ArticleNature structural & molecular biology2012
Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX.
Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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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.
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Who cites it
78 citing papers in PubMed, 112 citations in OpenAlex.
- Epigenetics in development, disease, and therapy: from mechanisms to clinical interventions.Science China. Life sciences · 2026Review
- Mechanisms controlling the deposition and dynamics of histone variant H2BE.bioRxiv : the preprint server for biology · 2026Article
- ATRX: From Chromatin Remodeling to Disease.Genesis (New York, N.Y. : 2000) · 2025Review
- Phosphorylation of H3.3 at Serine 31 acts as a switch of nucleosome dynamics for transcription.Nucleic acids research · 2025Article
- Single amino acid mutations in histone H3.3 illuminate the functional significance of H3K4 methylation in plants.Nature communications · 2025Article
- HIRA vs. DAXX: the two axes shaping the histone H3.3 landscape.Experimental & molecular medicine · 2024Review
- Cryo-EM and biochemical analyses of the nucleosome containing the human histone H3 variant H3.8.Journal of biochemistry · 2023Article
- Stitched peptides as potential cell permeable inhibitors of oncogenic DAXX protein.RSC chemical biology · 2023Article
- The cell-cycle choreography of H3 variants shapes the genome.Molecular cell · 2023Review
- Histone Variants and Their Chaperones in Hematological Malignancies.HemaSphere · 2023Review
- DAXX drives de novo lipogenesis and contributes to tumorigenesis.Nature communications · 2023Article
- Review
- Review
- Mechanisms of chromatin-based epigenetic inheritance.Science China. Life sciences · 2022Review
- The Role of the TSK/TONSL-H3.1 Pathway in Maintaining Genome Stability in Multicellular Eukaryotes.International journal of molecular sciences · 2022Review
- NASP maintains histone H3-H4 homeostasis through two distinct H3 binding modes.Nucleic acids research · 2022Article
- Topography of histone H3-H4 interaction with the Hat1-Hat2 acetyltransferase complex.Genes & development · 2022Article
- De novo variants in H3-3A and H3-3B are associated with neurodevelopmental delay, dysmorphic features, and structural brain abnormalities.NPJ genomic medicine · 2021Article
- Distinct histone H3-H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones.Genes & development · 2021Article
- Surprising phenotypic diversity of cancer-associated mutations of Gly 34 in the histone H3 tail.eLife · 2021Article
18 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Mammalian histone H3.3 is a variant of the canonical H3.1 essential for genome reprogramming in fertilized eggs and maintenance of chromatin structure in neuronal cells. An H3.3-specific histone chaperone, DAXX, directs the deposition of H3.3 onto pericentric and telomeric heterochromatin. H3.3 differs from H3.1 by only five amino acids, yet DAXX can distinguish the two with high precision. By a combination of structural, biochemical and cell-based targeting analyses, we show that Ala87 and Gly90 are the principal determinants of human H3.3 specificity. DAXX uses a shallow hydrophobic pocket to accommodate the small hydrophobic Ala87 of H3.3, whereas a polar binding environment in DAXX prefers Gly90 in H3.3 over the hydrophobic Met90 in H3.1. An H3.3-H4 heterodimer is bound by the histone-binding domain of DAXX, which makes extensive contacts with both H3.3 and H4.
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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.