Novel glutaredoxin activity of the yeast prion protein ure2 reveals a native-like dimer within fibrils

Journal of Biological Chemistry

Volumn 284, Issue 21, 2009, Pages 14058-14067

  Zhang, Zai Rong ^a,b   Perrett, Sarah ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC ENZYMES; AMYLOID-LIKE FIBRIL; CATALYTIC CYSTEINE RESIDUE; COOPERATIVITY; CYSTEINE RESIDUES; DIMERIC STRUCTURE; DISULFIDE REDUCTASE; GLUTATHIONE; GLUTATHIONE TRANSFERASE; GLUTATHIONYLATION; IN-VITRO; IN-VIVO; NATIVE STATE; PEROXIDASE ACTIVITIES; SACCHAROMYCES CEREVISIAE; STRUCTURAL SIMILARITY; THIOL-DISULFIDE; YEAST PRION;

ENZYME ACTIVITY; GLYCOPROTEINS; HEAVY METALS; METAL IONS; OXIDANTS; PLANTS (BOTANY); SIGNAL TRANSDUCTION; TOXICITY; YEAST;

ENZYMES;

DISULFIDE; FUNGAL PROTEIN; GLUTAREDOXIN; GLUTAREDOXIN 1; GLUTATHIONE; HEAVY METAL; METAL ION; OXIDIZING AGENT; PRION PROTEIN URE2; THIOL; UNCLASSIFIED DRUG; AMYLOID; CADMIUM CHLORIDE; GLUTATHIONE DEHYDROGENASE (ASCORBATE); HYDROGEN PEROXIDE; INSULIN; OXIDOREDUCTASE; REDUCING AGENT; SACCHAROMYCES CEREVISIAE PROTEIN; URE2 PROTEIN, S CEREVISIAE;

ALLOSTERISM; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SUBSTRATE; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN MOTIF; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; STEADY STATE; BINDING SITE; BIOCATALYSIS; CHEMISTRY; DRUG EFFECT; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; MUTATION; OXIDATION REDUCTION REACTION; PRION; PROTEIN MULTIMERIZATION; PROTEIN TERTIARY STRUCTURE; SACCHAROMYCES CEREVISIAE; SOLUBILITY; TIME;

SACCHAROMYCES CEREVISIAE;

AMYLOID; BINDING SITES; BIOCATALYSIS; CADMIUM CHLORIDE; GLUTAREDOXINS; GLUTATHIONE; HYDROGEN PEROXIDE; INSULIN; KINETICS; MUTATION; OXIDATION-REDUCTION; OXIDOREDUCTASES; PRIONS; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; REDUCING AGENTS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SOLUBILITY; TIME FACTORS;

EID: 67649815210     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M901189200     Document Type: Article

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