Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone

Journal of Biological Chemistry

Volumn 275, Issue 25, 2000, Pages 18759-18766

  Barbirz, Stefanie ^a   Jakob, Ursula ^b   Glocker, Michael O ^a,c  

^a UNIVERSITY OF KONSTANZ   (Germany)

^b UNIVERSITY OF MICHIGAN   (United States)

^c UNIVERSITY OF ROSTOCK   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 33; HYDROGEN PEROXIDE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; DISULFIDE BOND; IN VITRO STUDY; MASS SPECTROMETRY; MOLECULAR WEIGHT; NONHUMAN; OXIDATION REDUCTION POTENTIAL; OXIDATIVE STRESS; PEPTIDE MAPPING; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN MODIFICATION; PROTEIN STRUCTURE;

AIR; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; DISULFIDES; HEAT-SHOCK PROTEINS; HYDROGEN PEROXIDE; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; OXIDATION-REDUCTION; PEPTIDE MAPPING; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 0034705402     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M001089200     Document Type: Article

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