Evidence map›Paper›PMID 23473491›Full record

ArticleBiophysical journal2013

Clipping of flexible tails of histones H3 and H4 affects the structure and dynamics of the nucleosome.

Nathan P Nurse, Isabel Jimenez-Useche, Ian Tad Smith, Chongli Yuan

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.5field-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

39 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Histone Tail Cleavage as a Mechanism for Epigenetic Regulation.International journal of molecular sciences · 2024
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Machines on Genes through the Computational Microscope.Journal of chemical theory and computation · 2023
    Review
  15. Article
  16. Article
  17. Signal pathways of melanoma and targeted therapy.Signal transduction and targeted therapy · 2021
    Review
  18. Article
  19. Article
  20. Histone Tail Conformations: A Fuzzy Affair with DNA.Trends in biochemical sciences · 2021
    Review
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 1 institution in 1 country.

Nathan P NurseSchool of Chemical Engineering, Purdue University, West Lafayette, Indiana, USA.
Isabel Jimenez-Useche
Ian Tad Smith
Chongli Yuan
Purdue University West Lafayette · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Förster resonance energy transfer was used to monitor the dynamic conformations of mononucleosomes under different chromatin folding conditions to elucidate the role of the flexible N-terminal regions of H3 and H4 histones. The H3 tail was shown to partake in intranucleosomal interactions by restricting the DNA breathing motion and compacting the nucleosome. The H3 tail effects were mostly independent of the ionic strength and valency of the ions. The H4 tail was shown to not greatly affect the nucleosome conformation, but did slightly influence the relative population of the preferred conformation. The role of the H4 tail varied depending on the valency and ionic strength, suggesting that electrostatic forces play a primary role in H4 tail interactions. Interestingly, despite the H4 tail's lack of influence, when H3 and H4 tails were simultaneously clipped, a more dramatic effect was seen than when only H3 or H4 tails were clipped. The combinatorial effect of H3 and H4 tail truncation suggests a potential mechanism by which various combinations of histone tail modifications can be used to control accessibility of DNA-binding proteins to nucleosomal DNA.

Indexed as

Sequence DeletionAmino Acid SequenceAnimalsDNAFluorescence Resonance Energy TransferHistonesNucleosomesOsmolar ConcentrationProtein BindingProtein Structure, TertiaryRecombinant ProteinsStatic ElectricityXenopus laevisDNAHistonesNucleosomesRecombinant Proteins

Identifiers

PMID23473491
PMCPMC3870800
OpenAlexW2022069097

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.