Functional interaction between the two zinc finger domains of the v-erb A oncoprotein.

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Article

Functional interaction between the two zinc finger domains of the v-erb A oncoprotein.

Cell growth & differentiation : the molecular biology journal of the American Association for Cancer Research - 1 Apr 1992

Hall B L, Bonde B G, Judelson C, Privalsky M L

Abstract excerpt

The v-erb A oncogene of avian erythroblastosis virus is a mutated and virally transduced copy of a host cell gene encoding a thyroid hormone receptor. The protein expressed by the v-erb A oncogene binds to DNA and acts as a dominant negative inhibitor of both the thyroid hormone receptor and the closely related retinoic acid receptor. The v-erb A protein has sustained two amino acid alterations within its...

Topics

Amino Acid Sequence
Animals
Base Sequence
Binding Sites
Bone Marrow Cells
Breast Neoplasms
Carrier Proteins
Cell Nucleus
Cell Transformation, Viral
Cells, Cultured
Chickens

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

DNA-Binding Proteins

Erythroid Precursor Cells

Fibroblasts

Humans

Molecular Sequence Data

Mutation

Oncogene Proteins v-erbA

Source

Open in PubMed

Identifiers

PMID: 1355356

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1355356-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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Functional interaction between the two zinc finger domains of the v-erb A oncoprotein.PMID 1355356Read ↗

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 ↗

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 ↗

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

trans-dominant mutants of E1A provide genetic evidence that the zinc finger of the trans-activating domain binds a transcription factor.Semantic proximity Read ↗

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

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

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