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The NLRP1 inflammasome: new mechanistic insights and unresolved mysteries

Open access
Mitchell, Patrick S, Sandstrom, Andrew, Vance, Russell E·2019·Current Opinion in Immunology

Abstract

Nucleotide-binding domain, leucine-rich repeat (NLR) proteins constitute a diverse class of innate immune sensors that detect pathogens or stress-associated stimuli in plants and animals. Some NLRs are activated upon direct binding to pathogen-derived ligands. In contrast, we focus here on a vertebrate NLR called NLRP1 that responds to the enzymatic activities of pathogen effectors. We discuss a newly proposed ‘functional degradation’ mechanism that explains activation and assembly of NLRP1 into an oligomeric complex called an inflammasome. We also discuss how NLRP1 is activated by non-pathogen-associated triggers such as the anti- cancer drug Val-boroPro, or by human disease-associated mutations. Finally, we discuss how research on NLRP1 has led to additional biological insights, including the unexpected discovery of a new CARD8 inflammasome.

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Metadata

Authors
Mitchell, P. S., Sandstrom, A., & Vance, R. E.
Venue
Current Opinion in Immunology
Publisher
Elsevier BV
Published
2019-10
Volume
60
Pages
37-45
ISSN
0952-7915 (ISSN-L)
OpenAlex
W2945675033
Cited by
179
References
5
FWCI
1.67
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: The NLRP1 inflammasome: new mechanistic insights and unresolved mysteries. https://app.cochat.ai/papers/10.1016/j.coi.2019.04.015
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Mitchell, P. S., Sandstrom, A., & Vance, R. E. (2019). The NLRP1 inflammasome: new mechanistic insights and unresolved mysteries. Current Opinion in Immunology. https://doi.org/10.1016/j.coi.2019.04.015

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.