{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T13:17:51Z","timestamp":1792675071253,"version":"4.5.0"},"reference-count":63,"publisher":"American Association for the Advancement of Science (AAAS)","issue":"6435","funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["AI075039"],"award-info":[{"award-number":["AI075039"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["AI063302"],"award-info":[{"award-number":["AI063302"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["AI064285"],"award-info":[{"award-number":["AI064285"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000011","name":"Howard Hughes Medical Institute","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000011","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Science"],"published-print":{"date-parts":[[2019,4,5]]},"abstract":"<jats:title>Degradation triggers the alarm<\/jats:title>\n                  <jats:p>\n                    Inflammasomes are multiprotein complexes that orchestrate proinflammatory cytokine secretion and cell death. Proteases such as anthrax lethal factor can activate an inflammasome known as NLRP1B, but the mechanism for this activation has been unclear. Chui\n                    <jats:italic>et al.<\/jats:italic>\n                    used genome-wide knockout screens to show that proteolysis of NLRP1B by lethal factor induces proteasomal degradation of the amino-terminal domains of NLRP1B and eventual cell death. Sandstrom\n                    <jats:italic>et al.<\/jats:italic>\n                    found that degradation of the amino-terminal domains of NLRP1B resulted in the release of a carboxyl-terminal fragment that activates caspase-1. This process, called \u201cfunctional degradation,\u201d allows the immune system to detect pathogen-associated activities, much as it recognizes pathogen-associated antigens.\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\" issue=\"6435\" page=\"82\" related-article-type=\"in-this-issue\" vol=\"364\" xlink:href=\"10.1126\/science.aau1208\">82<\/jats:related-article>\n                    , 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.aau1330\">eaau1330<\/jats:related-article>\n                  <\/jats:p>","DOI":"10.1126\/science.aau1330","type":"journal-article","created":{"date-parts":[[2019,3,14]],"date-time":"2019-03-14T19:36:22Z","timestamp":1552592182000},"source":"Crossref","is-referenced-by-count":372,"title":["Functional degradation: A mechanism of NLRP1 inflammasome activation by diverse pathogen enzymes"],"prefix":"10.1126","volume":"364","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8629-9087","authenticated-orcid":true,"given":"Andrew","family":"Sandstrom","sequence":"first","affiliation":[{"name":"Division of Immunology and Pathogenesis, Department of Molecular &amp; Cell Biology, and Cancer Research Laboratory, University of California, Berkeley, CA, USA."},{"name":"Howard Hughes Medical Institute, University of California, Berkeley, CA, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patrick S.","family":"Mitchell","sequence":"additional","affiliation":[{"name":"Division of Immunology and Pathogenesis, Department of Molecular &amp; Cell Biology, and Cancer Research Laboratory, University of California, Berkeley, CA, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lisa","family":"Goers","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Harvard Medical School, Boston, MA, USA."},{"name":"Broad Institute of Harvard and MIT, Cambridge, MA, USA."},{"name":"Department of Medicine, Division of Infectious Diseases, Massachusetts General Hospital, Boston, MA, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9076-7517","authenticated-orcid":true,"given":"Edward W.","family":"Mu","sequence":"additional","affiliation":[{"name":"Division of Immunology and Pathogenesis, Department of Molecular &amp; 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