Evidence map›Paper›PMID 19794910›Full record

ArticlePloS one2009

Histone H1 subtypes differentially modulate chromatin condensation without preventing ATP-dependent remodeling by SWI/SNF or NURF.

Jaime Clausell, Nicole Happel, Tracy K Hale, Detlef Doenecke, Miguel Beato

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

70 citing papers in PubMed, 143 citations in OpenAlex.

  1. Linker H1 Histone Direct Top-Down Proteoform Analysis.Journal of proteome research · 2025
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  13. Review
  14. Molecular and Cellular Functions of the Linker Histone H1.2.Frontiers in cell and developmental biology · 2021
    Review
  15. The missing linkGenes & development · 2021
    Review
  16. Histone H1 Post-Translational Modifications: Update and Future Perspectives.International journal of molecular sciences · 2020
    Review
  17. Article
  18. Review
  19. Article
  20. Article

10 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

5 authors at 3 institutions in 3 countries.

Jaime ClausellCentre de Regulació Genòmica (CRG), Universitat Pompeu Fabra, Barcelona, Spain.
Nicole Happel
Tracy K Hale
Detlef Doenecke
Miguel Beato
Pompeu Fabra University · ESUniversity of Göttingen · DEUniversity of Otago · NZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although ubiquitously present in chromatin, the function of the linker histone subtypes is partly unknown and contradictory studies on their properties have been published. To explore whether the various H1 subtypes have a differential role in the organization and dynamics of chromatin we have incorporated all of the somatic human H1 subtypes into minichromosomes and compared their influence on nucleosome spacing, chromatin compaction and ATP-dependent remodeling. H1 subtypes exhibit different affinities for chromatin and different abilities to promote chromatin condensation, as studied with the Atomic Force Microscope. According to this criterion, H1 subtypes can be classified as weak condensers (H1.1 and H1.2), intermediate condensers (H1.3) and strong condensers (H1.0, H1.4, H1.5 and H1x). The variable C-terminal domain is required for nucleosome spacing by H1.4 and is likely responsible for the chromatin condensation properties of the various subtypes, as shown using chimeras between H1.4 and H1.2. In contrast to previous reports with isolated nucleosomes or linear nucleosomal arrays, linker histones at a ratio of one per nucleosome do not preclude remodeling of minichromosomes by yeast SWI/SNF or Drosophila NURF. We hypothesize that the linker histone subtypes are differential organizers of chromatin, rather than general repressors.

Indexed as

Gene Expression RegulationAdenosine TriphosphateAnimalsChromatinChromatin Assembly and DisassemblyChromosomal Proteins, Non-HistoneChromosomesDrosophila melanogasterDrosophila ProteinsHeLa CellsHistonesHumansMicroscopy, Atomic ForceNucleosomesProtein BindingProtein Structure, TertiaryAdenosine TriphosphateCaf1-55 protein, DrosophilaChromatinChromosomal Proteins, Non-HistoneDrosophila ProteinsHistonesNucleosomesRetinoblastoma-Binding Protein 4SWI-SNF-B chromatin-remodeling complexTranscription Factors

Identifiers

PMID19794910
PMCPMC2748705
OpenAlexW1984184017

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.