Evidence map›Paper›PMID 21329878›Full record

ArticleMolecular cell2011

The histone chaperones Nap1 and Vps75 bind histones H3 and H4 in a tetrameric conformation.

Andrew Bowman, Richard Ward, Nicola Wiechens, Vijender Singh, Hassane El-Mkami, David George Norman, Tom Owen-Hughes

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

54 citing papers in PubMed, 79 citations in OpenAlex.

  1. Review
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  3. Review
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  8. Review
  9. Review
  10. Chromatin regulation and dynamics in stem cells.Current topics in developmental biology · 2020
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Histone chaperone networks shaping chromatin function.Nature reviews. Molecular cell biology · 2017
    Review
  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

7 authors at 3 institutions in 1 country.

Andrew BowmanWellcome Trust Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Dundee DD15EH, UK.
Richard Ward
Nicola Wiechens
Vijender Singh
Hassane El-Mkami
David George Norman
Tom Owen-Hughes
University of Dundee · GBWellcome Trust · GBUniversity of St Andrews · GB

Funding

Biotechnology and Biological Sciences Research Council BB/E022286/1Wellcome Trust 064414Wellcome Trust 095062
6 · The paper itself

Abstract

Histone chaperones physically interact with histones to direct proper assembly and disassembly of nucleosomes regulating diverse nuclear processes such as DNA replication, promoter remodeling, transcription elongation, DNA damage, and histone variant exchange. Currently, the best-characterized chaperone-histone interaction is that between the ubiquitous chaperone Asf1 and a dimer of H3 and H4. Nucleosome assembly proteins (Nap proteins) represent a distinct class of histone chaperone. Using pulsed electron double resonance (PELDOR) measurements and protein crosslinking, we show that two members of this class, Nap1 and Vps75, bind histones in the tetrameric conformation also observed when they are sequestered within the nucleosome. Furthermore, H3 and H4 trapped in their tetrameric state can be used as substrates in nucleosome assembly and chaperone-mediated lysine acetylation. This alternate mode of histone interaction provides a potential means of maintaining the integrity of the histone tetramer during cycles of nucleosome reassembly.

Indexed as

AcetylationBinding SitesDNA ReplicationHistone ChaperonesHistonesModels, BiologicalNucleosomesHistone ChaperonesHistonesNucleosomes

Identifiers

PMID21329878
PMCPMC3093613
OpenAlexW2126451754

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.