S-glutathionylation at Cys328 and Cys542 impairs STAT3 phosphorylation

ACS Chemical Biology

Volumn 9, Issue 8, 2014, Pages 1885-1893

  Butturini, Elena ^a   Darra, Elena ^a   Chiavegato, Giulia ^a   Cellini, Barbara ^a   Cozzolino, Flora ^b   Monti, Maria ^b   Pucci, Piero ^b   Dell'Orco, Daniele ^a   Mariotto, Sofia ^a  

^a UNIVERSITY OF VERONA   (Italy)

^b UNIVERSITY OF NAPLES FEDERICO II   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DIAMIDE; DITHIOTHREITOL; GLUTATHIONE; RECOMBINANT PROTEIN; STAT3 PROTEIN; THIOL GROUP; TYROSINE; STAT3 PROTEIN, HUMAN;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DISULFIDE BOND; ENZYME ASSAY; HELA CELL LINE; HUMAN; HUMAN CELL; IN VITRO STUDY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN DOMAIN; PROTEIN MODIFICATION; PROTEIN PHOSPHORYLATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; REGULATORY MECHANISM; S GLUTATHIONYLATION; SITE DIRECTED MUTAGENESIS; TANDEM MASS SPECTROMETRY; WESTERN BLOTTING; X RAY CRYSTALLOGRAPHY; CHEMISTRY; MASS SPECTROMETRY; METABOLISM; PHOSPHORYLATION;

CYSTEINE; GLUTATHIONE; HELA CELLS; HUMANS; OXIDATION-REDUCTION; PHOSPHORYLATION; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; STAT3 TRANSCRIPTION FACTOR;

EID: 84906214869     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb500407d     Document Type: Article

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