Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Binding site of macrolide antibiotics on the ribosome: new resistance mutation identifies a specific interaction of ketolides with rRNA.

Journal of bacteriology - 1 Dec 2001

Garza-Ramos G, Xiong L, Zhong P, Mankin A

Abstract excerpt

Macrolides represent a clinically important class of antibiotics that block protein synthesis by interacting with the large ribosomal subunit. The macrolide binding site is composed primarily of rRNA. However, the mode of interaction of macrolides with rRNA and the exact location of the drug binding site have yet to be described. A new class of macrolide antibiotics, known as ketolides, show improved activity...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Anti-Bacterial Agents
Share to Base Sequence
Share to Binding Sites

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Drug Resistance, Bacterial

Share to Macrolides

Share to Molecular Sequence Data

Share to Ribosomes

Share to RNA, Ribosomal

Source

Open in PubMed Open full text

Identifiers

PMID: 11698379
DOI: 10.1128/JB.183.23.6898-6907.2001
PMCID: PMC95531

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Binding site of macrolide antibiotics on the ribosome: new resistance mutation identifies a specific interaction of ketolides with rRNA.PMID 11698379Read ↗

Ketolide antimicrobial activity persists after disruption of interactions with domain II of 23S rRNA.Semantic proximity Read ↗

Macrolide resistance from the ribosome perspective.Semantic proximity Read ↗

Binding site of the bridged macrolides in the Escherichia coli ribosome.Semantic proximity Read ↗

A ketolide resistance mutation in domain II of 23S rRNA reveals the proximity of hairpin 35 to the peptidyl transferase centre.Semantic proximity Read ↗

The macrolide binding site on the bacterial ribosome.Semantic proximity Read ↗

Structural Insight into the Antibiotic Action of Telithromycin against Resistant MutantsSemantic proximity Read ↗

Macrolide-ketolide inhibition of MLS-resistant ribosomes is improved by alternative drug interaction with domain II of 23S rRNA.Semantic proximity Read ↗

Macrolide antibiotic interaction and resistance on the bacterial ribosome.Semantic proximity Read ↗

23S rRNA 2058A-->G alteration mediates ketolide resistance in combination with deletion in L22.Semantic proximity Read ↗

[Ribosomal antibiotics].Semantic proximity Read ↗

Ribosome-binding and anti-microbial studies of the mycinamicins, 16-membered macrolide antibiotics from Micromonospora griseorubidaSemantic proximity Read ↗

Macrolide Antibiotics: Binding Site, Mechanism of Action, ResistanceSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.