Protein glutathionylation in health and disease

Principles of biochemistry

(1978) · Biochemical Education · doi:10.1016/0307-4412(78)90049-3 · Cited by 5,073 · see citing works

Thioredoxin and Glutaredoxin Systems

Holmgren, A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71625-6 · Cited by 1,804 · see citing works

Redefining Oxidative Stress

Jones, D. P. (2006) · Antioxidants & Redox Signaling · doi:10.1089/ars.2006.8.1865 · Cited by 1,726 · see citing works

Glutaredoxin systems

Lillig, C. H., Berndt, C., & Holmgren, A. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.06.003 · Cited by 563 · 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

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

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

EXTRACELLULAR THIOLS AND THIOL/DISULFIDE REDOX IN METABOLISM

Moriarty-Craige, S. E., & Jones, D. P. (2004) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.24.012003.132208 · Cited by 390 · 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

Of urfs and orfs : a primer on how to analyze devised amino acid sequences

Doolittle, R. F. (1986) · University Science Books · Cited by 357 · see citing works

Identification and quantitation of glutathione in hepatic protein mixed disulfides and its relationship to glutathione disulfide

Brigelius, R., Muckel, C., Akerboom, T. P. M., & Sies, H. (1983) · Biochemical Pharmacology · doi:10.1016/0006-2952(83)90014-x · Cited by 348 · 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

Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis

Lind, C., Gerdes, R. G., Hamnell-Pamment, Y., Schuppe‐Koistinen, I., von Löwenhielm, H. B., Holmgren, A., & Cotgreave, I. A. (2002) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(02)00468-x · Cited by 311 · 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

Of URFs and ORFs: A primer on how to analyze derived amino acid sequences

Barker, W. C. (1987) · Genomics · doi:10.1016/0888-7543(87)90013-9 · Cited by 296 · see citing works

Thioredoxin targets in plants: The first 30 years

Montrichard, F., Alkhalfioui, F., Yano, H., Vensel, W. H., Hurkman, W. J., & Buchanan, B. B. (2008) · Journal of Proteomics · doi:10.1016/j.jprot.2008.12.002 · Cited by 278 · see citing works

Redox control of enzyme activities by thiol/disulfide exchange

Gilbert, H. (1984) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(84)07022-1 · Cited by 270 · see citing works

ReviewRegulation of protein function by glutathionylation

Ghezzi, P. (2005) · Free Radical Research · doi:10.1080/10715760500072172 · Cited by 270 · see citing works

Role of nuclear factor κB in cardiovascular health and disease

der Heiden, K. V., Cuhlmann, S., Luong, L. A., Zakkar, M., & Evans, P. C. (2010) · Clinical Science · doi:10.1042/cs20090557 · Cited by 236 · see citing works

S-Thiolation of Individual Human Neutrophil Proteins Including Actin by Stimulation of the Respiratory Burst: Evidence against a Role for Glutathione Disulfide

Chai, Y. C., Ashraf, S. M., Rokutan, K., Johnston, R. B., & Thomas, J. A. (1994) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1994.1167 · Cited by 228 · 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

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

Molecular basis for the redox control of nuclear transport of the structural chromatin protein Hmgb1

Hoppe, G., Talcott, K. E., Bhattacharya, S. K., Crabb, J. W., & Sears, J. E. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2006.07.020 · Cited by 191 · see citing works

Detection and Mapping of Widespread Intermolecular Protein Disulfide Formation during Cardiac Oxidative Stress Using Proteomics with Diagonal Electrophoresis

Brennan, J. P., Wait, R., Begum, S., Bell, J. R., Dunn, M. J., & Eaton, P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403827200 · Cited by 190 · 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

Identification and characterization of oxidized human serum albumin

Kawakami, A., Kubota, K., Yamada, N., Tagami, U., Takehana, K., Sonaka, I., Suzuki, E., & Hirayama, K. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05341.x · Cited by 170 · 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

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

Reversible Oxidative Modification

Figtree, G. A., Liu, C., Bibert, S., Hamilton, E. J., Garcia, A., White, C. N., Chia, K. K. M., Cornelius, F., Geering, K., & Rasmussen, H. (2009) · Circulation Research · doi:10.1161/circresaha.109.199547 · Cited by 164 · 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

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

S-thiolation of glyceraldehyde-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes.

Ravichandran, V., Seres, T., Moriguchi, T., Thomas, J. A., & Johnston, R. B. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31491-6 · 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

Role of cytoplasmic thioltransferase in cellular regulation by thiol-disulphide interchange

Mannervik, B., & Axelsson, K. (1980) · Biochemical Journal · doi:10.1042/bj1900125 · Cited by 153 · 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

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

Oxidoreduction of protein thiols in redox regulation

Ghezzi, P. (2005) · Biochemical Society Transactions · doi:10.1042/bst20051378 · Cited by 146 · see citing works

Glutaredoxins in Thiol/Disulfide Exchange

Lillig, C. H., & Berndt, C. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5007 · Cited by 144 · 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

Glutathionylation of Adenine Nucleotide Translocase Induced by Carbon Monoxide Prevents Mitochondrial Membrane Permeabilization and Apoptosis

Queiroga, C. S. F., Almeida, A. S., Martel, C., Brenner, C., Alves, P. M., & Vieira, H. L. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.065052 · Cited by 133 · see citing works

S-glutathionylation impairs signal transducer and activator of transcription 3 activation and signaling

Xie, Y., Kole, S., Precht, P., Pazin, M. J., & Bernier, M. (2009) · Endocrinology · doi:10.1210/en.2008-1241 · Cited by 126 · see citing works

Glyceraldehyde phosphate dehydrogenase oxidation during cardiac ischemia and reperfusion.

Eaton, P., Wright, N., Hearse, D., & Shattock, M. (2002) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.2002.2108 · Cited by 126 · see citing works

Inhibition of caspase-3 activity and activation by protein glutathionylation

Huang, Z., Pinto, J. T., Deng, H., & Richie, J. P. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.02.026 · Cited by 125 · see citing works

The Utility of N,N-Biotinyl Glutathione Disulfide in the Study of Protein S-Glutathiolation

Brennan, J. P., Miller, J., Fuller, W., Wait, R., Begum, S., Dunn, M. J., & Eaton, P. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m500212-mcp200 · Cited by 125 · see citing works

Elevated protein carbonylation in the brain white matter and gray matter of patients with multiple sclerosis

Bizzozero, O. A., DeJesus, G., Callahan, K., & Pastuszyn, A. (2005) · Journal of Neuroscience Research · doi:10.1002/jnr.20587 · Cited by 124 · see citing works

Deglutathionylation of 2-Cys Peroxiredoxin Is Specifically Catalyzed by Sulfiredoxin

Park, J. W., Mieyal, J. J., Rhee, S. G., & Chock, P. B. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.021394 · Cited by 122 · see citing works

Regulation of LPS induced IL-12 production by IFN-γand IL-4 through intracellular glutathione status in human alveolar macrophages

Dobashi, K., Aihara, M., Araki, T., Shimizu, Y., Utsugi, M., Iizuka, K., Murata, Y., Hamuro, J., Nakazawa, T., & Mori, M. (2001) · Clinical & Experimental Immunology · doi:10.1046/j.1365-2249.2001.01535.x · Cited by 121 · see citing works

Increase in hepatic mixed disulphide and glutathione disulphide levels elicited by paraquat

Brigelius, R., Lenzen, R., & Sies, H. (1982) · Biochemical Pharmacology · doi:10.1016/0006-2952(82)90393-8 · Cited by 118 · see citing works

Studies on the Mechanism of Oxidative Modification of Human Glyceraldehyde-3-phosphate Dehydrogenase by Glutathione: Catalysis by Glutaredoxin

Lind, C., Gerdes, R. G., Schuppe‐Koistinen, I., & Cotgreave, I. A. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8695 · Cited by 116 · see citing works

Quantitative Analysis of Redox-Sensitive Proteome with DIGE and ICAT

Fu, C., Hu, J., Liu, T., Ago, T., Sadoshima, J., & Hong Li, A. (2008) · Journal of Proteome Research · doi:10.1021/pr800233r · Cited by 114 · see citing works

Increased Glutathionyl Hemoglobin in Diabetes Mellitus and Hyperlipidemia Demonstrated by Liquid Chromatography/Electrospray Ionization-Mass Spectrometry

Niwa, T., Naito, C., Mawjood, A. H. M., et al. (2000) · Clinical Chemistry · doi:10.1093/clinchem/46.1.82 · Cited by 107 · see citing works

Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia

Ho, Y.-S., Xiong, Y., Ho, D. S., Gao, J., Chua, B. H. L., Pai, H. V., & Mieyal, J. J. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.07.025 · Cited by 101 · see citing works

The Depletion of Nuclear Glutathione Impairs Cell Proliferation in 3t3 Fibroblasts

Marković, J., Mora, N. J., Broseta, A., Gimeno, A., de-la-Concepción, N., Viña, J., & Pallardó, F. V. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006413 · Cited by 97 · see citing works

Protein glutathionylation: coupling and uncoupling of glutathione to protein thiol groups in lymphocytes under oxidative stress and HIV infection

Ghezzi, P., Romines, B., Fratelli, M., Eberini, I., Gianazza, E., Casagrande, S., Laragione, T., Mengozzi, M., Herzenberg, L. A., & Herzenberg, L. A. (2002) · Molecular Immunology · doi:10.1016/s0161-5890(01)00114-6 · Cited by 97 · see citing works

NOV-002, a Glutathione Disulfide Mimetic, as a Modulator of Cellular Redox Balance

Townsend, D. M., He, L., Hutchens, S., Garrett, T. E., Pazoles, C. J., & Tew, K. D. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-5957 · Cited by 94 · see citing works

Cellular mixed disulphides between thiols and proteins, and their possible implication for radiation protection

Modig, H. G. (1968) · Biochemical Pharmacology · doi:10.1016/0006-2952(68)90321-3 · Cited by 91 · see citing works

The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm

Debarbieux, L., & Beckwith, J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.18.10751 · Cited by 86 · see citing works

Enhanced protein glutathiolation and oxidative stress in cigarette smokers

Muscat, J. E., Kleinman, W. A., Colosimo, S., et al. (2003) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2003.11.018 · Cited by 82 · see citing works

Glutaredoxin 2 knockout increases sensitivity to oxidative stress in mouse lens epithelial cells

Wu, H., Lin, L.-R., Giblin, F. J., Ho, Y.-S., & Lou, M. F. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.09.011 · Cited by 81 · see citing works

Sulfiredoxin: a potential therapeutic agent?

Findlay, V. J., Tapiero, H., & Townsend, D. M. (2005) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2005.07.003 · Cited by 80 · see citing works

Thiol groups in proteins as endogenous reductants to determine glutathione-protein mixed disulphides in biological systems

Rossi, R. (1995) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(94)00133-i · Cited by 80 · see citing works

Attenuation of doxorubicin-induced cardiac injury by mitochondrial glutaredoxin 2

Diotte, N. M., Xiong, Y., Gao, J., Chua, B. H. L., & Ho, Y.-S. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.10.014 · Cited by 78 · see citing works

Determination of site-specificity of S-glutathionylated cellular proteins

Hamnell-Pamment, Y., Lind, C., Palmberg, C., Bergman, T., & Cotgreave, I. A. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.04.130 · Cited by 73 · see citing works

GSH depletion, protein S-glutathionylation and mitochondrial transmembrane potential hyperpolarization are early events in initiation of cell death induced by a mixture of isothiazolinones in HL60 cells

Stefano, A. D., Frosali, S., Leonini, A., Ettorre, A., Priora, R., Simplicio, F. C. D., & Simplicio, P. D. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2005.12.012 · Cited by 73 · see citing works

Oxidative stress induces S-thiolation of specific proteins in cultured gastric mucosal cells

Rokutan, K., Johnston, R. B., & Kawai, K. (1994) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.1994.266.2.g247 · Cited by 72 · see citing works

Increased glutathionylated hemoglobin (HbSSG) in type 2 diabetes subjects with microangiopathy

Rangasamy, S., Balasubramanyam, M., Sudarslal, S., Rema, M., Mohan, V., & Balaram, P. (2005) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2005.06.009 · Cited by 71 · see citing works

Microheterogeneity of transthyretin in serum and ascitic fluid of ovarian cancer patients

Gericke, B., Raila, J., Sehouli, J., Haebel, S., Könsgen, D., Mustea, A., & Schweigert�, F. J. (2005) · BMC Cancer · doi:10.1186/1471-2407-5-133 · Cited by 68 · see citing works

Potent inactivation of representative members of each PKC isozyme subfamily and PKD via S-thiolation by the tumor-promotion/progression antagonist glutathione but not by its precursor cysteine.

Chu, F., Ward, N., & O'Brian, C. (2001) · Carcinogenesis · doi:10.1093/carcin/22.8.1221 · Cited by 68 · see citing works

Ablation of Glutaredoxin-1 Attenuates Lipopolysaccharide-Induced Lung Inflammation and Alveolar Macrophage Activation

Aesif, S. W., Anathy, V., Kuipers, I., Guala, A. S., Reiss, J. N., Ho, Y., & Janssen-Heininger, Y. M. W. (2010) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2009-0136oc · Cited by 67 · see citing works

The Glutaredoxin/Glutathione System Modulates NF-κB Activity by Glutathionylation of p65 in Cinnamaldehyde-Treated Endothelial Cells

Liao, B., Hsieh, C., Lin, Y.-C., & Wung, B. (2010) · Toxicological Sciences · doi:10.1093/toxsci/kfq098 · Cited by 67 · see citing works

In situ detection of S-glutathionylated proteins following glutaredoxin-1 catalyzed cysteine derivatization

Reynaert, N. L., Ckless, K., Guala, A. S., Wouters, E. F. �., van der Vliet, A., & Janssen-Heininger, Y. M. W. (2006) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2006.01.006 · Cited by 66 · see citing works

S-Glutathionylation Regulates Inflammatory Activities of S100A9

Lim, S. Y., Raftery, M. J., Goyette, J., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.075242 · Cited by 66 · see citing works

Protein s-glutathionylation in retinal pigment epithelium converts heat shock protein 70 to an active chaperone

Hoppe, G., Chai, Y.-C., Crabb, J. W., & Sears, J. E. (2004) · Experimental Eye Research · doi:10.1016/j.exer.2004.02.001 · Cited by 61 · see citing works

Phagocytosis and stimulation of the respiratory burst by phorbol diester initiate S-thiolation of specific proteins in macrophages

Rokutan, K., Thomas, J. A., & Johnston, R. B. (1991) · The Journal of Immunology · doi:10.4049/jimmunol.147.1.260 · Cited by 59 · see citing works

On the Functional Interchangeability, Oxidant versus Reductant, of Members of the Thioredoxin Superfamily

Debarbieux, L., & Beckwith, J. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.3.723-727.2000 · Cited by 56 · see citing works

Activation of the glutaredoxin-1 gene by nuclear factor κB enhances signaling

Aesif, S. W., Kuipers, I., van der Velden, J. L. J., Tully, J. E., Guala, A. S., Anathy, V., Sheely, J. I., Reynaert, N. L., Wouters, E. F. �., van der Vliet, A., et al. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.06.025 · Cited by 56 · see citing works

Posttranslational modification of the glycosylation inhibiting factor (GIF) gene product generates bioactive GIF

Watarai, H., Nozawa, R., Tokunaga, A., Yuyama, N., Tomas, M., Hinohara, A., Ishizaka, K., & Ishii, Y. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.230445397 · Cited by 56 · see citing works

Glutathionylation pathways in drug response

Ghezzi, P., & Simplicio, P. D. (2007) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2007.04.006 · Cited by 54 · see citing works

Quantitation and characterization of glutathionyl haemoglobin as an oxidative stress marker in chronic renal failure by mass spectrometry

Mandal, A. K., Woodi, M., Sood, V., Krishnaswamy, P. R., Rao, A., Ballal, S. H., & Balaram, P. (2007) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2007.05.006 · Cited by 54 · see citing works

Hormones, glutathione status and protein S-thiolation

Sies, H., Brigelius, R., & Gräf, P. (1987) · Advances in Enzyme Regulation · doi:10.1016/0065-2571(87)90013-6 · Cited by 52 · see citing works

Susceptibility of β1 Na+-K+ Pump Subunit to Glutathionylation and Oxidative Inhibition Depends on Conformational State of Pump

Liu, C., Garcia, A., Mahmmoud, Y. A., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.340893 · Cited by 49 · see citing works

Post-translational Modification of Transthyretin in Plasma

Terazaki, H., Ando, Y., Suhr, O. B., et al. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9097 · Cited by 45 · see citing works

Redox regulation of cyclophilin A by glutathionylation

Ghezzi, P., Casagrande, S., Massignan, T., et al. (2005) · PROTEOMICS · doi:10.1002/pmic.200500177 · Cited by 45 · see citing works

N‐Acetylcysteine infusion does not affect glucose disposal during prolonged moderate‐intensity exercise in humans

Merry, T. L., Wadley, G. D., Stathis, C. G., GARNHAM, A. P., Rattigan, S., Hargreaves, M., & McConell, G. K. (2010) · The Journal of Physiology · doi:10.1113/jphysiol.2009.184333 · Cited by 43 · see citing works

Characterization and stability of transthyretin isoforms in cerebrospinal fluid examined by immunoprecipitation and high-resolution mass spectrometry of intact protein

Poulsen, K., Bahl, J. M. C., Tanassi, J. T., et al. (2012) · Methods · doi:10.1016/j.ymeth.2011.12.009 · Cited by 42 · see citing works

Glutaredoxin 1 Protects Dopaminergic Cells by Increased Protein Glutathionylation in Experimental Parkinson's Disease

Rodríguez‐Rocha, H., Garcia, A. G., Zavala-Flores, L. M., Li, S., Madayiputhiya, N., & Franco, R. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4474 · Cited by 40 · see citing works

Segment-specific overexpression of redoxins after renal ischemia and reperfusion: protective roles of glutaredoxin 2, peroxiredoxin 3, and peroxiredoxin 6

Godoy, J. R., Oesteritz, S., Hanschmann, E.-M., Ockenga, W., Ackermann, W., & Lillig, C. H. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.04.036 · Cited by 40 · see citing works

Serum Levels of S-Glutathionylated Proteins as a Risk-Marker for Arteriosclerosis Obliterans

Nonaka, K., Kume, N., Urata, Y., Seto, S., Kohno, T., Honda, S., Ikeda, S., Muroya, T., Ikeda, Y., Ihara, Y., et al. (2006) · Circulation Journal · doi:10.1253/circj.71.100 · Cited by 37 · see citing works

Glutathionyl hemoglobin in uremic patients undergoing hemodialysis and continuous ambulatory peritoneal dialysis

Takayama, F., Tsutsui, S., Horie, M., et al. (2001) · Kidney International · doi:10.1046/j.1523-1755.2001.59780155.x · Cited by 37 · see citing works

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Al‐Abed, Y., VanPatten, S., Li, H., et al. (2001) · Molecular Medicine · doi:10.1007/bf03401868 · Cited by 36 · see citing works

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Liang, J. N., & Pelletier, M. R. (1988) · Experimental Eye Research · doi:10.1016/0014-4835(88)90020-6 · Cited by 36 · see citing works

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Adluri, R. S., Thirunavukkarasu, M., Zhan, L., Dunna, N. R., Akita, Y., Selvaraju, V., Otani, H., Sánchez, J. A., Ho, Y.-S., & Maulik, N. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034790 · Cited by 36 · see citing works

A novel thiol oxidation‐based mechanism for adriamycin‐induced cell injury in human macrophages

Asmis, R., Wang, Y., Xu, L., Kisgati, M., Begley, J. G., & Mieyal, J. J. (2005) · The FASEB Journal · doi:10.1096/fj.04-2991fje · Cited by 36 · see citing works

Attenuated cardiovascular hypertrophy and oxidant generation in response to angiotensin II infusion in glutaredoxin-1 knockout mice

Bachschmid, M. M., Xu, S., Maitland, K. A., Ho, Y., Cohen, R. A., & Matsui, R. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.07.005 · Cited by 34 · see citing works

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Cabras, T., Manconi, B., Iavarone, F., et al. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.10.006 · Cited by 32 · see citing works

Protein glutathionylation increases in the liver of patients with non‐alcoholic fatty liver disease

Piemonte, F., Petrini, S., Gaeta, L. M., Tozzi, G., Bertini, E., Vito, R. D., Boldrini, R., Marcellini, M., Ciacco, E., & Nobili, V. (2007) · Journal of Gastroenterology and Hepatology · doi:10.1111/j.1440-1746.2007.05070.x · Cited by 32 · see citing works

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Lin, Y.-C., Huang, G.-D., Hsieh, C., & Wung, B. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.028 · Cited by 29 · see citing works

Glutathionyl hemoglobin in uremic patients undergoing hemodialysis and continuous ambulatory peritoneal dialysis

Takayama, F., Tsutsui, S., Horie, M., et al. (2001) · Kidney International · doi:10.1046/j.1523-1755.2001.07834.x · Cited by 28 · see citing works

Determination of glutathionyl hemoglobin in hemodialysis patients using electrospray ionization liquid chromatography–mass spectrometry

Naito, C., Kajita, M., & Niwa, T. (1999) · Journal of Chromatography B Biomedical Sciences and Applications · doi:10.1016/s0378-4347(99)00139-5 · Cited by 27 · see citing works

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Pastore, A., Ciampalini, P., Tozzi, G., et al. (2011) · Pediatric Diabetes · doi:10.1111/j.1399-5448.2011.00806.x · Cited by 27 · see citing works

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Primavera, A., Fustinoni, S., Biroccio, A., et al. (2008) · Cancer Epidemiology Biomarkers & Prevention · doi:10.1158/1055-9965.epi-08-0443 · Cited by 27 · see citing works

Genetic variation in mouse beta globin cysteine content modifies glutathione metabolism: implications for the use of mouse models.

Hempe, J. M., Ory‐Ascani, J., & Hsia, D. S. (2007) · PubMed · Cited by 25 · see citing works

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Yang, X., Greenhaw, J. J., Ali, A. A., Shi, Q., Roberts, D. W., Hinson, J., Muskhelishvili, L., Beger, R. D., Pence, L. M., Ando, Y., et al. (2011) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.111.187948 · Cited by 24 · see citing works

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Kuipers, I., Bracke, K. R., Brusselle, G., Aesif, S. W., Krijgsman, R., Arts, I. C. W., Wouters, E. F. �., & Reynaert, N. L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0038984 · Cited by 23 · see citing works

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Kim, Y., Song, Y. B., Kim, T.-Y., et al. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.07.006 · Cited by 23 · see citing works

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Frey, S. K., Spranger, J., Henze, A., Pfeiffer, A. F. H., Schweigert�, F. J., & Raila, J. (2009) · Metabolism · doi:10.1016/j.metabol.2009.05.003 · Cited by 23 · see citing works

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Burgoyne, J. R., & Eaton, P. (2011) · Biochemical Society Transactions · doi:10.1042/bst0391260 · Cited by 23 · see citing works

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Hoffman, S. M., Tully, J. E., Lahue, K. G., Anathy, V., Nolin, J. D., Guala, A. S., van der Velden, J. L. J., Ho, Y.-S., Aliyeva, M., Daphtary, N., et al. (2012) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00167.2012 · Cited by 22 · see citing works

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Cerami, A. (2012) · Journal of Internal Medicine · doi:10.1111/j.1365-2796.2012.02514.x · Cited by 18 · see citing works

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Grek, C. L., Townsend, D. M., Uys, J. D. K., Manevich, Y., Coker, W. J., Pazoles, C. J., & Tew, K. D. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-4088 · Cited by 16 · see citing works

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Malvezzi, A., Higa, P. M., do Amaral, A. T., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039408 · Cited by 16 · see citing works

Alteration of Transthyretin Microheterogeneity in Serum of Multiple Trauma Patients

Gericke, B., Raila, J., Deja, M., Rohn, S., Donaubauer, B., Nagl, B., Haebel, S., Schweigert�, F. J., & Kaisers, U. (2007) · Biomarker Insights · doi:10.1177/117727190700200014 · Cited by 15 · see citing works

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Gericke, B., Raila, J., Deja, M., et al. (2007) · PubMed · doi:10.14279/depositonce-7843 · Cited by 14 · see citing works

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Henze, A., Raila, J., Scholze, A., et al. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5125 · Cited by 10 · see citing works

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Shet, A. S., Pinto, S. M., Mitra, G., et al. (2011) · Acta Haematologica · doi:10.1159/000330945 · Cited by 10 · see citing works

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Nakamoto, M., Hirose, M., Kawakatsu, M., et al. (2012) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2012.06.017 · Cited by 2 · see citing works

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Jomova, K., Raptova, R., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03562-9 · Cited by 2,638 · see citing works

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Wongtrakul, J., Thongtan, T., Kumrapich, B., Saisawang, C., & Ketterman, A. J. (2021) · Heliyon · doi:10.1016/j.heliyon.2021.e08172 · Cited by 52 · see citing works

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Jardim, F. R., de Almeida, F. J. S., Luckachaki, M. D., & de Oliveira, M. R. (2020) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b1900614 · Cited by 26 · see citing works

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Mustafa, N. H., Kelesbayev, D., & Alibekova, Z. D. (2018) · The Journal of Economic Research & Business Administration · doi:10.26577/be-2018-2-2141

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Hawkins, D. (2017)

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Cross, R. (2018) · C&EN Global Enterprise · doi:10.1021/cen-09635-buscon15

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Sari, D. (2023) · Jurnal Komplikasi Anestesi · doi:10.22146/jka.v5i1.7322

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Dib, A., Puig, L. B., Salvadori, D., et al. (1988) · Arquivos Brasileiros de Cardiologia