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1 , exhibited lower affinities for recombinant squalene synthase.
2 potencies as inhibitors of recombinant yeast squalene synthase.
3 ctivity against Ras farnesyl transferase and squalene synthase.
4 in isoprenylation that are not inhibitors of squalene synthase.
5 not nSREBP-1a, to activate the promoter for squalene synthase.
6 eductase, farnesyl diphosphate synthase, and squalene synthase.
9 l CoA (HMG CoA) synthase, HMG CoA reductase, squalene synthase, acetyl-CoA carboxylase, fatty acid sy
14 nes, less robust associations were found for squalene synthase and change in total cholesterol, apoli
15 that a botryococcene synthase would resemble squalene synthase and hence isolated squalene synthase-l
16 olesterol synthesis genes HMG CoA reductase, squalene synthase, and FPP synthase but did not alter le
17 f farnesyl-diphosphate farnesyl transferase (squalene synthase), but not 3-hydroxy-3-methylglutaryl-C
21 the crystal structures of recombinant human squalene synthase complexed with several different inhib
23 anosterol 14alpha-demethylase (CYP51A1), and squalene synthase (farnesyl diphosphate farnesyl transfe
24 yl-CoA carboxylase, stearoyl-CoA desaturase, squalene synthase, farnesyl-pyrophosphate synthase, 3-hy
29 tion of zaragozic acid--a known inhibitor of squalene synthases--impaired biofilm formation and prote
30 aryl-CoA reductase, fatty-acid synthase, and squalene synthase in livers of Zetia/lovastatin-treated
31 farnesyl diphosphate with recombinant yeast squalene synthase in the absence of NADPH gives a mixtur
33 f rat hepatocytes as a direct consequence of squalene synthase inhibition, we investigated possible u
36 A reductase inhibitor lovastatin and by the squalene synthase inhibitor zaragozic acid A and was pre
38 sterol biosynthetic pathway: squalestatin 1 (squalene synthase inhibitor), (E)N-ethyl-N-(6,6-dimethyl
40 tures with SQ-34919, a structurally distinct squalene synthase inhibitor, produced the same selective
43 ment with multiple statins, bisphosphonates, squalene synthase inhibitors, and small interfering RNA
44 ted a much improved in vitro antioxidant and squalene synthase inhibitory activity (at lower micromol
46 of PSPP or a prior conformational change in squalene synthase is the rate-limiting step for synthesi
47 nthase, farnesyl pyrophosphate synthase, and squalene synthase, key enzymes for cholesterol synthesis
48 ubation of [(14)C]FDP with recombinant human squalene synthase led to [(14)C]PSDP and [(14)C]squalene
49 l squalene synthase, none of the other three squalene synthase-like (SSL) genes encodes for botryococ
50 esemble squalene synthase and hence isolated squalene synthase-like genes from Botryococcus braunii r
51 4S-hydroxycholesterol, HMG CoA reductase and squalene synthase mRNA levels were significantly decreas
52 B. braunii does harbor at least one typical squalene synthase, none of the other three squalene synt
53 hen co-expressed in yeast with complementary squalene synthase or botryococcene synthase expression c
54 tores are reduced secondary to inhibition of squalene synthase or LDL receptor degradation is disrupt
55 se farnesyl diphosphate synthase rather than squalene synthase or phytoene synthase, which catalyze c
56 conversion to squalene through the action of squalene synthase represents the first committed step in
62 in which antioxidant, anti-inflammatory, and squalene synthase (SQS) inhibitory/hypolipidemic activit
65 he activity of these compounds against human squalene synthase (SQS), as a counterscreen, finding sev
70 ly enzymes of triterpene aglycone formation: squalene synthase (SS), squalene epoxidase (SE), and bet
72 n to inhibit cholesterol biosynthesis at the squalene synthase step, may afford a novel series of hyp
73 e-specific manner, whereas the expression of squalene synthase, sterol response element-binding prote
75 t with squalestatin 1, a potent inhibitor of squalene synthase, the first committed enzyme of sterol
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