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1 DGAT1 gene family (i.e. related to acyl-CoA:cholesterol acyltransferases).
2 aining particles by incubation with lecithin:cholesterol acyltransferase.
3 f cholesterol 7alpha-hydroxylase or acyl-CoA:cholesterol acyltransferase.
4 ribute to the optimum activation of lecithin:cholesterol acyltransferase.
5 he intracellular esterifying enzyme acyl-CoA:cholesterol acyltransferase.
6 viously characterized antagonist of acyl-CoA cholesterol acyltransferase.
13 ly active against the related MBOAT acyl-CoA:cholesterol acyltransferase 1 (ACAT1), yet a single-resi
16 pression of Niemann Pick C1 Like 1, Acyl-CoA:Cholesterol acyltransferase 1, and microsomal triglyceri
25 is 32% identical to the vertebrate lecithin:cholesterol acyltransferase, a secreted phospholipase.
30 r cholesterol esterification enzyme acyl-CoA:cholesterol acyltransferase (ACAT) are present in the no
33 e of cholesterol ester synthesis by acyl CoA:cholesterol acyltransferase (ACAT) enzymes in intestinal
35 thophysiological conditions, acyl-coenzyme A:cholesterol acyltransferase (ACAT) has attracted much at
38 The rationale was that the acyl-coenzyme A:cholesterol acyltransferase (ACAT) in homogenates should
39 s LDL cholesterol from lysosomes to acyl-CoA/cholesterol acyltransferase (ACAT) in the endoplasmic re
40 derived cholesterol is catalyzed by acyl-CoA:cholesterol acyltransferase (ACAT) in the endoplasmic re
41 25HC-mediated activation of acyl coenzyme A: cholesterol acyltransferase (ACAT) in the ER creates an
42 e have found previously that acyl-coenzyme A:cholesterol acyltransferase (ACAT) inhibition led to imp
43 Although originally designed as acyl CoA: cholesterol acyltransferase (ACAT) inhibitors, compariso
44 Esterification of cholesterol by acyl-CoA:cholesterol acyltransferase (ACAT) is a key element in m
55 The 25HC-mediated activation of acyl-CoA:cholesterol acyltransferase (ACAT) triggered rapid inter
56 Cholesterol trafficking to acyl-coenzyme A:cholesterol acyltransferase (ACAT) was also defective in
57 sion by activating the ER-localized acyl-CoA:cholesterol acyltransferase (ACAT) which leads to the de
58 used our studies on the activity of acyl-CoA:cholesterol acyltransferase (ACAT), a key enzyme for mai
59 ) synthase, squalene epoxidase, and acyl-CoA:cholesterol acyltransferase (ACAT), ACAT2, small heterod
60 ous studies have identified acyl-coenzyme A: cholesterol acyltransferase (ACAT), an enzyme that regul
61 as activator for the enzyme acyl-coenzyme A:cholesterol acyltransferase (ACAT), by monitoring the ac
62 terification reaction, catalyzed by acyl-CoA:cholesterol acyltransferase (ACAT), competes for the inc
63 sterol esterification, catalyzed by acyl-CoA:cholesterol acyltransferase (ACAT), plays a central role
64 The inhibition of macrophage acyl coenzyme A:cholesterol acyltransferase (ACAT), which catalyzes the
65 he sterol esterifying enzyme acyl-coenzyme A-cholesterol acyltransferase (ACAT), which likely occurs
66 teraction of the major SOAT, acyl-coenzyme A:cholesterol acyltransferase (ACAT)-related enzyme (Are)2
73 synthesis of cholesterol esters by acyl-CoA:cholesterol acyltransferase (ACAT, EC 2.3.1.26) is an im
75 o be catalyzed by the enzyme acyl-coenzyme A:cholesterol acyltransferase, ACAT, the neutral cholester
76 olesterol-esterifying enzyme acyl-coenzyme A:cholesterol acyltransferase (ACAT1), but not lecithin-ch
78 glycerol acyltransferase (DGAT) and acyl-CoA:cholesterol acyltransferases (ACAT1 and ACAT2) provided
79 cyltransferase 1 (also named acyl-coenzyme A:cholesterol acyltransferase, ACAT1) transfers a long-cha
81 erase (MBOAT) enzyme family, acyl-coenzyme A:cholesterol acyltransferases (ACATs) catalyse the transf
82 id binding, cholesterol efflux, and lecithin-cholesterol acyltransferase activities of the lipoprotei
83 SRBI cells was not due to increased acyl-coA:cholesterol acyltransferase activity and was observed ev
84 a-helicity, cholesterol efflux, and lecithin-cholesterol acyltransferase activity of the recombinant
85 ctivity and approximately 90% lower lecithin-cholesterol acyltransferase activity relative to circula
86 espite an increase in hepatic mRNA; lecithin:cholesterol acyltransferase activity toward endogenous E
87 orm with 88.1 +/- 8.5% reduction in lecithin-cholesterol acyltransferase activity, a finding corrobor
88 ol delivery to hepatocytes, support lecithin:cholesterol acyltransferase activity, and suppress infla
90 t shared regions of similarity with acyl CoA:cholesterol acyltransferase, an enzyme that also uses fa
93 he presence of normal activities of acyl-CoA:cholesterol acyltransferase and glycerol phosphate acylt
95 gests the possible interaction with lecithin-cholesterol acyltransferase and may shed light on the mo
96 ression on the microsomal levels of acyl-CoA:cholesterol acyltransferase and neutral cholesterol este
97 LDL-cholesterol to be esterified by acyl-CoA:cholesterol acyltransferase and stored in lipid droplets
98 logous to enzymes called glycerophospholipid-cholesterol acyltransferases and, following translocatio
100 e chemoattractant protein-1, acyl coenzyme A:cholesterol acyltransferase, and tissue factor, in lesio
101 s of diacylglycerol acyltransferase and acyl cholesterol acyltransferase are expressed in the lumen o
102 r-activated receptor modulators and lecithin-cholesterol acyltransferase-based therapy, hold great pr
103 associates more and activates human lecithin-cholesterol acyltransferase better than mouse apoA-I.
104 ., paraoxonase, apolipoprotein A-I, lecithin:cholesterol acyltransferase, cholesterol ester transfer
105 ce and the roles of plasma factors (lecithin-cholesterol acyltransferase, cholesterol ester transfer
106 (p = 0.0008, CI 95%: 1.58, 5.33); lecithin: cholesterol acyltransferase concentration (p = 0.024, CI
107 l particles reminiscent of those in lecithin/cholesterol acyltransferase deficiency and cholestasis).
109 (adrenocortical lipid depletion in acyl-CoA:cholesterol acyltransferase-deficient (Acact-/-) mice an
110 sc-associated apoA-I that binds the lecithin-cholesterol acyltransferase enzyme is well structured an
111 Cholesteryl ester synthesis by the acyl-CoA:cholesterol acyltransferase enzymes ACAT1 and ACAT2 is,
112 spholipases A (PLAs) and glycerophospholipid:cholesterol acyltransferases (GCATs), may target host ce
113 ted DGAT1), which is related to the acyl CoA:cholesterol acyltransferase gene family, or to any other
119 storage form by the enzyme acyl-coenzyme A: cholesterol acyltransferase, is a critical component of
120 residues and domains implicated in lecithin:cholesterol acyltransferase (LCAT) activation or lipid b
123 holipid transfer protein (PLTP) and lecithin cholesterol acyltransferase (LCAT) activities were decre
127 than other acyltransferases such as lecithin cholesterol acyltransferase (LCAT) and acyl CoA acyltran
128 laboratory previously reported that lecithin:cholesterol acyltransferase (LCAT) and LDL receptor doub
129 lesterol binding, esterification by lecithin/cholesterol acyltransferase (LCAT) and transfer by chole
130 pacity and 37% capacity to activate lecithin:cholesterol acyltransferase (LCAT) as compared to the WT
131 osomal phospholipase A2 (LPLA2) and lecithin:cholesterol acyltransferase (LCAT) belong to a structura
132 on dramatically reduces the rate of lecithin:cholesterol acyltransferase (LCAT) catalyzed cholesterol
135 revious studies have indicated that lecithin-cholesterol acyltransferase (LCAT) contributes significa
137 udy was to test the hypothesis that lecithin:cholesterol acyltransferase (LCAT) deficiency would acce
143 and interfacial binding activity of lecithin-cholesterol acyltransferase (LCAT) is affected different
145 Although the major function of lecithin-cholesterol acyltransferase (LCAT) is cholesterol esteri
146 fied cholesterol (UC) by the enzyme lecithin:cholesterol acyltransferase (LCAT) is cholesteryl ester
153 or protein-protein interaction with lecithin-cholesterol acyltransferase (LCAT) the enzyme for which
156 asma but reduces atherosclerosis in lecithin cholesterol acyltransferase (LCAT) transgenic (Tg) mice,
157 on in blood is closely regulated by lecithin-cholesterol acyltransferase (LCAT) which is produced in
159 pear to show that the reactivity of lecithin:cholesterol acyltransferase (LCAT) with the mutant is sl
160 ue T. gondii homologue of mammalian lecithin:cholesterol acyltransferase (LCAT), a key enzyme that pr
162 G esters (PE) by the plasma enzyme lecithin: cholesterol acyltransferase (LCAT), and by other enzyme(
163 ol acyltransferase (ACAT1), but not lecithin-cholesterol acyltransferase (LCAT), and to differ from h
164 apoA-I) activates the plasma enzyme lecithin:cholesterol acyltransferase (LCAT), catalyzing the rapid
165 ns, and had minimal reactivity with lecithin-cholesterol acyltransferase (LCAT), compared with rHDL p
166 l ester transfer protein (CETP) and lecithin:cholesterol acyltransferase (LCAT), on chromosome 16q; a
167 hydroxylase, Scavenger receptor B1, lecithin:cholesterol acyltransferase (LCAT), or apoA-I in the liv
168 show that certain proteins such as lecithin cholesterol acyltransferase (LCAT), phospholipid transfe
169 aturally occurring mutants of human lecithin-cholesterol acyltransferase (LCAT), T123I and N228K, wer
170 f cholesterol-containing r-HDL with lecithin-cholesterol acyltransferase (LCAT), to form cholesteryl
171 N-ethylmaleimide, an inhibitor of lecithin: cholesterol acyltransferase (LCAT), whereas CUC was enha
173 pathway is critically dependent on lecithin:cholesterol acyltransferase (LCAT), which rapidly conver
174 ted HDL and plasma from control and lecithin-cholesterol acyltransferase (LCAT)-deficient subjects to
181 quences identical to those of human lecithin:cholesterol acyltransferase-like lysophospholipase (LLPL
182 In this work, the functions of lecithin:cholesterol acyltransferase-like PLAs (LCAT-PLAs) in HFA
183 es, due primarily to an increase in lecithin:cholesterol acyltransferase-mediated (LCAT-mediated) cho
184 -term pharmacological inhibition of acyl-CoA:cholesterol acyltransferase-mediated cholesterol esterif
185 ates LDL uptake and degradation and acyl-CoA:cholesterol acyltransferase-mediated esterification of L
186 lesteryl ester transfer protein and lecithin:cholesterol acyltransferase only function optimally in h
187 lesteryl ester transfer protein and lecithin-cholesterol acyltransferase (phosphatidylcholine-sterol
188 cholesteryl ester transfer protein, lecithin:cholesterol acyltransferase (phosphatidylcholine-sterol
189 he first molecular probe of acyl-coenzyme A: cholesterol acyltransferase provided a key to understand
190 e of similar size, composition, and lecithin:cholesterol acyltransferase reactivity when compared to
191 apoA-I(-/-) HDL in the presence of lecithin cholesterol acyltransferase reorganized the large hetero
193 types toward a major plasma enzyme, lecithin:cholesterol acyltransferase responsible for the HDL matu
194 eletion of LRO1, a homolog of human lecithin cholesterol acyltransferase, resulted in a dramatic redu
195 phimurium translocates a glycerophospholipid:cholesterol acyltransferase (SseJ) into the host cytosol
196 mation, apoA-I activates the enzyme lecithin:cholesterol acyltransferase stimulating the formation of
197 MEDI6012 is a recombinant human lecithin-cholesterol acyltransferase that increases high-density
198 nzymes that esterify cholesterol (lecithin : cholesterol acyltransferase), transfer cholesterol (chol
200 ester formation in tissues, acyl coenzyme A:cholesterol acyltransferase types 1 and 2 (ACAT1 and ACA
203 ver, apoA-V was a poor activator of lecithin:cholesterol acyltransferase where the activity was 8.5 +
204 parameters of the lipophilic enzyme lecithin:cholesterol acyltransferase, which binds to phosphatidyl