Evidence map›Paper›PMID 33939809›Full record

ReviewNucleic acids research2021

The multi-functionality of UHRF1: epigenome maintenance and preservation of genome integrity.

Monica Mancini, Elena Magnani, Filippo Macchi, Ian Marc Bonapace

Open access · goldAbstract readReview
In one paragraph

Review in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
5.3field-weighted citation impact, top 3% 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

59 citing papers in PubMed, 94 citations in OpenAlex.

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  14. UHRF1 Controls the Timing of RAD51 Removal During DNA Damage Repair Through Suppressing RFWD3.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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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

4 authors at 2 institutions in 2 countries.

Monica ManciniDepartment of Biotechnology and Life Sciences, University of Insubria, Busto Arsizio, VA 21052, Italy.ORCID 0000-0003-4128-9018
Elena MagnaniProgram in Biology, New York University Abu Dhabi, Abu Dhabi, PO Box 129188, United Arab Emirates.
Filippo MacchiProgram in Biology, New York University Abu Dhabi, Abu Dhabi, PO Box 129188, United Arab Emirates.
Ian Marc BonapaceDepartment of Biotechnology and Life Sciences, University of Insubria, Busto Arsizio, VA 21052, Italy.
New York University Abu Dhabi · AEUniversity of Insubria · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During S phase, the cooperation between the macromolecular complexes regulating DNA synthesis, epigenetic information maintenance and DNA repair is advantageous for cells, as they can rapidly detect DNA damage and initiate the DNA damage response (DDR). UHRF1 is a fundamental epigenetic regulator; its ability to coordinate DNA methylation and histone code is unique across proteomes of different species. Recently, UHRF1's role in DNA damage repair has been explored and recognized to be as important as its role in maintaining the epigenome. UHRF1 is a sensor for interstrand crosslinks and a determinant for the switch towards homologous recombination in the repair of double-strand breaks; its loss results in enhanced sensitivity to DNA damage. These functions are finely regulated by specific post-translational modifications and are mediated by the SRA domain, which binds to damaged DNA, and the RING domain. Here, we review recent studies on the role of UHRF1 in DDR focusing on how it recognizes DNA damage and cooperates with other proteins in its repair. We then discuss how UHRF1's epigenetic abilities in reading and writing histone modifications, or its interactions with ncRNAs, could interlace with its role in DDR.

Indexed as

DNA RepairEpigenomeAnimalsCCAAT-Enhancer-Binding ProteinsDNA DamageEpigenesis, GeneticGenomic InstabilityHistone CodeHumansUbiquitin-Protein LigasesCCAAT-Enhancer-Binding ProteinsUbiquitin-Protein LigasesUHRF1 protein, human

Identifiers

PMID33939809
PMCPMC8216287
OpenAlexW3157161275

What OpenQuestion holds

Textmetadata
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.