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CAMKK2 and AMPK have opposing effects on lipogenesis, providing a potential mechanism for their contrasting effects on prostate cancer progression in vivo
AMPK activity in response to redox changes is not due to direct action on AMPK itself, but is a secondary consequence of redox effects on other processes, such as mitochondrial ATP production.
Oncogenic stress chronically activates AMPK in glioblastoma tumor stem cells that coopt the AMPK-CREB1 pathway to coordinate tumour bioenergetics through the transcription factors HIF1alpha and GABPA.
we studied the role of the beta 1 subunit in erythrocytes and observed microcytic anemia with compensatory extramedullary hematopoiesis together with splenomegaly and increased osmotic resistance.
Salicylate activates the AMP-activated protein kinase (AMPK) by binding at the A-769662 drug binding site on the AMPK beta1-subunit
findings suggest that the reduced expression of AMPK-beta1 confers lower AMPK activity, which enhances the oncogenic capacity of advanced-stage ovarian cancer.
The effects of ethanol on AMPK and PP2A may result in activation of ChREBP, providing another potential mechanism for ethanol-induced hepatic steatosis.
Data indicate that a diet high in iron improves glucose tolerance by activating AMPK through mechanisms that include deacetylation.
LKB1 controls IRS1-dependent adipogenesis via AMPK in white adipose tissue.
Data indicate that except AMPK-alpha1, expressions of the other five AMPK 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 and glycolysis were up-regulated to confer an advantage of survival for MERRF skin fibroblasts.
Adipose tissues of markedly obese insulin resistant individuals uniformly show decreased AMPK activity and increased oxidative stress compared with insulin sensitive patients.
In breast cancer cells SESN2 is associated with AMPK.
Adiponectin could attenuate renal dysfunction associated with mesangial cells disorders through AMPK-mTOR signal pathway.
1q21.1 copy number variant (CNV) results in gene function changes, specifically in the deletion containing lymphobalst cell lines, where AMPK was attenuated.
AMPK, Akt and mTOR pathways have roles in resveratrol-enhanced prostate cancer cell response to ionizing radiation
cisplatin-triggered activation of AMPK and subsequent suppression of mTOR activity can induce an autophagic response that protects tumour cells from cisplatin-mediated apoptotic death
Studies indicate that in most species, AMPK exists as an obligate heterotrimer, containing a catalytic subunit (alpha), and two regulatory subunits (beta and gamma).
LKB1-AMPK negatively regulated mTOR function in tumor.
the evidence indicates that AMPK is sufficient but not essential for the maintenance of DAPC expression in skeletal muscle, yet it is required for preserving extrasynaptic utrophin levels in slow oxidative muscles.
activation of AMPK at early stage of adipogenesis is involved in the anti-adipogenesis effect of Red Pepper Seed extract.
in the absence of the tumor suppressor p53, germline genetic deletion of AMPK beta1 accelerates the appearance of a T-cell lymphoma that reduces lifespan compared to p53 deficiency alone.
In lipid-laden macrophages, Ampk activation decreased cholesterol content (foam cell formation) and increased cholesterol efflux to HDL and apoA-I, effects that occurred in an Ampk beta1-dependent manner.
AMPK directly relaxes vascular smooth muscle cell by a decrease of [Ca(2+)]i. This is achieved by calcium sequestration via SERCA activation, as well as activation of BKCa channels.
Norepinephrine increases the expression of PGC-1alpha in parallel with the activation of AMPK signaling in mouse epididymal adipose tissue.
AMPK beta1beta2 have a role in preventing myopathy due to loss of capillary density in nonpostural muscles
PPARbeta/delta, but not PPARalpha, interacts with the exercise-inducible kinase AMP-activated protein kinase (AMPK) to synergistically activate Ldhb gene transcription by cooperating with myocyte enhancer factor 2A (MEF2A) in a PPARbeta/delta ligand-independent manner
The aim of this study was to determine whether activation of AMPK by acute renal ischemia influences the severity of renal ischemia-reperfusion injury.
AMPK 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.
Data show that beta1beta2M-KO mice are physically inactive and have a drastically impaired capacity for treadmill running that is associated with reductions in skeletal muscle mitochondrial content.
Phosphorylation of AMPK by Ulk1 represents a negative feedback circuit.
AMPK-mediated PLD1 activation is required for (14)C-glucose uptake through ERK stimulation
AMPK negatively regulates Nox4-dependent activation of p53 and podocytes apoptosis in diabetes.
AMPK negatively regulates lipid-induced inflammation, which acts through SIRT1, thereby contributing to the protection against obesity, inflammation, and insulin resistance
Germline deletion of either AMPK beta1 or beta2 subunit isoforms resulted in reduced trabecular bone density and mass, but without effects on osteoclast (OC) or osteoblast (OB) numbers.
The loss of AMPK beta1 reduces food intake and protects against the deleterious effects of an obesity-inducing diet.
metformin and AMPK have a previously unrecognized role in regulating the circadian rhythm
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 beta-1 subunit
, 5'-AMP-activated protein kinase subunit beta-1
, AMP-activated protein kinase beta subunit
, AMPK beta -1 chain
, AMPK beta 1
, AMPK subunit 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
, 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-activated protein kinase beta-1 subunit