{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,30]],"date-time":"2026-06-30T15:13:10Z","timestamp":1782832390721,"version":"3.54.5"},"reference-count":23,"publisher":"SAGE Publications","issue":"2","license":[{"start":{"date-parts":[[2016,3,1]],"date-time":"2016-03-01T00:00:00Z","timestamp":1456790400000},"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":["Microbial Drug Resistance"],"published-print":{"date-parts":[[2016,3]]},"abstract":"<jats:p>\n                    <jats:italic toggle=\"yes\">Serratia marcescens<\/jats:italic>\n                    IOMTU115 has a novel 6\u2032\n                    <jats:italic toggle=\"yes\">-N-<\/jats:italic>\n                    aminoglycoside acetyltransferase-encoding gene,\n                    <jats:italic toggle=\"yes\">aac(6<\/jats:italic>\n                    \u2032\n                    <jats:italic toggle=\"yes\">)-Ial<\/jats:italic>\n                    . The encoded protein AAC(6\u2032)-Ial has 146 amino acids, with 91.8% identity to the amino acid sequence of AAC(6\u2032)-Ic in\n                    <jats:italic toggle=\"yes\">S. marcescens<\/jats:italic>\n                    SM16 and 97.3% identity to the amino acid sequence of AAC(6\u2032)-Iap in\n                    <jats:italic toggle=\"yes\">S. marcescens<\/jats:italic>\n                    WW4. The minimum inhibitory concentrations of aminoglycosides for\n                    <jats:italic toggle=\"yes\">Escherichia coli<\/jats:italic>\n                    expressing AAC(6\u2032)-Ial were similar to those for\n                    <jats:italic toggle=\"yes\">E. coli<\/jats:italic>\n                    expressing AAC(6\u2032)-Ic or AAC(6\u2032)-Iap. Thin-layer chromatography showed that AAC(6\u2032)-Ial, AAC(6\u2032)-Ic, or AAC(6\u2032)-Iap acetylated all the aminoglycosides tested, except for apramycin, gentamicin, and lividomycin. Kinetics assays revealed that AAC(6\u2032)-Ial is a functional acetyltransferase against aminoglycosides. The\n                    <jats:italic toggle=\"yes\">aac(6\u2032)-Ial<\/jats:italic>\n                    gene was located on chromosomal DNA.\n                  <\/jats:p>","DOI":"10.1089\/mdr.2015.0126","type":"journal-article","created":{"date-parts":[[2015,8,13]],"date-time":"2015-08-13T10:33:11Z","timestamp":1439461991000},"page":"103-108","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":8,"title":["A Novel 6\u2032\n                    <i>-N-<\/i>\n                    Aminoglycoside Acetyltransferase, AAC(6\u2032)-Ial, from a Clinical Isolate of\n                    <i>Serratia marcescens<\/i>"],"prefix":"10.1177","volume":"22","author":[{"given":"Tatsuya","family":"Tada","sequence":"first","affiliation":[{"name":"Research Institute","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tohru","family":"Miyoshi-Akiyama","sequence":"additional","affiliation":[{"name":"Research Institute","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kayo","family":"Shimada","sequence":"additional","affiliation":[{"name":"Research Institute","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rajan K.","family":"Dahal","sequence":"additional","affiliation":[{"name":"Tribhuvan University","place":["Nepal"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shyam K.","family":"Mishra","sequence":"additional","affiliation":[{"name":"Tribhuvan University","place":["Nepal"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hiroshi","family":"Ohara","sequence":"additional","affiliation":[{"name":"National Center for Global Health and Medicine","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Teruo","family":"Kirikae","sequence":"additional","affiliation":[{"name":"Research Institute","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bharat M.","family":"Pokhrel","sequence":"additional","affiliation":[{"name":"Tribhuvan University","place":["Nepal"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"179","published-online":{"date-parts":[[2016,3]]},"reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1128\/AAC.48.2.491-496.2004","article-title":"Plasmid-mediated 16S rRNA methylase in Serratia marcescens conferring high-level resistance to aminoglycosides","volume":"48","author":"Doi Y.","year":"2004","unstructured":"Doi Y., , Yokoyama K., , Yamane K., , Wachino J., , Shibata N., , Yagi T., , Shibayama K., , Kato H., , and Arakawa Y. 2004. 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