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1 (via acetyl-CoA synthetase) or citrate (via ATP citrate lyase).
2 on a cytosolic enzyme of citrate metabolism, ATP citrate lyase.
3 inhibitors of the recombinant human form of ATP-citrate lyase.
4 een observed with mammalian, yeast, and mold ATP-citrate lyase.
5 s of the reductive tricarboxylic acid cycle, ATP citrate lyase, 2-oxoglutarate:ferredoxin oxidoreduct
7 n of these biosynthetic genes, which include ATP citrate lyase, ACC, FAS, and stearoyl-CoA desaturase
9 in BNIP-H/Caytaxin links kinesin-1 (KLC1) to ATP citrate lyase (ACL), a key enzyme for ACh synthesis,
11 ells is dependent on adenosine triphosphate (ATP)-citrate lyase (ACL), the enzyme that converts gluco
12 d has been previously shown to modulate both ATP-citrate lyase (ACL) and AMP-activated protein kinase
18 ytosolic acetyl CoA (Ac-CoA), is produced by ATP-citrate lyase (ACLY) from mitochondria-derived citra
24 nding proteins in breast cancer, identifying ATP-citrate lyase (ACLY), an enzyme in the de novo lipog
25 tion leads to increased levels of endogenous ATP-citrate lyase (ACLY), and this is accompanied by inc
26 c acidosis is associated with an increase in ATP citrate lyase activity and protein abundance, and is
31 r weight loss, is a competitive inhibitor of ATP-citrate lyase, an extramitochondrial enzyme involved
32 l-length HCV RNAs express elevated levels of ATP citrate lyase and acetyl-CoA synthetase genes, both
33 and elongation in tumour cells by targeting ATP citrate lyase and fatty acid elongase 6, as well as
34 cumulation of citrate and the stimulation of ATP citrate lyase and fatty-acid synthase leading to de
36 fically deubiquitinates and thus upregulates ATP citrate lyase and oxoglutarate dehydrogenase, two ke
38 fatty-acid synthase, acetyl-CoA carboxylase, ATP citrate lyase, and Glut-1 were significantly increas
42 ynthesis of fatty acids from glucose include ATP-citrate lyase (CL) and fatty acid synthase (FAS).
44 nes encoding the alpha- and beta-subunits of ATP citrate lyase could be amplified from both organisms
45 the situation observed for other prokaryotic ATP-citrate lyase enzymes, the C. tepidum enzyme was not
47 eam of FAS, acetyl-CoA carboxylase-alpha and ATP-citrate lyase, fails to activate caspase-8 or to eli
48 RNAs coding for key lipogenic (malic enzyme, ATP citrate-lyase, fatty acid synthase), glycolytic (pyr
49 ed induction of mRNAs encoding malic enzyme, ATP citrate-lyase, fatty acid synthase, liver-type pyruv
51 enic genes, including SCD1, FAS, ACC1, ACC2, ATP-citrate lyase, glycerol kinase, and HMG-CoA reductas
52 the hypothesis that compounds which inhibit ATP-citrate lyase have the potential to be a novel class
53 These results suggest an important role for ATP citrate lyase in proximal tubular citrate metabolism
55 nase and fumarase and activate the cytosolic ATP-citrate lyase in vivo, acting as a direct regulator
56 gnificant differences from other prokaryotic ATP-citrate lyases, including the enzyme from the closel
57 with the CRM hydroxycitrate, an inhibitor of ATP citrate lyase, induced the depletion of regulatory T
60 igh-fat diet (HFD) results in suppression of ATP citrate-lyase levels in tissues such as adipose and
65 ties, the catalytic properties of C. tepidum ATP-citrate lyase showed marked similarities to the euka
66 studies we show that the levels of mRNA for ATP citrate lyase, the enzyme that produces acetyl-CoA,
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