Evidence map›Paper›PMID 28934480›Full record

ArticleNucleic acids research2017

Hydroxyl-radical footprinting combined with molecular modeling identifies unique features of DNA conformation and nucleosome positioning.

Alexey K Shaytan, Hua Xiao, Grigoriy A Armeev, Carl Wu, David Landsman, Anna R Panchenko

Abstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Article
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  9. Review
  10. Article
  11. Article
  12. Article
  13. Molecular recognition of nucleosomes by binding partners.Current opinion in structural biology · 2019
    Review
  14. Article
  15. 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

6 authors.

Alexey K ShaytanNational Center for Biotechnology Information, NLM, NIH, Bethesda, MD 20894, USA.
Hua XiaoLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Grigoriy A ArmeevDepartment of Biology, Lomonosov Moscow State University, Moscow 119991, Russia.
Carl WuLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
David LandsmanNational Center for Biotechnology Information, NLM, NIH, Bethesda, MD 20894, USA.
Anna R PanchenkoNational Center for Biotechnology Information, NLM, NIH, Bethesda, MD 20894, USA.

Funding

Protein-protein binding: regulation and effect of disease mutationsZIALM090313 · NLM · NATIONAL LIBRARY OF MEDICINE · PI PANCHENKO, ANNA · 2013 to 2018
$5.2M
Structural And Functional Analysis Of Protein Sequence FamiliesZIALM000071 · NLM · NATIONAL LIBRARY OF MEDICINE · PI LANDSMAN, DAVID · 2009 to 2025
$3.7M
6 · The paper itself

Abstract

Nucleosomes are the most abundant protein-DNA complexes in eukaryotes that provide compaction of genomic DNA and are implicated in regulation of transcription, DNA replication and repair. The details of DNA positioning on the nucleosome and the DNA conformation can provide key regulatory signals. Hydroxyl-radical footprinting (HRF) of protein-DNA complexes is a chemical technique that probes nucleosome organization in solution with a high precision unattainable by other methods. In this work we propose an integrative modeling method for constructing high-resolution atomistic models of nucleosomes based on HRF experiments. Our method precisely identifies DNA positioning on nucleosome by combining HRF data for both DNA strands with the pseudo-symmetry constraints. We performed high-resolution HRF for Saccharomyces cerevisiae centromeric nucleosome of unknown structure and characterized it using our integrative modeling approach. Our model provides the basis for further understanding the cooperative engagement and interplay between Cse4p protein and the A-tracts important for centromere function.

Indexed as

Models, MolecularAlgorithmsCentromereChromosomal Proteins, Non-HistoneDNADNA-Binding ProteinsDNA CleavageDNA FootprintingHydroxyl RadicalNucleic Acid ConformationNucleosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsChromosomal Proteins, Non-HistoneCSE4 protein, S cerevisiaeDNADNA-Binding ProteinsHydroxyl RadicalNucleosomesSaccharomyces cerevisiae Proteins

Identifiers

PMID28934480
PMCPMC5765820

What OpenQuestion holds

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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.