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

A genetic model to investigate drug-target interactions at the ribosomal decoding site.

Biochimie - 1 Aug 2006

Hobbie S N, Bruell C, Kalapala S, Akshay S, Schmidt S, Pfister P, Böttger E C

Abstract excerpt

Recent advances in X-ray crystallography have greatly contributed to the understanding of the structural interactions between aminoglycosides and the ribosomal decoding site. Efforts to genetically probe the functional relevance of proposed drug-nucleotide contacts have in part been hampered by t...

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 Binding Sites
Share to Models, Genetic

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Molecular Structure

Share to Ribosomes

Share to RNA, Bacterial

Share to RNA, Ribosomal, 16S

Source

Identifiers

PMID: 16690195
DOI: 10.1016/j.biochi.2006.04.008

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-16690195-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A genetic model to investigate drug-target interactions at the ribosomal decoding site.PMID 16690195Read ↗

Introducing mutations into a chromosomal rRNA gene using a genetically modified eubacterial host with a single rRNA operon.Semantic proximity Read ↗

Analysis of the contribution of individual substituents in 4,6-aminoglycoside-ribosome interaction.Semantic proximity Read ↗

Loss of U1498 methylation in 16S rRNA by RsmE methyltransferase associates its role with aminoglycoside resistance in mycobacteriaSemantic proximity Read ↗

The role of ribosomal RNAs in macrolide resistance.Semantic proximity Read ↗

Deletion of RsmE 16S rRNA methyltransferase leads to low level increase in aminoglycoside resistance in <i>Mycobacterium smegmatis</i>Semantic proximity Read ↗

Ribosomal A site binding pattern differs between Arm methyltransferases from clinical pathogens and a natural producer of aminoglycosides.Semantic proximity Read ↗

30S subunit recognition and G1405 modification by the aminoglycoside-resistance 16S ribosomal RNA methyltransferase RmtCSemantic proximity Read ↗

Discovery of First-in-Class Inhibitors Targeting a Pathogen-Associated Aminoglycoside-Resistance 16S rRNA MethyltransferaseSemantic proximity Read ↗

Mechanisms of streptomycin resistance: selection of mutations in the 16S rRNA gene conferring resistance.Semantic proximity Read ↗

23S rRNA base pair 2057-2611 determines ketolide susceptibility and fitness cost of the macrolide resistance mutation 2058A-->G.Semantic proximity Read ↗

Potential new antibiotic sites in the ribosome revealed by deleterious mutations in RNA of the large ribosomal subunit.Semantic proximity Read ↗

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

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