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

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

Back to search

Article

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

Oncogene - 1 Mar 1993

Mosialos G, Gilmore T D

Abstract excerpt

The avian retroviral oncoprotein v-Rel and its cellular homolog c-Rel are members of a family of related site-specific DNA-binding proteins. Towards the carboxy-terminal end of the highly conserved Rel homology (RH) domain in the majority of Rel proteins, there is a consensus recognition sequence...

Topics

Amino Acid Sequence
Animals
Base Sequence
Binding Sites
Cell Transformation, Neoplastic
Chickens
DNA
Molecular Sequence Data
Mutation
Oncogene Proteins v-rel
Phosphorylation
Protein-Tyrosine Kinases
Proto-Oncogene Proteins
Proto-Oncogene Proteins c-rel
Retroviridae Proteins, Oncogenic
Structure-Activity Relationship
Transcriptional Activation

Source

Open in PubMed

Identifiers

PMID: 8437855

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8437855-2026-08-30.1. 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.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics