Evidence map›Paper›PMID 40035759›Full record

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

Structural basis of SARS-CoV-2 polymerase inhibition by nonnucleoside inhibitor HeE1-2Tyr.

Florian Kabinger, Valerie Doze, Jana Schmitzová, Michael Lidschreiber, Christian Dienemann, Patrick Cramer

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 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. 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.

Florian KabingerDepartment of Molecular Biology, Max Planck Institute for Multidisciplinary Sciences, Göttingen 37077, Germany.
Valerie DozeDepartment of Molecular Biology, Max Planck Institute for Multidisciplinary Sciences, Göttingen 37077, Germany.
Jana SchmitzováDepartment of Molecular Biology, Max Planck Institute for Multidisciplinary Sciences, Göttingen 37077, Germany.
Michael LidschreiberDepartment of Molecular Biology, Max Planck Institute for Multidisciplinary Sciences, Göttingen 37077, Germany.
Christian DienemannDepartment of Molecular Biology, Max Planck Institute for Multidisciplinary Sciences, Göttingen 37077, Germany.
Patrick CramerDepartment of Molecular Biology, Max Planck Institute for Multidisciplinary Sciences, Göttingen 37077, Germany.ORCID 0000-0001-5454-7755

Funding

Max Planck Society Core funding
6 · The paper itself

Abstract

Targeting the RNA-dependent RNA polymerase (RdRp) of SARS-CoV-2 with small molecules is a promising therapeutic strategy against COVID-19, but potent and safe inhibitors are lacking. HeE1-2Tyr, a nonnucleoside inhibitor of Dengue virus RdRp, was also shown to inhibit SARS-CoV-2 RdRp in vitro and to have antiviral activity in cells, but the underlying mechanism remains unclear. Here, we elucidate the molecular mechanism of HeE1-2Tyr-mediated SARS-CoV-2 RdRp inhibition. Biochemical assays confirm that HeE1-2Tyr inhibits RdRp with an IC

Indexed as

Antiviral AgentsCoronavirus RNA-Dependent RNA PolymeraseRNA-Dependent RNA PolymeraseSARS-CoV-2Binding SitesCOVID-19COVID-19 Drug TreatmentCryoelectron MicroscopyHumansProtein BindingAntiviral AgentsCoronavirus RNA-Dependent RNA PolymeraseRNA-Dependent RNA Polymerasecryo-EMnon-nucleoside inhibitorRNA-dependent RNA polymeraseSARS-CoV-2

Identifiers

PMID40035759
PMCPMC11912441

What OpenQuestion holds

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LicenceCC BY
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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.