Articles with "purine nucleotide" as a keyword



Photo from archive.org

Genetic investigation of purine nucleotide imbalance in Saccharomyces cerevisiae

Sign Up to like & get
recommendations!
Published in 2020 at "Current Genetics"

DOI: 10.1007/s00294-020-01101-y

Abstract: Because metabolism is a complex balanced process involving multiple enzymes, understanding how organisms compensate for transient or permanent metabolic imbalance is a challenging task that can be more easily achieved in simpler unicellular organisms. The… read more here.

Keywords: imbalance; purine nucleotide; investigation purine; nucleotide imbalance ... See more keywords
Photo by nichi_iro from unsplash

Horizontal transfer of a pathway for coumarate catabolism unexpectedly inhibits purine nucleotide biosynthesis

Sign Up to like & get
recommendations!
Published in 2019 at "Molecular Microbiology"

DOI: 10.1111/mmi.14393

Abstract: A microbe’s ecological niche and biotechnological utility are determined by its specific set of co‐evolved metabolic pathways. The acquisition of new pathways, through horizontal gene transfer or genetic engineering, can have unpredictable consequences. Here we… read more here.

Keywords: catabolism; purine nucleotide; coumarate catabolism; nucleotide biosynthesis ... See more keywords
Photo from wikipedia

Structural basis of purine nucleotide inhibition of human uncoupling protein 1.

Sign Up to like & get
recommendations!
Published in 2023 at "Science advances"

DOI: 10.1126/sciadv.adh4251

Abstract: Mitochondrial uncoupling protein 1 (UCP1) gives brown adipose tissue of mammals its specialized ability to burn calories as heat for thermoregulation. When activated by fatty acids, UCP1 catalyzes the leak of protons across the mitochondrial… read more here.

Keywords: uncoupling protein; purine; structural basis; basis purine ... See more keywords

Abstract MP121: Deleting the 2-oxoglutarate- and Iron-dependent Prolyl Hydroxylase Ogfod1 Alters Purine Nucleotide Regulation and is Cardioprotective

Sign Up to like & get
recommendations!
Published in 2020 at "Circulation Research"

DOI: 10.1161/res.127.suppl_1.mp121

Abstract: Prolyl hydroxylation is a post-translational modification that regulates protein stability, turnover, and activity. The proteins that catalyze prolyl hydroxylation belong to the 2-oxoglutarate- and iron-dependent oxygenase family of enzymes. A newly-described member of this family… read more here.

Keywords: ogfod1; purine nucleotide; iron dependent; mice ... See more keywords