Publications by authors named "Anuradha De Silva"

Article Synopsis
  • Numerous viruses carry deubiquitinating proteases in their genomes, which play a role in evading the host's immune response by cleaving ubiquitin chains from immune-related substrates.* -
  • Ubiquitination is a critical cellular process involved in signaling and immune response, and viral proteins can interfere with this process, impacting the effectiveness of antiviral defenses.* -
  • The review highlights potential drug targets within viral proteases, focusing on the development of small molecule inhibitors to block these enzymes and their functions.*
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Deubiquitination of cellular substrates by viral proteases is a mechanism used to interfere with host cellular signaling processes, shared between members of the coronavirus- and arterivirus families. In the case of Arteriviruses, deubiquitinating and polyprotein processing activities are accomplished by the virus-encoded papain-like protease 2 (PLP2). Several studies have implicated the deubiquitinating activity of the porcine reproductive and respiratory syndrome virus (PRRSV) PLP2 in the downregulation of cellular interferon production, however to date, the only arterivirus PLP2 structure described is that of equine arteritis virus (EAV), a distantly related virus.

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Introduction: Dopamine (DA) binds to five receptors (DAR), classified by their ability to increase (D1R-like) or decrease (D2R-like) cAMP. In humans, most DA circulates as dopamine sulfate (DA-S), which can be de-conjugated to bioactive DA by arylsulfatase A (ARSA). The objective was to examine expression of DAR and ARSA in human adipose tissue and determine whether DA regulates prolactin (PRL) and adipokine expression and release.

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