Results 41 to 50 of about 283 (118)

In vivo and in vitro phosphorylation of rotavirus NSP5 correlates with its localization in viroplasms [PDF]

open access: yesJournal of Virology, 1997
NSP5 (NS26), the product of rotavirus gene 11, is a phosphoprotein whose role in the virus replication cycle is unknown. To gain further insight into its function, we obtained monoclonal antibodies against the baculovirus-expressed protein. By immunoprecipitation and immunoblotting experiments, we showed that (i) NSP5 appears in many different ...
Poncet, Didier   +3 more
openaire   +3 more sources

SARS‐CoV‐2 targets mitochondria, exacerbating COVID‐19 pneumonia

open access: yesThe Journal of Physiology, EarlyView.
Abstract figure legend Following entry into airway epithelial cells (AECs), SARS‐CoV‐2 releases its single‐stranded RNA into the cytoplasm, where it is translated into viral proteins. Several of these viral proteins localize to mitochondria and interact with key mitochondrial components.
Danchen Wu   +5 more
wiley   +1 more source

Amino acid T25 in the substrate-binding domain of SARS-CoV-2 nsp5 is involved in viral replication in the mouse lung.

open access: yesPLoS ONE
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) non-structural protein 5 (nsp5) is a cysteine protease involved in viral replication and suppression of the host immune system.
Yoshiro Sugiura   +6 more
doaj   +1 more source

Autophagy Receptor p62 Regulates SARS-CoV-2-Induced Inflammation in COVID-19

open access: yesCells, 2023
As autophagy can promote or inhibit inflammation, we examined autophagy-inflammation interplay in COVID-19. Autophagy markers in the blood of 19 control subjects and 26 COVID-19 patients at hospital admission and one week later were measured by ELISA ...
Verica Paunovic   +12 more
doaj   +1 more source

The C117D oxidation mimic reveals the monomeric structure of SARS‐CoV‐2 main protease

open access: yesProtein Science, Volume 35, Issue 9, September 2026.
Abstract The SARS‐CoV‐2 main protease (Mpro) is essential for viral replication and functions as a homodimer, with dimerization being critical for catalytic activity. Mpro contains an unusually high number of cysteine residues. Among these, C117 and the catalytic nucleophile C145 can form a reversible disulfide bond under oxidative conditions.
Sam Andress   +2 more
wiley   +1 more source

NSP5 phosphorylation regulates the fate of viral mRNA in rotavirus infected cells

open access: yesArchives of Virology, 2002
Elucidation of the function of the non-structural rotavirus proteins during infection is difficult in the absence of a reverse genetic system. To study the role of NSP5, nonstructural phosphoprotein NSP5, we constructed a reassortant strain (SACC11) in the SA11 background that harbours a heterologous segment 11 encoding a variant protein (h-NSP5 ...
Chnaiderman, J, Barro, M, Spencer, E
openaire   +4 more sources

A VSV-based assay quantifies coronavirus Mpro/3CLpro/Nsp5 main protease activity and chemical inhibition

open access: yesCommunications Biology, 2022
A vesicular stomatitis virus (VSV)-based assay enables high-throughput screening for small molecular protease inhibitors that can block viral proteases, like the Mpro/3CLpro/Nsp5 in SARS-CoV-2.
Emmanuel Heilmann   +7 more
doaj   +1 more source

Exploration of Nirmatrelvir Derivatives as Optimized SARS‐CoV‐2 Antivirals

open access: yesChemMedChem, Volume 21, Issue 15, 14 August 2026.
Structure‐guided optimization of nirmatrelvir identifies aldehyde and dichloroacetamide warheads and a potency‐enhancing S4 thioamide. Crystal structures reveal an S2 rearrangement extending toward Cys44, suggesting a new covalent‐design opportunity.
Yugendar R. Alugubelli   +13 more
wiley   +1 more source

Feline Infectious Peritonitis Virus Nsp5 Inhibits Type I Interferon Production by Cleaving NEMO at Multiple Sites

open access: yesViruses, 2019
Feline infectious peritonitis (FIP), caused by virulent feline coronavirus, is the leading infectious cause of death in cats. The type I interferon (type I IFN)-mediated immune responses provide host protection from infectious diseases.
Si Chen   +8 more
doaj   +1 more source

Ferritinophagy Rewires Carnitine‐Dependent Lipid Metabolism to Inhibit PRRSV and IAV Replication

open access: yesAdvanced Science, Volume 13, Issue 45, 13 August 2026.
NCOA4‐mediated ferritinophagy reprograms carnitine metabolism by disrupting Fe‐S cluster biogenesis, thereby establishing an iron‐lipid axis that suppresses various viruses, including PRRSV and IAV. However, viruses counteract this mechanism by degrading NCOA4.
Kaifeng Guan   +7 more
wiley   +1 more source

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