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

Characterization of the ligand-dependent transactivation domain of thyroid hormone receptor.

The EMBO journal - 1 Jul 1994

Barettino D, Vivanco Ruiz M M, Stunnenberg H G

Abstract excerpt

Transcriptional activation by nuclear receptors is achieved through autonomous activation functions (AFs), a constitutive N-terminal AF-1 and a C-terminal, ligand-dependent AF-2 that comprises a motif conserved between nuclear receptors. We have performed an extensive mutational analysis of the putative AF-2 domain of chicken thyroid hormone receptor alpha (cT3R alpha). We show that the AF-2 region mediates...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Binding Sites
Share to Cell Line

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

Share to Molecular Sequence Data

Share to Mutation

Share to Promoter Regions, Genetic

Share to Sequence Homology, Amino Acid

Share to Transcription, Genetic

Source

Open in PubMed Open full text

Identifiers

PMID: 8039499
DOI: 10.1002/j.1460-2075.1994.tb06603.x
PMCID: PMC395194

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

Characterization of the ligand-dependent transactivation domain of thyroid hormone receptor.PMID 8039499Read ↗

The t4 Activation Domain of the Thyroid Hormone Receptor Is Required for Release of a Putative Corepressor(s) Necessary for Transcriptional SilencingSemantic proximity Read ↗

Functional analysis of a transactivation domain in the thyroid hormone beta receptor.Semantic proximity Read ↗

Mutations in the conserved C-terminal sequence in thyroid hormone receptor dissociate hormone-dependent activation from interference with AP-1 activity.Semantic proximity Read ↗

Human TAF(II)135 potentiates transcriptional activation by the AF-2s of the retinoic acid, vitamin D3, and thyroid hormone receptors in mammalian cells.Semantic proximity Read ↗

Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors.Semantic proximity Read ↗

Evidence for ligand-dependent intramolecular folding of the AF-2 domain in vitamin D receptor-activated transcription and coactivator interaction.Semantic proximity Read ↗

A novel natural mutation in the thyroid hormone receptor defines a dual functional domain that exchanges nuclear receptor corepressors and coactivators.Semantic proximity Read ↗

Distinct dimerization domains provide antagonist pathways for thyroid hormone receptor action.Semantic proximity Read ↗

Hormone-dependent and -independent transcriptional activation by thyroid hormone receptors are mediated by different mechanisms.Semantic proximity Read ↗

Identification of COUP-TFII Orphan Nuclear Receptor as a Retinoic Acid–Activated ReceptorSemantic proximity Read ↗

Unliganded T3R, but not its oncogenic variant, v-erbA, suppresses RAR-dependent transactivation by titrating out RXR.Semantic proximity Read ↗

A conserved surface on the ligand binding domain of nuclear receptors for allosteric control.Semantic proximity Read ↗

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