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ATP + [peptide HMRSAMSGLHLVKRR]
ADP + [peptide HMRSAMSGLHLVKRR] phosphate
i.e. SAMS peptide
-
-
?
ATP + 3-hydroxy-3-methyl-glutaryl-CoA reductase
ADP + [3-hydroxy-3-methyl-glutaryl-CoA reductase]phosphate
-
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + phosphorylated acetyl-CoA carboxylase
-
phosphorylation at Ser79
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase] phosphate
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase]phosphate
-
-
-
-
?
ATP + acetyl-CoA carboxylase 1
ADP + phosphorylated acetyl-CoA carboxylase 1
-
-
-
-
?
ATP + adipose hormone-sensitive lipase
ADP + [adipose hormone-sensitive lipase] phosphate
-
-
-
-
?
ATP + bovine serum albumin
ADP + [bovine serum albumin] phosphate
-
fraction V
-
-
?
ATP + casein
ADP + casein phosphate
-
relative kinase activity for low-MW kinase 8%, high MW-kinase 48%
-
-
?
ATP + dephospho-alpha,beta-tubulin
ADP + [alpha,beta-tubulin] phosphate
-
relative kinase activity high MW-kinase 15%
-
-
?
ATP + dephospho-beta-tubulin
ADP + [beta-tubulin]phosphate
-
-
-
-
?
ATP + glycerophosphate acyltransferase
ADP + [glycerophosphate acyltransferase]phosphate
-
-
-
-
?
ATP + glycogen synthase
ADP + [glycogen synthase] phosphate
-
relative kinase activity for low-MW kinase 7%, high MW-kinase 87%
-
-
?
ATP + heavy meromyosin
ADP + [heavy meromyosin] phosphate
-
relative kinase activity for low-MW kinase 2%, high MW-kinase 100%
-
-
?
ATP + histone 2A
?
-
-
-
-
?
ATP + histone H1
ADP + phosphohistone H1
-
-
-
-
?
ATP + histone H1 (IIIS)
ADP + [histone H1 (IIIS)] phosphate
-
histones are better substrates for high-MW kinase than hydroxymethylglutaryl-CoA reductase, relative kinase activity for low-MW kinase 275%, high MW-kinase 103%
-
-
?
ATP + histone II-S
ADP + [histone II-S] phosphate
-
relative kinase activity for low-MW kinase 38%, high MW-kinase 159%
-
-
?
ATP + histone VIIIS
ADP + [histone VIIIS] phosphate
-
relative kinase activity for low-MW kinase 65%, high MW-kinase 141%
-
-
?
ATP + HMRSAMSGLHLVKRR
ADP + ?
ATP + hormone-sensitive lipase
ADP + phosphorylated hormone-sensitive lipase
ATP + MAP-2
ADP + MAP-2 phosphate
-
relative kinase activity for low-MW kinase 14%, high MW-kinase 566%
-
-
?
ATP + myelin basic protein
ADP + [myelin basic protein] phosphate
-
moderate substrate for low-MW kinase, better than hydroxymethylglutaryl-CoA reductase for high-MW kinase, relative kinase activity for low-MW kinase 36%, high MW-kinase 238%
-
-
?
ATP + myosin mixed light chains
ADP + [myosin mixed light chains] phosphate
-
relative kinase activity for low-MW kinase 4%, high MW-kinase 27%
-
-
?
ATP + peptide SAMS
ADP + phosphorylated peptide SAMS
-
-
-
-
?
ATP + phosphorylase B
ADP + [phosphorylase B] phosphate
-
relative kinase activity high MW-kinase 12%
-
-
?
ATP + phosvitin
ADP + phosvitin phosphate
-
relative kinase activity for low-MW kinase 2%, high MW-kinase 2%
-
-
?
ATP + protamine
ADP + protamine phosphate
-
relative kinase activity for low-MW kinase 24%, high MW-kinase 38%
-
-
?
ATP + protein GFAP
ADP + [protein GFAP]phosphate
-
-
-
-
?
ATP + protein NF-L
ADP + [protein NF-L]phosphate
-
-
-
-
?
ATP + rabbit muscle glycogen synthase
ADP + [rabbit muscle glycogen synthase] phosphate
-
rabbit muscle glycogen synthase
-
-
?
ATP + recombinant human Kv1.5 channel
ADP + phosphorylated recombinant human Kv1.5 channel
-
-
-
-
?
ATP + synapsin 1
ADP + [synapsin 1] phosphate
-
as good substrate as hydroxymethylglutaryl-CoA reductase, relative kinase activity for low-MW kinase 151%, high MW-kinase 103%
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
ATP + [glucose hexokinase regulatory protein]
ADP + [glucose hexokinase regulatory protein] phosphate
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
ATP + [malonylCoAdecarboxylase]
ADP + [malonylCoAdecarboxylase]phosphate
-
-
-
-
?
ATP + [peptide HMRSAMSGLHLVKRR]
ADP + [peptide HMRSAMSGLHLVKRR] phosphate
ATP + [peptide QKFQRELSTKWVLN]
ADP + [peptide QKFQRELSTKWVLN] phosphate
-
a peptide derived from glucose hexokinase regulatory protein, residues 474-487
-
-
?
ATP + [peptide SAMS]
ADP + [peptide SAMS] phosphate
-
-
-
-
?
ATP + [sn-glycerol-3-phosphate acyltransferase]
ADP + [sn-glycerol-3-phosphate acyltransferase]phosphate
-
-
-
-
?
CTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
CDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
dATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
dADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
phosphorylation at about 90% the rate of ATP
-
-
?
GTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
GDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
ITP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
IDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
UTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
UDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
additional information
?
-
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase] phosphate
-
substrate Rattus norvegicus hepatic acetyl-CoA carboxylase, enzyme phosphorylates Ser-residues 79, 1200 and 1215
-
?
ATP + HMRSAMSGLHLVKRR
ADP + ?
-
-
-
-
?
ATP + HMRSAMSGLHLVKRR
ADP + ?
-
acetyl-CoA carboxylase-derived synthetic peptide substrate
-
-
?
ATP + hormone-sensitive lipase
ADP + phosphorylated hormone-sensitive lipase
-
-
-
-
?
ATP + hormone-sensitive lipase
ADP + phosphorylated hormone-sensitive lipase
-
HSL is a key enzyme in controlling lipolysis in adipocytes, phosphorylation at Ser565 by AMPK reduces its translocation toward lipid droplets
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylation at Ser79
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
copper deficiency results in AMP-activated protein kinase activation and acetyl-CoA carboxylase phosphorylation in rat cerebellum, overview
-
-
?
ATP + [glucose hexokinase regulatory protein]
ADP + [glucose hexokinase regulatory protein] phosphate
-
-
-
-
?
ATP + [glucose hexokinase regulatory protein]
ADP + [glucose hexokinase regulatory protein] phosphate
-
phosphorylation by AMPK at a site in residues 474-487
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
activated AMPK acts to down-regulate ATP-consuming pathways such as fatty acid synthesis by phosphorylating and inactivating acetyl-CoA carboxylase and protein synthesis by promoting the phosphorylation of eukaryotic elongation factor-2, in heart AMPK activation stimulates glycolysis by increasing glucose uptake
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
bicyclic phosphorylation system, enzyme is believed to be involved in protecting cells against ATP depletion due to environmental stress by inactivating several key biosynthetic enzymes
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [peptide HMRSAMSGLHLVKRR]
ADP + [peptide HMRSAMSGLHLVKRR] phosphate
-
i.e. SAMS peptide
-
-
?
ATP + [peptide HMRSAMSGLHLVKRR]
ADP + [peptide HMRSAMSGLHLVKRR] phosphate
i.e. SAMS peptide
-
-
?
GTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
GDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
GTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
GDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
phosphorylation at about 30% the rate of ATP
-
-
?
ITP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
IDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
ITP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
IDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
phosphorylation at about 10% the rate of ATP
-
-
?
UTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
UDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
UTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
UDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
phosphorylation at about 5% the rate of ATP
-
-
?
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
?
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
?
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
?
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
?
additional information
?
-
-
autophosphorylation in absence of substrate
-
-
?
additional information
?
-
-
autophosphorylation in absence of substrate
-
-
?
additional information
?
-
-
protein kinase C and Ca2+/calmodulin dependent reductase kinases are no substrates
-
-
?
additional information
?
-
-
incorporates 0.5 mol phosphate/mol MW 53000 enzyme substrate fragment, 2 mol phosphate/mol native enzyme substrate
-
-
?
additional information
?
-
-
acetyl-CoA carboxylase kinase EC 2.7.1.128 and hydroxymethylglutaryl-CoA reductase kinase activity are catalyzed by the same enzyme
-
-
?
additional information
?
-
-
regulates triacylglycerolsynthesis and fatty acid oxidation in liver and muscle reciprocally
-
-
?
additional information
?
-
-
AMPK regulation, AMPK mediates the autophagy suppression of okadaic acid and other protein phosphatase-inhibitory toxins, overview
-
-
?
additional information
?
-
-
mechanism of lipolytic enzyme activity modulation, regulation, overview
-
-
?
additional information
?
-
-
the enzyme is regulated by the nucleoside diphosphate kinase, complex formation in vivo, e.g. between isozyme alpha1 and NDPK-H1, inhibits the enzyme, overview
-
-
?
additional information
?
-
-
activation of AMPK leads to activation of PKC-zeta and promotes Na,K-ATPase endocytosis. AMPK mediates CO2-induced Na,K-ATPase endocytosis and alveolar epithelial dysfunction, which can be prevented with beta-adrenergic agonists and cAMP
-
-
?
additional information
?
-
-
AMP-activated protein kinase acts as a master regulator of cellular metabolism in skeletal muscle, biochemical regulation of AMPK by AMP, protein phosphatases, and its three known upstream kinases, LKB1, Ca2+/calmodulin-dependent protein kinase kinase, CaMKK, and transforming growth factor-beta activated kinase 1, TAK1. Physiological regulation of cellular metabolism in skeletal muscle, concerning glucose metabolism, glycogen synthesis, protein metabolism and degradation, lipid metabolism and lipolysis, detailed overview
-
-
?
additional information
?
-
-
AMP-activated protein kinase is essential for survival in chronic hypoxia
-
-
?
additional information
?
-
-
AMPK inhibits hepatioc lipogenesis through multisite control, involving inhibition of glucose hexokinase translocation with consequent inhibition of flux through glucose phosphorylation and glycolysis, overview
-
-
?
additional information
?
-
-
AMPK is a cellular energy sensor that is activated during mitochondrial inhibition and shuts down biosynthetic processes to help conserve cellular ATP levels
-
-
?
additional information
?
-
-
AMPK plays a central role in the regulation of lipid metabolism, AMPK activity may have an important role in the development of alcoholic fatty liver, AMPK activator AICAR strongly inhibits the activity of acetyl-CoA carboxylase in hepatocyte preparations in parallel to fatty acid synthesis, but cells from ethanol-fed rats show significantly lower sensitivity to inhibition by AICAR, overview
-
-
?
additional information
?
-
-
AMPK regulates the energy balance both at the cellular and whole body level, disorders of it are obesity, type 2 diabetes and the metabolic syndrome, overview. Activating mutations in AMPK can cause heart disease. AMPK is regulated by the AMP/ATP ratio and upstream kinases, e.g. CaMKKbeta and LBK1, overview. AMPK activation inhibits activation of the mammalian target-of-rapamycin pathway by the insulin/insulin-like growth factor-1 pathway, probably via phosphorylation of TSC2, an upstream regulator of mTOR
-
-
?
additional information
?
-
-
anti-obesity effects of Juniperus chinensis extract are associated with increased AMP-activated protein kinase expression and phosphorylation in the visceral adipose tissue, overview
-
-
?
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
?
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
?
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
?
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
?
additional information
?
-
-
hypoxic pulmonary vasoconstriction is precipitated, at least in part, by the inhibition of mitochondrial oxidative phosphorylation by hypoxia, an increase in the AMP/ATP ratio and consequent activation of AMP-activated protein kinase, mechanism, overview
-
-
?
additional information
?
-
-
key role for AMP-activated protein kinase in the ventromedial hypothalamus in regulating counterregulatory hormone responses to acute hypoglycemia
-
-
?
additional information
?
-
-
neuronal AMPK responds to cellular energy requirements as well as whole body energy demands, mechanism, in patholgical brain AMPK responds globally in the brain to energy challenge, while in healthy brain only to changes in energy balance/food/intake, increased AMPK activity leads to inhibition of energy-using processes and, during ischemia, can lead to complete energy failure and death by stroke, overview. AMPK mediates the physiological effects of C75, an alpha-methylene-gamma-butyrolactone beta-ketoacyl synthase inhibitor, brain injection of C75 increases ATP levels in neurons, glucose oxidation FAS activity, CPT-1 activity, food intake and body weight in rodents, detailed overview
-
-
?
additional information
?
-
-
the thrifty metabolism that favors fat storage after caloric restriction involves AMPK activity, AMPK signaling is diminished during refeeding after caloric restriction rats. Isocaloric refeeding with a high-fat diet, which exacerbates the suppression of thermogenesis, results in further reduction and in impaired AMPK phosphorylation, overview
-
-
?
additional information
?
-
-
AMPK promotes reactivation of mitochondrial aconitase
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + acetyl-CoA carboxylase 1
ADP + phosphorylated acetyl-CoA carboxylase 1
-
-
-
-
?
ATP + hormone-sensitive lipase
ADP + phosphorylated hormone-sensitive lipase
-
HSL is a key enzyme in controlling lipolysis in adipocytes, phosphorylation at Ser565 by AMPK reduces its translocation toward lipid droplets
-
-
?
ATP + recombinant human Kv1.5 channel
ADP + phosphorylated recombinant human Kv1.5 channel
-
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
ATP + [glucose hexokinase regulatory protein]
ADP + [glucose hexokinase regulatory protein] phosphate
-
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
additional information
?
-
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylation at Ser79
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
copper deficiency results in AMP-activated protein kinase activation and acetyl-CoA carboxylase phosphorylation in rat cerebellum, overview
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
activated AMPK acts to down-regulate ATP-consuming pathways such as fatty acid synthesis by phosphorylating and inactivating acetyl-CoA carboxylase and protein synthesis by promoting the phosphorylation of eukaryotic elongation factor-2, in heart AMPK activation stimulates glycolysis by increasing glucose uptake
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
bicyclic phosphorylation system, enzyme is believed to be involved in protecting cells against ATP depletion due to environmental stress by inactivating several key biosynthetic enzymes
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
?
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
?
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
?
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
?
additional information
?
-
-
AMPK regulation, AMPK mediates the autophagy suppression of okadaic acid and other protein phosphatase-inhibitory toxins, overview
-
-
?
additional information
?
-
-
mechanism of lipolytic enzyme activity modulation, regulation, overview
-
-
?
additional information
?
-
-
activation of AMPK leads to activation of PKC-zeta and promotes Na,K-ATPase endocytosis. AMPK mediates CO2-induced Na,K-ATPase endocytosis and alveolar epithelial dysfunction, which can be prevented with beta-adrenergic agonists and cAMP
-
-
?
additional information
?
-
-
AMP-activated protein kinase acts as a master regulator of cellular metabolism in skeletal muscle, biochemical regulation of AMPK by AMP, protein phosphatases, and its three known upstream kinases, LKB1, Ca2+/calmodulin-dependent protein kinase kinase, CaMKK, and transforming growth factor-beta activated kinase 1, TAK1. Physiological regulation of cellular metabolism in skeletal muscle, concerning glucose metabolism, glycogen synthesis, protein metabolism and degradation, lipid metabolism and lipolysis, detailed overview
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additional information
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AMP-activated protein kinase is essential for survival in chronic hypoxia
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?
additional information
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AMPK inhibits hepatioc lipogenesis through multisite control, involving inhibition of glucose hexokinase translocation with consequent inhibition of flux through glucose phosphorylation and glycolysis, overview
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additional information
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AMPK is a cellular energy sensor that is activated during mitochondrial inhibition and shuts down biosynthetic processes to help conserve cellular ATP levels
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additional information
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AMPK plays a central role in the regulation of lipid metabolism, AMPK activity may have an important role in the development of alcoholic fatty liver, AMPK activator AICAR strongly inhibits the activity of acetyl-CoA carboxylase in hepatocyte preparations in parallel to fatty acid synthesis, but cells from ethanol-fed rats show significantly lower sensitivity to inhibition by AICAR, overview
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additional information
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AMPK regulates the energy balance both at the cellular and whole body level, disorders of it are obesity, type 2 diabetes and the metabolic syndrome, overview. Activating mutations in AMPK can cause heart disease. AMPK is regulated by the AMP/ATP ratio and upstream kinases, e.g. CaMKKbeta and LBK1, overview. AMPK activation inhibits activation of the mammalian target-of-rapamycin pathway by the insulin/insulin-like growth factor-1 pathway, probably via phosphorylation of TSC2, an upstream regulator of mTOR
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additional information
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anti-obesity effects of Juniperus chinensis extract are associated with increased AMP-activated protein kinase expression and phosphorylation in the visceral adipose tissue, overview
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additional information
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cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
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?
additional information
?
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cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
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-
?
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
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?
additional information
?
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cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
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?
additional information
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hypoxic pulmonary vasoconstriction is precipitated, at least in part, by the inhibition of mitochondrial oxidative phosphorylation by hypoxia, an increase in the AMP/ATP ratio and consequent activation of AMP-activated protein kinase, mechanism, overview
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additional information
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key role for AMP-activated protein kinase in the ventromedial hypothalamus in regulating counterregulatory hormone responses to acute hypoglycemia
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additional information
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neuronal AMPK responds to cellular energy requirements as well as whole body energy demands, mechanism, in patholgical brain AMPK responds globally in the brain to energy challenge, while in healthy brain only to changes in energy balance/food/intake, increased AMPK activity leads to inhibition of energy-using processes and, during ischemia, can lead to complete energy failure and death by stroke, overview. AMPK mediates the physiological effects of C75, an alpha-methylene-gamma-butyrolactone beta-ketoacyl synthase inhibitor, brain injection of C75 increases ATP levels in neurons, glucose oxidation FAS activity, CPT-1 activity, food intake and body weight in rodents, detailed overview
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additional information
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the thrifty metabolism that favors fat storage after caloric restriction involves AMPK activity, AMPK signaling is diminished during refeeding after caloric restriction rats. Isocaloric refeeding with a high-fat diet, which exacerbates the suppression of thermogenesis, results in further reduction and in impaired AMPK phosphorylation, overview
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2',3',5'-tri-O-acetyl-N-(3-hydroxyphenyl)adenosine
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EC50 of 0.3273 mM
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5-amino-4-imidazolecarboxamide ribonucleoside
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-
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5-amino-4-imidazolecarboxamide ribotide
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-
5-aminoimidazole-4-carboxamide 1-beta-D-ribofuranoside
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i.e. AICAR, the pharmacological compound transported into cells by the adenosine transporter, and then metabolized by the enzyme adenosine kinase into 5-aminoimidazole-4-carboxamide 1-b-D-ribofuranosyl monophosphate, ZMP, an AMP analogue, which then functions like endogenous AMP by binding to the Bateman domains of AMPK and promoting allosteric activation of the kinase, AICAR does not alter endogenous levels of AMP or ATP, ZMP might prevent the dephosphorylation of AMPK by inhibition of AMP-sensitive phosphatase
5-aminoimidazole-4-carboxamide ribonucleoside
5-aminoimidazole-4-carboxamide riboside
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
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i.e. AICAR, activates the phosphorylation of peptide QKFQRELSTKWVLN 4fold, kinetics, overview
alpha,beta-methylene-ADP
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allosteric activator, can replace ADP, with 66% efficiency with bovine serum albumin as substrate
Ca2+/calmodulin-dependent protein kinase kinase
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i.e. CaMKKalpha/beta, increases AMPK activity regulating AMPK in a Ca2+/calmodulin-dependent, AMP-independent manner, overview
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Calmodulin
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activation of AMPK is mediated by a CO2-triggered increase in intracellular Ca2+ concentration and Ca2+/calmodulin-dependent kinase kinase-beta, CaMKK-beta
calyculin A
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stimulation of activating AMPK phosphorylation at Thr172, independent of narigin
CaMKKbeta
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phosphorylates
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cantharidin
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stimulation of activating AMPK phosphorylation at Thr172, independent of narigin
CDP
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allosteric activator
compound C
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inhibits AMPK and phase II, but not phase I, of hypoxic pulmonary vasoconstriction
corticosterone
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counteracts inhibiting effect of sucrose and increases hypothalamic AMPK activity to levels comparable with saline-drinking animals
dexamethasone
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induces increase in AMPK in primary rat hypothalamic cell cultures, suggesting a direct effect of glucocorticoids on AMPK activity
Diethylamine NONOate
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nitric oxide donor, stimulates rapid and transient AMPK phosphorylation in INS832/13 cells and islets
dinitrophenol
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a cellular metabolic poison that activates AMPK in numerous cell types, including skeletal muscle, mechanism, overview
glucocorticoid
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treatment inhibits AMPK activity in rat adipose tissue and heart, while stimulating it in the liver and hypothalamus, similar to activity in vitro in the primary adipose and hypothalamic cells
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Insulin
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insulin-induced hypoglycaemia in rats increases AMPK phosphorylation and alpha2AMPK activity in the arcuate nucleus/dorso-mediobasal hypothalamus and paraventricular nucleus
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interleukin-1
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induces nitric oxide-dependent activation of AMPK
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microcystin-LR
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stimulation of activating AMPK phosphorylation at Thr172
N-(3-hydroxyphenyl)adenosine
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activates the enzyme with 1.4fold maximal activity at 0.001 mM
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nitric oxide
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AMPK is transiently activated by nitric oxide in insulinoma cells and rat islets following interleukin-1 treatment or by the exogenous addition of nitric oxide
okadaic acid
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stimulation of activating AMPK phosphorylation at Thr172, activation is antagonized by naringin
pioglitazone
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i.e. 5-((4-(2-(5-ethyl-2-pyridinyl)ethoxy)-phenyl)methyl)-(+)-2,4-thiazolidinedione, a drug that is used to treat type 2 diabetes, a thiazolidinedione, reduces blood glucose levels in rodents via activation of AMPK in skeletal muscle
Reductase kinase kinase
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resveratrol
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resveratrol exerts anti-hypertrophic effects by activating AMPK via LKB1 and inhibiting Akt, thus suppressing protein synthesis and gene transcription. Level of phosphorylated AMPK is significantly increased in resveratrol-treated cardiac myocytes in the absence or presence of phenylephrine
rotenone
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a cellular metabolic poison that activates AMPK in numerous cell types, including skeletal muscle, mechanism, overview
tautomycin
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stimulation of activating AMPK phosphorylation at Thr172, independent of narigin
UDP
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allosteric activator
[([5-(5-oxo-4,5-dihydro-1,2-oxazol-3-yl)furan-2-yl]phosphoryl)bis(oxy)methylene]bis(2-methylpropanoate)
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i.e. C13
5'-AMP
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490912, 491403, 644957, 644959, 644961, 644964, 644967, 644977, 644978, 644985, 644988
5'-AMP
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regulated by allosteric activation
5'-AMP
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the gamma subunit of AMPK contains adenine nucleotide binding sites that facilitate the direct interaction of AMP with the AMPK heterotrimer. AMP regulates the activity of AMPK via the inhibition of AMPK dephosphorylation by protein phosphatases
5'-AMP
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up to 10fold activation, AMP also promotes net phosphorylation at a critical threonine residue Thr172 within the kinase domain that can generate a further 100fold activation, the combined effect being 1000fold
5-aminoimidazole-4-carboxamide ribonucleoside
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i.e. AICAR
5-aminoimidazole-4-carboxamide ribonucleoside
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AICAR, a potent activator of AMPK. If treated with small to moderate concentrations, embryonic hippocampal neurons cultured in conditions of glucose deprivation have improved survival
5-aminoimidazole-4-carboxamide riboside
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5-aminoimidazole-4-carboxamide riboside
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stimulation of activating AMPK phosphorylation at Thr172
5-aminoimidazole-4-carboxamide riboside
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i.e. AICAR, a specific AMPK activator
5-aminoimidazole-4-carboxamide riboside
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AICAR
5-aminoimidazole-4-carboxamide riboside
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AICAR, activation of the alpha2 isoform of AMPK in response to treatment with the AMPK activator AICAR, is much greater in the glycogen-depleted state
5-aminoimidazole-4-carboxamide riboside
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AICAR, in perfused hindlimb, AICAR induces glucose uptake, that is associated with increased translocation of the glucose transporter, GLUT4, to the plasma membrane. Reduces insulin-stimulated glycogen synthase activity in isolated skeletal muscle. Diminishes ectopic lipid deposition in liver and muscle of Zucker diabetic fatty rats and slows the progression to type 2 diabetes in these animals
5-aminoimidazole-4-carboxamide riboside
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AICAR, increases phosphorylation of acetyl-CoA carboxylase and AMPK in INS832/13 cells
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
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AICAR, activates AMPK, wherby altering the expression of a variety of genes, including those for uncoupling protein (UCP)-3 and GLUT-4 in muscle, and fatty acid synthase and phosphoenolpyruvate carboxykinase in hepatocytes
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
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AICAR, chronic AMPK activation with AICAR decreases blood pressure in rats displaying features of the insulin resistance syndrome
A-769662
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A-769662
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activates the liver enzyme, binds to the enzyme, acts allosterically
A-769662
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small molecule direct activator of AMPK, reduces fatty acid synthesis in primary hepatocytes
ADP
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AMP
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684366, 690726, 691132, 691165, 691556, 692000, 692195, 692267, 692277, 692682, 693207, 693356
AMP
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wild-type is activated about 2fold in the presence of 0.2 mM. The catalytic activity and substrate binding affinity of AMPK are separately regulated by AMP binding and the assembly of beta- and gamma-subunits onto the alpha-subunit
interleukin-6
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activates AMPK in skeletal muscle by increasing the phosphorylation of Thr172 of AMPK
interleukin-6
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directly activates AMPK in vivo and in vitro. Activates AMPK in skeletal muscle by increasing the concentration of cAMP and the AMP:ATP ratio. AMPK activation coincides temporally with a nearly 3fold increase in the AMP:ATP ratio in the extensor digitorum longus
leptin
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leptin
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induces AMPK phosphorylation and activation
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leptin
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the classical adipokine, released from adipocytes, stimulates the alpha2 isoform of AMPK and hence fatty acid oxidation in skeletal muscle
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leptin
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has a tissue-specific effect on AMPK. In the skeletal muscle, it stimulates AMPK activity
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metformin
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metformin
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antidiabetic drug
metformin
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co-administration of dexamethasone and metformin decreases insulin-stimulated glucose uptake compared with metformin alone
metformin
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i.e. N,N-dimethylimidodicarbonimidic diamide, one of the most commonly prescribed drugs for the treatment of type 2 diabetes, increases the activity of AMPK in skeletal muscle, mechanism, loss of TAK1 protein prevents the metformin-induced activation of AMPK, overview
Reductase kinase kinase
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EC 2.7.1.110, activation in presence of MgATP2-
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Reductase kinase kinase
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activation, i.e. EC 2.7.1.110, in the presence of MgATP2-
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rosiglitazone
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antidiabetic drug
rosiglitazone
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i.e. 5-((4-(2-(methyl-2-pyridinylamino)ethoxy)phenyl)methyl)-2,4-thiazol-idinedione, a drug that is used to treat type 2 diabetes, a thiazolidinedione, reduces blood glucose levels in rodents via activation of AMPK in skeletal muscle
additional information
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
additional information
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
additional information
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
additional information
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
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additional information
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no activation by cGMP
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additional information
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no activation by cAMP
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additional information
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no activation by cAMP
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additional information
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not activated by cAMP
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additional information
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not activated by cAMP
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additional information
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no activation by cIMP, cCMP
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additional information
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activated by phosphorylation by upstream protein kinases AMPKK and CaMKIK
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additional information
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AMPK can also be activated by hyperosmotic stress
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additional information
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stimulation by protein phosphatase-inhibitory toxins
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additional information
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activating phosphorylation of AMPK at Thr172 of the alpha-subunit, e.g. by CaMKKbeta or LBK1, inhibiting dephosphorylation by phosphatase PP2C
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additional information
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AMPKalpha needs to be activated by phosphorylation on Thr172. Reactive oxygen species contribute to AMPK activation, mechanism, overview
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additional information
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anti-obesity effects of Juniperus chinensis extract are associated with increased AMP-activated protein kinase expression and phosphorylation in the visceral adipose tissue, overview
-
additional information
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
additional information
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
additional information
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
additional information
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
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additional information
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phosphorylation of AMPK activates the enzyme
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additional information
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phosphorylation of AMPK at Thr172 of the alpha-subunit activates the enzyme
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additional information
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phosphorylation of AMPK at Thr172 of the alpha-subunit activates the enzyme
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additional information
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phosphorylation of AMPK at Thr172 of the alpha-subunit activates the enzyme, copper deficiency results in AMP-activated protein kinase activation and acetyl-CoA carboxylase phosphorylation in rat cerebellum, overview
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additional information
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the enzyme is activated by phosphorylation at Thr172
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additional information
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AMPK may be sensitive to the lipid status of a cell and activation may be influenced by intracellular fatty acid availability independent of cellular AMP levels
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additional information
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diabetic rats treated with cilostazol, a selective inhibitor of phosphodiesterase 3, exhibit normalization of endothelial function that is linked to AMPK activation producing increased endothelial nitric oxide synthase activity and NO production. In the ischemic heart, both catalytic alpha1-isoform and alpha2-isoform of AMPK containing regulatory gamma1-isoform or gamma2-isoform are activated
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additional information
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elevated phosphorylation of AMPK and R2-GABAB in the hippocampus of a rat ischemic in vivo model
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additional information
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inhibition of intracellular glucose utilisation through the administration of 2-deoxyglucose increases hypothalamic AMPK activity and food intake. Diabetic rats have enhanced AMPK activity, despite their high glucose levels, which should suppress hypothalamic AMPK. Thyroid hormones stimulate AMPK and acetyl-CoA carboxylase expression in skeletal muscle. 1 h of strenuous exercise in rats does not elicit significant changes in hypothalamic AMPK activity despite an increase in plasma ghrelin
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additional information
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adenosine (0.0001-0.5 mM) has no direct stimulating effect on enzyme activity
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Ingebritsen, T.S.; Parker, R.A.; Gibson, D.M.
Regulation of liver hydroxymethylglutaryl-CoA reductase by a bicyclic phosphorylation system
J. Biol. Chem.
256
1138-1144
1981
Rattus norvegicus
brenda
Carling, D.; Clarke, P.R.; Hardie, D.G.
Adenosine monophosphate-activated protein kinase: hydroxymethylglutaryl-CoA reductase kinase
Methods Enzymol.
200
362-371
1991
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Stapleton, D.; Mitchelhill, K.I.; Gao, G.; Widmer, J.; Michell, B.J.; Teh, T.; House, C.M.; Fernandez, C.S.; Cox, T.; Witters, L.A.; Kemp, B.E.
Mammalian AMP-activated protein kinase subfamily
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271
611-614
1996
Homo sapiens, Rattus norvegicus, Sus scrofa
brenda
Beg, Z.H.; Stonik, J.A.; Brewer, H.B.
3-Hydroxy-3-methylglutaryl coenzyme A reductase: regulation of enzymatic activity by phosphorylation and dephosphorylation
Proc. Natl. Acad. Sci. USA
75
3678-3682
1978
Rattus norvegicus
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Ingebritsen, T.S.; Lee, H.S.; Parker, R.A.; Gibson, D.M.
Reversible modulation of the activities of both liver microsomal hydroxymethylglutaryl coenzyme A reductase and its inactivating enzyme. Evidence for regulation by phosphorylation-dephosphorylation
Biochem. Biophys. Res. Commun.
81
1268-1277
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Rattus norvegicus
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Beg, Z.H.; Stonik, J.A.
Reversible inactivation of 3-hydroxy-3-methylglutaryl coenzyme A reductase: reductase kinase and mevalonate kinase are separate enzymes
Biochem. Biophys. Res. Commun.
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1982
Rattus norvegicus
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Ferrer, A.; Hegardt, F.G.
Phosphorylation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by microsomal 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase
Arch. Biochem. Biophys.
230
227-237
1984
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
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Harwood, H.J.; Brandt, K.G.; Rodwell, V.W.
Allosteric activation of rat liver cytosolic 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase by nucleoside diphosphates
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259
2810-2815
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Rattus norvegicus
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Ferrer, A.; Caelles, C.; Massot, N.; Hegardt, F.G.
Activation of rat liver cytosolic 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase by adenosine 5-monophosphate
Biochem. Biophys. Res. Commun.
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497-504
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Rattus norvegicus
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Beg, Z.H.; Stonik, J.A.; Brewer, H.B.
Phosphorylation and modulation of the enzymic activity of native and protease-cleaved purified hepatic 3-hydroxy-3-methylglutaryl-coenzyme A reductase by a calcium/calmodulin-dependent protein kinase
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262
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Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Ferrer, A.; Caelles, C.; Massot, N.; Hegardt, F.G.
Allosteric activation of rat liver microsomal [hydroxymethylglutaryl-CoA reductase (NADPH)]kinase by nucleoside phosphates
Biol. Chem. Hoppe-Seyler
368
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Weekes, J.; Ball, K.L.; Caudwell, F.B.; Hardie, D.G.
Specificity determinants for the AMP-activated protein kinase and its plant homologue analysed using synthetic peptides
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334
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Brassica oleracea, Rattus norvegicus
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Omkumar, R.V.; Darnay, B.G.; Rodwell, V.W.
Modulation of syrian hamster 3-hydroxy-3-methylglutaryl-CoA reductase activity by phosphorylation. Role of serine 871 [published erratum appears in J Biol Chem 1994 Jun 10;269(23):16518]
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Rattus norvegicus
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Henin, N.; Vincent, M.F.; Van den Berghe, G.
Stimulation of rat liver AMP-activated protein kinase by AMP analogues
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Park, H.; Kaushik, V.K.; Constant, S.; Prentki, M.; Przybytkowski, E.; Ruderman, N.B.; Saha, A.K.
Coordinate regulation of malonyl-CoA decarboxylase, sn-glycerol-3-phosphate acyltransferase, and acetyl-CoA carboxylase by AMP-activated protein kinase in rat tissues in response to exercise
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Beg, Z.H.; Stonik, J.A.; Brewer, B.
Characterization and regulation of reductase kinase, a protein kinase that modulates the enzymic activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
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Weekes, J.; Hawley, S.A.; Corton, J.; Shugar, D.; Hardie, D.G.
Activation of rat liver AMP-activated protein kinase by kinase kinase in a purified, reconstituted system. Effects of AMP and AMP analogues
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219
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Beg, Z.H.; Stonik, J.A.; Brewer, B.
In vivo modulation of rat liver 3-hydroxy-3-methylglutaryl-coenzyme A reductase, reductase kinase, and reductase kinase kinase by mevalonolactone
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Rattus norvegicus
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Hawley, S.A.; Selbert, M.A.; Goldstein, E.G.; Edelman, A.M.; Carling, D.; Hardie, D.G.
5'-AMP activates the AMP-activated protein kinase cascade, and Ca2+/calmodulin activates the calmodulin-dependent protein kinase I cascade, via three independent mechanisms
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Rattus norvegicus
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Hawley, S.A.; Davison, M.; Woods, A.; Davies, S.P.; Beri, R.K.; Carling, D.; Hardie, D.G.
Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase
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Woods, A.; Cheung, P.C.; Smith, F.C.; Davison, M.D.; Scott, J.; Beri, R.K.; Carling, D.
Characterization of AMP-activated protein kinase beta and gamma subunits. Assembly of the heterotrimeric complex in vitro
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Functional domains of the a1 catalytic subunit of the AMP-activated protein kinase
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Muoio, D.M.; Seefeld, K.; Witters, L.A.; Coleman, R.A.
AMP-activated kinase reciprocally regulates triacylglycerol synthesis and fatty acid oxidation in liver and muscle: evidence that sn-glycerol-3-phosphate acyltransferase is a novel target
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338
783-791
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Stein, S.C.; Woods, A.; Jones, N.A.; Davison, M.D.; Carling, D.
The regulation of AMP-activated protein kinase by phosphorylation
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-
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Musi, N.; Hayashi, T.; Fujii, N.; Hirshman, M.F.; Witters, L.A.; Goodyear, L.J.
AMP-activated protein kinase activity and glucose uptake in rat skeletal muscle
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280
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Woods, A.; Vertommen, D.; Neumann, D.; Tuerk, R.; Bayliss, J.; Schlattner, U.; Wallimann, T.; Carling, D.; Rider, M.H.
Identification of phosphorylation sites in AMP-activated protein kinase (AMPK) for upstream AMPK kinases and study of their roles by site-directed mutagenesis
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278
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Samari, H.R.; Moeller, M.T.N.; Holden, L.; Asmyhr, T.; Seglen, P.O.
Stimulation of hepatocytic AMP-activated protein kinase by okadaic acid and other autophygy-suppressive toxins
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Crawford, R.M.; Treharne, K.J.; Best, O.G.; Muimo, R.; Riemen, C.E.; Mehta, A
A novel physical and functional association between nucleoside diphosphate kinase A and AMP-activated protein kinase alpha1 in liver and lung
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392
201-209
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Homo sapiens, Rattus norvegicus
brenda
Daval, M.; Diot-Dupuy F.; Bazin, R.; Hainault, I.; Viollet, B.; Vaulont, S.; Hajduch, E.; Ferr, P.; Foufelle, F.
Anti-lipolytic action of AMP-activated protein kinase in rodent adipocytes
J. Biol. Chem.
280
25250-25257
2005
Mus musculus, Rattus norvegicus
brenda
Mukhtar, M.H.; Payne, V.A.; Arden, C.; Harbottle, A.; Khan, S.; Lange, A.J.; Agius, L.
Inhibition of glucokinase translocation by AMP-activated protein kinase is associated with phosphorylation of both GKRP and 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Am. J. Physiol. Regul. Integr. Comp. Physiol.
294
R766-R774
2008
Rattus norvegicus
brenda
Borger, D.R.; Gavrilescu, L.C.; Bucur, M.C.; Ivan, M.; Decaprio, J.A.
AMP-activated protein kinase is essential for survival in chronic hypoxia
Biochem. Biophys. Res. Commun.
370
230-234
2008
Rattus norvegicus
brenda
Garcia-Villafranca, J.; Guillen, A.; Castro, J.
Ethanol consumption impairs regulation of fatty acid metabolism by decreasing the activity of AMP-activated protein kinase in rat liver
Biochimie
90
460-466
2008
Rattus norvegicus
brenda
Kim, S.J.; Jung, J.Y.; Kim, H.W.; Park, T.
Anti-obesity effects of Juniperus chinensis extract are associated with increased AMP-activated protein kinase expression and phosphorylation in the visceral adipose tissue of rats
Biol. Pharm. Bull.
31
1415-1421
2008
Rattus norvegicus
brenda
Gybina, A.A.; Prohaska, J.R.
Copper deficiency results in AMP-activated protein kinase activation and acetyl-CoA carboxylase phosphorylation in rat cerebellum
Brain Res.
1204
69-76
2008
Rattus norvegicus
brenda
Witczak, C.A.; Sharoff, C.G.; Goodyear, L.J.
AMP-activated protein kinase in skeletal muscle: from structure and localization to its role as a master regulator of cellular metabolism
Cell. Mol. Life Sci.
65
3737-3755
2008
Saccharomyces cerevisiae, Homo sapiens, Rattus norvegicus
brenda
McCrimmon, R.J.; Shaw, M.; Fan, X.; Cheng, H.; Ding, Y.; Vella, M.C.; Zhou, L.; McNay, E.C.; Sherwin, R.S.
Key role for AMP-activated protein kinase in the ventromedial hypothalamus in regulating counterregulatory hormone responses to acute hypoglycemia
Diabetes
57
444-450
2008
Rattus norvegicus
brenda
Robertson, T.P.; Mustard, K.J.; Lewis, T.H.; Clark, J.H.; Wyatt, C.N.; Blanco, E.A.; Peers, C.; Hardie, D.G.; Evans, A.M.
AMP-activated protein kinase and hypoxic pulmonary vasoconstriction
Eur. J. Pharmacol.
595
39-43
2008
Rattus norvegicus
brenda
Christ-Crain, M.; Kola, B.; Lolli, F.; Fekete, C.; Seboek, D.; Wittmann, G.; Feltrin, D.; Igreja, S.C.; Ajodha, S.; Harvey-White, J.; Kunos, G.; Mueller, B.; Pralong, F.; Aubert, G.; Arnaldi, G.; Giacchetti, G.; Boscaro, M.; Grossman, A.B.; Korbonits, M.
AMP-activated protein kinase mediates glucocorticoid-induced metabolic changes: a novel mechanism in Cushings syndrome
FASEB J.
22
1672-1683
2008
Homo sapiens, Rattus norvegicus
brenda
Summermatter, S.; Mainieri, D.; Russell, A.P.; Seydoux, J.; Montani, J.P.; Buchala, A.; Solinas, G.; Dulloo, A.G.
Thrifty metabolism that favors fat storage after caloric restriction: a role for skeletal muscle phosphatidylinositol-3-kinase activity and AMP-activated protein kinase
FASEB J.
22
774-785
2008
Rattus norvegicus
brenda
Hardie, D.G.
Role of AMP-activated protein kinase in the metabolic syndrome and in heart disease
FEBS Lett.
582
81-89
2008
Arabidopsis thaliana, Saccharomyces cerevisiae, Caenorhabditis elegans, Dictyostelium discoideum, Drosophila melanogaster, Giardia intestinalis, Homo sapiens, Mus musculus, Physcomitrium patens, Rattus norvegicus, Schizosaccharomyces pombe, Trypanosoma brucei
brenda
Ronnett, G.V.; Aja, S.
AMP-activated protein kinase in the brain
Int. J. Obes.
32
S42-S48
2008
Rattus norvegicus
brenda
Riek, U.; Scholz, R.; Konarev, P.; Rufer, A.; Suter, M.; Nazabal, A.; Ringler, P.; Chami, M.; Mueller, S.A.; Neumann, D.; Forstner, M.; Hennig, M.; Zenobi, R.; Engel, A.; Svergun, D.; Schlattner, U.; Wallimann, T.
Structural properties of AMP-activated protein kinase: dimerization, molecular shape, and changes upon ligand binding
J. Biol. Chem.
283
18331-18343
2008
Rattus norvegicus (P54645), Rattus norvegicus (P80385), Rattus norvegicus (P80386), Rattus norvegicus (Q09137)
brenda
Iseli, T.J.; Oakhill, J.S.; Bailey, M.F.; Wee, S.; Walter, M.; van Denderen, B.J.; Castelli, L.A.; Katsis, F.; Witters, L.A.; Stapleton, D.; Macaulay, S.L.; Michell, B.J.; Kemp, B.E.
AMP-activated protein kinase subunit interactions: beta1:gamma1 association requires beta1 Thr-263 and Tyr-267
J. Biol. Chem.
283
4799-4807
2008
Homo sapiens, Rattus norvegicus
brenda
Vadasz, I.; Dada, L.A.; Briva, A.; Trejo, H.E.; Welch, L.C.; Chen, J.; Toth, P.T.; Lecuona, E.; Witters, L.A.; Schumacker, P.T.; Chandel, N.S.; Seeger, W.; Sznajder, J.I.
AMP-activated protein kinase regulates CO2-induced alveolar epithelial dysfunction in rats and human cells by promoting Na,K-ATPase endocytosis
J. Clin. Invest.
118
752-762
2008
Rattus norvegicus
brenda
Hegarty, B.D.; Turner, N.; Cooney, G.J.; Kraegen, E.W.
Insulin resistance and fuel homeostasis: the role of AMP-activated protein kinase
Acta Physiol. (Oxf.)
196
129-145
2009
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Oakhill, J.S.; Scott, J.W.; Kemp, B.E.
Structure and function of AMP-activated protein kinase
Acta Physiol. (Oxf.)
196
3-14
2009
Saccharomyces cerevisiae, Homo sapiens, Mus musculus, Rattus norvegicus, Schizosaccharomyces pombe, Sus scrofa
brenda
McBride, A.; Hardie, D.G.
AMP-activated protein kinase--a sensor of glycogen as well as AMP and ATP?
Acta Physiol. (Oxf.)
196
99-113
2009
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Zou, M.H.; Wu, Y.
AMP-activated protein kinase activation as a strategy for protecting vascular endothelial function
Clin. Exp. Pharmacol. Physiol.
35
535-545
2008
Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces sp.
brenda
Li, C.; Keaney, J.F.
AMP-activated protein kinase: a stress-responsive kinase with implications for cardiovascular disease
Curr. Opin. Pharmacol.
10
111-115
2010
Saccharomyces cerevisiae, Canis lupus familiaris, Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Kelly, M.; Gauthier, M.S.; Saha, A.K.; Ruderman, N.B.
Activation of AMP-activated protein kinase by interleukin-6 in rat skeletal muscle: association with changes in cAMP, energy state, and endogenous fuel mobilization
Diabetes
58
1953-1960
2009
Rattus norvegicus
brenda
Chan, A.Y.; Dolinsky, V.W.; Soltys, C.L.; Viollet, B.; Baksh, S.; Light, P.E.; Dyck, J.R.
Resveratrol inhibits cardiac hypertrophy via AMP-activated protein kinase and Akt
J. Biol. Chem.
283
24194-24201
2008
Mus musculus, Rattus norvegicus
brenda
Meares, G.P.; Hughes, K.J.; Jaimes, K.F.; Salvatori, A.S.; Rhodes, C.J.; Corbett, J.A.
AMP-activated protein kinase attenuates nitric oxide-induced beta-cell death
J. Biol. Chem.
285
3191-3200
2010
Rattus norvegicus
brenda
Bendayan, M.; Londono, I.; Kemp, B.E.; Hardie, G.D.; Ruderman, N.; Prentki, M.
Association of AMP-activated protein kinase subunits with glycogen particles as revealed in situ by immunoelectron microscopy
J. Histochem. Cytochem.
57
963-971
2009
Rattus norvegicus
brenda
Kola, B.
Role of AMP-activated protein kinase in the control of appetite
J. Neuroendocrinol.
20
942-951
2008
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Chen, L.; Jiao, Z.H.; Zheng, L.S.; Zhang, Y.Y.; Xie, S.T.; Wang, Z.X.; Wu, J.W.
Structural insight into the autoinhibition mechanism of AMP-activated protein kinase
Nature
459
1146-1149
2009
Saccharomyces cerevisiae, Rattus norvegicus, Schizosaccharomyces pombe
brenda
Spasic, M.R.; Callaerts, P.; Norga, K.K.
AMP-activated protein kinase (AMPK) molecular crossroad for metabolic control and survival of neurons
Neuroscientist
15
309-316
2009
Saccharomyces cerevisiae, Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Mobbs, J.I.; Koay, A.; Di Paolo, A.; Bieri, M.; Petrie, E.J.; Gorman, M.A.; Doughty, L.; Parker, M.W.; Stapleton, D.I.; Griffin, M.D.; Gooley, P.R.
Determinants of oligosaccharide specificity of the carbohydrate-binding modules of AMP-activated protein kinase
Biochem. J.
468
245-257
2015
Rattus norvegicus (P80386), Rattus norvegicus (Q9QZH4)
brenda
Gao, F.; Qian, Y.J.; Chen, F.H.; Zhu, H.B.
Comparative analysis of stimulation and binding characteristics of adenosine analogs to AMP-activated protein kinase
J. Asian Nat. Prod. Res.
21
916-927
2019
Rattus norvegicus
brenda
Moral-Sanz, J.; Mahmoud, A.; Ross, F.; Eldstrom, J.; Fedida, D.; Hardie, D.; Evans, A.
AMP-activated protein kinase inhibits Kv1.5 channel currents of pulmonary arterial myocytes in response to hypoxia and inhibition of mitochondrial oxidative phosphorylation
J. Physiol.
594
4901-4915
2016
Rattus norvegicus
brenda
Hermann, R.; Mestre Cordero, V.; Fernandez Pazos, M.; Reznik, F.; Velez, D.; Savino, E.; Marina Prendes, M.; Varela, A.
Differential effects of AMP-activated protein kinase in isolated rat atria subjected to simulated ischemia-reperfusion depending on the energetic substrates available
Pflugers Arch.
470
367-383
2018
Rattus norvegicus
brenda