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

Biochemical simulation of mutation synthesis and repair during SARS-CoV-2 RNA polymerization.

Virology - 1 Dec 2024

Oo Adrian, Chen Zhenhang, Cao Dongdong, Cho Young-Jae, Liang Bo, Schinazi Raymond F, Kim Baek

Abstract excerpt

We biochemically simulated the mutation synthesis process of SARS-CoV-2 RNA-dependent RNA polymerase (RdRp) complex (nsp7/nsp8/nsp12) involving two sequential mechanistic steps that occur during genomic replication: misinsertion (incorporation of incorrect nucleotides) and mismatch extension. Then, we also simulated mismatch repair process catalyzed by the viral nsp10/nsp14 ExoN complex. In these mechanistic...

Read the complete abstract on PubMed

Topics

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

Share to COVID-19
Share to Genome, Viral
Share to Polymerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to RNA-Dependent RNA Polymerase

Share to RNA, Viral

Share to SARS-CoV-2

Share to Viral Nonstructural Proteins

Share to Virus Replication

Source

Open in PubMed Open full text

Identifiers

PMID: 39366027
DOI: 10.1016/j.virol.2024.110255
PMCID: PMC13380264

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Biochemical simulation of mutation synthesis and repair during SARS-CoV-2 RNA polymerization.PMID 39366027Read ↗

Slow PPi release enhances fidelity of the SARS-CoV-2 RNA dependent RNA polymerase.Semantic proximity Read ↗

Loss of nsp14-exonuclease activity impairs the replication, proofreading, fitness, and pathogenesis of SARS-CoV-2.Semantic proximity Read ↗

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

Infidelity of SARS-CoV Nsp14-exonuclease mutant virus replication is revealed by complete genome sequencing.Semantic proximity Read ↗

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

The SARS-coronavirus nsp7+nsp8 complex is a unique multimeric RNA polymerase capable of both de novo initiation and primer extensionSemantic proximity Read ↗

Genome-Wide Analysis of the Indispensable Role of Non-structural Proteins in the Replication of SARS-CoV-2Semantic proximity Read ↗

The SARS-CoV nsp12 Polymerase Active Site Is Tuned for Large-Genome ReplicationSemantic proximity Read ↗

Mutations in SARS-CoV-2 nsp7 and nsp8 proteins and their predicted impact on replication/transcription complex structure.Semantic proximity Read ↗

A Proofreading Mutation with an Allosteric Effect Allows a Cluster of SARS-CoV-2 Viruses to Rapidly Evolve.Semantic proximity Read ↗

Loss of nsp14-exonuclease activity impairs the replication, proofreading, fitness and pathogenesis of SARS-CoV-2Semantic proximity Read ↗

Characterization of SARS-CoV-2 replication complex elongation and proofreading activitySemantic proximity Read ↗

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