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

Biochemical and structural characterization of mycobacterial aspartyl-tRNA synthetase AspS, a promising TB drug target.

PloS one - 1 Jan 2014

Gurcha Sudagar S, Usha Veeraraghavan, Cox Jonathan A G, Fütterer Klaus, Abrahams Katherine A, Bhatt Apoorva, Alderwick Luke J, Reynolds Robert C, Loman Nicholas J, Nataraj VijayaShankar, Alemparte Carlos, Barros David, Lloyd Adrian J, Ballell Lluis, Hobrath Judith V, Besra Gurdyal S

Abstract excerpt

The human pathogen Mycobacterium tuberculosis is the causative agent of pulmonary tuberculosis (TB), a disease with high worldwide mortality rates. Current treatment programs are under significant threat from multi-drug and extensively-drug resistant strains of M. tuberculosis, and it is essentia...

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 Aspartate-tRNA Ligase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dimerization

Share to Mycobacterium bovis

Share to Mycobacterium smegmatis

Share to Piperidines

Share to Thiazoles

Share to Tuberculosis, Pulmonary

Source

Open in PubMed Open full text

Identifiers

PMID: 25409504
DOI: 10.1371/journal.pone.0113568
PMCID: PMC4237437

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-25409504-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Biochemical and structural characterization of mycobacterial aspartyl-tRNA synthetase AspS, a promising TB drug target.PMID 25409504Read ↗

Identification of KasA as the cellular target of an anti-tubercular scaffold.Semantic proximity Read ↗

Natural product-mediated reaction hijacking mechanism validates <i>Plasmodium</i> aspartyl-tRNA synthetase as an antimalarial drug targetSemantic proximity Read ↗

Investigate Natural Product Indolmycin and the Synthetically Improved Analogue Toward Antimycobacterial Agents.Semantic proximity Read ↗

Lysine succinylation of Mycobacterium tuberculosis isocitrate lyase (ICL) fine-tunes the microbial resistance to antibiotics.Semantic proximity Read ↗

DapB is a conserved target for tackling antimicrobial resistance in Mycobacterium tuberculosisSemantic proximity Read ↗

Substrate specificity of MarP, a periplasmic protease required for resistance to acid and oxidative stress in Mycobacterium tuberculosis.Semantic proximity Read ↗

Molecular insights into inhibitor action on a key bacterial metabolic enzyme Cystathionine β-SynthaseSemantic proximity Read ↗

The emergence of resistance to the antiparasitic selamectin in Mycobacterium smegmatis is improbable and contingent on cell wall integrity.Semantic proximity Read ↗

Inhibiting mycobacterial tryptophan synthase by targeting the inter-subunit interface.Semantic proximity Read ↗

Mechanism of inhibition of Mycobacterium tuberculosis antigen 85 by ebselen.Semantic proximity Read ↗

Emergence of resistance to the antiparasitic selamectin in <i>Mycobacterium smegmatis</i> is improbable and contingent on cell wall integritySemantic proximity Read ↗

Essentiality Assessment of Cysteinyl and Lysyl-tRNA Synthetases of Mycobacterium smegmatis.Semantic proximity Read ↗

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