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Once they recognize pathogen-associated molecular patterns, they assemble into signaling complexes called inflammasomes, which induce proinflammatory cytokines and pyroptotic cell death. Although rodent NLR family pyrin domain containing 1 (NLRP1) can recognize bacterial toxins and protozoan pathogens, the ligands for human NLRP1 have remained elusive. Robinson\n                    <jats:italic>et al.<\/jats:italic>\n                    found that human NLRP1 senses and is activated by enteroviruses. During human rhinovirus (HRV) infection, the HRV 3C protease cleaves an autoinhibitory N-terminal fragment from NLRP1, which is subsequently degraded. The NLRP1 C-terminal fragment that is released then initiates inflammasome formation. This work offers insights into immune sensing of respiratory viral infections and provides an example of the N-terminal glycine degron pathway in human innate immunity.\n                  <\/jats:p>\n                  <jats:p>\n                    <jats:italic>Science<\/jats:italic>\n                    , this issue p.\n                    <jats:related-article xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"doi\" related-article-type=\"in-this-issue\" xlink:href=\"10.1126\/science.aay2002\">eaay2002<\/jats:related-article>\n                  <\/jats:p>","DOI":"10.1126\/science.aay2002","type":"journal-article","created":{"date-parts":[[2020,10,22]],"date-time":"2020-10-22T19:11:15Z","timestamp":1603393875000},"source":"Crossref","is-referenced-by-count":240,"title":["Enteroviral 3C protease activates the human NLRP1 inflammasome in airway 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