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Article

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

Oncogene - 1 Mar 1990

Forrest D, Muñoz A, Raynoschek C, Vennström B, Beug H

Abstract excerpt

In contrast to the normal thyroid hormone receptor, the v-erbA product fails to bind hormone due to mutations in the C-terminal ligand binding domain and thus appears to represent a hormone-independent, oncogenic transcription factor. Therefore, we asked whether or not the C-terminal domain of v-erbA is required for its biological activity and putative transcriptional control functions by analysing mutants with...

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PMID: 1969136

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

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Requirement for the C-terminal domain of the v-erbA oncogene protein for biological function and transcriptional repression.PMID 1969136Read ↗

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 ↗

Mapping of functional domains within the v-erb A oncogene protein: the remnants of the hormone binding domain play multiple, vital roles in protein action.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 ↗

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

Mutational analysis of the role of the carboxy-terminal region of the v-erbB protein in erythroid cell transformation.Semantic proximity Read ↗

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

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

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

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 ↗

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 ↗

Mapping C-terminal transactivation domains of the nuclear HER family receptor tyrosine kinase HER3.Semantic proximity Read ↗

The oncoprotein P75gag-v-erbA represses thyroid hormone induced transcription only via response elements containing palindromic half-sites.Semantic proximity Read ↗

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