ReviewEpigenetics2010
Reading chromatin: insights from yeast into YEATS domain structure and function.
Review in Epigenetics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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.
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
29 citing papers in PubMed.
- The impact of microbial metabolites on host chromatin and epigenetic regulation.Nature metabolism · 2026Review
- A chemical-genetic interaction between PAF1 and ENL/AF9 YEATS inhibition.RSC chemical biology · 2026Article
- Functional Roles and Mechanistic Insights of YEATS Domain Proteins in Digestive System Tumors.Digestive diseases and sciences · 2025Review
- Class IIa HDACs Are Important Signal Transducers with Unclear Enzymatic Activities.Biomolecules · 2025Review
- YEATS2 promotes malignant phenotypes of esophageal squamous cell carcinoma via H3K27ac activated-IL6ST.Frontiers in cell and developmental biology · 2025Article
- A potent and selective ENL degrader suppresses oncogenic gene expression and leukemia progression.Science advances · 2024Article
- Histone H3 lysine 27 crotonylation mediates gene transcriptional repression in chromatin.Molecular cell · 2023Article
- Mechanistic insights into genomic structure and functions of a novel oncogene YEATS4.Frontiers in cell and developmental biology · 2023Review
- Recognition of acetylated histone by Yaf9 regulates metabolic cycling of transcription initiation and chromatin regulatory factors.Genes & development · 2021Article
- Discovery of Selective Small-Molecule Inhibitors for the ENL YEATS Domain.Journal of medicinal chemistry · 2021Article
- The role of the Acanthamoeba castellanii Sir2-like protein in the growth and encystation of Acanthamoeba.Parasites & vectors · 2020Article
- Hdac4 Interactions in Huntington's Disease Viewed Through the Prism of Multiomics.Molecular & cellular proteomics : MCP · 2019Article
- Order in Disorder as Observed by the "Hydrophobic Cluster Analysis" of Protein Sequences.Proteomics · 2018Review
- GAS41 Recognizes Diacetylated Histone H3 through a Bivalent Binding Mode.ACS chemical biology · 2018Article
- re-TAMD: exploring interactions between H3 peptide and YEATS domain using enhanced sampling.BMC structural biology · 2018Article
- Yaf9 subunit of the NuA4 and SWR1 complexes targets histone H3K27ac through its YEATS domain.Nucleic acids research · 2018Article
- Merge and separation of NuA4 and SWR1 complexes control cell fate plasticity inCell discovery · 2018Article
- Acetylation on histone H3 lysine 9 mediates a switch from transcription initiation to elongation.The Journal of biological chemistry · 2017Article
- YEATS domain: Linking histone crotonylation to gene regulation.Transcription · 2017Article
- Reading and Interpreting the Histone Acylation Code.Genomics, proteomics & bioinformatics · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Chromatin-modifying complexes typically contain signature domains that either have catalytic activity or recognize and bind to specific histone modifications such as acetylation, methylation, and phosphorylation. Despite tremendous progress in this area, much remains to be learned in particular about the mechanistic functions of less well characterized signature domains. One such module is the evolutionary conserved YEATS domain, found in a variety of chromatin-modifying and transcription complexes from yeast to human. Three yeast proteins contain a YEATS domain, including Yaf9, a subunit of both the histone variant H2A.Z deposition complex SWR1-C and the histone acetyltransferase complex NuA4. The three-dimensional structure of the YEATS domain from Yaf9 was solved recently, revealing the existence of three distinct structural regions. One region is characterized by a shallow groove that might constitute a potential acetyl-lysine binding pocket, raising questions about potential protein interaction partners of the Yaf9 YEATS domain.
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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.