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486995, 487010, 661231, 688067, 702466, 703246, 703838, 486977, 663302, 735428, 487028
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a disulfide-linked apoprotein dimer is less effective as activator than apo A-I
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absolute requirement with phosphatidylcholine-cholesterol vesicles as a substrate
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activates recombinant enzymes
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activation level depends on the substrate, overview
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ApoA-I, required for activity, activation in inhibited by binding of haptoglobin
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association of Apo AI with HDLs activates LCAT activity, molecular mechanism, conformational changes in several exposed regions of Apo-AI might cause enzyyme LCAT activation. Apo AI-derived peptides display a disordered arrangement, with a strong tendency to adopt beta-sheet and random conformational structures as a function of concentration, but in the presence of lyso-C12-phosphocholine, maximal percentages of alpha-helical structures are observed
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both human and pig ApoA-1 can activate pig LCAT in cholesterol-lecithin liposomes
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can substitute LDL as activator of the LAT activity
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decreased stimulation of LCAT is observed when liposomes oxidized without haptoglobin are used
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distribution in HDL, overview
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glycation affects the structure of apoA-I and its ability to activate the enzyme
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glycosylated, the alpha-helix formed by residues 143-165 is essential for full activation activity
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in proteoliposomes, that stimulate the enzyme activity
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kinetic analysis of radioiodinated ApoA-I associated with HDL and radioiodinated ApoB on LDL, mechanism for the effect of LCAT on lipid and lipoprotein changes, overview
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most effective activator
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principal apolipoprotein of HDL, activates the enzyme, mutations of the activation site residues 110-160 of the apolipoprotein, responsible for activation, lead to loss of the activation activity, e.g. mutations A95D, Y100H, E110K, V156E, and H162Q of the protein
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principal apolipoprotein of HDL, activates the enzyme, the negative net charge of the protein is important for function in interaction with the enzyme, mutation of the negative charges to uncharged, or mutational doubling of the negatively charged residues, overview
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required for hydrolysis of ester linkage at carbon-2 position of phosphatidylcholine and for transesterification
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required for transferase and phospholipase activity
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required, other apolipoprotein are less effective
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the central helix 4-helix 5-helix 6 domain in apoA-I is the unique structural element that provides full specificity to apoA-I activation of LCAT through substantially more LCAT binding and substrate binding and presentation to LCAT thorough the presentation tunnel, molecular dynamics, role of apoA-I in activation of LCAT involved simulations of discoidal particles, overview
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the impact of glycation on apolipoprotein A-I structure and its ability to activate LCAT is investigated: The rate of LCAT-mediated cholesterol esterification in reconstituted HDL containing phosphatidylcholine and apoA-I varied according to the level of apoA-I glycation and progressively decreases as the extent of apoA-I glycation increases
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the naturally occurring mutant T123I is defective in activation by apo A-I
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Relaxed specificity of endoproteinase Asp-N: this enzyme cleaves at peptide bonds N-terminal to glutamate as well as aspartate and cysteic acid residues
1990
Tetaz, T.; Morrison, J.R.; Andreou, J.; Fidge, N.H.
Biochem. Int.
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Purification and partial characterization of a bacterial phospholipid: cholesterol acyltransferase
1982
Buckley, J.T.; Halasa, L.N.; MacIntyre, S.
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Lecithin-cholesterol acyltransferase from human plasma
1981
Doi, Y.; Nishida, T.
Methods Enzymol.
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Isolation, characterization, and assay of lecithin-cholesterol acyltransferase
1986
Albers, J.J.; Chen, C.H.; Lacko, A.G.
Methods Enzymol.
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Mechanisms of action of lecithin-cholesterol acyltransferase
1986
Fielding, C.J.
Methods Enzymol.
129
783-790
Isolation and properties of porcine lecithin:cholesterol acyltransferase
1986
Knipping, G.
Eur. J. Biochem.
154
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A rapid large-scale procedure for purification of lecithin-cholesterol acyltransferase from human and animal plasma
1985
Chen, C.H.; Albers, J.J.
Biochim. Biophys. Acta
834
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A method for isolating human plasma lecithin:cholesterol acyltransferase without using anti-apolipoprotein D, and its characterization
1983
Mahadevan, V.; Soloff, L.A.
Biochim. Biophys. Acta
752
89-97
Purification of human plasma lecithin:cholesterol acyltransferase and its specificity towards the acyl acceptor
1979
Kitabatake, K.; Piran, U.; Kamio, Y.; Doi, Y.; Nishida, T.
Biochim. Biophys. Acta
573
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Isolation, properties, and mechanism of in vitro action of lecithin: cholesterol acyltransferase from human plasma
1979
Chung, J.; Abano, D.A.; Fless, G.M.; Scanu, A.M.
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Lecithin cholesterol acyltransferase
2000
Jonas, A.
Biochim. Biophys. Acta
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Activation of plasma lysolecithin acyltransferase reaction by apolipoproteins A-I, C-I and E
1993
Liu, M.; Subbaiah, P.V.
Biochim. Biophys. Acta
1168
144-152
Biochemical and compositional analyses of recombinant lecithin:cholesterol acyltransferase (LCAT) obtained from a hepatic source
2000
Ayyobi, A.F.; Lacko, A.G.; Murray, K.; Nair, M.; Li, M.; Molhuizen, H.O.F.; Pritchard, P.H.
Biochim. Biophys. Acta
1484
1-13
Activation of lecithin cholesterol acyltransferase by a disulfide-linked apolipoprotein A-I dimer
1997
Calabresi, L.; Franceschini, G.; Burkybile, A.; Jonas, A.
Biochem. Biophys. Res. Commun.
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Structural and functional properties of two mutants of lecithin-cholesterol acyltransferase (T123I and N228K)
1998
Adimoolam, S.; Jin, L.; Grabbe, E.; Shieh, J.J.; Jonas, A.
J. Biol. Chem.
273
32561-32567
Chicken lecithin-cholesterol acyltransferase. Molecular characterization reveals unusual structure and expression pattern
1995
Hengstschlaeger-Ottnad, E.; Kuchler, K.; Schneider, W.J.
J. Biol. Chem.
270
26139-26145
Molecular mechanism of reverse cholesterol transport: reaction of pre-beta-migrating high-density lipoprotein with plasma lecithin/cholesterol acyltransferase
2004
Nakamura, Y.; Kotite, L.; Gan, Y.; Spencer, T.A.; Fielding, C.J.; Fielding, P.E.
Biochemistry
43
14811-14820
Apolipoprotein A-I helix 6 negatively charged residues attenuate lecithin-cholesterol acyltransferase (LCAT) reactivity
2005
Alexander, E.T.; Bhat, S.; Thomas, M.J.; Weinberg, R.B.; Cook, V.R.; Bharadwaj, M.S.; Sorci-Thomas, M.
Biochemistry
44
5409-5419
Natural mutations of apolipoprotein A-I impairing activation of lecithin:cholesterol acyltransferase
2003
Hoang, A.; Huang, W.; Sasaki, J.; Sviridov, D.
Biochim. Biophys. Acta
1631
72-76
Deletion of N-terminal amino acids from human lecithin:cholesterol acyltransferase differentially affects enzyme activity toward alpha- and beta-substrate lipoproteins
2003
Vickaryous, N.K.; Teh, E.M.; Stewart, B.; Dolphin, P.J.; Too, C.K.; McLeod, R.S.
Biochim. Biophys. Acta
1646
164-172
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Lecithin-cholesterol acyltransferase (LCAT) as a plasma glycoprotein: an overview
2004
Lima, V.L.M.; Coelho, L.C.B.B.; Kennedy, J.F.; Owen, J.S.; Dolphin, P.J.
Carbohydr. Polym.
55
179-191
Characterization of lecithin:cholesterol acyltransferase expressed in a human lung cell line
2004
Lane, S.B.; Tchedre, K.T.; Nair, M.P.; Thigpen, A.E.; Lacko, A.G.
Protein Expr. Purif.
36
157-164
Inhibitory effects of caffeic acid phenethyl ester on cancer cell metastasis mediated by the down-regulation of matrix metalloproteinase expression in human HT1080 fibrosarcoma cells
2006
Hwang, H.J.; Park, H.J.; Chung, H.J.; Min, H.Y.; Park, E.J.; Hong, J.Y.; Lee, S.K.
J. Nutr. Biochem.
17
356-362
Apolipoprotein E is the major physiological activator of lecithin-cholesterol acyltransferase (LCAT) on apolipoprotein B lipoproteins
2005
Zhao, Y.; Thorngate, F.E.; Weisgraber, K.H.; Williams, D.L.; Parks, J.S.
Biochemistry
44
1013-1025
The impact of glycation on apolipoprotein A-I structure and its ability to activate lecithin:cholesterol acyltransferase
2007
Nobecourt, E.; Davies, M.J.; Brown, B.E.; Curtiss, L.K.; Bonnet, D.J.; Charlton, F.; Januszewski, A.S.; Jenkins, A.J.; Barter, P.J.; Rye, K.A.
Diabetologia
50
643-653
Protein arginylation in rat brain cytosol: a proteomic analysis
2006
Decca, M.B.; Bosc, C.; Luche, S.; Brugiere, S.; Job, D.; Rabilloud, T.; Garin, J.; Hallak, M.E.
Neurochem. Res.
31
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Haptoglobin binding to apolipoprotein A-I prevents damage from hydroxyl radicals on its stimulatory activity of the enzyme lecithin-cholesterol acyl-transferase
2007
Salvatore, A.; Cigliano, L.; Bucci, E.M.; Corpillo, D.; Velasco, S.; Carlucci, A.; Pedone, C.; Abrescia, P.
Biochemistry
46
11158-11168
Effects of cross-link breakers, glycation inhibitors and insulin sensitisers on HDL function and the non-enzymatic glycation of apolipoprotein A-I
2008
Nobecourt, E.; Zeng, J.; Davies, M.J.; Brown, B.E.; Yadav, S.; Barter, P.J.; Rye, K.A.
Diabetologia
51
1008-1017
Haptoglobin from psoriatic patients exhibits decreased activity in binding haemoglobin and inhibiting lecithin-cholesterol acyltransferase activity
2008
Cigliano, L.; Maresca, B.; Salvatore, A.; Nino, M.; Monfrecola, G.; Ayala, F.; Carlucci, A.; Pugliese, R.C.; Pedone, C.; Abrescia, P.
J. Eur. Acad. Dermatol. Venereol.
22
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Dynamics of activation of lecithin:cholesterol acyltransferase by apolipoprotein A-I
2009
Jones, M.K.; Catte, A.; Li, L.; Segrest, J.P.
Biochemistry
48
11196-11210
Plasma lecithin: cholesterol acyltransferase activity modifies the inverse relationship of C-reactive protein with HDL cholesterol in nondiabetic men
2010
Dullaart, R.P.; Perton, F.; Kappelle, P.J.; de Vries, R.; Sluiter, W.J.; van Tol, A.
Biochim. Biophys. Acta
1801
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Lecithin: cholesterol acyltransferase and atherosclerosis: another high-density lipoprotein story that doesnt quite follow the script
2009
Rader, D.
Circulation
120
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Lecithin: cholesterol acyltransferase - from biochemistry to role in cardiovascular disease
2009
Rousset, X.; Vaisman, B.; Amar, M.; Sethi, A.; Remaley, A.
Curr. Opin. Endocrinol. Diabetes Obes.
16
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Haptoglobin binds the antiatherogenic protein apolipoprotein E - impairment of apolipoprotein E stimulation of both lecithin:cholesterol acyltransferase activity and cholesterol uptake by hepatocytes
2009
Cigliano, L.; Pugliese, C.R.; Spagnuolo, M.S.; Palumbo, R.; Abrescia, P.
FEBS J.
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Apolipoprotein A-I and lecithin:cholesterol acyltransferase transfer induce cholesterol unloading in complex atherosclerotic lesions
2009
Van Craeyveld, E.; Lievens, J.; Jacobs, F.; Feng, Y.; Snoeys, J.; De Geest, B.
Gene Ther.
16
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Plasma levels of lecithin:cholesterol acyltransferase and risk of future coronary artery disease in apparently healthy men and women: a prospective case-control analysis nested in the EPIC-Norfolk population study
2010
Holleboom, A.G.; Kuivenhoven, J.A.; Vergeer, M.; Hovingh, G.K.; van Miert, J.N.; Wareham, N.J.; Kastelein, J.J.; Khaw, K.T.; Boekholdt, S.M.
J. Lipid Res.
51
416-421
Adenoviral expression of human lecithin-cholesterol acyltransferase in nonhuman primates leads to an antiatherogenic lipoprotein phenotype by increasing high-density lipoprotein and lowering low-density lipoprotein
2009
Amar, M.J.; Shamburek, R.D.; Vaisman, B.; Knapper, C.L.; Foger, B.; Hoyt, R.F.; Santamarina-Fojo, S.; Brewer, H.B.; Remaley, A.T.
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58
568-575
Characterization and solution structure of mouse myristoylated methionine sulfoxide reductase A
2012
Lim, J.C.; Gruschus, J.M.; Ghesquiere, B.; Kim, G.; Piszczek, G.; Tjandra, N.; Levine, R.L.
J. Biol. Chem.
287
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A fluorescence method to detect and quantitate sterol esterification by lecithin:cholesterol acyltransferase
2013
Homan, R.; Esmaeil, N.; Mendelsohn, L.; Kato, G.J.
Anal. Biochem.
441
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Lecithin cholesterol acyltransferase (LCAT) activity in the presence of Apo-AI-derived peptides exposed to disorder-order conformational transitions
2013
Aguilar-Espinosa, S.L.; Mendoza-Espinosa, P.; Delgado-Coello, B.; Mas-Oliva, J.
Biochem. Biophys. Res. Commun.
441
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The enzyme lecithin-cholesterol acyltransferase esterifies cerebrosterol and limits the toxic effect of this oxysterol on SH-SY5Y cells
2014
La Marca, V.; Spagnuolo, M.S.; Cigliano, L.; Marasco, D.; Abrescia, P.
J. Neurochem.
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Myeloperoxidase targets apolipoprotein A-I for site-specific tyrosine chlorination in atherosclerotic lesions and generates dysfunctional high-density lipoprotein
2021
Jin, Z.; Zhou, L.; Tian, R.; Lu, N.
Chem. Res. Toxicol.
34
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