Phenylarsine oxide binding reveals redox-active and potential regulatory vicinal thiols on the catalytic subunit of protein phosphatase 2A

Neurochemical Research

Volumn 36, Issue 2, 2011, Pages 232-240

  Foley, Timothy D ^a   Melideo, Scott L ^a   Healey, Adriana E ^a   Lucas, Eugene J ^a   Koval, Jason A ^a  

^a UNIVERSITY OF SCRANTON   (United States)

Author keywords

Disulfide bonds; Oxidative stress; Phenylarsine oxide; Protein phosphatase 2A

Indexed keywords

ARSENOSOBENZENE; DITHIOTHREITOL; PHOSPHOPROTEIN PHOSPHATASE 2A; THIOL DERIVATIVE;

AFFINITY CHROMATOGRAPHY; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME REGULATION; FRACTIONATION; IN VITRO STUDY; NONHUMAN; OXIDATION; OXIDATION REDUCTION POTENTIAL; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PRIORITY JOURNAL; RAT; REGULATORY MECHANISM;

ANIMALS; ARSENICALS; BRAIN; DISULFIDES; DITHIOTHREITOL; ENZYME INHIBITORS; OXIDATION-REDUCTION; PROTEIN BINDING; PROTEIN PHOSPHATASE 2; PROTEIN SUBUNITS; RATS; RATS, SPRAGUE-DAWLEY; SULFHYDRYL COMPOUNDS;

RATTUS;

EID: 78751635809     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11064-010-0310-4     Document Type: Article

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