Evidence map›Paper›PMID 19618963›Full record

ArticleBiochemistry2009

Dynamics of nucleosomes revealed by time-lapse atomic force microscopy.

Luda S Shlyakhtenko, Alexander Y Lushnikov, Yuri L Lyubchenko

Abstract read
In one paragraph

Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

48 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Biophysical reviews · 2023
    Review
  5. PARP3 Affects Nucleosome Compaction Regulation.International journal of molecular sciences · 2023
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Sequence-dependent nucleosome nanoscale structure characterized by atomic force microscopy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  14. Article
  15. Article
  16. Nucleosome structure and dynamics are coming of age.Nature structural & molecular biology · 2019
    Review
  17. Article
  18. Article
  19. Studying protein-DNA interactions using atomic force microscopy.Seminars in cell & developmental biology · 2018
    Review
  20. 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

3 authors at 2 institutions in 1 country.

Luda S ShlyakhtenkoDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Nebraska Medical Center, Omaha, Nebraska 68198-6025, USA.
Alexander Y Lushnikov
Yuri L Lyubchenko
University of Nebraska Medical Center · USNebraska Medical Center · US

Funding

LOCAL AND GLOBAL STRUCTURES OF SUPERCOILED DNAR01GM062235 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI LYUBCHENKO, YURI L · 2001 to 2007
$1.7M
NIGMS NIH HHS GM062235NIGMS NIH HHS R01 GM062235
6 · The paper itself

Abstract

The dynamics of chromatin provides the access to DNA within nucleosomes, and therefore, this process is critically involved in the regulation of chromatin function. However, our knowledge of the large-range dynamics of nucleosomes is limited. Answers to the questions, such as the range of opening of the nucleosome and the mechanism via which the opening occurs and propagates, remain unknown. Here we applied single-molecule time-lapse atomic force microscopy (AFM) imaging to directly visualize the dynamics of nucleosomes and identify the mechanism of the large range DNA exposure. With this technique, we are able to observe the process of unwrapping of nucleosomes. The unwrapping of nucleosomes proceeds from the ends of the particles, allowing for the unwrapping of DNA regions as large as dozens of base pairs. This process may lead to a complete unfolding of nucleosomes and dissociation of the histone core from the complex. The unwrapping occurs in the absence of proteins involved in the chromatin remodeling that require ATP hydrolysis for their function, suggesting that the inherent dynamics of nucleosomes can contribute to the chromatin unwrapping process. These findings shed a new light on molecular mechanisms of nucleosome dynamics and provide novel hypotheses about the understanding of the action of remodeling proteins as well as other intracellular systems in chromatin dynamics.

Indexed as

Models, GeneticModels, MolecularDNA, SuperhelicalHistonesHumansMicroscopy, Atomic ForceNucleic Acid ConformationNucleosomesParticle SizeTemplates, GeneticTime FactorsDNA, SuperhelicalHistonesNucleosomes

Identifiers

PMID19618963
PMCPMC2752652
OpenAlexW2061764188

What OpenQuestion holds

Textmetadata
LicenceTDM
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.