The yeast prion protein Ure2 shows glutathione peroxidase activity in both native and fibrillar forms

Journal of Biological Chemistry

Volumn 279, Issue 48, 2004, Pages 50025-50030

  Bai, Ming ^a,b   Zhou, Jun Mei ^a   Perrett, Sarah ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

[No Author keywords available]

Indexed keywords

CONCENTRATION (PROCESS); HEAVY METALS; OXIDATION; PROTEINS; REACTION KINETICS; SENSITIVITY ANALYSIS;

HEAVY METAL IONS; OXIDANTS; PEROXIDASE ACTIVITY;

YEAST;

CUMENE HYDROPEROXIDE; FUNGAL PROTEIN; GLUTATHIONE; GLUTATHIONE PEROXIDASE; HYDROGEN PEROXIDE; ISOENZYME; PRION PROTEIN; PROTEIN URE2; TERT BUTYL HYDROPEROXIDE; UNCLASSIFIED DRUG;

ALKALINITY; AMINO TERMINAL SEQUENCE; ANALYTIC METHOD; ARTICLE; ASSAY; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBUNIT; MICHAELIS CONSTANT; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STRUCTURE; RANDOMIZATION; STEADY STATE; STRUCTURE ACTIVITY RELATION; TEMPERATURE DEPENDENCE;

GLUTATHIONE PEROXIDASE; KINETICS; PRIONS; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; TIME FACTORS;

SACCHAROMYCES CEREVISIAE;

EID: 9644287905     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M406612200     Document Type: Article

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