Protection of GroEL by its methionine residues against oxidation by hydrogen peroxide

Biochemical and Biophysical Research Communications

Volumn 347, Issue 2, 2006, Pages 534-539

  Melkani, Girish C ^a   Kestetter, Justin ^a   Sielaff, Robin ^a   Zardeneta, Gustavo ^b   Mendoza, Jose A ^a  

^a CALIFORNIA STATE UNIVERSITY   (United States)

^b UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO   (United States)

Author keywords

Chaperone activity; GroEL; Methionine oxidation; Oxidative stress; Refolding

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CARBOXYL GROUP; CHAPERONE; CHAPERONIN; CYANOGEN BROMIDE; CYSTEINE; HYDROGEN PEROXIDE; METHIONINE; THIOSULFATE SULFURTRANSFERASE; TYROSINE; UREA;

ANTIOXIDANT ACTIVITY; ARTICLE; BIOLOGY; CARBOXY TERMINAL SEQUENCE; CONCENTRATION (PARAMETERS); FLUORESCENCE; HYDROLYSIS; INCUBATION TIME; OXIDATION KINETICS; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN QUATERNARY STRUCTURE;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; CIRCULAR DICHROISM; CYSTEINE; DOSE-RESPONSE RELATIONSHIP, DRUG; GROEL PROTEIN; HYDROGEN PEROXIDE; HYDROLYSIS; METHIONINE; MOLECULAR CHAPERONES; OXIDANTS; OXIDATION-REDUCTION; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; THIOSULFATE SULFURTRANSFERASE; TYROSINE;

EID: 33745924414     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.06.136     Document Type: Article

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