Evidence map›Paper›PMID 26789756›Full record

ArticleBiophysical journal2016

Effects of MacroH2A and H2A.Z on Nucleosome Dynamics as Elucidated by Molecular Dynamics Simulations.

Samuel Bowerman, Jeff Wereszczynski

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.7field-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

42 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Mapping Allosteric Communication in the Nucleosome with Conditional Activity.Journal of chemical information and modeling · 2026
    Article
  3. Histone Variant H2A.Z Enhances Histone and Nucleosome Dynamics.Molecular & cellular proteomics : MCP · 2026
    Article
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  10. Review
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  14. Article
  15. Correlating histone acetylation with nucleosome core particle dynamics and function.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  16. Machines on Genes through the Computational Microscope.Journal of chemical theory and computation · 2023
    Review
  17. Article
  18. Review
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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

2 authors at 1 institution in 1 country.

Samuel BowermanDepartment of Physics and Center for Molecular Study of Condensed Soft Matter, Illinois Institute of Technology, Chicago, Illinois.
Jeff WereszczynskiDepartment of Physics and Center for Molecular Study of Condensed Soft Matter, Illinois Institute of Technology, Chicago, Illinois. Electronic address: jwereszc@iit.edu.
Illinois Institute of Technology · US

Funding

Molecular Simulations of the Structure/Function Relationship in Histone VariantsR15GM114758 · NIGMS · ILLINOIS INSTITUTE OF TECHNOLOGY · PI WERESZCZYNSKI, JEFFERY · 2015 to 2015
$325k
NIGMS NIH HHS R15 GM114758NIGMS NIH HHS R15GM114758
6 · The paper itself

Abstract

Eukaryotes tune the transcriptional activity of their genome by altering the nucleosome core particle through multiple chemical processes. In particular, replacement of the canonical H2A histone with the variants macroH2A and H2A.Z has been shown to affect DNA accessibility and nucleosome stability; however, the processes by which this occurs remain poorly understood. In this study, we elucidate the molecular mechanisms of these variants with an extensive molecular dynamics study of the canonical nucleosome along with three variant-containing structures: H2A.Z, macroH2A, and an H2A mutant with macroH2A-like L1 loops. Simulation results show that variant L1 loops play a pivotal role in stabilizing DNA binding to the octamer through direct interactions, core structural rearrangements, and altered allosteric networks in the nucleosome. All variants influence dynamics; however, macroH2A-like systems have the largest effect on energetics. In addition, we provide a comprehensive analysis of allosteric networks in the nucleosome and demonstrate that variants take advantage of stronger interactions between L1 loops to propagate dynamics throughout the complex. Furthermore, we show that posttranslational modifications are enriched at key locations in these networks. Taken together, these results provide, to our knowledge, new insights into the relationship between the structure, dynamics, and function of the nucleosome core particle and chromatin fibers, and how they are influenced by chromatin remodeling factors.

Indexed as

Molecular Dynamics SimulationAllosteric RegulationAmino Acid SequenceBase SequenceDNAHistonesMolecular Sequence DataNucleosomesProtein Structure, TertiaryDNAhistone H2A.F-ZHistonesmacroH2A histoneNucleosomes

Identifiers

PMID26789756
PMCPMC4724662
OpenAlexW2317141545

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.