NMR and Molecular Modelling Studies of the Binding of Amicetin Antibiotic to Conserved Secondary Structural Motifs of 23S Ribosomal RNAs
- 1 March 2006
- journal article
- research article
- Published by Springer Nature in The Journal of Antibiotics
- Vol. 59 (3) , 177-183
- https://doi.org/10.1038/ja.2006.25
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- The Ribosomal Peptidyl Transferase Center: Structure, Function, Evolution, InhibitionCritical Reviews in Biochemistry and Molecular Biology, 2005
- Chemical and functional diversity of small molecule ligands for RNABiopolymers, 2003
- The crystal structure of UUCG tetraloop 1 1Edited by J DoudnaJournal of Molecular Biology, 2000
- The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 Å ResolutionScience, 2000
- Conformational independence of N‐ and C‐domains in ribosomal protein L7/L12 and in the complex with protein L10FEBS Letters, 1998
- Antibiotic resistance origins, evolution, selection and spread, Ciba Foundation Symposium 207Public Health, 1997
- Mutations in the Peptidyl Transferase Center of 23 S rRNA Reveal the Site of Action of Sparsomycin, a Universal Inhibitor of TranslationJournal of Molecular Biology, 1996
- RNA Folding Topology and Intermolecular Contacts in the AMP−RNA Aptamer ComplexBiochemistry, 1996
- The interactions of Escherichia coli trp repressor with tryptophan and with an operator oligonucleotideEuropean Journal of Biochemistry, 1994
- The structure of the antibiotic amicetin consisting of nucleobase, disaccharide and amino acid moietiesActa Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 1981