The DOI matches its Crossref record; 140 of the 140 references it cites were found in a registry or an index.
AH RECEPTOR SIGNALING PATHWAYS
Abstract
▪ Abstract The aryl hydrocarbon (Ah) receptor has occupied the attention of toxicologists for over two decades. Interest arose from the early observation that this soluble protein played key roles in the adaptive metabolic response to polycyclic aromatic hydrocarbons and in the toxic mechanism of halogenated dioxins and dibenzofurans. More recent investigations have provided a fairly clear picture of the primary adaptive signaling pathway, from agonist binding to the transcriptional activation of genes involved in the metabolism of xenobiotics. Structure-activity studies have provided an understanding of the pharmacology of this receptor; recombinant DNA approaches have identified the enhancer sequences through which this factor regulates gene expression; and functional analysis of cloned cDNAs has allowed the characterization of the major signaling components in this pathway. Our objective is to review the Ah receptor's role in regulation of xenobiotic metabolism and use this model as a framework for understanding the less well-characterized mechanism of dioxin toxicity. In addition, it is hoped that this information can serve as a model for future efforts to understand an emerging superfamily of related signaling pathways that control biological responses to an array of environmental stimuli.
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“Among the various domains of the AhR that exhibit distinct functional activities (1,13-15), we have primarily focused our attention on that of PAS B, one of the two structural repeats (PAS A and PAS B) within the PAS domain, that is involved in both ligand and hsp90 binding.”
From Structural and Functional Characterization of the Aryl Hydrocarbon Receptor Ligand Binding Domain by Homology Modeling and Mutational Analysis (2007) · cites this paper as [1]
In the citing paper
“The aryl hydrocarbon receptor (AhR) 1 is a basic helix-loop-helix (bHLH), PAS- (Per-ArntSim-) containing transcription factor which is present in numerous species and tissues and activates gene expression in a ligand-dependent manner (1-3).”
From Structural and Functional Characterization of the Aryl Hydrocarbon Receptor Ligand Binding Domain by Homology Modeling and Mutational Analysis (2007) · cites this paper as [1]
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Metadata
- Authors
- Schmidt, J. V., & Bradfield, C. A.
- Affiliations
- Northwestern University (US)
- University of Wisconsin–Madison (US)
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 1996-11
- Volume
- 12
- Issue
- 1
- Pages
- 55-89
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- OpenAlex
- W2133972226
- Cited by
- 899
- References
- 140
- Citations by year
- 2026: 3 · 2025: 9 · 2024: 3 · 2023: 16 · 2022: 10 · 2021: 20 · 2020: 16 · 2019: 17 · 2018: 28 · 2017: 29 · 2016: 16 · 2015: 19 · 2014: 28 · 2013: 27 · 2012: 26
- FWCI
- 11.14
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Cell and Developmental Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (CA09560, T32CA009560)
- National Institute of Environmental Health Sciences (ES06883, R01ES006883)
- Topics
- Physical Sciences › Environmental Science › Health, Toxicology and Mutagenesis › Toxic Organic Pollutants Impact
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
- Keywords
- aryl hydrocarbon receptor, dioxin toxicity, dibenzofuran, polycyclic aromatic hydrocarbons, xenobiotic metabolism, transcriptional activation, gene expression regulation, enhancers, structure-activity relationship, signaling pathways, ecotoxicology
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Dioxins, Humans, Molecular Sequence Data, Peptide Mapping, Signal Transduction, Receptors, Aryl Hydrocarbon, Mice, Knockout, Mice
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