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1 DGAT1 gene family (i.e. related to acyl-CoA:cholesterol acyltransferases).
2 ribute to the optimum activation of lecithin:cholesterol acyltransferase.
3 he intracellular esterifying enzyme acyl-CoA:cholesterol acyltransferase.
4 viously characterized antagonist of acyl-CoA cholesterol acyltransferase.
5 aining particles by incubation with lecithin:cholesterol acyltransferase.
6 f cholesterol 7alpha-hydroxylase or acyl-CoA:cholesterol acyltransferase.
14 pression of Niemann Pick C1 Like 1, Acyl-CoA:Cholesterol acyltransferase 1, and microsomal triglyceri
22 is 32% identical to the vertebrate lecithin:cholesterol acyltransferase, a secreted phospholipase.
27 r cholesterol esterification enzyme acyl-CoA:cholesterol acyltransferase (ACAT) are present in the no
30 e of cholesterol ester synthesis by acyl CoA:cholesterol acyltransferase (ACAT) enzymes in intestinal
32 thophysiological conditions, acyl-coenzyme A:cholesterol acyltransferase (ACAT) has attracted much at
34 The rationale was that the acyl-coenzyme A:cholesterol acyltransferase (ACAT) in homogenates should
35 s LDL cholesterol from lysosomes to acyl-CoA/cholesterol acyltransferase (ACAT) in the endoplasmic re
36 derived cholesterol is catalyzed by acyl-CoA:cholesterol acyltransferase (ACAT) in the endoplasmic re
37 e have found previously that acyl-coenzyme A:cholesterol acyltransferase (ACAT) inhibition led to imp
38 Although originally designed as acyl CoA: cholesterol acyltransferase (ACAT) inhibitors, compariso
39 Esterification of cholesterol by acyl-CoA:cholesterol acyltransferase (ACAT) is a key element in m
49 Cholesterol trafficking to acyl-coenzyme A:cholesterol acyltransferase (ACAT) was also defective in
50 used our studies on the activity of acyl-CoA:cholesterol acyltransferase (ACAT), a key enzyme for mai
51 ) synthase, squalene epoxidase, and acyl-CoA:cholesterol acyltransferase (ACAT), ACAT2, small heterod
52 ous studies have identified acyl-coenzyme A: cholesterol acyltransferase (ACAT), an enzyme that regul
53 as activator for the enzyme acyl-coenzyme A:cholesterol acyltransferase (ACAT), by monitoring the ac
54 terification reaction, catalyzed by acyl-CoA:cholesterol acyltransferase (ACAT), competes for the inc
55 sterol esterification, catalyzed by acyl-CoA:cholesterol acyltransferase (ACAT), plays a central role
56 The inhibition of macrophage acyl coenzyme A:cholesterol acyltransferase (ACAT), which catalyzes the
57 he sterol esterifying enzyme acyl-coenzyme A-cholesterol acyltransferase (ACAT), which likely occurs
58 teraction of the major SOAT, acyl-coenzyme A:cholesterol acyltransferase (ACAT)-related enzyme (Are)2
65 synthesis of cholesterol esters by acyl-CoA:cholesterol acyltransferase (ACAT, EC 2.3.1.26) is an im
67 o be catalyzed by the enzyme acyl-coenzyme A:cholesterol acyltransferase, ACAT, the neutral cholester
68 olesterol-esterifying enzyme acyl-coenzyme A:cholesterol acyltransferase (ACAT1), but not lecithin-ch
70 glycerol acyltransferase (DGAT) and acyl-CoA:cholesterol acyltransferases (ACAT1 and ACAT2) provided
72 id binding, cholesterol efflux, and lecithin-cholesterol acyltransferase activities of the lipoprotei
73 SRBI cells was not due to increased acyl-coA:cholesterol acyltransferase activity and was observed ev
74 a-helicity, cholesterol efflux, and lecithin-cholesterol acyltransferase activity of the recombinant
75 ctivity and approximately 90% lower lecithin-cholesterol acyltransferase activity relative to circula
76 espite an increase in hepatic mRNA; lecithin:cholesterol acyltransferase activity toward endogenous E
77 orm with 88.1 +/- 8.5% reduction in lecithin-cholesterol acyltransferase activity, a finding corrobor
79 t shared regions of similarity with acyl CoA:cholesterol acyltransferase, an enzyme that also uses fa
82 he presence of normal activities of acyl-CoA:cholesterol acyltransferase and glycerol phosphate acylt
84 gests the possible interaction with lecithin-cholesterol acyltransferase and may shed light on the mo
85 ression on the microsomal levels of acyl-CoA:cholesterol acyltransferase and neutral cholesterol este
86 LDL-cholesterol to be esterified by acyl-CoA:cholesterol acyltransferase and stored in lipid droplets
87 logous to enzymes called glycerophospholipid-cholesterol acyltransferases and, following translocatio
89 e chemoattractant protein-1, acyl coenzyme A:cholesterol acyltransferase, and tissue factor, in lesio
90 s of diacylglycerol acyltransferase and acyl cholesterol acyltransferase are expressed in the lumen o
91 r-activated receptor modulators and lecithin-cholesterol acyltransferase-based therapy, hold great pr
92 associates more and activates human lecithin-cholesterol acyltransferase better than mouse apoA-I.
93 ., paraoxonase, apolipoprotein A-I, lecithin:cholesterol acyltransferase, cholesterol ester transfer
94 ce and the roles of plasma factors (lecithin-cholesterol acyltransferase, cholesterol ester transfer
95 l particles reminiscent of those in lecithin/cholesterol acyltransferase deficiency and cholestasis).
97 (adrenocortical lipid depletion in acyl-CoA:cholesterol acyltransferase-deficient (Acact-/-) mice an
98 sc-associated apoA-I that binds the lecithin-cholesterol acyltransferase enzyme is well structured an
99 Cholesteryl ester synthesis by the acyl-CoA:cholesterol acyltransferase enzymes ACAT1 and ACAT2 is,
100 spholipases A (PLAs) and glycerophospholipid:cholesterol acyltransferases (GCATs), may target host ce
101 ted DGAT1), which is related to the acyl CoA:cholesterol acyltransferase gene family, or to any other
105 storage form by the enzyme acyl-coenzyme A: cholesterol acyltransferase, is a critical component of
106 residues and domains implicated in lecithin:cholesterol acyltransferase (LCAT) activation or lipid b
109 holipid transfer protein (PLTP) and lecithin cholesterol acyltransferase (LCAT) activities were decre
113 than other acyltransferases such as lecithin cholesterol acyltransferase (LCAT) and acyl CoA acyltran
114 laboratory previously reported that lecithin:cholesterol acyltransferase (LCAT) and LDL receptor doub
115 lesterol binding, esterification by lecithin/cholesterol acyltransferase (LCAT) and transfer by chole
116 pacity and 37% capacity to activate lecithin:cholesterol acyltransferase (LCAT) as compared to the WT
117 osomal phospholipase A2 (LPLA2) and lecithin:cholesterol acyltransferase (LCAT) belong to a structura
118 on dramatically reduces the rate of lecithin:cholesterol acyltransferase (LCAT) catalyzed cholesterol
121 revious studies have indicated that lecithin-cholesterol acyltransferase (LCAT) contributes significa
122 udy was to test the hypothesis that lecithin:cholesterol acyltransferase (LCAT) deficiency would acce
128 and interfacial binding activity of lecithin-cholesterol acyltransferase (LCAT) is affected different
130 Although the major function of lecithin-cholesterol acyltransferase (LCAT) is cholesterol esteri
131 fied cholesterol (UC) by the enzyme lecithin:cholesterol acyltransferase (LCAT) is cholesteryl ester
138 or protein-protein interaction with lecithin-cholesterol acyltransferase (LCAT) the enzyme for which
141 asma but reduces atherosclerosis in lecithin cholesterol acyltransferase (LCAT) transgenic (Tg) mice,
142 on in blood is closely regulated by lecithin-cholesterol acyltransferase (LCAT) which is produced in
144 pear to show that the reactivity of lecithin:cholesterol acyltransferase (LCAT) with the mutant is sl
145 ue T. gondii homologue of mammalian lecithin:cholesterol acyltransferase (LCAT), a key enzyme that pr
147 G esters (PE) by the plasma enzyme lecithin: cholesterol acyltransferase (LCAT), and by other enzyme(
148 ol acyltransferase (ACAT1), but not lecithin-cholesterol acyltransferase (LCAT), and to differ from h
149 apoA-I) activates the plasma enzyme lecithin:cholesterol acyltransferase (LCAT), catalyzing the rapid
150 ns, and had minimal reactivity with lecithin-cholesterol acyltransferase (LCAT), compared with rHDL p
151 l ester transfer protein (CETP) and lecithin:cholesterol acyltransferase (LCAT), on chromosome 16q; a
152 hydroxylase, Scavenger receptor B1, lecithin:cholesterol acyltransferase (LCAT), or apoA-I in the liv
153 aturally occurring mutants of human lecithin-cholesterol acyltransferase (LCAT), T123I and N228K, wer
154 f cholesterol-containing r-HDL with lecithin-cholesterol acyltransferase (LCAT), to form cholesteryl
156 pathway is critically dependent on lecithin:cholesterol acyltransferase (LCAT), which rapidly conver
163 quences identical to those of human lecithin:cholesterol acyltransferase-like lysophospholipase (LLPL
164 es, due primarily to an increase in lecithin:cholesterol acyltransferase-mediated (LCAT-mediated) cho
165 ates LDL uptake and degradation and acyl-CoA:cholesterol acyltransferase-mediated esterification of L
166 lesteryl ester transfer protein and lecithin:cholesterol acyltransferase only function optimally in h
167 lesteryl ester transfer protein and lecithin-cholesterol acyltransferase (phosphatidylcholine-sterol
168 cholesteryl ester transfer protein, lecithin:cholesterol acyltransferase (phosphatidylcholine-sterol
169 he first molecular probe of acyl-coenzyme A: cholesterol acyltransferase provided a key to understand
170 e of similar size, composition, and lecithin:cholesterol acyltransferase reactivity when compared to
171 apoA-I(-/-) HDL in the presence of lecithin cholesterol acyltransferase reorganized the large hetero
173 types toward a major plasma enzyme, lecithin:cholesterol acyltransferase responsible for the HDL matu
174 eletion of LRO1, a homolog of human lecithin cholesterol acyltransferase, resulted in a dramatic redu
175 phimurium translocates a glycerophospholipid:cholesterol acyltransferase (SseJ) into the host cytosol
176 mation, apoA-I activates the enzyme lecithin:cholesterol acyltransferase stimulating the formation of
177 nzymes that esterify cholesterol (lecithin : cholesterol acyltransferase), transfer cholesterol (chol
179 ester formation in tissues, acyl coenzyme A:cholesterol acyltransferase types 1 and 2 (ACAT1 and ACA
182 ver, apoA-V was a poor activator of lecithin:cholesterol acyltransferase where the activity was 8.5 +
183 parameters of the lipophilic enzyme lecithin:cholesterol acyltransferase, which binds to phosphatidyl
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