Evidence map›Paper›PMID 29040671›Full record

ArticleNucleic acids research2018

Nanoscale dynamics of centromere nucleosomes and the critical roles of CENP-A.

Micah P Stumme-Diers, Siddhartha Banerjee, Mohtadin Hashemi, Zhiqiang Sun, Yuri L Lyubchenko

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

23 citing papers in PubMed, 52 citations in OpenAlex.

  1. Determinants of centromeric nucleosome conformation.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. PARP3 Affects Nucleosome Compaction Regulation.International journal of molecular sciences · 2023
    Article
  8. Review
  9. The Sequence Dependent Nanoscale Structure of CENP-A Nucleosomes.International journal of molecular sciences · 2022
    Article
  10. Article
  11. Article
  12. Transcription factor NF-κB unravels nucleosomes.Biochimica et biophysica acta. General subjects · 2021
    Article
  13. Dynamics of the PriA Helicase at Stalled DNA Replication Forks.The journal of physical chemistry. B · 2021
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. The base pair-scale diffusion of nucleosomes modulates binding of transcription factors.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  20. 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

5 authors at 1 institution in 1 country.

Micah P Stumme-DiersDepartment of Pharmaceutical Sciences, University of Nebraska Medical Center, 986025 Nebraska Medical Center, Omaha, NE 68198-6025, USA.
Siddhartha BanerjeeDepartment of Pharmaceutical Sciences, University of Nebraska Medical Center, 986025 Nebraska Medical Center, Omaha, NE 68198-6025, USA.
Mohtadin HashemiDepartment of Pharmaceutical Sciences, University of Nebraska Medical Center, 986025 Nebraska Medical Center, Omaha, NE 68198-6025, USA.
Zhiqiang SunDepartment of Pharmaceutical Sciences, University of Nebraska Medical Center, 986025 Nebraska Medical Center, Omaha, NE 68198-6025, USA.
Yuri L LyubchenkoDepartment of Pharmaceutical Sciences, University of Nebraska Medical Center, 986025 Nebraska Medical Center, Omaha, NE 68198-6025, USA.
Nebraska Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the absence of a functioning centromere, chromosome segregation becomes aberrant, leading to an increased rate of aneuploidy. The highly specific recognition of centromeres by kinetochores suggests that specific structural characteristics define this region, however, the structural details and mechanism underlying this recognition remains a matter of intense investigation. To address this, high-speed atomic force microscopy was used for direct visualization of the spontaneous dynamics of CENP-A nucleosomes at the sub-second time scale. We report that CENP-A nucleosomes change conformation spontaneously and reversibly, utilizing two major pathways: unwrapping, and looping of the DNA; enabling core transfer between neighboring DNA substrates. Along with these nucleosome dynamics we observed that CENP-A stabilizes the histone core against dissociating to histone subunits upon unwrapping DNA, unique from H3 cores which are only capable of such plasticity in the presence of remodeling factors. These findings have implications for the dynamics and integrity of nucleosomes at the centromere.

Indexed as

CentromereCentromere Protein ADNAHistonesHumansKinetochoresMicroscopy, Atomic ForceMolecular ConformationNucleic Acid ConformationNucleosomesTime-Lapse ImagingCentromere Protein ADNAHistonesNucleosomes

Identifiers

PMID29040671
PMCPMC5758880
OpenAlexW2951302676

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.