Evidence map›Paper›PMID 21170357›Full record

ArticlePLoS genetics2010

Histone H2A C-terminus regulates chromatin dynamics, remodeling, and histone H1 binding.

Christine Vogler, Claudia Huber, Tanja Waldmann, Ramona Ettig, Lora Braun, Annalisa Izzo, Sylvain Daujat, Isabelle Chassignet, Andres Joaquin Lopez-Contreras, Oscar Fernandez-Capetillo and 4 more

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

50 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Histone Tail Cleavage as a Mechanism for Epigenetic Regulation.International journal of molecular sciences · 2024
    Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Histone Tail Conformations: A Fuzzy Affair with DNA.Trends in biochemical sciences · 2021
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

14 authors at 6 institutions in 3 countries.

Christine VoglerMax-Planck Institute of Immunobiology, Freiburg, Germany.
Claudia Huber
Tanja Waldmann
Ramona Ettig
Lora Braun
Annalisa Izzo
Sylvain Daujat
Isabelle Chassignet
Andres Joaquin Lopez-Contreras
Oscar Fernandez-Capetillo
Miroslav Dundr
Karsten Rippe
Gernot Längst
Robert Schneider
Max Planck Institute of Immunobiology and Epigenetics · DESpanish National Cancer Research Centre · ESUniversity of Regensburg · DEGerman Cancer Research Center · DEHeidelberg University · DERosalind Franklin University of Medicine and Science · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The tails of histone proteins are central players for all chromatin-mediated processes. Whereas the N-terminal histone tails have been studied extensively, little is known about the function of the H2A C-terminus. Here, we show that the H2A C-terminal tail plays a pivotal role in regulating chromatin structure and dynamics. We find that cells expressing C-terminally truncated H2A show increased stress sensitivity. Moreover, both the complete and the partial deletion of the tail result in increased histone exchange kinetics and nucleosome mobility in vivo and in vitro. Importantly, our experiments reveal that the H2A C-terminus is required for efficient nucleosome translocation by ISWI-type chromatin remodelers and acts as a novel recognition module for linker histone H1. Thus, we suggest that the H2A C-terminal tail has a bipartite function: stabilisation of the nucleosomal core particle, as well as mediation of the protein interactions that control chromatin dynamics and conformation.

Indexed as

Chromatin Assembly and DisassemblyAmino Acid MotifsCell LineChromatinHistonesHumansNucleosomesProtein BindingChromatinHistonesNucleosomes

Identifiers

PMID21170357
PMCPMC3000355
OpenAlexW1977874695

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.