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

Structure–function analysis of the nsp14 N7–guanine methyltransferase reveals an essential role in Betacoronavirus replication

29 Nov 2021

Abstract excerpt

As coronaviruses (CoVs) replicate in the host cell cytoplasm, they rely on their own capping machinery to ensure the efficient translation of their messenger RNAs (mRNAs), protect them from degradation by cellular 5' exoribonucleases (ExoNs), and escape innate immune sensing. The CoV nonstructural protein 14 (nsp14) is a bifunctional replicase subunit harboring an N-terminal 3'-to-5' ExoN domain and a C-terminal...

Read the complete abstract on PubMed

Topics

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

Share to Animal Virus Infections Studies
Share to SARS-CoV-2 and COVID-19 Research
Share to Viral gastroenteritis research and epidemiology

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 34845015
DOI: 10.1073/pnas.2108709118

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure–function analysis of the nsp14 N7–guanine methyltransferase reveals an essential role in Betacoronavirus replicationPMID 34845015Read ↗

Structure-function analysis of the nsp14 N7-guanine methyltransferase reveals an essential role in <i>Betacoronavirus</i> replicationSemantic proximity Read ↗

Functional screen reveals SARS coronavirus nonstructural protein nsp14 as a novel cap N7 methyltransferase.Semantic proximity Read ↗

Structural basis and functional analysis of the SARS coronavirus nsp14–nsp10 complexSemantic proximity Read ↗

Structural and molecular basis of mismatch correction and ribavirin excision from coronavirus RNASemantic proximity Read ↗

One severe acute respiratory syndrome coronavirus protein complex integrates processive RNA polymerase and exonuclease activities.Semantic proximity Read ↗

The Enzymatic Activity of the nsp14 Exoribonuclease Is Critical for Replication of MERS-CoV and SARS-CoV-2.Semantic proximity Read ↗

Mutagenesis of S-Adenosyl-l-Methionine-Binding Residues in Coronavirus nsp14 N7-Methyltransferase Demonstrates Differing Requirements for Genome Translation and Resistance to Innate Immunity.Semantic proximity Read ↗

The enzymatic activity of the nsp14 exoribonuclease is critical for replication of Middle East respiratory syndrome-coronavirusSemantic proximity Read ↗

The SARS-CoV-2 RNA polymerase is a viral RNA capping enzymeSemantic proximity Read ↗

The coronavirus nsp14 exoribonuclease interface with the cofactor nsp10 is essential for efficient virus replication and enzymatic activity.Semantic proximity Read ↗

Porcine Epidemic Diarrhea Virus Deficient in RNA Cap Guanine-N-7 Methylation Is Attenuated and Induces Higher Type I and III Interferon Responses.Semantic proximity Read ↗

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

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