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

SARS-CoV-2 nsp15 preferentially degrades AU-rich dsRNA via its dsRNA nickase activity

5 Apr 2024

Abstract excerpt

It has been proposed that coronavirus nsp15 mediates evasion of host cell double-stranded (ds) RNA sensors via its uracil-specific endoribonuclease activity. However, how nsp15 processes viral dsRNA, commonly considered as a genome replication intermediate, remains elusive. Previous research has mainly focused on short single-stranded RNA as substrates, and whether nsp15 prefers single-stranded or double-stranded...

Read the complete abstract on PubMed

Topics

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

Share to RNA regulation and disease
Share to SARS-CoV-2 and COVID-19 Research
Share to Viral Infections and Immunology Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 38634805
DOI: 10.1093/nar/gkae290

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

SARS-CoV-2 nsp15 preferentially degrades AU-rich dsRNA via its dsRNA nickase activityPMID 38634805Read ↗

The nsp15 Nuclease as a Good Target to Combat SARS-CoV-2: Mechanism of Action and Its Inactivation with FDA-Approved DrugsSemantic proximity Read ↗

Structural and Biochemical Characterization of Endoribonuclease Nsp15 Encoded by Middle East Respiratory Syndrome CoronavirusSemantic proximity Read ↗

Biochemical Characterization of Emerging SARS-CoV-2 Nsp15 Endoribonuclease VariantsSemantic proximity Read ↗

RNA 3'-end mismatch excision by the severe acute respiratory syndrome coronavirus nonstructural protein nsp10/nsp14 exoribonuclease complexSemantic proximity Read ↗

The Role of Coronavirus RNA-Processing Enzymes in Innate Immune EvasionSemantic proximity Read ↗

SARS-CoV-2 nsp15 endoribonuclease antagonizes dsRNA-induced antiviral signalingSemantic proximity Read ↗

Structural basis for polyuridine tract recognition by SARS-CoV-2 Nsp15Semantic proximity Read ↗

Recent insights into the structure and function of coronavirus ribonucleases.Semantic proximity Read ↗

SARS-CoV-2 Nsp15 antagonizes the cGAS-STING-mediated antiviral innate immune responsesSemantic proximity Read ↗

SARS-CoV-2 EndoU-ribonuclease regulates RNA recombination and impacts viral fitnessSemantic proximity Read ↗

Structure and dynamics of SARS-CoV-2 proofreading exoribonuclease ExoNSemantic proximity Read ↗

The coronavirus nsp15 endoribonuclease: A puzzling protein and pertinent antiviral drug targetSemantic proximity Read ↗

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