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Large IL-1\u03b2 activating platforms, known as inflammasomes, can assemble in response to the detection of endogenous host and pathogen-associated danger molecules. Formation of these protein complexes results in the autocatalysis and activation of caspase-1, which processes precursor IL-1\u03b2 into its secreted biologically active form. Inflammasome and IL-1\u03b2 activity is required to efficiently control viral, bacterial and fungal pathogen infections. Conversely, excess IL-1\u03b2 activity contributes to human disease, and its inhibition has proved therapeutically beneficial in the treatment of a spectrum of serious, yet relatively rare, heritable inflammasomopathies. Recently, inflammasome function has been implicated in more common human conditions, such as gout, type II diabetes and cancer. This raises the possibility that anti-IL-1 therapeutics may have broader applications than anticipated previously, and may be utilized across diverse disease states that are linked insidiously through unwanted or heightened inflammasome activity.<\/jats:p>","DOI":"10.1111\/j.1365-2249.2011.04440.x","type":"journal-article","created":{"date-parts":[[2011,7,15]],"date-time":"2011-07-15T14:21:32Z","timestamp":1310739692000},"page":"1-15","source":"Crossref","is-referenced-by-count":351,"title":["The NLRP3 inflammasome in health and disease: the good, the bad and the ugly"],"prefix":"10.1093","volume":"166","author":[{"given":"P","family":"Menu","sequence":"first","affiliation":[{"name":"Department of Biochemistry, University of Lausanne, Epalinges, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J E","family":"Vince","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Lausanne, Epalinges, 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