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• W3008240066 abstract "African swine fever virus, a large and complex icosahedral DNA virus, causes a deadly infection in domestic pigs. In addition to Africa and Europe, countries in Asia, including China, Vietnam, and Mongolia, were negatively affected by the hazards posed by ASFV outbreaks in 2018 and 2019, at which time more than 30 million pigs were culled. Until now, there has been no vaccine for protection against ASFV infection or effective treatments to cure ASF. Here, we solved the high-resolution crystal structure of the ASFV pS273R protease. The pS273R protease has a two-domain structure that distinguishes it from other members of the SUMO protease family, while the unique “arm domain” has been proven to be essential for its hydrolytic activity. Moreover, the peptidomimetic aldehyde compounds designed to target the substrate binding pocket exert prominent inhibitory effects and can thus be used in a potential lead for anti-ASFV drug development." @default.
• W3008240066 created "2020-03-06" @default.
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• W3008240066 date "2020-05-04" @default.
• W3008240066 modified "2023-10-16" @default.
• W3008240066 title "Crystal Structure of African Swine Fever Virus pS273R Protease and Implications for Inhibitor Design" @default.
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• W3008240066 doi "https://doi.org/10.1128/jvi.02125-19" @default.
• W3008240066 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7199414" @default.
• W3008240066 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/32075933" @default.

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