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Stuart Smith

Researcher at Children's Hospital Oakland Research Institute

Publications -  75
Citations -  6640

Stuart Smith is an academic researcher from Children's Hospital Oakland Research Institute. The author has contributed to research in topics: Fatty acid synthase & Acyl carrier protein. The author has an hindex of 40, co-authored 75 publications receiving 6328 citations. Previous affiliations of Stuart Smith include University of California, San Francisco.

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Molecular cloning and sequencing of a cDNA encoding the thioesterase domain of the rat fatty acid synthetase.

TL;DR: The Thioesterase I domain exhibits a low, albeit discernible, homology with the discrete medium-chain S-acyl fatty acid synthetase thioester hydrolases from rat mammary gland and duck uropygial gland, suggesting a distant but common evolutionary ancestry for these proteins.
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Mammalian ACSF3 Protein Is a Malonyl-CoA Synthetase That Supplies the Chain Extender Units for Mitochondrial Fatty Acid Synthesis

TL;DR: The objective of this study was to identify a source of intramitochondrial malonyl-CoA that could be used for de novo fatty acid synthesis in mammalian mitochondria and found the mitochondrial ACSF3 enzyme is capable of filling this role by utilizing free malonic acid as substrate.
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Construction of a cDNA encoding the multifunctional animal fatty acid synthase and expression in Spodoptera frugiperda cells using baculoviral vectors.

TL;DR: Results indicate that, in the insect cell host, all seven catalytic components of the 2505-residue recombinant fatty acid synthase fold correctly, the acyl-carrier-protein domain is appropriately phosphopantetheinylated post-translationally, and the multifunctional polypeptide forms catalytically competent dimers.
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Head-to-Head Coiled Arrangement of the Subunits of the Animal Fatty Acid Synthase

TL;DR: The proximity of the N-terminal beta-ketoacyl synthase domains and their essential role in dimerization is consistent with a revised model for the FAS in which a head-to-head arrangement of two coiled subunits facilitates functional interactions between the dimeric beta- ketoacyL synthase and the acyl carrier protein domains of either subunit.