ReviewProtein science : a publication of the Protein Society2019
Molecular basis for chromatin assembly and modification by multiprotein complexes.
Review in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 15 citations in OpenAlex.
- Epigenetic modulation of ferroptosis in cancer: Identifying epigenetic targets for novel anticancer therapy.Cellular oncology (Dordrecht, Netherlands) · 2023Review
- Chaperoning of the histone octamer by the acidic domain of DNA repair factor APLF.Science advances · 2022Article
- Computational methods and next-generation sequencing approaches to analyze epigenetics data: Profiling of methods and applications.Methods (San Diego, Calif.) · 2021Review
- Interactions With Histone H3 & Tools to Study Them.Frontiers in cell and developmental biology · 2020Review
- SETD1A Methyltransferase Is Physically and Functionally Linked to the DNA Damage Repair Protein RAD18.Molecular & cellular proteomics : MCP · 2019Article
- Sleep and Neurochemical Modulation by DZNep and GSK-J1: Potential Link With Histone Methylation Status.Frontiers in neuroscience · 2019Article
- Fibromyalgia: Genetics and epigenetics insights may provide the basis for the development of diagnostic biomarkers.Molecular painReview
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Epigenetic regulation of the chromatin landscape is often orchestrated through modulation of nucleosomes. Nucleosomes are composed of two copies each of the four core histones, H2A, H2B, H3, and H4, wrapped in ~150 bp of DNA. We focus this review on recent structural studies that further elucidate the mechanisms used by macromolecular complexes to mediate histone modification and nucleosome assembly. Nucleosome assembly, spacing, and variant histone incorporation are coordinated by chromatin remodeler and histone chaperone complexes. Several recent structural studies highlight how disparate families of histone chaperones and chromatin remodelers share similar features that underlie how they interact with their respective histone or nucleosome substrates. Post-translational modification of histone residues is mediated by enzymatic subunits within large complexes. Until recently, relatively little was known about how association with auxiliary subunits serves to modulate the activity and specificity of the enzymatic subunit. Analysis of several recent structures highlights the different modes that auxiliary subunits use to influence enzymatic activity or direct specificity toward individual histone residues.
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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.