Methionine sulfoxide reductases preferentially reduce unfolded oxidized proteins and protect cells from oxidative protein unfolding

Journal of Biological Chemistry

Volumn 287, Issue 29, 2012, Pages 24448-24459

  Tarrago, Lionel ^a   Kaya, Alaattin ^a   Weerapana, Eranthie ^b   Marino, Stefano M ^a   Gladyshev, Vadim N ^a  

^a BRIGHAM AND WOMEN S HOSPITAL   (United States)

^b BOSTON COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC EFFICIENCIES; CATALYTIC PROPERTIES; CRITICAL FUNCTIONS; FOLDED PROTEINS; FOLDING PROCESS; GLUTATHIONE-S-TRANSFERASE; LOW MOLECULAR WEIGHT; METHIONINE SULFOXIDE; METHIONINE SULFOXIDE REDUCTASE; MICHAELIS-MENTEN KINETIC; MODEL SUBSTRATES; PHYSIOLOGICAL SUBSTRATE; PROTEIN UNFOLDING; STEREOSPECIFIC MANNER; THIOREDOXINS; UNFOLDED PROTEINS;

AMINO ACIDS; CATALYSIS; ENZYMES; MASS SPECTROMETRY; MOLECULAR WEIGHT; OXIDATION; SUBSTRATES;

PROTEINS;

GLUTATHIONE TRANSFERASE; METHIONINE SULFOXIDE REDUCTASE A; METHIONINE SULFOXIDE REDUCTASE B; POLYPEPTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; THIOREDOXIN;

ARTICLE; CATALYSIS; CELL PROTECTION; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SUBSTRATE COMPLEX; MASS SPECTROMETRY; MICHAELIS MENTEN KINETICS; MOLECULAR WEIGHT; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN METABOLISM; PROTEIN REPAIR; PROTEIN UNFOLDING; QUANTITATIVE ANALYSIS; SACCHAROMYCES CEREVISIAE;

MASS SPECTROMETRY; METHIONINE SULFOXIDE REDUCTASES; MUTAGENESIS, SITE-DIRECTED; OXIDATIVE STRESS; PROTEIN FOLDING; PROTEIN UNFOLDING;

EID: 84863797987     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.374520     Document Type: Article

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