Evidence map›Paper›PMID 19567737›Full record

ArticleNucleic acids research2009

Analysis of individual remodeled nucleosomes reveals decreased histone-DNA contacts created by hSWI/SNF.

Karim Bouazoune, Tina B Miranda, Peter A Jones, Robert E Kingston

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

26 citing papers in PubMed, 36 citations in OpenAlex.

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  13. Nucleosome sliding mechanisms: new twists in a looped history.Nature structural & molecular biology · 2013
    Review
  14. Article
  15. Article
  16. Chromatin remodeling by the CHD7 protein is impaired by mutations that cause human developmental disorders.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  17. 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

4 authors at 2 institutions in 1 country.

Karim BouazouneDepartment of Molecular Biology & Genetics, Massachusetts General Hospital, Harvard Medical School, Boston, MA 02114, USA.
Tina B Miranda
Peter A Jones
Robert E Kingston
University of Southern California · USHarvard University · US

Funding

MECHANISMS OF DE NOVO METHYLATION IN CANCERR01CA082422 · NCI · VAN ANDEL RESEARCH INSTITUTE · PI JONES, PETER A · 1999 to 2016
$5.1M
Mechanisms of De Novo Methylation in CancerR37CA082422 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI JONES, PETER A · 2009 to 2013
$2.2M
EBV BZLF1 GENE PRODUCTR01GM048045 · NIGMS · TULANE UNIVERSITY OF LOUISIANA · PI FLEMINGTON, ERIK K · 1998 to 2007
$1.9M
EPSTEIN-BARR VIRUS BZLF1 GENE PRODUCTR29GM048045 · NIGMS · DANA-FARBER CANCER INSTITUTE · PI FLEMINGTON, ERIK K · 1993 to 1997
–
NCI NIH HHS CA82422NIGMS NIH HHS GM48045
6 · The paper itself

Abstract

Chromatin remodeling enzymes use the energy of ATP hydrolysis to alter histone-DNA contacts and regulate DNA-based processes in eukaryotes. Whether different subfamilies of remodeling complexes generate distinct products remains uncertain. We have developed a protocol to analyze nucleosome remodeling on individual products formed in vitro. We used a DNA methyltransferase to examine DNA accessibility throughout nucleosomes that had been remodeled by the ISWI and SWI/SNF families of enzymes. We confirmed that ISWI-family enzymes mainly created patterns of accessibility consistent with canonical nucleosomes. In contrast, SWI/SNF-family enzymes generated widespread DNA accessibility. The protection patterns created by these enzymes were usually located at the extreme ends of the DNA and showed no evidence for stable loop formation on individual molecules. Instead, SWI/SNF family proteins created extensive accessibility by generating heterogeneous products that had fewer histone-DNA contacts than a canonical nucleosome, consistent with models in which a canonical histone octamer has been 'pushed' off of the end of the DNA.

Indexed as

Chromatin Assembly and DisassemblyAdenosine TriphosphatasesAdenosine TriphosphateBromodomain Containing ProteinsChromosomal Proteins, Non-HistoneDNADNA-Cytosine MethylasesDNA HelicasesHistonesNuclear ProteinsNucleosomesTranscription FactorsAdenosine TriphosphatasesAdenosine TriphosphateBAZ1A protein, humanBromodomain Containing ProteinsChromosomal Proteins, Non-HistoneDNADNA-Cytosine MethylasesDNA HelicasesDNA modification methylase SssIHistonesISWI proteinNuclear ProteinsNucleosomesSMARCA4 protein, humanSMARCA5 protein, humanTranscription Factors

Identifiers

PMID19567737
PMCPMC2760786
OpenAlexW2050156039

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.