2020年3月7日 · La Gran D - (KGDD) is a broadcast radio station in Portland, Oregon, United States, providing Mexican Grupera, Ranchera and Tejano music.

KGDD (1520 kHz) is an AM radio station broadcasting a Regional Mexican format. Licensed to Oregon City, Oregon, United States, it serves the Portland, Oregon area. The station is currently owned by Bustos Media of Oregon License, LLC.

2016年6月20日 · We found that PTP1B-deficient HER2+ xenografts have increased hypoxia, necrosis and impaired growth. In vitro, PTP1B deficiency sensitizes HER2+ BC lines to hypoxia by increasing NMOC by...

Alpha-ketoglutarate-dependent hydroxylases are a major class of non-heme iron proteins that catalyse a wide range of reactions. These reactions include hydroxylation reactions, demethylations, ring expansions, ring closures, and desaturations. [1][2] Functionally, the αKG-dependent hydroxylases are comparable to cytochrome P450 enzymes.

Ferrous iron and α-ketoglutarate (αKG)-dependent dioxygenases (αKGDs) are versatile enzymes that use dioxygen as an oxidant to catalyse various reactions via CH bond activation, including hydroxylation, dealkylation, desaturation, epoxidation, epimerisation, halogenation, cyclisation, peroxide formation, and ring expansion/contraction reactions.

RNF213 knockdown reverses the effects of PTP1B deficiency on α-KGDDs, NMOC and hypoxia-induced death of HER2 (+) BC cells, and partially restores tumorigenicity. We conclude that PTP1B acts via RNF213 to suppress α-KGDD activity and NMOC.

We discuss the biochemical and transcriptional mechanisms enabling these metabolites to control cell fate and review evidence that nutrient availability shapes tissue-specific fate programs via αKG-dependent dioxygenases. Keywords: 2-hydroxyglutarate; alpha-ketoglutarate; cell fate; chromatin modifications; succinate; αKG-dependent dioxygenases.

Damage from oxidative stress and mitochondrial dysfunction occur together in many common neurodegenerative diseases. The enzymes that form the mitochondrial α-ketoglutarate-dehydrogenase complex (KGDHC), a key and arguably rate-limiting enzyme system of the tricarboxylic acid cycle, might mediate the interaction of these processes.

含有Jumonji C结构域的组蛋白去甲基酶（JMJ）构成了KDM的主要群体，其中大多数在动植物中在进化上是保守的（Lu等，2008； Jambhekar等，2019）。 α-酮戊二酸（α-KG）主要来源于三羧酸（TCA）循环，是 JMJ 的必需底物（Klose 和Zhang，2007； Salminen 等，2014）。 迄今为止，是否以及如何调节 α-KG 的核可用性来调节 JMJ 活性，从而调节基因表达，尚不清楚。 在最新一期的 《科学》 杂志上， 黄等人。 (2023) 报告了 JMJ 在探索 α-KG 依赖性组蛋白去甲基 …

α-Ketoglutarate dehydrogenase (KGDH) dynamically regulates Jumonji C-domain-containing histone demethylase (JMJ)-dependent histone demethylation and gene expression in plants. Light promotes cytoplasmic KGDH translocation into the nucleus, where it catalyzes the oxidative decarboxylation of α-KG.