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ATP citrate lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Additionally we are shipping ACLY Antibodies (123) and ACLY Proteins (4) and many more products for this protein.
Showing 5 out of 20 products:
ACLY and ACSS2 are both activated to produce cytosolic Ac-CoA from glucose carbon for lipogenesis during human cytomegalovirus infection.
ACLY facilitates histone acetylation at double-strand break (DSB) sites, impairing 53BP1 localization and enabling BRCA1 recruitment and DNA repair by homologous recombination. ACLY phosphorylation and nuclear localization are necessary for its role in promoting BRCA1 recruitment.
The protein crystallized consisted of residues 2-425-ENLYFQ and S-488-810 of human ATP-citrate lyase. (2S,3S)-2-Hydroxycitrate binds in the same orientation as citrate, but the citrate-binding domain (residues 248-421) adopts a different orientation with respect to the rest of the protein (residues 4-247, 490-746 and 748-809) from that previously seen.
CUL3 interacts with ACLY through its adaptor protein, KLHL25 (Kelch-like family member 25), to ubiquitinate and degrade ACLY in cells
we found that depletion of ATP citrate lyase suppressed tumor growth, which suggests that ATP citrate lyase-related inhibitors might be potential therapeutic approaches for breast cancer.
Results show that ACLY is a key phosphoprotein effector of IL-2 (show IL2 ELISA Kits)-mediated T-cell responses. ACLY becomes phosphorylated on serine 455 in T lymphocytes upon IL-2 (show IL2 ELISA Kits)-driven activation of AKT (show AKT1 ELISA Kits), and depletion or inactivation of ACLY compromises IL-2 (show IL2 ELISA Kits)-promoted T-cell growth.
ACLY was also required for LMW-E-mediated transformation, migration, and invasion of breast cancer cells in vitro along with tumor growth in vivo In clinical specimens of breast cancer, the absence of LMW-E and low expression of adipophilin (PLIN2 (show PLIN2 ELISA Kits)), a marker of lipid droplet formation, associated with favorable prognosis
ACC1 (show ACACA ELISA Kits) and ACLY regulate the levels of ETV4 (show ETV4 ELISA Kits) under hypoxia via increased alpha-ketoglutarate. These results reveal that the ACC1 (show ACACA ELISA Kits)/ACLY-alpha-ketoglutarate-ETV4 (show ETV4 ELISA Kits) axis is a novel means by which metabolic states regulate transcriptional output
ACL activity is associated with increased ATP. Activation of this IGF1 (show IGF1 ELISA Kits)/ACL/cardiolipin pathway combines anabolic signaling with induction of mechanisms needed to provide required ATP.
These results suggest that the combined expression of GLUT1 (show SLC2A1 ELISA Kits) and ACLY could be a more valuable prognostic factor than their individual expression in node-negative patients with NSCLC.
We propose that D2-HG promotes cardiac dysfunction by impairing alpha-ketoglutarate dehydrogenase (show alphaKGDHC ELISA Kits) and induces histone modifications in an ACL (show APOC4 ELISA Kits)-dependent manner
these data indicate that engagement of acetate metabolism is a crucial, although partial, mechanism of compensation for ACLY deficiency.
ACL (show APOC4 ELISA Kits) plays a critical role in epigenetic regulation of diabetic renal fibrosis.
ATP-citrate lyase inhibitor bempedoic acid effectively prevents plasma and tissue lipid elevations and attenuates the onset of inflammation, leading to the prevention of atherosclerotic lesion development in a Ldlr (show LDLR ELISA Kits) knockout mouse model of metabolic dysregulation.
IL-4 (show IL4 ELISA Kits) signaling co-opts the Akt (show AKT1 ELISA Kits)-mTORC1 pathway to regulate Acly, a key enzyme in acetyl-CoA (show LPCAT1 ELISA Kits) synthesis, leading to increased histone acetylation and macrophage gene induction.
These data demonstrate that ACLY mediates glucose-dependent de novo lipogenesis in response to LPS (show TLR4 ELISA Kits) signaling and identify a role for ACLY in several phenotypic changes that define plasma cell differentiation
Results suggest a role for DNA methyltransferase 1 (DNMT1 (show DNMT1 ELISA Kits)) in modulating the timing of differentiation and describe a novel ATP-citrate lyase (ACL)-miR (show MLXIP ELISA Kits)-148a-dependent mechanism for regulating DNMT1 (show DNMT1 ELISA Kits) during adipogenesis.
Differences between human and rodent pancreatic islets: low pyruvate carboxylase (show PC ELISA Kits), atp citrate lyase, and pyruvate carboxylation and high glucose-stimulated acetoacetate in human pancreatic islets.
Results demonstrate that hepatic ATP-citrate lyase suppression exerts profound effects on triglyceride mobilization as well as fatty acid compositions in the liver, suggesting an important role for ACL (show APOC4 ELISA Kits) in lipid metabolism.
Data suggest that ATP-citrate lyase (ACLY) expression and activity can be suppressed by exogenous lipids and demonstrate a critical role for ACLY in pancreatic beta cell survival.
The results of this study indicate that a C/T mutation affects ACL mRNA expression, probably via the activator protein 2 (show TFAP2A ELISA Kits).
we identified three non-synonymous mutations in ACLY exons in five beef cattle populations. Single nucleotide polymorphism (SNP) g.17127C>T is significantly associated with chest girth and body height, and with body slanting length. SNP g.40427T>C is significantly associated with an increase in chest girth. ACLY gene are associated with growth traits in beef cattle in northwest China
ATP citrate lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. The enzyme is a tetramer (relative molecular weight approximately 440,000) of apparently identical subunits. It catalyzes the formation of acetyl-CoA and oxaloacetate from citrate and CoA with a concomitant hydrolysis of ATP to ADP and phosphate. The product, acetyl-CoA, serves several important biosynthetic pathways, including lipogenesis and cholesterogenesis. In nervous tissue, ATP citrate-lyase may be involved in the biosynthesis of acetylcholine. Two transcript variants encoding distinct isoforms have been identified for this gene.
ATP citrate lyase
, ATP citrate synthase
, ATP-citrate synthase-like
, ATP-citrate lyase
, ATP-citrate synthase
, citrate synthase, mitochondrial
, atp-citrate synthase
, ATP-citrate (pro-S-)-lyase
, citrate cleavage enzyme