Large unphosphorylated aggregates as the active form of hsp27 which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNFα in NIH-3T3-ras cells

Biochemical and Biophysical Research Communications

Volumn 241, Issue 1, 1997, Pages 187-192

  Mehlen, Patrick ^a   Hickey, Eilen ^b   Weber, Lee A ^b   Arrigo, André Patrick ^a,c  

^a CNRS   (France)

^b UNIVERSITY OF NEVADA   (United States)

^c CENTRE DE GÉNÉTIQUE MOLÉCULAIRE ET CELLULAIRE   (France)

Author keywords

Cell death; Glutathione; hsp27; Oxygen species; Phosphorylation mutant; Reactive; TNF

Indexed keywords

ALANINE; ASPARTIC ACID; GLUTATHIONE; GLYCINE; HEAT SHOCK PROTEIN 27; MUTANT PROTEIN; REACTIVE OXYGEN METABOLITE; SERINE; TUMOR NECROSIS FACTOR ALPHA;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CELL STRAIN 3T3; CONTROLLED STUDY; MOUSE; NONHUMAN; ONCOGENE RAS; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; STRUCTURE ACTIVITY RELATION;

ANIMALIA; MAMMALIA;

EID: 0007404243     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.1997.7635     Document Type: Article

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