Evidence map›Paper›PMID 24218562›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Structural insights into the histone H1-nucleosome complex.

Bing-Rui Zhou, Hanqiao Feng, Hidenori Kato, Liang Dai, Yuedong Yang, Yaoqi Zhou, Yawen Bai

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 123 papers.

0numbers the graph read from it
0cells of the map it votes in
123citing papers in PubMed
8.8field-weighted citation impact, top 2% 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

123 citing papers in PubMed, 215 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Histone Nuclear Import and Beyond: Multifunctional Roles of Importins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  8. Article
  9. Article
  10. Interrogating the regulatory epigenome of cellular senescence.Cellular and molecular life sciences : CMLS · 2025
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Beyond the mono-nucleosome.Biochemical Society transactions · 2025
    Review
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article

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

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

7 authors at 4 institutions in 1 country.

Bing-Rui ZhouLaboratory of Biochemistry and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.
Hanqiao Feng
Hidenori Kato
Liang Dai
Yuedong Yang
Yaoqi Zhou
Yawen Bai
Indiana University – Purdue University Indianapolis · USNational Cancer Institute · USCenter for Cancer Research · USNational Institutes of Health · US

Funding

Statistical Energy Functions: a Fragment-based ApproachR01GM085003 · NIGMS · INDIANA UNIVERSITY INDIANAPOLIS · PI ZHOU, YAOQI · 2008 to 2011
$1.1M
Intramural NIH HHSNIGMS NIH HHS R01 GM085003NIGMS NIH HHS R01GM085003
6 · The paper itself

Abstract

Linker H1 histones facilitate formation of higher-order chromatin structures and play important roles in various cell functions. Despite several decades of effort, the structural basis of how H1 interacts with the nucleosome remains elusive. Here, we investigated Drosophila H1 in complex with the nucleosome, using solution nuclear magnetic resonance spectroscopy and other biophysical methods. We found that the globular domain of H1 bridges the nucleosome core and one 10-base pair linker DNA asymmetrically, with its α3 helix facing the nucleosomal DNA near the dyad axis. Two short regions in the C-terminal tail of H1 and the C-terminal tail of one of the two H2A histones are also involved in the formation of the H1-nucleosome complex. Our results lead to a residue-specific structural model for the globular domain of the Drosophila H1 in complex with the nucleosome, which is different from all previous experiment-based models and has implications for chromatin dynamics in vivo.

Indexed as

Models, MolecularMolecular ConformationAmino Acid SequenceCalorimetryHistonesMacromolecular SubstancesMagnetic Resonance SpectroscopyMolecular Sequence DataMutagenesis, Site-DirectedNucleosomesProtein BindingHistonesMacromolecular SubstancesNucleosomes

Identifiers

PMID24218562
PMCPMC3845106
OpenAlexW1993646828

What OpenQuestion holds

Textmetadata
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.