Evidence map›Paper›PMID 38977862›Full record

ArticleScientific reports2024

Werner helicase interacting protein 1 contributes to G-quadruplex processing in human cells.

Lili Hegedus, Agnes Toth, Gabor M Harami, Janos Palinkas, Nargis Karatayeva, Eniko Sajben-Nagy, Szabolcs Bene, Sara Afzali Jaktajdinani, Mihaly Kovacs, Szilvia Juhasz and 1 more

Abstract read
In one paragraph

Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. The function of Mgs1/WRNIP1 in genome maintenance.Frontiers in molecular biosciences · 2026
    Review
  5. Review
  6. 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

11 authors.

Lili Hegedus *Institute of Genetics, Biological Research Centre, HUN-REN Szeged, Szeged, Hungary.
Agnes Toth *Institute of Genetics, Biological Research Centre, HUN-REN Szeged, Szeged, Hungary.
Gabor M HaramiELTE-MTA Momentum Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
Janos PalinkasELTE-MTA Momentum Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
Nargis KaratayevaInstitute of Genetics, Biological Research Centre, HUN-REN Szeged, Szeged, Hungary.
Eniko Sajben-NagyInstitute of Genetics, Biological Research Centre, HUN-REN Szeged, Szeged, Hungary.
Szabolcs BeneInstitute of Genetics, Biological Research Centre, HUN-REN Szeged, Szeged, Hungary.
Sara Afzali JaktajdinaniInstitute of Genetics, Biological Research Centre, HUN-REN Szeged, Szeged, Hungary.
Mihaly KovacsELTE-MTA Momentum Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
Szilvia JuhaszHCEMM Cancer Microbiome Core Group, Szeged, Hungary. juhasz.szilvia@brc.hu.
Peter BurkovicsInstitute of Genetics, Biological Research Centre, HUN-REN Szeged, Szeged, Hungary. burkovics.peter@brc.hu.

Funding

Eötvös Loránd Tudományegyetem KMOP-4.2.1/B-10-2011-0002Innovációs és Technológiai Minisztérium FEIF/433-4/2020-ITMInnovációs és Technológiai Minisztérium ÚNKP-19-2Magyar Tudományos Akadémia bo_656_20Nemzeti Kutatási, Fejlesztési és Innovaciós Alap FK-131961Nemzeti Kutatási, Fejlesztési és Innovaciós Alap K-119361Nemzeti Kutatási, Fejlesztési és Innovaciós Alap K-134595
6 · The paper itself

Abstract

Genome replication is frequently impeded by highly stable DNA secondary structures, including G-quadruplex (G4) DNA, that can hinder the progression of the replication fork. Human WRNIP1 (Werner helicase Interacting Protein 1) associates with various components of the replication machinery and plays a crucial role in genome maintenance processes. However, its detailed function is still not fully understood. Here we show that human WRNIP1 interacts with G4 structures and provide evidence for its contribution to G4 processing. The absence of WRNIP1 results in elevated levels of G4 structures, DNA damage and chromosome aberrations following treatment with PhenDC3, a G4-stabilizing ligand. Additionally, we establish a functional and physical relationship between WRNIP1 and the PIF1 helicase in G4 processing. In summary, our results suggest that WRNIP1 aids genome replication and maintenance by regulating G4 processing and this activity relies on Pif1 DNA helicase.

Indexed as

DNA HelicasesDNA ReplicationG-QuadruplexesATPases Associated with Diverse Cellular ActivitiesCarrier ProteinsChromosome AberrationsDNA-Binding ProteinsDNA DamageHumansATPases Associated with Diverse Cellular ActivitiesCarrier ProteinsDNA-Binding ProteinsDNA HelicasesPIF1 protein, humanWRNIP1 protein, humanDNA helicaseGenome stabilityG-quadruplexPIF1ReplicationWRNIP1

Identifiers

PMID38977862
PMCPMC11231340

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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.