Thyroid hormone receptor/and v-erbA. A single amino acid difference in the C-terminal region influences dominant negative activity and receptor dimer formation.

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Article

Thyroid hormone receptor/and v-erbA. A single amino acid difference in the C-terminal region influences dominant negative activity and receptor dimer formation.

The Journal of biological chemistry - 25 Jun 1991

Selmi S, Samuels H H

Abstract excerpt

Thyroid hormone receptors are cellular homologues (c-erbAs) of the v-erbA oncoprotein of the avian erythroblastosis virus. Exclusive of the viral gag region, v-erbA differs from the chick c-erbA-alpha receptor by two amino acid changes N-terminal of the DNA binding domain, two amino acid changes in the DNA binding domain, nine amino acid changes in the C-terminal region corresponding to the ligand binding domain...

Topics

Alpharetrovirus
Amino Acids
Animals
Carrier Proteins
Chickens
Chimera
DNA, Viral
Gene Expression Regulation, Viral
Genes, Viral
HeLa Cells
Humans

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Oncogene Proteins v-erbA

Plasmids

Precipitin Tests

Proto-Oncogene Proteins

Receptors, Retinoic Acid

Receptors, Thyroid Hormone

Source

Open in PubMed

Identifiers

PMID: 1675637

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1675637-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Thyroid hormone receptor/and v-erbA. A single amino acid difference in the C-terminal region influences dominant negative activity and receptor dimer formation.PMID 1675637Read ↗

The unique C-termini of the thyroid hormone receptor variant, c-erbA alpha 2, and thyroid hormone receptor alpha 1 mediate different DNA-binding and heterodimerization properties.Semantic proximity Read ↗

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

v-erbA oncogene function in neoplasia correlates with its ability to repress retinoic acid receptor action.Semantic proximity Read ↗

Ontogeny of the v-erbA oncoprotein from the thyroid hormone receptor: an alteration in the DNA binding domain plays a role crucial for v-erbA function.Semantic proximity Read ↗

Multiple mutations contribute to repression by the v-Erb A oncoprotein.Semantic 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 ↗

The lack of transcriptional activation of the v-erbA oncogene is in part due to a mutation present in the DNA binding domain of the protein.Semantic proximity Read ↗

Requirement for the C-terminal domain of the v-erbA oncogene protein for biological function and transcriptional repression.Semantic proximity Read ↗

v-erbA acts on retinoic acid receptors in immature avian erythroid cells.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 ↗

Mutations in the estrogen receptor ligand binding domain discriminate between hormone-dependent transactivation and transrepression.Semantic proximity Read ↗

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