Glutamate substitutions at a PKA consensus site are consistent with inactivation of calpain by phosphorylation

FEBS Letters

Volumn 542, Issue 1-3, 2003, Pages 115-118

  Smith, Scott D ^a   Jia, Zongchao ^a   Huynh, Kassidy K ^a   Wells, Alan ^b   Elce, John S ^a  

^a QUEEN S UNIVERSITY   (Canada)

^b UNIVERSITY OF PITTSBURGH SCHOOL OF MEDICINE   (United States)

Author keywords

Calpain phosphorylation; Calpain regulation; Cyclic adenosine monophosphate dependent kinase; Extracellular signal regulated kinase

Indexed keywords

ASPARTIC ACID; CALPAIN; CYCLIC AMP DEPENDENT PROTEIN KINASE; GLUTAMIC ACID; PHOSPHATE; SERINE; THREONINE;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME LOCALIZATION; ESCHERICHIA COLI; GENE MUTATION; MAMMAL; MUTANT; NONHUMAN; PRIORITY JOURNAL; PROBABILITY; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; REDUCTION; REGULATORY MECHANISM; WILD TYPE;

ESCHERICHIA COLI; MAMMALIA;

EID: 0038405008     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(03)00361-2     Document Type: Article

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