Evidence map›Paper›PMID 18927112›Full record

ArticleNucleic acids research2008

A role for the Dicer helicase domain in the processing of thermodynamically unstable hairpin RNAs.

Harris S Soifer, Masayuki Sano, Kumi Sakurai, Pritsana Chomchan, Pål Saetrom, Mark A Sherman, Michael A Collingwood, Mark A Behlke, John J Rossi

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

40 citing papers in PubMed, 56 citations in OpenAlex.

  1. The cellular landscape of druggable RNA-binding proteins.Nature reviews. Drug discovery · 2026
    Review
  2. Article
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  15. Review
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  17. DICER1: mutations, microRNAs and mechanisms.Nature reviews. Cancer · 2014
    Review
  18. Article
  19. Article
  20. Molecular mechanisms of RNA interference.Annual review of biophysics · 2013
    Review
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

9 authors at 4 institutions in 3 countries.

Harris S SoiferDepartment of Molecular Biology, Beckman Research Institute of the City of Hope, Duarte, CA 91010, USA.
Masayuki Sano
Kumi Sakurai
Pritsana Chomchan
Pål Saetrom
Mark A Sherman
Michael A Collingwood
Mark A Behlke
John J Rossi
National Institute of Advanced Industrial Science and Technology · JPCity of Hope · USIntegrated DNA Technologies (United States) · USNorwegian University of Science and Technology · NO

Funding

Enhancing the Intracellular Functioning of HIV RibozymesR37AI029329 · NIAID · CITY OF HOPE/BECKMAN RESEARCH INSTITUTE · PI ROSSI, JOHN JOSEPH · 2002 to 2011
$6.7M
Expression of anti-HIV siRNA in Blood CellsR01HL074704 · NHLBI · CITY OF HOPE/BECKMAN RESEARCH INSTITUTE · PI BURNETT, JOHN CORY, ROSSI, JOHN JOSEPH · 2003 to 2015
$5.0M
YEAST SYSTEM FOR DEVELOPING ANTI-HIV-1 RIBOZYMESR01AI029329 · NIAID · LOMA LINDA UNIVERSITY · PI ROSSI, JOHN JOSEPH · 1990 to 2018
$3.9M
SELECTED TOPICS IN CARDIOLOGYT32HL007470 · NHLBI · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI GETTES, LEONARD S · 1985 to 1989
–
NHLBI NIH HHS HL07470NHLBI NIH HHS R01 HL074704NIAID NIH HHS AI29329NIAID NIH HHS R01 AI029329NIAID NIH HHS R37 AI029329
6 · The paper itself

Abstract

In humans a single species of the RNAseIII enzyme Dicer processes both microRNA precursors into miRNAs and long double-stranded RNAs into small interfering RNAs (siRNAs). An interesting but poorly understood domain of the mammalian Dicer protein is the N-terminal helicase-like domain that possesses a signature DExH motif. Cummins et al. created a human Dicer mutant cell line by inserting an AAV targeting cassette into the helicase domain of both Dicer alleles in HCT116 cells generating an in-frame 43-amino-acid insertion immediately adjacent to the DExH box. This insertion creates a Dicer mutant protein with defects in the processing of most, but not all, endogenous pre-miRNAs into mature miRNA. Using both biochemical and computational approaches, we provide evidence that the Dicer helicase mutant is sensitive to the thermodynamic properties of the stems in microRNAs and short-hairpin RNAs, with thermodynamically unstable stems resulting in poor processing and a reduction in the levels of functional mi/siRNAs. Paradoxically, this mutant exhibits enhanced processing efficiency and concomitant RNA interference when thermodynamically stable, long-hairpin RNAs are used. These results suggest an important function for the Dicer helicase domain in the processing of thermodynamically unstable hairpin structures.

Indexed as

Cell LineHumansMicroRNAsMutationProtein Structure, TertiaryRibonuclease IIIRNA HelicasesRNA PrecursorsRNA Processing, Post-TranscriptionalRNA, UntranslatedThermodynamicsMicroRNAsRibonuclease IIIRNA HelicasesRNA PrecursorsRNA, Untranslated

Identifiers

PMID18927112
PMCPMC2582626
OpenAlexW2127509497

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.