Evidence map›Paper›PMID 21768347›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Histone fold modifications control nucleosome unwrapping and disassembly.

Marek Simon, Justin A North, John C Shimko, Robert A Forties, Michelle B Ferdinand, Mridula Manohar, Meng Zhang, Richard Fishel, Jennifer J Ottesen, Michael G Poirier

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 133 papers.

0numbers the graph read from it
0cells of the map it votes in
133citing papers in PubMed
7.3field-weighted citation impact, top 2% 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

133 citing papers in PubMed, 202 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. DNA Repair in Nucleosomes: Insights from Histone Modifications and Mutants.International journal of molecular sciences · 2024
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review

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

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

10 authors at 2 institutions in 1 country.

Marek SimonDepartment of Physics, The Ohio State University, Columbus, OH 43210, USA.
Justin A North
John C Shimko
Robert A Forties
Michelle B Ferdinand
Mridula Manohar
Meng Zhang
Richard Fishel
Jennifer J Ottesen
Michael G Poirier
The Ohio State University · USThe Ohio State University Wexner Medical Center · US

Funding

The Human Mismatch Repair Proteins and CarcinogenesisR01CA067007 · NCI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI Richard Fishel · 1995 to 2026
$9.6M
Recombination/Repair Complex in Human CellsR01GM080176 · NIGMS · OHIO STATE UNIVERSITY · PI FISHEL, RICHARD · 2006 to 2015
$3.2M
Mechanisms of Chromatin Transcriptional RegulationR01GM083055 · NIGMS · OHIO STATE UNIVERSITY · PI POIRIER, MICHAEL GUY · 2008 to 2016
$2.7M
NCI NIH HHS R01 CA067007NIGMS NIH HHS GM080176NIGMS NIH HHS R01 GM080176NIGMS NIH HHS R01 GM083055
6 · The paper itself

Abstract

Nucleosomes are stable DNA-histone protein complexes that must be unwrapped and disassembled for genome expression, replication, and repair. Histone posttranslational modifications (PTMs) are major regulatory factors of these nucleosome structural changes, but the molecular mechanisms associated with PTM function remains poorly understood. Here we demonstrate that histone PTMs within distinct structured regions of the nucleosome directly regulate the inherent dynamic properties of the nucleosome. Precise PTMs were introduced into nucleosomes by chemical ligation. Single molecule magnetic tweezers measurements determined that only PTMs near the nucleosome dyad increase the rate of histone release in unwrapped nucleosomes. In contrast, FRET and restriction enzyme analysis reveal that only PTMs throughout the DNA entry-exit region increase unwrapping and enhance transcription factor binding to nucleosomal DNA. These results demonstrate that PTMs in separate structural regions of the nucleosome control distinct dynamic events, where the dyad regulates disassembly while the DNA entry-exit region regulates unwrapping. These studies are consistent with the conclusion that histone PTMs may independently influence nucleosome dynamics and associated chromatin functions.

Indexed as

AcetylationAlgorithmsAnimalsDNAElectrophoretic Mobility Shift AssayFluorescence Resonance Energy TransferHistonesKineticsLysineMicroscopy, Atomic ForceModels, MolecularMutationNucleic Acid ConformationNucleosomesProtein BindingProtein MultimerizationDNAHistonesLysineNucleosomesRecombinant Proteins

Identifiers

PMID21768347
PMCPMC3150920
OpenAlexW2099369844

What OpenQuestion holds

Textmetadata
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.