{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lille-Langoy R"],"funding":["Norges Forskningsr??d"],"pagination":["15123-15135"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8600679"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["55(22)"],"pubmed_abstract":["Polycyclic aromatic hydrocarbons (PAHs) are among the most toxic and bioavailable components found in petroleum and represent a high risk to aquatic organisms. The aryl hydrocarbon receptor (Ahr) is a ligand-activated transcription factor that mediates the toxicity of 2,3,7,8-tetrachlorodibenzo-<i>p</i>-dioxin (TCDD) and other planar aromatic hydrocarbons, including certain PAHs. Ahr acts as a xenosensor and modulates the transcription of biotransformation genes in vertebrates, such as cytochrome P450 1A (<i>cyp1a</i>). Atlantic cod (<i>Gadus morhua</i>) possesses two Ahr proteins, Ahr1a and Ahr2a, which diverge in their primary structure, tissue-specific expression, ligand affinities, and transactivation profiles. Here, a luciferase reporter gene assay was used to assess the sensitivity o"],"journal":["Environmental science & technology"],"pubmed_title":["Substituted Two- to Five-Ring Polycyclic Aromatic Compounds Are Potent Agonists of Atlantic Cod (<i>Gadus morhua</i>) Aryl Hydrocarbon Receptors Ahr1a and Ahr2a."],"pmcid":["PMC8600679"],"funding_grant_id":["267820","244564","248840","229153"],"pubmed_authors":["Lille-Langoy R","Sydnes MO","Goksoyr A","Jorgensen KB","Pampanin DM","Karlsen OA"],"additional_accession":[]},"is_claimable":false,"name":"Substituted Two- to Five-Ring Polycyclic Aromatic Compounds Are Potent Agonists of Atlantic Cod (<i>Gadus morhua</i>) Aryl Hydrocarbon Receptors Ahr1a and Ahr2a.","description":"Polycyclic aromatic hydrocarbons (PAHs) are among the most toxic and bioavailable components found in petroleum and represent a high risk to aquatic organisms. The aryl hydrocarbon receptor (Ahr) is a ligand-activated transcription factor that mediates the toxicity of 2,3,7,8-tetrachlorodibenzo-<i>p</i>-dioxin (TCDD) and other planar aromatic hydrocarbons, including certain PAHs. Ahr acts as a xenosensor and modulates the transcription of biotransformation genes in vertebrates, such as cytochrome P450 1A (<i>cyp1a</i>). Atlantic cod (<i>Gadus morhua</i>) possesses two Ahr proteins, Ahr1a and Ahr2a, which diverge in their primary structure, tissue-specific expression, ligand affinities, and transactivation profiles. Here, a luciferase reporter gene assay was used to assess the sensitivity o","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Nov","modification":"2025-06-01T00:03:04.737Z","creation":"2025-06-01T00:03:04.737Z"},"accession":"S-EPMC8600679","cross_references":{"pubmed":["34739213"],"doi":["10.1021/acs.est.1c02946"]}}