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

Calculation of protein extinction coefficients from amino acid sequence data.

Gill, S., & von Hippel, P. H. (1989) · Analytical Biochemistry · doi:10.1016/0003-2697(89)90602-7 · Cited by 5,382 · see citing works

CLUSTAL: a package for performing multiple sequence alignment on a microcomputer

Higgins, D. G., & Sharp, P. M. (1988) · Gene · doi:10.1016/0378-1119(88)90330-7 · Cited by 3,394 · see citing works

Physiological functions of thioredoxin and thioredoxin reductase

Arnér, E. S. J., & Holmgren, A. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01701.x · Cited by 2,535 · see citing works

THIOREDOXIN

Holmgren, A. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.001321 · Cited by 1,955 · 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

Thioredoxin —a fold for all reasons

Martin, J. L. (1995) · Structure · doi:10.1016/s0969-2126(01)00154-x · Cited by 828 · see citing works

Rat liver thioredoxin and thioredoxin reductase: purification and characterization

Luthman, M., & Holmgren, A. (1982) · Biochemistry · doi:10.1021/bi00269a003 · Cited by 603 · 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

Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity.

Wells, W. W., Xu, D. P., Yang, Y., & Rocque, P. A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55401-6 · Cited by 450 · see citing works

Essential Role of Selenium in the Catalytic Activities of Mammalian Thioredoxin Reductase Revealed by Characterization of Recombinant Enzymes with Selenocysteine Mutations

Zhong, L., & Holmgren, A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000690200 · Cited by 430 · see citing works

Redox Potentials of Glutaredoxins and Other Thiol-Disulfide Oxidoreductases of the Thioredoxin Superfamily Determined by Direct Protein-Protein Redox Equilibria

Åslund, F., Berndt, K. D., & Holmgren, A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.49.30780 · Cited by 418 · 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

Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer

Weichsel, A., Gasdaska, J. R., Powis, G., & Montfort, W. R. (1996) · Structure · doi:10.1016/s0969-2126(96)00079-2 · Cited by 374 · see citing works

Glutathionylation of human thioredoxin: A possible crosstalk between the glutathione and thioredoxin systems

Casagrande, S., Bonetto, V., Fratelli, M., Gianazza, E., Eberini, I., Massignan, T., Salmona, M., Chang, G., Holmgren, A., & Ghezzi, P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.152168599 · Cited by 349 · see citing works

Rapid and Specific Efflux of Reduced Glutathione during Apoptosis Induced by Anti-Fas/APO-1 Antibody

van den Dobbelsteen, D. J., Nobel, S., Schlegel, J., Cotgreave, I. A., Orrenius, S., & Slater, A. F. G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.26.15420 · Cited by 343 · 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

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

Preparation and assay of mammalian thioredoxin and thioredoxin reductase

Arnér, E. S. J., Zhong, L., & Holmgren, A. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)00129-9 · Cited by 323 · see citing works

Selenoprotein oxidoreductase with specificity for thioredoxin and glutathione systems

Sun, Q.-A., Kirnarsky, L., Sherman, S., & Gladyshev, V. N. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051454398 · Cited by 312 · see citing works

Why is DsbA such an oxidizing disulfide catalyst?

Grauschopf, U., Winther, J. R., Korber, P., Zander, T., Dallinger, P., & Bardwell, J. C. A. (1995) · Cell · doi:10.1016/0092-8674(95)90210-4 · 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

Grx5 Glutaredoxin Plays a Central Role in Protection against Protein Oxidative Damage in Saccharomyces cerevisiae

Rodríguez‐Manzaneque, M. T., Ros, J., Cabiscol, E., Albert Sorribas, B., & Herrero, E. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.12.8180 · Cited by 302 · see citing works

[29] Glutaredoxin

Holmgren, A., & Åslund, F. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)52031-7 · Cited by 292 · 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

Protein disulfide-isomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity.

Lundström, J., & Holmgren, A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38819-2 · Cited by 272 · see citing works

Rat and Calf Thioredoxin Reductase Are Homologous to Glutathione Reductase with a Carboxyl-terminal Elongation Containing a Conserved Catalytically Active Penultimate Selenocysteine Residue

Zhong, L., Arnér, E. S. J., Lundström-Ljung, J., Åslund, F., & Holmgren, A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.15.8581 · Cited by 263 · see citing works

Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin

Krause, G., Lundström, J., Barea, J. L., Cuesta, C., & Holmgren, A. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)92848-6 · Cited by 259 · see citing works

The YeastSaccharomyces cerevisiaeContains Two Glutaredoxin Genes That Are Required for Protection against Reactive Oxygen Species

Luikenhuis, S., Perrone, G. G., Dawes, I. W., & Grant, C. M. (1998) · Molecular Biology of the Cell · doi:10.1091/mbc.9.5.1081 · Cited by 237 · see citing works

Glutathione-dependent synthesis of deoxyribonucleotides. Characterization of the enzymatic mechanism of Escherichia coli glutaredoxin.

Holmgren, A. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50814-0 · Cited by 235 · 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

Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14.fwdarw.S) and its mixed disulfide with glutathione

Bushweller, J. H., Åslund, F., Kurt Wüthrich, A., & Holmgren, A. (1992) · Biochemistry · doi:10.1021/bi00153a023 · Cited by 226 · see citing works

Identification and Functional Characterization of a Novel Mitochondrial Thioredoxin System in Saccharomyces cerevisiae

Pedrajas, J. R., Kosmidou, E., Miranda‐Vizuete, A., Gustafsson, J.-Α., Wright, A. P. H., & Spyrou, G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.10.6366 · Cited by 226 · see citing works

Two additional glutaredoxins exist in Escherichia coli: glutaredoxin 3 is a hydrogen donor for ribonucleotide reductase in a thioredoxin/glutaredoxin 1 double mutant.

Åslund, F., Ehn, B.-M., Miranda‐Vizuete, A., Pueyo, C., & Holmgren, A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.21.9813 · Cited by 192 · see citing works

Human Mitochondrial Thioredoxin

Damdimopoulos, A. E., Miranda-Vizuete, A., Pelto-Huikko, M., Gustafsson, J.-Å., & Spyrou, G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203036200 · Cited by 192 · see citing works

Human mitochondrial thioredoxin reductase

Miranda‐Vizuete, A., Damdimopoulos, A. E., Pedrajas, J. R., Gustafsson, J.-Α., & Spyrou, G. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00286.x · Cited by 178 · see citing works

Characterization of Escherichia coli thioredoxin variants mimicking the active‐sites of other thiol/disulfide oxidoreductases

Mössner, E., Huber‐Wunderlich, M., & Glockshuber, R. (1998) · Protein Science · doi:10.1002/pro.5560070519 · Cited by 174 · see citing works

The disulfide redox system of Schistosoma mansoni and the importance of a multifunctional enzyme, thioredoxin glutathione reductase

Alger, H. M., & Williams, D. L. (2002) · Molecular and Biochemical Parasitology · doi:10.1016/s0166-6851(02)00031-2 · Cited by 172 · 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

The Mitochondrial Thioredoxin System

Miranda‐Vizuete, A., Damdimopoulos, A. E., & Spyrou, G. (2000) · Antioxidants and Redox Signaling · doi:10.1089/ars.2000.2.4-801 · Cited by 155 · 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

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

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

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

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 · see citing works

Glutaredoxin from calf thymus. Purification to homogeneity.

Luthman, M., & Holmgren, A. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34484-3 · Cited by 134 · see citing works

Roles of long chain fatty acids and carnitine in mitochondrial membrane permeability transition11Abbreviations: CsA, cyclosporin A; Cyt. c, cytochrome c; FBS, fetal bovine serum; Pal-CoA, palmitoyl-CoA; Pi, inorganic phosphate; LCFA, long chain fatty acid; MPT, membrane permeability transition; PLA2, phospholipase A2; RCR, respiratory control ratio; and T3, 3,3′,5-triiodothyronine.

Furuno, T., Kanno, T., Arita, K., Asami, M., Utsumi, T., Doi, Y., Inoue, M., & Utsumi, K. (2001) · Biochemical Pharmacology · doi:10.1016/s0006-2952(01)00745-6 · 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

Distribution of Metabolites Between the Cytosolic and Mitochondrial Compartments of Hepatocytes Isolated from Fed Rats

SIESS, E. A., Brocks, D. G., & WIELAND, O. H. (1978) · Hoppe-Seyler´s Zeitschrift für physiologische Chemie · doi:10.1515/bchm2.1978.359.2.785 · Cited by 121 · see citing works

Identification and characterization of the functional amino acids at the active center of pig liver thioltransferase by site-directed mutagenesis

Yang, Y. F., & Wells, W. W. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98964-7 · Cited by 108 · see citing works

Glutathione-dependent hydrogen donor system for calf thymus ribonucleoside-diphosphate reductase.

Luthman, M., Eriksson, S., Holmgren, A., & Thelander, L. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.5.2158 · Cited by 106 · see citing works

Dopamine Biosynthesis Is Regulated byS-Glutathionylation

Borges, C. R., Geddes, T. J., Watson, J. T., & Kuhn, D. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209042200 · Cited by 102 · see citing works

Cloning, Overexpression, and Characterization of Glutaredoxin 2, An Atypical Glutaredoxin from Escherichia coli

Vlamis‐Gardikas, A., Åslund, F., Spyrou, G., Bergman, T., & Holmgren, A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.17.11236 · Cited by 100 · 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

Structure, dynamics and electrostatics of the active site of glutaredoxin 3 from Escherichia coli: comparison with functionally related proteins

Foloppe, N., Sagemark, J., Nordstrand, K., Berndt, K. D., & Nilsson, L. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4767 · Cited by 93 · see citing works

Thiotransferase in human red blood cells: kinetics and equilibrium

Mieyal, J. J., Starke, D. W., Gravina, S. A., & Hocevar, B. A. (1991) · Biochemistry · doi:10.1021/bi00100a023 · Cited by 93 · see citing works

The NMR solution structure of human glutaredoxin in the fully reduced form

Sun, C. C., Berardi, M. J., & Bushweller, J. H. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1913 · Cited by 93 · see citing works

Plasmodium falciparum Possesses a Classical Glutaredoxin and a Second, Glutaredoxin-like Protein with a PICOT Homology Domain

Rahlfs, S., Fischer, M., & Becker, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105524200 · Cited by 91 · see citing works

Purification and properties of thioltransferase.

Gan, Z., & Wells, W. W. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36043-x · Cited by 84 · see citing works

Proton Sharing between Cysteine Thiols in Escherichia coli Thioredoxin: Implications for the Mechanism of Protein Disulfide Reduction

Jeng, M.-F., Holmgren, A., & Dyson, H. J. (1995) · Biochemistry · doi:10.1021/bi00032a001 · Cited by 81 · see citing works

Purification from Placenta, Amino Acid Sequence, Structure Comparisons and cDNA Cloning of Human Glutaredoxin

Padilla, C. A., Martı́nez-Galisteo, E., Bárcena, J. A., Spyrou, G., & Holmgren, A. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.tb20356.x · Cited by 81 · see citing works

Mitochondrial thioredoxin reductase in bovine adrenal cortex

Watabe, S., Makino, Y., Ogawa, K., Hiroi, T., Yamamoto, Y., & TAKAHASHI, S. Y. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00578.x · Cited by 80 · see citing works

[17] S-Glutathionylation of glyceraldehyde-3-phosphate dehydrogenase: Role of thiol oxidation and catalysis by glutaredoxin

Cotgreave, I. A., Gerdes, R. G., Schuppe‐Koistinen, I., & Lind, C. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)48636-3 · Cited by 80 · see citing works

Glutaredoxin is essential for maintenance of brain mitochondrial complex I: studies with MPTP

Kenchappa, R. S., & Ravindranath, V. (2003) · The FASEB Journal · doi:10.1096/fj.02-0771fje · Cited by 80 · see citing works

Alternative mRNAs Arising from Trans-splicing Code for Mitochondrial and Cytosolic Variants of Echinococcus granulosus Thioredoxin Glutathione Reductase

Agorio, A., Chalar, C., Cardozo, S., & Salinas, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209266200 · Cited by 75 · see citing works

Direct NMR observation of the Cys‐14 thiol proton of reduced Escherichia coli glutaredoxin‐3 supports the presence of an active site thiol‐thiolate hydrogen bond

Nordstrand, K., Åslund, F., Meunier, S., Holmgren, A., Otting, G., & Berndt, K. D. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00401-9 · Cited by 69 · see citing works

The Catalytic Mechanism of the Glutathione-Dependent Dehydroascorbate Reductase Activity of Thioltransferase (Glutaredoxin),

Washburn, M. P., & Wells, W. W. (1998) · Biochemistry · doi:10.1021/bi980480v · Cited by 68 · see citing works

Influence of the pKa value of the buried, active‐site cysteine on the redox properties of thioredoxin‐like oxidoreductases

Mössner, E., Iwaï, H., & Glockshuber, R. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01738-5 · Cited by 59 · see citing works

Crystal structure of thioltransferase at 2.2 Å resolution

Katti, S. K., Robbins, A. H., Yang, Y., & Wells, W. W. (1995) · Protein Science · doi:10.1002/pro.5560041005 · Cited by 58 · see citing works

A putative glutathione-binding site in T4 glutaredoxin investigated by site-directed mutagenesis

Nikkola, M., Gleason, F. K., Saarinen, M., Joelson, T., Björnberg, O., & Eklund, H. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98522-4 · Cited by 57 · see citing works

Differential expression of glutaredoxin and thioredoxin during monocytic differentiation

Takashima, Y., Hirota, K., Nakamura, H., Nakamura, T., Akiyama, K., Cheng, F. S., Maeda, M., & Yodoi, J. (1999) · Immunology Letters · doi:10.1016/s0165-2478(99)00087-5 · Cited by 55 · see citing works

Catalytic mechanism of thioltransferase

Yang, Y., & Wells, W. W. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98965-9 · Cited by 50 · see citing works

Thioredoxin reductase-mediated hydrogen transfer from Escherichia coli thioredoxin-(SH)2 to phage T4 thioredoxin-S2.

Berglund, O., & Holmgren, A. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41557-3 · Cited by 36 · see citing works

High‐level expression of fully active human glutaredoxin (thioltransferase) in E. coli and characterization of Cys7 to Ser mutant protein

Padilla, C. A., Spyrou, G., & Holragren, A. (1996) · FEBS Letters · doi:10.1016/0014-5793(95)01413-6 · Cited by 35 · see citing works

Reactivity of glutaredoxins 1, 2 and 3 from Escherichia coli and protein disulfide isomerase towards glutathionyl‐mixed disulfides in ribonuclease A

Lundström-Ljung, J., Vlamis‐Gardikas, A., Åslund, F., & Holmgren, A. (1999) · FEBS Letters · doi:10.1016/s0014-5793(98)01698-6 · Cited by 32 · see citing works

Human lens thioltransferase: cloning, purification, and function.

Qiao, F., Xing, K., Liu, A., Ehlers, N., Raghavachari, N., & Lou, M. F. (2001) · PubMed · Cited by 31 · see citing works

[16] c-Jun regulation by s-glutathionylation

Klatt, P., & Lamas, S. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)48635-1 · Cited by 27 · see citing works

Characterization of a nucleotide-peptide from rat liver

Ondarza, R. N. (1965) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(65)90393-4 · Cited by 24 · see citing works

The structure of a reduced mutant T4 glutaredoxin

Ingelman, M., Nordlund, P., & Eklund, H. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00806-k · Cited by 16 · see citing works

Complete 1H, 13C, and 15N NMR resonance assignments and secondary structure of human glutaredoxin in the fully reduced form

Sun, C. C., Bushweller, J. H., & Holmgren, A. (1997) · Protein Science · doi:10.1002/pro.5560060214 · Cited by 13 · see citing works

Role of Oxidative Modifications in Atherosclerosis

Stocker, R., & Keaney, J. F. (2004) · Physiological Reviews · doi:10.1152/physrev.00047.2003 · Cited by 2,611 · 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

Oxidant and antioxidant signalling in plants: a re‐evaluation of the concept of oxidative stress in a physiological context

Foyer, C. H., & Noctor, G. (2005) · Plant Cell & Environment · doi:10.1111/j.1365-3040.2005.01327.x · Cited by 1,891 · see citing works

Mitochondrial metabolism of reactive oxygen species

Andreyev, A. Y., Kushnareva, Y. E., & Starkov, A. A. (2005) · Biochemistry (Moscow) · doi:10.1007/s10541-005-0102-7 · Cited by 1,336 · see citing works

Glutathione Peroxidase-1 in Health and Disease: From Molecular Mechanisms to Therapeutic Opportunities

Lubos, E., Loscalzo, J., & Handy, D. E. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3586 · Cited by 1,280 · see citing works

Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes

Deponte, M. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.09.018 · Cited by 1,104 · 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

Thioredoxins, Glutaredoxins, and Peroxiredoxins—Molecular Mechanisms and Health Significance: from Cofactors to Antioxidants to Redox Signaling

Hanschmann, E., Godoy, J. R., Berndt, C., Hudemann, C., & Lillig, C. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4599 · Cited by 649 · see citing works

Focus on mammalian thioredoxin reductases — Important selenoproteins with versatile functions

Arnér, E. S. J. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.01.014 · Cited by 675 · see citing works

Redox regulation of mitochondrial function

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

Thioredoxin reductase: A target for gold compounds acting as potential anticancer drugs

Bindoli, A., Rigobello, M. P., Scutari, G., Gabbiani, C., Casini, A., & Luigi Messori, A. (2009) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2009.02.026 · Cited by 594 · see citing works

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 · see citing works

Glutathione and mitochondria

Ribas, V., García‐Ruiz, C., & Fernández-Checa, J. C. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00151 · Cited by 572 · 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

Molecular Mechanisms and Clinical Implications of Reversible Protein <i>S</i> -Glutathionylation

Mieyal, J. J., Gallogly, M. M., Qanungo, S., Sabens, E. A., & Shelton, M. D. (2008) · Antioxidants &amp; Redox Signaling · doi:10.1089/ars.2008.2089 · Cited by 523 · 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

Thiol redox control via thioredoxin and glutaredoxin systems

Holmgren, A., Johansson, C., Berndt, C., Lönn, M. E., Hudemann, C., & Lillig, C. H. (2005) · Biochemical Society Transactions · doi:10.1042/bst20051375 · Cited by 463 · see citing works

Thioredoxin and Glutaredoxin Systems in Plants: Molecular Mechanisms, Crosstalks, and Functional Significance

Meyer, Y., Belin, C., Delorme‐Hinoux, V., Reichheld, J., & Riondet, C. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4327 · Cited by 404 · 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

NUCLEAR AND MITOCHONDRIAL COMPARTMENTATION OF OXIDATIVE STRESS AND REDOX SIGNALING

Hansen, J. M., Go, Y., & Jones, D. P. (2005) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.46.120604.141122 · Cited by 401 · 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

Redox Signaling Mediated by Thioredoxin and Glutathione Systems in the Central Nervous System

Ren, X., Zou, L., Zhang, X., Branco, V., Wang, J., Carvalho, C. M. L., Holmgren, A., & Lu, J. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6925 · Cited by 365 · see citing works

Glutathione-Related Enzymes and Proteins: A Review

Vašková, J., Kočan, L., Vaško, L., & Perjési, P. (2023) · Molecules · doi:10.3390/molecules28031447 · Cited by 363 · see citing works

Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system

Berndt, C., Lillig, C. H., & Holmgren, A. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01162.2006 · Cited by 350 · see citing works

Mitochondrial Thiols in Antioxidant Protection and Redox Signaling: Distinct Roles for Glutathionylation and Other Thiol Modifications

Murphy, M. P. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4289 · Cited by 341 · see citing works

Genes of the antioxidant system of the honey bee: annotation and phylogeny

Corona, M., & Robinson, G. E. (2006) · Insect Molecular Biology · doi:10.1111/j.1365-2583.2006.00695.x · Cited by 313 · see citing works

Dissecting Redox Biology Using Fluorescent Protein Sensors

Schwarzländer, M., Dick, T. P., Meyer, A. J., & Morgan, B. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6266 · Cited by 298 · 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

Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis

Morgan, B., Ezeriņa, D., Amoako, T. N. E., Riemer, J., Seedorf, M., & Dick, T. P. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1142 · Cited by 288 · see citing works

Cytochrome <i>c</i> Biogenesis: Mechanisms for Covalent Modifications and Trafficking of Heme and for Heme-Iron Redox Control

Kranz, R. G., Richard-Fogal, C., Taylor, J.-S., & Frawley, E. R. (2009) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00001-09 · Cited by 275 · see citing works

Thiol Chemistry in Peroxidase Catalysis and Redox Signaling

Bindoli, A., Fukuto, J. M., & Forman, H. J. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2063 · Cited by 242 · see citing works

Role of glutathione, glutathione transferase, and glutaredoxin in regulation of redox-dependent processes

Kalinina, E. V., Чернов, Н. Н., & Novichkova, M. (2014) · Biochemistry (Moscow) · doi:10.1134/s0006297914130082 · Cited by 258 · see citing works

Mechanistic and Kinetic Details of Catalysis of Thiol-Disulfide Exchange by Glutaredoxins and Potential Mechanisms of Regulation

Gallogly, M. M., Starke, D. W., & Mieyal, J. J. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2291 · Cited by 224 · see citing works

Mitochondrial glutathione: Features, regulation and role in disease

Marı́, M., Morales, A., Colell, A., García‐Ruiz, C., Kaplowitz, N., & Fernández-Checa, J. C. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.10.018 · Cited by 205 · see citing works

Glutathione de novo synthesis but not recycling process coordinates with glutamine catabolism to control redox homeostasis and directs murine T cell differentiation

Lian, G., Gnanaprakasam, J. R., Wang, T., Wu, R., Chen, X., Liu, L., Shen, Y., Yang, M., Yang, J. J. J., Chen, Y., et al. (2018) · eLife · doi:10.7554/elife.36158 · Cited by 199 · 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

Thioredoxin and Its Related Molecules: Update 2005

Nakamura, H. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.823 · Cited by 185 · see citing works

Principles in Redox Signaling: From Chemistry to Functional Significance

Bindoli, A., & Rigobello, M. P. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4655 · Cited by 189 · see citing works

Glutaredoxin: Discovery, redox defense and much more

Ogata, F. T., Branco, V., Vale, F. F., & Coppo, L. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101975 · Cited by 189 · see citing works

Complex I within Oxidatively Stressed Bovine Heart Mitochondria Is Glutathionylated on Cys-531 and Cys-704 of the 75-kDa Subunit

Hurd, T. R., Requejo, R., Filipovska, A., Brown, S., Prime, T. A., Robinson, A. J., Fearnley, I. M., & Murphy, M. P. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803432200 · Cited by 182 · see citing works

Redox Regulation in Photosynthetic Organisms: Focus on Glutathionylation

Zaffagnini, M., Bedhomme, M., Marchand, C. H., Morisse, S., Trost, P., & Lemaire, S. D. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4255 · Cited by 181 · see citing works

Disruption of mitochondrial redox circuitry in oxidative stress

Jones, D. P. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2006.07.008 · Cited by 176 · see citing works

Thioredoxin Reductase Inhibition for Cancer Therapy

Gencheva, R., & Arnér, E. S. J. (2021) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-052220-102509 · Cited by 178 · see citing works

Regulation of calcium signalling and gene expression by glutathione

Gomez, L. D. (2004) · Journal of Experimental Botany · doi:10.1093/jxb/erh202 · Cited by 173 · see citing works

Molecular Mechanisms of Thioredoxin and Glutaredoxin as Hydrogen Donors for Mammalian S Phase Ribonucleotide Reductase

Avval, F. Z., & Holmgren, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809338200 · Cited by 169 · see citing works

Evolution and diversity of glutaredoxins in photosynthetic organisms

Couturier, J., Jacquot, J., & Rouhier, N. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0054-y · Cited by 170 · 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

The thioredoxin h system of higher plants

Gelhaye, É., Rouhier, N., & Jacquot, J. (2004) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2004.03.002 · Cited by 158 · see citing works

Protein Tyrosine Phosphorylation and Protein Tyrosine Nitration in Redox Signaling

Monteiro, H. P., Arai, R. J., & Travassos, L. R. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1853 · Cited by 157 · see citing works

A Novel Monothiol Glutaredoxin (Grx4) from Escherichia coli Can Serve as a Substrate for Thioredoxin Reductase

Fernandes, A. P., Fladvad, M., Berndt, C., Andrésen, C., Lillig, C. H., Neubauer, P. B., Sunnerhagen, M., Holmgren, A., & Vlamis‐Gardikas, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500678200 · Cited by 155 · see citing works

The Incomplete Glutathione Puzzle: Just Guessing at Numbers and Figures?

Deponte, M. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7123 · Cited by 154 · 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

Involvement of thio-, peroxi-, and glutaredoxins in cellular redox-dependent processes

Kalinina, E. V., Chernov, N., & Saprin, A. (2008) · Biochemistry (Moscow) · doi:10.1134/s0006297908130099 · Cited by 159 · see citing works

Glutathione: Role in Oxidative/Nitrosative Stress, Antioxidant Defense, and Treatments

Raj, S. R., Bhattacharyya, C., Sarkar, A., Chakraborty, S., Sircar, E., Dutta, S., & Sengupta, R. (2021) · ChemistrySelect · doi:10.1002/slct.202100773 · Cited by 147 · see citing works

An Atlas of the Thioredoxin Fold Class Reveals the Complexity of Function-Enabling Adaptations

Atkinson, H. J., & Babbitt, P. C. (2009) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000541 · Cited by 147 · 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

Oxidoreduction of protein thiols in redox regulation

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

Redox Environment, Free Radical, and Oxidative DNA Damage

Storr, S. J., Woolston, C. M., Zhang, Y., & Martin, S. G. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4920 · Cited by 145 · see citing works

Glutathione, Glutaredoxins, and Iron

Berndt, C., & Lillig, C. H. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7132 · Cited by 141 · see citing works

Biochemical Characterization of Glutaredoxins from Chlamydomonas reinhardtii Reveals the Unique Properties of a Chloroplastic CGFS-type Glutaredoxin

Zaffagnini, M., Michelet, L., Massot, V., Trost, P., & Lemaire, S. D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709567200 · Cited by 138 · see citing works

Significance of the mitochondrial thioredoxin reductase in cancer cells: An update on role, targets and inhibitors

Scalcon, V., Bindoli, A., & Rigobello, M. P. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.03.043 · Cited by 138 · see citing works

Selenocysteine in mammalian thioredoxin reductase and application of ebselen as a therapeutic

Ren, X., Zou, L., Lu, J., & Holmgren, A. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.05.081 · Cited by 138 · see citing works

Redox Regulation of Cell Survival by the Thioredoxin Superfamily: An Implication of Redox Gene Therapy in the Heart

Ahsan, M., Lekli, I., Ray, D., Yodoi, J., & Das, D. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2683 · Cited by 134 · see citing works

Kinetic and Thermodynamic Aspects of Cellular Thiol–Disulfide Redox Regulation

Jensen, K. S., Hansen, R. E., & Winther, J. R. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2297 · Cited by 135 · see citing works

Selenium Cytotoxicity in Cancer

Wallenberg, M., Misra, S., & Björnstedt, M. (2014) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.12207 · Cited by 135 · see citing works

Redox Homeostasis in Photosynthetic Organisms: Novel and Established Thiol-Based Molecular Mechanisms

Zaffagnini, M., Fermani, S., Marchand, C. H., Costa, A., Sparla, F., Rouhier, N., Geigenberger, P., Lemaire, S. D., & Trost, P. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7617 · Cited by 130 · see citing works

S-glutathionylation reactions in mitochondrial function and disease

Mailloux, R. J., & Willmore, W. G. (2014) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2014.00068 · Cited by 125 · see citing works

Thioredoxins, glutaredoxins, and glutathionylation: new crosstalks to explore

Michelet, L., Zaffagnini, M., Massot, V., Keryer, E., Vanacker, H., Miginiac-Maslow, M., Issakidis-Bourguet, E., & Lemaire, S. (2006) · Photosynthesis Research · doi:10.1007/s11120-006-9096-2 · Cited by 120 · see citing works

Redox atlas of the mouse

Godoy, J. R., Funke, M., Ackermann, W., Haunhorst, P., Oesteritz, S., Capani, F., Elsässer, H., & Lillig, C. H. (2010) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2010.05.006 · Cited by 124 · see citing works

Mitochondrial Thiols in the Regulation of Cell Death Pathways

Yin, F., Sancheti, H., & Cadenas, E. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4639 · Cited by 112 · see citing works

Kinetic and Mechanistic Characterization and Versatile Catalytic Properties of Mammalian Glutaredoxin 2: Implications for Intracellular Roles

Gallogly, M. M., Starke, D. W., Leonberg, A. K., Ospina, S. M. E., & Mieyal, J. J. (2008) · Biochemistry · doi:10.1021/bi800966v · Cited by 123 · see citing works

The crystal structure of human GLRX5: iron–sulfur cluster co-ordination, tetrameric assembly and monomer activity

Johansson, C., Roos, A. K., Montaño, S., Sengupta, R., Filippakopoulos, P., Guo, K., von Delft, F., Holmgren, A., Oppermann, U. C. T., & Kavanagh, K. L. (2010) · Biochemical Journal · doi:10.1042/bj20101286 · Cited by 123 · see citing works

The roles of glutaredoxins ligating Fe–S clusters: Sensing, transfer or repair functions?

Couturier, J., Przybyla‐Toscano, J., Roret, T., Claude Didierjean, B., & Rouhier, N. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.09.018 · Cited by 122 · see citing works

Substrate and inhibitor specificities differ between human cytosolic and mitochondrial thioredoxin reductases: Implications for development of specific inhibitors

Rackham, O., Shearwood, A.-M. J., Thyer, R. T., McNamara, E. L., Davies, S. M. K., Callus, B. A., Miranda‐Vizuete, A., Berners‐Price, S. J., Cheng, Q., Arnér, E. S. J., et al. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.12.015 · Cited by 121 · see citing works

Changes in the mitochondrial antioxidant systems in neurodegenerative diseases and acute brain disorders

Ruszkiewicz, J. A., & Albrecht, J. (2015) · Neurochemistry International · doi:10.1016/j.neuint.2014.12.012 · Cited by 122 · see citing works

The biological roles of glutaredoxins

Ströher, E., & Millar, A. H. (2012) · Biochemical Journal · doi:10.1042/bj20112131 · Cited by 117 · see citing works

Molecular architecture of Streptococcus pneumoniae surface thioredoxin‐fold lipoproteins crucial for extracellular oxidative stress resistance and maintenance of virulence

Saleh, M., Bartual, S. G., Abdullah, M. R., Jensch, I., Asmat, T. M., Petruschka, L., Pribyl, T. M., Gellert, M., Lillig, C. H., Antelmann, H., et al. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201202435 · Cited by 116 · see citing works

Both Thioredoxin 2 and Glutaredoxin 2 Contribute to the Reduction of the Mitochondrial 2-Cys Peroxiredoxin Prx3

Hanschmann, E.-M., Lönn, M. E., Schütte, L. D., Funke, M., Godoy, J. R., Eitner, S., Hudemann, C., & Lillig, C. H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.185827 · Cited by 112 · see citing works

The Redox State of SECIS Binding Protein 2 Controls Its Localization and Selenocysteine Incorporation Function

Papp, L. V., Lu, J., Striebel, F., Kennedy, D. D., Holmgren, A., & Khanna, K. K. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.02284-05 · Cited by 112 · see citing works

Arabidopsis Chloroplastic Glutaredoxin C5 as a Model to Explore Molecular Determinants for Iron-Sulfur Cluster Binding into Glutaredoxins

Couturier, J., Ströher, E., Albetel, A., Roret, T., Muthuramalingam, M., Tarrago, L., Seidel, T., Tsan, P., Jacquot, J., Johnson, M. K., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.228726 · Cited by 111 · see citing works

The relationships between cytochromes P450 and H 2 O 2 : Production, reaction, and inhibition

Albertolle, M. E., & Guengerich, F. P. (2018) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2018.05.014 · Cited by 111 · see citing works

Disulfide bond based polymeric drug carriers for cancer chemotherapy and relevant redox environments in mammals

Zhang, P., Wu, J., Xiao, F., Zhao, D., & Luan, Y. (2018) · Medicinal Research Reviews · doi:10.1002/med.21485 · Cited by 108 · see citing works

Metabolic Reprogramming in Modulating T Cell Reactive Oxygen Species Generation and Antioxidant Capacity

Gnanaprakasam, J. R., Wu, R., & Wang, R. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01075 · Cited by 105 · see citing works

The Thioredoxin-Thioredoxin Reductase System Can Function in Vivo as an Alternative System to Reduce Oxidized Glutathione in Saccharomyces cerevisiae

Tan, S., Greetham, D., Raeth, S., Grant, C. M., Dawes, I. W., & Perrone, G. G. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.062844 · Cited by 106 · see citing works

Effect of Auranofin on the mitochondrial generation of hydrogen peroxide. Role of thioredoxin reductase

Rigobello, M., Folda, A., Baldoin, M. C., Scutari, G., & Bindoli, A. (2005) · Free radical research · doi:10.1080/10715760500135391 · Cited by 103 · see citing works

The Oxidized Protein Repair Enzymes Methionine Sulfoxide Reductases and Their Roles in Protecting against Oxidative Stress, in Ageing and in Regulating Protein Function

Lourenço dos Santos, S., Petropoulos, I., & Friguet, B. (2018) · Antioxidants · doi:10.3390/antiox7120191 · Cited by 109 · see citing works

Platyhelminth Mitochondrial and Cytosolic Redox Homeostasis Is Controlled by a Single Thioredoxin Glutathione Reductase and Dependent on Selenium and Glutathione

Bonilla, M., Denicola, A., Novoselov, S. V., Turanov, A. A., Protasio, A. V., Izmendi, D., Gladyshev, V. N., & Salinas, G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710609200 · Cited by 103 · see citing works

Oxidation and S-Nitrosylation of Cysteines in Human Cytosolic and Mitochondrial Glutaredoxins

Hashemy, S. I., Johansson, C., Berndt, C., Lillig, C. H., & Holmgren, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700927200 · Cited by 102 · see citing works

How Does Iron–Sulfur Cluster Coordination Regulate the Activity of Human Glutaredoxin 2?

Berndt, C., Hudemann, C., Hanschmann, E.-M., Axelsson, R., Holmgren, A., & Lillig, C. H. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.9.151 · Cited by 101 · see citing works

Glutaredoxin-2 Is Required to Control Oxidative Phosphorylation in Cardiac Muscle by Mediating Deglutathionylation Reactions

Mailloux, R. J., Xuan, J. Y., McBride, S., Maharsy, W. M., Thorn, S., Holterman, C. E., Kennedy, C., Rippstein, P. U., deKemp, R. A., da Silva, J., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.550574 · Cited by 99 · see citing works

Nuclear Monothiol Glutaredoxins of Saccharomyces cerevisiae Can Function as Mitochondrial Glutaredoxins

Molina‐Navarro, M. M., Bellı́, G., de la Torre-Ruiz, M. Á., Rodríguez‐Manzaneque, M. T., & Herrero, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410219200 · Cited by 100 · see citing works

What is the Functional Significance of the Unique Location of Glutaredoxin 1 (GRx1) in the Intermembrane Space of Mitochondria?

Pai, H. V., Starke, D. W., Lesnefsky, E. J., Hoppel, C. L., & Mieyal, J. J. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1642 · Cited by 99 · see citing works

The A to Z of modulated cell patterning by mammalian thioredoxin reductases

Dagnell, M., Schmidt, E. E., & Arnér, E. S. J. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.12.029 · Cited by 100 · see citing works

Expression Pattern of Human Glutaredoxin 2 Isoforms: Identification and Characterization of Two Testis/Cancer Cell-Specific Isoforms

Lönn, M. E., Hudemann, C., Berndt, C., Cherkasov, V., Capani, F., Holmgren, A., & Lillig, C. H. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1821 · Cited by 99 · see citing works

The Pancreatic β-Cell: A Bioenergetic Perspective

Nicholls, D. G. (2016) · Physiological Reviews · doi:10.1152/physrev.00009.2016 · Cited by 95 · see citing works

Structural and evolutionary aspects of thioredoxin reductases in photosynthetic organisms

Jacquot, J., Eklund, H., Rouhier, N., & Schürmann, P. (2009) · Trends in Plant Science · doi:10.1016/j.tplants.2009.03.005 · Cited by 97 · see citing works

A Mycothiol Synthase Mutant of Mycobacterium tuberculosis Has an Altered Thiol-Disulfide Content and Limited Tolerance to Stress

Buchmeier, N. A., Newton, G. L., & Fahey, R. C. (2006) · Journal of Bacteriology · doi:10.1128/jb.00393-06 · Cited by 97 · see citing works

Redox Control of Neural Function: Background, Mechanisms, and Significance

Maher, P. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1941 · Cited by 99 · see citing works

Human Mitochondrial Glutaredoxin Reduces S-Glutathionylated Proteins with High Affinity Accepting Electrons from Either

Reductase, G. O. T., Johansson, C., Lillig, C. H., & Holmgren, A. (2013)

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

Kinetics of the Mammalian Glutaredoxins: GRx2 Is Less Active, But Mimics the Catalytic Mechanism of GRx1

Gallogly, M. M., Starke, D. W., Leonberg, A. K., & Mieyal, J. J. (2007) · The FASEB Journal · doi:10.1096/fasebj.21.5.a274-a

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