SARS-CoV-2 viruso helikazės nsp13 mechanistiniai tyrimai
In the face of still ongoing COVID-19 diagnoses and mortality rates around the world, the development of drugs capable of targeting all SARS-CoV-2 strains is crucial, given the constant mutations and potential emergence of more dangerous virus variants. To address this, identifying a conserved protein target that remains unaffected by variation between
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SARS-CoV-2 Nsp13 helicase modulates miR-146a-mediated signaling pathways
Despite the successful development of vaccines and antiviral therapeutics against SARS-CoV-2, its tendency to mutate rapidly has emphasized the need for continued research to better understand this virus's mechanism of pathogenesis and interactions with host signaling pathways.
Eryn Lundrigan +4 more
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Copy-back RNA synthesis by coronavirus polymerase requires helicase activity and is stimulated by remdesivir and molnupiravir. [PDF]
Rakib A +23 more
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RNA virus polymerase-helicase coupling enables rapid elongation through duplex RNA. [PDF]
America PPB +11 more
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A funnel approach to enable analyses of epitope-specific human CD4 T cells specific for influenza and SARS-CoV-2. [PDF]
Richards KA +10 more
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Evolutionary inferences from the analysis of mutation dynamics in the SARS-CoV-2 replication-transcription complex. [PDF]
Palyanov AY +3 more
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Motif V is an allosteric couple between the SARS-CoV-2 nsp13 nucleotide triphosphatase and helicase active sites. [PDF]
Mingroni MA +3 more
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Hippo signalling as a nexus in host-virus interactions. [PDF]
Bahrami A, Walter C, Ardestani A.
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The regulatory mechanisms of SARS-CoV-2 N protein helicase and its annealing activity. [PDF]
Zhang B +13 more
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Protocol for the detection of RHIM-protein oligomeric complex formation using DSP-mediated crosslinking in HEK293T cultured cells. [PDF]
Mishra S, Dey AA, Kesavardhana S.
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