EC Number |
Title |
Organism |
---|
2.1.1.184 | Alanine-scanning mutagenesis of the predicted rRNA-binding domain of ErmC' redefines the substrate-binding site and suggests a model for protein-RNA interactions |
Bacillus subtilis |
2.1.1.184 | Alanine-scanning mutagenesis of the predicted rRNA-binding domain of ErmC' redefines the substrate-binding site and suggests a model for protein-RNA interactions |
Bacillus subtilis BD1167 |
2.1.1.184 | Crystal structure of ErmC', an rRNA methyltransferase which mediates antibiotic resistance in bacteria |
Bacillus subtilis |
2.1.1.184 | Dubnau, D.: Binding of Bacillus subtilis ermC' methyltransferase to 23S rRNA |
Bacillus subtilis |
2.1.1.184 | Evolved Escherichia coli strains for amplified, functional expression of membrane proteins |
Escherichia coli |
2.1.1.184 | Induction of ermC methylase in the absence of macrolide antibiotics and by pseudomonic acid A |
Bacillus subtilis |
2.1.1.184 | Kavanaugh, T.J.; Abad-Zapatero, C.: The 2.2 A structure of the rRNA methyltransferase ErmC' and its complexes with cofactor and cofactor analogs: implications for the reaction mechanism |
Bacillus subtilis |
2.1.1.184 | Mono- and dimethylating activities and kinetic studies of the ermC 23 S rRNA methyltransferase |
Bacillus subtilis |
2.1.1.184 | Mono- and dimethylating activities and kinetic studies of the ermC 23 S rRNA methyltransferase |
Bacillus subtilis BD170 |
2.1.1.184 | Mutational analysis defines the roles of conserved amino acid residues in the predicted catalytic pocket of the rRNA:m6A methyltransferase ErmC' |
Bacillus subtilis |