Evidence map›Paper›PMID 29754816›Full record

ArticleCell2018

The Cohesin Ring Uses Its Hinge to Organize DNA Using Non-topological as well as Topological Mechanisms.

Madhusudhan Srinivasan, Johanna C Scheinost, Naomi J Petela, Thomas G Gligoris, Maria Wissler, Sugako Ogushi, James E Collier, Menelaos Voulgaris, Alexander Kurze, Kok-Lung Chan and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
8.1field-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

83 citing papers in PubMed, 173 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Protein turnover downstream of the Nipbl/CRL4 axis contributes to abnormal development in zebrafish embryos.Developmental dynamics : an official publication of the American Association of Anatomists · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. NIPBL and STAG1 enable loop extrusion by providing differential DNA-cohesin affinity.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Nucleic Acids and Electrical Signals.Reviews of physiology, biochemistry and pharmacology · 2025
    Review
  18. Article
  19. Review
  20. In through the out door: A loop-binding-first model for topological cohesin loading.BioEssays : news and reviews in molecular, cellular and developmental biology · 2024
    Article

23 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

13 authors at 4 institutions in 2 countries.

Madhusudhan SrinivasanDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Johanna C ScheinostDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Naomi J PetelaDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Thomas G GligorisDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Maria WisslerDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Sugako OgushiDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
James E CollierDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Menelaos VoulgarisDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Alexander KurzeDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Kok-Lung ChanGenome Centre, University of Sussex, Sussex House, Brighton BN1 9RH, UK.
Bin HuDepartment of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK.
Vincenzo CostanzoDNA Metabolism Laboratory, IFOM, The FIRC Institute of Molecular Oncology, Via Adamello 16, 21139 Milan, Italy.
Kim A NasmythDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. Electronic address: ashley.nasmyth@bioch.ox.ac.uk.
University of Oxford · GBFIRC Institute of Molecular Oncology · ITUniversity of Sheffield · GBUniversity of Sussex · GB

Funding

Cancer Research UK 26747Cancer Research UK C573/A 12386European Research Council 294401Medical Research Council MR/L018047/1Wellcome TrustWellcome Trust 107935/Z/15/Z
6 · The paper itself

Abstract

As predicted by the notion that sister chromatid cohesion is mediated by entrapment of sister DNAs inside cohesin rings, there is perfect correlation between co-entrapment of circular minichromosomes and sister chromatid cohesion. In most cells where cohesin loads without conferring cohesion, it does so by entrapment of individual DNAs. However, cohesin with a hinge domain whose positively charged lumen is neutralized loads and moves along chromatin despite failing to entrap DNAs. Thus, cohesin engages chromatin in non-topological, as well as topological, manners. Since hinge mutations, but not Smc-kleisin fusions, abolish entrapment, DNAs may enter cohesin rings through hinge opening. Mutation of three highly conserved lysine residues inside the Smc1 moiety of Smc1/3 hinges abolishes all loading without affecting cohesin's recruitment to CEN loading sites or its ability to hydrolyze ATP. We suggest that loading and translocation are mediated by conformational changes in cohesin's hinge driven by cycles of ATP hydrolysis.

Indexed as

Adenosine TriphosphateAnimalsBinding SitesCell Cycle ProteinsChromatidsChromatinChromosomal Proteins, Non-HistoneCohesinsDNAHumansHydrolysisLysineMiceMutationNuclear ProteinsProtein ConformationAdenosine TriphosphateCell Cycle ProteinsChromatinChromosomal Proteins, Non-HistoneCohesinsDNALysineNuclear ProteinsSaccharomyces cerevisiae Proteinschromosome condensationcohesincondensinloop extrusionsister chromatid cohesionSMC

Identifiers

PMID29754816
PMCPMC6371919
OpenAlexW2951726997

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.