Evidence map›Paper›PMID 24267451›Full record

ArticleMolecular cell2013

PrimPol bypasses UV photoproducts during eukaryotic chromosomal DNA replication.

Julie Bianchi, Sean G Rudd, Stanislaw K Jozwiakowski, Laura J Bailey, Violetta Soura, Elaine Taylor, Irena Stevanovic, Andrew J Green, Travis H Stracker, Howard D Lindsay and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 199 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
199citing papers in PubMed, 1 pooled it
8.2field-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

199 citing papers in PubMed, 1 synthesis or guideline pooled it, 284 citations in OpenAlex.

  1. Pooled it
  2. Quiescence to proliferation transition regulates asynchronous mitochondrial DNA replication dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  19. DNA polymerase α-primase can function as a translesion DNA polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  20. Article

139 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

11 authors at 3 institutions in 2 countries.

Julie BianchiGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Brighton BN1 9RQ, UK.
Sean G Rudd
Stanislaw K Jozwiakowski
Laura J Bailey
Violetta Soura
Elaine Taylor
Irena Stevanovic
Andrew J Green
Travis H Stracker
Howard D Lindsay
Aidan J Doherty
University of Sussex · GBInstitute for Research in Biomedicine · ESLancaster University · GB

Funding

Biotechnology and Biological Sciences Research Council BB/H019723/1
6 · The paper itself

Abstract

DNA damage can stall the DNA replication machinery, leading to genomic instability. Thus, numerous mechanisms exist to complete genome duplication in the absence of a pristine DNA template, but identification of the enzymes involved remains incomplete. Here, we establish that Primase-Polymerase (PrimPol; CCDC111), an archaeal-eukaryotic primase (AEP) in eukaryotic cells, is involved in chromosomal DNA replication. PrimPol is required for replication fork progression on ultraviolet (UV) light-damaged DNA templates, possibly mediated by its ability to catalyze translesion synthesis (TLS) of these lesions. This PrimPol UV lesion bypass pathway is not epistatic with the Pol η-dependent pathway and, as a consequence, protects xeroderma pigmentosum variant (XP-V) patient cells from UV-induced cytotoxicity. In addition, we establish that PrimPol is also required for efficient replication fork progression during an unperturbed S phase. These and other findings indicate that PrimPol is an important player in replication fork progression in eukaryotic cells.

Indexed as

DNA ReplicationAmino Acid SequenceAnimalsCell ProliferationCell SurvivalChickensChromosomes, HumanDNA AdductsDNA DamageDNA-Directed DNA PolymeraseDNA PrimaseDNA, Single-StrandedG2 Phase Cell Cycle CheckpointsGene Knockdown TechniquesHEK293 CellsHumansDNA AdductsDNA-Directed DNA PolymeraseDNA PrimaseDNA, Single-StrandedMultifunctional EnzymesPrimPol protein, human

Identifiers

PMID24267451
PMCPMC4228047
OpenAlexW2090081292

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.