Discover Community Create You

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

Article

A single amino acid substitution results in a retinoblastoma protein defective in phosphorylation and oncoprotein binding.

Proceedings of the National Academy of Sciences of the United States of America - 1 Sept 1990

Kaye F J, Kratzke R A, Gerster J L, Horowitz J M

Abstract excerpt

We have previously identified a small-cell lung cancer cell line (NCI-H209) that expresses an aberrant, underphosphorylated form of the retinoblastoma protein RB1. Molecular analysis of RB1 mRNA from this cell line revealed a single point mutation within exon 21 that resulted in a nonconservative amino acid substitution (cysteine to phenylalanine) at codon 706. Stable expression of this mutant RB1 cDNA in a human...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Base Sequence

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cell Line

Share to DNA-Binding Proteins

Share to Molecular Sequence Data

Share to Mutation

Share to Polymerase Chain Reaction

Share to RNA, Messenger

Source

Open in PubMed Open full text

Identifiers

PMID: 2168563
DOI: 10.1073/pnas.87.17.6922
PMCID: PMC54650

Provenance

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

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A single amino acid substitution results in a retinoblastoma protein defective in phosphorylation and oncoprotein binding.PMID 2168563Read ↗

A single Cys706 to Phe substitution in the retinoblastoma protein causes the loss of binding to SV40 T antigen.Semantic proximity Read ↗

Functional analysis at the Cys706 residue of the retinoblastoma protein.Semantic proximity Read ↗

RB1-I680T mutation potentiates tumor growth and chemotherapy sensitivity in non-small cell lung cancer via derepressing E2F1 transcription.Semantic proximity Read ↗

Oncogenic point mutations in exon 20 of the RB1 gene in families showing incomplete penetrance and mild expression of the retinoblastoma phenotype.Semantic proximity Read ↗

Nonfunctional mutants of the retinoblastoma protein are characterized by defects in phosphorylation, viral oncoprotein association, and nuclear tethering.Semantic proximity Read ↗

The amino terminus of the retinoblastoma (Rb) protein associates with a cyclin-dependent kinase-like kinase via Rb amino acids required for growth suppression.Semantic proximity Read ↗

The extreme COOH terminus of the retinoblastoma tumor suppressor protein pRb is required for phosphorylation on Thr-373 and activation of E2F.Semantic proximity Read ↗

Reverse mutational analysis reveals threonine-373 as a potentially sufficient phosphorylation site for inactivation of the retinoblastoma tumor suppressor protein (pRB).Semantic proximity Read ↗

Functional implications of mutations within polyomavirus large T antigen Rb-binding domain: effects on pRb and p107 binding in vitro and immortalization activity in vivo.Semantic proximity Read ↗

Temperature-sensitive RB mutations linked to incomplete penetrance of familial retinoblastoma in 12 families.Semantic proximity Read ↗

The regions of the retinoblastoma protein needed for binding to adenovirus E1A or SV40 large T antigen are common sites for mutations.Semantic proximity Read ↗

Retinoblastoma protein binding properties are dependent on 4 cysteine residues in the protein binding pocket.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.