{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,3]],"date-time":"2026-05-03T12:34:26Z","timestamp":1777811666409,"version":"3.51.4"},"reference-count":25,"publisher":"SAGE Publications","issue":"10","license":[{"start":{"date-parts":[[2013,8,19]],"date-time":"2013-08-19T00:00:00Z","timestamp":1376870400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.sagepub.com\/page\/policies\/text-and-data-mining-license"}],"content-domain":{"domain":["journals.sagepub.com"],"crossmark-restriction":true},"short-container-title":["J Dent Res"],"published-print":{"date-parts":[[2013,10]]},"abstract":"<jats:p>\n                    Enoxacin inhibits binding between the B-subunit of vacuolar H\n                    <jats:sup>+<\/jats:sup>\n                    -ATPase (V-ATPase) and microfilaments, and also between osteoclast formation and bone resorption in vitro. We hypothesized that a bisphosphonate derivative of enoxacin, bis-enoxacin (BE), which was previously studied as a bone-directed antibiotic, might have similar activities. BE shared a number of characteristics with enoxacin: It blocked binding between the recombinant B-subunit and microfilaments and inhibited osteoclastogenesis in cell culture with IC\n                    <jats:sub>50<\/jats:sub>\n                    s of about 10 \u00b5M in each case. BE did not alter the relative expression levels of various osteoclast-specific proteins. Even though tartrate-resistant acid phosphatase 5b was expressed, proteolytic activation of the latent pro-enzyme was inhibited. However, unlike enoxacin, BE stimulated caspase-3 activity. BE bound to bone slices and inhibited bone resorption by osteoclasts on BE-coated bone slices in cell culture. BE reduced the amount of orthodontic tooth movement achieved in rats after 28 days. Analysis of these data suggests that BE is a novel anti-resorptive molecule that is active both in vitro and in vivo and may have clinical uses. Abbreviations: BE, bis-enoxacin; V-ATPase, vacuolar H\n                    <jats:sup>+<\/jats:sup>\n                    -ATPase; TRAP, tartrate-resistant acid phosphatase; \u03b1MEM D10, minimal essential media, alpha modification with 10% fetal bovine serum; SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoresis; RANKL, receptor activator of nuclear factor kappa B-ligand; NFATc1, nuclear factor of activated T-cells; ADAM, a disintegrin and metalloprotease domain; OTM, orthodontic tooth movement.\n                  <\/jats:p>","DOI":"10.1177\/0022034513501876","type":"journal-article","created":{"date-parts":[[2013,8,20]],"date-time":"2013-08-20T01:06:19Z","timestamp":1376960779000},"page":"925-931","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":23,"title":["Bis-enoxacin Inhibits Bone Resorption and Orthodontic Tooth Movement"],"prefix":"10.1177","volume":"92","author":[{"given":"E.J.","family":"Toro","sequence":"first","affiliation":[{"name":"Department of Orthodontics, University of Florida College of Dentistry, Gainesville, FL 32610, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J.","family":"Zuo","sequence":"additional","affiliation":[{"name":"Department of Orthodontics, University of Florida College of Dentistry, Gainesville, FL 32610, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A.","family":"Guiterrez","sequence":"additional","affiliation":[{"name":"Department of Orthodontics, University of Florida College of Dentistry, Gainesville, FL 32610, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R.L.","family":"La Rosa","sequence":"additional","affiliation":[{"name":"Department of Orthodontics, University of Florida College of Dentistry, Gainesville, FL 32610, 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