Evidence map›Paper›PMID 21810178›Full record

ReviewThe FEBS journal2011

Mechanisms for ATP-dependent chromatin remodelling: the means to the end.

Andrew Flaus, Tom Owen-Hughes

Open access · bronzeAbstract readReview
In one paragraph

Review in The FEBS journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

69 citing papers in PubMed, 121 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Remodeling of Individual Nucleosomes in Nucleosome Arrays.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  5. Review
  6. Article
  7. Article
  8. Fun30 nucleosome remodeller regulates white-to-opaque switching inActa biochimica et biophysica Sinica · 2023
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Short Peptides Induce Development of Root HairPlants (Basel, Switzerland) · 2022
    Article
  14. Article
  15. Article
  16. Eyes on CHARGE syndrome: Roles of CHD7 in ocular development.Frontiers in cell and developmental biology · 2022
    Review
  17. Article
  18. Article
  19. Article
  20. Article

9 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

2 authors at 2 institutions in 2 countries.

Andrew FlausCentre for Chromosome Biology, Biochemistry, School of Natural Sciences, National University of Ireland Galway, Galway, Ireland. andrew.flaus@nuigalway.ie
Tom Owen-Hughes
Ollscoil na Gaillimhe – University of Galway · IEWellcome Trust · GB

Funding

Wellcome Trust 064414Wellcome Trust 095062
6 · The paper itself

Abstract

Chromatin remodelling is the ATP-dependent change in nucleosome organisation driven by Snf2 family ATPases. The biochemistry of this process depends on the behaviours of ATP-dependent motor proteins and their dynamic nucleosome substrates, which brings significant technical and conceptual challenges. Steady progress has been made in characterising the polypeptides of which these enzymes are comprised. Divergence in the sequences of different subfamilies of Snf2-related proteins suggests that the motors are adapted for different functions. Recently, structural insights have suggested that the Snf2 ATPase acts as a context-sensitive DNA translocase. This may have arisen as a means to enable efficient access to DNA in the high density of the eukaryotic nucleus. How the enzymes engage nucleosomes and how the network of noncovalent interactions within the nucleosome respond to the force applied remains unclear, and it remains prudent to recognise the potential for both DNA distortions and dynamics within the underlying histone octamer structure.

Indexed as

Chromatin Assembly and DisassemblyAdenosine TriphosphatasesAdenosine TriphosphateAllosteric RegulationAnimalsChromatinDNAHumansMacromolecular SubstancesModels, MolecularNucleosomesProtein ConformationSaccharomyces cerevisiae ProteinsTranscription FactorsAdenosine TriphosphatasesAdenosine TriphosphateChromatinDNAMacromolecular SubstancesNucleosomesSaccharomyces cerevisiae ProteinsSNF2 protein, S cerevisiaeTranscription Factors

Identifiers

PMID21810178
PMCPMC4162296
OpenAlexW2145968307

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.