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- W1919531331 endingPage "598" @default.
- W1919531331 startingPage "589" @default.
- W1919531331 abstract "The innate immune system of mammals encodes several families of immune detector proteins that monitor the cytosol for signs of pathogen invasion. One important but poorly understood family of cytosolic immunosurveillance proteins is the NLR (nucleotide-binding domain, leucine-rich repeat containing) proteins. Recent work has demonstrated that one subfamily of NLRs, the NAIPs (NLR family, apoptosis inhibitory proteins), are activated by specific interaction with bacterial ligands, such as flagellin. NAIP activation leads to assembly of a large multiprotein complex called the inflammasome, which initiates innate immune responses by activation of the Caspase-1 protease. NAIPs therefore appear to detect pathogen molecules via a simple and direct receptor-ligand mechanism. Interestingly, other NLR family members appear to detect pathogens indirectly, perhaps by responding to host cell “stress” caused by the pathogen. Thus, the NLR family may have evolved surprisingly diverse mechanisms for detecting pathogens." @default.
- W1919531331 created "2016-06-24" @default.
- W1919531331 creator A5034080122 @default.
- W1919531331 creator A5061473047 @default.
- W1919531331 date "2012-04-19" @default.
- W1919531331 modified "2023-10-17" @default.
- W1919531331 title "NAIPs: Building an innate immune barrier against bacterial pathogens" @default.
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