The Helicobacter pylori Urel protein: Role in adaptation to acidity and identification of residues essential for its activity and for acid activation

Molecular Microbiology

Volumn 42, Issue 4, 2001, Pages 1021-1034

  Bury Moné, Stéphanie ^a   Skouloubris, Stéphane ^a,b   Labigne, Agnès ^a   De Reuse, Hilde ^a  

^a INSTITUT PASTEUR   (France)

^b JOHNS HOPKINS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACETAMIDE; AMMONIA; BACTERIAL PROTEIN; HISTIDINE; MEMBRANE PROTEIN; PROTEIN UREL; UNCLASSIFIED DRUG; UREA; UREASE; ACETAMIDE DERIVATIVE; CHIMERIC PROTEIN; UREI PROTEIN;

ACIDITY; ADAPTATION; ARTICLE; BACTERIUM COLONY; CHROMOSOME MUTATION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME KINETICS; EXPOSURE; HELICOBACTER PYLORI; HYDROLYSIS; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; STIMULATION; STOMACH ACID; AMINO ACID SEQUENCE; ANIMAL; BACTERIAL GENE; CHEMISTRY; CYTOLOGY; DRUG EFFECT; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; PH; PHENOTYPE; PHYSIOLOGY; PROTEIN SECONDARY STRUCTURE; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS;

BACTERIA (MICROORGANISMS); HELICOBACTER PYLORI; NEGIBACTERIA;

ACETAMIDES; ADAPTATION, PHYSIOLOGICAL; AMINO ACID SEQUENCE; AMMONIA; ANIMAL; BACTERIAL PROTEINS; CHIMERIC PROTEINS; GENES, BACTERIAL; HELICOBACTER PYLORI; HUMAN; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PHENOTYPE; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; UREA; UREASE;

EID: 0034747001     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2001.02689.x     Document Type: Article

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