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

Anti-tubercular Activity of Pyrazinamide is Independent of trans-Translation and RpsA.

Scientific reports - 21 Jul 2017

Dillon Nicholas A, Peterson Nicholas D, Feaga Heather A, Keiler Kenneth C, Baughn Anthony D

Abstract excerpt

Pyrazinamide (PZA) is a first line anti-tubercular drug for which the mechanism of action remains unresolved. Recently, it was proposed that the active form of PZA, pyrazinoic acid (POA), disrupts the ribosome rescue process of trans-translation in Mycobacterium tuberculosis. This model suggested that POA binds within the carboxy-terminal domain of ribosomal protein S1 (RpsA) and inhibits trans-translation...

Read the complete abstract on PubMed

Topics

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

Share to Antitubercular Agents
Share to Drug Resistance, Bacterial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mycobacterium tuberculosis

Share to Oligonucleotides

Share to Protein Biosynthesis

Share to Pyrazinamide

Share to Ribosomal Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 28733601
DOI: 10.1038/s41598-017-06415-5
PMCID: PMC5522395

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Anti-tubercular Activity of Pyrazinamide is Independent of trans-Translation and RpsA.PMID 28733601Read ↗

Pyrazinamide inhibits trans-translation in Mycobacterium tuberculosis.Semantic proximity Read ↗

Structural basis for targeting the ribosomal protein S1 of Mycobacterium tuberculosis by pyrazinamide.Semantic proximity Read ↗

Mycobacterium tuberculosis ribosomal protein S1 (RpsA) and variants with truncated C-terminal end show absence of interaction with pyrazinoic acid.Semantic proximity Read ↗

Pyrazinamide resistance in Mycobacterium tuberculosis: Review and update.Semantic proximity Read ↗

The Bewildering Antitubercular Action of Pyrazinamide.Semantic proximity Read ↗

Pyrazinoic Acid Inhibits a Bifunctional Enzyme in Mycobacterium tuberculosisSemantic proximity Read ↗

Mutations Associated with Pyrazinamide Resistance in Mycobacterium tuberculosis: A Review and Update.Semantic proximity Read ↗

Atypical Genetic Basis of Pyrazinamide Resistance in Monoresistant Mycobacterium tuberculosis.Semantic proximity Read ↗

Insight into novel clinical mutants of RpsA-S324F, E325K, and G341R of Mycobacterium tuberculosis associated with pyrazinamide resistanceSemantic proximity Read ↗

The molecular basis of pyrazinamide activity on Mycobacterium tuberculosis PanD.Semantic proximity Read ↗

Mutations in <i>panD</i> encoding aspartate decarboxylase are associated with pyrazinamide resistance in <i>Mycobacterium tuberculosis</i>Semantic proximity Read ↗

Pyrazinamide Resistance Is Caused by Two Distinct Mechanisms: Prevention of Coenzyme A Depletion and Loss of Virulence Factor SynthesisSemantic proximity Read ↗

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