Evidence map›Paper›PMID 40434637›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2025

Biochemical and structural basis of Dicer helicase function unveiled by resurrecting ancient proteins.

Adedeji M Aderounmu, Josephine Maus-Conn, Claudia D Consalvo, Peter S Shen, Brenda L Bass

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Adedeji M AderounmuDepartment of Biochemistry, University of Utah, Salt Lake City, UT 84112.ORCID 0000-0002-9981-7533
Josephine Maus-ConnDepartment of Biochemistry, University of Utah, Salt Lake City, UT 84112.ORCID 0009-0000-7505-0385
Claudia D ConsalvoDepartment of Biochemistry, University of Utah, Salt Lake City, UT 84112.ORCID 0000-0003-2038-4315
Peter S ShenDepartment of Biochemistry, University of Utah, Salt Lake City, UT 84112.ORCID 0000-0002-6256-6910
Brenda L BassDepartment of Biochemistry, University of Utah, Salt Lake City, UT 84112.ORCID 0000-0003-1728-2254

Funding

Elucidating roles and mechanisms of double-stranded RNA-mediated pathwaysR35GM141262 · NIGMS · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Brenda L. Bass · 2021 to 2026
$3.7M
Visualizing the Mechanisms of Protein Quality ControlR35GM133772 · NIGMS · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Peter Shen · 2019 to 2026
$3.4M
University of Utah Genetics Training ProgramT32GM141848 · NIGMS · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI GOLIC, KENT G, GRUNWALD, DAVID J. · 2021 to 2025
$2.9M
HHS | NIH | National Institute of General Medical Sciences (NIGMS) R35GM133772HHS | NIH | National Institute of General Medical Sciences (NIGMS) R35GM141262NIGMS NIH HHS R35 GM133772NIGMS NIH HHS R35 GM141262NIGMS NIH HHS T32 GM141848
6 · The paper itself

Abstract

A fully functional Dicer helicase, present in the modern arthropod, uses energy from ATP hydrolysis to power translocation on bound dsRNA, enabling the processive dsRNA cleavage required for efficient antiviral defense. However, modern Dicer orthologs exhibit divergent helicase functions that affect their ability to contribute to antiviral defense. Moreover, mechanisms that couple ATP hydrolysis to Dicer helicase movement on dsRNA remain enigmatic. We used biochemical and structural analyses of ancestrally reconstructed Dicer helicases to map evolution of dsRNA binding affinity, ATP hydrolysis and translocation. Loss of affinity for dsRNA occurred early in Dicer evolution, coinciding with a decline in translocation activity, despite preservation of ATP hydrolysis activity. Ancestral nematode Dicer also exhibited significant decline in ATP hydrolysis and translocation, but studies of antiviral activities in the modern nematode

Indexed as

DEAD-box RNA HelicasesRibonuclease IIIAdenosine TriphosphateAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCryoelectron MicroscopyEvolution, MolecularHydrolysisModels, MolecularRNA, Double-StrandedAdenosine TriphosphateCaenorhabditis elegans ProteinsDEAD-box RNA HelicasesRibonuclease IIIRNA, Double-Strandedcryo-EMDicerevolutionary biochemistryhelicase

Identifiers

PMID40434637
PMCPMC12146746

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LicenceCC BY-NC-ND
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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.