Evidence map›Paper›PMID 31802118›Full record

ArticleNucleic acids research2020

The human HELLS chromatin remodelling protein promotes end resection to facilitate homologous recombination and contributes to DSB repair within heterochromatin.

Gabriel Kollárovič, Caitríona E Topping, Edward P Shaw, Anna L Chambers

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

44 citing papers in PubMed, 57 citations in OpenAlex.

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  19. SFPQ and Its Isoform as Potential Biomarker for Non-Small-Cell Lung Cancer.International journal of molecular sciences · 2023
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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 1 institution in 1 country.

Gabriel KollárovičDNA-protein Interactions Unit, School of Biochemistry, University of Bristol, Bristol BS8 1TD, UK.
Caitríona E ToppingDNA-protein Interactions Unit, School of Biochemistry, University of Bristol, Bristol BS8 1TD, UK.
Edward P ShawDNA-protein Interactions Unit, School of Biochemistry, University of Bristol, Bristol BS8 1TD, UK.
Anna L ChambersDNA-protein Interactions Unit, School of Biochemistry, University of Bristol, Bristol BS8 1TD, UK.
University of Bristol · GB

Funding

Cancer Research UK 17506Cancer Research UK C49963/A1750Wellcome Trust
6 · The paper itself

Abstract

Efficient double-strand break repair in eukaryotes requires manipulation of chromatin structure. ATP-dependent chromatin remodelling enzymes facilitate different DNA repair pathways, during different stages of the cell cycle and in varied chromatin environments. The contribution of remodelling factors to double-strand break repair within heterochromatin during G2 is unclear. The human HELLS protein is a Snf2-like chromatin remodeller family member and is mutated or misregulated in several cancers and some cases of ICF syndrome. HELLS has been implicated in the DNA damage response, but its mechanistic function in repair is not well understood. We discover that HELLS facilitates homologous recombination at two-ended breaks and contributes to repair within heterochromatic regions during G2. HELLS promotes initiation of HR by facilitating end-resection and accumulation of CtIP at IR-induced foci. We identify an interaction between HELLS and CtIP and establish that the ATPase domain of HELLS is required to promote DSB repair. This function of HELLS in maintenance of genome stability is likely to contribute to its role in cancer biology and demonstrates that different chromatin remodelling activities are required for efficient repair in specific genomic contexts.

Indexed as

DNA Breaks, Double-StrandedChromatin Assembly and DisassemblyDNA DamageDNA HelicasesDNA RepairGenome, HumanGenomic InstabilityHeterochromatinHomologous RecombinationHumansDNA HelicasesHELLS protein, humanHeterochromatin

Identifiers

PMID31802118
PMCPMC7038987
OpenAlexW2994559041

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.