Evidence map›Paper›PMID 21670264›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

In vitro assembly of physiological cohesin/DNA complexes.

Itay Onn, Douglas Koshland

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

19 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. It's all in the numbers: Cohesin stoichiometry.Frontiers in molecular biosciences · 2022
    Review
  5. Article
  6. Intermediate step of cohesin's ATPase cycle allows cohesin to entrap DNA.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Cell cycle-specific cleavage of Scc2 regulates its cohesin deposition activity.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. In vitro loading of human cohesin on DNA by the human Scc2-Scc4 loader complex.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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

2 authors at 2 institutions in 1 country.

Itay OnnHoward Hughes Medical Institute, Department of Embryology, Carnegie Institution, Baltimore, MD 21218, USA.
Douglas Koshland
Howard Hughes Medical Institute · USUniversity of California, Berkeley · US

Funding

Establishment of sister chromatid cohesionR01GM092813 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KOSHLAND, DOUGLAS E · 2010 to 2015
$2.2M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM092813
6 · The paper itself

Abstract

Cohesin is a member of the Smc family of protein complexes that mediates higher-order chromosome structure by tethering different regions of chromatin. We present a new in vitro system that assembles cohesin-DNA complexes with in vivo properties. The assembly of these physiological salt-resistant complexes requires the cohesin holo-complex, its ability to bind ATP, the cohesin loader Scc2p and a closed DNA topology. Both the number of cohesin molecules bound to the DNA substrate and their distribution on the DNA substrate are limited. Cohesin and Scc2p bind preferentially to cohesin associated regions (CARs), DNA sequences with enriched cohesin binding in vivo. A subsequence of CARC1 promotes cohesin binding to neighboring sequences within CARC1. The enhancer-like function of this sequence is validated by in vivo deletion analysis. By demonstrating the physiological relevance of these in vitro assembled cohesin-DNA complexes, we establish our in vitro system as a powerful tool to elucidate the mechanism of cohesin and other Smc complexes.

Indexed as

Base SequenceCell Cycle ProteinsChromatin ImmunoprecipitationChromosomal Proteins, Non-HistoneChromosomes, FungalCohesinsDNA, FungalMacromolecular SubstancesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsDNA, FungalMacromolecular SubstancesSaccharomyces cerevisiae ProteinsSCC2 protein, S cerevisiae

Identifiers

PMID21670264
PMCPMC3145678
OpenAlexW2053336056

What OpenQuestion holds

Textmetadata
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.