3 results match your criteria: "Institute for Molecular Biology (IBMB-CSIC)[Affiliation]"
Metabolic and mitochondria alterations induced by SARS-CoV-2 accessory proteins ORF3a, ORF9b, ORF9c and ORF10.
J Med Virol
July 2024
Viral Immunology Lab, Molecular Biomedicine Department, BICS Unit. Margarita Salas Center for Biological Research (CIB-CSIC), Madrid, Spain.
Article Synopsis
- - SARS-CoV-2 accessory proteins ORF3a, ORF9b, ORF9c, and ORF10 disrupt mitochondrial functions and cell metabolism in lung epithelial cells, affecting antiviral signaling and immune responses.
- - While ORF9b, ORF9c, and ORF10 have similar effects on gene expression, ORF3a shows unique impacts, including significant changes in mitochondrial structure and the downregulation of key mitochondrial genes.
- - Research reveals that different accessory proteins modify metabolic processes, with lower amino acid metabolism in ORF9b, ORF9c, and ORF10, and increased lipid metabolism in ORF3a, highlighting potential new therapeutic targets for COVID-19 intervention.
Protein-protein interaction antagonists as novel inhibitors of non-canonical polyubiquitylation.
PLoS One
June 2010
Department of Cell Biology, Institute for Molecular Biology (IBMB-CSIC), Barcelona, Spain.
Background: Several pathways that control cell survival under stress, namely RNF8-dependent DNA damage recognition and repair, PCNA-dependent DNA damage tolerance and activation of NF-kappaB by extrinsic signals, are regulated by the tagging of key proteins with lysine 63-based polyubiquitylated chains, catalyzed by the conserved ubiquitin conjugating heterodimeric enzyme Ubc13-Uev.
Methodology/principal Findings: By applying a selection based on in vivo protein-protein interaction assays of compounds from a combinatorial chemical library followed by virtual screening, we have developed small molecules that efficiently antagonize the Ubc13-Uev1 protein-protein interaction, inhibiting the enzymatic activity of the heterodimer. In mammalian cells, they inhibit lysine 63-type polyubiquitylation of PCNA, inhibit activation of NF-kappaB by TNF-alpha and sensitize tumor cells to chemotherapeutic agents.