Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Alla Klyuyeva"'
Autor:
Olga V. Belyaeva, Kelli R. Goggans, Seung-Ah Lee, Lizhi Wu, Alla Klyuyeva, Natalia Y. Kedishvili, Kirill M. Popov, Mark K. Adams, Robert A. Kesterson
Publikováno v:
J Biol Chem
Retinol dehydrogenases catalyze the rate-limiting step in the biosynthesis of retinoic acid, a bioactive lipid molecule that regulates the expression of hundreds of genes by binding to nuclear transcription factors, the retinoic acid receptors. Sever
Autor:
Olga V. Belyaeva, Wojciech Krezel, Kelli R. Goggans, Kirill M. Popov, Natalia Y. Kedishvili, Alla Klyuyeva
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, 2021, 296, ⟨10.1016/j.jbc.2021.100323⟩
The Journal of Biological Chemistry
Journal of Biological Chemistry, 2021, 296, ⟨10.1016/j.jbc.2021.100323⟩
The Journal of Biological Chemistry
Liver is the central metabolic hub that coordinates carbohydrate and lipid metabolism. The bioactive derivative of vitamin A, retinoic acid (RA), was shown to regulate major metabolic genes including phosphoenolpyruvate carboxykinase, fatty acid synt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::482164d931d63e8619988426a47c4614
https://hal.science/hal-03708081
https://hal.science/hal-03708081
Several human enzymes of the short-chain dehydrogenase/reductase (SDR) superfamily of proteins exhibit catalytic oxidoreductive activity toward retinoid substrates in vitro. For some retinoid-active enzymes, their physiological significance for retin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f7e44f9219cf5d79cbb69bfeee9057bb
https://doi.org/10.1016/bs.mie.2020.02.013
https://doi.org/10.1016/bs.mie.2020.02.013
The pyruvate dehydrogenase complex (PDC) is a multienzyme assembly that converts pyruvate to acetyl-CoA. As pyruvate and acetyl-CoA play central roles in cellular metabolism, understanding PDC regulation is pivotal to understanding the larger metabol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7374d3dd5c092c299c138b8f8ada49d3
https://europepmc.org/articles/PMC6341403/
https://europepmc.org/articles/PMC6341403/
Publikováno v:
Biochemistry. 47:8358-8366
Mitochondrial pyruvate dehydrogenase kinase 2 (PDHK2) phosphorylates the pyruvate dehydrogenase multienzyme complex (PDC) and thereby controls the rate of oxidative decarboxylation of pyruvate. The activity of PDHK2 is regulated by a variety of metab
Publikováno v:
Journal of Biological Chemistry. 283:15789-15798
PDHK2 is a mitochondrial protein kinase that phosphorylates pyruvate dehydrogenase complex, thereby down-regulating the oxidation of pyruvate. Here, we present the crystal structure of PDHK2 bound to the inner lipoyl-bearing domain of dihydrolipoamid
Publikováno v:
Biochemistry. 46(29)
Pyruvate dehydrogenase kinase 2 (PDHK2) is a unique mitochondrial protein kinase that regulates the activity of the pyruvate dehydrogenase multienzyme complex (PDC). PDHK2 is an integral component of PDC tightly bound to the inner lipoyl-bearing doma
Publikováno v:
FEBS letters. 581(16)
Dichloroacetate (DCA) is a promising anticancer and antidiabetic compound targeting the mitochondrial pyruvate dehydrogenase kinase (PDHK). This study was undertaken in order to map the DCA-binding site of PDHK2. Here, we present evidence that R114,
Publikováno v:
The FASEB Journal. 21
Publikováno v:
The FASEB Journal. 21