Evidence map›Paper›PMID 29018282›Full record

ReviewNature reviews. Molecular cell biology2018

Emerging roles of linker histones in regulating chromatin structure and function.

Dmitry V Fyodorov, Bing-Rui Zhou, Arthur I Skoultchi, Yawen Bai

Open access · greenAbstract readReview
In one paragraph

Review in Nature reviews. Molecular cell biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 279 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
279citing papers in PubMed, 2 pooled it
16.3field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

279 citing papers in PubMed, 2 syntheses or guidelines pooled it, 489 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Review
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  5. Article
  6. Review
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  9. G-Quadruplexes: Structural Diversity and Emerging Roles in Biomolecular Condensation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Histone Density and Dynamics Shape Mitotic Chromatid Architecture in Xenopus Egg Extracts.Genes to cells : devoted to molecular & cellular mechanisms · 2026
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review

219 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Dmitry V FyodorovDepartment of Cell Biology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Bing-Rui ZhouLaboratory of Biochemistry and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
Arthur I SkoultchiDepartment of Cell Biology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Yawen BaiLaboratory of Biochemistry and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
Albert Einstein College of Medicine · USNational Cancer Institute · US

Funding

Nucleosome DynamicsZIABC010808 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI BAI, YAWEN · 2009 to 2025
$26.5M
Chromatin Transitions during Early Embryonic Development in Drosophila melanogasterR01GM074233 · NIGMS · ALBERT EINSTEIN COL OF MED YESHIVA UNIV · PI FYODOROV, DMITRY V · 2005 to 2021
$5.8M
Functions of Mammalian H1 Linker Histones in Gene Regulation and DevelopmentR01GM116143 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI SKOULTCHI, ARTHUR I · 2015 to 2018
$1.9M
Drosophila Linker Histone H1 Functions in Chromosome Architecture and ActivityR01GM093190 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI SKOULTCHI, ARTHUR I · 2011 to 2014
$1.6M
Regulation of Nuclear Functions by Drosophila Linker Histone H1R01GM129244 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI FYODOROV, DMITRY V, SKOULTCHI, ARTHUR I · 2018 to 2021
$1.5M
NIGMS NIH HHS R01 GM074233NIGMS NIH HHS R01 GM093190NIGMS NIH HHS R01 GM116143NIGMS NIH HHS R01 GM129244
6 · The paper itself

Abstract

Together with core histones, which make up the nucleosome, the linker histone (H1) is one of the five main histone protein families present in chromatin in eukaryotic cells. H1 binds to the nucleosome to form the next structural unit of metazoan chromatin, the chromatosome, which may help chromatin to fold into higher-order structures. Despite their important roles in regulating the structure and function of chromatin, linker histones have not been studied as extensively as core histones. Nevertheless, substantial progress has been made recently. The first near-atomic resolution crystal structure of a chromatosome core particle and an 11 Å resolution cryo-electron microscopy-derived structure of the 30 nm nucleosome array have been determined, revealing unprecedented details about how linker histones interact with the nucleosome and organize higher-order chromatin structures. Moreover, several new functions of linker histones have been discovered, including their roles in epigenetic regulation and the regulation of DNA replication, DNA repair and genome stability. Studies of the molecular mechanisms of H1 action in these processes suggest a new paradigm for linker histone function beyond its architectural roles in chromatin.

Indexed as

Amino Acid SequenceAnimalsChromatinChromatin Assembly and DisassemblyDNADNA RepairDNA ReplicationEpigenesis, GeneticGenetic VariationGenomic InstabilityHistonesHumansModels, BiologicalModels, MolecularNucleic Acid ConformationNucleosomesChromatinDNAHistonesNucleosomes

Identifiers

PMID29018282
PMCPMC5897046
OpenAlexW2763769301

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.