Thioredoxin and Related Molecules–From Biology to Health and Disease

The hallmarks of cancer

Hanahan, D., & Weinberg, R. A. (2000) · Cell · doi:10.1016/s0092-8674(00)81683-9 · Cited by 29,219

Aging: a theory based on free radical and radiation chemistry

Harman, D. (1956) · Journal of Gerontology · doi:10.1093/geronj/11.3.298 · Cited by 8,567

Detection and isolation of type C retrovirus particles from fresh and cultured lymphocytes of a patient with cutaneous T-cell lymphoma

Poiesz, B. J., Ruscetti, F. W., Gazdar, A. F., Bunn, P. A., Minna, J. D., & Gallo, R. C. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.12.7415 · Cited by 5,043

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

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

Adult T-cell leukemia: clinical and hematologic features of 16 cases

Uchiyama, T., Yodoi, J., Sagawa, K., Takatsuki, K., & Uchino, H. (1977) · Blood · doi:10.1182/blood.v50.3.481.bloodjournal503481 · Cited by 2,315

Induction of Apoptosis by ASK1, a Mammalian MAPKKK That Activates SAPK/JNK and p38 Signaling Pathways

Ichijo, H., Nishida, E., Irie, K., ten Dijke, P., Saitoh, M., Moriguchi, T., Takagi, M., Matsumoto, K., Miyazono, K., & Gotoh, Y. (1997) · Science · doi:10.1126/science.275.5296.90 · Cited by 2,310

THIOREDOXIN

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

Oxidative stress in neurodegeneration: Cause or consequence?

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

Thioredoxin and Glutaredoxin Systems

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

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

Post-translational modification of p53 in tumorigenesis

Bode, A. M., & Dong, Z. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1455 · Cited by 1,270

Reduction of Ribonucleotides

Thelander, L., & Reichard, P. A. (1979) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.48.070179.001025 · Cited by 1,160

REDOX REGULATION OF CELLULAR ACTIVATION

Nakamura, H., Nakamura, K., & Yodoi, J. (1997) · Annual Review of Immunology · doi:10.1146/annurev.immunol.15.1.351 · Cited by 1,106

Enzymatic Synthesis of Deoxyribonucleotides

Laurent, T. C., Moore, E. C., & Reichard, P. A. (1964) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)97742-2 · Cited by 933

AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1

Hirota, K., Matsui, M., Iwata, S., Nishiyama, A., Mori, K., & Yodoi, J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.3633 · Cited by 847

Thiordoxin regulates the DNA binding activity of NF-χB by reduction of a disulphid bond involving cysteine 62

Matthews, J. R., Wakasugi, N., Virelizier, J., Yodoi, J., & Hay, R. T. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.15.3821 · Cited by 836

Thioredoxin —a fold for all reasons

Martin, J. L. (1995) · Structure · doi:10.1016/s0969-2126(01)00154-x · Cited by 832

Identification of Thioredoxin-binding Protein-2/Vitamin D3 Up-regulated Protein 1 as a Negative Regulator of Thioredoxin Function and Expression

Nishiyama, A., Matsui, M., Iwata, S., Hirota, K., Masutani, H., Nakamura, H., Takagi, Y., Sono, H., Gon, Y., & Yodoi, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.31.21645 · Cited by 740

Oxidant and antioxidant balance in the airways and airway diseases

Rahman, I., Biswas, S. K., & Kode, A. (2006) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2005.12.087 · Cited by 732

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

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

Selenium metabolism, selenoproteins and mechanisms of cancer prevention: complexities with thioredoxin reductase

Ganther, H. E. (1999) · Carcinogenesis · doi:10.1093/carcin/20.9.1657 · Cited by 690

RIBONUCLEOTIDE REDUCTASES

Jordan, A., & Reichard, P. A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.71 · Cited by 675

Glutaredoxins: Glutathione-Dependent Redox Enzymes with Functions Far Beyond a Simple Thioredoxin Backup System

Fernandes, A. P., & Holmgren, A. (2004) · Antioxidants and Redox Signaling · doi:10.1089/152308604771978354 · Cited by 670

Oxidative stress in malaria parasite-infected erythrocytes: host–parasite interactions

Becker, K., Tilley, L. M., Vennerstrom, J. L., Roberts, D. J., Rogerson, S. J., & Ginsburg, H. (2003) · International Journal for Parasitology · doi:10.1016/j.ijpara.2003.09.011 · Cited by 665

Peroxiredoxins

Hofmann, B., Hecht, H., & Flohé, L. (2002) · Biological Chemistry · doi:10.1515/bc.2002.040 · Cited by 620

Distinct Roles of Thioredoxin in the Cytoplasm and in the Nucleus

Hirota, K., Murata, M., Sachi, Y., Nakamura, H., Takeuchi, J. S., Mori, K., & Yodoi, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.39.27891 · Cited by 615

Redox Regulation of NF-κB Activation: Distinct Redox Regulation Between the Cytoplasm and the Nucleus

Kabe, Y., Ando, K., Hirao, S., Yoshida, M., & Handa, H. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.395 · Cited by 585

ATL‐derived factor (ADF), an IL‐2 receptor/Tac inducer homologous to thioredoxin; possible involvement of dithiol‐reduction in the IL‐2 receptor induction.

Tagaya, Y., Maeda, Y., Mitsui, A., Kondo, N., Matsui, H., Hamuro, J., Brown, N., Arai, K., Yokota, T., & Wakasugi, H. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03436.x · Cited by 562

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

A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity.

Tamura, T., & Stadtman, T. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.3.1006 · Cited by 538

Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence

Zhong, L., Arnér, E. S. J., & Holmgren, A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.100114897 · Cited by 528

The histone deacetylase inhibitor SAHA arrests cancer cell growth, up-regulates thioredoxin-binding protein-2, and down-regulates thioredoxin

Butler, L. M., Zhou, X., Xu, W., Scher, H. I., Rifkind, R. A., Marks, P. A., & Richon, V. M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.182372299 · Cited by 511

Role of thioredoxin in the response of normal and transformed cells to histone deacetylase inhibitors

Ungerstedt, J. S., Sowa, Y., Xu, W., Shao, Y., Dokmanovic, M., Perez, G., Ngo, L., Holmgren, A., Jiang, X., & Marks, P. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408732102 · Cited by 504

Vitamin D3 Up-Regulated Protein 1 Mediates Oxidative Stress Via Suppressing the Thioredoxin Function

Junn, E., Han, S. H., Im, J. Y., Yang, Y. D., Cho, E., Um, H., Kim, D. K., Lee, K. W., Han, P., Rhee, S. G., et al. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.12.6287 · Cited by 500

The isolation and purification of a specific “protector” protein which inhibits enzyme inactivation by a thiol/Fe(III)/O2 mixed-function oxidation system.

Kim, K., Kim, I. H., Lee, K. Y., Rhee, S. G., & Stadtman, E. R. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68840-4 · Cited by 492

Oxidoreductive regulation of nuclear factor kappa B. Involvement of a cellular reducing catalyst thioredoxin

Hayashi, T., Ueno, Y., & Okamoto, T. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82135-4 · Cited by 485

Identification of redox/repair protein Ref-1 as a potent activator of p53.Preprint

Jayaraman, L., Murthy, K. G. K., Zhu, C., Curran, T., Xanthoudakis, S., & Prives, C. L. (1997) · Genes & Development · doi:10.1101/gad.11.5.558 · Cited by 485

Essential Role for Mitochondrial Thioredoxin Reductase in Hematopoiesis, Heart Development, and Heart Function

Conrad, M., Jakupoglu, C., Moreno, S. G., Lippl, S., Banjac, A., Schneider, M., Beck, H., Hatzopoulos, A. K., Just, U., Sinowatz, F., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.21.9414-9423.2004 · Cited by 485

The thioredoxin system—From science to clinic

Gromer, S., Urig, S., & Becker, K. (2003) · Medicinal Research Reviews · doi:10.1002/med.10051 · Cited by 482

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

Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene.

Gladyshev, V. N., Jeang, K.-T., & Stadtman, T. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.12.6146 · Cited by 471

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

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

Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway.

Rubartelli, A., Bajetto, A., Allavena, G., Wollman, E. E., & Sitia, R. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35742-9 · Cited by 459

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

Identification and characterization of rod-derived cone viability factor

Léveillard, T., Mohand‐Saïd, S., Lorentz, O., Hicks, D., Fintz, A.-C., Clérin, E., Simonutti, M., Forster, V., Cavusoglu, N., Chalmel, F., et al. (2004) · Nature Genetics · doi:10.1038/ng1386 · Cited by 450

Properties and Biological Activities of Thioredoxins

Powis, G., & Montfort, W. R. (2001) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.41.1.261 · Cited by 449

Oxidation of Methionine in Proteins: Roles in Antioxidant Defense and Cellular Regulation

Levine, R. L., Moskovitz, J., & Stadtman, E. R. (2000) · IUBMB Life · doi:10.1080/713803735 · Cited by 446

The Absence of Mitochondrial Thioredoxin 2 Causes Massive Apoptosis, Exencephaly, and Early Embryonic Lethality in Homozygous Mice

Nonn, L., Williams, R. R., Erickson, R. P., & Powis, G. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.3.916-922.2003 · Cited by 438

Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution.

Holmgren, A., Söderberg, B.-O., Eklund, H., & Brändén, C.-I. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.6.2305 · Cited by 438

Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide

Holmgren, A. (1995) · Structure · doi:10.1016/s0969-2126(01)00153-8 · Cited by 437

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

Thioredoxin-dependent Redox Regulation of p53-mediated p21 Activation

Ueno, M., Masutani, H., Arai, R. J., Yamauchi, A., Hirota, K., Sakai, T., Inamoto, T., Yamaoka, Y., Yodoi, J., & Nikaido, T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.50.35809 · Cited by 428

Redox regulation in the lens

Lou, M. F. (2003) · Progress in Retinal and Eye Research · doi:10.1016/s1350-9462(03)00050-8 · Cited by 422

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

Redox modulation of p53 conformation and sequence-specific DNA binding in vitro.

Hainaut, P. L., & Milner, J. (1993) · PubMed · Cited by 408

Cloning and Expression of a Novel Mammalian Thioredoxin

Spyrou, G., Enmark, E., Miranda‐Vizuete, A., & Gustafsson, J.-Α. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.5.2936 · Cited by 399

Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69

Haendeler, J., Hoffmann, J., Tischler, V., Berk, B. C., Zeiher, A. M., & Dimmeler, S. (2002) · Nature Cell Biology · doi:10.1038/ncb851 · Cited by 399

Methionine oxidation and aging

Stadtman, E. R., Remmen, H. V., Richardson, A. G., Wehr, N. B., & Levine, R. L. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.08.010 · Cited by 398

Glutathione, iron and Parkinson’s disease

Bharath, S., Hsu, M., Kaur, D., Rajagopalan, S., & Andersen, J. K. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(02)01174-7 · Cited by 394

Commentary on and reprint of Poiesz BJ, Ruscetti FW, Gazdar AF, Bunn PA, Minna JD, Gallo RC, Detection and isolation of type C retrovirus particles from fresh and cultured lymphocytes of a patient with cutaneous T cell lymphoma, in Proceedings of the National Academy of Sciences (1980) 77:7415–7419

LICHTMAN, M., Spivak, J. L., Boxer, L. A., Shattil, S. J., & HENDERSON, E. (2000) · Elsevier eBooks · doi:10.1016/b978-012448510-5/50140-0 · Cited by 392

Thioredoxin Promotes ASK1 Ubiquitination and Degradation to Inhibit ASK1-Mediated Apoptosis in a Redox Activity-Independent Manner

Liu, Y., & Wang, M. (2002) · Circulation Research · doi:10.1161/01.res.0000022160.64355.62 · Cited by 391

Thioredoxin reductase as a pathophysiological factor and drug target

Becker, K., Gromer, S., Schirmer, R. H., & Müller, S. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01703.x · Cited by 389

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

The MPTP model of Parkinson's disease

Smeyne, R. J., & Jackson-Lewis, V. R. (2004) · Molecular Brain Research · doi:10.1016/j.molbrainres.2004.09.017 · Cited by 387

The thioredoxin-related redox-regulating protein nucleoredoxin inhibits Wnt–β-catenin signalling through Dishevelled

Funato, Y., Michiue, T., Asashima, M., & Miki, H. (2006) · Nature Cell Biology · doi:10.1038/ncb1405 · Cited by 386

Components involved in assembly and dislocation of iron–sulfur clusters on the scaffold protein Isu1p

Mühlenhoff, U., Gerber, J., Richhardt, N., & Lill, R. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg446 · Cited by 383

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 377

Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis.

The Tübingen 2000 Screen Consortium, Wingert, R. A., Galloway, J. L., Barut, B., Foott, H., Fraenkel, P., Axe, J. L., Weber, G. J., Dooley, K., Davidson, A. J., et al. (2005) · Nature · doi:10.1038/nature03887 · Cited by 370

Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli.

Kallis, G. B., & Holmgren, A. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70458-x · Cited by 368

S-Nitrosoglutathione Is Cleaved by the Thioredoxin System with Liberation of Glutathione and Redox Regulating Nitric Oxide

Nikitovic, D., & Holmgren, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.32.19180 · Cited by 368

Cytoplasmic Thioredoxin Reductase Is Essential for Embryogenesis but Dispensable for Cardiac Development

Jakupoglu, C., Przemeck, G. K. H., Schneider, M., Moreno, S. G., Mayr, N., Hatzopoulos, A. K., de Angelis, M. H., Wurst, W., Bornkamm, G. W., Brielmeier, M., et al. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.5.1980-1988.2005 · Cited by 357

The redox and DNA-repair activities of Ref-1 are encoded by nonoverlapping domains.

Xanthoudakis, S., Miao, G. G., & Curran, T. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.1.23 · Cited by 353

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

Untitled work

(2002) · PubMed · Cited by 349

Pathways for protein disulphide bond formation

Frand, A. R., Cuozzo, J. W., & Kaiser, C. A. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01745-1 · Cited by 347

Overexpression of thioredoxin in transgenic mice attenuates focal ischemic brain damage

Takagi, Y., Mitsui, A., Nishiyama, A., Nozaki, K., Sono, H., Gon, Y., Hashimoto, N., & Yodoi, J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.4131 · Cited by 342

Enzymatic Synthesis of Deoxyribonucleotides

Moore, E. C., Reichard, P. A., & Thelander, L. (1964) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)97743-4 · Cited by 340

Thioredoxin, a Redox Enzyme Released in Infection and Inflammation, Is a Unique Chemoattractant for Neutrophils, Monocytes, and T Cells

Bertini, R., Howard, O. M. Z., Dong, H., Oppenheim, J. J., Bizzarri, C., Sergi, R., Caselli, G., Pagliei, S., Romines, B., Wilshire, J. A., et al. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.189.11.1783 · Cited by 337

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

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

Reduction of disulfides by thioredoxin. Exceptional reactivity of insulin and suggested functions of thioredoxin in mechanism of hormone action.

Holmgren, A. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86818-7 · Cited by 329

Mouse cloning with nucleus donor cells of different age and type

Wakayama, T., & Yanagimachi, R. (2001) · Molecular Reproduction and Development · doi:10.1002/1098-2795(20010401)58:4 · Cited by 323

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

Expression profile of transcripts in Alzheimer's disease tangle-bearing CA1 neurons

Ginsberg, S. D., Hemby, S. E., Lee, V. M. ‐., Eberwine, J. H., & Trojanowski, J. Q. (2000) · Annals of Neurology · doi:10.1002/1531-8249(200007)48:1 · Cited by 315

Human Thioredoxin Reductase Directly Reduces Lipid Hydroperoxides by NADPH and Selenocystine Strongly Stimulates the Reaction via Catalytically Generated Selenols

Björnstedt, M., Hámberg, M., Kumar, S., Xue, J., & Holmgren, A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.20.11761 · Cited by 312

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

Enzymatic Synthesis of Deoxyribonucleotides

Bertani, L. E., Häggmark, A., & Reichard, P. A. (1963) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48681-4 · Cited by 311

Thioltransferase is a specific glutathionyl mixed-disulfide oxidoreductase

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

Thioredoxin and thioredoxin reductase gene expression in human tumors and cell lines, and the effects of serum stimulation and hypoxia.

Berggren, M. I., Gallegos, A. C., Gasdaska, J. R., Gasdaska, P. Y., Warneke, J. A., & Powis, G. (1996) · PubMed · Cited by 306

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

Biochemistry and physiological role of methionine sulfoxide residues in proteins

Brot, N., & Weissbach, H. (1983) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(83)90592-1 · Cited by 298

Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine

Mitchell, D. A., & Marletta, M. A. (2005) · Nature Chemical Biology · doi:10.1038/nchembio720 · Cited by 298

Bovine thioredoxin system. Purification of thioredoxin reductase from calf liver and thymus and studies of its function in disulfide reduction.

Holmgren, A. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40204-3 · Cited by 296

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 295

Overexpression of Human Thioredoxin in Transgenic Mice Controls Oxidative Stress and Life Span

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