AMPK: An Energy-Sensing Pathway with Multiple Inputs and Outputs

Trends in Cell Biology

Volumn 26, Issue 3, 2016, Pages 190-201

  Hardie, D Grahame ^a   Schaffer, Bethany E ^b   Brunet, Anne ^b  

^a UNIVERSITY OF DUNDEE   (United Kingdom)

^b STANFORD UNIVERSITY   (United States)

Author keywords

Allosteric activation; AMPK; Energy sensing; Kinase recognition motif; Kinase target identification; Pharmacological activators

Indexed keywords

ADENINE NUCLEOTIDE; ADENOSINE TRIPHOSPHATE; AMP ACTIVATED PROTEIN KINASE GAMMA; BETA CYCLODEXTRIN; CALCIUM ION; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; STAUROSPORINE; UNCLASSIFIED DRUG;

CATABOLISM; CELL ENERGY; CRYSTAL STRUCTURE; ENERGY; ENZYME ACTIVATION; ENZYME REGULATION; ENZYME STRUCTURE; HOMEOSTASIS; HUMAN; LIGAND BINDING; MOLECULAR RECOGNITION; PRIORITY JOURNAL; REVIEW; ALLOSTERISM; AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; ENERGY METABOLISM; ENZYME ACTIVE SITE; PHOSPHORYLATION; PHYSIOLOGY; PROTEIN PROCESSING; SIGNAL TRANSDUCTION;

ALLOSTERIC REGULATION; AMINO ACID SEQUENCE; AMP-ACTIVATED PROTEIN KINASES; ANIMALS; CATALYTIC DOMAIN; ENERGY METABOLISM; ENZYME ACTIVATION; HUMANS; PHOSPHORYLATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; SIGNAL TRANSDUCTION;

EID: 84958120581     PISSN: 09628924     EISSN: 18793088     Source Type: Journal    
DOI: 10.1016/j.tcb.2015.10.013     Document Type: Review

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