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

<i>In silico</i>approach towards identification of potential inhibitors of<i>Helicobacter pylori</i>DapE

9 Sept 2014

Abstract excerpt

Helicobacter pylori is a gastric mucosal pathogen and is associated with diseases like peptic ulcer and gastric cancer. To combat H. pylori infection, there is an urgent need for new class of antibiotics due to the emergence of drug-resistant strains. Enzymes involved in bacterial lysine biosynthetic pathways may be potential targets for antibacterial drug development, since lysine is an essential component of...

Read the complete abstract on PubMed

Topics

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

Share to Biochemical and Molecular Research
Share to Enzyme Structure and Function
Share to Peptidase Inhibition and Analysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 25204745
DOI: 10.1080/07391102.2014.954272

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

<i>In silico</i>approach towards identification of potential inhibitors of<i>Helicobacter pylori</i>DapEPMID 25204745Read ↗

Peptide deformylase is a potential target for anti‐Helicobacter pylori drugs: Reverse docking, enzymatic assay, and X‐ray crystallography validationSemantic proximity Read ↗

The dimerization domain in DapE enzymes is required for catalysis.Semantic proximity Read ↗

Characterization of Helicobacter pylori dapE and construction of a conditionally lethal dapE mutantSemantic proximity Read ↗

<scp>l</scp> -Asparaginase as a new molecular target against leishmaniasis: insights into the mechanism of action and structure-based inhibitor designSemantic proximity Read ↗

Force field parameters for Fe <sup>2+</sup> <sub>4</sub> S <sup>2-</sup> <sub>4</sub> clusters of dihydropyrimidine dehydrogenase, the 5-fluorouracil cancer drug deactivation protein: a step towards <i>in silico</i> pharmacogenomics studiesSemantic proximity Read ↗

Identification of novel drug targets for Helicobacter pylori: structure-based virtual screening of potential inhibitors against DAH7PS protein involved in the shikimate pathwaySemantic proximity Read ↗

Molecular investigation of antimicrobial peptides against Helicobacter pylori proteins using a peptide-protein docking approachSemantic proximity Read ↗

Modification of <i>Helicobacter pylori</i> Peptidoglycan Enhances NOD1 Activation and Promotes Cancer of the StomachSemantic proximity Read ↗

Repurposing FDA-Approved Agents to Develop a Prototype Helicobacter Pylori Shikimate Kinase (HPSK) inhibitor: A Computational Approach Using Virtual Screening, MM-GBSA Calculation, MD Simulations, and DFT AnalysisSemantic proximity Read ↗

High-throughput screening and molecular dynamics simulations of natural products targeting LuxS/AI-2 system as a novel antibacterial strategy for antibiotic resistance in Helicobacter pyloriSemantic proximity Read ↗

Loss of Catalytic Activity in the E134D, H67A, and H349A Mutants of DapE: Mechanistic Analysis with QM/MM Investigation.Semantic proximity Read ↗

Mechanistic inhibition of gastric cancer-associated bacteria Helicobacter pylori by selected phytocompounds: A new cutting-edge computational approachSemantic proximity Read ↗

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