Evidence map›Paper›PMID 39121215›Full record

ArticleScience advances2024

Cyclin F-EXO1 axis controls cell cycle-dependent execution of double-strand break repair.

Hongbin Yang, Shahd Fouad, Paul Smith, Eun Young Bae, Yu Ji, Xinhui Lan, Ava Van Ess, Francesca M Buffa, Roman Fischer, Iolanda Vendrell and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Science advances, 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. Article
  3. ALS-FTD-linked CCNFJournal of neuroinflammation · 2026
    Article
  4. Article
  5. Article
  6. Structural mechanism for the recognition of E2F1 by the ubiquitin ligase adaptor Cyclin F.Proceedings of the National Academy of Sciences of the United States of America · 2025
    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

12 authors.

Hongbin YangMRC Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Headington, Oxford OX3 9DS, UK.ORCID 0000-0001-7757-9178
Shahd FouadMRC Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Headington, Oxford OX3 9DS, UK.
Paul SmithMRC Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Headington, Oxford OX3 9DS, UK.ORCID 0000-0003-1079-9330
Eun Young BaeMRC Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Headington, Oxford OX3 9DS, UK.ORCID 0009-0002-7294-0141
Yu JiMRC Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Headington, Oxford OX3 9DS, UK.ORCID 0009-0004-6257-180X
Xinhui LanMRC Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Headington, Oxford OX3 9DS, UK.ORCID 0009-0005-1618-4881
Ava Van EssMRC Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Headington, Oxford OX3 9DS, UK.ORCID 0000-0003-2473-5717
Francesca M BuffaMRC Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Headington, Oxford OX3 9DS, UK.ORCID 0000-0003-0409-406X
Roman FischerTarget Discovery Institute, Centre for Medicines Discovery, Nuffield Department of Medicine, University of Oxford, Oxford OX3 7FZ, UK.ORCID 0000-0002-9715-5951
Iolanda VendrellTarget Discovery Institute, Centre for Medicines Discovery, Nuffield Department of Medicine, University of Oxford, Oxford OX3 7FZ, UK.ORCID 0000-0001-7187-4061
Benedikt M KesslerTarget Discovery Institute, Centre for Medicines Discovery, Nuffield Department of Medicine, University of Oxford, Oxford OX3 7FZ, UK.ORCID 0000-0002-8160-2446
Vincenzo D'AngiolellaMRC Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Headington, Oxford OX3 9DS, UK.ORCID 0000-0001-8365-9094

Funding

European Research CouncilMedical Research Council MR/X006980/1
6 · The paper itself

Abstract

Ubiquitination is a crucial posttranslational modification required for the proper repair of DNA double-strand breaks (DSBs) induced by ionizing radiation (IR). DSBs are mainly repaired through homologous recombination (HR) when template DNA is present and nonhomologous end joining (NHEJ) in its absence. In addition, microhomology-mediated end joining (MMEJ) and single-strand annealing (SSA) provide backup DSBs repair pathways. However, the mechanisms controlling their use remain poorly understood. By using a high-resolution CRISPR screen of the ubiquitin system after IR, we systematically uncover genes required for cell survival and elucidate a critical role of the E3 ubiquitin ligase SCF

Indexed as

Cell CycleCyclinsDNA Breaks, Double-StrandedDNA RepairExodeoxyribonucleasesDNA End-Joining RepairDNA Repair EnzymesHumansRadiation, IonizingUbiquitinationCCNF protein, humanCyclinsDNA Repair EnzymesEXO1 protein, humanExodeoxyribonucleases

Identifiers

PMID39121215
PMCPMC11313846

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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.