ArticleNature communications2025
Multivalent binding of the tardigrade Dsup protein to chromatin promotes yeast survival and longevity upon exposure to oxidative damage.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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.
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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.
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Who cites it
12 citing papers in PubMed.
- PBRM1-dependent PBAF targeting is required for EMT and metastasis in breast cancer.Science advances · 2026Article
- Different modes of engagement with the nucleosome acidic patch yield distinct functional outcomes.Nucleic acids research · 2026Article
- Integrative bioinformatics analysis of potential convergent evolution in tardigrade stress-response proteins.Stress biology · 2026Article
- Insights into Tardigrade Damage-Suppression Protein, Dsup.Biomolecules · 2026Review
- Structural and Biochemical Characterization of an Atypical α-Carbonic Anhydrase from the TardigradeMolecules (Basel, Switzerland) · 2026Article
- Different modes of engagement with the nucleosome acidic patch yield distinct functional outcomes.bioRxiv : the preprint server for biology · 2026Article
- Biochemical and Structural Analyses of the Tardigrade DNA-Damage Suppressor Protein, Dsup.Journal of molecular biology · 2025Article
- Tardigrade Dsup extendsScience advances · 2025Article
- Structural basis of nucleosome recognition by the conserved Dsup and HMGN nucleosome-binding motif.Genes & development · 2025Article
- Radioprotection of healthy tissue via nanoparticle-delivered mRNA encoding for a damage-suppressor protein found in tardigrades.Nature biomedical engineering · 2025Article
- Structural basis of nucleosome recognition by the conserved Dsup and HMGN nucleosome-binding motif.bioRxiv : the preprint server for biology · 2025Article
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Authors and funding
24 authors.
Funding
Abstract
Tardigrades are remarkable in their ability to survive extreme environments. The damage suppressor (Dsup) protein is thought to contribute to their extreme resistance to reactive oxygen species (ROS) generated by irradiation. Here we show that expression of Ramazzottius varieornatus Dsup in Saccharomyces cerevisiae reduces oxidative DNA damage and extends lifespan in response to chronic oxidative genotoxicity. Dsup uses multiple modes of engagement with the nucleosomal H2A/H2B acidic patch, H3/H4 histone tails and DNA to bind across the yeast genome without bias. Effective chromatin binding and genome protection requires the Dsup HMGN-like motif and C-terminal sequences. These findings give precedent and mechanistic understanding for engineering an organism by physically shielding its genome to promote survival and longevity in the face of oxidative 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.