The macrolide-ketolide antibiotic binding site is formed by structures in domains II and V of 23S ribosomal RNA.
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Binding and action of CEM-101, a new fluoroketolide antibiotic that inhibits protein synthesisAntibiotics that target protein synthesisStructural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteriaStructure of 23S rRNA hairpin 35 and its interaction with the tylosin-resistance methyltransferase RlmAII.Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug actionRevisiting the structures of several antibiotics bound to the bacterial ribosomeThe bacterial ribosome as a target for antibioticsImpact of ribosomal modification on the binding of the antibiotic telithromycin using a combined grand canonical monte carlo/molecular dynamics simulation approachSynthesis and evaluation of chloramphenicol homodimers: molecular target, antimicrobial activity, and toxicity against human cellsThe tylosin resistance gene tlrB of Streptomyces fradiae encodes a methyltransferase that targets G748 in 23S rRNA.Pharmacokinetics of the new ketolide telithromycin (HMR 3647) administered in ascending single and multiple doses.Identifying the methyltransferases for m(5)U747 and m(5)U1939 in 23S rRNA using MALDI mass spectrometryKetolide resistance in Streptococcus pyogenes correlates with the degree of rRNA dimethylation by Erm.Emergence of macrolide-resistant Mycoplasma pneumoniae with a 23S rRNA gene mutation.ABT-773: a new ketolide antibiotic.23S rRNA base pair 2057-2611 determines ketolide susceptibility and fitness cost of the macrolide resistance mutation 2058A-->G.In vitro activities of the novel ketolide telithromycin (HMR 3647) against erythromycin-resistant Streptococcus speciesSuppression of nonsense mutations induced by expression of an RNA complementary to a conserved segment of 23S rRNA.Binding site of macrolide antibiotics on the ribosome: new resistance mutation identifies a specific interaction of ketolides with rRNADiversity of ribosomal mutations conferring resistance to macrolides, clindamycin, streptogramin, and telithromycin in Streptococcus pneumoniae.Macrolide resistance conferred by base substitutions in 23S rRNA.Ribosomal mutations in Streptococcus pneumoniae clinical isolatesMethylation at nucleotide G745 or G748 in 23S rRNA distinguishes Gram-negative from Gram-positive bacteria.Ketolides: an emerging treatment for macrolide-resistant respiratory infections, focusing on S. pneumoniae.Resistance to the macrolide antibiotic tylosin is conferred by single methylations at 23S rRNA nucleotides G748 and A2058 acting in synergy.Telithromycin: an oral ketolide for respiratory infections.Macrolide-peptide conjugates as probes of the path of travel of the nascent peptides through the ribosome.Macrolide resistance by ribosomal mutation in clinical isolates of Streptococcus pneumoniae from the PROTEKT 1999-2000 studyMolecular characterization of resistance to macrolides in Bartonella henselae.Dead bugs don't mutate: susceptibility issues in the emergence of bacterial resistance.Novel antibacterial agents for the treatment of serious Gram-positive infections.23S rRNA 2058A-->G alteration mediates ketolide resistance in combination with deletion in L22.Activities of cethromycin and telithromycin against recent North American isolates of Streptococcus pneumoniaeApplication of molecular genetic methods in macrolide, lincosamide and streptogramin resistance diagnostics and in detection of drug-resistant Mycobacterium tuberculosis.New research in macrolides and ketolides since 1997.The ribosomal peptidyl transferase center: structure, function, evolution, inhibition.Telithromycin resistance in Streptococcus pneumoniae is conferred by a deletion in the leader sequence of erm(B) that increases rRNA methylation.Antibiotics and the ribosome.Induction of erm(C) expression by noninducing antibiotics.PCR-Based Rapid Identification System Using Bridged Nucleic Acids for Detection of Clarithromycin-Resistant Mycobacterium avium-M. intracellulare Complex Isolates.
P2860
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P2860
The macrolide-ketolide antibiotic binding site is formed by structures in domains II and V of 23S ribosomal RNA.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh
1999年學術文章
@zh-hant
name
The macrolide-ketolide antibio ...... II and V of 23S ribosomal RNA.
@en
The macrolide-ketolide antibio ...... II and V of 23S ribosomal RNA.
@nl
type
label
The macrolide-ketolide antibio ...... II and V of 23S ribosomal RNA.
@en
The macrolide-ketolide antibio ...... II and V of 23S ribosomal RNA.
@nl
prefLabel
The macrolide-ketolide antibio ...... II and V of 23S ribosomal RNA.
@en
The macrolide-ketolide antibio ...... II and V of 23S ribosomal RNA.
@nl
P2860
P1476
The macrolide-ketolide antibio ...... II and V of 23S ribosomal RNA.
@en
P2093
P2860
P304
P356
10.1046/J.1365-2958.1999.01202.X
P407
P577
1999-01-01T00:00:00Z