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This study assessed the relation of GLS2 downregulation in glioblastoma cells to its methylation and TP53 (Montrer TP53 Protéines) status. Aberrant methylation of CpG islands, appear to contribute to silencing of GLS2 in glioblastoma cells by a mechanism bypassing TP53 (Montrer TP53 Protéines) mutations.
Non-glutaminolysis function of GLS2 inhibits migration and invasion of hepatocellular carcinoma cells by repressing the epithelial-mesenchymal transition via the Dicer (Montrer DICER1 Protéines)-miR (Montrer MLXIP Protéines)-34a-Snail (Montrer SNAI1 Protéines) axis.
observe that while miR (Montrer MLXIP Protéines)-23 is capable of down-regulating the shortened KGA (Montrer GLS Protéines) 3'UTR, it has only minor impact on the full-length KGA (Montrer GLS Protéines) 3'UTR, demonstrating that additional potent negative regulation of GLS (Montrer GLS Protéines) expression exists beyond this single microRNA targeting site
the crystal structure of full-length KGA (Montrer GLS Protéines) and present a small-angle X-ray scattering model for full-length GLS2. These structures explain these proteins' compromised ability to assemble into catalytically active supra-tetrameric filaments, as previously shown for GAC (Montrer GLS Protéines).
Cox (Montrer COX8A Protéines) multivariate regression analysis demonstrated that DUOX1 (Montrer DUOX1 Protéines), GLS2, FBP1 (Montrer FBP1 Protéines) and age were independent risk factors for the prognosis of HCC (Montrer FAM126A Protéines) patients after surgery
As a p53 target, GLS2 mediates p53's function in metastasis suppression through inhibiting Rac1.
IDO (Montrer IDO1 Protéines), through GCN2 (Montrer EIF2AK4 Protéines) kinase activation, downregulates the levels of TCRcomplex tchain and cMyc (Montrer MYC Protéines), resulting in the suppression of Tcell proliferation and a reduction in the levels of LDHA (Montrer LDHA Protéines) and GLS2
GABAergic neurons and astrocytes express Gls (Montrer GLS Protéines) and Gls2 isoenzymes in nucleus and mitochondria, in addition to glutamatergic neurons
Phosphate-activated glutaminase and GAD65 (Montrer GAD2 Protéines)/67 concentrations are compared in Alzheimer's disease cerebellum versus normal cerebellum controls
GLS2 expression is significantly decreased in hepatocellular carcinoma.
Data (including data from studies in knockout/transgenic mice) suggest Ppp2ca (Montrer PPP2CA Protéines) supports cortical neuronal growth and cognitive function via regulating p73 (Montrer ARHGAP24 Protéines)/Gls2 signal transduction in neurons of hippocampus. Ppp2ca (Montrer PPP2CA Protéines) gene knock-out results in embryonic cortical atrophy with learning/memory deficits. (Ppp2ca (Montrer PPP2CA Protéines) = protein phosphatase 2a catalytic subunit alpha isoform; p73 (Montrer ARHGAP24 Protéines) = transformation related protein 73; Gls2 = glutaminase-2)
Gls2 expression is regulated by the dietary protein/carbohydrate ratio. This effect was not observed in Ppara (Montrer PPARA Protéines)-null mice.
Study demonstrated expression of alternative transcripts of the mammalian Gls2 gene. Transcriptional mechanisms giving rise to GLS2 variants and isolation of novel GLS2 transcripts in human, rat and mouse are presented.
Phosphate-activated glutaminase (GLS2) is a p53 (Montrer TP53 Protéines)-inducible regulator of glutamine (Montrer GFPT1 Protéines) metabolism and reactive oxygen species
The protein encoded by this gene is a mitochondrial phosphate-activated glutaminase that catalyzes the hydrolysis of glutamine to stoichiometric amounts of glutamate and ammonia. This protein is functionally similar to the kidney glutaminase but is a little smaller in size. Originally thought to be liver-specific, this protein has been found in other tissues as well. At least one transcribed pseudogene has been found for this gene.
, L-glutamine amidohydrolase
, breast cell glutaminase
, glutaminase I
, glutaminase liver isoform, mitochondrial
, phosphate-activated glutaminase
, phosphate-dependent glutaminase
, liver mitochondrial glutaminase