ReviewCommunications biology2026
Molecular mechanisms of NLR proteins in inflammasome activation.
Review in Communications biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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3 authors.
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Abstract
Nucleotide-binding domain and leucine-rich repeat-containing proteins (NLRs) are central mediators of inflammasome signaling, activating caspase-1 to drive pyroptotic cell death and pro-inflammatory responses. Although NLR activation is generally thought to involve conformational rearrangements that oligomerize their N- or C-terminal death domains to nucleate ASC or pro-caspase-1 oligomerization, the molecular mechanisms that enable these transitions vary substantially among family members. Here, we highlight recent structural advances that reveal how distinct NLRs are activated and assemble into higher-order signaling platforms, providing mechanistic insights into the diverse activation mechanisms that converge on a common inflammatory outcome.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.