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Volumn 397, Issue 2-3, 1996, Pages 347-351
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The α1 and α2 isoforms of the AMP-activated protein kinase have similar activities in rat liver but exhibit differences in substrate specificity in vitro
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Author keywords
AMP activated protein kinase; Consensus sequence; Specificity determinant; Subunit isoform
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Indexed keywords
ADENOSINE PHOSPHATE;
PROTEIN KINASE;
5' AMP ACTIVATED PROTEIN KINASE;
5'-AMP-ACTIVATED PROTEIN KINASE;
COMPLEMENTARY DNA;
ISOENZYME;
MULTIENZYME COMPLEX;
OLIGOPEPTIDE;
PROTEIN SERINE THREONINE KINASE;
ANIMAL TISSUE;
ARTICLE;
ENZYME SPECIFICITY;
IN VITRO STUDY;
LIVER;
NONHUMAN;
PRIORITY JOURNAL;
AMINO ACID SEQUENCE;
ANIMAL;
CELL LINE;
COMPARATIVE STUDY;
ENZYMOLOGY;
GENETIC TRANSFECTION;
GENETICS;
KINETICS;
METABOLISM;
MOLECULAR GENETICS;
PHOSPHORYLATION;
RAT;
AMINO ACID SEQUENCE;
ANIMALS;
CELL LINE;
DNA, COMPLEMENTARY;
ISOENZYMES;
KINETICS;
LIVER;
MOLECULAR SEQUENCE DATA;
MULTIENZYME COMPLEXES;
OLIGOPEPTIDES;
PHOSPHORYLATION;
PROTEIN KINASES;
PROTEIN-SERINE-THREONINE KINASES;
RATS;
SUBSTRATE SPECIFICITY;
TRANSFECTION;
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EID: 0030592623
PISSN: 00145793
EISSN: None
Source Type: Journal
DOI: 10.1016/S0014-5793(96)01209-4 Document Type: Article |
Times cited : (237)
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References (18)
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