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Salicylate activates the AMP-activated protein kinase (AMPK (show PRKAA2 Proteins)) by binding at the A-769662 drug binding site on the AMPK (show PRKAA1 Proteins) beta1-subunit
findings suggest that the reduced expression of AMPK (show PRKAA1 Proteins)-beta1 confers lower AMPK (show PRKAA1 Proteins) activity, which enhances the oncogenic capacity of advanced-stage ovarian cancer.
The effects of ethanol on AMPK (show PRKAA1 Proteins) and PP2A (show PPP2R4 Proteins) may result in activation of ChREBP (show MLXIPL Proteins), providing another potential mechanism for ethanol-induced hepatic steatosis.
Data indicate that a diet high in iron improves glucose tolerance by activating AMPK (show PRKAA1 Proteins) through mechanisms that include deacetylation.
LKB1 (show STK11 Proteins) controls IRS1 (show IRS1 Proteins)-dependent adipogenesis via AMPK (show PRKAA1 Proteins) in white adipose tissue.
Data indicate that except AMPK (show PRKAA1 Proteins)-alpha1, expressions of the other five AMPK (show PRKAA1 Proteins) subunits -alpha2, -beta1, -beta2, -gamma1 and -gamma2 are significantly higher in ovarian carcinomas.
Changes in translational control of mitochondrial proteins are signaled by the activation of AMPK and general control non-derepressible kinase 2 (GCN2), leading also to the activation of autophagy.
Phosphorylation levels of AMPK (show PRKAA1 Proteins) and glycolysis were up-regulated to confer an advantage of survival for MERRF skin fibroblasts.
Adipose tissues of markedly obese insulin (show INS Proteins) resistant individuals uniformly show decreased AMPK (show PRKAA1 Proteins) activity and increased oxidative stress compared with insulin (show INS Proteins) sensitive patients.
In breast cancer cells SESN2 (show SESN2 Proteins) is associated with AMPK (show PRKAA1 Proteins).
In lipid-laden macrophages, Ampk (show PRKAA1 Proteins) activation decreased cholesterol content (foam cell formation) and increased cholesterol efflux to HDL (show HSD11B1 Proteins) and apoA-I (show APOA1 Proteins), effects that occurred in an Ampk (show PRKAA1 Proteins) beta1-dependent manner.
AMPK (show PRKAA1 Proteins) directly relaxes vascular smooth muscle cell by a decrease of [Ca(2 (show CA2 Proteins)+)]i. This is achieved by calcium sequestration via SERCA (show ATP2A3 Proteins) activation, as well as activation of BKCa (show KCNMA1 Proteins) channels.
Norepinephrine increases the expression of PGC-1alpha in parallel with the activation of AMPK (show PRKAA1 Proteins) signaling in mouse epididymal adipose tissue.
AMPK (show PRKAA1 Proteins) beta1beta2 have a role in preventing myopathy due to loss of capillary density in nonpostural muscles
PPARbeta (show PPARD Proteins)/delta, but not PPARalpha (show PPARA Proteins), interacts with the exercise-inducible kinase AMP-activated protein kinase (AMPK (show PRKAA2 Proteins)) to synergistically activate Ldhb (show LDHB Proteins) gene transcription by cooperating with myocyte enhancer factor 2A (MEF2A (show MEF2A Proteins)) in a PPARbeta (show PPARD Proteins)/delta ligand-independent manner
The aim of this study was to determine whether activation of AMPK (show PRKAA1 Proteins) by acute renal ischemia influences the severity of renal ischemia-reperfusion injury.
AMPK (show PRKAA1 Proteins) beta1 protects macrophages from inflammation under high lipid exposure from a high fat diet. beta1(-/-) macrophages displayed increased levels of diacylglycerol and markers of inflammation.
cisplatin-triggered activation of AMPK (show PRKAA1 Proteins) and subsequent suppression of mTOR (show FRAP1 Proteins) activity can induce an autophagic response that protects tumour cells from cisplatin-mediated apoptotic death
Phosphorylation of AMPK (show PRKAA1 Proteins) by Ulk1 (show ULK1 Proteins) represents a negative feedback circuit.
The extent of genetic polymorphisms in the promoter region of PRKAB1 gene was investigated in a sample of 811 Chinese indigenous bovine individuals.
Sequence analysis of 811 Chinese indigenous bovine individuals revealed 29 single nucleotide polymorphisms (SNPs) of bovine PRKAB1 gene.
The protein encoded by this gene is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. This subunit may be a positive regulator of AMPK activity. The myristoylation and phosphorylation of this subunit have been shown to affect the enzyme activity and cellular localization of AMPK. This subunit may also serve as an adaptor molecule mediating the association of the AMPK complex.
5'-AMP-activated protein kinase subunit beta-1
, AMPK-activated protein kinase beta-1 subunit
, 5'AMP-activated protein kinase beta-1 non-catalytic subunit
, protein kinase, AMP-activated, beta 1 non-catalytic subunit
, AMP-activated protein kinase beta 1 non-catalytic subunit
, AMPK subunit beta-1
, 5'-AMP-activated protein kinase beta-1 subunit
, AMP-activated protein kinase beta subunit
, AMPK beta -1 chain
, AMPK beta 1
, protein kinase, AMP-activated, noncatalytic, beta-1
, 5'-AMP-activated protein kinase 40 kDa subunit
, 5'-AMP-activated protein kinase, beta subunit
, 5-AMP-activated protein kinase beta subunit
, AMPK beta-1 chain