{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T22:01:51Z","timestamp":1790978511822,"version":"4.1.0"},"reference-count":29,"publisher":"Wiley","issue":"15","license":[{"start":{"date-parts":[[2005,9,9]],"date-time":"2005-09-09T00:00:00Z","timestamp":1126224000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["analyticalsciencejournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Proteomics"],"published-print":{"date-parts":[[2005,10]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    <jats:italic>Helicobacter pylori<\/jats:italic>\n                    is a spiral, slow growing gram\u2010negative microaerophilic bacterium. It has been shown to be the etiological agent of gastroduodenal diseases, such as chronic gastritis, gastric and duodenal ulcers, and gastric cancer. To address the influence of oxidative stress and its underlying mechanisms, we have compared proliferation, urease activity and protein expression profile of\n                    <jats:italic>H. pylori<\/jats:italic>\n                    incubated under normal microaerophilic (5% O\n                    <jats:sub>2<\/jats:sub>\n                    ) and aerobic stress (20% O\n                    <jats:sub>2<\/jats:sub>\n                    ) conditions. Oxidative\u2010stress cells displayed coccoid morphology and time\u2010dependent decrease in proliferation. The urease activity was completely abrogated after 32\u2009h. We have further compared the protein expression profiles of\n                    <jats:italic>H. pylori<\/jats:italic>\n                    under normal growing and oxidative\u2010stress conditions by a global proteomic analysis, which includes high\u2010resolution 2\u2010DE followed by MALDI\u2010TOF\u2010MS and bioinformatic databases search\/peptide\u2010mass comparison. The results revealed that more than ten proteins were differentially expressed under oxidative stress. Most notably, the protein expression levels of urease accessory protein E (UreE, an essential metallochaperone for urease activity) and alkylhydroperoxide reductase (AhpC) with antioxidant potential are greatly decreased under stress conditions. Measurements of messenger RNA transcription level by performing RT\u2010PCR on total mRNA also confirmed that gene expressions for these two proteins are consistently repressed under oxygen tension. These changes form a firm basis to account for the loss of urease activity and anti\u2010oxidative ability of\n                    <jats:italic>H. pylori<\/jats:italic>\n                    after long\u2010term exposure to reactive oxygen. Conceivably, UreE and AhpC may thus be listed as potential targets for the development of therapeutic drugs against\n                    <jats:italic>H. pylori<\/jats:italic>\n                    .\n                  <\/jats:p>","DOI":"10.1002\/pmic.200401232","type":"journal-article","created":{"date-parts":[[2005,9,9]],"date-time":"2005-09-09T04:46:34Z","timestamp":1126241194000},"page":"3895-3901","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":41,"title":["Proteomic analysis of proteins expressed by\n                    <b>\n                      <i>Helicobacter pylori<\/i>\n                    <\/b>\n                    under oxidative stress"],"prefix":"10.1002","volume":"5","author":[{"given":"Ming\u2010Hong","family":"Chuang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ming\u2010Shiang","family":"Wu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jou\u2010Town","family":"Lin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shyh\u2010Horng","family":"Chiou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2005,10,10]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"crossref","first-page":"1311","DOI":"10.1016\/S0140-6736(84)91816-6","volume":"1","author":"Marshell B. 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