Evidence map›Paper›PMID 20097898›Full record

ArticleThe Journal of biological chemistry2010

Dynamics of pre-replicative complex assembly.

Vasiliki Tsakraklides, Stephen P Bell

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

42 citing papers in PubMed, 70 citations in OpenAlex.

  1. Review
  2. Article
  3. Regulation of replication origin licensing by ORC phosphorylation reveals a two-step mechanism for Mcm2-7 ring closing.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Article
  5. Article
  6. Regulation of DNA Replication Licensing and Re-Replication by Cdt1.International journal of molecular sciences · 2021
    Review
  7. Article
  8. Review
  9. Article
  10. The Inherent Asymmetry of DNA Replication.Annual review of cell and developmental biology · 2017
    Review
  11. Article
  12. Article
  13. Mechanisms and regulation of DNA replication initiation in eukaryotes.Critical reviews in biochemistry and molecular biology · 2017
    Review
  14. The Temporal Regulation of S Phase Proteins During GAdvances in experimental medicine and biology · 2017
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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 1 institution in 1 country.

Vasiliki TsakraklidesDepartment of Biology, Cambridge, Massachusetts 02139.
Stephen P BellDepartment of Biology, Cambridge, Massachusetts 02139; Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139. Electronic address: spbell@mit.edu.
Howard Hughes Medical Institute · US

Funding

INITIATION OF DNA REPLICATION OF YEAST CHROMOSOMESR01GM052339 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BELL, STEPHEN P. · 1995 to 2019
$5.5M
Howard Hughes Medical InstituteNIGMS NIH HHS GM52339NIGMS NIH HHS R01 GM052339
6 · The paper itself

Abstract

The pre-replicative complex (pre-RC) is formed at all potential origins of replication through the action of the origin recognition complex (ORC), Cdc6, Cdt1, and the Mcm2-7 complex. The end result of pre-RC formation is the loading of the Mcm2-7 replicative helicase onto origin DNA. We examined pre-RC formation in vitro and found that it proceeds through separable binding events. Origin-bound ORC recruits Cdc6, and this ternary complex then promotes helicase loading in the presence of a pre-formed Mcm2-7-Cdt1 complex. Using a stepwise pre-RC assembly assay, we investigated the fate of pre-RC components during later stages of the reaction. We determined that helicase loading is accompanied by dissociation of ORC, Cdc6, and Cdt1 from origin DNA. This dissociation requires ATP hydrolysis at a late stage of pre-RC assembly. Our results indicate that pre-RC formation is a dynamic process.

Indexed as

Adenosine TriphosphateCell Cycle ProteinsChromosomal Proteins, Non-HistoneDNADNA-Binding ProteinsDNA ReplicationG1 PhaseGene Expression Regulation, FungalHydrolysisModels, BiologicalOrigin Recognition ComplexProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphateCDC6 protein, S cerevisiaeCell Cycle ProteinsChromosomal Proteins, Non-HistoneDNADNA-Binding ProteinsMCM2 protein, S cerevisiaeOrigin Recognition ComplexSaccharomyces cerevisiae ProteinsTAH11 protein, S cerevisiae

Identifiers

PMID20097898
PMCPMC2843193
OpenAlexW2108539297

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.