{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T23:17:12Z","timestamp":1785453432733,"version":"3.56.0"},"reference-count":65,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,7,1]],"date-time":"2025-07-01T00:00:00Z","timestamp":1751328000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,7,1]],"date-time":"2025-07-01T00:00:00Z","timestamp":1751328000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,7,1]],"date-time":"2025-07-01T00:00:00Z","timestamp":1751328000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,7,1]],"date-time":"2025-07-01T00:00:00Z","timestamp":1751328000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,7,1]],"date-time":"2025-07-01T00:00:00Z","timestamp":1751328000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,7,1]],"date-time":"2025-07-01T00:00:00Z","timestamp":1751328000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,7,1]],"date-time":"2025-07-01T00:00:00Z","timestamp":1751328000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100011260","name":"FP7 Research infrastructures","doi-asserted-by":"publisher","award":["315997"],"award-info":[{"award-number":["315997"]}],"id":[{"id":"10.13039\/100011260","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100007675","name":"International Center for Genetic Engineering and Biotechnology","doi-asserted-by":"publisher","award":["CRP\/CRO08-02"],"award-info":[{"award-number":["CRP\/CRO08-02"]}],"id":[{"id":"10.13039\/100007675","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100011102","name":"Seventh Framework Programme","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100011102","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001688","name":"International Centre for Genetic Engineering and Biotechnology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001688","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100006588","name":"Republic of Croatia Ministry of Science and Education","doi-asserted-by":"publisher","award":["006-0982913-1219"],"award-info":[{"award-number":["006-0982913-1219"]}],"id":[{"id":"10.13039\/501100006588","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Archives of Biochemistry and Biophysics"],"published-print":{"date-parts":[[2025,7]]},"DOI":"10.1016\/j.abb.2025.110422","type":"journal-article","created":{"date-parts":[[2025,4,11]],"date-time":"2025-04-11T04:42:31Z","timestamp":1744346551000},"page":"110422","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":2,"special_numbering":"C","title":["Methylation of immature small ribosomal subunits by methyltransferases conferring aminoglycoside resistance"],"prefix":"10.1016","volume":"769","author":[{"given":"Marko","family":"Mo\u010dibob","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sonja","family":"Obrani\u0107","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Domagoj","family":"Kifer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jasmina","family":"Rokov-Plavec","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0253-4028","authenticated-orcid":false,"given":"Gordana","family":"Maravi\u0107-Vlahovi\u010dek","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.abb.2025.110422_bib1","series-title":"Critically Important Antimicrobials for Human Medicine","year":"2019"},{"key":"10.1016\/j.abb.2025.110422_bib2","first-page":"597","article-title":"Aminoglycosides--50 years on","volume":"39","author":"Begg","year":"1995","journal-title":"Br. J. Clin. Pharmacol."},{"key":"10.1016\/j.abb.2025.110422_bib3","doi-asserted-by":"crossref","first-page":"3249","DOI":"10.1128\/AAC.44.12.3249-3256.2000","article-title":"Aminoglycosides: perspectives on mechanisms of action and resistance and strategies to counter resistance","volume":"44","author":"Kotra","year":"2000","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.abb.2025.110422_bib4","doi-asserted-by":"crossref","first-page":"485","DOI":"10.7164\/antibiotics.24.485","article-title":"3\u2019,4\u2019-dideoxy-kanamycin B active against kanamycin-resistant Escherichia coli and Pseudomonas aeruginosa","volume":"24","author":"Umezawa","year":"1971","journal-title":"J. Antibiot. (Tokyo)"},{"key":"10.1016\/j.abb.2025.110422_bib5","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1016\/j.mib.2010.09.004","article-title":"Combating evolution with intelligent design: the neoglycoside ACHN-490","volume":"13","author":"Armstrong","year":"2010","journal-title":"Curr. Opin. Microbiol."},{"key":"10.1016\/j.abb.2025.110422_bib6","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a027029","article-title":"Aminoglycosides: an overview","volume":"6","author":"Krause","year":"2016","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"10.1016\/j.abb.2025.110422_bib7","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1016\/0022-2836(87)90349-4","article-title":"Sites of action of two ribosomal RNA methylases responsible for resistance to aminoglycosides","volume":"193","author":"Beauclerk","year":"1987","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.abb.2025.110422_bib8","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/0378-1119(91)90103-I","article-title":"Cloning and characterization of gentamicin-resistance genes from Micromonospora purpurea and Micromonospora rosea","volume":"98","author":"Kelemen","year":"1991","journal-title":"Gene"},{"key":"10.1016\/j.abb.2025.110422_bib9","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/0378-1119(93)90617-C","article-title":"Analysis of the self-defense gene (fmrO) of a fortimicin A (astromicin) producer, Micromonospora olivasterospora: comparison with other aminoglycoside-resistance-encoding genes","volume":"127","author":"Toshio","year":"1993","journal-title":"Gene"},{"key":"10.1016\/j.abb.2025.110422_bib10","first-page":"915","article-title":"Cloning of aminoglycoside-resistance determinants from Streptomyces tenebrarius and comparison with related genes from other actinomycetes","volume":"133","author":"Skeggs","year":"1987","journal-title":"J. Gen. Microbiol."},{"key":"10.1016\/j.abb.2025.110422_bib11","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1016\/j.jmb.2005.09.056","article-title":"Analysis of conformational changes in 16 S rRNA during the course of 30 S subunit assembly","volume":"354","author":"Holmes","year":"2005","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.abb.2025.110422_bib12","doi-asserted-by":"crossref","first-page":"2565","DOI":"10.1128\/AAC.47.8.2565-2571.2003","article-title":"Plasmid-mediated high-level resistance to aminoglycosides in Enterobacteriaceae due to 16S rRNA methylation","volume":"47","author":"Galimand","year":"2003","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.abb.2025.110422_bib13","doi-asserted-by":"crossref","first-page":"1888","DOI":"10.1016\/S0140-6736(03)14959-8","article-title":"Acquisition of 16S rRNA methylase gene in Pseudomonas aeruginosa","volume":"362","author":"Yokoyama","year":"2003","journal-title":"Lancet Lond. Engl."},{"key":"10.1016\/j.abb.2025.110422_bib14","doi-asserted-by":"crossref","first-page":"2397","DOI":"10.1128\/AAC.02108-12","article-title":"Coproduction of 16S rRNA methyltransferase RmtD or RmtG with KPC-2 and CTX-M group extended-spectrum \u03b2lactamases in Klebsiella pneumoniae","volume":"57","author":"Bueno","year":"2013","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.abb.2025.110422_bib15","doi-asserted-by":"crossref","first-page":"2666","DOI":"10.1128\/AAC.01743-09","article-title":"Discovery of a gene conferring multiple-aminoglycoside resistance in Escherichia coli","volume":"54","author":"Davis","year":"2010","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.abb.2025.110422_bib16","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","year":"2004","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.abb.2025.110422_bib17","doi-asserted-by":"crossref","first-page":"852","DOI":"10.1128\/AAC.01345-06","article-title":"Coproduction of novel 16S rRNA methylase RmtD and metallo-\u03b2-lactamase SPM-1 in a panresistant Pseudomonas aeruginosa isolate from Brazil","volume":"51","author":"Doi","year":"2007","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.abb.2025.110422_bib18","doi-asserted-by":"crossref","first-page":"3960","DOI":"10.1128\/AAC.00660-12","article-title":"RmtF, a new member of the aminoglycoside resistance 16S rRNA N7 G1405 methyltransferase family","volume":"56","author":"Galimand","year":"2012","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.abb.2025.110422_bib19","doi-asserted-by":"crossref","first-page":"2413","DOI":"10.1128\/AAC.00266-13","article-title":"Novel 16S rRNA methyltransferase RmtH produced by Klebsiella pneumoniae associated with war-related trauma, Antimicrob","volume":"57","author":"O'Hara","year":"2013","journal-title":"Agents Chemother."},{"key":"10.1016\/j.abb.2025.110422_bib20","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1111\/j.1574-6968.2010.02068.x","article-title":"RmtC introduces G1405 methylation in 16S rRNA and confers high-level aminoglycoside resistance on Gram-positive microorganisms","volume":"311","author":"Wachino","year":"2010","journal-title":"FEMS Microbiol. Lett."},{"key":"10.1016\/j.abb.2025.110422_bib21","doi-asserted-by":"crossref","first-page":"4401","DOI":"10.1128\/AAC.00926-07","article-title":"Novel plasmid-mediated 16S rRNA m1A1408 methyltransferase, NpmA, found in a clinically isolated Escherichia coli strain resistant to structurally diverse aminoglycosides","volume":"51","author":"Wachino","year":"2007","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.abb.2025.110422_bib22","doi-asserted-by":"crossref","DOI":"10.1099\/mgen.0.000946","article-title":"Global scenario of the RmtE pan- aminoglycoside- resistance mechanism: emergence of the rmtE4 gene in South America associated with a hospital- related IncL plasmid","volume":"9","author":"Delgado-Blas","year":"2023","journal-title":"Microb. GENOMICS"},{"key":"10.1016\/j.abb.2025.110422_bib23","doi-asserted-by":"crossref","first-page":"898","DOI":"10.1111\/jam.15615","article-title":"Novel amikacin resistance genes identified from human gut microbiota by functional metagenomics","volume":"133","author":"Wang","year":"2022","journal-title":"J. Appl. Microbiol."},{"key":"10.1016\/j.abb.2025.110422_bib24","doi-asserted-by":"crossref","DOI":"10.1128\/AAC.01009-21","article-title":"Functional and structural characterization of acquired 16S rRNA methyltransferase NpmB1 conferring pan-aminoglycoside resistance","volume":"65","author":"Kawai","year":"2021","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.abb.2025.110422_bib25","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijantimicag.2024.107089","article-title":"WarA, a remote homolog of NpmA and KamB from Nocardia wallacei, confers broad spectrum aminoglycoside resistance in Nocardia and Mycobacteria","volume":"63","author":"Hershko","year":"2024","journal-title":"Int. J. Antimicrob. Agents"},{"key":"10.1016\/j.abb.2025.110422_bib26","doi-asserted-by":"crossref","first-page":"2306","DOI":"10.1093\/jac\/dkad236","article-title":"Phenotypic and genotypic analysis of antimicrobial resistance in Nocardia species","volume":"78","author":"Hershko","year":"2023","journal-title":"J. Antimicrob. Chemother."},{"key":"10.1016\/j.abb.2025.110422_bib27","article-title":"NpmC, a novel A1408 16S rRNA methyltransferase in the gut of humans and animals","author":"Matamoros","year":"2024","journal-title":"Int. J. Antimicrob. Agents"},{"key":"10.1016\/j.abb.2025.110422_bib28","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1016\/j.cbpa.2008.09.024","article-title":"RNA folding and ribosome assembly","volume":"12","author":"Woodson","year":"2008","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.abb.2025.110422_bib29","doi-asserted-by":"crossref","first-page":"1312","DOI":"10.1021\/ar2000474","article-title":"RNA folding pathways and the self-assembly of ribosomes","volume":"44","author":"Woodson","year":"2011","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.abb.2025.110422_bib30","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1016\/j.tibs.2009.01.011","article-title":"Deconstructing ribosome construction","volume":"34","author":"Connolly","year":"2009","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.abb.2025.110422_bib31","doi-asserted-by":"crossref","first-page":"747","DOI":"10.3390\/microorganisms10040747","article-title":"Protein assistants of small ribosomal subunit biogenesis in bacteria","volume":"10","author":"Maksimova","year":"2022","journal-title":"Microorganisms"},{"key":"10.1016\/j.abb.2025.110422_bib32","doi-asserted-by":"crossref","first-page":"4567","DOI":"10.1128\/jb.179.14.4567-4574.1997","article-title":"A novel ribosome-associated protein is important for efficient translation in Escherichia coli","volume":"179","author":"Bylund","year":"1997","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.abb.2025.110422_bib33","doi-asserted-by":"crossref","first-page":"2609","DOI":"10.1093\/nar\/gks1256","article-title":"Dissecting the in vivo assembly of the 30S ribosomal subunit reveals the role of RimM and general features of the assembly process","volume":"41","author":"Guo","year":"2013","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.abb.2025.110422_bib34","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1016\/j.molcel.2013.09.020","article-title":"In vivo X-ray footprinting of pre-30S ribosomes reveals chaperone-dependent remodeling of late assembly intermediates","volume":"52","author":"Clatterbuck Soper","year":"2013","journal-title":"Mol. Cell"},{"key":"10.1016\/j.abb.2025.110422_bib35","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1016\/S0022-2836(03)00061-5","article-title":"Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock adaptation protein from Escherichia coli","volume":"327","author":"Huang","year":"2003","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.abb.2025.110422_bib36","doi-asserted-by":"crossref","first-page":"789","DOI":"10.1261\/rna.037523.112","article-title":"Escherichia coli rimM and yjeQ null strains accumulate immature 30S subunits of similar structure and protein complement","volume":"19","author":"Leong","year":"2013","journal-title":"RNA"},{"key":"10.1016\/j.abb.2025.110422_bib37","doi-asserted-by":"crossref","first-page":"11109","DOI":"10.1021\/bi020355q","article-title":"YjeQ, an essential, conserved, uncharacterized protein from Escherichia coli, is an unusual GTPase with circularly permuted G-motifs and marked burst kinetics","volume":"41","author":"Daigle","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.abb.2025.110422_bib38","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1038\/nbt0998-851","article-title":"A genome-based approach for the identification of essential bacterial genes","volume":"16","author":"Arigoni","year":"1998","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.abb.2025.110422_bib39","doi-asserted-by":"crossref","first-page":"5303","DOI":"10.1093\/nar\/gkh861","article-title":"A novel GTPase activated by the small subunit of ribosome","volume":"32","author":"Himeno","year":"2004","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.abb.2025.110422_bib40","doi-asserted-by":"crossref","first-page":"E3396","DOI":"10.1073\/pnas.1618016114","article-title":"The cryo-EM structure of YjeQ bound to the 30S subunit suggests a fidelity checkpoint function for this protein in ribosome assembly","volume":"114","author":"Razi","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.abb.2025.110422_bib41","doi-asserted-by":"crossref","first-page":"6945","DOI":"10.1093\/nar\/gkx324","article-title":"RsgA couples the maturation state of the 30S ribosomal decoding center to activation of its GTPase pocket","volume":"45","author":"L\u00f3pez-Alonso","year":"2017","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.abb.2025.110422_bib42","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1038\/emboj.2010.291","article-title":"RsgA releases RbfA from 30S ribosome during a late stage of ribosome biosynthesis","volume":"30","author":"Goto","year":"2011","journal-title":"EMBO J."},{"key":"10.1016\/j.abb.2025.110422_bib43","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.abf7547","article-title":"A conserved rRNA switch is central to decoding site maturation on the small ribosomal subunit","volume":"7","author":"Schedlbauer","year":"2021","journal-title":"Sci. Adv."},{"key":"10.1016\/j.abb.2025.110422_bib44","doi-asserted-by":"crossref","first-page":"1468","DOI":"10.1038\/s41594-023-01078-5","article-title":"KsgA facilitates ribosomal small subunit maturation by proofreading a key structural lesion","volume":"30","author":"Sun","year":"2023","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.abb.2025.110422_bib45","doi-asserted-by":"crossref","first-page":"358","DOI":"10.1016\/j.jmb.2006.03.038","article-title":"Aminoglycoside resistance by ArmA-mediated ribosomal 16 S methylation in human bacterial pathogens","volume":"359","author":"Liou","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.abb.2025.110422_bib46","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1016\/S0092-8674(00)00084-2","article-title":"Structure of functionally activated small ribosomal subunit at 3.3 angstroms resolution","volume":"102","author":"Schluenzen","year":"2000","journal-title":"Cell"},{"key":"10.1016\/j.abb.2025.110422_bib47","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1126\/science.1060089","article-title":"Crystal structure of the ribosome at 5.5 A resolution","volume":"292","author":"Yusupov","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.abb.2025.110422_bib48","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1016\/S0092-8674(00)80690-X","article-title":"Solution structure of the E. coli 70S ribosome at 11.5 A resolution","volume":"100","author":"Gabashvili","year":"2000","journal-title":"Cell"},{"key":"10.1016\/j.abb.2025.110422_bib49","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1261\/rna.2314311","article-title":"The aminoglycoside resistance methyltransferases from the ArmA\/Rmt family operate late in the 30S ribosomal biogenesis pathway","volume":"17","author":"Zarubica","year":"2011","journal-title":"RNA"},{"key":"10.1016\/j.abb.2025.110422_bib50","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1128\/AAC.50.1.178-184.2006","article-title":"Novel plasmid-mediated 16S rRNA methylase, RmtC, found in a Proteus mirabilis isolate demonstrating extraordinary high-level resistance against various aminoglycosides","volume":"50","author":"Wachino","year":"2006","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.abb.2025.110422_bib51","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1128\/AAC.02482-15","article-title":"Heterologous expression and functional characterization of the exogenously acquired aminoglycoside resistance methyltransferases RmtD, RmtD2, and RmtG","volume":"60","author":"Corr\u00eaa","year":"2016","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.abb.2025.110422_bib52","doi-asserted-by":"crossref","first-page":"1903","DOI":"10.1093\/nar\/gkq1033","article-title":"Structural basis for the methylation of A1408 in 16S rRNA by a panaminoglycoside resistance methyltransferase NpmA from a clinical isolate and analysis of the NpmA interactions with the 30S ribosomal subunit","volume":"39","author":"Husain","year":"2011","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.abb.2025.110422_bib53","doi-asserted-by":"crossref","first-page":"4120","DOI":"10.1093\/nar\/gkq122","article-title":"Structural basis for the methylation of G1405 in 16s rRNA by aminoglycoside resistance methyltransferase Sgm from an antibiotic producer: a diversity of active sites in m7G methyltransferases","volume":"38","author":"Husain","year":"2010","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.abb.2025.110422_bib54","doi-asserted-by":"crossref","first-page":"2807","DOI":"10.1128\/AAC.00056-15","article-title":"30S Subunit-dependent activation of the Sorangium cellulosum So ce56 aminoglycoside resistance-conferring 16S rRNA methyltransferase Kmr","volume":"59","author":"Savi\u0107","year":"2015","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.abb.2025.110422_bib55","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1007\/s13238-014-0044-1","article-title":"Structural insights into the assembly of the 30S ribosomal subunit in vivo: functional role of S5 and location of the 17S rRNA precursor sequence","volume":"5","author":"Yang","year":"2014","journal-title":"Protein Cell"},{"key":"10.1016\/j.abb.2025.110422_bib56","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1261\/rna.2509811","article-title":"Understanding ribosome assembly: the structure of in vivo assembled immature 30S subunits revealed by cryo-electron microscopy","volume":"17","author":"Jomaa","year":"2011","journal-title":"RNA"},{"key":"10.1016\/j.abb.2025.110422_bib57","doi-asserted-by":"crossref","first-page":"6140","DOI":"10.3390\/ijms22116140","article-title":"RbfA is involved in two important stages of 30S subunit assembly: formation of the central pseudoknot and docking of helix 44 to the decoding center","volume":"22","author":"Maksimova","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.abb.2025.110422_bib58","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1016\/j.bbapap.2007.09.009","article-title":"Modeling and experimental analyses reveal a two-domain structure and amino acids important for the activity of aminoglycoside resistance methyltransferase Sgm","volume":"1784","author":"Vlahovi\u010dek","year":"2008","journal-title":"Biochim. Biophys. Acta, Proteins Proteomics"},{"key":"10.1016\/j.abb.2025.110422_bib59","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2024.137015","article-title":"Ribosomal A site binding pattern differs between Arm methyltransferases from clinical pathogens and a natural producer of aminoglycosides","volume":"282","author":"Obrani\u0107","year":"2024","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.abb.2025.110422_bib60","doi-asserted-by":"crossref","first-page":"e15","DOI":"10.1093\/nar\/gkn992","article-title":"A single-step method for purification of active His-tagged ribosomes from a genetically engineered Escherichia coli","volume":"37","author":"Ederth","year":"2009","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.abb.2025.110422_bib61","doi-asserted-by":"crossref","first-page":"2006.0008","DOI":"10.1038\/msb4100050","article-title":"Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection","volume":"2","author":"Baba","year":"2006","journal-title":"Mol. Syst. Biol."},{"key":"10.1016\/j.abb.2025.110422_bib62","doi-asserted-by":"crossref","first-page":"614","DOI":"10.1016\/j.str.2013.02.017","article-title":"Adaptation of aminoacyl-tRNA synthetase catalytic core to carrier protein aminoacylation","volume":"21","author":"Mo\u010dibob","year":"2013","journal-title":"Structure"},{"key":"10.1016\/j.abb.2025.110422_bib63","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1111\/j.1432-1033.1985.tb08704.x","article-title":"Specific fragmentation of tRNA and rRNA at a 7-methylguanine residue in the presence of methylated carrier RNA","volume":"146","author":"Zueva","year":"1985","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.abb.2025.110422_bib64","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1111\/j.1432-1033.1983.tb07258.x","article-title":"Comparison of Escherichia coli tRNAPhe in the free state, in the ternary complex and in the ribosomal A and P sites by chemical probing","volume":"131","author":"Douthwaite","year":"1983","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.abb.2025.110422_bib65","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/S0076-6879(88)64064-X","article-title":"Structural analysis of RNA using chemical and enzymatic probing monitored by primer extension","volume":"164","author":"Stern","year":"1988","journal-title":"Methods Enzymol."}],"container-title":["Archives of Biochemistry and Biophysics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0003986125001353?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0003986125001353?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,7]],"date-time":"2026-05-07T08:02:54Z","timestamp":1778140974000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0003986125001353"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,7]]},"references-count":65,"alternative-id":["S0003986125001353"],"URL":"https:\/\/doi.org\/10.1016\/j.abb.2025.110422","relation":{},"ISSN":["0003-9861"],"issn-type":[{"value":"0003-9861","type":"print"}],"subject":[],"published":{"date-parts":[[2025,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Methylation of immature small ribosomal subunits by methyltransferases conferring aminoglycoside resistance","name":"articletitle","label":"Article Title"},{"value":"Archives of Biochemistry and Biophysics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.abb.2025.110422","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"110422"}}