Thioredoxin and Glutaredoxin Systems

Exercise-Induced Oxidative Stress: Cellular Mechanisms and Impact on Muscle Force Production

Powers, S. K., & Jackson, M. J. (2008) · Physiological Reviews · doi:10.1152/physrev.00031.2007 · Cited by 2,459

Mammalian thioredoxin is a direct inhibitor of apoptosis signal‐regulating kinase (ASK) 1

Saitoh, M., Nishitoh, H., Fujii, M., Takeda, K., Tobiume, K., Sawada, Y., Kawabata, M., Miyazono, K., & Ichijo, H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.9.2596 · Cited by 2,377

Redox Regulation of Fos and Jun DNA-Binding Activity in Vitro

Abate, C., Patel, L., Rauscher, F. J., & Curran, T. (1990) · Science · doi:10.1126/science.2118682 · Cited by 1,573

Drug delivery strategy utilizing conjugation via reversible disulfide linkages: Role and site of cellular reducing activities

Saito, G., Swanson, J. A., & Lee, K.-D. (2003) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(02)00179-5 · Cited by 1,407

Molecular inflammation: Underpinnings of aging and age-related diseases

Chung, H. Y., Cesari, M., Anton, S., Marzetti, E., Giovannini, S., Seo, A. Y., Carter, C., Yu, B. P., & Leeuwenburgh, C. (2009) · Ageing Research Reviews · doi:10.1016/j.arr.2008.07.002 · Cited by 1,203

Recent progresses in small-molecule enzymatic fluorescent probes for cancer imaging

Liu, H.-W., Chen, L., Xu, C., Li, Z., Zhang, H., Zhang, X.-B., & Tan, W. (2018) · Chemical Society Reviews · doi:10.1039/c7cs00862g · Cited by 948

Selenium, selenoproteins and human health: a review

Brown, K., & Arthur, Jr. (2001) · Public Health Nutrition · doi:10.1079/phn2001143 · Cited by 927

Thioredoxin and Related Molecules–From Biology to Health and Disease

Lillig, C. H., & Holmgren, A. (2007) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.9.25 · Cited by 724

Identification and characterization of Ref‐1, a nuclear protein that facilitates AP‐1 DNA‐binding activity.

Xanthoudakis, S., & Curran, T. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05097.x · Cited by 708

Redox signaling: hydrogen peroxide as intracellular messenger

Rhee, S. G. (1999) · Experimental & Molecular Medicine · doi:10.1038/emm.1999.9 · Cited by 701

The thioredoxin system in cancer

Arnér, E. S. J., & Holmgren, A. (2006) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2006.10.009 · Cited by 589

Positive and Negative Regulation of Insulin Signaling by Reactive Oxygen and Nitrogen Species

Bashan, N., Kovsan, J., Kachko, I., Ovadia, H., & Rudich, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00014.2008 · Cited by 542

Targeting thioredoxin reductase is a basis for cancer therapy by arsenic trioxide

Lu, J., Chew, E.-H., & Holmgren, A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701549104 · Cited by 526

S -Nitrosylation in Cardiovascular Signaling

Lima, B., Forrester, M. T., Hess, D. T., & Stamler, J. S. (2010) · Circulation Research · doi:10.1161/circresaha.109.207381 · Cited by 490

Grx5 Is a Mitochondrial Glutaredoxin Required for the Activity of Iron/Sulfur Enzymes

Rodrı́guez-Manzaneque, M. T., Tamarit, J., Bellı́, G., Ros, J., & Herrero, E. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-10-0517 · Cited by 464

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

ATM deficiency and oxidative stress: a new dimension of defective response to DNA damage

Barzilai, A. (2002) · DNA Repair · doi:10.1016/s1568-7864(01)00007-6 · Cited by 359

Monitoring disulfide bond formation in the eukaryotic cytosol

Østergaard, H., Tachibana, C., & Winther, J. R. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200402120 · Cited by 333

Inhibition of Mammalian Thioredoxin Reductase by Some Flavonoids: Implications for Myricetin and Quercetin Anticancer Activity

Lu, J., Papp, L. V., Fang, J., Rodriguez-Nieto, S., Zhivotovsky, B., & Holmgren, A. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3310 · Cited by 326

Human Mitochondrial Glutaredoxin Reduces S-Glutathionylated Proteins with High Affinity Accepting Electrons from Either Glutathione or Thioredoxin Reductase

Johansson, C., Lillig, C. H., & Holmgren, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312719200 · Cited by 320

Mitochondrial NADPH, transhydrogenase and disease

Rydström, J. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.03.010 · Cited by 256

Staphylococcal response to oxidative stress

Gaupp, R., Ledala, N., & Somerville, G. A. (2012) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2012.00033 · Cited by 253

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

Glutathione and Glutaredoxin Act as a Backup of Human Thioredoxin Reductase 1 to Reduce Thioredoxin 1 Preventing Cell Death by Aurothioglucose

Du, Y., Zhang, H., Lu, J., & Holmgren, A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.392225 · Cited by 230

Sex differences in inflammation, redox biology, mitochondria and autoimmunity

Di Florio, D. N., Sin, J., Coronado, M. J., Atwal, P. S., & Fairweather, D. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101482 · Cited by 185

Protein glutathionylation in health and disease

Ghezzi, P. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.02.009 · Cited by 169

Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells toward doxorubicin and phenylarsine oxide

Lillig, C. H., Lönn, M. E., Enoksson, M., Fernandes, A. P., & Holmgren, A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401896101 · Cited by 147

Reversible Sequestration of Active Site Cysteines in a 2Fe-2S-bridged Dimer Provides a Mechanism for Glutaredoxin 2 Regulation in Human Mitochondria

Johansson, C., Kavanagh, K. L., Gileadi, O., & Oppermann, U. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608179200 · Cited by 147

Driving the cell cycle through metabolism

Cai, L., & Tu, B. P. (2012) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154010 · Cited by 140

Purification of Mitochondrial Thioredoxin Reductase and Its Involvement in the Redox Regulation of Membrane Permeability

Rigobello, M. P., Callegaro, M. T., Barzon, E., Benetti, M., & Bindoli, A. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00216-5 · Cited by 138

The use of thiols by ribonucleotide reductase

Holmgren, A., & Sengupta, R. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.09.005 · Cited by 116

The Follicle-Stimulating Hormone Receptor: Biochemistry, Molecular Biology, Physiology, and Pathophysiology

Simoni, M., Gromoll, J., & Nieschlag, E. (1997) · Endocrine Reviews · doi:10.1210/edrv.18.6.0320 · Cited by 82

Inhibition of the glutaredoxin and thioredoxin systems and ribonucleotide reductase by mutant p53-targeting compound APR-246

Haffo, L., Lu, J., Bykov, V. J. N., Martin, S. S., Ren, X., Coppo, L., Wiman, K. G., & Holmgren, A. (2018) · Scientific Reports · doi:10.1038/s41598-018-31048-7 · Cited by 73

Evolution and cellular function of monothiol glutaredoxins: involvement in iron–sulphur cluster assembly

Vilella, F., Alves, R., Rodríguez‐Manzaneque, M. T., Bellí, G., Swaminathan, S., Sunnerhagen, P., & Herrero, E. (2004) · Comparative and Functional Genomics · doi:10.1002/cfg.406 · Cited by 54

Endoplasmic reticulum (ER) stress–induced reactive oxygen species (ROS) are detrimental for the fitness of a thioredoxin reductase mutant

Kritsiligkou, P., Rand, J. D., Weids, A. J., Wang, X., Kershaw, C. J., & Grant, C. M. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.001824 · Cited by 36

Intracellular free radical scavenging activity and protective role of mammalian cells by antioxidant peptide from thioredoxin disulfide reductase of Arthrospira platensis

Sannasimuthu, A., & Arockiaraj, J. (2019) · Journal of Functional Foods · doi:10.1016/j.jff.2019.103513 · Cited by 32

Redox-Regulated, Targeted Affinity Isolation of NADH-Dependent Protein Interactions with the Branched Chain Aminotransferase Proteins

Hindy, M. E. L., & Conway, M. E. (2019) · Methods in Molecular Biology · doi:10.1007/978-1-4939-9463-2_13 · Cited by 5