Functionally critical residues in the aminoglycoside resistance-associated methyltransferase RmtC pl...
Functionally critical residues in the aminoglycoside resistance-associated methyltransferase RmtC play distinct roles in 30S substrate recognition
About this item
Full title
Author / Creator
Publisher
Cold Spring Harbor: Cold Spring Harbor Laboratory Press
Journal title
Language
English
Formats
Publication information
Publisher
Cold Spring Harbor: Cold Spring Harbor Laboratory Press
Subjects
More information
Scope and Contents
Contents
Methylation of the small ribosome subunit rRNA in the ribosomal decoding center results in exceptionally high-level aminoglycoside resistance in bacteria. Enzymes that methylate 16S rRNA on N7 of nucleotide G1405 (m7G1405) have been identified in both aminoglycoside-producing and clinically drug-resistant pathogenic bacteria. Using a fluorescence p...
Alternative Titles
Full title
Functionally critical residues in the aminoglycoside resistance-associated methyltransferase RmtC play distinct roles in 30S substrate recognition
Authors, Artists and Contributors
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_proquest_journals_2266690779
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2266690779
Other Identifiers
E-ISSN
2692-8205
DOI
10.1101/712810
How to access this item
https://www.proquest.com/docview/2266690779?pq-origsite=primo&accountid=13902