Results 11 to 20 of about 38,142 (142)

Redefining NSP12 activity in SARS-CoV-2 and its regulation by NSP8 and NSP7 [PDF]

open access: yesMolecular Therapy: Nucleic Acids
RdRp is a critical component of an RNA virus life cycle. Among coronaviruses, NSP12, along with one copy of NSP7 and two copies of NSP8, forms the RdRp holoenzyme and exhibits polymerase activity.
Deepa Singh   +17 more
doaj   +4 more sources

Cellular eEF1G Inhibits Porcine Deltacoronavirus Replication by Binding Nsp12 and Disrupting Its Interaction with Viral Genomic RNA [PDF]

open access: yesViruses
Porcine deltacoronavirus (PDCoV) is an emerging pathogen that causes severe, often fatal, diarrhea in suckling piglets and has zoonotic potential. Its nonstructural protein 12 (Nsp12), functioning as the RNA-dependent RNA polymerase (RdRp), is a central ...
Weijia Yin   +6 more
doaj   +4 more sources

Development of novel monoclonal antibodies against nsp12 of SARS-CoV-2

open access: yesVirology Journal, 2022
A novel coronavirus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has caused a global pandemic of coronavirus disease 19. Coronaviruses, including SARS-CoV-2, use RNA-dependent RNA polymerase (RdRP) for viral replication and ...
Mitsuhiro Machitani   +7 more
doaj   +3 more sources

SARS-CoV-2 Remdesivir Exposure Leads to Different Evolutionary Pathways That Converge in Moderate Levels of Drug Resistance [PDF]

open access: yesViruses
Various SARS-CoV-2 remdesivir resistance-associated substitutions (RAS) have been reported, but a comprehensive comparison of their resistance levels is lacking.
Carlota Fernandez-Antunez   +10 more
doaj   +2 more sources

Structural Homology-Based Drug Repurposing Approach for Targeting NSP12 SARS-CoV-2

open access: yesMolecules, 2022
The severe acute respiratory syndrome coronavirus 2, also known as SARS-CoV-2, is the causative agent of the COVID-19 global pandemic. SARS-CoV-2 has a highly conserved non-structural protein 12 (NSP-12) involved in RNA-dependent RNA polymerase (RdRp ...
Abdulelah Aljuaid   +10 more
doaj   +3 more sources

Galectin 3-binding protein suppresses PRRSV replication via Cullin3-mediated ubiquitination degradation of non-structural protein 12 [PDF]

open access: yesJournal of Virology
Porcine reproductive and respiratory syndrome virus (PRRSV) poses a major threat to the global swine industry, yet effective antiviral strategies remain limited.
Xinrong Wang   +8 more
doaj   +2 more sources

Antiviral Activity of Remdesivir and Obeldesivir Against SARS-CoV-2 Omicron Subvariants That Were Circulating from September 2023 Through June 2025 [PDF]

open access: yesViruses
With the ongoing emergence of SARS-CoV-2 variants, continued surveillance of antiviral susceptibility remains critical for detecting resistance that could compromise treatment efficacy.
Lauren Rodriguez   +10 more
doaj   +2 more sources

The P323L substitution in the SARS-CoV-2 polymerase (NSP12) confers a selective advantage during infection [PDF]

open access: yesGenome Biology, 2023
Background The mutational landscape of SARS-CoV-2 varies at the dominant viral genome sequence and minor genomic variant population. During the COVID-19 pandemic, an early substitution in the genome was the D614G change in the spike protein, associated ...
Hannah Goldswain   +29 more
doaj   +11 more sources

Fisetin as an Antiviral Agent Targeting the RNA-Dependent RNA Polymerase of SARS-CoV-2: Computational Prediction and In Vitro Experimental Validation [PDF]

open access: yesMicroorganisms
SARS-CoV-2 continues to evolve into immune-evasive variants, and although vaccination remains the cornerstone of prevention, the search for antiviral molecules targeting conserved viral enzymes remains essential.
Ximena Hernández-Rodríguez   +15 more
doaj   +2 more sources

Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-factors [PDF]

open access: yesNature Communications, 2019
The pathogenic human coronaviruses SARS- and MERS-CoV can cause severe respiratory disease. Here the authors present the 3.1Å cryo-EM structure of the SARS-CoV RNA polymerase nsp12 bound to its essential co-factors nsp7 and nsp8, which is of interest for
Robert N. Kirchdoerfer, Andrew B. Ward
doaj   +3 more sources

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