A common phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation

Molecular Cell

Volumn 7, Issue 6, 2001, Pages 1321-1327

  Frame, Sheelagh ^a   Cohen, Philip ^a   Biondi, Ricardo M ^a  

^a UNIVERSITY OF DUNDEE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE KINASE; AXIN; BETA CATENIN; GLYCOGEN SYNTHASE; GLYCOGEN SYNTHASE KINASE 3; GLYCOGEN SYNTHASE KINASE 3 INHIBITOR; GLYCOGEN SYNTHASE KINASE 3BETA; INSULIN; MUTANT PROTEIN; PHOSPHATE; PROTEIN KINASE B; PROTEIN KINASE INHIBITOR; PROTEIN SERINE KINASE; UNCLASSIFIED DRUG; WNT PROTEIN;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BINDING SITE; CONTROLLED STUDY; DIABETES MELLITUS; DRUG DESIGN; EMBRYO; ENZYME INACTIVATION; ENZYME INHIBITION; ENZYME PHOSPHORYLATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; HUMAN; HUMAN CELL; KIDNEY CELL; NONHUMAN; PROTEIN PROTEIN INTERACTION; RABBIT;

ANIMALIA; ORYCTOLAGUS CUNICULUS;

EID: 0034969088     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(01)00253-2     Document Type: Article

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