Evidence map›Paper›PMID 28988770›Full record

ArticleCell2017

Structural Basis for a Safety-Belt Mechanism That Anchors Condensin to Chromosomes.

Marc Kschonsak, Fabian Merkel, Shveta Bisht, Jutta Metz, Vladimir Rybin, Markus Hassler, Christian H Haering

Open access · hybridAbstract read
In one paragraph

Article in Cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
10.0field-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

95 citing papers in PubMed, 179 citations in OpenAlex.

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  10. SMC4 Promotes Prostate Cancer Cell Proliferation and Metastasis via the Rheb/mTOR Pathway.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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  14. Nucleic Acids and Electrical Signals.Reviews of physiology, biochemistry and pharmacology · 2025
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

35 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Marc KschonsakCell Biology and Biophysics Unit, Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Meyerhofstraße 1, 69117 Heidelberg, Germany.
Fabian MerkelCell Biology and Biophysics Unit, Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Meyerhofstraße 1, 69117 Heidelberg, Germany.
Shveta BishtCell Biology and Biophysics Unit, Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Meyerhofstraße 1, 69117 Heidelberg, Germany.
Jutta MetzCell Biology and Biophysics Unit, Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Meyerhofstraße 1, 69117 Heidelberg, Germany.
Vladimir RybinProtein Expression and Purification Core Facility, European Molecular Biology Laboratory (EMBL), Meyerhofstraße 1, 69117 Heidelberg, Germany.
Markus HasslerCell Biology and Biophysics Unit, Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Meyerhofstraße 1, 69117 Heidelberg, Germany. Electronic address: markus.hassler@embl.de.
Christian H HaeringCell Biology and Biophysics Unit, Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Meyerhofstraße 1, 69117 Heidelberg, Germany. Electronic address: christian.haering@embl.de.
European Molecular Biology Laboratory · DEEuropean Molecular Biology Laboratory · DE

Funding

European Research Council 681365
6 · The paper itself

Abstract

Condensin protein complexes coordinate the formation of mitotic chromosomes and thereby ensure the successful segregation of replicated genomes. Insights into how condensin complexes bind to chromosomes and alter their topology are essential for understanding the molecular principles behind the large-scale chromatin rearrangements that take place during cell divisions. Here, we identify a direct DNA-binding site in the eukaryotic condensin complex, which is formed by its Ycg1

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceChaetomiumChromosomesCrystallography, X-RayDNADNA-Binding ProteinsEukaryotaFungal ProteinsHeLa CellsHumansModels, MolecularMultiprotein ComplexesSaccharomyces cerevisiaeSequence AlignmentAdenosine Triphosphatasescondensin complexesDNADNA-Binding ProteinsFungal ProteinsMultiprotein Complexescell divisionchromosome organizationchromosome segregationcondensinDNA-bindingHEAT repeatloop extrusionmitosisSMCx-ray crystallography

Identifiers

PMID28988770
PMCPMC5651216
OpenAlexW2761651210

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.