Evidence map›Paper›PMID 41750343›Full record

ReviewBiomolecules2026

Structure, Function and Inhibition of Helicases Involved in Virus Infection.

Gisoo Sarvari, David D Boehr

Abstract readReview
In one paragraph

Review in Biomolecules, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

2 authors.

Gisoo SarvariDepartment of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA.ORCID 0000-0002-7976-5705
David D BoehrDepartment of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA.ORCID 0000-0002-8886-2873

Funding

Watching Conformational Rearrangements in Poliovirus RNA-Dependent RNA PolymeraseR01AI104878 · NIAID · PENNSYLVANIA STATE UNIVERSITY, THE · PI BOEHR, DAVID DOUGLAS · 2014 to 2024
$3.0M
NIAID NIH HHS R01 AI104878NIH HHS 2R01AI104878-25
6 · The paper itself

Abstract

Viral helicases are conserved nucleic acid-dependent ATPases that drive genome replication, gene expression, and virion assembly, thereby playing a central role in viral replication and pathogenicity. Here, we discuss structural, biochemical, and virological data to compare helicase superfamilies, their conserved motifs, and translocation models that couple ATP hydrolysis to strand separation. We then analyze how viral helicases regulate replication fork progression, transcription and translation of viral RNAs, viral genome remodeling during replication, genome-packaging strategies, and evasion of innate immune signaling. Mechanistic examples from picornaviruses, flaviviruses, herpesviruses, and coronaviruses demonstrate how helicase architecture, substrate specificity, and cofactors control these activities. Finally, we discuss the opportunities and drawbacks of targeting viral helicases with antiviral drugs, recent screening and structure-guided discovery efforts, and emerging resistance mechanisms. Overall, this review provides a virus-centered synthesis of helicase structure, function, and inhibition that links conserved enzymatic activities to diverse infection outcomes and antiviral strategies across viral families.

Indexed as

DNA HelicasesRNA HelicasesViral ProteinsVirus DiseasesAnimalsAntiviral AgentsHumansVirus ReplicationAntiviral AgentsDNA HelicasesRNA HelicasesViral Proteinsantiviral drug targetsgenome packaginghelicase inhibitorsviral gene expressionviral helicases

Identifiers

PMID41750343
PMCPMC12938291

What OpenQuestion holds

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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.