Evidence map›Paper›PMID 30718488›Full record

ArticleNature communications2019

The CENP-A centromere targeting domain facilitates H4K20 monomethylation in the nucleosome by structural polymorphism.

Yasuhiro Arimura, Hiroaki Tachiwana, Hiroki Takagi, Tetsuya Hori, Hiroshi Kimura, Tatsuo Fukagawa, Hitoshi Kurumizaka

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
6.4field-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

20 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
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  4. A brief historical perspective on cell cycle control of CENP-A assembly and inheritance.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. CENP-A Regulation and Cancer.Frontiers in cell and developmental biology · 2022
    Review
  11. Structural studies of functional nucleosome complexes with transacting factors.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2022
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
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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

7 authors at 3 institutions in 1 country.

Yasuhiro ArimuraLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-0032, Japan.ORCID http://orcid.org/0000-0002-1903-6076
Hiroaki TachiwanaGraduate School of Advanced Science and Engineering, Waseda University, 2-2 Wakamatsu-cho, Shinjuku-ku, Tokyo, 162-8480, Japan.
Hiroki TakagiLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-0032, Japan.
Tetsuya HoriGraduate School of Frontier Biosciences, Osaka University, Suita, Osaka, 565-0871, Japan.
Hiroshi KimuraCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama, 226-8501, Japan.ORCID http://orcid.org/0000-0003-0854-083X
Tatsuo FukagawaGraduate School of Frontier Biosciences, Osaka University, Suita, Osaka, 565-0871, Japan.ORCID http://orcid.org/0000-0001-8564-6852
Hitoshi KurumizakaLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-0032, Japan. kurumizaka@iam.u-tokyo.ac.jp.ORCID http://orcid.org/0000-0001-7412-3722
Waseda University · JPThe University of Osaka · JPTokyo Institute of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Centromeric nucleosomes are composed of the centromere-specific histone H3 variant CENP-A and the core histones H2A, H2B, and H4. To establish a functional kinetochore, histone H4 lysine-20 (H4K20) must be monomethylated, but the underlying mechanism has remained enigmatic. To provide structural insights into H4K20 methylation, we here solve the crystal structure of a nucleosome containing an H3.1-CENP-A chimera, H3.1

Indexed as

AnimalsBlotting, WesternCell LineCentromereCentromere Protein AChickensHumansMethylationMutationNucleosomesPolymorphism, GeneticCentromere Protein ANucleosomes

Identifiers

PMID30718488
PMCPMC6362020
OpenAlexW2913686253

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.