Drug pipeline
Full profile accessExplore the programs pursuing this target and their development progress.
- Drug candidates
- Developers
- Development stage
Target intelligence / Profile preview
Helicobacter pylori urease is a nickel-dependent enzyme that plays a pivotal role in the pathogenesis of gastric infections by neutralizing stomach acid through the production of ammonia [1]. This neutralization creates a habitable microenvironment for the bacterium, allowing it to colonize the gastric mucosa [2]. In addition to urease, H. pylori relies on various sulfhydryl-containing enzyme systems that are essential for its metabolism and cellular homeostasis [3]. Therapeutic interventions, most notably bismuth-containing compounds, exert their antimicrobial effects by inhibiting urease activity and binding to the sulfhydryl groups of these vital bacterial enzymes [4]. This dual mechanism of action leads to the disruption of the bacterial cell wall, inhibition of protein and ATP synthesis, and eventual cell death [5]. Targeting these systems is a cornerstone in the eradication of H. pylori, which is a primary risk factor for peptic ulcers and gastric adenocarcinoma [6].
Inhibition of the urease enzyme prevents the neutralization of gastric acid, while the binding to sulfhydryl groups disrupts multiple bacterial metabolic pathways.
3 more in the full profile.
Beyond the preview
Explore the evidence, development activity, and competitive landscape with Gosset’s full data platform.
Explore the programs pursuing this target and their development progress.
Follow the clinical studies evaluating therapies directed at this target.
Compare approaches across drug candidates, modalities, and indications.
Investigate the research and source evidence behind target biology and development.
Explore patent activity around therapies and technologies addressing this target.
Connect target biology, drug development, and emerging evidence in your research.
See how Gosset can support your research on Helicobacter pylori urease and sulfhydryl-containing enzymes (N/A).