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

Mutations outside the anisomycin-binding site can make ribosomes drug-resistant.

Journal of molecular biology - 6 Jun 2008

Blaha Gregor, Gürel Güliz, Schroeder Susan J, Moore Peter B, Steitz Thomas A

Abstract excerpt

Eleven mutations that make Haloarcula marismortui resistant to anisomycin, an antibiotic that competes with the amino acid side chains of aminoacyl tRNAs for binding to the A-site cleft of the large ribosomal unit, have been identified in 23S rRNA. The correlation observed between the sensitivity of H. marismortui to anisomycin and the affinity of its large ribosomal subunits for the drug indicates that its...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Drug Resistance, Microbial
Share to Molecular Structure

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

Share to Protein Structure, Tertiary

Share to Protein Subunits

Share to Protein Synthesis Inhibitors

Share to Ribosomes

Share to RNA, Ribosomal, 23S

Source

Open in PubMed Open full text

Identifiers

PMID: 18455733
DOI: 10.1016/j.jmb.2008.03.075
PMCID: PMC2442718

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

Mutations outside the anisomycin-binding site can make ribosomes drug-resistant.PMID 18455733Read ↗

Macrolide resistance from the ribosome perspective.Semantic proximity Read ↗

Structures of MLSBK antibiotics bound to mutated large ribosomal subunits provide a structural explanation for resistance.Semantic proximity Read ↗

The structures of four macrolide antibiotics bound to the large ribosomal subunit.Semantic proximity Read ↗

A mutation in the large subunit ribosomal RNA gene of Tetrahymena confers anisomycin resistance and cold sensitivity.Semantic proximity Read ↗

Crystal Structure of the Oxazolidinone Antibiotic Linezolid Bound to the 50S Ribosomal SubunitSemantic proximity Read ↗

Interaction of avilamycin with ribosomes and resistance caused by mutations in 23S rRNA.Semantic proximity Read ↗

Resistance mutations in 23 S rRNA identify the site of action of the protein synthesis inhibitor linezolid in the ribosomal peptidyl transferase center.Semantic proximity Read ↗

An intragenic suppressor of cold sensitivity identifies potentially interacting bases in the peptidyl transferase center of Tetrahymena rRNA.Semantic proximity Read ↗

A sparsomycin-resistant mutant of Halobacterium salinarium lacks a modification at nucleotide U2603 in the peptidyl transferase centre of 23 S rRNA.Semantic proximity Read ↗

A genetic model to investigate drug-target interactions at the ribosomal decoding site.Semantic proximity Read ↗

Mutation K42R in ribosomal protein S12 does not affect susceptibility of Mycobacterium smegmatis 16S rRNA A-site mutants to 2-deoxystreptamines.Semantic proximity Read ↗

Gene replacement in Haloarcula marismortui: construction of a strain with two of its three chromosomal rRNA operons deleted.Semantic proximity Read ↗

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