Evidence map›Paper›PMID 27612385›Full record

ArticleeLife2016

Human DNA2 possesses a cryptic DNA unwinding activity that functionally integrates with BLM or WRN helicases.

Cosimo Pinto, Kristina Kasaciunaite, Ralf Seidel, Petr Cejka

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

48 citing papers in PubMed, 82 citations in OpenAlex.

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  19. Generation of double Holliday junction DNAs and their dissolution/resolution within a chromatin context.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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.

Cosimo PintoInstitute of Molecular Cancer Research, University of Zurich, Zurich, Switzerland.
Kristina KasaciunaiteInstitute of Experimental Physics I, University of Leipzig, Leipzig, Germany.
Ralf SeidelInstitute of Experimental Physics I, University of Leipzig, Leipzig, Germany.
Petr CejkaInstitute of Molecular Cancer Research, University of Zurich, Zurich, Switzerland.ORCID 0000-0002-9087-032X
Leipzig University · DEUniversity of Zurich · CH

Funding

European Research Council 261224
6 · The paper itself

Abstract

Human DNA2 (hDNA2) contains both a helicase and a nuclease domain within the same polypeptide. The nuclease of hDNA2 is involved in a variety of DNA metabolic processes. Little is known about the role of the hDNA2 helicase. Using bulk and single-molecule approaches, we show that hDNA2 is a processive helicase capable of unwinding kilobases of dsDNA in length. The nuclease activity prevents the engagement of the helicase by competing for the same substrate, hence prominent DNA unwinding by hDNA2 alone can only be observed using the nuclease-deficient variant. We show that the helicase of hDNA2 functionally integrates with BLM or WRN helicases to promote dsDNA degradation by forming a heterodimeric molecular machine. This collectively suggests that the hDNA2 motor promotes the enzyme's capacity to degrade dsDNA in conjunction with BLM or WRN and thus promote the repair of broken DNA.

Indexed as

DNADNA HelicasesHumansProtein MultimerizationRecQ HelicasesWerner Syndrome HelicaseBloom syndrome proteinDNADNA2 protein, humanDNA HelicasesRecQ HelicasesWerner Syndrome HelicaseWRN protein, humanbiochemistrychromosomesDNA end resectionDNA helicasegeneshomologous recombinationhuman

Identifiers

PMID27612385
PMCPMC5030094
OpenAlexW2516052007

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.