Browsing by Subject Metabolism

Jump to: 0-9 A B C D E F G H I J K L M N O P Q R S T U V W X Y Z
or enter first few letters:  
Showing results 1 to 4 of 4
  • OER000000863.pdf.jpg
  • Journal article


  • Authors : Romeiro, Natália C; Ferreira, Caroline M; Oliveira, Marcus F (2020)

  • White adipose tissue (WAT) is classically associated with energy storage in the form of triacylglycerol and is directly associated with metabolic disorders, including obesity. Mitochondria regulates cellular expenditure and are active in WAT. Although isolated mitochondria have been classically used to assess their functions, several artifacts can be introduced by this approach. Although methods to assess mitochondrial physiology in permeabilized WAT were proposed, importan...

  • OER000000379.pdf.jpg
  • Periodicals (Báo – Tạp chí)


  • Authors : Doan, Mary T; Neinast, Michael D; Varner, Erika L (2020)

  • Anabolic metabolism of carbon in mammals is mediated via the one and two carbon carriers S-adenosyl methionine and acetyl-coenzyme A (acetyl-CoA). In contrast, anabolic metabolism using three carbon units via propionate is not thought to occur. Mammals are primarily thought to oxidize the 3-carbon short chain fatty acid propionate by shunting propionyl-CoA to succinyl-CoA for entry into the TCA cycle. We found that this may not be absolute and ...

  • OER000000688.pdf.jpg
  • Journal article


  • Authors : Duran, Jordi; Brewer, M. Kathryn (2020)

  • Brain glycogen is mainly stored in astrocytes. However, recent studies both in vitro and in vivo indicate that glycogen also plays important roles in neurons. By conditional deletion of glycogen synthase (GYS1), we previously developed a mouse model entirely devoid of glycogen in the central nervous system (GYS1Nestin-KO). These mice displayed altered electrophysiological properties in the hippocampus and increased susceptibility to kainate-induced seizures. To underst...

  • OER000000363.pdf.jpg
  • Periodicals (Báo – Tạp chí)


  • Authors : Varner, Erika L; Trefel, Sophie; Bartee, David (2020)

  • Lysine lactoylation is a recently described protein post-translational modification (PTM). However, the biochemical pathways responsible for this acylation remain unclear. Two metabolite-dependent mechanisms have been proposed: enzymatic histone lysine lactoylation derived from lactoyl-coenzyme A (lactoyl-CoA, also termed lactyl-CoA), and non-enzymatic lysine lactoylation resulting from acyl-transfer via lactoyl-glutathione. While the former has precedent in the form of enzyme-catalyzed lysine acyl...