ArticleScience (New York, N.Y.)2011
Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0 Å resolution.
Article in Science (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 169 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
169 citing papers in PubMed, 268 citations in OpenAlex.
- BRD4 binds the nucleosome via both histone and DNA interactions.Molecular cell · 2026Article
- Physical interactions within the SIR heterochromatin complex potentiate inter-subunit communication and gene repression.Cell reports · 2026Article
- Different modes of engagement with the nucleosome acidic patch yield distinct functional outcomes.Nucleic acids research · 2026Article
- A Chromatin Biology Assessment of AlphaFold3.bioRxiv : the preprint server for biology · 2026Article
- Histone 3 lysine 9 dimethylation by the G9a-GLP heterodimer requires intranucleosomal product reading.bioRxiv : the preprint server for biology · 2026Article
- Different modes of engagement with the nucleosome acidic patch yield distinct functional outcomes.bioRxiv : the preprint server for biology · 2026Article
- Article
- Article
- Transcriptional silencing in Saccharomyces cerevisiae: known unknowns.Epigenetics & chromatin · 2024Review
- Ubiquitinated histone H2B as gatekeeper of the nucleosome acidic patch.Nucleic acids research · 2024Article
- Cancer-associated DNA hypermethylation of Polycomb targets requires DNMT3A dual recognition of histone H2AK119 ubiquitination and the nucleosome acidic patch.Science advances · 2024Article
- Review
- Yeast heterochromatin stably silences only weak regulatory elements by altering burst duration.Cell reports · 2024Article
- Minimal requirements for the epigenetic inheritance of engineered silent chromatin domains.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The odyssey of cGAS: From cytosol to nucleus.Cytokine & growth factor reviews · 2023Review
- Regulation of the heterochromatin spreading reaction byOpen biology · 2023Review
- Yeast Heterochromatin Only Stably Silences Weak Regulatory Elements by Altering Burst Duration.bioRxiv : the preprint server for biology · 2023Article
- Structural basis of histone H2A lysine 119 deubiquitination by Polycomb repressive deubiquitinase BAP1/ASXL1.Science advances · 2023Article
- A potential histone-chaperone activity for the MIER1 histone deacetylase complex.Nucleic acids research · 2023Article
- Catalytic and non-catalytic mechanisms of histone H4 lysine 20 methyltransferase SUV420H1.bioRxiv : the preprint server for biology · 2023Article
109 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Gene silencing is essential for regulating cell fate in eukaryotes. Altered chromatin architectures contribute to maintaining the silenced state in a variety of species. The silent information regulator (Sir) proteins regulate mating type in Saccharomyces cerevisiae. One of these proteins, Sir3, interacts directly with the nucleosome to help generate silenced domains. We determined the crystal structure of a complex of the yeast Sir3 BAH (bromo-associated homology) domain and the nucleosome core particle at 3.0 angstrom resolution. We see multiple molecular interactions between the protein surfaces of the nucleosome and the BAH domain that explain numerous genetic mutations. These interactions are accompanied by structural rearrangements in both the nucleosome and the BAH domain. The structure explains how covalent modifications on H4K16 and H3K79 regulate formation of a silencing complex that contains the nucleosome as a central component.
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.