Evidence map›Paper›PMID 30174299›Full record

ReviewDNA repair2018

Eukaryotic translesion synthesis: Choosing the right tool for the job.

Kyle T Powers, M Todd Washington

Open access · greenAbstract readReview
In one paragraph

Review in DNA repair, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

44 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Ubiquitin System-Driven Proteostasis in DNA Damage Response.International journal of molecular sciences · 2026
    Review
  5. Dynamic Assemblies in Genome Maintenance.Advances in experimental medicine and biology · 2026
    Review
  6. Review
  7. Article
  8. The DREAM complex links somatic mutation, lifespan, and disease.bioRxiv : the preprint server for biology · 2025
    Article
  9. Article
  10. A bipartite interaction with the processivity clamp potentiates Pol IV-mediated TLS.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Disentangling sources of clock-like mutations in germline and soma.bioRxiv : the preprint server for biology · 2023
    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.

Kyle T PowersDepartment of Biochemistry, University of Iowa College of Medicine, Iowa City, IA 52242-1109, United States.
M Todd WashingtonDepartment of Biochemistry, University of Iowa College of Medicine, Iowa City, IA 52242-1109, United States. Electronic address: todd-washington@uiowa.edu.
University of Iowa · US

Funding

Viral VectorP30CA086862 · NCI · UNIVERSITY OF IOWA · PI Christopher K Laubenthal · 2000 to 2026
$70.0M
Mechanisms of Damaged DNA Replication in EukaryotesR01GM081433 · NIGMS · UNIVERSITY OF IOWA · PI WASHINGTON, M. TODD · 2008 to 2021
$4.2M
NIGMS NIH HHS R01 GM081433
6 · The paper itself

Abstract

Normal DNA replication is blocked by DNA damage in the template strand. Translesion synthesis is a major pathway for overcoming these replication blocks. In this process, multiple non-classical DNA polymerases are thought to form a complex at the stalled replication fork that we refer to as the mutasome. This hypothetical multi-protein complex is structurally organized by the replication accessory factor PCNA and the non-classical polymerase Rev1. One of the non-classical polymerases within this complex then catalyzes replication through the damage. Each non-classical polymerase has one or more cognate lesions, which the enzyme bypasses with high accuracy and efficiency. Thus, the accuracy and efficiency of translesion synthesis depends on which non-classical polymerase is chosen to bypass the damage. In this review article, we discuss how the most appropriate polymerase is chosen. In so doing, we examine the structural motifs that mediate the protein interactions in the mutasome; the multiple architectures that the mutasome can adopt, such as PCNA tool belts and Rev1 bridges; the intrinsically disordered regions that tether the polymerases to PCNA and to one another; and the kinetic selection model in which the most appropriate polymerase is chosen via a competition among the multiple polymerases within the mutasome.

Indexed as

DNA DamageDNA RepairAnimalsDNADNA-Directed DNA PolymeraseDNA ReplicationEukaryotaHumansProliferating Cell Nuclear AntigenSaccharomyces cerevisiaeDNADNA-Directed DNA PolymeraseProliferating Cell Nuclear AntigenDNA polymeraseDNA repairDNA replicationGenome instabilityMutasomePCNAProtein-protein interactionsStructure

Identifiers

PMID30174299
PMCPMC6340752
OpenAlexW2888661492

What OpenQuestion holds

Textmetadata
LicenceTDM
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.