Evidence map›Paper›PMID 32453425›Full record

ArticleNucleic acids research2020

CryoEM structures of human CMG-ATPγS-DNA and CMG-AND-1 complexes.

Neil J Rzechorzek, Steven W Hardwick, Vincentius A Jatikusumo, Dimitri Y Chirgadze, Luca Pellegrini

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
6.4field-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

55 citing papers in PubMed, 105 citations in OpenAlex.

  1. Article
  2. Structural Activation of DNA Unwinding by MCM8/9/HROB.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Review
  5. A Meier-Gorlin syndrome mutation impairs the loading of the MCM2-7 complex during DNA replication initiation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Dynamic Assemblies in Genome Maintenance.Advances in experimental medicine and biology · 2026
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Structure of the Saccharolobus solfataricus GINS tetramer.Acta crystallographica. Section F, Structural biology communications · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Article
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  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

5 authors at 1 institution in 1 country.

Neil J RzechorzekDepartment of Biochemistry, Tennis Court Road, Cambridge CB2 1GA, UK.
Steven W HardwickDepartment of Biochemistry, Tennis Court Road, Cambridge CB2 1GA, UK.
Vincentius A JatikusumoDepartment of Biochemistry, Tennis Court Road, Cambridge CB2 1GA, UK.
Dimitri Y ChirgadzeDepartment of Biochemistry, Tennis Court Road, Cambridge CB2 1GA, UK.
Luca PellegriniDepartment of Biochemistry, Tennis Court Road, Cambridge CB2 1GA, UK.
Lawn Tennis Association · GB

Funding

Wellcome TrustWellcome Trust 104641/Z/14/ZWellcome Trust 202905/Z/16/ZWellcome Trust 206171/Z/17/Z
6 · The paper itself

Abstract

DNA unwinding in eukaryotic replication is performed by the Cdc45-MCM-GINS (CMG) helicase. Although the CMG architecture has been elucidated, its mechanism of DNA unwinding and replisome interactions remain poorly understood. Here we report the cryoEM structure at 3.3 Å of human CMG bound to fork DNA and the ATP-analogue ATPγS. Eleven nucleotides of single-stranded (ss) DNA are bound within the C-tier of MCM2-7 AAA+ ATPase domains. All MCM subunits contact DNA, from MCM2 at the 5'-end to MCM5 at the 3'-end of the DNA spiral, but only MCM6, 4, 7 and 3 make a full set of interactions. DNA binding correlates with nucleotide occupancy: five MCM subunits are bound to either ATPγS or ADP, whereas the apo MCM2-5 interface remains open. We further report the cryoEM structure of human CMG bound to the replisome hub AND-1 (CMGA). The AND-1 trimer uses one β-propeller domain of its trimerisation region to dock onto the side of the helicase assembly formed by Cdc45 and GINS. In the resulting CMGA architecture, the AND-1 trimer is closely positioned to the fork DNA while its CIP (Ctf4-interacting peptide)-binding helical domains remain available to recruit partner proteins.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateCell Cycle ProteinsCryoelectron MicroscopyCrystallography, X-RayDNADNA-Binding ProteinsDNA HelicasesDNA ReplicationHumansMinichromosome Maintenance ProteinsModels, MolecularMultiprotein ComplexesNucleic Acid ConformationProtein Conformationadenosine 5'-O-(3-thiotriphosphate)Adenosine TriphosphatasesAdenosine TriphosphateCDC45 protein, humanCell Cycle ProteinsDNADNA-Binding ProteinsDNA HelicasesMinichromosome Maintenance ProteinsMultiprotein ComplexesWDHD1 protein, human

Identifiers

PMID32453425
PMCPMC7337937
OpenAlexW3029343900

What OpenQuestion holds

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Registered trials

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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.