The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
Transcription Factor Nrf2 Regulates Inflammation by Mediating the Effect of 15-Deoxy-Δ12,14-Prostaglandin J2
Open accessAbstract
Activated macrophages express high levels of Nrf2, a transcription factor that positively regulates the gene expression of antioxidant and detoxication enzymes. In this study, we examined how Nrf2 contributes to the anti-inflammatory process. As a model system of acute inflammation, we administered carrageenan to induce pleurisy and found that in Nrf2-deficient mice, tissue invasion by neutrophils persisted during inflammation and the recruitment of macrophages was delayed. Using an antibody against 15-deoxy-Delta(12,14)-prostaglandin J(2) (15d-PGJ(2)), it was observed that macrophages from pleural lavage accumulate 15d-PGJ(2). We show that in mouse peritoneal macrophages 15d-PGJ(2) can activate Nrf2 by forming adducts with Keap1, resulting in an Nrf2-dependent induction of heme oxygenase 1 and peroxiredoxin I (PrxI) gene expression. Administration of the cyclooxygenase 2 inhibitor NS-398 to mice with carrageenan-induced pleurisy caused persistence of neutrophil recruitment and, in macrophages, attenuated the 15d-PGJ(2) accumulation and PrxI expression. Administration of 15d-PGJ(2) into the pleural space of NS-398-treated wild-type mice largely counteracted both the decrease in PrxI and persistence of neutrophil recruitment. In contrast, these changes did not occur in the Nrf2-deficient mice. These results demonstrate that Nrf2 regulates the inflammation process downstream of 15d-PGJ(2) by orchestrating the recruitment of inflammatory cells and regulating the gene expression within those cells.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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
“Nrf2 plays a role in regulating the anti-inflammatory response through redox control and activation of ARE-mediated anti-inflammatory genes, including the expression of the antioxidant genes NQO1, HO-1, and PRX1, all of which exhibit anti-inflammatory effects [191,192,193,194].”
From Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease (2022) · cites this paper as [194]
Citations
Cites
Inhibition of Prostaglandin Synthesis as a Mechanism of Action for Aspirin-like Drugs
VANE, J. R. (1971) · Nature New Biology · doi:10.1038/newbio231232a0 · Cited by 8,605
Itoh, K., Chiba, T., Takahashi, S., Ishii, T., Igarashi, K., Katoh, Y., Oyake, T., Hayashi, N., Satoh, K., Hatayama, I., et al. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6943 · Cited by 3,999
Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., Igarashi, K., Engel, J. D., & Yamamoto, M. (1999) · Genes & Development · doi:10.1101/gad.13.1.76 · Cited by 3,634
Self-citationThe peroxisome proliferator-activated receptor-γ is a negative regulator of macrophage activation
Ricote, M., Li, A. C., Willson, T. M., Kelly, C. J., & Glass, C. K. (1998) · Nature · doi:10.1038/34178 · Cited by 3,525
PPAR-γ agonists inhibit production of monocyte inflammatory cytokines
Jiang, C., Ting, A. T., & Seed, B. (1998) · Nature · doi:10.1038/34184 · Cited by 2,899
Points of control in inflammation
Nathan, C. (2002) · Nature · doi:10.1038/nature01320 · Cited by 2,738
Carbon monoxide has anti-inflammatory effects involving the mitogen-activated protein kinase pathway
Otterbein, L. E., Bach, F. H., Alam, J., Soares, M., Tao Lu, H., Wysk, M., Davis, R. J., Flavell, R. A., & Choi, A. M. K. (2000) · Nature Medicine · doi:10.1038/74680 · Cited by 2,153
Dinkova-Kostova, A. T., Holtzclaw, W. D., Cole, R. N., Itoh, K., Wakabayashi, N., Katoh, Y., Yamamoto, M., & Talalay, P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172398899 · Cited by 1,947
Self-citationSeibert, K., Zhang, Y., Leahy, K., Hauser, S. D., Masferrer, J. L., Perkins, W., Lee, L., & Isakson, P. C. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.12013 · Cited by 1,551
Warner, T. D., Giuliano, F., Vojnovic, I., Bukasa, A., Mitchell, J. A., & Vane, J. R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.13.7563 · Cited by 1,521
Flagged first, then by citations
Research works printed but not linked: 1
- Narumiya S., 1987, J. Pharmacol. Exp. Ther., 242, 306
Cited by
Sorted by citations
Items 301–400 of 406
Chigusa, Y., Kishore, A. H., Mogami, H., & Word, R. A. (2016) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2016-1059 · Cited by 21
Silva, Á. J. C., & de Lavor, M. S. L. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26052050 · Cited by 21
Redox-dependent signaling system Nrf2/ARE in inflammation
Брониславовна, М. Е., Tkachev, V., & Зенков, Н. К. (2010) · Molecular Biology · doi:10.1134/s0026893310030015 · Cited by 20
Ano, S., Panariti, A., Allard, B., O’Sullivan, M. J., McGovern, T. K., Hamamoto, Y., Ishii, Y., Yamamoto, M. P., Powell, W. S., & Martin, J. G. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.11.017 · Cited by 20
Self-citationChang, J. Y., Bora, P. S., & Bora, N. S. (2008) · PPAR Research · doi:10.1155/2008/720163 · Cited by 20
Kelly, V. P., Suzuki, T., Nakajima, O., Arai, T., Tamai, Y., Takahashi, S., Nishimura, S., & Yamamoto, M. P. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.9.3658-3669.2005 · Cited by 20
Self-citationKo, S., Ko, H.-A., Shieh, T., Chi, T.-C., Chen, H., Chen, Y., Yu, Y.-H., Yang, S.-H., & Chang, S.-S. (2017) · Oncology Letters · doi:10.3892/ol.2017.5809 · Cited by 20
NRF2 signaling in cytoprotection and metabolismPreprint
Murakami, S., Kusano, Y., Okazaki, K., Akaike, T., & Motohashi, H. (2023) · doi:10.22541/au.168872044.49044735/v1 · Cited by 20
Shimizu, S., Saito, M., Oiwa, H., Ohmasa, F., Tsounapi, P., Oikawa, R., Dimitriadis, F., Martin, D. T., Satoh, I., Kinoshita, Y., et al. (2013) · Neurourology and Urodynamics · doi:10.1002/nau.22405 · Cited by 19
Choi, W., Jeong, J., Kim, S. O., Kim, G., Kim, B., Kim, C. M., Seo, Y.-B., Kim, W., Lee, S. Y., JO, K.-H., et al. (2014) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2014.1881 · Cited by 19
Ishii‐Osai, Y., Yamashita, T., Tamura, Y., Sato, N., Itô, A., Honda, H., Wakamatsu, K., Ito, S., Nakayama, E., Okura, M., et al. (2012) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2012.04.009 · Cited by 19
Fröde, T. S., Buss, Z. D. S., dos Reis, G. O., & Medeiros, Y. S. (2009) · International Immunopharmacology · doi:10.1016/j.intimp.2009.08.011 · Cited by 19
Chang, J. Y., & Tsai, P. (2008) · NeuroToxicology · doi:10.1016/j.neuro.2008.08.003 · Cited by 18
“This compound is normally present in tissues at low levels ( 1 nM), but can reach high concentrations during infection and inflammation (Gilroy et al., 1999, Itoh et al., 2004).”
BackgroundRana, R., Mukherjee, R., Mehan, S., Khan, Z., Gupta, G. D., & Narula, A. S. (2025) · Behavioural Brain Research · doi:10.1016/j.bbr.2025.115545 · Cited by 17
Jin, H., Li, Y., Shen, K., Li, J., Yu, F., & Yang, Z. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.104811 · Cited by 17
Pensabene, K. M., LaMorte, J. P., Allender, A., Wehr, J., Kaur, P., Savage, M., & Eggler, A. L. (2023) · Antioxidants · doi:10.3390/antiox12091735 · Cited by 16
“Due to its short half-life of ~20 min [35], NRF2 protein rapidly accumulates when its degradation is blocked, allowing NRF2 protein synthesis activity to be measured by the extent of NRF2 accumulation (Figure 2A, first two lanes).”
BackgroundDuarte, S., Melo, T., Domingues, R., Ramírez, J. D. D. A., & Pérez‐Sala, D. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.06.003 · Cited by 16
Wung, B., Wu, C., Hsu, M. C., & Hsieh, C. (2006) · Life Sciences · doi:10.1016/j.lfs.2005.12.013 · Cited by 16
Zhang, H., Tanji, K., Yoshida, H., Hayakari, M., Shibata, T., Mori, F., Uchida, K., & Wakabayashi, K. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2010.01.007 · Cited by 17
“Indeed, 15d-PGJ2 covalently binds to IκB kinase and Keap1 (Itoh et al., 2004; Rossi et al., 2000), resulting in altered protein complex and activation of NF-κB and Nrf2-related genes that play a role in inflammation and oxidative stress responses.”
Self-citationFerroptosis plays a novel role in nonalcoholic steatohepatitis pathogenesis
Xiong, F., Zhou, Q., Huang, X., Cao, P., & Wang, Y. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1055793 · Cited by 15
Speciale, A., Molonia, M. S., Muscarà, C., Cristani, M., Salamone, F. L., Saija, A., & Cimino, F. (2024) · Fitoterapia · doi:10.1016/j.fitote.2024.105953 · Cited by 17
Pulmonary Arterial Hypertension
McLaughin, V., & Hoeper, M. M. (2005) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.2503002 · Cited by 15
DHA sensitizes FaO cells to tert-BHP-induced oxidative effects. Protective role of EGCG
Fernández‐Iglesias, A., Quesada, H., Díaz, S., Reguera, D. P., Bladé, C., Arola, L., Salvadó, M. J., & Mulero, M. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.10.013 · Cited by 14
Redox Sensitive Transcription via Nrf2-Keap1 in Suppression of Inflammation
Bhakkiyalakshmi, E., Sireesh, D., & Ramkumar, K. M. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-805417-8.00012-3 · Cited by 14
Gioia, M. D., Poli, V., Tan, P. J., Spreafico, R., Chu, A., Cuenca, A. G., Wu, Z., Benamar, M., Pandolfi, L., Meloni, F., et al. (2025) · Immunity · doi:10.1016/j.immuni.2025.06.017 · Cited by 13
Liver Growth Factor “LGF” as a Therapeutic Agent for Alzheimer’s Disease
Gonzalo‐Gobernado, R., Perucho, J., Vallejo-Muñoz, M., Casarejos, M. J., Reimers, D., Jiménez‐Escrig, A., Gómez, A., de Asanza, G. M. U., & Bazán, E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239201 · Cited by 13
Mathew, G., & Unnikrishnan, M. K. (2015) · Inflammation Research · doi:10.1007/s00011-015-0851-8 · Cited by 13
PGD2 and PGE2 regulate gene expression of Prx 6 in primary macrophages via Nrf2
Erttmann, S. F., Bast, A., Seidel, J., Breitbach, K., Walther, R., & Steinmetz, I. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.05.022 · Cited by 13
Properties of macerated herbal oil
Kantawong, F., Singhatong, S., Aomjai, A., Boonyuen, K., Mooti, N., Wanachantararak, P., & Kuboki, T. (2017) · Bioimpacts · doi:10.15171/bi.2017.03 · Cited by 13
Nrf2 in Host Defense: Over the Rainbow
Cho, H., Kwak, M., & Pi, J. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/975839 · Cited by 13
Delivery strategies to improve the pharmacological efficacy of NRF2 modulators: a review
Bayındır, Z. S., Sova, M., Yüksel, N., & Saso, L. (2025) · RSC Medicinal Chemistry · doi:10.1039/d5md00571j · Cited by 13
Hu, Q., Zhang, J., Luo, X., Hu, P., Li, J., Li, F., Wang, Z., Zhang, S., Jiao, Z., Liu, Y., et al. (2025) · Circulation · doi:10.1161/circulationaha.124.070936 · Cited by 13
Li, X., Luo, B., Wang, L. J., Zhang, W., & Liu, Z. G. (2015) · Genetics and Molecular Research · doi:10.4238/2015.october.29.22 · Cited by 12
“15d-PGJ2 possesses anti-inflammatory properties, and plays a protective role against oxidative stress both in vitro and in vivo (Giri et al., 2004; Itoh et al., 2004; Qin et al., 2006).”
BackgroundHung, H.-C., Feng, C., Lin, Y., Chen, C., Tsui, K., Chen, W.-F., Pan, C., Sheu, J., Sung, C., & Wen, Z. (2018) · Experimental & Molecular Medicine · doi:10.1038/emm.2017.272 · Cited by 12
Linetsky, M. D., Bondelid, K. S., Losovskiy, S., Gabyak, V., Rullo, M. J., Stiadle, T. I., Munjapara, V., Saxena, P., Ma, D., Cheng, Y.-S., et al. (2018) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.8b00028 · Cited by 12
Niino, T., Tago, K., Yasuda, D., Takahashi, K., Mashino, T., Tamura, H., & Funakoshi‐Tago, M. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.06.021 · Cited by 12
Im, N.-K., Zhou, W. P., Na, M., & Jeong, G. (2014) · International Immunopharmacology · doi:10.1016/j.intimp.2014.12.014 · Cited by 11
RetractedSong, C., Kim, N., Nam, R. H., Choi, S. I., Kang, C., Jang, J. Y., Nho, H., Shin, E. H., & Lee, H. (2021) · Journal of Cancer Prevention · doi:10.15430/jcp.2021.26.1.41 · Cited by 11
“Nrf2 is a key modulator of the adaptive response to a variety of environmental and endogenous stresses [32-36].”
BackgroundManandhar, S., You, A., Lee, E.-S., Kim, J., & Kwak, M. (2008) · Journal of Pharmacy and Pharmacology · doi:10.1211/jpp.60.7.0009 · Cited by 11
Choo, J., Heo, G., Kim, S. J., Lee, Y., Ishigami, A., Maruyama, N., Chung, H. Y., & Im, E. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.09.031 · Cited by 11
Oxygen needs sulfur, sulfur needs oxygen: a relationship of interdependence
Sekine, H., Akaike, T., & Motohashi, H. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00464-7 · Cited by 11
Lee, S. C., Kwon, Y., Park, J.-Y., Park, S. Y., Lee, J., & Park, S.-D. (2017) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2017/1725246 · Cited by 10
“Furthermore, HO-1, a gene targeted by Nrf2 in macrophages, is considered to have anti-inflammatory roles [32, 33].”
BackgroundNrf2 attenuates the innate immune response after experimental myocardial infarction
Bromage, D. I., Trevelin, S. C., Huntington, J., Yang, V. X., Muthukumar, A., Mackie, S., Sawyer, G. J., Zhang, X., Santos, C. X. C., Safinia, N., et al. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.03.043 · Cited by 9
Saikosaponins: A Review of Structures and Pharmacological Activities
Jia, A., Yang, X.-H., Zou, B., Li, J., Wang, Y., Ma, R., Li, J., & Yao, Y. (2022) · Natural Product Communications · doi:10.1177/1934578x221094908 · Cited by 10
Ding, Y., Haks, M. C., Forn‐Cuní, G., He, J., Nowik, N., Harms, A. C., Hankemeier, T., Eeza, M. N. H., Matysik, J., Alia, A., et al. (2021) · Cell & Bioscience · doi:10.1186/s13578-021-00642-0 · Cited by 10
“Genes MAP2K6 and Nfe2l2 were added to the pathway based on literature [57, 58].”
BackgroundGenotoxic Properties of Cyclopentenone Prostaglandins and the Onset of Glutathione Depletion
Solecki, G. M., Groh, I. A. M., Kajzar, J., Haushofer, C., Scherhag, A., Schrenk, D., & Esselen, M. (2013) · Chemical Research in Toxicology · doi:10.1021/tx300435p · Cited by 10
Park, S. R., Kim, K. H., Kwun, M. J., Lee, J. Y., Won, R., Han, C. W., Choi, J., & Joo, M. (2018) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2018/5059469 · Cited by 10
“For instance, Nrf2 KO mice were found to be more susceptible to developing lupus-like autoimmune nephritis [16], a greater lung inflammation in response to LPS and TNF-α [14], and a prolonged neutrophil infiltration into the inflammatory sites [17].”
BackgroundChowdhury, S., Mukhopadhyay, R., Saha, S. T., Mishra, A., Sengupta, S., Roy, S., & Majumder, H. K. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.539742 · Cited by 9
“The action of Keap1 is analogous to that of IK B, which prevents activation and translocation of transcription factor NF B (55, 56).”
BackgroundMacías‐Barragán, J., Caligiuri, A., Garcia-Bañuelos, J. J., Parola, M., Pinzani, M., & Armendáriz‐Borunda, J. (2014) · Revista médica de Chile · doi:10.4067/s0034-98872014001200009 · Cited by 9
Abraki, S. B., Khalaj, L., Shaerzadeh, F., & Khodagholi, F. (2012) · Journal of Molecular Neuroscience · doi:10.1007/s12031-012-9903-5 · Cited by 9
“It is reported that HO-1 is activated by 15d-PGJ2 through the Nrf2 mechanism and mediated by the stress-responsive element (Itoh et al. 2004; Gong et al. 2002).”
InfluentialNRF2-Mediated Gene Regulation and Glucose Homeostasis
Yagishita, Y., Uruno, A., & Yamamoto, M. P. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-801585-8.00027-0 · Cited by 10
Self-citationMathew, G., Sharma, A., Pickering, R. J., Rosado, C. J., Lemarie, J., Mudgal, J., Thambi, M., Sebastian, S., Jandeleit-Dahm, K. A. M., de Haan, J. B., et al. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1533636 · Cited by 9
Regulatory Role of the COX-2 Pathway in the Nrf2-Mediated Anti-Inflammatory Response
Itoh, K., & Yamamoto, M. P. (2005) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.37.9 · Cited by 9
Self-citationAlcohol abuse is associated with enhanced pulmonary and systemic xanthine oxidoreductase activity
Fini, M. A., Gaydos, J., McNally, A., Karoor, V., & Burnham, E. L. (2017) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00570.2016 · Cited by 8
Glutathione S-Transferases as Modulators of Signal Transduction
Awasthi, Y. C. (2006) · CRC Press eBooks · doi:10.1201/9781420004489-13 · Cited by 8
Nrf2 in Immune Responses During Inflammation
Hohmann, M. S., Zaninelli, T. H., Staurengo‐Ferrari, L., Manchope, M. F., Badaro‐Garcia, S., de Freitas, A., Casagrande, R., & Verri, W. A., Jr. (2020) · Progress in inflammation research · doi:10.1007/978-3-030-44599-7_2 · Cited by 7
Rissel, R., Gosling, M., Kamuf, J., Renz, M., Ruemmler, R., Ziebart, A., & Hartmann, E. K. (2022) · Biomedicines · doi:10.3390/biomedicines10051031 · Cited by 7
Deramaudt, T. B., Chehaitly, A., Charrière, T., Arnaud, J., & Bonay, M. (2023) · Antioxidants · doi:10.3390/antiox12091695 · Cited by 8
“Animals and Isolation of Primary Mouse Alveolar Macrophages Breeding of the C57BL/6J Nrf2 knockout (Nrf2−/−) mouse strain, provided by Dr Yamamoto (Tohoku University) and purchased from Riken BRC [20], was conducted according to National and European legislation and institutional guidelines for the care and use of lab…”
MethodFrom germ cells to neonates: the beginning of life and the KEAP1–NRF2 system
Matsumaru, D., & Motohashi, H. (2019) · The Journal of Biochemistry · doi:10.1093/jb/mvz070 · Cited by 7
The role of Nrf2 in autoimmunity and infectious disease: Therapeutic possibilities
Freeborn, R. A., & Rockwell, C. E. (2021) · Advances in pharmacology · doi:10.1016/bs.apha.2020.10.003 · Cited by 7
Physiological Substrates of Glutathione S-Transferases
Sharma, R., Ansari, G. S., & Awasthi, S. (2006) · Informa Healthcare eBooks · doi:10.1201/9781420004489.ch9 · Cited by 7
Physiological Substrates of Glutathione S-Transferases
Awasthi, Y. C. (2006) · CRC Press eBooks · doi:10.1201/9781420004489-12 · Cited by 7
Uhlig, S. (2005) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.2503003 · Cited by 7
Nrf2 deficiency in muscle attenuates experimental autoimmune myositis‐induced muscle weakness
Himori, K., Yamada, M., Onoki, T., Matsumaru, D., Motohashi, H., & Okutsu, M. (2024) · The Journal of Physiology · doi:10.1113/jp286534 · Cited by 6
Ganesh, G. V., Ganesan, K., Xu, B., & Ramkumar, K. M. (2022) · BioFactors · doi:10.1002/biof.1867 · Cited by 6
Uruno, A., Kadoguchi, S., Saito, R., Koiso, S., Saigusa, D., Chu, C., Suzuki, T., Saito, T., Saido, T. C., Cuadrado, A., et al. (2024) · The Journal of Biochemistry · doi:10.1093/jb/mvae060 · Cited by 7
Self-citationIshida, N., Aoki, Y., Katsuoka, F., Nishijima, I., Nobukuni, T., Anzawa, H., Li, B., Tsuda, M., Kumada, K., Kudo, H., et al. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.09.023 · Cited by 6
Self-citationYuan, B., Jin, X., Li, C., Shen, Y., Tian, J., & Duan, S. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1806176 · Cited by 6
“Consistent with these findings, NRF2-deficient mice exhibit exaggerated inflammatory responses in multiple inflammation models (Itoh et al., 2004; Ishii et al., 2005).”
Lactobacillus species modulates TNF-α and Nrf2 expression in carrageenan-induced rat paw oedema
Oladejo, B. O., Akingbade, G. T., Adeboboye, C. F., & Adeoye, S. B. (2024) · The Microbe · doi:10.1016/j.microb.2024.100050 · Cited by 6
Kang, E. S., Hwang, J. S., Ham, S. A., Park, M. H., Kim, G. H., Paek, K. S., Yoo, T., Lee, W. J., Kang, K. R., Lee, J. H., et al. (2013) · Free Radical Research · doi:10.3109/10715762.2013.860224 · Cited by 5
Nilsson, L. L., Palm, F., & Nørregaard, R. (2017) · Mediators of Inflammation · doi:10.1155/2017/3924912 · Cited by 5
Guan, R., Wen, X., Leung, C. H., Ciano‐Oliveira, C. D., Lam, S., Dai, S. Y., Karbassi, F., Mauro, A., Wang, Y., & Rotstein, O. D. (2021) · PLoS ONE · doi:10.1371/journal.pone.0260442 · Cited by 5
The KEAP1-NRF2 system and neurodegenerative diseases
Uruno, A., & Yamamoto, M. P. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0005 · Cited by 8
Self-citationGlutathione S-Transferases as Modulators of Signal Transduction
Yang, Y., & Awasthi, S. (2006) · Informa Healthcare eBooks · doi:10.1201/9781420004489.ch10 · Cited by 5
Gioia, M. D., Poli, V., Tan, P. J., Spreafico, R., Chu, A., Cuenca, A. G., Gordts, P. L. S. M., Pandolfi, L., Meloni, F., Witztum, J. L., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.21.568047 · Cited by 5
Molecular Mechanisms of Nrf2 in Inflammation: Interactions Between Nrf2 and Inflammatory Mediators
Wang, R., & Pérez, V. (2020) · Progress in inflammation research · doi:10.1007/978-3-030-44599-7_1 · Cited by 3
Hashimoto, H., Okazaki, T., Honkura, Y., Ren, Y., Ngamsnae, P., Hisaoka, T., Koshiba, Y., Suzuki, J., Ebihara, S., & Katori, Y. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252111829 · Cited by 3
Metabolism and Roles of Eicosanoids in Brain
Farooqui, A. A. (2011) · Springer eBooks · doi:10.1007/978-1-4419-9940-5_1 · Cited by 3
Inflammation, a Key Factor in Cancer Ambush
Amjadi, O., Rafiei, A., Ajami, A., Hosseini, V., & Asgarian‐Omran, H. (2014) · Research in Molecular Medicine · doi:10.18869/acadpub.rmm.2.2.1 · Cited by 3
Takatani, N., Miyafusa, H., Yamano, Y., Beppu, F., & Hosokawa, M. (2024) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2024.110125 · Cited by 2
Žagar, A. M., Kolobarić, N., Šušnjara, P., Mihaljević, J., Mihaljević, Z., & Drenjancevic, I. (2026) · Life · doi:10.3390/life16040642 · Cited by 2
Cytoprotection Against Oxidative Damage by Nrf2-regulated Genes
Kwak, M., & Kensler, T. W. (2007) · Toxicological Research · doi:10.5487/tr.2007.23.3.207 · Cited by 2
Kim, K., Park, J., Kim, N., Kim, S., Moon, H., An, H., Lee, J., Park, H., Surh, Y., & Suh, Y. (2016) · ChemBioChem · doi:10.1002/cbic.201600165 · Cited by 2
Nrf2 and Inflammation-Triggered Carcinogenesis
Sarkar, S., Ghosh, N., Kundu, M., & Sil, P. C. (2020) · Progress in inflammation research · doi:10.1007/978-3-030-44599-7_6 · Cited by 2
Lee, D., Nam, T., Jeong, B., & Jeong, G. (2016) · Molecules · doi:10.3390/molecules21050594 · Cited by 2
RetractedSomatic Genome Alterations in Human Lung Cancers
Imielinski, M. B., Hammerman, P. S., Thomas, R. K., & Meyerson, M. M. (2014) · Lung Cancer · doi:10.1002/9781118468791.ch4 · Cited by 2
Survival Strategy and Disease Pathogenesis According to the Nrf2‐Small Maf Heterodimer
Morita, M., & Motohashi, H. (2011) · doi:10.1002/9781118148143.ch5 · Cited by 2
Impact and Application of Nutraceuticals on Inflammation-Induced Colorectal Cancer Development
Liu, Y. (2017) · Springer eBooks · doi:10.1007/978-3-319-53082-6_14 · Cited by 1
Hidaka, T., Kobayashi, E. H., & Yamamoto, M. P. (2016) · Springer eBooks · doi:10.1007/978-4-431-56068-5_20 · Cited by 1
Self-citationNitric Oxide and Endothelial Dysfunction
Noiri, E., & Minami, K. (2014) · Oxidative stress in applied basic research and clinical practice · doi:10.1007/978-1-4939-0679-6_4
Konkin, D. J. F. (2013) · University Library - University of Saskatchewan (University of Saskatchewan)
Multidrug resistant protein-three gene regulation
Mahaffey, C. M. (2010) · eScholarship (California Digital Library)
in mesangial cells: role in the inhibition of pro-inflammatory genes*
Sánchez-Gómez, F. J., Cernuda‐Morollón, E., Stamatakis, K., & Pérez‐Sala, D. (2004)
Molecular and pharmacological study of transcription factor Nrf2
Lin, W. (2009) · Rutgers University Community Repository (Rutgers University) · doi:10.7282/t34x5819
Inhibition of lung tumorigenesis and cancer cell growth by EGCG and other chemopreventive agents
Jin, H. (2013) · doi:10.7282/t3w9576r
“Nuclear factor (erythroid-derived 2)-like 2 (Nrf2) is a transcription factor that plays a key role in the transcriptional regulation of antioxidant and detoxification genes to inhibit inflammation and protect against oxidative stress [240-242, 277].”
BackgroundQian, W., Chang, R., Jia, H., Fu, S., & Sun, X. (2022) · Research Square · doi:10.21203/rs.3.rs-1450309/v1
Kubota, K., Katsurabayashi, S., Watanabe, T., Iwasaki, K., Nagamatsu, T., & Akaike, N. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.07.592882
Clerigué, J., Pascual-Guerra, J., Leon, R. M., & Menéndez, J. C. (2024) · Neuromethods · doi:10.1007/978-1-0716-4232-0_5
Reverter, A., Ballester, M., Alexandre, P. A., Mármol‐Sánchez, E., Dalmau, A., Quintanilla, R., & Ramayo‐Caldas, Y. (2021) · Figshare · doi:10.6084/m9.figshare.14072260
Ding, Y., Haks, M. C., Forn‐Cuní, G., He, J., Nowik, N., Harms, A. C., Hankemeier, T., Eeza, M. N. H., Matysik, J., Alia, A., et al. (2021) · Figshare · doi:10.6084/m9.figshare.14926867
Metadata
- Authors
- Itoh, K., Mochizuki, M., Ishii, Y., Ishii, T., Shibata, T., Kawamoto, Y., Kelly, V., Sekizawa, K., Uchida, K., & Yamamoto, M.
- Affiliations
- Life Science Center for Survival Dynamics, Tsukuba Advanced Research Alliance (TARA) (JP)
- Institute of Clinical Medicines
- University of Tsukuba (JP)
- Nagoya University (JP)
- Institute of Social Medicines, University of Tsukuba, Tsukuba 305-8577
- Corresponding author
- Yamamoto, Masayuki
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2004-01-01
- Volume
- 24
- Issue
- 1
- Pages
- 36-45
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC303336
- OpenAlex
- W2113971187
- Cited by
- 407
- References
- 46
- Citations by year
- 2026: 4 · 2025: 8 · 2024: 9 · 2023: 13 · 2022: 13 · 2021: 21 · 2020: 20 · 2019: 20 · 2018: 21 · 2017: 21 · 2016: 24 · 2015: 23 · 2014: 14 · 2013: 21 · 2012: 11
- FWCI
- 6.55
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Molecular and Cellular Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
- Health Sciences › Medicine › Pharmacology (medical) › Inflammatory mediators and NSAID effects
- Keywords
- Nrf2, 15-deoxy-Δ12,14-prostaglandin J2, anti-inflammatory signaling, macrophages, neutrophil recruitment, carrageenan-induced pleurisy, Keap1, heme oxygenase-1, peroxiredoxin 1, cyclooxygenase-2, NS-398, acute inflammation, Nrf2-deficient mice
- MeSH terms
- Animals, DNA-Binding Proteins, Inflammation, Isoenzymes, Macrophages, Peritoneum, Pleurisy, Prostaglandin-Endoperoxide Synthases, Prostaglandin D2, Trans-Activators, Hepatocytes, NF-E2-Related Factor 2, Mice, Cyclooxygenase 2
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