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Article

Mutations in the DNA-binding and dimerization domains of v-Rel are responsible for altered kappa B DNA-binding complexes in transformed cells.

Journal of virology - 1 Jun 1995

Hrdlicková R, Nehyba J, Bose H R

Abstract excerpt

The c-rel proto-oncogene encodes a member of the Rel/NF-kappa B family of transcription factors. The oncogenic viral form, v-rel, transduced by avian reticuloendotheliosis virus T, induces lymphoid tumors. v-Rel transformation may be mediated directly by binding of v-Rel to cognate DNA sites, resulting in altered gene expression, and/or indirectly by releasing Rel/NF-kappa B transcription factors from cytoplasmic...

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Identifiers

PMID: 7745683
DOI: 10.1128/JVI.69.6.3369-3380.1995
PMCID: PMC189049

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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

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Research trail→

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Mutations in the DNA-binding and dimerization domains of v-Rel are responsible for altered kappa B DNA-binding complexes in transformed cells.PMID 7745683Read ↗

Differences in kappaB DNA-binding properties of v-Rel and c-Rel are the result of oncogenic mutations in three distinct functional regions of the Rel protein.Semantic proximity Read ↗

Discreet mutations from c-Rel to v-Rel alter kappaB DNA recognition, IkappaBalpha binding, and dimerization: implications for v-Rel oncogenicity.Semantic proximity Read ↗

Multiple mutations contribute to the oncogenicity of the retroviral oncoprotein v-Rel.Semantic proximity Read ↗

ERK and JNK activation is essential for oncogenic transformation by v-Rel.Semantic proximity Read ↗

v-Rel and c-Rel are differentially affected by mutations at a consensus protein kinase recognition sequence.Semantic proximity Read ↗

In vivo evolution of c-rel oncogenic potential.Semantic proximity Read ↗

Malignant transformation by mutant Rel proteins.Semantic proximity Read ↗

Mutant envelope residues confer a transactivation function onto N-terminal sequences of the v-Rel oncoprotein.Semantic proximity Read ↗

Interaction of the v-Rel oncoprotein with NF-kappaB and IkappaB proteins: heterodimers of a transformation-defective v-Rel mutant and NF-2 are functional in vitro and in vivo.Semantic proximity Read ↗

Transformation by the vRel oncoprotein requires sequences carboxy-terminal to the Rel homology domain.Semantic proximity Read ↗

A protein kinase-A recognition sequence is structurally linked to transformation by p59v-rel and cytoplasmic retention of p68c-rel.Semantic proximity Read ↗

An optimal range of transcription potency is necessary for efficient cell transformation by c-Rel to ensure optimal nuclear localization and gene-specific activation.Semantic proximity Read ↗

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