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

Structural insights into the substrate specificity of the endonuclease activity of the influenza virus cap-snatching mechanism

31 Dec 2020

Abstract excerpt

The endonuclease activity within the influenza virus cap-snatching process is a proven therapeutic target. The anti-influenza drug baloxavir is highly effective, but is associated with resistance mutations that threaten its clinical efficacy. The endonuclease resides within the N-terminal domain of the PA subunit (PAN) of the influenza RNA dependent RNA polymerase, and we report here complexes of PAN with RNA and...

Read the complete abstract on PubMed

Topics

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

Share to Influenza Virus Research Studies
Share to RNA and protein synthesis mechanisms
Share to Viral Infections and Immunology Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 33469660
DOI: 10.1093/nar/gkaa1294

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

Structural insights into the substrate specificity of the endonuclease activity of the influenza virus cap-snatching mechanismPMID 33469660Read ↗

Insights into Two-Metal-Ion Catalytic Mechanism of Cap-Snatching Endonuclease of Ebinur Lake Virus in Bunyavirales.Semantic proximity Read ↗

Comparative Structural and Functional Analysis of Bunyavirus and Arenavirus Cap-Snatching EndonucleasesSemantic proximity Read ↗

The Influenza Virus Polymerase Complex: An Update on Its Structure, Functions, and Significance for Antiviral Drug DesignSemantic proximity Read ↗

Structural insight into the essential PB1-PB2 subunit contact of the influenza virus RNA polymerase.Semantic proximity Read ↗

The Cap-Snatching SFTSV Endonuclease Domain Is an Antiviral TargetSemantic proximity Read ↗

In vitro characterization of baloxavir acid, a first-in-class cap-dependent endonuclease inhibitor of the influenza virus polymerase PA subunitSemantic proximity Read ↗

Structure and function of the Toscana virus cap-snatching endonucleaseSemantic proximity Read ↗

Characterization of influenza virus variants induced by treatment with the endonuclease inhibitor baloxavir marboxil.Semantic proximity Read ↗

Biochemical and structural studies reveal differences and commonalities among cap-snatching endonucleases from segmented negative-strand RNA virusesSemantic proximity Read ↗

Parameterization of the PA Endonuclease Bimetallic Center Reveals the Dynamics of Clinically Relevant Mutations.Semantic proximity Read ↗

Parameterization of the PA endonuclease bimetallic center reveals the dynamics of clinically relevant mutationsSemantic proximity Read ↗

Mutational analysis of the binding pockets of the diketo acid inhibitor L-742,001 in the influenza virus PA endonuclease.Semantic proximity Read ↗

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