Evidence map›Paper›PMID 30079888›Full record

ArticleeLife2018

Structure of the chromatin remodelling enzyme Chd1 bound to a ubiquitinylated nucleosome.

Ramasubramanian Sundaramoorthy, Amanda L Hughes, Hassane El-Mkami, David G Norman, Helder Ferreira, Tom Owen-Hughes

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
7.1field-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

53 citing papers in PubMed, 108 citations in OpenAlex.

  1. Cryo-EM structure of ALC1 in an open conformation bound to a PARylated nucleosome.Acta crystallographica. Section D, Structural biology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
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  7. How does CHD4 slide nucleosomes?Biochemical Society transactions · 2024
    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

6 authors at 2 institutions in 1 country.

Ramasubramanian SundaramoorthyCentre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee, United Kingdom.ORCID http://orcid.org/0000-0003-4895-0980
Amanda L HughesCentre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee, United Kingdom.ORCID http://orcid.org/0000-0002-1976-6634
Hassane El-MkamiSchool of Physics and Astronomy, University of St Andrews, St Andrews, United Kingdom.
David G NormanNucleic Acids Structure Research Group, University of Dundee, Dundee, United Kingdom.ORCID http://orcid.org/0000-0002-7658-7720
Helder FerreiraSchool of Biology, University of St Andrews, St Andrews, United Kingdom.
Tom Owen-HughesCentre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee, United Kingdom.ORCID http://orcid.org/0000-0002-0618-8185
University of Dundee · GBUniversity of St Andrews · GB

Funding

European Molecular Biology Organization ALTF 380-2015Wellcome 094090Wellcome 095062Wellcome 097945Wellcome 099149Wellcome 94090Wellcome 95062Wellcome 97945Wellcome 99149Wellcome TrustWellcome Trust 094090Wellcome Trust 095062Wellcome Trust 097945Wellcome Trust 099149
6 · The paper itself

Abstract

ATP-dependent chromatin remodelling proteins represent a diverse family of proteins that share ATPase domains that are adapted to regulate protein-DNA interactions. Here, we present structures of the

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAmino Acid SequenceChromatinChromatin Assembly and DisassemblyDNA-Binding ProteinsHistonesNucleosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsUbiquitinAdenosine TriphosphatasesAdenosine TriphosphateCHD1 protein, S cerevisiaeChromatinDNA-Binding ProteinsHistonesNucleosomesSaccharomyces cerevisiae ProteinsSNF2 protein, S cerevisiaeTranscription FactorsUbiquitinATPasechromatin remodelingchromosomesgene expressionhistone modificaitonmolecular biophysicsnucleosomeS. cerevisiaestructural biologyubiquitinxenopus

Identifiers

PMID30079888
PMCPMC6118821
OpenAlexW2795042203

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.