Evidence map›Paper›PMID 31712435›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Intrinsic elasticity of nucleosomes is encoded by histone variants and calibrated by their binding partners.

Daniël P Melters, Mary Pitman, Tatini Rakshit, Emilios K Dimitriadis, Minh Bui, Garegin A Papoian, Yamini Dalal

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.1field-weighted citation impact, top 7% 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

36 citing papers in PubMed, 64 citations in OpenAlex.

  1. Determinants of centromeric nucleosome conformation.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. 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

7 authors at 3 institutions in 1 country.

Daniël P MeltersLaboratory Receptor Biology and Gene Expression, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892.
Mary PitmanLaboratory Receptor Biology and Gene Expression, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892.
Tatini RakshitLaboratory Receptor Biology and Gene Expression, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892.
Emilios K DimitriadisScanning Probe Microscopy Unit, Biomedical Engineering and Physical Science Shared Resource, National Institute for Biomedical Imaging and Bioengineering, National Institutes of Health, Bethesda, MD 20892.
Minh BuiLaboratory Receptor Biology and Gene Expression, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892.
Garegin A PapoianDepartment of Chemistry and Biochemistry, Institute for Physical Science and Technology, University of Maryland, College Park, MD 20742; gpapoian@umd.edu dalaly@mail.nih.gov.ORCID 0000-0001-8580-3790
Yamini DalalLaboratory Receptor Biology and Gene Expression, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892; gpapoian@umd.edu dalaly@mail.nih.gov.ORCID 0000-0002-7655-6182
National Cancer Institute · USNational Institutes of Health · USUniversity of Maryland, College Park · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone variants fine-tune transcription, replication, DNA damage repair, and faithful chromosome segregation. Whether and how nucleosome variants encode unique mechanical properties to their cognate chromatin structures remains elusive. Here, using in silico and in vitro nanoindentation methods, extending to in vivo dissections, we report that histone variant nucleosomes are intrinsically more elastic than their canonical counterparts. Furthermore, binding proteins, which discriminate between histone variant nucleosomes, suppress this innate elasticity and also compact chromatin. Interestingly, when we overexpress the binding proteins in vivo, we also observe increased compaction of chromatin enriched for histone variant nucleosomes, correlating with diminished access. Taken together, these data suggest a plausible link between innate mechanical properties possessed by histone variant nucleosomes, the adaptability of chromatin states in vivo, and the epigenetic plasticity of the underlying locus.

Indexed as

Centromere Protein AChromosomal Proteins, Non-HistoneChromosome SegregationComputer SimulationDNA RepairDNA ReplicationHistonesMolecular Dynamics SimulationNucleosomesProtein Structure, TertiaryTranscription, GeneticCentromere Protein Acentromere protein CChromosomal Proteins, Non-HistoneHistonesNucleosomeschromatincomputational modelingelasticityepigeneticshistone variants

Identifiers

PMID31712435
PMCPMC6883791
OpenAlexW2983049401

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.