Evidence map›Paper›PMID 23202585›Full record

ArticleNature structural & molecular biology2013

The ATPase domain of ISWI is an autonomous nucleosome remodeling machine.

Felix Mueller-Planitz, Henrike Klinker, Johanna Ludwigsen, Peter B Becker

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing 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

56 citing papers in PubMed, 87 citations in OpenAlex.

  1. Remodeling of Individual Nucleosomes in Nucleosome Arrays.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  2. Article
  3. ISWI catalyzes nucleosome sliding in condensed nucleosome arrays.Nature structural & molecular biology · 2024
    Article
  4. Article
  5. Article
  6. ISWI catalyzes nucleosome sliding in condensed nucleosome arrays.bioRxiv : the preprint server for biology · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Chromatin-Remodelling ATPasesInternational journal of molecular sciences · 2022
    Article
  12. Article
  13. Review
  14. Article
  15. Review
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  17. Review
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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.

Felix Mueller-PlanitzAdolf Butenandt Institut, Ludwig-Maximilians-Universität, Munich, Germany. Felix.Mueller-Planitz@med.uni-muenchen.de
Henrike Klinker
Johanna Ludwigsen
Peter B Becker
Ludwig-Maximilians-Universität München · DECenter for Integrated Protein Science Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ISWI slides nucleosomes along DNA, enabling the structural changes of chromatin required for the regulated use of eukaryotic genomes. Prominent mechanistic models imply cooperation of the ISWI ATPase domain with a C-terminal DNA-binding function residing in the HAND-SANT-SLIDE (HSS) domain. Contrary to these models, we show by quantitative biochemical means that all fundamental aspects of nucleosome remodeling are contained within the compact ATPase module of Drosophila ISWI. This domain can independently associate with DNA and nucleosomes, which in turn activate ATP turnover by inducing a conformational change in the enzyme, and it can autonomously reposition nucleosomes. The role of the HSS domain is to increase the affinity and specificity for nucleosomes. Nucleosome-remodeling enzymes may thus have evolved directly from ancestral helicase-type motors, and peripheral domains have furnished regulatory capabilities that bias the remodeling reaction toward different structural outcomes.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAnimalsBinding SitesChromatinChromatin Assembly and DisassemblyDNADNA-Binding ProteinsDrosophila melanogasterDrosophila ProteinsHistonesNucleosomesProtein BindingProtein ConformationProtein Structure, TertiaryTranscription FactorsAdenosine TriphosphatasesAdenosine TriphosphateChromatinDNADNA-Binding ProteinsDrosophila ProteinsHistonesISWI proteinNucleosomesTranscription Factors

Identifiers

PMID23202585
OpenAlexW2038124186

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.