Evidence map›Paper›PMID 27820823›Full record

ArticlePloS one2016

CENP-A and H3 Nucleosomes Display a Similar Stability to Force-Mediated Disassembly.

Sung Hyun Kim, Rifka Vlijm, Jaco van der Torre, Yamini Dalal, Cees Dekker

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

18 citing papers in PubMed, 31 citations in OpenAlex.

  1. Structure and function of the centromere and inner kinetochore.Nature reviews. Molecular cell biology · 2026
    Review
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  3. Review
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  5. Article
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  10. The Sequence Dependent Nanoscale Structure of CENP-A Nucleosomes.International journal of molecular sciences · 2022
    Article
  11. Article
  12. Article
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  15. The regulation of chromosome segregation via centromere loops.Critical reviews in biochemistry and molecular biology · 2019
    Review
  16. Article
  17. Article
  18. 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

5 authors at 2 institutions in 2 countries.

Sung Hyun KimDepartment of Bionanoscience, Kavli Institute of Nanoscience Delft, Delft University of Technology, Delft, the Netherlands.
Rifka VlijmDepartment of Bionanoscience, Kavli Institute of Nanoscience Delft, Delft University of Technology, Delft, the Netherlands.
Jaco van der TorreDepartment of Bionanoscience, Kavli Institute of Nanoscience Delft, Delft University of Technology, Delft, the Netherlands.
Yamini DalalChromatin Structure and Epigenetic Mechanisms Unit, Laboratory of Receptor Biology and Gene Expression, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, Maryland, United States of America.
Cees DekkerDepartment of Bionanoscience, Kavli Institute of Nanoscience Delft, Delft University of Technology, Delft, the Netherlands.
Delft University of Technology · NLCenter for Cancer Research · US

Funding

Biomechanical properties of chromatin in cancer and normal cellsZIABC011207 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI DALAL, YAMINI P · 2009 to 2025
$8.8M
European Research Council 669598
6 · The paper itself

Abstract

Centromere-specific nucleosomes are a central feature of the kinetochore complex during mitosis, in which microtubules exert pulling and pushing forces upon the centromere. CENP-A nucleosomes have been assumed to be structurally unique, thereby providing resilience under tension relative to their H3 canonical counterparts. Here, we directly test this hypothesis by subjecting CENP-A and H3 octameric nucleosomes, assembled on random or on centromeric DNA sequences, to varying amounts of applied force by using single-molecule magnetic tweezers. We monitor individual disassembly events of CENP-A and H3 nucleosomes. Regardless of the DNA sequence, the force-mediated disassembly experiments for CENP-A and H3 nucleosomes demonstrate similar rupture forces, life time residency and disassembly steps. From these experiments, we conclude that CENP-A does not, by itself, contribute unique structural features to the nucleosome that lead to a significant resistance against force-mediated disruption. The data present insights into the mechanistic basis for how CENP-A nucleosomes might contribute to the structural foundation of the centromere in vivo.

Indexed as

Mechanical PhenomenaAnimalsAutoantigensBiomechanical PhenomenaCentromere Protein AChromosomal Proteins, Non-HistoneDNAHistonesHumansKineticsNucleosomesXenopus laevisAutoantigensCENPA protein, humanCentromere Protein AChromosomal Proteins, Non-HistoneDNAHistonesNucleosomes

Identifiers

PMID27820823
PMCPMC5098787
OpenAlexW2553770352

What OpenQuestion holds

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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.