Molecular Mechanisms and Clinical Implications of Reversible Protein S -Glutathionylation

Biochemistry and molecular cell biology of diabetic complications

Brownlee, M. (2001) · Nature · doi:10.1038/414813a · Cited by 9,107 · see citing works

Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium.

Murry, C. E., Jennings, R. B., & Reimer, K. A. (1986) · Circulation · doi:10.1161/01.cir.74.5.1124 · Cited by 7,813 · see citing works

Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases

Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455 · see citing works

Cancer chemoprevention with dietary phytochemicals

Surh, Y.-J. (2003) · Nature reviews. Cancer · doi:10.1038/nrc1189 · Cited by 2,955 · see citing works

The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth

Christofk, H. R., Vander Heiden, M. G., Harris, M. H., Ramanathan, A., Gerszten, R. E., Wei, R., Fleming, M. D., Schreiber, S. L., & Cantley, L. C. (2008) · Nature · doi:10.1038/nature06734 · Cited by 2,820 · see citing works

Biochemistry of nitric oxide and its redox-activated forms

Stamler, J. S., Singel, D. J., & Loscalzo, J. (1992) · Science · doi:10.1126/science.1281928 · Cited by 2,744 · see citing works

NF-κB at the crossroads of life and death

Karin, M., & Lin, A. (2002) · Nature Immunology · doi:10.1038/ni0302-221 · Cited by 2,709 · see citing works

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 · see citing works

Local and systemic insulin resistance resulting from hepatic activation of IKK-β and NF-κB

Cai, D., Yuan, M., Frantz, D. F., Melendez, P. A., Hansen, L., Lee, J., & Shoelson, S. E. (2005) · Nature Medicine · doi:10.1038/nm1166 · Cited by 2,245 · see citing works

Oxidative stress in neurodegeneration: Cause or consequence?

Andersen, J. K. (2004) · Nature Medicine · doi:10.1038/nrn1434 · Cited by 1,869 · see citing works

Regulation of cardiac hypertrophy by intracellular signalling pathways

Heineke, J., & Molkentin, J. D. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1983 · Cited by 1,856 · see citing works

Reactive Oxygen Species Promote TNFα-Induced Death and Sustained JNK Activation by Inhibiting MAP Kinase Phosphatases

Kamata, H., Honda, S.-I., Maeda, S., Chang, L., Hirata, H., & Karin, M. (2005) · Cell · doi:10.1016/j.cell.2004.12.041 · Cited by 1,792 · see citing works

IKK-β links inflammation to obesity-induced insulin resistance

Arkan, M. C., Hevener, A. L., Greten, F. R., Maeda, S., Li, Z.-W., Long, J. M., Wynshaw-Boris, A., Poli, G., Olefsky, J., & Karin, M. (2005) · Nature Medicine · doi:10.1038/nm1185 · Cited by 1,773 · see citing works

The c-Jun NH2-terminal kinase promotes insulin resistance during association with insulin receptor substrate-1 and phosphorylation of Ser307

Aguirre, V., Uchida, T., Yenush, L., Davis, R., & White, M. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.9047 · Cited by 1,487 · see citing works

Peroxiredoxins: A historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling

Rhee, S. G., Chae, H. Z., & Kim, K. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.02.026 · Cited by 1,409 · see citing works

ETIOLOGY AND PATHOGENESIS OF PARKINSON'S DISEASE

Olanow, C. W., & Tatton, W. G. (1999) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.22.1.123 · Cited by 1,394 · see citing works

Protein kinase C activation and the development of diabetic complications.

Koya, D., & King, G. L. (1998) · Diabetes · doi:10.2337/diabetes.47.6.859 · Cited by 1,335 · see citing works

Triggering and amplifying pathways of regulation of insulin secretion by glucose.

Henquin, J. C. (2000) · Diabetes · doi:10.2337/diabetes.49.11.1751 · Cited by 1,201 · see citing works

Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia

Sian, J., Dexter, D. T., Lees, A. J., Daniel, S., Agid, Y., Javoy‐Agid, F., Jenner, P., & Marsden, C. D. (1994) · Annals of Neurology · doi:10.1002/ana.410360305 · Cited by 1,161 · see citing works

S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding

Hara, M. R., Agrawal, N., Kim, S. F., Cascio, M. B., Fujimuro, M., Ozeki, Y., Takahashi, M., Cheah, J. H., Tankou, S. K., Hester, L. D., et al. (2005) · Nature Cell Biology · doi:10.1038/ncb1268 · Cited by 1,071 · see citing works

Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor

Lee, S.-R., Kwon, K.-S., Kim, S.-R., & Rhee, S. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.25.15366 · Cited by 969 · see citing works

Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate

Salmeen, A., Andersen, J. N., Myers, M. P., Meng, T.-C., Hinks, J. A., Tonks, N. K., & Barford, D. (2003) · Nature · doi:10.1038/nature01680 · Cited by 951 · see citing works

Inhibition of GAPDH activity by poly(ADP-ribose) polymerase activates three major pathways of hyperglycemic damage in endothelial cells

Du, X., Matsumura, T., Edelstein, D., Rossetti, L., Zsengellér, Z. K., Szabó, C., & Brownlee, M. (2003) · Journal of Clinical Investigation · doi:10.1172/jci18127 · Cited by 832 · see citing works

ATP Activates a Reactive Oxygen Species-dependent Oxidative Stress Response and Secretion of Proinflammatory Cytokines in Macrophages

Cruz, C. M., Rinna, A., Forman, H. J., Ventura, A. L. M., Persechini, P. M., & Ojcius, D. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608083200 · Cited by 786 · see citing works

Serine Phosphorylation of Insulin Receptor Substrate 1 by Inhibitor κB Kinase Complex

Gao, Z., Hwang, D. H., Bataille, F., Lefevre, M., York, D. A., Quon, M. J., & Ye, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209459200 · Cited by 777 · see citing works

Hyperoxia increases oxygen radical production in rat lungs and lung mitochondria.

Freeman, B. Α., & Crapo, J. D. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68544-3 · Cited by 762 · see citing works

Molecular and Cellular Aspects of Thiol–Disulfide Exchange

Gilbert, H. (1990) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470123096.ch2 · Cited by 759 · see citing works

Regulation of protein function by S‐glutathiolation in response to oxidative and nitrosative stress

Klatt, P., & Lamas, S. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01601.x · Cited by 751 · see citing works

Calcium and neurodegeneration

Mattson, M. P. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2007.00275.x · Cited by 751 · see citing works

Oxidative stress and nitration in neurodegeneration: Cause, effect, or association?

Ischiropoulos, H., & Beckman, J. S. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200317638 · Cited by 748 · see citing works

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 · see citing works

S-Glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide

Adachi, T. K., Weisbrod, R. M., Pimentel, D. R., Ying, J., Sharov, V. S., Schöneich, C., & Cohen, R. A. (2004) · Nature Medicine · doi:10.1038/nm1119 · Cited by 662 · see citing works

Changes in thiol content and expression of glutathione redox system genes in the hippocampus and cerebellum in Alzheimer's disease

Aksenov, M. Y., & Markesbery, W. R. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(01)01636-6 · Cited by 661 · see citing works

Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B

van Montfort, R. L. M., Congreve, M., Tisi, D., Carr, R. A. E., & Jhoti, H. (2003) · Nature · doi:10.1038/nature01681 · Cited by 642 · see citing works

Cell death in the nervous system

Bredesen, D. E., Rao, R. V., & Mehlen, P. (2006) · Nature · doi:10.1038/nature05293 · Cited by 638 · see citing works

Redox modifications of protein-thiols: emerging roles in cell signaling.

Biswas, S., Chida, A., & Rahman, I. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2005.10.044 · Cited by 631 · see citing works

ATP-sensitive potassium channelopathies: focus on insulin secretion

Ashcroft, F. M. (2005) · Journal of Clinical Investigation · doi:10.1172/jci25495 · Cited by 627 · see citing works

NO+, NO, and NO- donation by S-nitrosothiols-implications for regulation of physiological functions by S-nitrosylation and acceleration of disulfide formation

Arnelle, D. R., & Stamler, J. S. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1231 · Cited by 604 · 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

Increasing Complexity of the Ras Signaling Pathway

Vojtek, A. B., & Der, C. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.32.19925 · Cited by 580 · see citing works

Role of p47 phox in Vascular Oxidative Stress and Hypertension Caused by Angiotensin II

Landmesser, U., Cai, H. “., Dikalov, S., McCann, L. A., Hwang, J., Jo, H., Holland, S. M., & Harrison, D. G. (2002) · Hypertension · doi:10.1161/01.hyp.0000032100.23772.98 · Cited by 572 · see citing works

Glucose neurotoxicity

Tomlinson, D. R., & Gardiner, N. J. (2007) · Nature reviews. Neuroscience · doi:10.1038/nrn2294 · Cited by 566 · see citing works

The Unstable Atheroma

Lee, R. T., & Libby, P. (1997) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.17.10.1859 · Cited by 557 · see citing works

Molecular aspects of lipoic acid in the prevention of diabetes complications

Packer, L., Kraemer, K., & Rimbach, G. (2001) · Nutrition · doi:10.1016/s0899-9007(01)00658-x · Cited by 556 · see citing works

Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes

Fratelli, M., Demol, H., Puype, M., Casagrande, S., Eberini, I., Salmona, M., Bonetto, V., Mengozzi, M., Duffieux, F., Miclet, E., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052592699 · Cited by 556 · see citing works

[2] Thiol/disulfide exchange equilibria and disulfidebond stability

Gilbert, H. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)51107-5 · Cited by 549 · see citing works

Early Embryonic Lethality Caused by Targeted Disruption of the Mouse Thioredoxin Gene

Matsui, M., Oshima, M., Oshima, H., Takaku, K., Maruyama, T., Yodoi, J., & Taketo, M. M. (1996) · Developmental Biology · doi:10.1006/dbio.1996.0208 · Cited by 546 · cited 1× · see citing works

Role of Aldose Reductase and Oxidative Damage in Diabetes and the Consequent Potential for Therapeutic Options

Sk, S., Ramana, K. V., & Bhatnagar, A. (2005) · Endocrine Reviews · doi:10.1210/er.2004-0028 · Cited by 529 · see citing works

Activation and phosphorylation of a pleckstrin homology domain containing protein kinase (RAC-PK/PKB) promoted by serum and protein phosphatase inhibitors.

Andjelkovic, M., Jakubowicz, T., Cron, P., Ming, X., Han, J. W., & Hemmings, B. (1996) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.93.12.5699 · Cited by 525 · see citing works

Glutathione S-transferase polymorphisms: cancer incidence and therapy

McIlwain, C., Townsend, D. M., & Tew, K. D. (2006) · Oncogene · doi:10.1038/sj.onc.1209373 · Cited by 525 · see citing works

GAPDH and Autophagy Preserve Survival after Apoptotic Cytochrome c Release in the Absence of Caspase Activation

Colell, A., Ricci, J.-E., Tait, S., Milasta, S., Maurer, U., Bouchier-Hayes, L., Fitzgerald, P., Guio-Carrion, A., Waterhouse, N. J., Li, C. W., et al. (2007) · Cell · doi:10.1016/j.cell.2007.03.045 · Cited by 516 · see citing works

Regulation of PTP1B via Glutathionylation of the Active Site Cysteine 215

Barrett, W. C., DeGnore, J. P., König, S., Fales, H. M., Keng, Y., Zhang, Z., Yim, M. B., & Chock, P. B. (1999) · Biochemistry · doi:10.1021/bi990240v · Cited by 488 · see citing works

Recent Trends in Glutathione Biochemistry—Glutathione–Protein Interactions: A Molecular Link between Oxidative Stress and Cell Proliferation?

Cotgreave, I. A., & Gerdes, R. G. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7812 · Cited by 481 · see citing works

Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione.

Holmgren, A. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.7.2275 · Cited by 477 · see citing works

Inflammation and the IKKβ/IκB/NF-κB axis in obesity- and diet-induced insulin resistance

Shoelson, S. E., Lee, J., & Yuan, M. (2003) · International Journal of Obesity · doi:10.1038/sj.ijo.0802501 · Cited by 474 · see citing works

Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress

Gallogly, M. M., & Mieyal, J. J. (2007) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2007.06.003 · Cited by 470 · see citing works

Survival kinases in ischemic preconditioning and postconditioning

Hausenloy, D. J., & Yellon, D. M. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2006.01.017 · Cited by 467 · see citing works

Activation of Matrix Metalloproteinases by Peroxynitrite-induced Protein S-Glutathiolation via Disulfide S-Oxide Formation

Okamoto, T., Akaike, T., Sawa, T., Miyamoto, Y., van der Vliet, A., & Maeda, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102417200 · Cited by 466 · see citing works

Inhibition of protein kinase C by tamoxifen.

O'Brian, C. A., Liskamp, R. M. J., Solomon, D. H., & Weinstein, I. B. (1985) · PubMed · Cited by 461 · see citing works

Oxidative Stress and Hypertension

Harrison, D. G., & Góngora, M. C. (2009) · Medical Clinics of North America · doi:10.1016/j.mcna.2009.02.015 · Cited by 451 · see citing works

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

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

Glutaredoxin: Role in Reversible Protein S-Glutathionylation and Regulation of Redox Signal Transduction and Protein Translocation

Shelton, M. D., Chock, P., & Mieyal, J. J. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.348 · Cited by 425 · see citing works

Modular Activation of Nuclear Factor-κB Transcriptional Programs in Human Diabetic Nephropathy

Schmid, H., Boucherot, A., Yasuda, Y., Henger, A., Brunner, B., Eichinger, F. H., Nitsche, A., Kiss, É., Bleich, M., Gröne, H., et al. (2006) · Diabetes · doi:10.2337/db06-0477 · Cited by 420 · see citing works

Inactivation of tyrosine hydroxylase by nitration following exposure to peroxynitrite and 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)

Ara, J. E., Przedborski, S., Naini, A., Jackson-Lewis, V. R., Trifiletti, R. R., Horwitz, J., & Ischiropoulos, H. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7659 · Cited by 414 · see citing works

Activation of Nuclear Factor-κB Induced by Diabetes and High Glucose Regulates a Proapoptotic Program in Retinal Pericytes

Romeo, G. R., Liu, W.-H., Asnaghi, V., Kern, T. S., & Lorenzi, M. (2002) · Diabetes · doi:10.2337/diabetes.51.7.2241 · Cited by 413 · see citing works

The Biochemistry and Physiology of S-Nitrosothiols

Hogg, N. (2002) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.42.092501.104328 · Cited by 412 · see citing works

Glutaredoxin 2 Catalyzes the Reversible Oxidation and Glutathionylation of Mitochondrial Membrane Thiol Proteins

Beer, S. M., Taylor, E. R., Brown, S. E., Dahm, C. C., Costa, N. J., Runswick, M. J., & Murphy, M. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408011200 · Cited by 404 · see citing works

Protein Sulfhydryls and Their Role in the Antioxidant Function of Protein S-Thiolation

Thomas, J. A., Poland, B. W., & Honzatko, R. B. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1261 · Cited by 399 · see citing works

Reversible Glutathionylation of Complex I Increases Mitochondrial Superoxide Formation

Taylor, E. R., Hurrell, F., Shannon, R. J., Lin, T., Hirst, J., & Murphy, M. P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209359200 · Cited by 389 · see citing works

Glutathionylation of the p50 Subunit of NF-κB: a Mechanism for Redox-Induced Inhibition of DNA Binding

Pineda‐Molina, E., Klatt, P., Vázquez, J., Marina, A., de Lacoba, M. G., Pérez‐Sala, D., & Lamas, S. (2001) · Biochemistry · doi:10.1021/bi011459o · Cited by 389 · see citing works

The nuclear encoded subunits of complex I from bovine heart mitochondria

Hirst, J., Carroll, J., Fearnley, I. M., Shannon, R. J., & Walker, J. E. (2003) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(03)00059-8 · Cited by 384 · see citing works

PTP1B: From the sidelines to the front lines!

Tonks, N. K. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00603-3 · Cited by 374 · see citing works

Targeting the protein kinase C family: are we there yet?

MacKay, H. J., & Twelves, C. (2007) · Nature reviews. Cancer · doi:10.1038/nrc2168 · Cited by 373 · see citing works

Roles of Superoxide Radical Anion in Signal Transduction Mediated by Reversible Regulation of Protein-tyrosine Phosphatase 1B

Barrett, W. C., DeGnore, J. P., Keng, Y., Zhang, Z., Yim, M. B., & Chock, P. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.49.34543 · Cited by 355 · see citing works

Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with πGST

Manevich, Y., Feinstein, S. I., & Fisher, A. B. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400181101 · Cited by 349 · see citing works

Role of NADPH Oxidase in the Vascular Hypertrophic and Oxidative Stress Response to Angiotensin II in Mice

Wang, H. D., Xu, S., Johns, D. G., Du, Y., Quinn, M. T., Cayatte, A. J., & Cohen, R. A. (2001) · Circulation Research · doi:10.1161/hh0901.089987 · Cited by 342 · see citing works

Reversible Glutathionylation Regulates Actin Polymerization in A431 Cells

Wang, J., Boja, E. S., Tan, W., Tekle, E., Fales, H. M., English, S., Mieyal, J. J., & Chock, P. B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100415200 · Cited by 336 · see citing works

The chemistry of the <i>S</i> -nitrosoglutathione/glutathione system

Singh, S. P., Wishnok, J. S., Keshive, M., Deen, W. M., & Tannenbaum, S. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.25.14428 · Cited by 336 · see citing works

Cloning and Expression of a Novel Human Glutaredoxin (Grx2) with Mitochondrial and Nuclear Isoforms

Lundberg, M., Johansson, C., Chandra, J., Enoksson, M., Jacobsson, G., Lundström-Ljung, J., Johansson, M., & Holmgren, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011605200 · Cited by 335 · see citing works

Acute Cadmium Exposure Inactivates Thioltransferase (Glutaredoxin), Inhibits Intracellular Reduction of Protein-glutathionyl-mixed Disulfides, and Initiates Apoptosis

Chrestensen, C. A., Starke, D. W., & Mieyal, J. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004097200 · Cited by 333 · see citing works

Redox Paradox

Goldstein, B. J., Mahadev, K., & Wu, X. (2005) · Diabetes · doi:10.2337/diabetes.54.2.311 · Cited by 326 · see citing works

Signaling pathways in ischemic preconditioning

Downey, J. M., Davis, A., & Cohen, M. V. (2007) · Heart Failure Reviews · doi:10.1007/s10741-007-9025-2 · Cited by 321 · see citing works

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 · see citing works

Glutathione S-transferase P1–1 (GSTP1–1) Inhibits c-Jun N-terminal Kinase (JNK1) Signaling through Interaction with the C Terminus

Wang, T., Arifoglu, P., Ronai, Z. A., & Tew, K. D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101355200 · Cited by 313 · see citing works

Nitric Oxide-induced S-Glutathionylation and Inactivation of Glyceraldehyde-3-phosphate Dehydrogenase

Mohr, S., Hallak, H., de Boitte, A., Lapetina, E. G., & Brüne, B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.14.9427 · Cited by 309 · see citing works

Thioltransferase is a specific glutathionyl mixed-disulfide oxidoreductase

Gravina, S. A., & Mieyal, J. J. (1993) · Biochemistry · doi:10.1021/bi00064a021 · Cited by 306 · see citing works

Role of Cysteine Residues in Regulation of p53 Function

Rainwater, R., Parks, D., Anderson, M. E., Tegtmeyer, P., & Mann, K. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.7.3892 · Cited by 305 · see citing works

Glutaredoxin Exerts an Antiapoptotic Effect by Regulating the Redox State of Akt*

Murata, H., Ihara, Y., Nakamura, H., Yodoi, J., Sumikawa, K., & Kondo, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m310171200 · Cited by 304 · see citing works

S-Glutathiolation of Ras Mediates Redox-sensitive Signaling by Angiotensin II in Vascular Smooth Muscle Cells

Adachi, T. K., Pimentel, D. R., Heibeck, T. H., Hou, X., Lee, Y. J., Jiang, B., Ido, Y., & Cohen, R. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313320200 · Cited by 301 · see citing works

Molecular Mechanisms and Potential Clinical Significance of S -Glutathionylation

Dalle‐Donne, I., Milzani, A., Gagliano, N., Colombo, R., Giustarini, D., & Rossi, R. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1716 · Cited by 296 · see citing works

Characterization of human glutaredoxin 2 as iron–sulfur protein: A possible role as redox sensor

Lillig, C. H., Berndt, C., Vergnolle, O., Lönn, M. E., Hudemann, C., Bill, E., & Holmgren, A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500735102 · Cited by 290 · see citing works

Regulation of Ubiquitin-conjugating Enzymes by Glutathione Following Oxidative Stress

Jahngen-Hodge, J., Obin, M. S., Gong, X., Shang, F., Nowell, T., Gong, J., Abasi, H., Blumberg, J. B., & Taylor, A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.45.28218 · Cited by 283 · see citing works

Redox regulation of c‐Jun DNA binding by reversible S‐glutathiolation

Klatt, P., Pineda‐Molina, E., de Lacoba, M. G., Padilla, C. A., Martı́nez-Galisteo, E., Bárcena, J. A., & Lamas, S. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.12.1481 · Cited by 280 · see citing works

PTP1B inhibitors as potential therapeutics in the treatment of Type 2 diabetes and obesity

Zhang, Z., & Lee, S.-Y. (2003) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.12.2.223 · Cited by 275 · see citing works

Direct evidence for S-nitrosation of mitochondrial complex I

Burwell, L. S., Nadtochiy, S. M., Tompkins, A. J., Young, S., & Brookes, P. S. (2006) · Biochemical Journal · doi:10.1042/bj20051435 · Cited by 274 · see citing works

Nitric oxide and thiol groups

Gaston, B. M. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00023-7 · Cited by 265 · see citing works

Redox Control of Exocytosis

Ivarsson, R., Quintens, R., Dejonghe, S., Tsukamoto, K., in ’t Veld, P., Renström, E., & Schuit, F. C. (2005) · Diabetes · doi:10.2337/diabetes.54.7.2132 · Cited by 265 · see citing works

Involvement of Oxidative Stress in the Pathogenesis of Diabetes

Kaneto, H., Katakami, N., Kawamori, D., Miyatsuka, T., Sakamoto, K., Matsuoka, T., Matsuhisa, M., & Yamasaki, Y. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.1465 · Cited by 264 · see citing works

Cellular localization of tyrosine hydroxylase by immunohistochemistry.

Pickel, V. M., JOH, T. H., Field, P. M., Becker, C. G., & Reis, D. J. (1975) · Journal of Histochemistry & Cytochemistry · doi:10.1177/23.1.234988 · Cited by 262 · see citing works

Role of Glutaredoxin in Metabolic Oxidative Stress

Song, J. J., Rhee, J. G., Suntharalingam, M., Walsh, S. A., Spitz, D. R., & Lee, Y. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206826200 · Cited by 260 · see citing works

Glycogen phosphorylase inhibitors for treatment of type 2 diabetes mellitus

Treadway, J. L., Mendys, P., & Hoover, D. J. (2001) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.10.3.439 · Cited by 260 · see citing works

The electrophile counterattack response: Protection against neoplasia and toxicity

Prestera, T., Zhang, Y., Spencer, S. R., Wilczak, C. A., & Talalay, P. (1993) · Advances in Enzyme Regulation · doi:10.1016/0065-2571(93)90024-8 · Cited by 256 · see citing works

Identification of Cysteines Involved in S-Nitrosylation, S-Glutathionylation, and Oxidation to Disulfides in Ryanodine Receptor Type 1

Aracena-Parks, P., Goonasekera, S. A., Gilman, C. P., Dirksen, R. T., Hidalgo, C., & Hamilton, S. L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600876200 · Cited by 254 · see citing works

Peroxynitrite Modification of Protein Thiols: Oxidation, Nitrosylation, and S-Glutathiolation of Functionally Important Cysteine Residue(s) in the Sarcoplasmic Reticulum Ca-ATPase

Viner, R. I., Williams, T. D., & Schöneich, C. (1999) · Biochemistry · doi:10.1021/bi9909445 · Cited by 253 · see citing works

Glutathione Depletion in PC12 Results in Selective Inhibition of Mitochondrial Complex I Activity

Jha, N., Jurma, O. P., Lalli, G., Liu, Y., Pettus, E. H., Greenamyre, J. T., Liu, R.-M., Forman, H. J., & Andersen, J. K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000120200 · Cited by 252 · see citing works

Protein‐sulfenic acid stabilization and function in enzyme catalysis and gene regulation

Claiborne, A., Miller, H., Parsonage, D., & Ross, R. P. (1993) · The FASEB Journal · doi:10.1096/fasebj.7.15.8262333 · Cited by 251 · see citing works

p53 protein, interferon-γ, and NF-κB levels are elevated in the parkinsonian brain

Mogi, M., Kondo, T., Mizuno, Y., & Nagatsu, T. (2006) · Neuroscience Letters · doi:10.1016/j.neulet.2006.12.003 · Cited by 242 · see citing works

Phorbol esters induce multidrug resistance in human breast cancer cells.

Fine, R. L., Patel, J. B., & Chabner, B. A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.2.582 · Cited by 240 · see citing works

Poly(ADP-Ribose) Polymerase Is Involved in the Development of Diabetic Retinopathy via Regulation of Nuclear Factor-κB

Zheng, L., Szabó, C., & Kern, T. S. (2004) · Diabetes · doi:10.2337/diabetes.53.11.2960 · Cited by 238 · see citing works

Identification and Characterization of a New Mammalian Glutaredoxin (Thioltransferase), Grx2

Gladyshev, V. N., Liu, A., Novoselov, S. V., Krysan, K., Sun, Q., Kryukov, V. M., Kryukov, G. V., & Lou, M. F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100020200 · Cited by 234 · see citing works

Characterization of Sulfur-centered Radical Intermediates Formed during the Oxidation of Thiols and Sulfite by Peroxynitrite

Karoui, H., Hogg, N., Fréjaville, C., Tordo, P., & Kalyanaraman, B. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.11.6000 · Cited by 231 · cited 1× · see citing works

Mitochondrial Complex II in the Post-ischemic Heart

Chen, Y., Chen, C., Pfeiffer, D. R., & Zweier, J. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702294200 · Cited by 230 · see citing works

An essential role of NFκB in tyrosine kinase signaling of p38 MAP kinase regulation of myocardial adaptation to ischemia

Maulik, N., Sato, M., Price, B. D., & Das, D. K. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00632-2 · Cited by 229 · see citing works

Blockade of Electron Transport during Ischemia Protects Cardiac Mitochondria

Lesnefsky, E. J., Chen, Q., Moghaddas, S., Hassan, M. O., Tandler, B., & Hoppel, C. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409720200 · Cited by 229 · see citing works

Two adjacent AP-1-like binding sites form the electrophile-responsive element of the murine glutathione S-transferase Ya subunit gene.

Friling, R. S., Bergelson, S., & Daniel, V. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.2.668 · Cited by 229 · see citing works

Specificity in reactive oxidant signaling: think globally, act locally

Terada, L. S. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200605036 · Cited by 214 · see citing works

Ischemic Preconditioning Reduces Apoptosis By Upregulating Anti-Death Gene Bcl-2

Maulik, N., Engelman, R. M., Rousou, J. A., Flack, J. E., Deaton, D. W., & Das, D. K. (1999) · Circulation · doi:10.1161/01.cir.100.suppl_2.ii-369 · Cited by 214 · see citing works

Pathophysiology of nitric oxide and related species: free radical reactions and modification of biomolecules

Eiserich, J. P., Patel, R. P., & O’Donnell, V. B. (1998) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(99)00002-3 · Cited by 210 · see citing works

Mitochondrial dysfunction, oxidative stress and neurodegeneration

Mancuso, M., Coppedè, F., Migliore, L., Siciliano, G., & Murri, L. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-10110 · Cited by 209 · see citing works

Identification of Oxidant-Sensitive Proteins: TNF-α Induces Protein Glutathiolation

Sullivan, D. M., Wehr, N. B., Fergusson, M. M., Levine, R. L., & Finkel, T. (2000) · Biochemistry · doi:10.1021/bi0007674 · Cited by 209 · see citing works

Reversible S-glutathionylation of Cys374 regulates actin filament formation by inducing structural changes in the actin molecule

Dalle‐Donne, I., Giustarini, D., Rossi, R., Colombo, R., & Milzani, A. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01182-6 · Cited by 208 · see citing works

Importance of oxidative stress in the pathogenesis and treatment of asthma

Riedl, M. A., & Nel, A. E. (2008) · Current Opinion in Allergy and Clinical Immunology · doi:10.1097/aci.0b013e3282f3d913 · Cited by 208 · see citing works

S-Glutathionylation: Indicator of Cell Stress and Regulator of the Unfolded Protein Response

Townsend, D. M. (2007) · Molecular Interventions · doi:10.1124/mi.7.6.7 · Cited by 206 · see citing works

Redox regulation of ubiquitin‐conjugating enzymes: mechanistic insights using the thiol‐specific oxidant diamide

Obin, M. S., Shang, F., Gong, X., Handelman, G. J., Blumberg, J. B., & Taylor, A. (1998) · The FASEB Journal · doi:10.1096/fasebj.12.7.561 · Cited by 205 · see citing works

Oxidative Stress and Antioxidants in the Pathogenesis of Pulmonary Fibrosis: A Potential Role for Nrf2

Walters, D. M., Cho, H., & Kleeberger, S. R. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1901 · Cited by 205 · see citing works

[3] Kinetic factors that control the fate of thiyl radicals in cells

Wardman, P., & von Sonntag, C. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)51108-3 · Cited by 204 · see citing works

Superoxide dismutase, catalase and scavengers of hydroxyl radical protect against the toxic action of alloxan on pancreatic islet cells in vitro

Grankvist, K., Marklund, S. L., Sehlin, J., & Täljedal, I. ‐. (1979) · Biochemical Journal · doi:10.1042/bj1820017 · Cited by 204 · see citing works

Nucleoredoxin, Glutaredoxin, and Thioredoxin Differentially Regulate NF-κB, AP-1, and CREB Activation in HEK293 Cells

Hirota, K., Matsui, M., Murata, M., Takashima, Y., Cheng, F. S., Itoh, T., Fukuda, K., & Yodoi, J. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3106 · Cited by 203 · see citing works

Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes

Thorpe, C., Hoober, K. L., Raje, S., Glynn, N. M., Burnside, J., Turi, G. K., & Coppock, D. L. (2002) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(02)00337-5 · Cited by 201 · see citing works

Human p53 Is Inhibited by Glutathionylation of Cysteines Present in the Proximal DNA-Binding Domain during Oxidative Stress,

Velu, C. S., Niture, S. K., Doneanu, C. E., Pattabiraman, N., & Srivenugopal, K. S. (2007) · Biochemistry · doi:10.1021/bi700425y · Cited by 201 · see citing works

Variability of Antioxidant-Related Gene Expression in the Airway Epithelium of Cigarette Smokers

Hackett, N. R., Heguy, A., Harvey, B., O’Connor, T. P., Luettich, K., Flieder, D. B., Kaplan, R., & Crystal, R. G. (2003) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2002-0321oc · Cited by 200 · see citing works

Initiation of Neuronal Damage by Complex I Deficiency and Oxidative Stress in Parkinson's Disease

Tretter, L., Sipos, I., & Ádám‐Vizi, V. (2004) · Neurochemical Research · doi:10.1023/b:nere.0000014827.94562.4b · Cited by 199 · see citing works

Biothiols in Health and Disease

Packer, L., & Cadenas, E. (1995) · Medical Entomology and Zoology · Cited by 198 · see citing works

Oxidative stress inhibits MEKK1 by site-specific glutathionylation in the ATP-binding domain

Cross, J. V., & Templeton, D. J. (2004) · Biochemical Journal · doi:10.1042/bj20040591 · Cited by 196 · see citing works

Caspase Activation in Retinas of Diabetic and Galactosemic Mice and Diabetic Patients

Mohr, S., Xi, X., Tang, J., et al. (2002) · Diabetes · doi:10.2337/diabetes.51.4.1172 · Cited by 196 · see citing works

Glutathionylation of Mitochondrial Proteins

Hurd, T., Costa, N. J., Dahm, C., Beer, S. M., Brown, S. E., Filipovska, A., & Murphy, M. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.999 · Cited by 195 · see citing works

Oxidation and Nitrosation of Thiols at Low Micromolar Exposure to Nitric Oxide

Jourd’heuil, D., Jourd’heuil, F. L., & Feelisch, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300203200 · Cited by 194 · see citing works

A Novel Role for Human Sulfiredoxin in the Reversal of Glutathionylation

Findlay, V. J., Townsend, D. M., Morris, T. E., Fraser, J. P., He, L., & Tew, K. D. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-0484 · Cited by 193 · see citing works

The Active Site Cysteine of the Proapoptotic Protein Glyceraldehyde-3-phosphate Dehydrogenase Is Essential in Oxidative Stress-induced Aggregation and Cell Death

Nakajima, H., Amano, W., Fujita, A., Fukuhara, A., Azuma, Y., Hata, F., Inui, T., & Takeuchi, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704199200 · Cited by 190 · see citing works

S-Glutathiolated Hepatocyte Proteins and Insulin Disulfides as Substrates for Reduction by Glutaredoxin, Thioredoxin, Protein Disulfide Isomerase, and Glutathione

Jung, C., & Thomas, J. A. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0482 · Cited by 187 · see citing works

Mitochondrial Dysfunction in Aging and Alzheimer's Disease: Strategies to Protect Neurons

Reddy, P. H. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1754 · Cited by 187 · see citing works

Differential role of glutaredoxin and thioredoxin in metabolic oxidative stress-induced activation of apoptosis signal-regulating kinase 1

Song, J. J., & Lee, Y. J. (2003) · Biochemical Journal · doi:10.1042/bj20030275 · Cited by 187 · see citing works

Induction of Phase I and Phase II Drug-Metabolizing Enzyme mRNA, Protein, and Activity by BHA, Ethoxyquin, and Oltipraz

Buetler, T. M., Gallagher, E. P., Wang, C. H., Stahl, D., Hayes, J. D., & Eaton, D. L. (1995) · Toxicology and Applied Pharmacology · doi:10.1006/taap.1995.1207 · Cited by 184 · see citing works

Catalytic and Chemical Competence of Regulation of Cdc25 Phosphatase by Oxidation/Reduction

Sohn, J., & Rudolph, J. (2003) · Biochemistry · doi:10.1021/bi0345081 · Cited by 183 · see citing works

Regulation of cAMP-dependent Protein Kinase Activity by Glutathionylation

Humphries, K. M., Juliano, C. E., & Taylor, S. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207088200 · Cited by 183 · see citing works

Involvement of glutaredoxin-1 and thioredoxin-1 in β-amyloid toxicity and Alzheimer's disease

Akterin, S., Cowburn, R. F., Miranda‐Vizuete, A., Jiménez, A., Bogdanović, N., Winblad, B. G., & Cedazo-Mı́nguez, Á. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401818 · Cited by 182 · see citing works

The Redox Regulation of Thiol Dependent Signaling Pathways in Cancer

Giles, G. I. (2006) · Current Pharmaceutical Design · doi:10.2174/138161206779010549 · Cited by 182 · see citing works

Glutathione-Thiyl Radical Scavenging and Transferase Properties of Human Glutaredoxin (Thioltransferase)

Starke, D. W., Chock, P. B., & Mieyal, J. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210434200 · Cited by 179 · see citing works

Akt in Ischemia and Reperfusion

Mullonkal, C. J., & Toledo-Pereyra, L. H. (2007) · Journal of Investigative Surgery · doi:10.1080/08941930701366471 · Cited by 175 · see citing works

Glutathione in blood of patients with Friedreich's ataxia

Piemonte, F., Pastore, A., Tozzi, G., Tagliacozzi, D., Santorelli, F. M., Carrozzo, R., Casali, C., Damiano, M. G., Federici, G., & Bertini, E. (2001) · European Journal of Clinical Investigation · doi:10.1046/j.1365-2362.2001.00922.x · Cited by 174 · see citing works

S-Nitrosylation and S-Glutathiolation of Protein Sulfhydryls byS-Nitroso Glutathione

Ji, Y., Akerboom, T. P. M., Sies, H., & Thomas, J. A. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.1013 · Cited by 173 · see citing works

Regulation 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

Effects of Diabetes on Ryanodine Receptor Ca Release Channel (RyR2) and Ca2+ Homeostasis in Rat Heart

Yaraş, N., Uğur, M., Özdemir, S., Gürdal, H., Puralı, N., Lacampagne, A., Vassort, G., & Turan, B. (2005) · Diabetes · doi:10.2337/diabetes.54.11.3082 · Cited by 172 · see citing works

Molecular Analysis of ATP-sensitive K Channel Gating and Implications for Channel Inhibition by ATP

Trapp, S., Proks, P., Tucker, S. J., & Ashcroft, F. M. (1998) · The Journal of General Physiology · doi:10.1085/jgp.112.3.333 · Cited by 170 · cited 9× · see citing works

Glutathiolation Regulates Tumor Necrosis Factor-α–Induced Caspase-3 Cleavage and Apoptosis

Pan, S., & Berk, B. C. (2006) · Circulation Research · doi:10.1161/01.res.0000256089.30318.20 · Cited by 169 · see citing works

Reversible Inactivation of α-Ketoglutarate Dehydrogenase in Response to Alterations in the Mitochondrial Glutathione Status

Nulton-Persson, A. C., Starke, D. W., Mieyal, J. J., & Szweda, L. I. (2003) · Biochemistry · doi:10.1021/bi027370f · Cited by 168 · see citing works

Oxidative modification of H-ras: S-thiolation and S-nitrosylation of reactive cysteines

Mallis, R. J., Buss, J. E., & Thomas, J. A. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3550145 · Cited by 168 · see citing works

The mitochondrial permeability transition in neurologic disease

Norenberg, M. D., & RAO, K. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.02.008 · Cited by 167 · see citing works

An increase in S‐glutathionylated proteins in the Alzheimer's disease inferior parietal lobule, a proteomics approach

Newman, S. F., Rukhsana Sultana, A., Marzia Perluigi, A., Coccia, R., Cai, J., Pierce, W. M. J., Klein, J. B., Turner, D. M., & Butterfield, D. A. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21275 · Cited by 166 · see citing works

Glycogen Phosphorylase as a Molecular Target for Type 2 Diabetes Therapy

Oikonomakos, N. G. (2002) · Current Protein and Peptide Science · doi:10.2174/1389203023380422 · Cited by 166 · see citing works

Angiotensin type 1 receptor antagonist losartan, reduces MPTP-induced degeneration of dopaminergic neurons in substantia nigra

Grammatopoulos, T. N., Jones, S. M., Ahmadi, F. A., Hoover, B. R., Snell, L. D., Skoch, J. M., Jhaveri, V. V., Poczobutt, A. M., Weyhenmeyer, J. A., & Zawada, W. M. (2007) · Molecular Neurodegeneration · doi:10.1186/1750-1326-2-1 · Cited by 165 · see citing works

Thioltransferase (Glutaredoxin) Is Detected Within HIV-1 and Can Regulate the Activity of Glutathionylated HIV-1 Protease in Vitro

Davis, D. A., Newcomb, F. M., Starke, D. W., Ott, D. E., Mieyal, J. J., & Yarchoan, R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.41.25935 · Cited by 162 · see citing works

Overexpression of glutaredoxin 2 attenuates apoptosis by preventing cytochrome c release

Enoksson, M., Fernandes, A. P., Prast‐Nielsen, S., Lillig, C. H., Holmgren, A., & Orrenius, S. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.12.067 · Cited by 162 · see citing works

Actin Glutathionylation Increases in Fibroblasts of Patients with Friedreich's Ataxia

Pastore, A., Tozzi, G., Gaeta, L. M., Bertini, E., Serafini, V., Cesare, S. D., Bonetto, V., Casoni, F., Carrozzo, R., Federici, G., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301872200 · Cited by 161 · see citing works

Glutathione Supplementation Potentiates Hypoxic Apoptosis by S-Glutathionylation of p65-NFκB

Qanungo, S., Starke, D. W., Pai, H. V., Mieyal, J. J., & Nieminen, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610934200 · Cited by 160 · see citing works

Thioltransferase (Glutaredoxin) Reactivates the DNA-binding Activity of Oxidation-inactivated Nuclear Factor I

Bandyopadhyay, S., Starke, D. W., Mieyal, J. J., & Gronostajski, R. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.1.392 · Cited by 160 · see citing works

Oxidants and Signaling by Mitogen-Activated Protein Kinases in Lung Epithelium

Mossman, B. T., Lounsbury, K. M., & Reddy, S. P. (2006) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2006-0047sf · Cited by 159 · see citing works

Kinetics and equilibria of S‐nitrosothiol—thiol exchange between glutathione, cysteine, penicillamines and serum albumin

Meyer, D. J., Kramer, H., Özer, N., Coles, B., & KETTERER, B. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00429-3 · Cited by 156 · see citing works

Nitric Oxide Inhibits c-Jun DNA Binding by Specifically TargetedS-Glutathionylation

Klatt, P., Pineda‐Molina, E., & Lamas, S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.22.15857 · Cited by 156 · see citing works

Protein-Tyrosine Phosphatase 1B (PTP1B): A Novel Therapeutic Target for Type 2 Diabetes Mellitus, Obesity and Related States of Insulin Resistance

Goldstein, B. J. (2001) · Current Drug Targets - Immune Endocrine & Metabolic Disorders · doi:10.2174/1568008013341163 · Cited by 154 · see citing works

Reactivity of the Human Thioltransferase (Glutaredoxin) C7S, C25S, C78S, C82S Mutant and NMR Solution Structure of Its Glutathionyl Mixed Disulfide Intermediate Reflect Catalytic Specificity,

Yang, Y., Jao, S., Nanduri, S., Starke, D. W., Mieyal, J. J., & Qin, J. (1998) · Biochemistry · doi:10.1021/bi9806504 · Cited by 153 · see citing works

Caspase-3-Dependent β-Cell Apoptosis in the Initiation of Autoimmune Diabetes Mellitus

Liadis, N., Murakami, K., Eweida, M., Elford, A. R., Sheu, L., Gaisano, H. Y., Hakem, R., Ohashi, P. S., & Woo, M. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.9.3620-3629.2005 · Cited by 152 · see citing works

Metabolic, Metallic, and Mitotic Sources of Oxidative Stress in Alzheimer Disease

Smith, M. A., Nunomura, A., Zhu, X., Takeda, A., & Perry, G. L. (2000) · Antioxidants and Redox Signaling · doi:10.1089/15230860050192198 · Cited by 151 · see citing works

Alterations in the ryanodine receptor calcium release channel correlate with Alzheimer's disease neurofibrillary and β-amyloid pathologies

Kelliher, M., Fastbom, J., Cowburn, R. F., Bonkale, W. L., Ohm, T. G., Ravid, R., Sorrentino, V., & O’Neill, C. (1999) · Neuroscience · doi:10.1016/s0306-4522(99)00042-1 · Cited by 151 · see citing works

1-Methyl-4-Phenylpyridinium Induces Autocrine Excitotoxicity, Protease Activation, and Neuronal Apoptosis

Leist, M., Volbracht, C., Fava, E., et al. (1998) · Molecular Pharmacology · doi:10.1124/mol.54.5.789 · Cited by 151 · see citing works

The phosphatase activity of carbonic anhydrase III is reversibly regulated by glutathiolation.

Cabiscol, E., & Levine, R. L. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.9.4170 · Cited by 148 · see citing works

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 · see citing works

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 · see citing works

NF-κB as an Integrator of Diverse Signaling Pathways: The Heart of Myocardial Signaling?

Jones, W. K., Brown, M. A., Ren, X., He, S., & McGuinness, M. (2003) · Cardiovascular Toxicology · doi:10.1385/ct:3:3:229 · Cited by 145 · see citing works

pH Profiles Indicative of Rate-Limiting Nucleophilic Displacement in Thioltransferase Catalysis

Srinivasan, U., Mieyal, P. A., & Mieyal, J. J. (1997) · Biochemistry · doi:10.1021/bi962017t · Cited by 142 · see citing works

Reduction of glyceraldehyde‐3‐phosphate dehydrogenase activity in Alzheimer's disease and in Huntington's disease fibroblasts

Mazzola, J. L., & Sirover, M. A. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00033.x · Cited by 141 · see citing works

Stable and controllable RNA interference: Investigating the physiological function of glutathionylated actin

Wang, J., Tekle, E., Oubrahim, H., Mieyal, J. J., Stadtman, E. R., & Chock, P. B. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0931345100 · Cited by 141 · see citing works

Activation of apoptosis signal regulating kinase 1 (ASK1) and translocation of death‐associated protein, Daxx, in substantia nigra pars compacta in a mouse model of Parkinson's disease: protection by α‐lipoic acid

Karunakaran, S., Diwakar, L., Saeed, U., Agarwal, V., Ramakrishnan, S., Iyengar, S., & Ravindranath, V. (2007) · The FASEB Journal · doi:10.1096/fj.06-7580com · Cited by 140 · see citing works

Critical role of ASK1 in the 6‐hydroxydopamine‐induced apoptosis in human neuroblastoma SH‐SY5Y cells

Ouyang, M., & Shen, X. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03730.x · Cited by 139 · see citing works

Tachycardia increases NADPH oxidase activity and RyR2 S-glutathionylation in ventricular muscle

Sánchez, G., Pedrozo, Z., DOMENECH, R. J., Hidalgo, C., & Donoso, P. (2005) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2005.08.010 · Cited by 137 · see citing works

Regulation of Mitochondrial NADP+-dependent Isocitrate Dehydrogenase Activity by Glutathionylation

Kil, I. S., & Park, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411306200 · Cited by 137 · see citing works

Reversible Inhibition of α-Ketoglutarate Dehydrogenase by Hydrogen Peroxide: Glutathionylation and Protection of Lipoic Acid

Applegate, M. A. B., Humphries, K. M., & Szweda, L. I. (2007) · Biochemistry · doi:10.1021/bi7017464 · Cited by 137 · see citing works

Oxidant-Induced S-Glutathiolation Inactivates Protein Kinase C-α (PKC-α): A Potential Mechanism of PKC Isozyme Regulation

Ward, N. E., Stewart, J. R., Ioannides, C. G., & O’Brian, C. A. (2000) · Biochemistry · doi:10.1021/bi000781g · Cited by 134 · see citing works

S -Nitrosation versus S -Glutathionylation of Protein Sulfhydryl Groups by S -Nitrosoglutathione

Giustarini, D., Milzani, A., Aldini, G., Carini, M., Rossi, R., & Dalle‐Donne, I. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.930 · Cited by 131 · see citing works

Thioltransferase in human red blood cells: purification and properties

Mieyal, J. J., Starke, D. W., Gravina, S. A., Dothey, C., & Chung, J. S. (1991) · Biochemistry · doi:10.1021/bi00239a002 · Cited by 130 · see citing works

S‐glutathiolation by peroxynitrite of p21ras at cysteine‐118 mediates its direct activation and downstream signaling in endothelial cells

Clavreul, N., Adachi, T. K., Pimental, D. R., Ido, Y., Schöneich, C., & Cohen, R. A. (2006) · The FASEB Journal · doi:10.1096/fj.05-4875fje · Cited by 130 · see citing works

The Glutathione Peroxidase Reaction: Molecular Basis of the Antioxidant Function of Selenium in Mammals

Flohé, L. (1985) · Current topics in cellular regulation · doi:10.1016/b978-0-12-152827-0.50047-5 · Cited by 129 · see citing works

Expression of Glutaredoxin in Human Coronary Arteries

Okuda, M., Inoue, N., Azumi, H., Seno, T., Sumi, Y., Hirata, K., Kawashima, S., Hayashi, Y., Itoh, H., Yodoi, J., et al. (2001) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/hq0901.095550 · Cited by 129 · see citing works

Cellular and Molecular Abnormalities in the Vascular Endothelium of Diabetes Mellitus

King, G. L., Shiba, T., Oliver, F. J., Inoguchi, T., & Bursell, S. (1994) · Annual Review of Medicine · doi:10.1146/annurev.med.45.1.179 · Cited by 129 · see citing works

20 S Proteasome from Saccharomyces cerevisiae Is Responsive to Redox Modifications and IsS-Glutathionylated

Demasi, M., Silva, G. M., & Netto, L. E. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209282200 · Cited by 126 · see citing works

S-Glutathionylation Decreases Mg2+ Inhibition and S-Nitrosylation Enhances Ca2+ Activation of RyR1 Channels

Aracena-Parks, P., Sánchez, G., Donoso, P., Hamilton, S. L., & Hidalgo, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306969200 · Cited by 126 · see citing works

The thioredoxin antioxidant system

Lu, J., & Holmgren, A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.07.036 · Cited by 2,055 · see citing works

Glutathione Homeostasis and Functions: Potential Targets for Medical Interventions

Lushchak, V. I. (2012) · Journal of Amino Acids · doi:10.1155/2012/736837 · Cited by 1,266 · see citing works

The Redox Code

Jones, D. P., & Sies, H. (2015) · Antioxidants &amp; Redox Signaling · doi:10.1089/ars.2015.6247 · Cited by 647 · see citing works

Redox regulation of mitochondrial function

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

Exposure to hydrogen peroxide induces oxidation and activation of AMP-activated protein kinase

Zmijewski, J. W., Banerjee, S., Bae, H., Friggeri, A., Lazarowski, E. R., & Abraham, E. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.143685 · Cited by 441 · see citing works

Causes and consequences of cysteine S-glutathionylation

Grek, C. L., Zhang, J., Manevich, Y., Townsend, D. M., & Tew, K. D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.461368 · Cited by 312 · see citing works

What 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

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

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 · see citing works

Air pollution and circulating biomarkers of oxidative stress

Delfino, R. J., Staimer, N., & Vaziri, N. D. (2011) · Air Quality, Atmosphere &amp; Health · doi:10.1007/s11869-010-0095-2 · Cited by 181 · see citing works

Production of adeno-associated virus vectors for in vitro and in vivo applications

Kimura, T., Ferran, B., Tsukahara, Y., Shang, Q., Desai, S., Fedoce, A., Pimentel, D. R., Luptak, I., Adachi, T., Ido, Y., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-49624-w · Cited by 155 · see citing works

Signaling and stress: The redox landscape in NOS2 biology

Thomas, D. D., Heinecke, J. L., Ridnour, L. A., Cheng, R. Y., Kesarwala, A. H., Switzer, C. H., McVicar, D. W., Roberts, D. D., Glynn, S., Fukuto, J. M., et al. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.002 · Cited by 150 · see citing works

Redox signaling, Nox5 and vascular remodeling in hypertension

Montezano, A. C., Tsiropoulou, S., Dulak-Lis, M., Harvey, A., Camargo, L. D. L., & Touyz, R. M. (2015) · Current Opinion in Nephrology and Hypertension · doi:10.1097/mnh.0000000000000153 · Cited by 93 · see citing works

Cellular Redox Imbalance and Changes of Protein S-glutathionylation Patterns Are Associated with Senescence Induced by Oncogenic H-Ras

Armeni, T., Ercolani, L., Urbanelli, L., Magini, A., Magherini, F., Pugnaloni, A., Piva, F., Modesti, A., Emiliani, C., & Principato, G. (2012) · PLoS ONE · doi:10.1371/journal.pone.0052151 · Cited by 28 · see citing works

A critical evaluation of probes for cysteine sulfenic acid

Pople, J. M. M., & Chalker, J. M. (2020) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2020.07.011 · Cited by 22 · see citing works

Methylmercury alters glutathione homeostasis by inhibiting glutaredoxin 1 and enhancing glutathione biosynthesis in cultured human astrocytoma cells

Robitaille, S., Mailloux, R. J., & Chan, H. M. (2016) · Toxicology Letters · doi:10.1016/j.toxlet.2016.05.013 · Cited by 27 · see citing works

Norbornene probes for the study of cysteine oxidation

Alcock, L. J., Farrell, K. D., Akol, M. T., et al. (2017) · Tetrahedron · doi:10.1016/j.tet.2017.11.011 · Cited by 41 · see citing works

Proteome-Wide Survey Reveals Norbornene Is Complementary to Dimedone and Related Nucleophilic Probes for Cysteine Sulfenic AcidPreprint

Alcock, L., Langini, M., Stühler, K., et al. (2019) · ChemRxiv · doi:10.26434/chemrxiv.8874077

The Utilization of N-Acetylcysteine and 2-Oxothiazolidine-4-Carboxylate by Rat Hepatocytes Is Limited by Their Rate of Uptake and Conversion to Cysteine

Banks, M. F., & Stipanuk, M. H. (1994) · Journal of Nutrition · doi:10.1093/jn/124.3.378 · Cited by 39 · see citing works