Evidence map›Paper›PMID 29269875›Full record

ArticleNature communications2017

Cryo-EM structure of a licensed DNA replication origin.

Ferdos Abid Ali, Max E Douglas, Julia Locke, Valerie E Pye, Andrea Nans, John F X Diffley, Alessandro Costa

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

70 citing papers in PubMed, 98 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Compact Origins and Where to Find Them: ORC's Guide to Genome-Wide Licensing.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Multiple pathways for licensing human replication origins.bioRxiv : the preprint server for biology · 2024
    Article
  20. Review

10 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

7 authors at 1 institution in 1 country.

Ferdos Abid AliMacromolecular Machines Laboratory, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Max E DouglasChromosome Replication Laboratory, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Julia LockeMacromolecular Machines Laboratory, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Valerie E PyeChromatin Structure and Mobile DNA Laboratory, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.ORCID http://orcid.org/0000-0001-9616-2992
Andrea NansStructural Biology of Cells and Viruses, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
John F X DiffleyChromosome Replication Laboratory, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.ORCID http://orcid.org/0000-0001-5184-7680
Alessandro CostaMacromolecular Machines Laboratory, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK. alessandro.costa@crick.ac.uk.
The Francis Crick Institute · GB

Funding

Cancer Research UK 15669Cancer Research UK 15852Wellcome Trust FC001065Wellcome Trust FC001066
6 · The paper itself

Abstract

Eukaryotic origins of replication are licensed upon loading of the MCM helicase motor onto DNA. ATP hydrolysis by MCM is required for loading and the post-catalytic MCM is an inactive double hexamer that encircles duplex DNA. Origin firing depends on MCM engagement of Cdc45 and GINS to form the CMG holo-helicase. CMG assembly requires several steps including MCM phosphorylation by DDK. To understand origin activation, here we have determined the cryo-EM structures of DNA-bound MCM, either unmodified or phosphorylated, and visualize a phospho-dependent MCM element likely important for Cdc45 recruitment. MCM pore loops touch both the Watson and Crick strands, constraining duplex DNA in a bent configuration. By comparing our new MCM-DNA structure with the structure of CMG-DNA, we suggest how the conformational transition from the loaded, post-catalytic MCM to CMG might promote DNA untwisting and melting at the onset of replication.

Indexed as

DNA ReplicationNucleic Acid ConformationProtein ConformationCell Cycle ProteinsCryoelectron MicroscopyDNADNA-Binding ProteinsDNA HelicasesHoloenzymesImage Processing, Computer-AssistedMinichromosome Maintenance ProteinsNuclear ProteinsPhosphorylationProtein Serine-Threonine KinasesProtein Structure, QuaternarySaccharomyces cerevisiaeCDC45 protein, S cerevisiaeCDC7 protein, S cerevisiaeCell Cycle ProteinsDNADNA-Binding ProteinsDNA HelicasesHoloenzymesMinichromosome Maintenance ProteinsNuclear ProteinsProtein Serine-Threonine KinasesSaccharomyces cerevisiae Proteins

Identifiers

PMID29269875
PMCPMC5740162
OpenAlexW2771250096

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.