ArticleCell2006
Structural basis for the histone chaperone activity of Asf1.
Article in Cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 283 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
283 citing papers in PubMed, 447 citations in OpenAlex.
- Downsizing the Histone H3-H4 Quaternary Structure Into Foldamer Mimetics Yields High-Affinity and Cell-Permeable Ligands of ASF1.Angewandte Chemie (International ed. in English) · 2026Article
- ASF1A: A versatile histone chaperone bridging chromatin dynamics, disease mechanisms and clinical potential (Review).Experimental and therapeutic medicine · 2026Review
- Newly synthesized histones: passive or active players in the regulation of epigenetic inheritance?Nucleic acids research · 2026Review
- Anemia-associated mutations disrupt the CDIN1-Codanin1 complex in inherited congenital dyserythropoietic anemia I (CDA-I) disease.The FEBS journal · 2026Article
- Co-Phosphoregulatory Network Underlying Functional Coherence of TLK1 and TLK2 Kinase Paralogs.International journal of molecular sciences · 2026Article
- Histone Nuclear Import and Beyond: Multifunctional Roles of Importins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Article
- Histone supply: a precious commodity for cell identity.The Biochemical journal · 2025Review
- Physiology and molecular biology of plants : an international journal of functional plant biology · 2025Article
- Insights into the synchronization between DNA replication and parental histone recycling.Biochemical Society transactions · 2025Review
- RBAP48 facilitates the oral squamous cell carcinoma process in an androgen receptor-dependent and independent manners.Communications biology · 2025Article
- Always on the Move: Overview on Chromatin Dynamics within Nuclear Processes.Biochemistry · 2025Review
- Histone tetrasome dynamics affects chromatin transcription.Nucleic acids research · 2025Article
- CODANIN-1 sequesters ASF1 by using a histone H3 mimic helix to regulate the histone supply.Nature communications · 2025Article
- The ortholog of human DNAJC9 promotes histone H3-H4 degradation and is counteracted by Asf1 in fission yeast.Nucleic acids research · 2025Article
- H3K56 acetylation regulates chromatin maturation following DNA replication.Nature communications · 2025Article
- Repair of replication-dependent double-strand breaks differs between the leading and lagging strands.Molecular cell · 2025Article
- Stepwise order in protein complex assembly: approaches and emerging themes.Open biology · 2025Review
- Replication-coupled inheritance of chromatin states.Cell insight · 2024Review
- Tackling Undruggable Targets with Designer Peptidomimetics and Synthetic Biologics.Chemical reviews · 2024Review
223 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Anti-silencing function 1 (Asf1) is a highly conserved chaperone of histones H3/H4 that assembles or disassembles chromatin during transcription, replication, and repair. The structure of the globular domain of Asf1 bound to H3/H4 determined by X-ray crystallography to a resolution of 1.7 Angstroms shows how Asf1 binds the H3/H4 heterodimer, enveloping the C terminus of histone H3 and physically blocking formation of the H3/H4 heterotetramer. Unexpectedly, the C terminus of histone H4 that forms a mini-beta sheet with histone H2A in the nucleosome undergoes a major conformational change upon binding to Asf1 and adds a beta strand to the Asf1 beta sheet sandwich. Interactions with both H3 and H4 were required for Asf1 histone chaperone function in vivo and in vitro. The Asf1-H3/H4 structure suggests a "strand-capture" mechanism whereby the H4 tail acts as a lever to facilitate chromatin disassembly/assembly that may be used ubiquitously by histone chaperones.
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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.