Evidence map›Paper›PMID 28424519›Full record

ArticleNature2017

Mechanism of chromatin remodelling revealed by the Snf2-nucleosome structure.

Xiaoyu Liu, Meijing Li, Xian Xia, Xueming Li, Zhucheng Chen

Abstract read
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In one paragraph

Article in Nature, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 152 papers.

0numbers the graph read from it
0cells of the map it votes in
152citing papers in PubMed
15.9field-weighted citation impact, top 1% 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

152 citing papers in PubMed, 236 citations in OpenAlex.

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  7. Cryo-EM structure of ALC1 in an open conformation bound to a PARylated nucleosome.Acta crystallographica. Section D, Structural biology · 2026
    Article
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92 more citing papers are in PubMed but not listed here.

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

5 authors at 2 institutions in 1 country.

Xiaoyu LiuMinistry of Education Key Laboratory of Protein Science, Tsinghua University, Beijing 100084, China.
Meijing LiMinistry of Education Key Laboratory of Protein Science, Tsinghua University, Beijing 100084, China.
Xian XiaMinistry of Education Key Laboratory of Protein Science, Tsinghua University, Beijing 100084, China.
Xueming LiMinistry of Education Key Laboratory of Protein Science, Tsinghua University, Beijing 100084, China.
Zhucheng ChenMinistry of Education Key Laboratory of Protein Science, Tsinghua University, Beijing 100084, China.
Tsinghua University · CNCenter for Life Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chromatin remodellers are helicase-like, ATP-dependent enzymes that alter chromatin structure and nucleosome positions to allow regulatory proteins access to DNA. Here we report the cryo-electron microscopy structure of chromatin remodeller Switch/sucrose non-fermentable (SWI2/SNF2) from Saccharomyces cerevisiae bound to the nucleosome. The structure shows that the two core domains of Snf2 are realigned upon nucleosome binding, suggesting activation of the enzyme. The core domains contact each other through two induced Brace helices, which are crucial for coupling ATP hydrolysis to chromatin remodelling. Snf2 binds to the phosphate backbones of one DNA gyre of the nucleosome mainly through its helicase motifs within the major domain cleft, suggesting a conserved mechanism of substrate engagement across different remodellers. Snf2 contacts the second DNA gyre via a positively charged surface, providing a mechanism to anchor the remodeller at a fixed position of the nucleosome. Snf2 locally deforms nucleosomal DNA at the site of binding, priming the substrate for the remodelling reaction. Together, these findings provide mechanistic insights into chromatin remodelling.

Indexed as

Chromatin Assembly and DisassemblyAdenosine TriphosphatasesAmino Acid SequenceBinding SitesCryoelectron MicroscopyDNAHistonesModels, MolecularNucleosomesProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsAdenosine TriphosphatasesDNAHistonesNucleosomesSaccharomyces cerevisiae ProteinsSNF2 protein, S cerevisiaeTranscription Factors

Identifiers

PMID28424519
OpenAlexW2605394820

What OpenQuestion holds

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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.