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

Quantitative proteomics analysis of the effects of ionizing radiation in wild type and p53 K317R knock-in mouse thymocytes.

Molecular & cellular proteomics : MCP - 1 Apr 2008

Jenkins Lisa M Miller, Mazur Sharlyn J, Rossi Matteo, Gaidarenko Olga, Xu Yang, Appella Ettore

Abstract excerpt

The tumor suppressor protein p53 is a sequence-specific transcription factor that has crucial roles in apoptosis, cell cycle arrest, cellular senescence, and DNA repair. Following exposure to a variety of stresses, p53 becomes post-translationally modified with concomitant increases in activity and stability. To better understand the role of acetylation of Lys-317 in mouse p53, the effect of ionizing radiation...

Read the complete abstract on PubMed

Topics

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

Share to Acetylation
Share to Arginine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lysine

Share to Mass Spectrometry

Share to Mice, Mutant Strains

Share to Protein Biosynthesis

Share to Proteomics

Share to Radiation, Ionizing

Source

Open in PubMed Open full text

Identifiers

PMID: 18178582
DOI: 10.1074/mcp.M700482-MCP200
PMCID: PMC2401331

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Quantitative proteomics analysis of the effects of ionizing radiation in wild type and p53 K317R knock-in mouse thymocytes.PMID 18178582Read ↗

Jun NH2-terminal kinase phosphorylation of p53 on Thr-81 is important for p53 stabilization and transcriptional activities in response to stress.Semantic proximity Read ↗

Acetylation dynamics of human nuclear proteins during the ionizing radiation-induced DNA damage responseSemantic proximity Read ↗

Expression profiling reveals transcriptional regulation by Fbxw7/mTOR pathway in radiation-induced mouse thymic lymphomas.Semantic proximity Read ↗

The p53 endoplasmic reticulum stress-response pathway evolved in humans but not in mice via PERK-regulated p53 mRNA structuresSemantic proximity Read ↗

SnapShot: p53 posttranslational modifications.Semantic proximity Read ↗

The role of acetylation sites in the regulation of p53 activity.Semantic proximity Read ↗

The transcription-independent mitochondrial cell death pathway is defective in non-transformed cells containing the Pro47Ser variant of p53.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 ↗

Targeting Mutant p53 by a SIRT1 Activator YK-3-237 Inhibits the Proliferation of Triple-Negative Breast Cancer CellsSemantic proximity Read ↗

Phosphorylation Control of p53 DNA-Binding Cooperativity Balances Tumorigenesis and AgingSemantic proximity Read ↗

The C terminus of p53 regulates gene expression by multiple mechanisms in a target- and tissue-specific manner in vivo.Semantic proximity Read ↗

p53 C-terminal phosphorylation by CHK1 and CHK2 participates in the regulation of DNA-damage-induced C-terminal acetylation.Semantic proximity Read ↗

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