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Nuclear factor (erythroid-derived 2)-like 2
Symbols NFE2L2; NRF2
External IDs OMIM600492 MGI108420 HomoloGene2412 GeneCards: NFE2L2 Gene
RNA expression pattern
PBB GE NFE2L2 201146 at tn.png
More reference expression data
Species Human Mouse
Entrez 4780 18024
Ensembl ENSG00000116044 ENSMUSG00000015839
UniProt Q16236 Q05DU7
RefSeq (mRNA) NM_006164 NM_010902
RefSeq (protein) NP_006155 NP_035032
Location (UCSC) Chr 2:
177.8 - 177.97 Mb
Chr 2:
75.48 - 75.51 Mb
PubMed search [1] [2]

Nuclear factor (erythroid-derived 2)-like 2, also known as NFE2L2 or Nrf2, is a transcription factor which in humans is encoded by the NFE2L2 gene.[1] Nrf2 is a master regulator of the antioxidant response.[2][3] The antioxidant response is important for the amelioration of oxidative stress. Oxidative stress can result in cancer, cardiovascular diseases, inflammation, neurological diseases, and renal disease. Because Nrf2 is able to induce genes important in combating oxidative stress, thereby activating the body’s own protective response, it is able to protect from a variety of [oxidative stress]-related complications , even in situations where the administration of exogenous antioxidants (such as Vitamin C and Vitamin E) have failed.



NFE2, NFE2L1, and NFE2L2 (this protein) comprise a family of human genes encoding basic leucine zipper (bZIP) transcription factors. They share highly conserved regions that are distinct from other bZIP families, such as JUN and FOS, although remaining regions have diverged considerably from each other.[4][5]

Under normal or unstressed conditions, Nrf2 is tethered in the cytoplasm by another protein call Kelch like-ECH-associated protein 1 (Keap1).[6] Keap1 acts as a substrate adaptor protein for Cullin 3-based ubiquitination, which results in the [proteasomal] degradation of Nrf2, and under normal conditions Nrf2 has a half-life of only 20 minutes.[7] Oxidative stress or electrophilic stress disrupts critical cysteine residues in Keap1, resulting in a disruption of the Keap1-Cul3 ubitquitination system and a build-up of Nrf2 in the cytoplasm.[8][9] Unbound Nrf2 is then able to translocate into the nucleus, where it will heterodimerize with a small Maf protein and bind to the Antioxidant Response Element (ARE) in the upstream promoter region of many antioxidative genes, where it will initiate their transcription.[10] The coordinated effort of the induction of the many Nrf2 target genes has a profound impact on combating oxidative stress, inflammation, and thus, disease. Nrf2 upregulates its own expression by binding to an Antioxidant Response Element (ARE) sequence in its promoter region.

Target Genes

Activation of Nrf2 results in the induction of many cytoprotective proteins. These include, but are not limited to, the following:

  • NAD(P)H quinone oxidoreductase 1 (Nqo1) is a prototypical Nrf2 target gene that catalyzes the reduction and detoxification of highly reactive quinones that can cause [redox cycling] and oxidative stress.[11]
  • Glutamate-cysteine ligase, catalytic (Gclc) and glutamate-cysteine ligase, modifier (GCLM) subunits form a heterodimer, which is the rate-limiting step in the synthesis of glutathione (GSH), a very powerful endogenous antioxidant. Both Gclc and Gclm are characteristic Nrf2 target genes, which establish Nrf2 as a regulator of glutathione, one of the most important antioxidants in the body.[12]
  • Heme oxygenase-1 (HMOX1) is an enzyme that catalyzes the breakdown of heme into the antioxidant biliverdin, the anti-inflammatory agent carbon monoxide, and iron. HO-1 is a Nrf2 target gene that has been shown to protect from a variety of pathologies, including sepsis, hypertension, atherosclerosis, acute lung injury, kidney injury, and pain.[13]
  • The glutathione S-transferase (GST) family includes cytosolic, mitochondrial, and microsomal enzymes that catalyze the conjugation of GSH with endogenous and xenobiotic electrophiles. After detoxification by [GSH] conjugation catalyzed by GSTs, the body can eliminate potentially harmful and toxic compounds. GSTs are induced by Nrf2 activation and represent an important route of detoxification.[14]
  • The UDP-glucuronosyltransferase (UGT) family catalyze the conjugation of a glucuronic acid moiety to a variety of endogenous and exogenous substances, making them more water soluble and readily excreted. Important substrates for glucuronidation include bilirubin and acetaminophen. Nrf2 has been shown to induce UGT1A1 and UGT1A6.[15]
  • Multidrug resistance-associated proteins (Mrps) are important membrane transporters that efflux various compounds from various organs and into bile or plasma, with subsequent excretion in the feces or urine, respectively. Mrps have been shown to be upregulated by Nrf2 and alteration in their expression can dramatically alter the pharamacokinetics and toxicity of compounds.[16][17]


Nrf2 is a basic leucine zipper (bZip) transcription factor with a Cap “n” Collar (CNC) structure.[1]

Nrf2 possesses six highly conserved domains called Nrf2-ECH homology (Neh) domains. The Neh1 domain is a CNC-bZIP domain that allows Nrf2 to heterodimerize with small Maf proteins. The Neh2 domain allows for binding of Nrf2 to its cytosolic repressor Keap1.[18] The Neh3 domain may play a role in Nrf2 protein stability and may act as a transactivation domain, interacting with component of the transcriptional apparatus.[19] The Neh4 and Neh5 domains also act as transactivation domains, but bind to a different protein called cAMP [Response Element Binding Protein] (CBP), which possesses intrinsic [histone acetyltransferase] activity.[18] Finally, the Neh6 domain may contain a degron that is involved in the degradation of Nrf2, even in stressed cells, where the half-life of Nrf2 protein is longer than in unstressed conditions.[20]

Tissue distribution

Nrf2 is ubiquitously expressed with the highest concentrations (in descending order) in the kidney, muscle, lung, heart, liver, and brain.[1]

Nrf2 as a drug target

In recent years, Nrf2 has become an area of intense research (See Figure). A common theme in most of this research is that activation of Nrf2 upregulates a coordinated antioxidant response and is therefore, capable of protecting in a wide variety of animal models of [oxidative stress]-related injury and inflammatory disease. Therefore, Nrf2 represents a novel drug target. The diseases that could be treated or prevented by Nrf2 activation seem extensive as most have an etiology in oxidative stress.

Nrf2 Publications by Year.

Some Nrf2 activators have been given to humans in clinical trials. The [dithiolethiones] are a class of organosulfur compounds, of which, [oltipraz] is the most well-studied. Oltirpraz has been shown to inhibit cancer formation in a variety of rodent organs, including the bladder, blood, colon, kidney, liver, lung, pancreas, stomach, and trachea, skin, and mammary tissue.[21] However, clinical trials involving oltipraz have demonstrated significant side effects with no or questionable chemopreventive efficacy.[21] In one clinical study, side effects after 8 weeks of treatment included numbness, tingling, and pain in the extremities. In another study, side effects after 4 weeks included gastrointestinal toxicity. Oltipraz has also been shown to generate [superoxide] radical, which can be quite toxic.[22]

A series of synthetic oleane triterpenoid compounds that are Nrf2 activators and referred to as Antioxidant Inflammatory Modulators (AIMs), are in clinical development at Reata Pharmaceuticals. The lead compound in this series, bardoxolone methyl (also known as CDDO-Me or RTA 402), is currently in phase II clinical trials for the treatment of chronic kidney disease (CKD) in patients with diabetes mellitus. It has been established that there is a clear relationship between oxidative stress and inflammation and the various pathologies associated with diabetes, including diabetic nephropathy and chronic kidney disease.[23] Therefore, Nrf2 represents a very novel target for the treatment of CKD. In fact, a recent presentation of data from a Phase 2a trial of bardoxolone methyl indicated that this novel agent produced a dose and time-dependent improvement in kidney function (eGFR) as well as measures of diabetes and cardiovascular risk.[24 ] Reata also indicates that it has other Nrf2 inducers in the same class that are in preclinical development for the treatment of CNS and respiratory diseases, which also have been shown to have causality from oxidative stress.


NFE2L2 has been shown to interact with CREB binding protein,[25] KEAP1,[26][27][28] C-jun,[29] EIF2AK3[26] and Ubiquitin C.[27][30]


  1. ^ a b c Moi P, Chan K, Asunis I, Cao A, Kan YW (October 1994). "Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region". Proc. Natl. Acad. Sci. U.S.A. 91 (21): 9926–30. doi:10.1073/pnas.91.21.9926. PMID 7937919.  
  2. ^ Li W, Kong AN (February 2009). "Molecular mechanisms of Nrf2-mediated antioxidant response". Mol. Carcinog. 48 (2): 91–104. doi:10.1002/mc.20465. PMID 18618599.  
  3. ^ Nguyen T, Nioi P, Pickett CB (May 2009). "The Nrf2-antioxidant response element signaling pathway and its activation by oxidative stress". J. Biol. Chem. 284 (20): 13291–5. doi:10.1074/jbc.R900010200. PMID 19182219.  
  4. ^ Chan JY, Cheung MC, Moi P, Chan K, Kan YW (March 1995). "Chromosomal localization of the human NF-E2 family of bZIP transcription factors by fluorescence in situ hybridization". Hum. Genet. 95 (3): 265–9. doi:10.1007/BF00225191. PMID 7868116.  
  5. ^ "Entrez Gene: NFE2L2 nuclear factor (erythroid-derived 2)-like 2".  
  6. ^ Itoh K, Wakabayashi N, Katoh Y, Ishii T, Igarashi K, Engel JD, Yamamoto M (January 1999). "Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain". Genes Dev. 13 (1): 76–86. doi:10.1101/gad.13.1.76. PMID 9887101.  
  7. ^ Kobayashi A, Kang MI, Okawa H, Ohtsuji M, Zenke Y, Chiba T, Igarashi K, Yamamoto M (August 2004). "Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2". Mol. Cell. Biol. 24 (16): 7130–9. doi:10.1128/MCB.24.16.7130-7139.2004. PMID 15282312.  
  8. ^ Yamamoto T, Suzuki T, Kobayashi A, Wakabayashi J, Maher J, Motohashi H, Yamamoto M (April 2008). "Physiological significance of reactive cysteine residues of Keap1 in determining Nrf2 activity". Mol. Cell. Biol. 28 (8): 2758–70. doi:10.1128/MCB.01704-07. PMID 18268004.  
  9. ^ Sekhar KR, Rachakonda G, Freeman ML (June 2009). "Cysteine-based regulation of the CUL3 adaptor protein Keap1". Toxicol. Appl. Pharmacol.. doi:10.1016/j.taap.2009.06.016. PMID 19560482.  
  10. ^ Itoh K, Chiba T, Takahashi S, Ishii T, Igarashi K, Katoh Y, Oyake T, Hayashi N, Satoh K, Hatayama I, Yamamoto M, Nabeshima Y (July 1997). "An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements". Biochem. Biophys. Res. Commun. 236 (2): 313–22. doi:10.1006/bbrc.1997.6943. PMID 9240432.  
  11. ^ Venugopal R, Jaiswal AK (December 1996). "Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H:quinone oxidoreductase1 gene". Proc. Natl. Acad. Sci. U.S.A. 93 (25): 14960–5. doi:10.1073/pnas.93.25.14960. PMID 8962164.  
  12. ^ Solis WA, Dalton TP, Dieter MZ, Freshwater S, Harrer JM, He L, Shertzer HG, Nebert DW (May 2002). "Glutamate-cysteine ligase modifier subunit: mouse Gclm gene structure and regulation by agents that cause oxidative stress". Biochem. Pharmacol. 63 (9): 1739–54. doi:10.1016/S0006-2952(02)00897-3. PMID 12007577.  
  13. ^ Jarmi T, Agarwal A (February 2009). "Heme oxygenase and renal disease". Curr. Hypertens. Rep. 11 (1): 56–62. doi:10.1007/s11906-009-0011-z. PMID 19146802.  
  14. ^ Hayes JD, Chanas SA, Henderson CJ, McMahon M, Sun C, Moffat GJ, Wolf CR, Yamamoto M (February 2000). "The Nrf2 transcription factor contributes both to the basal expression of glutathione S-transferases in mouse liver and to their induction by the chemopreventive synthetic antioxidants, butylated hydroxyanisole and ethoxyquin". Biochem. Soc. Trans. 28 (2): 33–41. PMID 10816095.  
  15. ^ Yueh MF, Tukey RH (March 2007). "Nrf2-Keap1 signaling pathway regulates human UGT1A1 expression in vitro and in transgenic UGT1 mice". J. Biol. Chem. 282 (12): 8749–58. doi:10.1074/jbc.M610790200. PMID 17259171.  
  16. ^ Maher JM, Dieter MZ, Aleksunes LM, Slitt AL, Guo G, Tanaka Y, Scheffer GL, Chan JY, Manautou JE, Chen Y, Dalton TP, Yamamoto M, Klaassen CD (November 2007). "Oxidative and electrophilic stress induces multidrug resistance-associated protein transporters via the nuclear factor-E2-related factor-2 transcriptional pathway". Hepatology 46 (5): 1597–610. doi:10.1002/hep.21831. PMID 17668877.  
  17. ^ Reisman SA, Csanaky IL, Aleksunes LM, Klaassen CD (May 2009). "Altered disposition of acetaminophen in Nrf2-null and Keap1-knockdown mice". Toxicol. Sci. 109 (1): 31–40. doi:10.1093/toxsci/kfp047. PMID 19246624.  
  18. ^ a b Motohashi H, Yamamoto M (November 2004). "Nrf2-Keap1 defines a physiologically important stress response mechanism". Trends Mol Med 10 (11): 549–57. doi:10.1016/j.molmed.2004.09.003. PMID 15519281.  
  19. ^ Nioi P, Nguyen T, Sherratt PJ, Pickett CB (December 2005). "The carboxy-terminal Neh3 domain of Nrf2 is required for transcriptional activation". Mol. Cell. Biol. 25 (24): 10895–906. doi:10.1128/MCB.25.24.10895-10906.2005. PMID 16314513.  
  20. ^ McMahon M, Thomas N, Itoh K, Yamamoto M, Hayes JD (July 2004). "Redox-regulated turnover of Nrf2 is determined by at least two separate protein domains, the redox-sensitive Neh2 degron and the redox-insensitive Neh6 degron". J. Biol. Chem. 279 (30): 31556–67. doi:10.1074/jbc.M403061200. PMID 15143058.  
  21. ^ a b Zhang Y, Gordon GB (July 2004). "A strategy for cancer prevention: stimulation of the Nrf2-ARE signaling pathway". Mol. Cancer Ther. 3 (7): 885–93. PMID 15252150.  
  22. ^ Velayutham M, Villamena FA, Fishbein JC, Zweier JL (March 2005). "Cancer chemopreventive oltipraz generates superoxide anion radical". Arch. Biochem. Biophys. 435 (1): 83–8. doi:10.1016/ PMID 15680910.  
  23. ^ Brownlee M (December 2001). "Biochemistry and molecular cell biology of diabetic complications". Nature 414 (6865): 813–20. doi:10.1038/414813a. PMID 11742414.  
  24. ^ Schwartz SL, Denham DS, Hurwitz CA, Meyer CJ, Pergola PE (2009). "Bardoxolone Methyl Shown To Improve Renal Function in Patients with Chronic Kidney Disease and Type 2 Diabetes Mellitus". Novel Diabetes Therapies in Development in Humans. American Diabetes Association. Retrieved 2009-08-14.  
  25. ^ Katoh, Y; Itoh K, Yoshida E, Miyagishi M, Fukamizu A, Yamamoto M (Oct. 2001). "Two domains of Nrf2 cooperatively bind CBP, a CREB binding protein, and synergistically activate transcription". Genes Cells (England) 6 (10): 857–68. doi:10.1046/j.1365-2443.2001.00469.x. ISSN 1356-9597. PMID 11683914.  
  26. ^ a b Cullinan, Sara B; Zhang Donna, Hannink Mark, Arvisais Edward, Kaufman Randal J, Diehl J Alan (Oct. 2003). "Nrf2 is a direct PERK substrate and effector of PERK-dependent cell survival". Mol. Cell. Biol. (United States) 23 (20): 7198–209. doi:10.1128/MCB.23.20.7198-7209.2003. ISSN 0270-7306. PMID 14517290.  
  27. ^ a b Shibata, Tatsuhiro; Ohta Tsutomu, Tong Kit I, Kokubu Akiko, Odogawa Reiko, Tsuta Koji, Asamura Hisao, Yamamoto Masayuki, Hirohashi Setsuo (Sep. 2008). "Cancer related mutations in NRF2 impair its recognition by Keap1-Cul3 E3 ligase and promote malignancy". Proc. Natl. Acad. Sci. U.S.A. (United States) 105 (36): 13568–73. doi:10.1073/pnas.0806268105. PMID 18757741.  
  28. ^ Wang, Xiao-Jun; Sun Zheng, Chen Weimin, Li Yanjie, Villeneuve Nicole F, Zhang Donna D (Aug. 2008). "Activation of Nrf2 by arsenite and monomethylarsonous acid is independent of Keap1-C151: enhanced Keap1-Cul3 interaction". Toxicol. Appl. Pharmacol. (United States) 230 (3): 383–9. doi:10.1016/j.taap.2008.03.003. ISSN 0041-008X. PMID 18417180.  
  29. ^ Venugopal, R; Jaiswal A K (Dec. 1998). "Nrf2 and Nrf1 in association with Jun proteins regulate antioxidant response element-mediated expression and coordinated induction of genes encoding detoxifying enzymes". Oncogene (ENGLAND) 17 (24): 3145–56. doi:10.1038/sj.onc.1202237. ISSN 0950-9232. PMID 9872330.  
  30. ^ Patel, Rachana; Maru Girish (Jun. 2008). "Polymeric black tea polyphenols induce phase II enzymes via Nrf2 in mouse liver and lungs". Free Radic. Biol. Med. (United States) 44 (11): 1897–911. doi:10.1016/j.freeradbiomed.2008.02.006. ISSN 0891-5849. PMID 18358244.  

Further reading

  • Alam J, Cook JL (2003). "Transcriptional regulation of the heme oxygenase-1 gene via the stress response element pathway.". Curr. Pharm. Des. 9 (30): 2499–511. doi:10.2174/1381612033453730. PMID 14529549.  
  • Zhang DD (2007). "Mechanistic studies of the Nrf2-Keap1 signaling pathway.". Drug Metab. Rev. 38 (4): 769–89. doi:10.1080/03602530600971974. PMID 17145701.  
  • Aleksunes LM, Manautou JE (2007). "Emerging role of Nrf2 in protecting against hepatic and gastrointestinal disease.". Toxicologic pathology 35 (4): 459–73. doi:10.1080/01926230701311344. PMID 17562481.  
  • Chan JY, Cheung MC, Moi P, et al. (1995). "Chromosomal localization of the human NF-E2 family of bZIP transcription factors by fluorescence in situ hybridization.". Hum. Genet. 95 (3): 265–9. doi:10.1007/BF00225191. PMID 7868116.  
  • Moi P, Chan K, Asunis I, et al. (1994). "Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region.". Proc. Natl. Acad. Sci. U.S.A. 91 (21): 9926–30. doi:10.1073/pnas.91.21.9926. PMID 7937919.  
  • Toki T, Itoh J, Kitazawa J, et al. (1997). "Human small Maf proteins form heterodimers with CNC family transcription factors and recognize the NF-E2 motif.". Oncogene 14 (16): 1901–10. doi:10.1038/sj.onc.1201024. PMID 9150357.  
  • Venugopal R, Jaiswal AK (1999). "Nrf2 and Nrf1 in association with Jun proteins regulate antioxidant response element-mediated expression and coordinated induction of genes encoding detoxifying enzymes.". Oncogene 17 (24): 3145–56. doi:10.1038/sj.onc.1202237. PMID 9872330.  
  • Itoh K, Wakabayashi N, Katoh Y, et al. (1999). "Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain.". Genes Dev. 13 (1): 76–86. doi:10.1101/gad.13.1.76. PMID 9887101.  
  • Wang Y, Devereux W, Stewart TM, Casero RA (1999). "Cloning and characterization of human polyamine-modulated factor-1, a transcriptional cofactor that regulates the transcription of the spermidine/spermine N(1)-acetyltransferase gene.". J. Biol. Chem. 274 (31): 22095–101. doi:10.1074/jbc.274.31.22095. PMID 10419538.  
  • Ohtsubo T, Kamada S, Mikami T, et al. (2000). "Identification of NRF2, a member of the NF-E2 family of transcription factors, as a substrate for caspase-3(-like) proteases.". Cell Death Differ. 6 (9): 865–72. doi:10.1038/sj.cdd.4400566. PMID 10510468.  
  • Nguyen T, Huang HC, Pickett CB (2000). "Transcriptional regulation of the antioxidant response element. Activation by Nrf2 and repression by MafK.". J. Biol. Chem. 275 (20): 15466–73. doi:10.1074/jbc.M000361200. PMID 10747902.  
  • Ikeda Y, Sugawara A, Taniyama Y, et al. (2000). "Suppression of rat thromboxane synthase gene transcription by peroxisome proliferator-activated receptor gamma in macrophages via an interaction with NRF2.". J. Biol. Chem. 275 (42): 33142–50. doi:10.1074/jbc.M002319200. PMID 10930400.  
  • Dhakshinamoorthy S, Jaiswal AK (2001). "Small maf (MafG and MafK) proteins negatively regulate antioxidant response element-mediated expression and antioxidant induction of the NAD(P)H:Quinone oxidoreductase1 gene.". J. Biol. Chem. 275 (51): 40134–41. doi:10.1074/jbc.M003531200. PMID 11013233.  
  • Huang HC, Nguyen T, Pickett CB (2001). "Regulation of the antioxidant response element by protein kinase C-mediated phosphorylation of NF-E2-related factor 2.". Proc. Natl. Acad. Sci. U.S.A. 97 (23): 12475–80. doi:10.1073/pnas.220418997. PMID 11035812.  
  • Wang Y, Devereux W, Stewart TM, Casero RA (2001). "Characterization of the interaction between the transcription factors human polyamine modulated factor (PMF-1) and NF-E2-related factor 2 (Nrf-2) in the transcriptional regulation of the spermidine/spermine N1-acetyltransferase (SSAT) gene.". Biochem. J. 355 (Pt 1): 45–9. doi:10.1042/0264-6021:3550045. PMID 11256947.  
  • He CH, Gong P, Hu B, et al. (2001). "Identification of activating transcription factor 4 (ATF4) as an Nrf2-interacting protein. Implication for heme oxygenase-1 gene regulation.". J. Biol. Chem. 276 (24): 20858–65. doi:10.1074/jbc.M101198200. PMID 11274184.  
  • Dhakshinamoorthy S, Jaiswal AK (2001). "Functional characterization and role of INrf2 in antioxidant response element-mediated expression and antioxidant induction of NAD(P)H:quinone oxidoreductase1 gene.". Oncogene 20 (29): 3906–17. doi:10.1038/sj.onc.1204506. PMID 11439354.  
  • Katoh Y, Itoh K, Yoshida E, et al. (2002). "Two domains of Nrf2 cooperatively bind CBP, a CREB binding protein, and synergistically activate transcription.". Genes Cells 6 (10): 857–68. doi:10.1046/j.1365-2443.2001.00469.x. PMID 11683914.  
  • Wang Y, Devereux W, Stewart TM, Casero RA (2002). "Polyamine-modulated factor 1 binds to the human homologue of the 7a subunit of the Arabidopsis COP9 signalosome: implications in gene expression.". Biochem. J. 366 (Pt 1): 79–86. doi:10.1042/BJ20020211. PMID 12020345.  
  • Tirumalai R, Rajesh Kumar T, Mai KH, Biswal S (2002). "Acrolein causes transcriptional induction of phase II genes by activation of Nrf2 in human lung type II epithelial (A549) cells.". Toxicol. Lett. 132 (1): 27–36. doi:10.1016/S0378-4274(02)00055-3. PMID 12084617.  

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.



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