Results 91 to 100 of about 40,674 (185)

Engagement of nsp9cov19 with the nsp12 NiRAN domain and VHH2nsp23.

open access: yes, 2023
A) Cartoon representation nsp9COV19 when engaged with the nsp12 NiRAN domain (10). B) Aligned nsp9COV19 structure when VHH2nsp23-bound demonstrating distortion of the NiRAN-engaging structural elements.
Indu R. Chandrashekaran (448750)   +4 more
core   +1 more source

A Cross‐Sectional Study Shows Emergence of the Delta, 19B, 20A, 20B, 19A, and Omicron Variants of SARS‐CoV‐2 in Burkina Faso: A Conundrum Within a Conundrum

open access: yesHealth Science Reports, Volume 9, Issue 4, April 2026.
ABSTRACT Context and Objective SARS‐CoV‐2 is an RNA virus that emerged in Wuhan, China. Adaptive mutations in its genome can influence the virus's pathogenicity, enhance its ability to evade the host immune system, and complicate vaccine development. This study aimed to identify the circulating SARS‐CoV‐2 variants in Burkina Faso and trace their origin.
Tatiana Doriane Lallogo   +20 more
wiley   +1 more source

Increased flexibility of the SARS-CoV-2 RNA-binding site causes resistance to remdesivir.

open access: yesPLoS Pathogens, 2023
Mutations continue to accumulate within the SARS-CoV-2 genome, and the ongoing epidemic has shown no signs of ending. It is critical to predict problematic mutations that may arise in clinical environments and assess their properties in advance to ...
Shiho Torii   +17 more
doaj   +1 more source

DataSheet1_Investigation of protein-protein interactions and hotspot region on the NSP7-NSP8 binding site in NSP12 of SARS-CoV-2.docx

open access: yes
Background: The RNA-dependent RNA polymerase (RdRp) complex, essential in viral transcription and replication, is a key target for antiviral therapeutics.
Emmanuel Duarte Barbosa (17806169)   +11 more
core   +1 more source

The Open Reading Frame 7b of the SARS‐CoV‐2 Disperse Trans‐Golgi and Activate the NLRP3 Inflammasome

open access: yesJournal of Medical Virology, Volume 98, Issue 4, April 2026.
ABSTRACT Inflammasomes orchestrate the inflammatory response against bacterial and viral infections, thereby initiating the synthesis of pro‐inflammatory cytokines, mainly IL‐1β and IL‐18. SARS‐CoV‐2 infection induces an inflammatory response mediated by the activation of NLRP1 and NLRP3 inflammasomes.
Julio García‐Villalba   +4 more
wiley   +1 more source

Rapid incorporation of Favipiravir by the fast and permissive viral RNA polymerase complex results in SARS-CoV-2 lethal mutagenesis

open access: yesNature Communications, 2020
Favipiravir (T-705) is an inhibitor of viral RNA-dependent-RNA-polymerases (RdRp) and clinical trials for the treatment of COVID-19 are ongoing. Here, the authors show that SARS-CoV nsp12 is the fastest known viral RdRp and they provide insights into the
Ashleigh Shannon   +12 more
doaj   +1 more source

Liquid–Liquid Phase Separation in Viral Infection and Immunology

open access: yesMedComm, Volume 7, Issue 4, April 2026.
LLPS organizes viral replication and antiviral immunity. Viruses hijack LLPS to form replication factories and evade immune sensors, while hosts assemble LLPS‐driven signaling hubs (e.g., MAVS, RIG‐I, and SGs) to amplify interferon responses. Targeting these condensate interfaces offers novel therapeutic strategies against infectious diseases ...
Jiuzhi Xu   +5 more
wiley   +1 more source

Rapid selection of P323L in the SARS-CoV-2 polymerase (NSP12) in humans and non-human primate models and confers a large plaque phenotype

open access: yes, 2021
The mutational landscape of SARS-CoV-2 varies at both the dominant viral genome sequence and minor genomic variant population. An early change associated with transmissibility was the D614G substitution in the spike protein.
Salguero, Francisco   +53 more
core   +1 more source

Antivirals Targeting Coronavirus RNA‐Dependent RNA Polymerase and Main Protease: From Mechanisms of Action to Outcomes in COVID‐19 Clinical Trials

open access: yesMicrobial Biotechnology, Volume 19, Issue 4, April 2026.
The target sites of COVID‐19 antivirals discussed in the present opinion paper, namely the RNA dependent RNA polymerase Nsp12 and of the main viral protease Nsp5, are indicated by a red star in the overview of the replication cycle of coronavirus SARS‐CoV‐2.
Harald Brüssow
wiley   +1 more source

Galectin-3 inhibits replication of porcine reproductive and respiratory syndrome virus by interacting with viral Nsp12 in vitro

open access: yesVirus Research, 2018
Porcine galectin-3 (GAL3) is a 29-kDa protein encoded by a single gene, LGALS3, located on chromosome 1. Here, using a yeast two-hybrid screen of a cDNA library from porcine alveolar macrophage cells (PAMs), we report for the first time that GAL3 interacts with nonstructural protein 12 (Nsp12) of the porcine reproductive and respiratory syndrome virus (
Li, Liwei   +8 more
openaire   +2 more sources

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