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However, shortly after the introduction of a new antibiotic, bacteria often develop resistance. The bacterial cell envelope is essential for cell viability and is the target of many of the most commonly used antibiotics, including \u03b2-lactam antibiotics. Resistance to \u03b2-lactams is often dependent upon \u03b2-lactamases. In\n                    <jats:named-content content-type=\"genus-species\">B. cereus<\/jats:named-content>\n                    ,\n                    <jats:named-content content-type=\"genus-species\">B. thuringiensis<\/jats:named-content>\n                    , and some\n                    <jats:named-content content-type=\"genus-species\">B. anthracis<\/jats:named-content>\n                    strains, the expression of some \u03b2-lactamases is inducible. This inducible \u03b2-lactamase expression is controlled by activation of an alternative \u03c3 factor called \u03c3\n                    <jats:sup>P<\/jats:sup>\n                    . Here, we show that \u03b2-lactam antibiotics induce \u03c3\n                    <jats:sup>P<\/jats:sup>\n                    activation by degradation of the anti-\u03c3 factor RsiP.\n                  <\/jats:p>","DOI":"10.1128\/msphere.00511-19","type":"journal-article","created":{"date-parts":[[2019,8,6]],"date-time":"2019-08-06T09:23:24Z","timestamp":1565083404000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":10,"title":["Activation of the Extracytoplasmic Function \u03c3 Factor \u03c3\n                    <sup>P<\/sup>\n                    by \u03b2-Lactams in Bacillus thuringiensis Requires the Site-2 Protease RasP"],"prefix":"10.1128","volume":"4","author":[{"given":"Theresa D.","family":"Ho","sequence":"first","affiliation":[{"name":"Department of Microbiology and Immunology, Carver College of Medicine, University of Iowa, Iowa City, Iowa, 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