Results 291 to 300 of about 89,084 (326)
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Acyl-coenzyme A binding protein (ACBP)
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 1999Acyl-coenzyme A binding proteins are known from a large group of eukaryote species and to bind a long chain length acyl-CoA ester with very high affinity. Detailed biochemical mapping of ligand binding properties has been obtained as well as in-depth structural studies on the bovine apo-protein and of the complex with palmitoyl-CoA using NMR ...
Kragelund, B.B. +2 more
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Acyl-Coenzyme A Binding Protein Expression Alters Liver Fatty Acyl-Coenzyme A Metabolism
Biochemistry, 2005Although studies in vitro and in yeast suggest that acyl-CoA binding protein ACBP may modulate long-chain fatty acyl-CoA (LCFA-CoA) distribution, its physiological function in mammals is unresolved. To address this issue, the effect of ACBP on liver LCFA-CoA pool size, acyl chain composition, distribution, and transacylation into more complex lipids ...
Huan, Huang +4 more
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Acyl coenzyme A dependent retinol esterification by acyl coenzyme A:diacylglycerol acyltransferase 1
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2005We provide biochemical evidence that enzymes involved in the synthesis of triacylglycerol, namely acyl coenzyme A:diacylglycerol acyltransferase (DGAT) and acyl coenzyme A:monoacylglycerol acyltransferase (MGAT), are capable of carrying out the acyl coenzyme A:retinol acyltransferase (ARAT) reaction.
Michael D, Orland +7 more
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Annals of Neurology, 2018
Riboflavin‐responsive multiple acyl–coenzyme A dehydrogenation deficiency (RR‐MADD) is an inherited fatty acid metabolism disorder mainly caused by genetic defects in electron transfer flavoprotein–ubiquinone oxidoreductase (ETF:QO).
Jingwen Xu +14 more
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Riboflavin‐responsive multiple acyl–coenzyme A dehydrogenation deficiency (RR‐MADD) is an inherited fatty acid metabolism disorder mainly caused by genetic defects in electron transfer flavoprotein–ubiquinone oxidoreductase (ETF:QO).
Jingwen Xu +14 more
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Inhibitors of Acyl-Coenzyme A: Cholesterol Acyltransferase
Current Drug Target -Cardiovascular & Hematological Disorders, 2005Acyl-coenzyme A: cholesterol acyltransferase (ACAT) is an intracellular enzyme that catalyzes the formation of cholesterol esters from cholesterol and fatty acyl-coenzyme A. Animal experiments showed that ACAT inhibitors reduce plasma cholesterol levels by suppressing absorption of dietary cholesterol and by suppressing the assembly and secretion of ...
Akira, Miyazaki +2 more
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ACS Chemical Biology, 2019
Malaria remains a worldwide concern in terms of morbidity and mortality. Limited understanding of the Plasmodium proteome makes it challenging to control malaria. Understanding of the expression and functions of different Plasmodium proteins will help in
Abhishek Kumar +3 more
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Malaria remains a worldwide concern in terms of morbidity and mortality. Limited understanding of the Plasmodium proteome makes it challenging to control malaria. Understanding of the expression and functions of different Plasmodium proteins will help in
Abhishek Kumar +3 more
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Fatty Acyl-Coenzyme A Dehydrogenases
Biochemical Society Transactions, 1978The general enzymology of @-oxidation has suffered extraordinary neglect since the broad outlines of the pathway were established in the 1950’s. For the acyl-CoA dehydrogenases the contributions from the Institute for Enzyme Research at the University of Wisconsin still represent the major part of our knowledge.
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Acyl-coenzyme A: cholesterol acyltransferase family
Frontiers of Biology in China, 2008The enzymes of the acyl-coenzyme A: cholesterol acyltransferase (ACAT) family are responsible for the in vivo synthesis of neutral lipids. They are potential drug targets for the intervention of atherosclerosis, hyperlipidemia, obesity, type II diabetes and even Alzheimer’s disease.
Yali Liu, Zhanyun Guo
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Biochemical Pharmacology, 1990
Cyclandelate was an effective inhibitor of rat hepatic acycloenzyme A: cholesterol acyltransferase (ACAT) with a concentration of 80 microM being required for half maximal inhibition. A similar effect was seen with human and rabbit liver microsomal enzymes.
F, Heffron, B, Middleton, D A, White
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Cyclandelate was an effective inhibitor of rat hepatic acycloenzyme A: cholesterol acyltransferase (ACAT) with a concentration of 80 microM being required for half maximal inhibition. A similar effect was seen with human and rabbit liver microsomal enzymes.
F, Heffron, B, Middleton, D A, White
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Sensor for free fatty acids based on acyl coenzyme-a synthetase and acyl coenzyme-a oxidase
Analytica Chimica Acta, 1989Abstract The measurement is based on monitoring dissolved oxgyen consumed by the two sequential reactions catalyzed by the enzymes immobilized in photo-cross-linkable poly (vinyl alcohol) resin (PVA-SbQ). A linear correlation was observed between current decrease and 0.3–2.6 mM oleic or palmitic acid.
Koji Sode +3 more
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