{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,16]],"date-time":"2025-10-16T20:17:07Z","timestamp":1760645827850},"reference-count":50,"publisher":"Elsevier BV","issue":"7","license":[{"start":{"date-parts":[[2011,7,1]],"date-time":"2011-07-01T00:00:00Z","timestamp":1309478400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biochimie"],"published-print":{"date-parts":[[2011,7]]},"DOI":"10.1016\/j.biochi.2011.03.008","type":"journal-article","created":{"date-parts":[[2011,4,15]],"date-time":"2011-04-15T00:23:44Z","timestamp":1302827024000},"page":"1115-1123","source":"Crossref","is-referenced-by-count":17,"title":["Alkylhydroperoxide reductase of Helicobacter pylori as a biomarker for gastric patients with different pathological manifestations"],"prefix":"10.1016","volume":"93","author":[{"given":"Chun-Hao","family":"Huang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ming-Hong","family":"Chuang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wan-Lin","family":"Lo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ming-Shiang","family":"Wu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yuan-Heng","family":"Wu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Deng-Chyang","family":"Wu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shyh-Horng","family":"Chiou","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.biochi.2011.03.008_bib1","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1038\/nature01322","article-title":"Inflammation and cancer","volume":"420","author":"Coussens","year":"2002","journal-title":"Nature"},{"key":"10.1016\/j.biochi.2011.03.008_bib2","doi-asserted-by":"crossref","first-page":"1175","DOI":"10.1172\/JCI31537","article-title":"A\u00a0cytokine-mediated link between innate immunity, inflammation, and cancer","volume":"117","author":"Lin","year":"2007","journal-title":"J.\u00a0Clin. Invest."},{"key":"10.1016\/j.biochi.2011.03.008_bib3","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1007\/s00011-010-0245-x","article-title":"Helicobacter pylori: a ROS-inducing bacterial species in the stomach","volume":"59","author":"Handa","year":"2010","journal-title":"Inflamm. Res."},{"key":"10.1016\/j.biochi.2011.03.008_bib4","doi-asserted-by":"crossref","first-page":"1092","DOI":"10.1172\/JCI27177","article-title":"The neutrophil-activating protein of Helicobacter pylori promotes Th1 immune responses","volume":"116","author":"Amedei","year":"2006","journal-title":"J.\u00a0Clin. Invest."},{"key":"10.1016\/j.biochi.2011.03.008_bib5","doi-asserted-by":"crossref","first-page":"56","DOI":"10.3164\/jcbn.39.56","article-title":"Oxidative stress in Helicobacter pylori-associated gastroduodenal disease","volume":"39","author":"Suzuki","year":"2006","journal-title":"J.\u00a0Clin. Biochem. Nutr."},{"key":"10.1016\/j.biochi.2011.03.008_bib6","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1172\/JCI12672","article-title":"Helicobacter pylori genetic diversity and risk of human disease","volume":"107","author":"Blaser","year":"2001","journal-title":"J.\u00a0Clin. Invest."},{"key":"10.1016\/j.biochi.2011.03.008_bib7","doi-asserted-by":"crossref","first-page":"1657","DOI":"10.1111\/j.1440-1746.2008.05659.x","article-title":"Proteomic identification of biomarkers related to Helicobacter pylori-associated gastroduodenal disease: challenges and opportunities","volume":"23","author":"Wu","year":"2008","journal-title":"J.\u00a0Gastroenterol. Hepatol."},{"key":"10.1016\/j.biochi.2011.03.008_bib8","doi-asserted-by":"crossref","first-page":"1329","DOI":"10.1016\/j.micinf.2003.09.011","article-title":"Mechanisms of pathogenesis: evasion of killing by polymorphonuclear leukocytes","volume":"5","author":"Allen","year":"2003","journal-title":"Microbes Infect."},{"key":"10.1016\/j.biochi.2011.03.008_bib9","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1038\/nrmicro955","article-title":"Persistent bacterial infections: the interface of the pathogen and the host immune system","volume":"2","author":"Monack","year":"2004","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.biochi.2011.03.008_bib10","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1038\/35041687","article-title":"Oxidants, oxidative stress and the biology of ageing","volume":"408","author":"Finkel","year":"2000","journal-title":"Nature"},{"key":"10.1016\/j.biochi.2011.03.008_bib11","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/S0891-5849(02)00868-7","article-title":"Molecular and cellular mechanisms involved in Helicobacter pylori-induced inflammation and oxidative stress","volume":"33","author":"Naito","year":"2002","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.biochi.2011.03.008_bib12","doi-asserted-by":"crossref","first-page":"3186","DOI":"10.1128\/JB.184.12.3186-3193.2002","article-title":"Oxidative-stress resistance mutants of Helicobacter pylori","volume":"184","author":"Olczak","year":"2002","journal-title":"J.\u00a0Bacteriol."},{"key":"10.1016\/j.biochi.2011.03.008_bib13","doi-asserted-by":"crossref","first-page":"3895","DOI":"10.1002\/pmic.200401232","article-title":"Proteomic analysis of proteins expressed by Helicobacter pylori under oxidative stress","volume":"5","author":"Chuang","year":"2005","journal-title":"Proteomics"},{"key":"10.1016\/j.biochi.2011.03.008_bib14","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/S0968-0004(02)00003-8","article-title":"Structure, mechanism and regulation of peroxiredoxins","volume":"28","author":"Wood","year":"2003","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.biochi.2011.03.008_bib15","doi-asserted-by":"crossref","first-page":"1961","DOI":"10.1128\/JB.183.6.1961-1973.2001","article-title":"Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization","volume":"183","author":"Baker","year":"2001","journal-title":"J.\u00a0Bacteriol."},{"key":"10.1016\/j.biochi.2011.03.008_bib16","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1128\/IAI.73.1.378-384.2005","article-title":"Contribution of the Helicobacter pylori thiol peroxidase bacterioferritin comigratory protein to oxidative stress resistance and host colonization","volume":"73","author":"Wang","year":"2005","journal-title":"Infect. Immun."},{"key":"10.1016\/j.biochi.2011.03.008_bib17","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1128\/IAI.71.1.580-583.2003","article-title":"Association of Helicobacter pylori antioxidant activities with host colonization proficiency","volume":"71","author":"Olczak","year":"2003","journal-title":"Infect. Immun."},{"key":"10.1016\/j.biochi.2011.03.008_bib18","doi-asserted-by":"crossref","first-page":"3912","DOI":"10.1021\/bi002766h","article-title":"Activity of one of two engineered heterodimers of AhpF, the NADH:peroxiredoxin oxidoreductase from Salmonella typhimurium, reveals intrasubunit electron transfer between domains","volume":"40","author":"Reynolds","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.biochi.2011.03.008_bib19","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.abb.2004.04.017","article-title":"Intermolecular interactions in the AhpC\/AhpD antioxidant defense system of Mycobacterium tuberculosis","volume":"427","author":"Koshkin","year":"2004","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.biochi.2011.03.008_bib20","doi-asserted-by":"crossref","first-page":"2552","DOI":"10.1073\/pnas.0510770103","article-title":"The antioxidant protein alkylhydroperoxide reductase of Helicobacter pylori switches from a peroxide reductase to a molecular chaperone function","volume":"103","author":"Chuang","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"10.1016\/j.biochi.2011.03.008_bib21","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1016\/j.cell.2004.05.002","article-title":"Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function","volume":"117","author":"Jang","year":"2004","journal-title":"Cell"},{"key":"10.1016\/j.biochi.2011.03.008_bib22","doi-asserted-by":"crossref","first-page":"28775","DOI":"10.1074\/jbc.M505362200","article-title":"Oxidative stress-dependent structural and functional switching of a human 2-Cys peroxiredoxin isotype II that enhances HeLa cell resistance to H2O2-induced cell death","volume":"280","author":"Moon","year":"2005","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2011.03.008_bib23","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1093\/jb\/mvp209","article-title":"Characterization of site-specific mutants of alkylhydroperoxide reductase with dual functionality from Helicobacter pylori","volume":"147","author":"Huang","year":"2010","journal-title":"J.\u00a0Biochem."},{"key":"10.1016\/j.biochi.2011.03.008_bib24","doi-asserted-by":"crossref","first-page":"791","DOI":"10.3748\/wjg.v11.i6.791","article-title":"Helicobacter pylori infection, glandular atrophy and intestinal metaplasia in superficial gastritis, gastric erosion, erosive gastritis, gastric ulcer and early gastric cancer","volume":"11","author":"Zhang","year":"2005","journal-title":"World J. Gastroenterol."},{"key":"10.1016\/j.biochi.2011.03.008_bib25","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1111\/j.1574-695X.2007.00248.x","article-title":"Antiadhesive property of microalgal polysaccharide extract on the binding of Helicobacter pylori to gastric mucin","volume":"50","author":"Loke","year":"2007","journal-title":"FEMS Immunol. Med. Microbiol."},{"key":"10.1016\/j.biochi.2011.03.008_bib26","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1006\/mpat.2000.0388","article-title":"A\u00a026 kDa protein of helicobacter pylori shows alkyl hydroperoxide reductase (AhpC) activity and the mono-cistronic transcription of the gene is affected by pH","volume":"29","author":"Lundstrom","year":"2000","journal-title":"Microb. Pathog."},{"key":"10.1016\/j.biochi.2011.03.008_bib27","doi-asserted-by":"crossref","first-page":"17771","DOI":"10.1074\/jbc.270.30.17771","article-title":"Mosaicism in vacuolating cytotoxin alleles of Helicobacter pylori. Association of specific vacA types with cytotoxin production and peptic ulceration","volume":"270","author":"Atherton","year":"1995","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2011.03.008_bib28","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1046\/j.1523-5378.2003.00153.x","article-title":"Surface localized Heat Shock protein 20 (HslV) of Helicobacter pylori","volume":"8","author":"Du","year":"2003","journal-title":"Helicobacter"},{"key":"10.1016\/j.biochi.2011.03.008_bib29","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1046\/j.1523-5378.2001.00038.x","article-title":"Immune response to a 26-kDa protein, alkyl hydroperoxide reductase, in Helicobacter pylori-infected Mongolian gerbil model","volume":"6","author":"Yan","year":"2001","journal-title":"Helicobacter"},{"key":"10.1016\/j.biochi.2011.03.008_bib30","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1089\/hyb.2008.0054","article-title":"Production of polyclonal antibody against alkyl hydroperoxide reductase of Helicobacter pylori and its antigenicity","volume":"27","author":"Mohammadian","year":"2008","journal-title":"Hybridoma (Larchmt)"},{"key":"10.1016\/j.biochi.2011.03.008_bib31","doi-asserted-by":"crossref","first-page":"3687","DOI":"10.1128\/JB.187.11.3687-3692.2005","article-title":"Iron-responsive regulation of the Helicobacter pylori iron-cofactored superoxide dismutase SodB is mediated by Fur","volume":"187","author":"Ernst","year":"2005","journal-title":"J.\u00a0Bacteriol."},{"key":"10.1016\/j.biochi.2011.03.008_bib32","doi-asserted-by":"crossref","first-page":"2014","DOI":"10.1002\/pmic.200300740","article-title":"Proteomic analysis of a ferric uptake regulator mutant of Helicobacter pylori: regulation of Helicobacter pylori gene expression by ferric uptake regulator and iron","volume":"4","author":"Lee","year":"2004","journal-title":"Proteomics"},{"key":"10.1016\/j.biochi.2011.03.008_bib33","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1099\/mic.0.27404-0","article-title":"Transcriptional profiling of Helicobacter pylori Fur- and iron-regulated gene expression","volume":"151","author":"Ernst","year":"2005","journal-title":"Microbiology"},{"key":"10.1016\/j.biochi.2011.03.008_bib34","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1099\/jmm.0.05070-0","article-title":"NapA protects Helicobacter pylori from oxidative stress damage, and its production is influenced by the ferric uptake regulator","volume":"52","author":"Cooksley","year":"2003","journal-title":"J.\u00a0Med. Microbiol."},{"key":"10.1016\/j.biochi.2011.03.008_bib35","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1093\/jb\/mvp200","article-title":"Upregulation of a non-heme iron-containing ferritin with dual ferroxidase and DNA-binding activities in Helicobacter pylori under acid stress","volume":"147","author":"Huang","year":"2010","journal-title":"J.\u00a0Biochem."},{"key":"10.1016\/j.biochi.2011.03.008_bib36","article-title":"Two amino acids mutation of ferric uptake regulator determines Helicobacter pylori resistance to metronidazole","author":"Tsugawa","year":"2010","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.biochi.2011.03.008_bib37","doi-asserted-by":"crossref","first-page":"1697","DOI":"10.1016\/j.bcp.2006.10.022","article-title":"CagA protein of Helicobacter pylori: a hijacker of gastric epithelial cell signaling","volume":"73","author":"Handa","year":"2007","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.biochi.2011.03.008_bib38","first-page":"1","article-title":"Schistosomes, liver flukes and Helicobacter pylori","volume":"61","author":"IARC","year":"1994","journal-title":"IARC Monogr. Eval. Carcinog. Risks. Hum."},{"key":"10.1016\/j.biochi.2011.03.008_bib39","doi-asserted-by":"crossref","first-page":"1111","DOI":"10.1093\/carcin\/21.6.1111","article-title":"Helicobacter pylori causes DNA damage in gastric epithelial cells","volume":"21","author":"Obst","year":"2000","journal-title":"Carcinogenesis"},{"key":"10.1016\/j.biochi.2011.03.008_bib40","doi-asserted-by":"crossref","first-page":"8521","DOI":"10.1158\/0008-5472.CAN-04-3511","article-title":"Spermine oxidation induced by Helicobacter pylori results in apoptosis and DNA damage: implications for gastric carcinogenesis","volume":"64","author":"Xu","year":"2004","journal-title":"Cancer Res."},{"key":"10.1016\/j.biochi.2011.03.008_bib41","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1172\/JCI30111","article-title":"Inflammation, atrophy, and gastric cancer","volume":"117","author":"Fox","year":"2007","journal-title":"J.\u00a0Clin. Invest."},{"key":"10.1016\/j.biochi.2011.03.008_bib42","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1038\/nature05765","article-title":"Helicobacter pylori CagA targets PAR1\/MARK kinase to disrupt epithelial cell polarity","volume":"447","author":"Saadat","year":"2007","journal-title":"Nature"},{"key":"10.1016\/j.biochi.2011.03.008_bib43","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1016\/S0140-6736(00)04046-0","article-title":"Inflammation and cancer: back to Virchow?","volume":"357","author":"Balkwill","year":"2001","journal-title":"Lancet"},{"key":"10.1016\/j.biochi.2011.03.008_bib44","doi-asserted-by":"crossref","first-page":"5517","DOI":"10.1093\/emboj\/18.20.5517","article-title":"Formation of anion-selective channels in the cell plasma membrane by the toxin VacA of Helicobacter pylori is required for its biological activity","volume":"18","author":"Szabo","year":"1999","journal-title":"Embo J."},{"key":"10.1016\/j.biochi.2011.03.008_bib45","doi-asserted-by":"crossref","first-page":"1099","DOI":"10.1126\/science.1086871","article-title":"Helicobacter pylori vacuolating cytotoxin inhibits T lymphocyte activation","volume":"301","author":"Gebert","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.biochi.2011.03.008_bib46","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1016\/j.ejca.2006.01.020","article-title":"Helicobacter pylori infection and gastric cancer","volume":"42","author":"Matysiak-Budnik","year":"2006","journal-title":"Eur. J. Cancer"},{"key":"10.1016\/j.biochi.2011.03.008_bib47","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1111\/j.1365-2958.2006.05302.x","article-title":"The diverse antioxidant systems of Helicobacter pylori","volume":"61","author":"Wang","year":"2006","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.biochi.2011.03.008_bib48","doi-asserted-by":"crossref","first-page":"10646","DOI":"10.1073\/pnas.0504927102","article-title":"Activation of beta-catenin by carcinogenic Helicobacter pylori","volume":"102","author":"Franco","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"10.1016\/j.biochi.2011.03.008_bib49","doi-asserted-by":"crossref","first-page":"2493","DOI":"10.3748\/wjg.v10.i17.2493","article-title":"Helicobacter pylori cagA, iceA and vacA genotypes in patients with gastric cancer in Taiwan","volume":"10","author":"Lin","year":"2004","journal-title":"World J. Gastroenterol."},{"key":"10.1016\/j.biochi.2011.03.008_bib50","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1038\/nrmicro1658","article-title":"Helicobacter pylori evolution and phenotypic diversification in a changing host","volume":"5","author":"Suerbaum","year":"2007","journal-title":"Nat. Rev. Microbiol."}],"container-title":["Biochimie"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908411000824?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908411000824?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,12,3]],"date-time":"2018-12-03T15:53:07Z","timestamp":1543852387000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0300908411000824"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2011,7]]},"references-count":50,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2011,7]]}},"alternative-id":["S0300908411000824"],"URL":"https:\/\/doi.org\/10.1016\/j.biochi.2011.03.008","relation":{},"ISSN":["0300-9084"],"issn-type":[{"value":"0300-9084","type":"print"}],"subject":[],"published":{"date-parts":[[2011,7]]}}}