2026-06-27T13:54:10Zhttps://docta.ucm.es/rest/oai/request

oai:docta.ucm.es:20.500.14352/1127232025-09-18T13:16:37Zcom_20.500.14352_14col_20.500.14352_15

López Díaz, María Carmen Culebras López, Esther Rodríguez-Avial Infante, Iciar Ríos Dueñas, Esther Viñuela Prieto, José Manuel Picazo De La Garza, Juan José Rodríguez-Avial López-Doriga, Carmen 2024-12-17T09:16:27Z 2024-12-17T09:16:27Z 2016 López-Diaz MDC, Culebras E, Rodríguez-Avial I, Rios E, Viñuela-Prieto JM, Picazo JJ, Rodríguez-Avial C. 2017. Plazomicin Activity against 346 Extended-Spectrum-β-Lactamase/AmpC-Producing Escherichia coli Urinary Isolates in Relation to Aminoglycoside-Modifying Enzymes. Antimicrob Agents Chemother 61:10.1128/aac.02454-16. https://doi.org/10.1128/aac.02454-16 0066-4804 10.1128/AAC.02454-16 https://hdl.handle.net/20.500.14352/112723 1098-6596 https://doi.org/10.1128/aac.02454-16 https://journals.asm.org/doi/10.1128/aac.02454-16 The activity of plazomicin and clinically relevant aminoglycosides was tested against 346 extended-spectrum-β-lactamase/AmpC-producing Escherichia coli urinary isolates, and the results were correlated with the presence of aminoglycoside-modifying enzymes (AMEs). Data showed that plazomicin was very active against all ESBL/AmpC-producing E. coli urinary isolates. Its activity was not related to the AME genes studied. spa restricted access Plazomicin activity against 346 extended-spectrum-beta-lactamase/AmpC producing Escherichia coli urinary isolates in relation to aminoglycoside-modifying enzymes journal article