ArticleACS chemical biology2018
GAS41 Recognizes Diacetylated Histone H3 through a Bivalent Binding Mode.
Article in ACS chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 43 citations in OpenAlex.
- Structural mechanism of histone H2A.Z exchange by human SRCAP-CFDP1 holoenzyme.Science advances · 2026Article
- Discovery and Development of a Small-Molecule Inhibitor Targeting the GAS41 YEATS Domain in Nonsmall Cell Lung Cancer.Journal of medicinal chemistry · 2025Article
- The human chromatin remodeling complex p400 restricts HIV-1 transcription in a Tat-dependent manner.Nucleic acids research · 2025Article
- Chromatin Regulatory Targets for Anticancer Therapeutics.Chemical reviews · 2025Review
- H2A.Z is essential for oocyte maturation and fertility in female mouse.Nature structural & molecular biology · 2025Article
- YEATS2: a novel cancer epigenetic reader and potential therapeutic target.Cancer cell international · 2025Review
- Epigenetics-targeted drugs: current paradigms and future challenges.Signal transduction and targeted therapy · 2024Review
- Structures of H2A.Z-associated human chromatin remodelers SRCAP and TIP60 reveal divergent mechanisms of chromatin engagement.bioRxiv : the preprint server for biology · 2024Article
- Development of Complementary Photo-arginine/lysine to Promote Discovery of Arg/Lys hPTMs Interactomes.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- GAS41 modulates ferroptosis by anchoring NRF2 on chromatin.Nature communications · 2024Article
- Structural insights into histone exchange by human SRCAP complex.Cell discovery · 2024Article
- Small-molecule tools for YEATS domain proteins.Current opinion in chemical biology · 2023Review
- GAS41 promotes H2A.Z deposition through recognition of the N terminus of histone H3 by the YEATS domain.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Unveiling the role of GAS41 in cancer progression.Cancer cell international · 2023Review
- Histone H3 lysine 27 crotonylation mediates gene transcriptional repression in chromatin.Molecular cell · 2023Article
- Histone Readers and Their Roles in Cancer.Cancer treatment and research · 2023Article
- Mechanistic insights into genomic structure and functions of a novel oncogene YEATS4.Frontiers in cell and developmental biology · 2023Review
- Multifaceted roles of YEATS domain-containing proteins and novel links to neurological diseases.Cellular and molecular life sciences : CMLS · 2022Review
- Development of potent dimeric inhibitors of GAS41 YEATS domain.Cell chemical biology · 2021Article
- Toward a Personalized Therapy in Soft-Tissue Sarcomas: State of the Art and Future Directions.Cancers · 2021Review
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
GAS41 is a chromatin-associated protein that belongs to the YEATS family and is involved in the recognition of acetyl-lysine in histone proteins. A unique feature of GAS41 is the presence of a C-terminal coiled-coil domain, which is responsible for protein dimerization. Here, we characterized the specificity of the GAS41 YEATS domain and found that it preferentially binds to acetylated H3K18 and H3K27 peptides. Interestingly, we found that full-length, dimeric GAS41 binds to diacetylated H3 peptides with an enhanced affinity when compared to those for monoacetylated peptides, through a bivalent binding mode. We determined the crystal structure of the GAS41 YEATS domain with H3K23acK27ac to visualize the molecular basis of diacetylated histone binding. Our results suggest a unique binding mode in which full-length GAS41 is a reader of diacetylated histones.
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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.