Evidence map›Paper›PMID 28257701›Full record

ArticleMolecular cell2017

The SMX DNA Repair Tri-nuclease.

Haley D M Wyatt, Rob C Laister, Stephen R Martin, Cheryl H Arrowsmith, Stephen C West

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

78 citing papers in PubMed, 123 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Deep structure-function analysis of the endonuclease Mus81 with dominant mutational scanning.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

18 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

5 authors at 3 institutions in 2 countries.

Haley D M WyattThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Rob C LaisterPrincess Margaret Cancer Centre and Department of Medical Biophysics, University of Toronto, 101 College Street, Toronto, ON M5G 1L7, Canada.
Stephen R MartinStructural Biology Science Technology Platform, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Cheryl H ArrowsmithPrincess Margaret Cancer Centre and Department of Medical Biophysics, University of Toronto, 101 College Street, Toronto, ON M5G 1L7, Canada.
Stephen C WestThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK. Electronic address: stephen.west@crick.ac.uk.
The Francis Crick Institute · GBPrincess Margaret Cancer Centre · CAUniversity of Toronto · CA

Funding

STRUCTURAL GENOMICS OF EUKARYOTIC MODEL ORGANISMSP50GM062413 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI MONTELIONE, GAETANO T · 2000 to 2004
$33.5M
Cancer Research UK 11582European Research Council 249145NIGMS NIH HHS P50 GM062413Wellcome Trust
6 · The paper itself

Abstract

The efficient removal of replication and recombination intermediates is essential for the maintenance of genome stability. Resolution of these potentially toxic structures requires the MUS81-EME1 endonuclease, which is activated at prometaphase by formation of the SMX tri-nuclease containing three DNA repair structure-selective endonucleases: SLX1-SLX4, MUS81-EME1, and XPF-ERCC1. Here we show that SMX tri-nuclease is more active than the three individual nucleases, efficiently cleaving replication forks and recombination intermediates. Within SMX, SLX4 co-ordinates the SLX1 and MUS81-EME1 nucleases for Holliday junction resolution, in a reaction stimulated by XPF-ERCC1. SMX formation activates MUS81-EME1 for replication fork and flap structure cleavage by relaxing substrate specificity. Activation involves MUS81's conserved N-terminal HhH domain, which mediates incision site selection and SLX4 binding. Cell cycle-dependent formation and activation of this tri-nuclease complex provides a unique mechanism by which cells ensure chromosome segregation and preserve genome integrity.

Indexed as

DNA RepairDNA ReplicationGenomic InstabilityCell CycleDNADNA-Binding ProteinsEndodeoxyribonucleasesEndonucleasesEnzyme ActivationHumansMultienzyme ComplexesNucleic Acid ConformationProtein BindingProtein Interaction Domains and MotifsRecombinasesStructure-Activity RelationshipDNADNA-Binding ProteinsEme1 protein, humanEndodeoxyribonucleasesEndonucleasesERCC1 protein, humanMultienzyme ComplexesMUS81 protein, humanRecombinasesSLX1 protein, humanSLX4 protein, humanxeroderma pigmentosum group F proteinDNA repairDNA replicationFanconi anemiagenome stabilityHolliday junctionhomologous recombinationresolutionstructure-selective endonuclease

Identifiers

PMID28257701
PMCPMC5344696
OpenAlexW2591772585

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.