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Updated: Jul 11, 2025

Activation and Measurement of NLRP3 Inflammasome Activity Using IL-1β in Human Monocyte-derived Dendritic Cells
Published on: May 22, 2014
Oxidized thioredoxin 1 places a leash on NLRP1 inflammasome activity
Jeremy Ky Yap1, Stefan Emming1, Kate Schroder1
1Centre for Cell Biology of Chronic Disease, Institute for Molecular Bioscience, The University of Queensland, St Lucia, QLD, Australia.
Abstract:
The biology of the NACHT domain and leucine-rich repeat (NLR) and pyrin domain-containing 1 (NLRP1) inflammasome has perplexed researchers since this inflammasome was first described about two decades ago. The identification of oxidized thioredoxin 1 (TRX1) as a suppressor of NLRP1 recently linked cellular redox homeostasis to NLRP1 inflammasome signaling. Now, Zhang et al. present a molecular structure of TRX1-bound NLRP1 with unprecedented detail. This structure gives key insight into regulatory mechanisms governing NLRP1 activation and offers enormous potential for structure-based anti-inflammatory drug design.
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