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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Acetoacetyl-CoA synthetase

acetoacetyl-CoA synthetase, AACS
activates acetoacetate to its CoA ester [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: ACID, Insulin, CAN, V1a, HAD
Papers on acetoacetyl-CoA synthetase
DNA hypermethylation of acetoacetyl-CoA synthetase contributes to inhibited cholesterol supply and steroidogenesis in fetal rat adrenals under prenatal nicotine exposure.
Ping et al., Wuhan, China. In Toxicology, Feb 2016
The following conjoint analysis of DNA methylation array with these differentially expressed genes suggested that acetoacetyl-CoA synthetase (AACS), the enzyme utilizing ketones for cholesterol supply, may play an important role in nicotine-induced cholesterol supply deficiency.
The structure of S. lividans acetoacetyl-CoA synthetase shows a novel interaction between the C-terminal extension and the N-terminal domain.
Gulick et al., Buffalo, United States. In Proteins, Mar 2015
The structure of an acetoacetyl-CoA synthetase (AacS) is presented that illustrates a novel aspect of this C-terminal domain.
BRAFV600E-Associated Gene Expression Profile: Early Changes in the Transcriptome, Based on a Transgenic Mouse Model of Papillary Thyroid Carcinoma.
Jarzab et al., Gliwice, Poland. In Plos One, 2014
CONCLUSION: The study identified 7 BRAF-induced genes that are specific for BRAF V600E-driven PTC and not previously reported as related to BRAF mutation or thyroid carcinoma: MMD, ITPR3, AACS, LAD1, PVRL3, ALDH3B1, and RASA1.
Differential Expression Profile of Chicken Embryo Fibroblast DF-1 Cells Infected with Cell-Adapted Infectious Bursal Disease Virus.
Leung et al., Hong Kong, Hong Kong. In Plos One, 2014
Over-expression of LIPA and CH25H, together with the suppression of STARD4, LSS and AACS genes implied a modulation of membrane fluidity and lipid raft arrangement in the infected cells.
Transcriptome analysis of hen preadipocytes treated with an adipogenic cocktail (DMIOA) with or without 20(S)-hydroxylcholesterol.
Kim et al., Winnipeg, Canada. In Bmc Genomics, 2014
Genes over-expressed in cells treated with DMIOA compared with those treated with DMIOA+20(S) include those involved in lipid metabolism (ENPP2, DHCR7, DHCR24), molecular transport (FADS2, SLC6A2, CD36), and vitamin and mineral metabolism (BCMO1, AACS, AR).
Degradation of acetoacetyl-CoA synthetase, a ketone body-utilizing enzyme, by legumain in the mouse kidney.
Fukui et al., Tokyo, Japan. In Biochem Biophys Res Commun, 2014
Acetoacetyl-CoA synthetase (AACS) is a ketone body-utilizing enzyme, which is responsible for the synthesis of cholesterol and fatty acids from ketone bodies in lipogenic tissues, such as the liver and adipocytes.
Identification of typical miRNAs and target genes in hepatocellular carcinoma by DNA microarray technique.
Zhang et al., Shanghai, China. In Eur Rev Med Pharmacol Sci, 2013
Four functional modules in the network were obtained, from which EGLN3, ALDOA, NCAM1 and AACS were the high confident target genes, respectively.
Acetoacetyl-CoA synthetase activity is controlled by a protein acetyltransferase with unique domain organization in Streptomyces lividans.
Escalante-Semerena et al., Madison, United States. In Mol Microbiol, 2013
Here we identify SlPatA, a GNAT in Streptomyces lividans with unique domain organization, and a new acetylation target, namely acetoacetyl-CoA synthetase (SlAacS).
Acetoacetyl-CoA synthetase, a ketone body-utilizing enzyme, is controlled by SREBP-2 and affects serum cholesterol levels.
Fukui et al., Tokyo, Japan. In Mol Genet Metab, 2012
However, ketone bodies have also been suggested to be used during the lipogenesis by the ketone body-utilizing enzyme, acetoacetyl-CoA synthetase (AACS).
Acetoacetyl-CoA synthetase is essential for normal neuronal development.
Fukui et al., Tokyo, Japan. In Biochem Biophys Res Commun, 2012
Acetoacetyl-CoA synthetase (AACS) is a ketone body-utilizing enzyme for the synthesis of cholesterol and fatty acids and is highly expressed in the brain.
The role of acetoacetyl-CoA synthetase, a ketone body-utilizing enzyme, in 3T3-L1 adipocyte differentiation.
Fukui et al., Tokyo, Japan. In Biol Pharm Bull, 2011
Acetoacetyl-CoA synthetase (AACS) is a ketone body-utilizing enzyme that converts acetoacetate to acetoacetyl-CoA in the cytosol and consequently provides acetyl units as the precursors for lipogenesis.
Comparison of vascular calcification scoring systems using plain radiographs to predict vascular stiffness in peritoneal dialysis patients.
Oh et al., Seoul, South Korea. In Nephrology (carlton), 2011
Peripheral vascular calcification score (PVCS) and abdominal aortic calcification score (AACS) were measured from plain radiographs.
Differences between human and rodent pancreatic islets: low pyruvate carboxylase, atp citrate lyase, and pyruvate carboxylation and high glucose-stimulated acetoacetate in human pancreatic islets.
Odorico et al., Madison, United States. In J Biol Chem, 2011
Human islets possessed high levels of succinyl-CoA:3-ketoacid-CoA transferase, an enzyme that forms acetoacetate in the mitochondria, and acetoacetyl-CoA synthetase, which uses acetoacetate to form acyl-CoAs in the cytosol.
A new pathway for poly(3-hydroxybutyrate) production in Escherichia coli and Corynebacterium glutamicum by functional expression of a new acetoacetyl-coenzyme A synthase.
Taguchi et al., Sapporo, Japan. In Biosci Biotechnol Biochem, 2010
A biosynthetic pathway for poly(3-hydroxybutyrate) [P(3HB)] was developed in Escherichia coli and Corynebacterium glutamicum by an acetoacetyl-coenzyme A (CoA) synthase (AACS) recently isolated from terpenoid-producing Streptomyces sp.
Transcriptional regulation of the human acetoacetyl-CoA synthetase gene by PPARgamma.
Haro et al., Barcelona, Spain. In Biochem J, 2010
the human AACS promoter is a PPARgamma target gene and this nuclear receptor is recruited to the AACS promoter by direct interaction with Sp1
Genetic obesity affects neural ketone body utilization in the rat brain.
Fukui et al., Tokyo, Japan. In Obesity (silver Spring), 2009
As acetoacetyl-CoA synthetase was expressed in neural-like cells, ketone bodies are assumed to be utilized for the synthesis of lipidic substances and to cause metabolic disorders in the nervous system of genetically obese rats.
Transcriptional regulation of ketone body-utilizing enzyme, acetoacetyl-CoA synthetase, by C/EBPalpha during adipocyte differentiation.
Fukui et al., Tokyo, Japan. In Biochim Biophys Acta, 2008
AACS promoter activity was controlled mainly by C/EBPalpha during adipogenesis.
Acetoacetyl-CoA synthetase gene is abundant in rat adipose, and related with fatty acid synthesis in mature adipocytes.
Fukui et al., Tokyo, Japan. In Biochem Biophys Res Commun, 2005
AACS in adipose tissue plays an important role in utilizing ketone body for the fatty acid-synthesis during adipose tissue development
Preferential utilization of ketone bodies in the brain and lung of newborn rats.
Sheehan et al., In Fed Proc, 1985
The preferential selection of AcAc for lipid synthesis in brain, as well as lung, stems in part from the active cytoplasmic pathway for generation of acetyl-CoA and acetoacetyl-CoA from the ketone via the actions of cytoplasmic acetoacetyl-CoA synthetase and thiolase.
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