Biochemical characterization of CK2α and α′ paralogues and their derived holoenzymes: Evidence for the existence of a heterotrimeric CK2α′-holoenzyme forming trimeric complexes

Molecular and Cellular Biochemistry

Volumn 316, Issue 1-2, 2008, Pages 37-47

  Olsen, Birgitte B ^a   Rasmussen, Tine ^a   Niefind, Karsten ^b   Issinger, Olaf Georg ^a  

^a UNIVERSITY OF SOUTHERN DENMARK   (Denmark)

^b UNIVERSITY OF COLOGNE   (Germany)

Author keywords

Inhibitors; Isozymes; Protein kinase CK2; Substrate

Indexed keywords

APIGENIN; CALMODULIN; CASEIN KINASE II; CASEIN KINASE IIALPHA; EMODIN; HISTIDINE; HOLOENZYME; POLYLYSINE; PROTEIN SERINE THREONINE KINASE INHIBITOR; SODIUM CHLORIDE; MULTIPROTEIN COMPLEX; PROTEIN KINASE INHIBITOR;

ARTICLE; CATALYSIS; COMPLEX FORMATION; CONCENTRATION RESPONSE; CONTROLLED STUDY; ELUTION; ENZYME INACTIVATION; ENZYME PHOSPHORYLATION; ENZYME PURIFICATION; ENZYME SUBSTRATE; ENZYME SUBUNIT; ESCHERICHIA COLI; GEL FILTRATION; HIGH TEMPERATURE PROCEDURES; HUMAN; IC 50; INCUBATION TIME; INSECT CELL; MOLECULAR WEIGHT; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; SENSITIVITY ANALYSIS; SEQUENCE ALIGNMENT; AMINO ACID SEQUENCE; ANIMAL; AUTORADIOGRAPHY; CELL LINE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG ANTAGONISM; DRUG EFFECT; ENZYME ACTIVATION; GEL CHROMATOGRAPHY; INSECT; ISOLATION AND PURIFICATION; KINETICS; METABOLISM; MOLECULAR GENETICS; PHOSPHORYLATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN QUATERNARY STRUCTURE; SEQUENCE HOMOLOGY; TEMPERATURE;

ESCHERICHIA COLI; HEXAPODA;

AMINO ACID SEQUENCE; ANIMALS; AUTORADIOGRAPHY; CALMODULIN; CASEIN KINASE II; CELL LINE; CHROMATOGRAPHY, GEL; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME ACTIVATION; HOLOENZYMES; INSECTS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIPROTEIN COMPLEXES; PHOSPHORYLATION; PROTEIN KINASE INHIBITORS; PROTEIN STRUCTURE, QUATERNARY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SODIUM CHLORIDE; TEMPERATURE;

EID: 50649118318     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-008-9824-3     Document Type: Article

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