ArticleNucleic acids research2014
A nanobody modulates the p53 transcriptional program without perturbing its functional architecture.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis that pooled it.
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Who cites it
23 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Targeting p53 pathways: mechanisms, structures, and advances in therapy.Signal transduction and targeted therapy · 2023Pooled it
- The NanoBridge system for targeted post-translational modification of challenging proteins.bioRxiv : the preprint server for biology · 2026Article
- Nanobody-mediated control of long RSH Rel and RelA catalysis by restriction of their conformational landscape.Nature communications · 2026Article
- A Modular Platform for Effector Discovery in Induced-Proximity Lysine Acetylation.bioRxiv : the preprint server for biology · 2026Article
- Tuning Polyacrylate Composition to Recognize and Modulate Fluorescent Proteins.Angewandte Chemie (International ed. in English) · 2026Article
- Regulation of cellular states via targeted phosphorylation of p53 using a nanobody-coupled kinase system.Cell death discovery · 2025Article
- A chimeric viral platform for directed evolution in mammalian cells.Nature communications · 2025Article
- Principles and Design of Molecular Tools for Sensing and Perturbing Cell Surface Receptor Activity.Chemical reviews · 2025Review
- Aggregate-selective removal of pathological tau by clustering-activated degraders.Science (New York, N.Y.) · 2024Article
- Design of Oscillatory Networks through Post-Translational Control of Network Components.Synthetic biology and engineering · 2023Article
- Protease-controlled secretion and display of intercellular signals.Nature communications · 2022Article
- Investigating Conformational Dynamics and Allostery in the p53 DNA-Binding Domain Using Molecular Simulations.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Optogenetic activation of intracellular antibodies for direct modulation of endogenous proteins.Nature methods · 2019Article
- Nb-induced stabilisation of p53 in HPV-infected cells.Scientific reports · 2019Article
- Advances and challenges in targeting IRF5, a key regulator of inflammation.The FEBS journal · 2019Review
- p53-Pirh2 Complex Promotes Twist1 Degradation and Inhibits EMT.Molecular cancer research : MCR · 2019Article
- Intracellular displacement of p53 using transactivation domain (p53 TAD) specific nanobodies.mAbs · 2018Article
- Escherichia coli surface display for the selection of nanobodies.Microbial biotechnology · 2017Review
- Nanobody Technology: A Versatile Toolkit for Microscopic Imaging, Protein-Protein Interaction Analysis, and Protein Function Exploration.Frontiers in immunology · 2017Review
- DNA-binding protects p53 from interactions with cofactors involved in transcription-independent functions.Nucleic acids research · 2016Article
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The p53 transcription factor plays an important role in genome integrity. To perform this task, p53 regulates the transcription of genes promoting various cellular outcomes including cell cycle arrest, apoptosis or senescence. The precise regulation of this activity remains elusive as numerous mechanisms, e.g. posttranslational modifications of p53 and (non-)covalent p53 binding partners, influence the p53 transcriptional program. We developed a novel, non-invasive tool to manipulate endogenous p53. Nanobodies (Nb), raised against the DNA-binding domain of p53, allow us to distinctively target both wild type and mutant p53 with great specificity. Nb3 preferentially binds 'structural' mutant p53, i.e. R175H and R282W, while a second but distinct nanobody, Nb139, binds both mutant and wild type p53. The co-crystal structure of the p53 DNA-binding domain in complex with Nb139 (1.9 Å resolution) reveals that Nb139 binds opposite the DNA-binding surface. Furthermore, we demonstrate that Nb139 does not disturb the functional architecture of the p53 DNA-binding domain using conformation-specific p53 antibody immunoprecipitations, glutaraldehyde crosslinking assays and chromatin immunoprecipitation. Functionally, the binding of Nb139 to p53 allows us to perturb the transactivation of p53 target genes. We propose that reduced recruitment of transcriptional co-activators or modulation of selected post-transcriptional modifications account for these observations.
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