Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation.
By B. Faustin, Lydia Lartigue, J. Bruey, F. Luciano, E. Sergienko, B. Bailly-maitre, N. Volkmann, D. Hanein, I. Rouiller, John Calvin Reed. Molecules and Cells, 2007
729 citations recorded by the source corpus.
Subfields: Molecular Biology, Physiology
View Paper: https://www.semanticscholar.org/paper/7f0946bf6fd43a20120ba9dd5c4b9e6247fcbb7d
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Citations in the corpus
- Inflammasomes in health and disease (2012, background): “NLRP1, like NOD2 and NLRP3, can sense muramyl dipeptide (MDP), a building block of the bacterial cell wall, suggesting possible cooperative roles of the different pattern recognition receptors in the sensing of and response to bacteri”
- Pyroptosis: host cell death and inflammation (2009, methodology): “NLRs that have encountered their signal undergo nucleotide-dependent oligomerization using their nucleotide-binding domai”
- The Inflammasome: A Caspase-1 Activation Platform Regulating Immune Responses and Disease Pathogenesis (2009, methodology): “The NLRP1 inflammasome is the only caspase-1-activating platform that has been reconstituted in vitro with purified protein”
- The pyroptosome: a supramolecular assembly of ASC dimers mediating inflammatory cell death via caspase-1 activation (2007, background): “activate specifically the IPAF inflammasome (reviewed in Mariathasan S(6)), whereas exposure to anthrax lethal toxin or MDP have been shown to activate the NALP1 inflammasome.(11,12) Interestingly, the cryopyrin inflammasome is activated by a broad range of signals including infection with intracell”
- Redox Regulation of NLRP3 Inflammasomes: ROS as Trigger or Effector? (2015, neutral): “Extensive studies in macrophages and in reconstituted systems have demonstrated that NLRP1 is sensitive to both bacterial cell wall component muramyl dipeptide (MDP) and Bacillus anthracis lethal toxin (19, 38).”
- The inflammasomes. (2010, positive): “NLRP1 contains a C-terminal extension that harbors a CARD domain, which can interact directly with procaspase-1 and bypass the requirement for ASC, although ASC inclusion in the complex augmented human NLRP1 inflammasome activity (Faustin et al., 2007).”
- Understanding the mechanism of IL-1β secretion (2011, background): “The NLRP1 inflammasome is activated by muramyl dipeptide (MDP) [29], and in mouse, NLRP1b-inflammasome is activated by Bacillus anthracis”
- Horror autoinflammaticus: the molecular pathophysiology of autoinflammatory disease (*). (2009, background): “Another domain of the NLRP3 protein is the ATP-binding cassette (nucleotide binding domain, NBD, or NACHT domain; Figure 1), which has now been confirmed as such both in a cell-free system (44) and in a number of other in vitro settings (45), and is the major locus of CAPS-associated mutations.”
- The inflammasomes: guardians of the body. (2009, background): “It is therefore possible that this CARD-containing region is able to activate caspase-1 in an ASC-independent manner, as was suggested for human NALP1 in vitro (26).”
- Function of Nod‐like receptors in microbial recognition and host defense (2009, background): “Intriguingly, the adapter molecule ASC was not required for caspase-1 activation, but its presence did enhance NLRP1-mediated caspase-1 activation in vitro (166).”
- Pyroptotic cell death defends against intracellular pathogens (2015, background): “Earlier reports indicated that human NLRP1 can detect muramyldipeptide (MDP) in vitro (75, 76), but it is unclear if this observation is physiologically relevant, as murine NLRP1 proteins do not detect MDP (68), and the relevance of MDP responses in vivo in humans has not been examined.”
- Mechanisms and functions of inflammasomes. (2014, background): “Second, each complex consumes ATP and may have a double-ringed wheel structure with 7-or 8-fold symmetry (Duncan et al., 2007; Faustin et al., 2007; Riedl and Salvesen, 2007).”