The DOI matches its Crossref record; 33 of the 34 references it cites were found in a registry or an index.
The Absence of Mitochondrial Thioredoxin 2 Causes Massive Apoptosis, Exencephaly, and Early Embryonic Lethality in Homozygous Mice
Open accessAbstract
Thioredoxin 2 (Trx-2) is a small redox protein containing the thioredoxin active site Trp-Cys-Gly-Pro-Cys that is localized to the mitochondria by a mitochondrial leader sequence and encoded by a nuclear gene (Trx-2). Trx-2 plays an important role in cell viability and the regulation of apoptosis in vitro. To investigate the role of Trx-2 in mouse development, we studied the phenotype of mice that have the Trx-2 gene silenced by mutational insertion. Homozygous mutant embryos do not survive to birth and die after implantation at Theiler stage 15/16. The homozygous mutant embryos display an open anterior neural tube and show massively increased apoptosis at 10.5 days postcoitus and are not present by 12.5 days postcoitus. The timing of the embryonic lethality coincides with the maturation of the mitochondria, since they begin oxidative phosphorylation during this stage of embryogenesis. In addition, embryonic fibroblasts cultured from homozygous Trx-2-null embryos were not viable. Heterozygous mice are fertile and have no discernible phenotype visible by external observation, despite having decreased Trx-2 mRNA and protein. These results show that the mitochondrial redox protein Trx-2 is required for normal development of the mouse embryo and for actively respiring cells.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Both Trx1 and Trx2 appear to be essential, as complete deficiency of either subtype causes early embryonic lethality in mice (280, 317).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [317]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Induction of Apoptotic Program in Cell-Free Extracts: Requirement for dATP and Cytochrome c
Liu, X., Kim, C. N., Yang, J., Jemmerson, R., & Wang, X. (1996) · Cell · doi:10.1016/s0092-8674(00)80085-9 · Cited by 5,167
Role of reactive oxygen species (ROS) in apoptosis induction
Simon, H.-U., Haj-Yehia, A., & Levi-Schaffer, F. (2000) · Apoptosis · doi:10.1023/a:1009616228304 · Cited by 2,774
The mitochondrial permeability transition
Zoratti, M., & Szabó, I. (1995) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(95)00003-a · Cited by 2,410
Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
Li, Y., Huang, T.-T., Carlson, E. J., Melov, S., Ursell, P. C., Olson, J. L., Noble, L. J., Yoshimura, M. P., Berger, C., Chan, P. H., et al. (1995) · Nature Genetics · doi:10.1038/ng1295-376 · Cited by 1,789
The Atlas of Mouse Development
Kaufman, M. H. (1992) · Medical Entomology and Zoology · Cited by 1,750
Bcl-2 inhibits the mitochondrial release of an apoptogenic protease.
Susín, S. A., Zamzami, N., Castedo, M., Hirsch, T., Marchetti, P., Macho, A., Daugas, É., Geuskens, M., & Kroemer, G. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.184.4.1331 · Cited by 1,133
Chae, H. Z., Robison, K. E., Poole, L. B., Church, G. M., Storz, G., & Rhee, S. G. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.15.7017 · Cited by 749
Detection of catalase in rat heart mitochondria.
Radi, R., Turrens, J. F., Chang, L. Y., Bush, K. M., Crapo, J. D., & Freeman, B. A. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54740-2 · Cited by 573
Theiler, K. (1972) · Cited by 550
[57] Determination of the production of superoxide radicals and hydrogen peroxide in mitochondria
Boveris, A. (1984) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(84)05060-6 · Cited by 488
Research works printed but not linked: 1
- Radi R., 1991, J. Biol. Chem., 266, 22022
Cited by
Sorted by citations
Crosstalk of reactive oxygen species and NF-κB signaling
Morgan, M. J., & Liu, Z.-G. (2011) · Cell Research · doi:10.1038/cr.2010.178 · Cited by 3,505
Mitochondria, oxidative stress and cell death
Ott, M., Gogvadze, V. G., Orrenius, S., & Zhivotovsky, B. (2007) · APOPTOSIS · doi:10.1007/s10495-007-0756-2 · Cited by 2,020
From Selenium to Selenoproteins: Synthesis, Identity, and Their Role in Human Health
Papp, L. V., Lu, J., Holmgren, A., & Khanna, K. K. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1528 · Cited by 1,357
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
Mitochondrial Oxidative Stress: Implications for Cell Death
Orrenius, S., Gogvadze, V. G., & Zhivotovsky, B. (2006) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.47.120505.105122 · Cited by 1,294
Trends in oxidative aging theories
Muller, F. L., Lustgarten, M. S., Jang, Y., Richardson, A., & Van Remmen, H. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.03.034 · Cited by 1,053
Selenium, Selenoproteins, and Immunity
Avery, J., & Hoffmann, P. R. (2018) · Nutrients · doi:10.3390/nu10091203 · Cited by 948
Chemical biology of peroxynitrite: Kinetics, diffusion, and radicals
Ferrer-Sueta, G., & Radi, R. (2009) · ACS Chemical Biology · doi:10.1021/cb800279q · Cited by 776
Mitochondrial Energetics and Therapeutics
Wallace, D. C., Fan, W., & Procaccio, V. (2010) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092314 · Cited by 747
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
Hanschmann, E.-M., Godoy, J. R., Berndt, C., Hudemann, C., & Lillig, C. H. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4599 · Cited by 696
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 696
Redox compartmentalization in eukaryotic cells
Go, Y., & Jones, D. P. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.01.011 · Cited by 645
Is the oxidative stress theory of aging dead?
Pérez, V. I., Bokov, A., Remmen, H. V., Mele, J., Ran, Q., Ikeno, Y., & Richardson, A. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.06.003 · Cited by 604
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 608
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
Redox regulation of mitochondrial function
Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588
Anticancer Activity of Metal Complexes: Involvement of Redox Processes
Jungwirth, U., Kowol, C. R., Keppler, B. K., Hartinger, C. G., Berger, W., & Heffeter, P. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3663 · Cited by 568
Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling
Cox, A. G., Winterbourn, C. C., & Hampton, M. B. (2009) · Biochemical Journal · doi:10.1042/bj20091541 · Cited by 550
Thioredoxins and Glutaredoxins: Unifying Elements in Redox Biology
Meyer, Y., Buchanan, B. B., Vignols, F., & Reichheld, J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102108-134201 · Cited by 498
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
Genetics and development of neural tube defects
Copp, A. J., & Greene, N. D. E. (2009) · The Journal of Pathology · doi:10.1002/path.2643 · Cited by 488
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
Salmon, A. B., Richardson, A. G., & Pérez, V. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.12.015 · Cited by 451
Paradoxical Roles of Antioxidant Enzymes: Basic Mechanisms and Health Implications
Lei, X. G., Zhu, J., Cheng, W.-H., Bao, Y., Ho, Y.-S., Reddi, A. R., Holmgren, A., & Arnér, E. S. J. (2015) · Physiological Reviews · doi:10.1152/physrev.00010.2014 · Cited by 455
Prevention of the neurocristopathy Treacher Collins syndrome through inhibition of p53 function
Jones, N. C., Lynn, M. L., Gaudenz, K., Sakai, D., Aoto, K., Rey, J., Glynn, E. F., Ellington, L. R., Du, C., Dixon, J., et al. (2008) · Nature Medicine · doi:10.1038/nm1725 · Cited by 440
Reactive Oxygen Species in Mitochondria-Mediated Cell Death
Orrenius, S. (2007) · Drug Metabolism Reviews · doi:10.1080/03602530701468516 · Cited by 431
Function of reactive oxygen species during animal development: Passive or active?
Covarrubias, L., Hernández-García, D., Schnabel, D., Vidal, E. S., & Castro‐Obregón, S. (2008) · Developmental Biology · doi:10.1016/j.ydbio.2008.04.041 · Cited by 418
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
Early embryonic lethality caused by targeted disruption of the mouse PHGPx gene
Imai, H., Hirao, F., Sakamoto, T., Sekine, K., Mizukura, Y., Saito, M., Kitamoto, T., Hayasaka, M., Hanaoka, K., & Nakagawa, Y. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00734-4 · Cited by 357
Selenocysteine in proteins—properties and biotechnological use
Johansson, L., Gafvelin, G., & Arnér, E. S. J. (2005) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2005.05.010 · Cited by 353
Berndt, C., Lillig, C. H., & Holmgren, A. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01162.2006 · Cited by 355
Karihtala, P., & Soini, Y. (2007) · Apmis · doi:10.1111/j.1600-0463.2007.apm_514.x · Cited by 352
Kehrer, J. P., & Klotz, L. (2015) · Critical Reviews in Toxicology · doi:10.3109/10408444.2015.1074159 · Cited by 359
Mitochondria as therapeutic targets for cancer chemotherapy
Galluzzi, L., Larochette, N., Zamzami, N., & Kroemer, G. (2006) · Oncogene · doi:10.1038/sj.onc.1209598 · Cited by 342
The cystine/cysteine cycle: a redox cycle regulating susceptibility versus resistance to cell death
Banjac, A., Perisic, T., Sato, H., Seiler, A., Bannai, S., Weiss, N., Kölle, P., Tschoep, K., Issels, R. D., Daniel, P. T., et al. (2007) · Oncogene · doi:10.1038/sj.onc.1210796 · Cited by 324
Harris, M. J., & Juriloff, D. M. (2006) · Birth Defects Research Part A Clinical and Molecular Teratology · doi:10.1002/bdra.20333 · Cited by 311
The Thioredoxin System as a Therapeutic Target in Human Health and Disease
Mahmood, D. F. D., Abderrazak, A., Hadri, K. E., Simmet, T., & Rouis, M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4757 · Cited by 311
Leung, L., Kwong, M., Hou, S., Lee, C., & Chan, J. Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308439200 · Cited by 299
Inhibition of endogenous thioredoxin in the heart increases oxidative stress and cardiac hypertrophy
Yamamoto, M., Yang, G., Hong, C., Liu, J., Holle, E., Yu, X., Wagner, T. E., Vatner, S. F., & Sadoshima, J. (2003) · Journal of Clinical Investigation · doi:10.1172/jci17700 · Cited by 274
System xc− and Thioredoxin Reductase 1 Cooperatively Rescue Glutathione Deficiency
Mandal, P. K., Seiler, A., Perisic, T., Kölle, P., Banjac Canak, A., Förster, H., Weiss, N., Kremmer, E., Lieberman, M. W., Bannai, S., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.121327 · Cited by 269
Thioredoxin-2 Inhibits Mitochondria-Located ASK1-Mediated Apoptosis in a JNK-Independent Manner
Zhang, R., Al‐Lamki, R. S., Bai, L., Streb, J. W., Miano, J. M., Bradley, J. R., & Wang, M. (2004) · Circulation Research · doi:10.1161/01.res.0000130525.37646.a7 · Cited by 265
Papaconstantinou, J. (2019) · Cells · doi:10.3390/cells8111383 · Cited by 264
Thioredoxin and Its Role in Toxicology
Watson, W. H. (2003) · Toxicological Sciences · doi:10.1093/toxsci/kfh050 · Cited by 246
Human selenoproteins at a glance
Gromer, S., Eubel, J., Lee, B. L., & Jacob, J. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5143-y · Cited by 250
Calabrese, V., Guagliano, E., Sapienza, M. A., Panebianco, M., Calafato, S., Puleo, E., Pennisi, G., Mancuso, C., Butterfield, D. A., & Stella, A. G. (2006) · Neurochemical Research · doi:10.1007/s11064-006-9203-y · Cited by 242
Nonn, L., Berggren, M. M., & Powis, G. (2003) · PubMed · Cited by 215
Self-citationLu, Z., Xu, X., Hu, X., Fassett, J., Zhu, G., Tao, Y., Li, J., Huang, Y., Zhang, P., Zhao, B., et al. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2940 · Cited by 215
Zhang, Y., Ikeno, Y., Qi, W., Chaudhuri, A., Li, Y., Bokov, A., Thorpe, S. R., Baynes, J. W., Epstein, C., Richardson, A., et al. (2009) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/glp132 · Cited by 172
Respiration-dependent H2O2 removal in brain mitochondria via the thioredoxin/peroxiredoxin system
Drechsel, D. A., & Patel, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.101196 · Cited by 199
Stanley, B. A., Sivakumaran, V., Shi, S., McDonald, I., Lloyd, D., Watson, W. H., Aon, M. A., & Paolocci, N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.284612 · Cited by 203
Glutathione‐dependent reductive stress triggers mitochondrial oxidation and cytotoxicity
Zhang, H., Limphong, P., Pieper, J., Liu, Q., Rodesch, C. K., Christians, E., & Benjamin, I. J. (2011) · The FASEB Journal · doi:10.1096/fj.11-199869 · Cited by 201
Brennan, L., & Kantorow, M. (2008) · Experimental Eye Research · doi:10.1016/j.exer.2008.05.018 · Cited by 197
Oxidative stress and cell death
Rumora, L., Petrik, J., & Žanić‐Grubišić, T. (2003) · Cited by 192
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 194
Thioredoxin and Its Related Molecules: Update 2005
Nakamura, H. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.823 · Cited by 194
Alzheimer's Disease: Redox Dysregulation As a Common Denominator for Diverse Pathogenic Mechanisms
Rommy von Bernhardi, M., & Eugenín, J. L. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4082 · Cited by 193
Reactive oxygen species: A radical role in development?
Hernández-García, D., Wood, C. D., Castro‐Obregón, S., & Covarrubias, L. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.03.020 · Cited by 199
Liu, X., Zhang, Y., Zhuang, L., Olszewski, K. L., & Gan, B. (2020) · Genes & Diseases · doi:10.1016/j.gendis.2020.11.010 · Cited by 191
Thioredoxin-2 Inhibits Mitochondrial ROS Generation and ASK1 Activity to Maintain Cardiac Function
Huang, Q.-H., Zhou, H., Zhang, H.-F., Huang, Y., Hinojosa-Kirschenbaum, F., Fan, P., Yao, L., Belardinelli, L., Tellides, G., Giordano, F. J., et al. (2015) · Circulation · doi:10.1161/circulationaha.114.012725 · Cited by 149
Oxr1 Is Essential for Protection against Oxidative Stress-Induced Neurodegeneration
Oliver, P. L., Finelli, M. J., Edwards, B., Bitoun, E., Butts, D. L., Becker, E. B. E., Cheeseman, M. T., Davies, B., & Davies, K. E. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002338 · Cited by 172
Santos, A. L., Sinha, S., & Lindner, A. B. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/1941285 · Cited by 168
Cox, A. G., Brown, K., Arnér, E. S. J., & Hampton, M. B. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.08.021 · Cited by 167
Mitochondrial Thioredoxin-Responding Off–On Fluorescent Probe
Lee, M. H., Han, J. H., Lee, J.-H., Choi, H. G., Kang, C., & Kim, J. S. (2012) · Journal of the American Chemical Society · doi:10.1021/ja308446y · Cited by 161
Tolédano, M. B., Kumar, C., Moan, N. L., Spector, D., & Tacnet, F. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.07.002 · Cited by 166
He, F., Huang, Y., Song, Z. Q., Zhou, H. J., Zhang, H., Perry, R. J., Shulman, G. I., & Wang, M. (2020) · The Journal of Experimental Medicine · doi:10.1084/jem.20201416 · Cited by 160
Increased susceptibility of MER5 (peroxiredoxin III) knockout mice to LPS-induced oxidative stress
Li, L., Shoji, W., Takano, H., Nishimura, N., Aoki, Y., Takahashi, R., Goto, S., Kaifu, T., Takai, T., & Obinata, M. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.02.022 · Cited by 156
Involvement of thio-, peroxi-, and glutaredoxins in cellular redox-dependent processes
Kalinina, E. V., Чернов, Н. Н., & Saprin, A. N. (2008) · Biochemistry (Moscow) · doi:10.1134/s0006297908130099 · Cited by 149
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
Redox balance and cardioprotection
Tullio, F., Angotti, C., Perrelli, M.-G., Penna, C. R. R., & Pagliaro, P. (2013) · Basic Research in Cardiology · doi:10.1007/s00395-013-0392-7 · Cited by 152
Mandal, P. K., Schneider, M., Kölle, P., Kuhlencordt, P., Förster, H., Beck, H., Bornkamm, G. W., & Conrad, M. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-1509 · Cited by 147
NADPH oxidases: key modulators in aging and age-related cardiovascular diseases?
Sahoo, S., Meijles, D. N., & Pagano, P. J. (2016) · Clinical Science · doi:10.1042/cs20150087 · Cited by 147
Ahsan, M. K., Lekli, I., Ray, D., Yodoi, J., & Das, D. K. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2683 · Cited by 142
Selenium Cytotoxicity in Cancer
Wallenberg, M., Misra, S., & Björnstedt, M. (2014) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.12207 · Cited by 137
Selenoproteins and the aging brain
Zhang, S., Rocourt, C. R. B., & Cheng, W. (2010) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2010.02.006 · Cited by 136
High levels of thioredoxin reductase 1 modulate drug-specific cytotoxic efficacy
Eriksson, S. E., Prast‐Nielsen, S., Flaberg, E., Székely, L., & Arnér, E. S. J. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.09.016 · Cited by 128
McCann, J. C., & Ames, B. N. (2011) · The FASEB Journal · doi:10.1096/fj.11-180885 · Cited by 125
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 127
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 128
Emerging potential of thioredoxin and thioredoxin interacting proteins in various disease conditions
Maulik, N., & Das, D. K. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2007.12.008 · Cited by 128
Negative regulators of cardiac hypertrophy
Hardt, S. E. (2004) · Cardiovascular Research · doi:10.1016/j.cardiores.2004.03.015 · Cited by 122
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
Redox Control in Mammalian Embryo Development
Ufer, C., Wang, C. C., Borchert, A., Heydeck, D., & Kühn, H. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.3044 · Cited by 121
Thioredoxin h 5 Is Required for Victorin Sensitivity Mediated by a CC-NBS-LRR Gene in Arabidopsis
Sweat, T. A., & Wolpert, T. (2007) · The Plant Cell · doi:10.1105/tpc.106.047563 · Cited by 120
Čėnas, N., Prast‐Nielsen, S., Nivinskas, H., Šarlauskas, J., & Arnér, E. S. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m511972200 · Cited by 119
The Emerging Role of the Thioredoxin System in Angiogenesis
Dunn, L., Buckle, A., Cooke, J. P., & Ng, M. (2010) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.110.209643 · Cited by 119
Free Radicals and Reactive Oxygen Species
Kehrer, J. P., Robertson, J. D., & Smith, C. V. (2010) · Elsevier eBooks · doi:10.1016/b978-0-08-046884-6.00114-7 · Cited by 132
Salmonella Type III Secretion Effector SlrP Is an E3 Ubiquitin Ligase for Mammalian Thioredoxin
Bernal-Bayard, J., & Ramos‐Morales, F. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.010363 · Cited by 117
Effects of thioredoxin reductase-1 deletion on embryogenesis and transcriptome
Bondareva, A. A., Capecchi, M. R., Iverson, S. V., Li, Y., Lopez, N. I., Lucas, O., Merrill, G. F., Prigge, J. R., Siders, A. M., Wakamiya, M., et al. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.05.026 · Cited by 119
The Role of Thioredoxin Reductases in Brain Development
Soerensen, J., Jakupoglu, C., Beck, H., Förster, H., Schmidt, J., Schmahl, W., Schweizer, U., Conrad, M., & Brielmeier, M. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001813 · Cited by 120
The thioredoxin system in retroviral infection and apoptosis
Masutani, H., Ueda, S., & Yodoi, J. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401625 · Cited by 116
Beneficial Effects of Exercise Pretreatment in a Sporadic Alzheimer’s Rat Model
Wu, C., Yang, L., Tucker, D., Dong, Y., Zhu, L., Duan, R., Liu, T. C., & Zhang, Q. (2017) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0000000000001519 · Cited by 115
Mitochondrial Thioredoxin System
Patenaude, A., Murthy, M. R. V., & Mirault, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402496200 · Cited by 140
Nucleoredoxin, a Novel Thioredoxin Family Member Involved in Cell Growth and Differentiation
Funato, Y., & Miki, H. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1550 · Cited by 117
Pérez, V. I., Lew, C. M., Cortez, L. A., Webb, C. R., Rodriguez, M. R., Liu, Y.-H., Qi, W., Li, Y., Chaudhuri, A., Remmen, H. V., et al. (2008) · Free Radical Biology & Medicine · doi:10.1016/j.freeradbiomed.2007.11.018 · Cited by 118
Stress Induction and Mitochondrial Localization of Oxr1 Proteins in Yeast and Humans
Elliott, N., & Volkert, M. R. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.8.3180-3187.2004 · Cited by 111
Regulation of Cell Survival and Death by Pyridine Nucleotides
Oka, S., Hsu, C., & Sadoshima, J. (2012) · Circulation Research · doi:10.1161/circresaha.111.247932 · Cited by 113
Compartment-specific Control of Reactive Oxygen Species Scavenging by Antioxidant Pathway Enzymes
Dey, S., Sidor, A., & O'Rourke, B. P. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.726968 · Cited by 115
Cause or casualty: The role of mitochondrial DNA in aging and age-associated disease
Chocrón, E. S., Munkácsy, E., & Pickering, A. M. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.09.035 · Cited by 117
Reactive Oxygen Species and the Aging Eye
Babizhayev, M. A., & Yegorov, Y. E. (2010) · American Journal of Therapeutics · doi:10.1097/mjt.0b013e3181ea31ff · Cited by 105
Metadata
- Authors
- Nonn, L., Williams, R. R., Erickson, R. P., & Powis, G.
- Affiliations
- University of Arizona (US)
- Corresponding author
- Nonn, Larisa
- Powis, Garth
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2003-02-01
- Volume
- 23
- Issue
- 3
- Pages
- 916-922
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC140716
- OpenAlex
- W2061958603
- Cited by
- 438
- References
- 34
- Citations by year
- 2026: 7 · 2025: 2 · 2024: 9 · 2023: 11 · 2022: 13 · 2021: 14 · 2020: 13 · 2019: 16 · 2018: 17 · 2017: 19 · 2016: 20 · 2015: 28 · 2014: 17 · 2013: 17 · 2012: 18
- FWCI
- 8.50
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular and Cellular Biology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (CA 23074, R01CA077204, CA77204, P30CA023074)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- thioredoxin 2, mitochondrial thioredoxin, apoptosis, exencephaly, embryonic lethality, neural tube defects, oxidative phosphorylation, mitochondrial maturation, embryonic fibroblasts, heterozygous mice
- MeSH terms
- Animals, Female, Fetal Death, Gestational Age, Heterozygote, Homozygote, Membrane Proteins, Mice, Inbred C57BL, Mitochondria, Neural Tube Defects, Phenotype, Pregnancy, RNA, Messenger, Thioredoxins, Apoptosis, Mice, Knockout, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review