Evidence map›Paper›PMID 27045313›Full record

ArticleScientific reports2016

Revealing a new activity of the human Dicer DUF283 domain in vitro.

Anna Kurzynska-Kokorniak, Maria Pokornowska, Natalia Koralewska, Weronika Hoffmann, Krystyna Bienkowska-Szewczyk, Marek Figlerowicz

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

24 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
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  4. Identification ofFrontiers in microbiology · 2025
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  7. Research Progress in RNA-Binding Proteins.International journal of molecular sciences · 2022
    Article
  8. Article
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  10. RNA Interference: Promising Approach to Combat Plant Viruses.International journal of molecular sciences · 2022
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. RNA and DNA G-quadruplexes bind to human dicer and inhibit its activity.Cellular and molecular life sciences : CMLS · 2021
    Article
  16. Review
  17. The RNA-RNA base pairing potential of human Dicer and Ago2 proteins.Cellular and molecular life sciences : CMLS · 2020
    Article
  18. Article
  19. Review
  20. Dicer's Helicase Domain: A Meeting Place for Regulatory Proteins.Cold Spring Harbor symposia on quantitative biology · 2019
    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

6 authors at 3 institutions in 1 country.

Anna Kurzynska-KokorniakInstitute of Bioorganic Chemistry, Polish Academy of Sciences, 61-704 Poznan, Poland.
Maria PokornowskaInstitute of Bioorganic Chemistry, Polish Academy of Sciences, 61-704 Poznan, Poland.
Natalia KoralewskaInstitute of Bioorganic Chemistry, Polish Academy of Sciences, 61-704 Poznan, Poland.
Weronika HoffmannIntercollegiate Faculty of Biotechnology of University of Gdansk and Medical University of Gdansk, 80-822 Gdansk, Poland.
Krystyna Bienkowska-SzewczykIntercollegiate Faculty of Biotechnology of University of Gdansk and Medical University of Gdansk, 80-822 Gdansk, Poland.
Marek FiglerowiczInstitute of Bioorganic Chemistry, Polish Academy of Sciences, 61-704 Poznan, Poland.
Institute of Bioorganic Chemistry, Polish Academy of Sciences · PLGdańsk Medical University · PLPoznań University of Technology · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ribonuclease Dicer is a multidomain enzyme that plays a fundamental role in the biogenesis of small regulatory RNAs (srRNAs), which control gene expression by targeting complementary transcripts and inducing their cleavage or repressing their translation. Recent studies of Dicer's domains have permitted to propose their roles in srRNA biogenesis. For all of Dicer's domains except one, called DUF283 (domain of unknown function), their involvement in RNA substrate recognition, binding or cleavage has been postulated. For DUF283, the interaction with Dicer's protein partners has been the only function suggested thus far. In this report, we demonstrate that the isolated DUF283 domain from human Dicer is capable of binding single-stranded nucleic acids in vitro. We also show that DUF283 can act as a nucleic acid annealer that accelerates base-pairing between complementary RNA/DNA molecules in vitro. We further demonstrate an annealing activity of full length human Dicer. The overall results suggest that Dicer, presumably through its DUF283 domain, might facilitate hybridization between short RNAs and their targets. The presented findings reveal the complex nature of Dicer, whose functions may extend beyond the biogenesis of srRNAs.

Indexed as

Cell Line, TumorDEAD-box RNA HelicasesDNA, ComplementaryDNA, Single-StrandedHumansImmunoblottingMagnesiumModels, MolecularNucleic Acid HybridizationOligonucleotidesProtein BindingProtein DomainsRibonuclease IIIRNA, MessengerRNA, Small InterferingZincDEAD-box RNA HelicasesDICER1 protein, humanDNA, ComplementaryDNA, Single-StrandedMagnesiumOligonucleotidesRibonuclease IIIRNA, MessengerRNA, Small InterferingZinc

Identifiers

PMID27045313
PMCPMC4820750
OpenAlexW2335744039

What OpenQuestion holds

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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.