Evidence map›Paper›PMID 30107417›Full record

ArticleNucleic acids research2018

The helicase Pif1 functions in the template switching pathway of DNA damage bypass.

Néstor García-Rodríguez, Ronald P Wong, Helle D Ulrich

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

20 citing papers in PubMed, 34 citations in OpenAlex.

  1. Regulation of Pfh1 helicase activity by nucleic acid interactions and mitochondrial SSB.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  2. Review
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  5. Integration of DNA Repair, Antigenic Variation, Cytoadhesion, and Chance inFrontiers in cellular and infection microbiology · 2022
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  7. Review
  8. TheGenes & development · 2021
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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

3 authors at 1 institution in 1 country.

Néstor García-RodríguezInstitute of Molecular Biology (IMB), Ackermannweg 4, D-55128 Mainz, Germany.
Ronald P WongInstitute of Molecular Biology (IMB), Ackermannweg 4, D-55128 Mainz, Germany.
Helle D UlrichInstitute of Molecular Biology (IMB), Ackermannweg 4, D-55128 Mainz, Germany.
Institute of Molecular Biology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Replication of damaged DNA is challenging because lesions in the replication template frequently interfere with an orderly progression of the replisome. In this situation, complete duplication of the genome is ensured by the action of DNA damage bypass pathways effecting either translesion synthesis by specialized, damage-tolerant DNA polymerases or a recombination-like mechanism called template switching (TS). Here we report that budding yeast Pif1, a helicase known to be involved in the resolution of complex DNA structures as well as the maturation of Okazaki fragments during replication, contributes to DNA damage bypass. We show that Pif1 expands regions of single-stranded DNA, so-called daughter-strand gaps, left behind the replication fork as a consequence of replisome re-priming. This function requires interaction with the replication clamp, proliferating cell nuclear antigen, facilitating its recruitment to damage sites, and complements the activity of an exonuclease, Exo1, in the processing of post-replicative daughter-strand gaps in preparation for TS. Our results thus reveal a novel function of a conserved DNA helicase that is known as a key player in genome maintenance.

Indexed as

DNADNA DamageDNA-Directed DNA PolymeraseDNA HelicasesDNA RepairDNA ReplicationDNA, Single-StrandedExodeoxyribonucleasesGenome, FungalNucleic Acid ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNADNA-Directed DNA PolymeraseDNA HelicasesDNA, Single-Strandedexodeoxyribonuclease IExodeoxyribonucleasesOkazaki fragmentsPIF1 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID30107417
PMCPMC6144865
OpenAlexW2886984403

What OpenQuestion holds

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LicenceCC BY-NC
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.