ArticleScience advances2023
Cryo-EM structure of the human Sirtuin 6-nucleosome complex.
Article in Science advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
15 citing papers in PubMed, 38 citations in OpenAlex.
- BRD4 binds the nucleosome via both histone and DNA interactions.Molecular cell · 2026Article
- Histone modification cross-talk: analytical tools and molecular mechanisms.The Biochemical journal · 2026Review
- Sirtuins as Therapeutic Targets for Treating Cancer, Metabolic Diseases, and Neurodegenerative Diseases.Pharmaceuticals (Basel, Switzerland) · 2025Review
- Kinetic Analysis of HDAC- and Sirtuin-Mediated Deacylation on Chemically Defined Histones and Nucleosomes.Current protocols · 2025Article
- Sirtuins in Central Nervous System Tumors-Molecular Mechanisms and Therapeutic Targeting.Cells · 2025Review
- A large-scale curated and filterable dataset for cryo-EM foundation model pre-training.Scientific data · 2025Article
- Structural and enzymatic plasticity of SIRT6 deacylase activity.The Journal of biological chemistry · 2025Article
- Structural basis of SIRT7 nucleosome engagement and substrate specificity.Nature communications · 2025Article
- FRET analysis of the unwrapping of nucleosomal DNA containing a sequence characteristic of the + 1 nucleosome.Scientific reports · 2025Article
- Structural Insights Into centSIRT6: Bioinformatic Analysis of N308K and A313S Substitution Effects.Bioinformatics and biology insights · 2025Article
- Mechanisms of DNA Methylation Regulatory Function and Crosstalk with Histone Lysine Methylation.Journal of molecular biology · 2024Review
- Article
- Antiaging Strategies and Remedies: A Landscape of Research Progress and Promise.ACS chemical neuroscience · 2024Review
- Structure of the complete Saccharomyces cerevisiae Rpd3S-nucleosome complex.Nature communications · 2023Article
- Deciphering the Allosteric Activation Mechanism of SIRT6 Using Molecular Dynamics Simulations.Journal of chemical information and modeling · 2023Article
Corrections and comments
- Update of
Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Sirtuin 6 (SIRT6) is a multifaceted protein deacetylase/deacylase and a major target for small-molecule modulators of longevity and cancer. In the context of chromatin, SIRT6 removes acetyl groups from histone H3 in nucleosomes, but the molecular basis for its nucleosomal substrate preference is unknown. Our cryo-electron microscopy structure of human SIRT6 in complex with the nucleosome shows that the catalytic domain of SIRT6 pries DNA from the nucleosomal entry-exit site and exposes the histone H3 N-terminal helix, while the SIRT6 zinc-binding domain binds to the histone acidic patch using an arginine anchor. In addition, SIRT6 forms an inhibitory interaction with the C-terminal tail of histone H2A. The structure provides insights into how SIRT6 can deacetylate both H3 K9 and H3 K56.
Indexed as
Identifiers
What OpenQuestion holds
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.