2013
DOI: 10.1556/eujmi.3.2013.1.11
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Inhibition ofHelicobacter pyloriurease activityin vivoby the synthetic nickel binding protein Hpn

Abstract: Helicobacter pylori infection is the most common cause of gastroduodenal ulcerations worldwide. Adaptation of H. pylori to the acidic environment is mediated by urease splitting urea into carbon dioxide and ammonia. Whereas neutralization of acid by ammonia is essential for gastric H. pylori colonization, the catalytic activity of urease is mediated by nickel ions. Therefore, nickel uptake and metabolism play key roles in H. pylori infection and urease is considered first line target for drug development and v… Show more

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Cited by 2 publications
(1 citation statement)
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“…104 Recently, synthetic Hpn was shown to completely inhibit the urease activity of H. pylori in liquid cultures, indicating that nickel uptake was effectively blocked by Hpn. 105 Thus, Hpn can be considered interesting not only because of its unique coordination chemistry or biological significance, but also because of its potential therapeutic use.…”
Section: Bacterial His-rich Sequencesmentioning
confidence: 99%
“…104 Recently, synthetic Hpn was shown to completely inhibit the urease activity of H. pylori in liquid cultures, indicating that nickel uptake was effectively blocked by Hpn. 105 Thus, Hpn can be considered interesting not only because of its unique coordination chemistry or biological significance, but also because of its potential therapeutic use.…”
Section: Bacterial His-rich Sequencesmentioning
confidence: 99%