{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,5]],"date-time":"2026-08-05T01:04:09Z","timestamp":1785891849360,"version":"3.56.0"},"reference-count":15,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2013,12,16]],"date-time":"2013-12-16T00:00:00Z","timestamp":1387152000000},"content-version":"vor","delay-in-days":15,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["CP Chemical Biology"],"published-print":{"date-parts":[[2013,12]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p>Penicillin\u2010binding proteins (PBPs) are membrane\u2010associated proteins involved in the biosynthesis of peptidoglycan (PG), the main component of bacterial cell walls. These proteins were discovered and named for their affinity to bind the \u03b2\u2010lactam antibiotic penicillin. The importance of the PBPs has long been appreciated; however, the apparent functional redundancy of the \u223c5 to 15 proteins that most bacteria possess makes determination of their individual roles difficult. Existing techniques to study PBPs are not ideal because they do not directly visualize protein activity and can suffer from artifacts. Therefore, development of new methods for studying the roles of distinct PBPs in cell wall synthesis was compulsory. Due to penicillin's covalent mode of inhibition, fluorophore\u2010conjugated analogs can be utilized to visualize PBP activity. Herein, we describe a general protocol to label and detect subsets of active PBPs in live, Gram\u2010positive bacteria using fluorescent \u03b2\u2010lactams. <jats:italic>Curr. Protoc. Chem. Biol<\/jats:italic>. 5:239\u2010250 \u00a9 2013 by John Wiley &amp; Sons, Inc.<\/jats:p>","DOI":"10.1002\/9780470559277.ch130102","type":"journal-article","created":{"date-parts":[[2013,12,16]],"date-time":"2013-12-16T16:58:27Z","timestamp":1387213107000},"page":"239-250","source":"Crossref","is-referenced-by-count":33,"title":["Penicillin\u2010Binding Protein Imaging Probes"],"prefix":"10.1002","volume":"5","author":[{"given":"Ozden","family":"Kocaoglu","sequence":"first","affiliation":[{"name":"Department of Molecular and Cellular Biochemistry Indiana University  Bloomington Indiana"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erin E.","family":"Carlson","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cellular Biochemistry Indiana University  Bloomington Indiana"},{"name":"Department of Chemistry Indiana University  Bloomington Indiana"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2013,12,16]]},"reference":[{"key":"e_1_2_8_2_1","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.38.5.973"},{"key":"e_1_2_8_3_1","doi-asserted-by":"publisher","DOI":"10.1021\/cr030102i"},{"key":"e_1_2_8_4_1","doi-asserted-by":"publisher","DOI":"10.1002\/0471142727.mb1002as97"},{"key":"e_1_2_8_5_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj2910019"},{"key":"e_1_2_8_6_1","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.18.1.148"},{"key":"e_1_2_8_7_1","doi-asserted-by":"publisher","DOI":"10.1021\/ar200067r"},{"key":"e_1_2_8_8_1","doi-asserted-by":"crossref","first-page":"4856","DOI":"10.1016\/S0021-9258(17)30091-1","article-title":"Studies of the high molecular weight penicillin\u2010binding proteins of Bacillus subtilis","volume":"254","author":"Kleppe G.","year":"1979","journal-title":"J. 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