| http://purl.uniprot.org/citations/37537169 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/37537169 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/37537169 | http://www.w3.org/2000/01/rdf-schema#comment | "Aminoglycosides are a class of antibiotics that bind to ribosomal RNA and exert pleiotropic effects on ribosome function. Amikacin, the semisynthetic derivative of kanamycin, is commonly used for treating severe infections with multidrug-resistant, aerobic Gram-negative bacteria. Amikacin carries the 4-amino-2-hydroxy butyrate (AHB) moiety at the N1 amino group of the central 2-deoxystreptamine (2-DOS) ring, which may confer amikacin a unique ribosome inhibition profile. Here we use in vitro fast kinetics combined with X-ray crystallography and cryo-EM to dissect the mechanisms of ribosome inhibition by amikacin and the parent compound, kanamycin. Amikacin interferes with tRNA translocation, release factor-mediated peptidyl-tRNA hydrolysis, and ribosome recycling, traits attributed to the additional interactions amikacin makes with the decoding center. The binding site in the large ribosomal subunit proximal to the 3'-end of tRNA in the peptidyl (P) site lays the groundwork for rational design of amikacin derivatives with improved antibacterial properties."xsd:string |
| http://purl.uniprot.org/citations/37537169 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41467-023-40416-5"xsd:string |
| http://purl.uniprot.org/citations/37537169 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41467-023-40416-5"xsd:string |
| http://purl.uniprot.org/citations/37537169 | http://purl.uniprot.org/core/author | "Ge X."xsd:string |
| http://purl.uniprot.org/citations/37537169 | http://purl.uniprot.org/core/author | "Ge X."xsd:string |
| http://purl.uniprot.org/citations/37537169 | http://purl.uniprot.org/core/author | "Gagnon M.G."xsd:string |
| http://purl.uniprot.org/citations/37537169 | http://purl.uniprot.org/core/author | "Gagnon M.G."xsd:string |
| http://purl.uniprot.org/citations/37537169 | http://purl.uniprot.org/core/author | "Sanyal S."xsd:string |
| http://purl.uniprot.org/citations/37537169 | http://purl.uniprot.org/core/author | "Sanyal S."xsd:string |
| http://purl.uniprot.org/citations/37537169 | http://purl.uniprot.org/core/author | "De Tarafder A."xsd:string |
| http://purl.uniprot.org/citations/37537169 | http://purl.uniprot.org/core/author | "De Tarafder A."xsd:string |
| http://purl.uniprot.org/citations/37537169 | http://purl.uniprot.org/core/author | "Parajuli N.P."xsd:string |
| http://purl.uniprot.org/citations/37537169 | http://purl.uniprot.org/core/author | "Parajuli N.P."xsd:string |
| http://purl.uniprot.org/citations/37537169 | http://purl.uniprot.org/core/author | "Seely S.M."xsd:string |
| http://purl.uniprot.org/citations/37537169 | http://purl.uniprot.org/core/author | "Seely S.M."xsd:string |
| http://purl.uniprot.org/citations/37537169 | http://purl.uniprot.org/core/date | "2023"xsd:gYear |
| http://purl.uniprot.org/citations/37537169 | http://purl.uniprot.org/core/date | "2023"xsd:gYear |
| http://purl.uniprot.org/citations/37537169 | http://purl.uniprot.org/core/name | "Nat. Commun."xsd:string |
| http://purl.uniprot.org/citations/37537169 | http://purl.uniprot.org/core/name | "Nat Commun"xsd:string |
| http://purl.uniprot.org/citations/37537169 | http://purl.uniprot.org/core/pages | "4666"xsd:string |
| http://purl.uniprot.org/citations/37537169 | http://purl.uniprot.org/core/pages | "4666"xsd:string |
| http://purl.uniprot.org/citations/37537169 | http://purl.uniprot.org/core/title | "Molecular basis of the pleiotropic effects by the antibiotic amikacin on the ribosome."xsd:string |
| http://purl.uniprot.org/citations/37537169 | http://purl.uniprot.org/core/title | "Molecular basis of the pleiotropic effects by the antibiotic amikacin on the ribosome."xsd:string |