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

Lysines in the tetramerization domain of p53 selectively modulate G1 arrest.

Cell cycle (Georgetown, Tex.) - 2 Jun 2016

Beckerman Rachel, Yoh Kathryn, Mattia-Sansobrino Melissa, Zupnick Andrew, Laptenko Oleg, Karni-Schmidt Orit, Ahn Jinwoo, Byeon In-Ja, Keezer Susan, Prives Carol

Abstract excerpt

Functional in a tetrameric state, the protein product of the p53 tumor suppressor gene confers its tumor-suppressive activity by transactivating genes which promote cell-cycle arrest, senescence, or programmed cell death. How p53 distinguishes between these divergent outcomes is still a matter of considerable interest. Here we discuss the impact of 2 mutations in the tetramerization domain that confer unique...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Cellular Senescence

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cyclin-Dependent Kinase Inhibitor p21

Share to G1 Phase Cell Cycle Checkpoints

Share to Glutamine

Share to Lysine

Share to Protein Domains

Share to Protein Multimerization

Source

Open in PubMed Open full text

Identifiers

PMID: 27210019
DOI: 10.1080/15384101.2016.1170270
PMCID: PMC4934057

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Lysines in the tetramerization domain of p53 selectively modulate G1 arrest.PMID 27210019Read ↗

Cancer-associated p53 tetramerization domain mutants: quantitative analysis reveals a low threshold for tumor suppressor inactivation.Semantic proximity Read ↗

p53 oligomerization status modulates cell fate decisions between growth, arrest and apoptosisSemantic proximity Read ↗

The role of tetramerization in p53 function.Semantic proximity Read ↗

C-terminus of p53 is required for G(2) arrest.Semantic proximity Read ↗

A single mutant, A276S of p53, turns the switch to apoptosis.Semantic proximity Read ↗

p53 mutants without a functional tetramerisation domain are not oncogenic.Semantic proximity Read ↗

The gain of function of the p53 mutant Asp281Gly is dependent on its ability to form tetramers.Semantic proximity Read ↗

Unfolding, aggregation, and amyloid formation by the tetramerization domain from mutant p53 associated with lung cancer.Semantic proximity Read ↗

Endogenous Leu332Gln mutation in p53 disrupts the tetramerization ability in a canine mammary gland tumor cell line.Semantic proximity Read ↗

Acetylation Is Crucial for p53-Mediated Ferroptosis and Tumor Suppression.Semantic proximity Read ↗

The C-terminal lysines fine-tune P53 stress responses in a mouse model but are not required for stability control or transactivation.Semantic proximity Read ↗

An engineered four-stranded coiled coil substitutes for the tetramerization domain of wild-type p53 and alleviates transdominant inhibition by tumor-derived p53 mutants.Semantic proximity Read ↗

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