The NADPH quinone reductase MdaB confers oxidative stress resistance to Helicobacter hepaticus

Microbial Pathogenesis

Volumn 44, Issue 2, 2008, Pages 169-174

  Hong, Yang ^a   Wang, Ge ^a   Maier, Robert J ^a  

^a UNIVERSITY OF GEORGIA   (United States)

Author keywords

Helicobacter hepaticus; mdaB; Oxidative stress; Quinone reductase

Indexed keywords

CUMENE HYDROPEROXIDE; HYDROGEN PEROXIDE; PARAQUAT; QUINONE REDUCTASE MDAB; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); SUPEROXIDE DISMUTASE; TERT BUTYL HYDROPEROXIDE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL STRAIN; CONTROLLED STUDY; ELECTRON TRANSPORT; ENZYME PURIFICATION; GENE DISRUPTION; HELICOBACTER HEPATICUS; HELICOBACTER PYLORI; MUTAGENESIS; NONHUMAN; OXIDATIVE STRESS; PHENOTYPE; PRIORITY JOURNAL; PROTEIN EXPRESSION; WESTERN BLOTTING; WILD TYPE;

ANTI-BACTERIAL AGENTS; BACTERIAL PROTEINS; BENZENE DERIVATIVES; GENE DELETION; HELICOBACTER HEPATICUS; HELICOBACTER PYLORI; HYDROGEN PEROXIDE; KINETICS; MUTAGENESIS, INSERTIONAL; NAD(P)H DEHYDROGENASE (QUINONE); NADP; OXIDATIVE STRESS; OXYGEN; PARAQUAT; PROTEOME; SUPEROXIDE DISMUTASE; TERT-BUTYLHYDROPEROXIDE;

HELICOBACTER HEPATICUS; HELICOBACTER PYLORI;

EID: 37349111737     PISSN: 08824010     EISSN: 10961208     Source Type: Journal    
DOI: 10.1016/j.micpath.2006.08.005     Document Type: Article

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