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1 a acetyl-CoA synthetase) or citrate (via ATP citrate lyase).
2 ibitors of the recombinant human form of ATP-citrate lyase.
3 observed with mammalian, yeast, and mold ATP-citrate lyase.
4 cytosolic enzyme of citrate metabolism, ATP citrate lyase.
5 the reductive tricarboxylic acid cycle, ATP citrate lyase, 2-oxoglutarate:ferredoxin oxidoreductase,
9 s been previously shown to modulate both ATP-citrate lyase (ACL) and AMP-activated protein kinase (AM
12 NIP-H/Caytaxin links kinesin-1 (KLC1) to ATP citrate lyase (ACL), a key enzyme for ACh synthesis, and
13 is dependent on adenosine triphosphate (ATP)-citrate lyase (ACL), the enzyme that converts glucose-de
18 olic acetyl CoA (Ac-CoA), is produced by ATP-citrate lyase (ACLY) from mitochondria-derived citrate o
21 In this study, we report that nuclear ATP-citrate lyase (ACLY) is phosphorylated at S455 downstrea
24 g proteins in breast cancer, identifying ATP-citrate lyase (ACLY), an enzyme in the de novo lipogenes
25 leads to increased levels of endogenous ATP-citrate lyase (ACLY), and this is accompanied by increas
27 idosis is associated with an increase in ATP citrate lyase activity and protein abundance, and is par
33 ight loss, is a competitive inhibitor of ATP-citrate lyase, an extramitochondrial enzyme involved in
34 ngth HCV RNAs express elevated levels of ATP citrate lyase and acetyl-CoA synthetase genes, both of w
37 elongation in tumour cells by targeting ATP citrate lyase and fatty acid elongase 6, as well as impa
38 lation of citrate and the stimulation of ATP citrate lyase and fatty-acid synthase leading to de novo
40 lly deubiquitinates and thus upregulates ATP citrate lyase and oxoglutarate dehydrogenase, two key en
42 to the inhibition of adenosine triphosphate-citrate lyase and the activation of adenosine monophosph
43 y-acid synthase, acetyl-CoA carboxylase, ATP citrate lyase, and Glut-1 were significantly increased t
46 the 3-D crystal structure of M. tuberculosis citrate lyase beta-subunit (CitE), which as annotated sh
47 biosynthesis that is analogous to bacterial citrate lyase but producing acetyl-CoA rather than a pro
51 encoding the alpha- and beta-subunits of ATP citrate lyase could be amplified from both organisms.
52 situation observed for other prokaryotic ATP-citrate lyase enzymes, the C. tepidum enzyme was not abl
54 of FAS, acetyl-CoA carboxylase-alpha and ATP-citrate lyase, fails to activate caspase-8 or to elicit
55 coding for key lipogenic (malic enzyme, ATP citrate-lyase, fatty acid synthase), glycolytic (pyruvat
56 nduction of mRNAs encoding malic enzyme, ATP citrate-lyase, fatty acid synthase, liver-type pyruvate
57 Both forms of RuBisCO, together with ATP citrate lyase genes in the rTCA cycle, increase with dis
58 genes, including SCD1, FAS, ACC1, ACC2, ATP-citrate lyase, glycerol kinase, and HMG-CoA reductase.
59 hypothesis that compounds which inhibit ATP-citrate lyase have the potential to be a novel class of
60 se results suggest an important role for ATP citrate lyase in proximal tubular citrate metabolism.
62 and fumarase and activate the cytosolic ATP-citrate lyase in vivo, acting as a direct regulator of c
63 icant differences from other prokaryotic ATP-citrate lyases, including the enzyme from the closely re
64 the CRM hydroxycitrate, an inhibitor of ATP citrate lyase, induced the depletion of regulatory T cel
68 e show that acetyl-CoA synthase, rather than citrate lyase, is essential for acetyl-CoA synthesis in
70 fat diet (HFD) results in suppression of ATP citrate-lyase levels in tissues such as adipose and live
72 er that transcribes genes having homology to citrate lyase operon genes, citC, citD and citE, of Kleb
76 ose bisphosphate carboxylase (Calvin cycle), citrate lyase (reverse citric acid cycle), and malyl coe
77 , the catalytic properties of C. tepidum ATP-citrate lyase showed marked similarities to the eukaryot
78 dies we show that the levels of mRNA for ATP citrate lyase, the enzyme that produces acetyl-CoA, are
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