Human acyl-CoA:cholesterol acyltransferase-1 in the endoplasmic reticulum contains seven transmembrane domains
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Multiple functions of microsomal triglyceride transfer proteinHuman acyl-coenzyme A:cholesterol acyltransferase expressed in chinese hamster ovary cells: membrane topology and active site locationA critical role for the histidine residues in the catalytic function of acyl-CoA:cholesterol acyltransferase catalysis: evidence for catalytic difference between ACAT1 and ACAT2ACAT1 and ACAT2 membrane topology segregates a serine residue essential for activity to opposite sides of the endoplasmic reticulum membraneHuman acyl-coenzyme A:cholesterol acyltransferase 1 (acat1) sequences located in two different chromosomes (7 and 1) are required to produce a novel ACAT1 isoenzyme with additional sequence at the N terminusLipase maturation factor LMF1, membrane topology and interaction with lipase proteins in the endoplasmic reticulumMembrane topology of mouse stearoyl-CoA desaturase 1INF2 is an endoplasmic reticulum-associated formin protein.Acyl-CoA-binding and self-associating properties of a recombinant 13.3 kDa N-terminal fragment of diacylglycerol acyltransferase-1 from oilseed rape.Targeting of neutral cholesterol ester hydrolase to the endoplasmic reticulum via its N-terminal sequence.ACAT inhibition and amyloid beta reduction.The enzymes of neutral lipid synthesis.ACAT2 stimulates cholesteryl ester secretion in apoB-containing lipoproteins.Microsomal triglyceride transfer protein enhances cellular cholesteryl esterification by relieving product inhibition.The lipid-laden foam cell: an elusive target for therapeutic intervention.Acyl-coenzyme A:cholesterol acyltransferases.Diacylglycerol enrichment of endoplasmic reticulum or lipid droplets recruits perilipin 3/TIP47 during lipid storage and mobilization.Isoform-specific inhibitors of ACATs: recent advances and promising developments.Acyltransferase inhibitors: a patent review (2010-present).The ACAT2 expression of human leukocytes is responsible for the excretion of lipoproteins containing cholesteryl/steryl esters.Investigating the allosterism of acyl-CoA:cholesterol acyltransferase (ACAT) by using various sterols: in vitro and intact cell studies.Topological orientation of acyl-CoA:diacylglycerol acyltransferase-1 (DGAT1) and identification of a putative active site histidine and the role of the n terminus in dimer/tetramer formation.Identification of the interaction site within acyl-CoA:cholesterol acyltransferase 2 for the isoform-specific inhibitor pyripyropene ASterol metabolism.Mutant acyl-coenzyme A:cholesterol acyltransferase 1 devoid of cysteine residues remains catalytically active.Functional organization of MIR2, a novel viral regulator of selective endocytosis.Selective inhibition of sterolO-acyltransferase 1 isozyme by beauveriolide III in intact cells.Caveolin, cholesterol, and lipid droplets?Apicoplast targeting of a Toxoplasma gondii transmembrane protein requires a cytosolic tyrosine-based motif.Membrane topology of the murine fatty acid transport protein 1.The active site His-460 of human acyl-coenzyme A:cholesterol acyltransferase 1 resides in a hitherto undisclosed transmembrane domain.Role of Niemann-Pick type C1 protein in intracellular trafficking of low density lipoprotein-derived cholesterol.SOAT1;2 transfer acyl group to CHOL forming CHESTLocalization, topology, and function of the LCB1 subunit of serine palmitoyltransferase in mammalian cells.Mitochondrial glycerol phosphate acyltransferase contains two transmembrane domains with the active site in the N-terminal domain facing the cytosol.
P2860
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P2860
Human acyl-CoA:cholesterol acyltransferase-1 in the endoplasmic reticulum contains seven transmembrane domains
description
1999 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1999
@ast
im August 1999 veröffentlichter wissenschaftlicher Artikel
@de
scientific article (publication date: 13 August 1999)
@en
vedecký článok (publikovaný 1999/08/13)
@sk
vědecký článek publikovaný v roce 1999
@cs
wetenschappelijk artikel (gepubliceerd op 1999/08/13)
@nl
наукова стаття, опублікована в серпні 1999
@uk
name
Human acyl-CoA:cholesterol acy ...... ns seven transmembrane domains
@ast
Human acyl-CoA:cholesterol acy ...... ns seven transmembrane domains
@en
Human acyl-CoA:cholesterol acy ...... ns seven transmembrane domains
@nl
type
label
Human acyl-CoA:cholesterol acy ...... ns seven transmembrane domains
@ast
Human acyl-CoA:cholesterol acy ...... ns seven transmembrane domains
@en
Human acyl-CoA:cholesterol acy ...... ns seven transmembrane domains
@nl
prefLabel
Human acyl-CoA:cholesterol acy ...... ns seven transmembrane domains
@ast
Human acyl-CoA:cholesterol acy ...... ns seven transmembrane domains
@en
Human acyl-CoA:cholesterol acy ...... ns seven transmembrane domains
@nl
P2093
P2860
P356
P1476
Human acyl-CoA:cholesterol acy ...... ns seven transmembrane domains
@en
P2093
P2860
P304
23276-23285
P356
10.1074/JBC.274.33.23276
P407
P577
1999-08-01T00:00:00Z