Download full-text PDF |
Source |
|---|
Publication Analysis
Top Keywords
Similar Publications
The SARS-CoV-2 nucleocapsid protein interferes with the full enzymatic activation of UPF1 and its interaction with UPF2.
Nucleic Acids Res
January 2025
Molecular Microbiology and Structural Biochemistry, MMSB-IBCP, CNRS UMR 5086 , Université Claude Bernard Lyon 1, F-69367 Lyon, France.
The nonsense-mediated mRNA decay (NMD) pathway triggers the degradation of defective mRNAs and governs the expression of mRNAs with specific characteristics. Current understanding indicates that NMD is often significantly suppressed during viral infections to protect the viral genome. In numerous viruses, this inhibition is achieved through direct or indirect interference with the RNA helicase UPF1, thereby promoting viral replication and enhancing pathogenesis.
View Article and Find Full Text PDFCrucial role of the cGAS N terminus in mediating flowable and functional cGAS-DNA condensate formation via DNA interactions.
Proc Natl Acad Sci U S A
January 2025
Department of General Surgery, The First Affiliated Hospital of University of Science and Technology of China, Key Laboratory of Immune Response and Immunotherapy, Center for Advanced Interdisciplinary Science Interdisciplinary Science & Biomedicine of Institute of Health and Medicine, Division of Life Sciences & Medicine, University of Science and Technology of China, Hefei 230027, Anhui, China.
The DNA-sensing protein cGAS plays a pivotal role in the innate immune response and pathogenesis of various diseases. DNA triggers liquid-liquid phase separation (LLPS) and enhances the enzymatic activity of cGAS. However, the regulatory mechanisms of the disordered N terminus remain unclear.
View Article and Find Full Text PDFThiol-Reactive or Redox-Active: Revising a Repurposing Screen Led to a New Invalidation Pipeline and Identified a True Noncovalent Inhibitor Against Papain-like Protease from SARS-CoV-2.
ACS Pharmacol Transl Sci
January 2025
Fraunhofer Institute for Translational Medicine and Pharmacology ITMP, Discovery Research ScreeningPort, Schnackenburgallee 114, 22525 Hamburg, Germany.
The SARS-CoV-2 papain-like protease PLpro has multiple roles in the viral replication cycle, related to both its polypeptide cleavage function and its ability to antagonize the host immune response. Targeting the PLpro function is recognized as a promising mechanism to modulate viral replication, while supporting host immune responses. However, the development of PLpro-specific inhibitors remains challenging.
View Article and Find Full Text PDFEnzyme kinetics model for the coronavirus main protease including dimerization and ligand binding.
bioRxiv
January 2025
Department of Chemistry, Illinois Institute of Technology, Chicago, IL 60616, USA.
The coronavirus main protease (MPro) plays a pivotal role in viral replication and is the target of several antivirals against SARS-CoV-2. In some species, CRCs of MPro enzymatic activity can exhibit biphasic behavior in which low ligand concentrations activate the enzyme whereas higher ones inhibit it. While this behavior has been attributed to ligand-induced dimerization, quantitative enzyme kinetics models have not been fit to it.
View Article and Find Full Text PDFCys44 of SARS-CoV-2 3CL affects its catalytic activity.
Int J Biol Macromol
January 2025
Department of Chemical Sciences, University of Naples "Federico II", Via Cintia, 21, 80126 Napoli, Italy; CEINGE Advanced Biotechnologies s.c.a r.l. "Franco Salvatore", Via Gaetano Salvatore 486, 80131 Napoli, Italy. Electronic address:
SARS-CoV-2 encodes a 3C-like protease (3CL) that is essential for viral replication. This cysteine protease cleaves viral polyproteins to release functional nonstructural proteins, making it a prime target for antiviral drug development. We investigated the inhibitory effects of halicin, a known c-Jun N-terminal kinase inhibitor, on 3CL.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!