Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mutational analysis of the mouse aryl hydrocarbon receptor tyrosine residues necessary for recognition of dioxin response elements.

Archives of biochemistry and biophysics - 1 Apr 2003

Minsavage Gary D, Vorojeikina Daria P, Gasiewicz Thomas A

Abstract excerpt

Tyrosine phosphorylation of the aryl hydrocarbon receptor (AhR), a member of the basic helix-loop-helix/PER-ARNT-SIM transcription factor family, has been shown to regulate its dioxin response elements (DRE) binding ability, although no specific residues have been directly demonstrated to be phosphorylated. Of the 23 tyrosines in the mouse AhR, 19 are conserved across all mammalian species sequenced thus far. The...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Electrophoresis, Gel, Two-Dimensional
Share to Immunoblotting

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Precipitin Tests

Share to Protein Biosynthesis

Share to Protein Processing, Post-Translational

Share to Receptors, Aryl Hydrocarbon

Share to Response Elements

Share to Tyrosine

Source

Identifiers

PMID: 12646272
DOI: 10.1016/s0003-9861(03)00033-x

Genes

ARNT

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutational analysis of the mouse aryl hydrocarbon receptor tyrosine residues necessary for recognition of dioxin response elements.PMID 12646272Read ↗

Identification of functional domains of the aryl hydrocarbon receptor.Semantic proximity Read ↗

Functional analysis of aryl hydrocarbon receptor nuclear translocator interactions with aryl hydrocarbon receptor in the yeast two-hybrid system.Semantic proximity Read ↗

Analysis of the four alleles of the murine aryl hydrocarbon receptor.Semantic proximity Read ↗

Interaction of the regulatory domains of the murine Cyp1a1 gene with two DNA-binding proteins in addition to the Ah receptor and the Ah receptor nuclear translocator (ARNT).Semantic proximity Read ↗

Resistance to 2,3,7,8-tetrachlorodibenzo-p-dioxin toxicity and abnormal liver development in mice carrying a mutation in the nuclear localization sequence of the aryl hydrocarbon receptor.Semantic proximity Read ↗

Identification of phosphorylation sites for Bruton's tyrosine kinase within the transcriptional regulator BAP/TFII-I.Semantic proximity Read ↗

A tetratricopeptide repeat half-site in the aryl hydrocarbon receptor is important for DNA binding and trans-activation potential.Semantic proximity Read ↗

Role of the aryl hydrocarbon receptor nuclear translocator protein in aryl hydrocarbon (dioxin) receptor action.Semantic proximity Read ↗

Characterization and colocalization of steroid binding and dimerization activities in the mouse estrogen receptor.Semantic proximity Read ↗

Deciphering Dimerization Modes of PAS Domains: Computational and Experimental Analyses of the AhR:ARNT Complex Reveal New Insights Into the Mechanisms of AhR Transformation.Semantic proximity Read ↗

Characterization of ligand-dependent phosphorylation of the estrogen receptor.Semantic proximity Read ↗

The aryl hydrocarbon receptor regulates mouse Fshr promoter activity through an e-box binding site.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.