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

Functional analysis of a transactivation domain in the thyroid hormone beta receptor.

The Journal of biological chemistry - 9 Dec 1994

Tone Y, Collingwood T N, Adams M, Chatterjee V K

Abstract excerpt

Hormone-dependent transcriptional activation (AF-2) by the thyroid hormone beta receptor (TR beta) localizes to its carboxyl-terminal domain. A putative transactivation sequence within this domain was analyzed by mutating individual residues to alanine. Mutant receptor carboxyl-terminal domains w...

Topics

Amino Acid Sequence
Base Sequence
Cells, Cultured
DNA
Molecular Sequence Data
Mutation
Receptors, Retinoic Acid
Receptors, Thyroid Hormone
Retinoid X Receptors
Sequence Homology, Amino Acid
Thyroid Hormones
Transcription Factor TFIIB

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Transcription Factors

Transcriptional Activation

Source

Identifiers

PMID: 7983057

Genes

TBP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7983057-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional analysis of a transactivation domain in the thyroid hormone beta receptor.PMID 7983057Read ↗

A natural transactivation mutation in the thyroid hormone beta receptor: impaired interaction with putative transcriptional mediators.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 ↗

Specific mutations in the ligand binding domain selectively abolish the silencing function of human thyroid hormone receptor beta.Semantic proximity Read ↗

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

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

Thyroid hormone resistance syndrome. Inhibition of normal receptor function by mutant thyroid hormone receptors.Semantic proximity Read ↗

N-terminal variants of thyroid hormone receptor beta: differential function and potential contribution to syndrome of resistance to thyroid hormone.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 ↗

Molecular and structural biology of thyroid hormone receptors.Semantic proximity Read ↗

Interaction of human thyroid hormone receptor beta with transcription factor TFIIB may mediate target gene derepression and activation by thyroid hormone.Semantic proximity Read ↗

DNA binding and dimerization determinants for thyroid hormone receptor alpha and its interaction with a nuclear protein.Semantic proximity Read ↗

Enhancement of thyroid hormone receptor isoform specificity by insertion of a distant half-site into a thyroid hormone response element.Semantic proximity Read ↗

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