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1 core-containing particles by incubation with lecithin:cholesterol acyltransferase.
2 nd 9 contribute to the optimum activation of lecithin:cholesterol acyltransferase.
3 inus that is 32% identical to the vertebrate lecithin:cholesterol acyltransferase, a secreted phospho
4 pairs lipid binding, cholesterol efflux, and lecithin-cholesterol acyltransferase activities of the l
6 ion, alpha-helicity, cholesterol efflux, and lecithin-cholesterol acyltransferase activity of the rec
7 efflux activity and approximately 90% lower lecithin-cholesterol acyltransferase activity relative t
8 apoA-I form with 88.1 +/- 8.5% reduction in lecithin-cholesterol acyltransferase activity, a finding
9 changed despite an increase in hepatic mRNA; lecithin:cholesterol acyltransferase activity toward end
12 cture suggests the possible interaction with lecithin-cholesterol acyltransferase and may shed light
15 oliferator-activated receptor modulators and lecithin-cholesterol acyltransferase-based therapy, hold
16 A-I self-associates more and activates human lecithin-cholesterol acyltransferase better than mouse a
17 ail in mice and the roles of plasma factors (lecithin-cholesterol acyltransferase, cholesterol ester
18 lism (e.g., paraoxonase, apolipoprotein A-I, lecithin:cholesterol acyltransferase, cholesterol ester
19 discoidal particles reminiscent of those in lecithin/cholesterol acyltransferase deficiency and chol
21 ion of disc-associated apoA-I that binds the lecithin-cholesterol acyltransferase enzyme is well stru
23 sma phospholipid transfer protein (PLTP) and lecithin cholesterol acyltransferase (LCAT) activities w
24 complex than other acyltransferases such as lecithin cholesterol acyltransferase (LCAT) and acyl CoA
25 ATP-binding cassette transfer protein A1 and lecithin cholesterol acyltransferase (LCAT) gene loci.
29 els in plasma but reduces atherosclerosis in lecithin cholesterol acyltransferase (LCAT) transgenic (
33 ances have been made in our understanding of lecithin-cholesterol acyltransferase (LCAT) function.
34 nzymatic and interfacial binding activity of lecithin-cholesterol acyltransferase (LCAT) is affected
36 shown to be a physiological inhibitor of the lecithin-cholesterol acyltransferase (LCAT) reaction.
37 rmation for protein-protein interaction with lecithin-cholesterol acyltransferase (LCAT) the enzyme f
38 CE fraction in blood is closely regulated by lecithin-cholesterol acyltransferase (LCAT) which is pro
40 cholesterol acyltransferase (ACAT1), but not lecithin-cholesterol acyltransferase (LCAT), and to diff
41 ipoproteins, and had minimal reactivity with lecithin-cholesterol acyltransferase (LCAT), compared wi
42 Two naturally occurring mutants of human lecithin-cholesterol acyltransferase (LCAT), T123I and N
43 eatment of cholesterol-containing r-HDL with lecithin-cholesterol acyltransferase (LCAT), to form cho
47 ells but had diminished capacity to activate lecithin/cholesterol acyltransferase (LCAT) in vitro.
48 ted to PREG esters (PE) by the plasma enzyme lecithin: cholesterol acyltransferase (LCAT), and by oth
49 mino acid residues and domains implicated in lecithin:cholesterol acyltransferase (LCAT) activation o
51 asic motif responsible for lipid binding and lecithin:cholesterol acyltransferase (LCAT) activation.
54 her the altered secondary structure affected lecithin:cholesterol acyltransferase (LCAT) activity.
56 efflux capacity and 37% capacity to activate lecithin:cholesterol acyltransferase (LCAT) as compared
58 is mutation dramatically reduces the rate of lecithin:cholesterol acyltransferase (LCAT) catalyzed ch
60 resent study was to test the hypothesis that lecithin:cholesterol acyltransferase (LCAT) deficiency w
62 unesterified cholesterol (UC) by the enzyme lecithin:cholesterol acyltransferase (LCAT) is cholester
69 ements appear to show that the reactivity of lecithin:cholesterol acyltransferase (LCAT) with the mut
70 ed a unique T. gondii homologue of mammalian lecithin:cholesterol acyltransferase (LCAT), a key enzym
72 ein A-I (apoA-I) activates the plasma enzyme lecithin:cholesterol acyltransferase (LCAT), catalyzing
73 holesteryl ester transfer protein (CETP) and lecithin:cholesterol acyltransferase (LCAT), on chromoso
74 f 7alpha-hydroxylase, Scavenger receptor B1, lecithin:cholesterol acyltransferase (LCAT), or apoA-I i
80 o acid sequences identical to those of human lecithin:cholesterol acyltransferase-like lysophospholip
81 macrophages, due primarily to an increase in lecithin:cholesterol acyltransferase-mediated (LCAT-medi
82 human cholesteryl ester transfer protein and lecithin:cholesterol acyltransferase only function optim
83 s and cholesteryl ester transfer protein and lecithin-cholesterol acyltransferase (phosphatidylcholin
84 lipase, cholesteryl ester transfer protein, lecithin:cholesterol acyltransferase (phosphatidylcholin
85 poA-I were of similar size, composition, and lecithin:cholesterol acyltransferase reactivity when com
86 apoA-I to apoA-I(-/-) HDL in the presence of lecithin cholesterol acyltransferase reorganized the lar
87 particle types toward a major plasma enzyme, lecithin:cholesterol acyltransferase responsible for the
88 ntrast, deletion of LRO1, a homolog of human lecithin cholesterol acyltransferase, resulted in a dram
89 nd conformation, apoA-I activates the enzyme lecithin:cholesterol acyltransferase stimulating the for
90 encoding enzymes that esterify cholesterol (lecithin : cholesterol acyltransferase), transfer choles
93 The plasma cholesterol esterification enzyme lecithin:cholesterol acyltransferase was also compared.
95 kinetic parameters of the lipophilic enzyme lecithin:cholesterol acyltransferase, which binds to pho
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