Evidence map›Paper›PMID 29735656›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Suppressor mutation analysis combined with 3D modeling explains cohesin's capacity to hold and release DNA.

Xingya Xu, Ryuta Kanai, Norihiko Nakazawa, Li Wang, Chikashi Toyoshima, Mitsuhiro Yanagida

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

18 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Cohesin organization, dynamics, and subdomain functions revealed by genetic suppressor screening.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2023
    Article
  4. Cohesin ATPase activities regulate DNA binding and coiled-coil configuration.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. It's all in the numbers: Cohesin stoichiometry.Frontiers in molecular biosciences · 2022
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Suppressor screening reveals common kleisin-hinge interaction in condensin and cohesin, but different modes of regulation.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Article
  16. A folded conformation of MukBEF and cohesin.Nature structural & molecular biology · 2019
    Article
  17. Review
  18. Article
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 2 countries.

Xingya XuG0 Cell Unit, Okinawa Institute of Science and Technology Graduate University, Onna-son, 904-0495 Okinawa, Japan.ORCID 0000-0002-3728-2633
Ryuta KanaiInstitute of Quantitative Biosciences, The University of Tokyo, 113-0032 Tokyo, Japan.
Norihiko NakazawaG0 Cell Unit, Okinawa Institute of Science and Technology Graduate University, Onna-son, 904-0495 Okinawa, Japan.
Li WangG0 Cell Unit, Okinawa Institute of Science and Technology Graduate University, Onna-son, 904-0495 Okinawa, Japan.
Chikashi ToyoshimaInstitute of Quantitative Biosciences, The University of Tokyo, 113-0032 Tokyo, Japan.
Mitsuhiro YanagidaG0 Cell Unit, Okinawa Institute of Science and Technology Graduate University, Onna-son, 904-0495 Okinawa, Japan; myanagid@gmail.com.
Okinawa Institute of Science and Technology Graduate University · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cohesin is a fundamental protein complex that holds sister chromatids together. Separase protease cleaves a cohesin subunit Rad21/SCC1, causing the release of cohesin from DNA to allow chromosome segregation. To understand the functional organization of cohesin, we employed next-generation whole-genome sequencing and identified numerous extragenic suppressors that overcome either inactive separase/Cut1 or defective cohesin in the fission yeast

Indexed as

MutationCell Cycle ProteinsChromatidsChromosomal Proteins, Non-HistoneChromosome SegregationCohesinsDNA, FungalModels, MolecularNuclear ProteinsPhosphoproteinsPhosphorylationProtein ConformationProtein SubunitsSchizosaccharomycesSchizosaccharomyces pombe ProteinsSuppression, GeneticCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsDNA, FungalNuclear ProteinsPhosphoproteinsProtein SubunitsRad21 protein, S pombeSchizosaccharomyces pombe Proteinscohesincohesin loader Mis4securinseparasesuppressor screen

Identifiers

PMID29735656
PMCPMC6003501
OpenAlexW2801189843

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.