D., Li, M., Gawęda, A. E., Benz, F. W., Roman, J., & Watson, W. H. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/2468986 · Cited by 16 · see citing works

Disulfidptosis: A novel cell death mechanism with pathological significance and therapeutic potential in diseases

Qian, S., Pan, L., Chen, G., Qiu, F., Ma, Y., Li, R., Mehta, J. L., & Wang, X. (2026) · Pharmacological Reviews · doi:10.1016/j.pharmr.2026.100127 · Cited by 16 · see citing works

Importance of Oxidative Stress and Antioxidant System in Health and Disease

Sabuncuoğlu, S., & Yalçınkaya, A. S. (2022) · Biochemistry · doi:10.5772/intechopen.100949 · Cited by 16 · see citing works

Differential Regulation of the Extracellular Cysteine/Cystine Redox State (EhCySS) by Lung Fibroblasts from Young and Old Mice

Watson, W. H., Burke, T. J., Zelko, I. N., Torres-González, E., Ritzenthaler, J. D., & Roman, J. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/1561305 · Cited by 17 · see citing works

Hypoxia inhibits expression and function of mitochondrial thioredoxin 2 to promote pulmonary hypertension

Adesina, S. E., Wade, B. E., Bijli, K. M., Kang, B., Williams, C. R., Ma, J., Go, Y., Hart, C. M., & Sutliff, R. L. (2017) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00258.2016 · Cited by 15 · see citing works

Proteome-wide identification of S-sulfenylated cysteines reveals metabolic response to freezing stress after cold acclimation in Brassica napus

Yu, L.-Q., Dai, Z., Zhang, Y.-T., Iqbal, S., Lu, S.-P., Guo, L., & Yao, X. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.1014295 · Cited by 13 · see citing works

Aryl Hydrocarbon Receptor and Cysteine Redox Dynamics Underlie (Mal)adaptive Mechanisms to Chronic Intermittent Hypoxia in Kidney Cortex

Correia, M. J., Pimpão, A. B., Lopes‐Coelho, F., Sequeira, C. O., Coelho, N. R., Dias, C. G., Barouki, R., Coumoul, X., Serpa, J., Morelló, J., et al. (2021) · Antioxidants · doi:10.3390/antiox10091484 · Cited by 14 · see citing works

The Synthesis of a 2D Ultra‐Large Protein Supramolecular Nanofilm by Chemoselective Thiol–Disulfide Exchange and its Emergent Functions

Xu, Y., Liu, Y., Hu, X., Qin, R., Su, H., Li, J., & Yang, P. (2019) · Angewandte Chemie · doi:10.1002/ange.201912848 · Cited by 13 · see citing works

Effect of dehydroepiandrosterone treatment on hormone levels and antioxidant parameters in aged rats.

Yin, F.-J., Kang, J., Han, N., & Ma, H.-T. (2015) · Genetics and Molecular Research · doi:10.4238/2015.september.22.24 · Cited by 10 · see citing works

Impact of sex, age and diet on the cysteine/cystine and glutathione/glutathione disulfide plasma redox couples in mice

Watson, W. H., Greenwell, J. C., Zheng, Y., Furmanek, S. P., Torres-González, E., Ritzenthaler, J. D., & Roman, J. (2020) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2020.108431 · Cited by 12 · see citing works

Simultaneous Determination of Endogenous Antioxidants and Malondialdehyde by RP-HPLC Coupled with Electrochemical Detector in Serum Samples

Hannan, P. A., Khan, J. A., Iqbal, Z., Ullah, I., Rehman, W. U., Rehman, M., Nasir, F., Khan, A., Ismail, I., Muhammad, S., et al. (2015) · Journal of Liquid Chromatography & Related Technologies · doi:10.1080/10826076.2015.1012522 · Cited by 11 · see citing works

Redox Equivalents and Mitochondrial Bioenergetics

Roede, J. R., Go, Y., & Jones, D. P. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-382-0_17 · Cited by 11 · see citing works

Quantitative proteomic analyses uncover regulatory roles of Nrf2 in human endothelial cells

Amin, K. N., Rajaguru, P., Suzuki, T., Sarkar, K., Ganesan, K., & Ramkumar, K. M. (2023) · Cell Stress and Chaperones · doi:10.1007/s12192-023-01366-5 · Cited by 7 · see citing works

Oxidative Stress: An Intersection Between Radiation and Sulfur Mustard Lung Injury

Day, B. J. (2024) · Disaster Medicine and Public Health Preparedness · doi:10.1017/dmp.2023.238 · Cited by 7 · see citing works

Transsulfuration metabolites and the association with incident atrial fibrillation – An observational cohort study among Norwegian patients with stable angina pectoris

Svenningsson, M. M., Svingen, G. F. T., Lysne, V., Ueland, P. M., Tell, G. S., Pedersen, E. R., Dhar, I., Nilsen, D. W. T., & Nygard, O. K. (2020) · International Journal of Cardiology · doi:10.1016/j.ijcard.2020.05.010 · Cited by 7 · see citing works

Redox Equivalents and Mitochondrial Bioenergetics

Roede, J. R., Go, Y., & Jones, D. P. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-7831-1_12 · Cited by 7 · see citing works

Hyperinsulinemia: cause or consequence

Yang, J. (2011) · Intern J Endocrinol Metab · doi:10.3760/cma.j.issn.1673-4157.2011.05.002 · Cited by 7 · see citing works

Living/controlled supramolecular protein polymerization

Ren, H., Zhang, Q., Wang, K., Xu, S., Liu, W., Tao, F., Han, Q., Miao, S., Zhang, Y., Liu, Y., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2510077122 · Cited by 6 · see citing works

Homocysteine and atrial fibrillation: novel evidences and insights

Ivanov, V., Smereka, Y., Rasputin, V., & Dmytriiev, K. D. (2022) · Monaldi Archives for Chest Disease · doi:10.4081/monaldi.2022.2241 · Cited by 6 · see citing works

Detection of the oxidation products of thiols: Disulfides, and sulfenic, sulfinic, and sulfonic acids

Shi, Y., & Carroll, K. S. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-90219-9.00010-8 · Cited by 5 · see citing works

Systemic remodeling of the redox regulatory network due to RNAi perturbations of glutaredoxin 1, thioredoxin 1, and glucose-6-phosphate dehydrogenase

Kippner, L. E., Finn, N. A., Shukla, S., & Kemp, M. L. (2011) · BMC Systems Biology · doi:10.1186/1752-0509-5-164 · Cited by 5 · see citing works

Extracellular superoxide dismutase (EC-SOD) R213G variant reduces mitochondrial ROS and preserves mitochondrial function in bleomycin-induced lung injury

Elajaili, H. B., Hernandez‐Lagunas, L., Harris, P. S., Sparagna, G. C., Jonscher, R. L., Ohlstrom, D. J., Sucharov, C. C., Bowler, R. P., Suliman, H. B., Fritz, K. S., et al. (2022) · Advances in Redox Research · doi:10.1016/j.arres.2022.100035 · Cited by 4 · see citing works

Importance of Oxidative Stress Mechanism in Reproductive Functions and Infertility

Onaolapo, M. C., Nzekwe, S. C., Okeleji, L. O., Amos, V., Ajayi, O. H., & Ajayi, A. F. (2022) · Biochemistry · doi:10.5772/intechopen.107839 · Cited by 3 · see citing works

The role of mitochondrial oxidation in endotoxin-induced liver-dependent swine pulmonary edema

Siore, A. M., Parker, R., Cuppels, C., Thorn, N. E., Hansen, J. M., Stecenko, A. A., & Brigham, K. L. (2012) · Pulmonary Pharmacology & Therapeutics · doi:10.1016/j.pupt.2012.08.002 · Cited by 2 · see citing works

Micellar Effect of Ammonium Based Cationic Surfactants on Kinetics of Methylene Blue‐Assisted Ru (III) and Cu (II) Catalyzed Cysteine/Cystine Transformation in Acidic Aqueous Media

Jan, R., Bhat, M. A., Islam, N., & Khan, B. (2015) · Journal of Surfactants and Detergents · doi:10.1007/s11743-015-1713-7 · Cited by 1 · see citing works

Method of Cysteine/Cystine Ratio Assessment Suitable for Physiological Applications

Vasilescu, I., Lițescu, S. C., Eremia, S. A. V., Penu, R., & Radu, G. L. (2013) · Cited by 1 · see citing works

EFEITO DA SUPLEMENTAÇÃO COM ÓLEO DE PEIXE NO MODELO EXPERIMENTAL DE SEPSE

Campos, R., Bortoti, A. A., Steclan, C. A., Pawlowytsch, P. W. D. M., Valério, M. C. J., Paluch, C. H., & Fernandes, L. C. (2020) · Revista Contexto & Saúde · doi:10.21527/2176-7114.2020.39.27-34 · Cited by 1 · see citing works

Environmental Toxicology: Oxidative Stress

Jones, D. P. (2012) · Springer eBooks · doi:10.1007/978-1-4614-5764-0_12

Free radical biology and medicine

(2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00485-4

Contribución del co-transportador Na+- HCO3- y de la anhidrasa carbónica a las alteraciones por isquemia y reperfusión: rol de la mitocondria

Pardo, A. C. (2019) · doi:10.35537/10915/72902

Cysteine/cystine redox signaling in cardiovascular disease

Go, Y.-M., & Jones, D. P. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.11.029 · Cited by 447 · see citing works

Gene and Protein Responses of Human Monocytes to Extracellular Cysteine Redox Potential

Go, Y., Craige, S. M., Orr, M. L., Gernert, K. M., & Jones, D. P. (2009) · Toxicological Sciences · doi:10.1093/toxsci/kfp205 · Cited by 23 · see citing works

Extracellular communication and signaling by thiol/disulfide redox states

Jones, D. P. (2011) · The FASEB Journal · doi:10.1096/fasebj.25.1_supplement.196.1

145 Mitochondrial thioredoxin-2 blocks pro-inflammatory signaling by plasma cysteine redox potential

Go, Y., Koval, M. H., Reed, M. S., Liang, Y., Smith, D., Pohl, J., & Jones, D. P. (2010) · Mitochondrion · doi:10.1016/j.mito.2009.12.136

Intracellular Proatherogenic Events and Cell Adhesion Modulated by Extracellular Thiol/Disulfide Redox State

Go, Y., & Jones, D. P. (2005) · Circulation · doi:10.1161/circulationaha.104.515155 · Cited by 153 · see citing works