Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Preferential remdesivir triphosphate incorporation by SARS-CoV-2 polymerase is altered to ATP by the S759A mutation.

Communications biology - 13 Mar 2026

Gordon Calvin J, Oliva Mizar F, Lee Hery W, Goovaerts Quinten, De Wijngaert Brent, Götte Matthias, Das Kalyan

Abstract excerpt

Nucleoside analogs are successful in treating viral infections. dNTP analogs are primarily DNA chain terminators, while NTP analog remdesivir can inhibit RNA synthesis by delayed chain termination or when embedded in the template strand. Here, enzymatic assays, mass spectrometry, and cryo-EM structures demonstrate that SARS-CoV-2 RNA-dependent RNA polymerase (RdRp) preferentially incorporates remdesivir...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adenosine Monophosphate
Share to Adenosine Triphosphate

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Alanine

Share to Antiviral Agents

Share to Mutation

Share to SARS-CoV-2

Source

Open in PubMed Open full text

Identifiers

PMID: 41826755
DOI: 10.1038/s42003-026-09844-z
PMCID: PMC13125513

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Preferential remdesivir triphosphate incorporation by SARS-CoV-2 polymerase is altered to ATP by the S759A mutation.PMID 41826755Read ↗

Unveiling the “Template-Dependent” Inhibition on the Viral Transcription of SARS-CoV-2Semantic proximity Read ↗

Remdesivir and SARS-CoV-2: Structural requirements at both nsp12 RdRp and nsp14 Exonuclease active-sites.Semantic proximity Read ↗

Remdesivir overcomes the S861 roadblock in SARS-CoV-2 polymerase elongation complexSemantic proximity Read ↗

Remdesivir is a Delayed Translocation Inhibitor of SARS CoV-2 ReplicationSemantic proximity Read ↗

Impact of Remdesivir Incorporation along the Primer Strand on SARS-CoV-2 RNA-Dependent RNA PolymeraseSemantic proximity Read ↗

Remdesivir for the treatment of Covid-19: the value of biochemical studiesSemantic proximity Read ↗

Template-dependent inhibition of coronavirus RNA-dependent RNA polymerase by remdesivir reveals a second mechanism of action.Semantic proximity Read ↗

Mechanism and spectrum of inhibition of a 4′-cyano modified nucleotide analog against diverse RNA polymerases of prototypic respiratory RNA virusesSemantic proximity Read ↗

Mechanism of Inhibition of Ebola Virus RNA-Dependent RNA Polymerase by RemdesivirSemantic proximity Read ↗

Mutations in the SARS-CoV-2 RNA-dependent RNA polymerase confer resistance to remdesivir by distinct mechanisms.Semantic proximity Read ↗

Substrate and target selectivity of 4′-fluoroadenosine against viral and host polymerasesSemantic proximity Read ↗

A cell-based assay to discover inhibitors of SARS-CoV-2 RNA dependent RNA polymeraseSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.