Evidence map›Paper›PMID 24251097›Full record

ArticleFEBS open bio2013

Contribution of histone N-terminal tails to the structure and stability of nucleosomes.

Wakana Iwasaki, Yuta Miya, Naoki Horikoshi, Akihisa Osakabe, Hiroyuki Taguchi, Hiroaki Tachiwana, Takehiko Shibata, Wataru Kagawa, Hitoshi Kurumizaka

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in FEBS open bio, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

71 citing papers in PubMed, 135 citations in OpenAlex.

  1. Article
  2. Determinants of centromeric nucleosome conformation.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
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  6. Article
  7. Review
  8. Review
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  11. Article
  12. Article
  13. Article
  14. Genomic Instability and Epigenetic Changes during Aging.International journal of molecular sciences · 2023
    Review
  15. Article
  16. Review
  17. Article
  18. Arginine anchor points govern H3 tail dynamics.Frontiers in molecular biosciences · 2023
    Article
  19. Article
  20. Article

11 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Wakana IwasakiLaboratory of Structural Biology, Graduate School of Advanced Science and Engineering, Waseda University, 2-2 Wakamatsu-cho, Shinjuku-ku, Tokyo 162-8480, Japan ; RIKEN, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan.
Yuta Miya
Naoki Horikoshi
Akihisa Osakabe
Hiroyuki Taguchi
Hiroaki Tachiwana
Takehiko Shibata
Wataru Kagawa
Hitoshi Kurumizaka
Waseda University · JPRIKEN · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histones are the protein components of the nucleosome, which forms the basic architecture of eukaryotic chromatin. Histones H2A, H2B, H3, and H4 are composed of two common regions, the "histone fold" and the "histone tail". Many efforts have been focused on the mechanisms by which the post-translational modifications of histone tails regulate the higher-order chromatin architecture. On the other hand, previous biochemical studies have suggested that histone tails also affect the structure and stability of the nucleosome core particle itself. However, the precise contributions of each histone tail are unclear. In the present study, we determined the crystal structures of four mutant nucleosomes, in which one of the four histones, H2A, H2B, H3, or H4, lacked the N-terminal tail. We found that the deletion of the H2B or H3 N-terminal tail affected histone-DNA interactions and substantially decreased nucleosome stability. These findings provide important information for understanding the complex roles of histone tails in regulating chromatin structure.

Indexed as

ChromatinCrystal structureHistone tailNucleosomePDB, Protein Data BankRMSD, root mean square deviationSHL, superhelical locationThermal stability assaytlH2A, human histone H2A lacking N-terminal tailtlH2B, human histone H2B lacking N-terminal tailtlH3, human histone H3 lacking N-terminal tailtlH4, human histone H4 lacking N-terminal tailwt, wild-type

Identifiers

PMID24251097
PMCPMC3821030
OpenAlexW2037895696

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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.