Evidence map›Paper›PMID 36864251›Full record

ArticleCommunications biology2023

PARP1 allows proper telomere replication through TRF1 poly (ADP-ribosyl)ation and helicase recruitment.

C Maresca, A Dello Stritto, C D'Angelo, E Petti, A Rizzo, E Vertecchi, F Berardinelli, L Bonanni, A Sgura, A Antoccia and 3 more

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

19 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Cancer-associated TRF1 mutations alter PARP1 interaction dynamics: an in silico study.Mammalian genome : official journal of the International Mammalian Genome Society · 2026
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  15. Article
  16. Telomere maintenance and the DNA damage response: a paradoxical alliance.Frontiers in cell and developmental biology · 2024
    Article
  17. Review
  18. The Altered Functions of Shelterin Components in ALT Cells.International journal of molecular sciences · 2023
    Review
  19. Review
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

13 authors at 6 institutions in 2 countries.

C Maresca *Translational Oncology Research Unit, IRCCS Regina Elena National Cancer Institute, Rome, Italy.
A Dello Stritto *Department of Biology and Biotechnology "Charles Darwin", Sapienza University of Rome, Rome, Italy.
C D'AngeloTranslational Oncology Research Unit, IRCCS Regina Elena National Cancer Institute, Rome, Italy.
E PettiTranslational Oncology Research Unit, IRCCS Regina Elena National Cancer Institute, Rome, Italy.
A RizzoTranslational Oncology Research Unit, IRCCS Regina Elena National Cancer Institute, Rome, Italy.
E VertecchiInstitute of Molecular Biology and Pathology, National Research Council, Rome, Italy.
F BerardinelliDepartment of Biology, Roma Tre University, Rome, Italy.
L BonanniDepartment of Biology, Roma Tre University, Rome, Italy.
A SguraDepartment of Biology, Roma Tre University, Rome, Italy.
A AntocciaDepartment of Biology, Roma Tre University, Rome, Italy.
G GrazianiDepartment of Systems Medicine, University of Rome Tor Vergata, Rome, Italy.
A BiroccioTranslational Oncology Research Unit, IRCCS Regina Elena National Cancer Institute, Rome, Italy. annamaria.biroccio@ifo.it.ORCID 0000-0003-3198-3532
E SalvatiInstitute of Molecular Biology and Pathology, National Research Council, Rome, Italy. erica.salvati@cnr.it.ORCID 0000-0002-3373-7442
Istituti di Ricovero e Cura a Carattere Scientifico · ITRoma Tre University · ITInstitute of Molecular Biology and Pathology · ITIstituto di Genetica Molecolare · ITNational Cancer Institute · MYUniversity of Rome Tor Vergata · IT

Funding

Associazione Italiana per la Ricerca sul Cancro (Italian Association for Cancer Research) 17121Associazione Italiana per la Ricerca sul Cancro (Italian Association for Cancer Research) 21579
6 · The paper itself

Abstract

Telomeres are nucleoprotein structures at eukaryotic chromosome termini. Their stability is preserved by a six-protein complex named shelterin. Among these, TRF1 binds telomere duplex and assists DNA replication with mechanisms only partly clarified. Here we found that poly (ADP-ribose) polymerase 1 (PARP1) interacts and covalently PARylates TRF1 in S-phase modifying its DNA affinity. Therefore, genetic and pharmacological inhibition of PARP1 impairs the dynamic association of TRF1 and the bromodeoxyuridine incorporation at replicating telomeres. Inhibition of PARP1 also affects the recruitment of WRN and BLM helicases in TRF1 containing complexes during S-phase, triggering replication-dependent DNA-damage and telomere fragility. This work unveils an unprecedented role for PARP1 as a "surveillant" of telomere replication, which orchestrates protein dynamics at proceeding replication fork.

Indexed as

Shelterin ComplexTelomereADP-RibosylationDNA DamageDNA HelicasesPoly (ADP-Ribose) Polymerase-1DNA HelicasesPoly (ADP-Ribose) Polymerase-1Shelterin Complex

Identifiers

PMID36864251
PMCPMC9981704
OpenAlexW4322775235

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.