Publications by authors named "Seong Shil Park"

Article Synopsis
  • - SERTAD1 is identified as an adaptor protein that regulates the K63-linked polyubiquitination of NLRP3, playing a key role in inflammasome activation by interfering with the Cullin1 E3 ubiquitin ligase interaction.
  • - The interaction between SERTAD1 and NLRP3 increases following inflammasome activation and is essential for proper secretion of inflammatory cytokines IL-1β and IL-18, as well as the cleavage of gasdermin D.
  • - Mice lacking SERTAD1 exhibit less severe inflammation in response to certain conditions, and SERTAD1 expression is found to be elevated in patients with autoimmune diseases, highlighting its importance in NLRP3
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Rice bran, a by-product of rice milling, is abundant in bioactive molecules and is highly recognized for its health-promoting properties, particularly in improving metabolic conditions. Building on this knowledge, we aimed to optimize the extraction conditions to maximize the functional efficacy of rice bran extract (RBE) and further validate its impact on lipid metabolism. We found that the optimized RBE (ORBE) significantly suppressed high-fat diet-induced weight gain, hyperlipidemia, and hepatosteatosis in mouse models.

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The signaling pathways governing acetaminophen (APAP)-induced liver injury have been extensively studied. However, little is known about the ubiquitin-modifying enzymes needed for the regulation of APAP-induced liver injury. Here, we examined whether the Pellino3 protein, which has E3 ligase activity, is needed for APAP-induced liver injury and subsequently explored its molecular mechanism.

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