{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,27]],"date-time":"2026-02-27T03:29:47Z","timestamp":1772162987646,"version":"3.50.1"},"reference-count":73,"publisher":"American Society for Microbiology","issue":"2","license":[{"start":{"date-parts":[[2019,1,15]],"date-time":"2019-01-15T00:00:00Z","timestamp":1547510400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/100000001","name":"National Science Foundation","doi-asserted-by":"publisher","award":["1810599"],"award-info":[{"award-number":["1810599"]}],"id":[{"id":"10.13039\/100000001","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000005","name":"U.S. Department of Defense","doi-asserted-by":"publisher","award":["PR172445"],"award-info":[{"award-number":["PR172445"]}],"id":[{"id":"10.13039\/100000005","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2019,1,15]]},"abstract":"<jats:p>\n                    <jats:named-content content-type=\"genus-species\">Chlamydia trachomatis<\/jats:named-content>\n                    is the leading cause of preventable infectious blindness and of bacterial sexually transmitted infections worldwide. Chlamydiae are developmentally regulated obligate intracellular pathogens that alternate between two functional and morphologic forms, with distinct repertoires of proteins. We hypothesize that protein degradation is a critical aspect to the developmental cycle. A key system involved in protein turnover in bacteria is the Clp protease system. Here, we characterized the two chlamydial ClpP paralogs by examining their expression in\n                    <jats:named-content content-type=\"genus-species\">Chlamydia<\/jats:named-content>\n                    spp., their ability to oligomerize, and their proteolytic activity. This work will help understand the evolutionarily diverse Clp proteases in the context of intracellular organisms, which may aid in the study of other clinically relevant intracellular bacteria.\n                  <\/jats:p>","DOI":"10.1128\/jb.00635-18","type":"journal-article","created":{"date-parts":[[2018,11,1]],"date-time":"2018-11-01T06:03:22Z","timestamp":1541052202000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":16,"title":["Initial Characterization of the Two ClpP Paralogs of\n                    <i>Chlamydia trachomatis<\/i>\n                    Suggests Unique Functionality for Each"],"prefix":"10.1128","volume":"201","author":[{"given":"Nicholas A.","family":"Wood","sequence":"first","affiliation":[{"name":"Department of Pathology and Microbiology, College of Medicine, University of Nebraska Medical Center, Omaha, Nebraska, USA"},{"name":"Division of Basic Biomedical Sciences, Sanford School of 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