ArticleStructure (London, England : 1993)2015
Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed, 1 synthesis or guideline pooled it, 37 citations in OpenAlex.
- Targeting p53 pathways: mechanisms, structures, and advances in therapy.Signal transduction and targeted therapy · 2023Pooled it
- Centromere-size reduction and chromatin state dynamics following intergenomic hybridization in cotton.PLoS genetics · 2025Article
- Molecular dynamics-based computational investigations on the influence of tumor suppressor p53 binding protein against other proteins/peptides.Scientific reports · 2024Article
- NEAT1 modulates the TIRR/53BP1 complex to maintain genome integrity.Nature communications · 2024Article
- An autoinhibited state of 53BP1 revealed by small molecule antagonists and protein engineering.Nature communications · 2023Article
- Review
- Regulation of p53 Function by Formation of Non-Nuclear Heterologous Protein Complexes.Biomolecules · 2022Review
- TIRR inhibits the 53BP1-p53 complex to alter cell-fate programs.Molecular cell · 2021Article
- A Degenerate Peptide Library Approach to Reveal Sequence Determinants of Methyllysine-Driven Protein Interactions.Frontiers in cell and developmental biology · 2020Article
- Review
- UVA irradiation strengthened an interaction between UBF1/2 proteins and H4K20 di-/tri-methylation.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2019Article
- H3K9me3 and H4K20me3 represent the epigenetic landscape for 53BP1 binding to DNA lesions.Aging · 2018Article
- Switching 53BP1 on and off via Tudors.Nature structural & molecular biology · 2018Article
- Molecular basis for the inhibition of the methyl-lysine binding function of 53BP1 by TIRR.Nature communications · 2018Article
- Mechanism of 53BP1 activity regulation by RNA-binding TIRR and a designer protein.Nature structural & molecular biology · 2018Article
- DOT1L and H3K79 Methylation in Transcription and Genomic Stability.Biomolecules · 2018Review
- Reading chromatin signatures after DNA double-strand breaks.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- The Tail That Wags the Dog: How the Disordered C-Terminal Domain Controls the Transcriptional Activities of the p53 Tumor-Suppressor Protein.Trends in biochemical sciences · 2016Review
- p53 Proteoforms and Intrinsic Disorder: An Illustration of the Protein Structure-Function Continuum Concept.International journal of molecular sciences · 2016Review
- The upstreams and downstreams of H3K79 methylation by DOT1L.Chromosoma · 2016Review
Corrections and comments
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Authors and funding
11 authors at 6 institutions in 1 country.
Funding
Abstract
p53 is dynamically regulated through various posttranslational modifications (PTMs), which differentially modulate its function and stability. The dimethylated marks p53K370me2 and p53K382me2 are associated with p53 activation or stabilization and both are recognized by the tandem Tudor domain (TTD) of 53BP1, a p53 cofactor. Here we detail the molecular mechanisms for the recognition of p53K370me2 and p53K382me2 by 53BP1. The solution structures of TTD in complex with the p53K370me2 and p53K382me2 peptides show a remarkable plasticity of 53BP1 in accommodating these diverse dimethyllysine-containing sequences. We demonstrate that dimeric TTDs are capable of interacting with the two PTMs on a single p53K370me2K382me2 peptide, greatly strengthening the 53BP1-p53 interaction. Analysis of binding affinities of TTD toward methylated p53 and histones reveals strong preference of 53BP1 for p53K382me2, H4K20me2, and H3K36me2 and suggests a possible role of multivalent contacts of 53BP1 in p53 targeting to and accumulation at the sites of DNA damage.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.