Dynamic redox control of NF-κB through glutaredoxin-regulated S-glutathionylation of inhibitory κB kinase β
Open accessAbstract
The transcription factor NF-κB, a central regulator of immunity, is subject to regulation by redox changes. We now report that cysteine-179 of the inhibitory κB kinase (IKK) β-subunit of the IKK signalosome is a central target for oxidative inactivation by means of S-glutathionylation. S-glutathionylation of IKK-β Cys-179 is reversed by glutaredoxin (GRX), which restores kinase activity. Conversely, GRX1 knockdown sensitizes cells to oxidative inactivation of IKK-β and dampens TNF-α-induced IKK and NF-κB activation. Primary tracheal epithelial cells from Glrx1 -deficient mice display reduced NF-κB DNA binding, RelA nuclear translocation, and MIP-2 (macrophage inflammatory protein 2) and keratinocyte-derived chemokine production in response to LPS. Collectively, these findings demonstrate the physiological relevance of the S-glutathionylation–GRX redox module in controlling the magnitude of activation of the NF-κB pathway.
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
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?
The IKK complex is a core component of NF-κB and a target of ROS, affecting NF-κB and S-glutathionylation and inhibited IKKβ activity.
“In addition, I-κB-Kinase (IKK) complex is the core component of NF-κB and is a target of ROS, affecting thus NF-κB and S-glutathionylation and inhibited IKKβ activity (Reynaert et al. 2006).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Reynaert et al. 2006
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
NOX enzymes and the biology of reactive oxygen
Lambeth, J. D. (2004) · Nature Reviews Immunology · doi:10.1038/nri1312 · Cited by 3,125 · see citing works
A cytokine-responsive IκB kinase that activates the transcription factor NF-κB
DiDonato, J. A., Hayakawa, M., Rothwarf, D. M., Zandi, E., & Karin, M. (1997) · Nature · doi:10.1038/41493 · Cited by 2,125 · see citing works
IKK-1 and IKK-2: Cytokine-Activated IκB Kinases Essential for NF-κB Activation
Mercurio, F., Zhu, H., Murray, B. W., Shevchenko, A., Bennett, B. L., Li, J. W., Young, D. B., Barbosa, M. S., Mann, M., Manning, A. M., et al. (1997) · Science · doi:10.1126/science.278.5339.860 · Cited by 2,042 · see citing works
Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IκB kinase
Rossi, A., Kapahi, P., Natoli, G., Takahashi, T., Chen, Y., Karin, M., & Santoro, M. G. (2000) · Nature · doi:10.1038/47520 · Cited by 1,310 · see citing works
IKK-γ is an essential regulatory subunit of the IκB kinase complex
Rothwarf, D. M., Zandi, E., Natoli, G., & Karin, M. (1998) · Nature · doi:10.1038/26261 · Cited by 958 · see citing works
Positive and Negative Regulation of IκB Kinase Activity Through IKKβ Subunit Phosphorylation
Delhase, M., Hayakawa, M., Chen, Y., & Karin, M. (1999) · Science · doi:10.1126/science.284.5412.309 · Cited by 852 · see citing works
Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD
Budanov, A. V., Sablina, A. A., Feinstein, E., Koonin, E. V., & Chumakov, P. M. (2004) · Science · doi:10.1126/science.1095569 · Cited by 731 · see citing works
Fernandes, A. P., & Holmgren, A. (2004) · Antioxidants and Redox Signaling · doi:10.1089/152308604771978354 · Cited by 670 · see citing works
S-Glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide
Adachi, T. K., Weisbrod, R. M., Pimentel, D. R., Ying, J., Sharov, V. S., Schöneich, C., & Cohen, R. A. (2004) · Nature Medicine · doi:10.1038/nm1119 · Cited by 662 · see citing works
Histone H3 phosphorylation by IKK-α is critical for cytokine-induced gene expression
Yamamoto, Y., Verma, U. N., Prajapati, S., Kwak, Y.-T., & Gaynor, R. B. (2003) · Nature · doi:10.1038/nature01576 · Cited by 577 · see citing works
Redox‐dependent signal transduction
Finkel, T. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01669-0 · Cited by 565 · see citing works
A nucleosomal function for IκB kinase-α in NF-κB-dependent gene expression
Anest, V., Ostrander, J. H., Cogswell, P. C., Steinbrecher, K. A., Strahl, B. D., & Baldwin, A. S. (2003) · Nature · doi:10.1038/nature01648 · Cited by 522 · see citing works
Kwok, B. H. B., Koh, B. D., Ndubuisi, M. I., Elofsson, M., & Crews, C. M. (2001) · Chemistry & Biology · doi:10.1016/s1074-5521(01)00049-7 · Cited by 516 · see citing works
Inhibition of NF- B DNA Binding by Nitric Oxide
Matthews, J. R., Botting, C. H., Panico, M., Morris, H. R., & Hay, R. T. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.12.2236 · Cited by 489 · see citing works
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
Pineda‐Molina, E., Klatt, P., Vázquez, J., Marina, A., de Lacoba, M. G., Pérez‐Sala, D., & Lamas, S. (2001) · Biochemistry · doi:10.1021/bi011459o · Cited by 389 · see citing works
Chang, T.-S., Jeong, W., Woo, H. A., Lee, S. M., Park, S., & Rhee, S. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409482200 · Cited by 388 · see citing works
Nitric oxide represses inhibitory κB kinase through S-nitrosylation
Reynaert, N. L., Ckless, K., Korn, S. H., Vos, N., Guala, A. S., Wouters, E. F. �., van der Vliet, A., & Janssen-Heininger, Y. M. W. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400588101 · Cited by 388 · see citing works
Self-citationKapahi, P., Takahashi, T., Natoli, G., Adams, S., Chen, Y., Tsien, R. Y., & Karin, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007204200 · Cited by 359 · 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
Reduction of Cysteine Sulfinic Acid by Sulfiredoxin Is Specific to 2-Cys Peroxiredoxins
Woo, H. A., Jeong, W., Chang, T., Park, K. J., Park, S. J., Yang, J. S., & Rhee, S. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400496200 · Cited by 331 · 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
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
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
Korn, S. H., Wouters, E. F. �., Vos, N., & Janssen-Heininger, Y. M. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104321200 · Cited by 200 · see citing works
Self-citationWu, R., & Smith, D. L. (1982) · In Vitro Cellular & Developmental Biology - Plant · doi:10.1007/bf02796504 · Cited by 181 · see citing works
Gold compound auranofin inhibits IκB kinase (IKK) by modifying Cys-179 of IKKβ subunit
Jeon, K., Byun, M.-S., & Jue, D. (2003) · Experimental & Molecular Medicine · doi:10.1038/emm.2003.9 · Cited by 173 · see citing works
Oxidative modification of H-ras: S-thiolation and S-nitrosylation of reactive cysteines
Mallis, R. J., Buss, J. E., & Thomas, J. A. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3550145 · Cited by 168 · see citing works
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
Demasi, M., Silva, G. M., & Netto, L. E. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209282200 · Cited by 126 · see citing works
IκB Kinases: Kinsmen with Different Crafts
May, M. J., & Ghosh, S. (1999) · Science · doi:10.1126/science.284.5412.271 · Cited by 125 · see citing works
Oxidative modification of H-ras: S-thiolation and S-nitrosylation of reactive cysteines
Mallis, R. J., Buss, J. E., & Thomas, J. A. (2001) · Biochemical Journal · doi:10.1042/bj3550145 · Cited by 113 · see citing works
Regulation of HIV-1 Protease Activity through Cysteine Modification
Davis, D. A., Dorsey, K. E., Wingfield, P. T., Stahl, S. J., Kaufman, J. D., Fales, H. M., & Levine, R. L. (1996) · Biochemistry · doi:10.1021/bi951525k · Cited by 99 · see citing works
Janssen-Heininger, Y. M. W., Driscoll, K. E., Howard, B. W., Quinlan, T. R., Treadwell, M. D., Barchowsky, A., & Mossman, B. T. (1997) · Europe PMC (PubMed Central) · Cited by 97 · see citing works
Self-citationPantano, C., Shrivastava, P., McElhinney, B., & Janssen-Heininger, Y. M. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308487200 · Cited by 80 · see citing works
Self-citationReynaert, N. L., Ckless, K., Guala, A. S., Wouters, E. F. �., van der Vliet, A., & Janssen-Heininger, Y. M. W. (2006) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2006.01.006 · Cited by 66 · see citing works
Self-citationSu, D., & Gladyshev, V. N. (2004) · Biochemistry · doi:10.1021/bi048478t · Cited by 58 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- Reynaert, N. L., Ckless, K., Korn, S. H., Vos, N., Guala, A. S., Wouters, E. F., van der Vliet, A. & Janssen-Heininger, Y. M. (2004) Proc. Natl. Acad. Sci. USA 101, 8945-8950.
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 · see citing works
Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging
Jomova, K., Raptova, R., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03562-9 · Cited by 2,638 · see citing works
Ros and ros-mediated cellular signaling
Zhang, J., Wang, X., Vikash, V., Ye, Q., Wu, D., Liu, Y., & Dong, W. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/4350965 · Cited by 1,980 · see citing works
Redox regulation of cell survival
Trachootham, D., Lu, W., Ogasawara, M. A., Valle, N. R.-D., & Huang, P. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1957 · Cited by 1,781 · see citing works
Redox metabolism: ROS as specific molecular regulators of cell signaling and function
Lennicke, C., & Cochemé, H. M. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.08.018 · Cited by 1,273 · see citing works
A Dynamic Pathway for Calcium-Independent Activation of CaMKII by Methionine Oxidation
Erickson, J. R., Joiner, M.-L. A., Guan, X., Kutschke, W., Yang, J., Oddis, C. V., Bartlett, R. K., Lowe, J. S., O'Donnell, S. E., Aykin-Burns, N., et al. (2008) · Cell · doi:10.1016/j.cell.2008.02.048 · Cited by 1,122 · 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
Iron homeostasis and oxidative stress: An intimate relationship
Galaris, D., Barbouti, A., & Pantopoulos, K. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.118535 · Cited by 922 · see citing works
Measurement and Clinical Significance of Biomarkers of Oxidative Stress in Humans
Marrocco, I., Fabio Altieri, F., & Peluso, I. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/6501046 · Cited by 874 · see citing works
Limón-Pacheco, J. H., & Gonsebatt, M. E. (2008) · Mutation Research/Genetic Toxicology and Environmental Mutagenesis · doi:10.1016/j.mrgentox.2008.09.015 · Cited by 842 · see citing works
Expanding the functional diversity of proteins through cysteine oxidation
Reddie, K. G., & Carroll, K. S. (2008) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2008.07.028 · Cited by 658 · see citing works
Protein S-glutathionylation: a regulatory device from bacteria to humans.
Dalle-Donne, I., Rossi, R., Colombo, G., Giustarini, D., & Milzani, A. (2009) · TIBS -Trends in Biochemical Sciences. Regular ed · doi:10.1016/j.tibs.2008.11.002 · Cited by 640 · see citing works
Jiang, T., Sun, Q., & Chen, S. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.07.005 · Cited by 594 · see citing works
Rouhier, N., Lemaire, S. D., & Jacquot, J. (2008) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.59.032607.092811 · Cited by 571 · 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 & Redox Signaling · doi:10.1089/ars.2008.2089 · Cited by 523 · see citing works
S-glutathionylation in protein redox regulation
Dalle‐Donne, I., Rossi, R., Giustarini, D., Colombo, R., & Milzani, A. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.06.014 · Cited by 498 · see citing works
Reactive Oxygen Species (ROS) Regulates Different Types of Cell Death by Acting as a Rheostat
Villalpando-Rodriguez, G. E., & Gibson, S. B. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/9912436 · Cited by 499 · 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
Oxidative stress, consequences and ROS mediated cellular signaling in rheumatoid arthritis
Phull, A. R., Nasir, B., Haq, I. U., & Kim, S. J. (2017) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2017.12.024 · Cited by 460 · see citing works
Molecular Biology of Atherosclerosis
Hopkins, P. N. (2013) · Physiological Reviews · doi:10.1152/physrev.00004.2012 · Cited by 456 · see citing works
Lee, H., Lee, Y. J., Choi, H., Ko, E. H., & Kim, J. W. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808742200 · Cited by 428 · see citing works
Reactive oxygen species and cell signaling. Review
Averill‐Bates, D. A. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2023.119573 · Cited by 412 · see citing works
Molecular biology of inflammation and sepsis: A primer*
Cinel, İ., & Opal, S. M. (2008) · Critical Care Medicine · doi:10.1097/ccm.0b013e31819267fb · Cited by 386 · see citing works
Thomas, S. R., Witting, P. K., & Drummond, G. R. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2027 · Cited by 383 · see citing works
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
Oxidative Stress and Iron Homeostasis: Mechanistic and Health Aspects
Galaris, D., & Pantopoulos, K. (2008) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360701713104 · Cited by 352 · see citing works
Lin, A., Wang, Y., Tang, J., Xue, P., Li, C., Liu, L., Hu, B., Yang, F., Loake, G. J., & Chu, C. (2011) · PLANT PHYSIOLOGY · doi:10.1104/pp.111.184531 · Cited by 346 · see citing works
Melatonin signaling and cell protection function
Luchetti, F., Canonico, B., Betti, M., Arcangeletti, M., Pilolli, F., Piroddi, M., Canesi, L., Papa, S., & Galli, F. (2010) · The FASEB Journal · doi:10.1096/fj.10-154450 · Cited by 343 · see citing works
Glutathione and modulation of cell apoptosis
Circu, M. L., & Aw, T. Y. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.06.019 · Cited by 333 · see citing works
Bidirectional regulation of NF-κB by reactive oxygen species: A role of unfolded protein response
Nakajima, S., & Kitamura, M. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.06.020 · Cited by 315 · see citing works
S-Glutathionylation: From Molecular Mechanisms to Health Outcomes
Xiong, Y., Uys, J. D., Tew, K. D., & Townsend, D. M. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3540 · Cited by 314 · see citing works
Causes and consequences of cysteine S-glutathionylation
Grek, C. L., Zhang, J., Manevich, Y., Townsend, D. M., & Tew, K. D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.461368 · Cited by 312 · see citing works
The Redox Biochemistry of Protein Sulfenylation and Sulfinylation
Conte, M. L., & Carroll, K. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.467738 · Cited by 305 · see citing works
Kaileh, M., Berghe, W. V., Heyerick, A., Horion, J., Piette, J. G., Libert, C., Keukeleire, D. D., Essawi, T. A., & Haegeman, G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606728200 · Cited by 303 · see citing works
ROS and RNS signalling: adaptive redox switches through oxidative/nitrosative protein modifications
Moldogazieva, N. T., Mokhosoev, I. M., Feldman, N. B., & Lutsenko, S. V. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1457217 · Cited by 291 · see citing works
Sadiq, I. Z. (2021) · Current Molecular Medicine · doi:10.2174/1566524022666211222161637 · Cited by 284 · see citing works
Redox Proteomics: Chemical Principles, Methodological Approaches and Biological/Biomedical Promises
Bachi, A., Dalle‐Donne, I., & Scaloni, A. (2012) · Chemical Reviews · doi:10.1021/cr300073p · Cited by 262 · see citing works
IκB kinase β (IKKβ/IKK2/IKBKB)—A key molecule in signaling to the transcription factor NF-κB
Schmid, J. A., & Birbach, A. (2008) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2008.01.006 · Cited by 260 · see citing works
Kalinina, E. V., Чернов, Н. Н., & Novichkova, M. (2014) · Biochemistry (Moscow) · doi:10.1134/s0006297914130082 · Cited by 258 · see citing works
Glutathione synthesis and its role in redox signaling
Zhang, H., & Forman, H. J. (2012) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2012.03.017 · Cited by 248 · see citing works
Glutathione S-Transferases in Cancer
Singh, R. R., & Reindl, K. M. (2021) · Antioxidants · doi:10.3390/antiox10050701 · Cited by 239 · see citing works
Wang, Y., Cheng, H., Wang, T., Zhang, K., Zhang, Y., & Kang, X. (2023) · Cell Proliferation · doi:10.1111/cpr.13448 · Cited by 239 · see citing works
CaMKII in the Cardiovascular System: Sensing Redox States
Erickson, J. R., He, B. J., Grumbach, I. M., & Anderson, M. E. (2011) · Physiological Reviews · doi:10.1152/physrev.00018.2010 · Cited by 238 · see citing works
Protein Damage by Reactive Electrophiles: Targets and Consequences
Liebler, D. C. (2007) · Chemical Research in Toxicology · doi:10.1021/tx700235t · Cited by 235 · see citing works
Salehi, B., Azzini, E., Zucca, P., Varoni, E. M., Kumar, N. V. A., Dini, L., Panzarini, E., Rajković, J., Fokou, P. V. T., Peluso, I., et al. (2020) · Applied Sciences · doi:10.3390/app10030947 · Cited by 234 · see citing works
The role of glutathione S-transferase P in signaling pathways and S-glutathionylation in cancer
Tew, K. D., Manevich, Y., Grek, C. L., Xiong, Y., Uys, J. D. K., & Townsend, D. M. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.04.013 · Cited by 233 · see citing works
Role of thiols in oxidative stress
Baba, S. P., & Bhatnagar, A. (2018) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2018.03.005 · Cited by 230 · see citing works
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
Redox signaling in cardiovascular health and disease
Madamanchi, N. R., & Runge, M. S. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.04.001 · Cited by 223 · see citing works
Metal-Based Photosensitizers as Inducers of Regulated Cell Death Mechanisms
Zhang, Y., Doan, B., & Gasser, G. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00161 · Cited by 214 · see citing works
The anti-inflammatory activity of curcumin is mediated by its oxidative metabolites
Edwards, R. L., Luis, P. B., Varuzza, P. V., Joseph, A. I., Presley, S. H., Chaturvedi, R., & Schneider, C. G. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.000123 · Cited by 209 · see citing works
Redox Regulation of Inflammation: Old Elements, a New Story
Lei, Y., Wang, K., Deng, L., Chen, Y., Nice, E. C., & Huang, C. (2014) · Medicinal Research Reviews · doi:10.1002/med.21330 · Cited by 208 · see citing works
S-Glutathionylation: Indicator of Cell Stress and Regulator of the Unfolded Protein Response
Townsend, D. M. (2007) · Molecular Interventions · doi:10.1124/mi.7.6.7 · Cited by 206 · see citing works
Reactive Oxygen Species in TNFα-Induced Signaling and Cell Death
Morgan, M. J., & Liu, Z.-G. (2010) · Molecules and Cells · doi:10.1007/s10059-010-0105-0 · Cited by 198 · see citing works
Redox Control of Skeletal Muscle Regeneration
Moal, E. L., Pialoux, V., Juban, G., Groussard, C., Zouhal, H., Chazaud, B., & Mounier, R. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6782 · Cited by 197 · see citing works
Redox control of cell proliferation
Chiu, J., & Dawes, I. W. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.08.002 · Cited by 193 · see citing works
NF-κB signaling pathway and free radical impact.
Siomek, A. (2012) · Acta Biochimica Polonica · doi:10.18388/abp.2012_2116 · Cited by 192 · see citing works
Role of nuclear glutathione as a key regulator of cell proliferation
Pallardó, F. V., Marković, J., García‐Giménez, J. L., & Viña, J. (2009) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2009.01.001 · Cited by 191 · 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
The Glutathione System: A New Drug Target in Neuroimmune Disorders
Morris, G., Anderson, G., Dean, O. M., Berk, M., Gałecki, P., Martín-Subero, M., & Maes, M. H. J. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8705-x · Cited by 187 · see citing works
Jiang, X., Yu, Y., Chen, J., Zhao, M., Chen, H., Song, X., Matzuk, A. J., Carroll, S. L., Tan, X., Sizovs, A., et al. (2014) · ACS Chemical Biology · doi:10.1021/cb500986w · Cited by 185 · see citing works
NADPH Oxidase Limits Innate Immune Responses in the Lungs in Mice
Segal, B. H., Han, W., Bushey, J. J., Joo, M., Bhatti, Z., Feminella, J., Dennis, C. G., Vethanayagam, R. R., Yull, F. E., Capitano, M. L., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009631 · Cited by 180 · see citing works
Moldogazieva, N. T., Lutsenko, S. V., & Terentiev, A. A. (2018) · Cancer Research · doi:10.1158/0008-5472.can-18-0980 · Cited by 177 · see citing works
Glutathionylation Acts as a Control Switch for Uncoupling Proteins UCP2 and UCP3
Mailloux, R. J., Seifert, E. L., Bouillaud, F., Aguer, C., Collins, S., & Harper, M.-E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.240242 · Cited by 174 · see citing works
Redox regulation of protein kinases
Truong, T. H., & Carroll, K. S. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.790873 · Cited by 172 · see citing works
Protein-Thiol Oxidation and Cell Death: Regulatory Role of Glutaredoxins
Allen, E. M. G., & Mieyal, J. J. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4644 · Cited by 164 · see citing works
Redox Regulation of Tumor Necrosis Factor Signaling
Han, D., Ybanez, M. D., Ahmadi, S., Yeh, K., & Kaplowitz, N. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2611 · Cited by 169 · see citing works
ROS signaling and redox biology in endothelial cells
Panieri, E., & Santoro, M. M. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1928-9 · Cited by 168 · see citing works
Mitochondrial Respiratory Complex I Regulates Neutrophil Activation and Severity of Lung Injury
Żmijewski, J. W., Lorne, E., Zhao, X., Tsuruta, Y., Sha, Y., Liu, G., Siegal, G. P., & Abraham, E. H. (2008) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200710-1602oc · Cited by 167 · see citing works
Akhtar, M. J., Ahamed, M., Alhadlaq, H. A., & Alshamsan, A. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.01.018 · Cited by 166 · see citing works
Withaferin A inhibits NF-kappaB activation by targeting cysteine 179 in IKKβ
Heyninck, K., Lahtela-Kakkonen, M. K., der Veken, P. V., Haegeman, G., & Berghe, W. V. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.08.004 · Cited by 164 · see citing works
S-Glutathionylation signaling in cell biology: Progress and prospects
Pastore, A., & Piemonte, F. (2012) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2012.03.010 · Cited by 163 · see citing works
Glutathione Supplementation Potentiates Hypoxic Apoptosis by S-Glutathionylation of p65-NFκB
Qanungo, S., Starke, D. W., Pai, H. V., Mieyal, J. J., & Nieminen, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610934200 · Cited by 160 · see citing works
Glutathionylation in the Photosynthetic Model Organism Chlamydomonas reinhardtii: A Proteomic Survey
Zaffagnini, M., Bedhomme, M., Groni, H., Marchand, C. H., Puppo, C., Gontero, B., Cassier‐Chauvat, C., Decottignies, P., & Lemaire, S. D. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.014142 · Cited by 158 · see citing works
Yang, L., Jin, M., Wang, Y., Zhu, J., Tan, R., Zhao, J., Ji, X., Jin, C., Jia, Y., Ren, T., et al. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0155-5 · Cited by 158 · see citing works
Redox Control of the Survival of Healthy and Diseased Cells
Zhang, Y., Du, Y., Le, W., Wang, K., Kieffer, N., & Zhang, J. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3685 · Cited by 156 · see citing works
Redox regulation of neuronal survival mediated by electrophilic compounds
Satoh, T., & Lipton, S. A. (2006) · Trends in Neurosciences · doi:10.1016/j.tins.2006.11.004 · Cited by 154 · see citing works
Reversible and irreversible protein glutathionylation: biological and clinical aspects
Cooper, A. J. L., Pinto, J., & Callery, P. (2011) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1517/17425255.2011.577738 · Cited by 148 · see citing works
Reactive oxygen species and protein modifications in spermatozoa†
O’Flaherty, C., & Matsushita-Fournier, D. (2017) · Biology of Reproduction · doi:10.1093/biolre/iox104 · Cited by 149 · see citing works
Rehder, D. S., & Borges, C. R. (2010) · Biochemistry · doi:10.1021/bi1008694 · Cited by 148 · see citing works
Macrophage inflammatory protein-2 as mediator of inflammation in acute liver injury
Qin, C.-C., Liu, Y.-N., Hu, Y., Yang, Y., & Chen, Z. J. (2017) · World Journal of Gastroenterology · doi:10.3748/wjg.v23.i17.3043 · Cited by 148 · 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
Reddy, N. M., Kleeberger, S. R., Bream, J. H., Fallon, P. G., Kensler, T. W., Yamamoto, M. P., & Reddy, S. P. (2008) · Oncogene · doi:10.1038/onc.2008.188 · Cited by 141 · see citing works
Regulation of innate immunity by NADPH oxidase
Segal, B. H., Grimm, M. J., Khan, A. N. H., Han, W., & Blackwell, T. S. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.04.022 · Cited by 139 · see citing works
Prescott, J. A., & Cook, S. J. (2018) · Cells · doi:10.3390/cells7090115 · Cited by 139 · see citing works
Redox Regulation via Glutaredoxin-1 and Protein S -Glutathionylation
Matsui, R., Ferrán, B., Oh, A., Croteau, D., Shao, D., Han, J., Pimentel, D. R., & Bachschmid, M. M. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7963 · Cited by 139 · see citing works
Zhou, Z., Ni, K., Deng, H., & Chen, X. S. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.06.006 · Cited by 139 · 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
Regulation by Reversible S-Glutathionylation: Molecular Targets Implicated in Inflammatory Diseases
Shelton, M. D., & Mieyal, J. J. (2008) · Molecules and Cells · doi:10.1016/s1016-8478(23)17590-x · Cited by 135 · see citing works
Gonzalez‐Dosal, R., Horan, K., Rahbek, S. H., Ichijo, H., Chen, Z. J., Mieyal, J. J., Hartmann, R., & Paludan, S. R. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002250 · Cited by 134 · see citing works
Anathy, V., Aesif, S. W., Guala, A. S., Havermans, M., Reynaert, N. L., Ho, Y.-S., Budd, R. C., & Janssen-Heininger, Y. M. W. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200807019 · Cited by 134 · see citing works
Self-citationReiniers, M. J., van Golen, R. F., van Gulik, T. M., & Heger, M. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5486 · Cited by 131 · see citing works
Nuclear Factor κB, Airway Epithelium, and Asthma: Avenues for Redox Control
Janssen-Heininger, Y. M. W., Poynter, M. E., Aesif, S. W., Pantano, C., Ather, J. L., Reynaert, N. L., Ckless, K., Anathy, V., van der Velden, J. L. J., Irvin, C. G., et al. (2009) · Proceedings of the American Thoracic Society · doi:10.1513/pats.200806-054rm · Cited by 128 · see citing works
Self-citationGlutathione during embryonic development
Hansen, J. M., & Harris, C. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.12.001 · Cited by 127 · see citing works
Checker, R., Sharma, D., Sandur, S. K., Subrahmanyam, G., Krishnan, S., Poduval, T. B., & Sainis, K. B. (2010) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22620 · Cited by 127 · see citing works
Xie, Y., Kole, S., Precht, P., Pazin, M. J., & Bernier, M. (2009) · Endocrinology · doi:10.1210/en.2008-1241 · Cited by 126 · see citing works
Qu, Y., Wang, J., Ray, P., Guo, H. B., Huang, J., Shin-Sim, M., Bukoye, B. A., Liu, B., Lee, A. V., Lin, X., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci43144 · Cited by 126 · see citing works
Glutaredoxin Regulates Nuclear Factor κ-B and Intercellular Adhesion Molecule in Müller Cells
Shelton, M. D., Kern, T. S., & Mieyal, J. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610863200 · Cited by 126 · see citing works
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
Mitochondrial proticity and ROS signaling: lessons from the uncoupling proteins
Mailloux, R. J., & Harper, M. (2012) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2012.04.004 · Cited by 122 · see citing works
- Authors
- Reynaert, N. L., van der Vliet, A., Guala, A. S., McGovern, T., Hristova, M., Pantano, C., Heintz, N. H., Heim, J., Ho, Y.-S., Matthews, D. E., Wouters, E. F. M., & Janssen-Heininger, Y. M. W.
- Affiliations
- Maastricht University (NL)
- Departments of *Pathology and
- University of Vermont (US)
- Wayne State University (US)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2006-08-29
- Volume
- 103
- Issue
- 35
- Pages
- 13086-13091
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC1559757
- OpenAlex
- W2166902551
- Cited by
- 442
- References
- 37
- Citations by year
- 2026: 19 · 2025: 12 · 2024: 19 · 2023: 19 · 2022: 18 · 2021: 20 · 2020: 23 · 2019: 23 · 2018: 13 · 2017: 25 · 2016: 18 · 2015: 24 · 2014: 22 · 2013: 28 · 2012: 29
- FWCI
- 9.51
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Research Publications (Maastricht University) (submittedVersion, other-oa)
- Funders
- National Institutes of Health (P20 RL15557)
- U.S. Public Health Service (P20 RL-15557)
- National Heart, Lung, and Blood Institute (R01 HL60014, P01 HL074295, R01HL074295, R01HL060812, R01HL060014, HL 60812)
- National Center for Research Resources (P20RR015557)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
- Keywords
- NF-κB, S-glutathionylation, glutaredoxin, redox regulation, oxidative inactivation, TNF signaling, tracheal epithelial cells, lipopolysaccharide response, chemokine production, p65 nuclear translocation
- MeSH terms
- Animals, Cells, Cultured, Cysteine, Glutathione, Hydrogen Peroxide, Lipopolysaccharides, Mice, Inbred C57BL, Oxidation-Reduction, Oxidoreductases, Respiratory System, Sulfenic Acids, Keratinocytes, Monokines, NF-kappa B, Chemokines, Protein Subunits, Mice, I-kappa B Kinase, Chemokine CXCL2, Glutaredoxins
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
