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PDK2/PARL senses defects in mitochondrial bioenergetics.
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The data demonstrate potential roles of PDK2 and ABCG2 polymorphisms in the metabolic phenotypes of Tibetan gout patients.
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High glycolysis and PDK2 overexpression are closely linked to cisplatin resistance in head and neck cancer cells, which can be reversed by PDK2 nhibition.
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both PDK 1 and 2 isoforms are overexpressed in cutaneous melanoma compared to nevi, this expression being associated with the expression of the mTOR pathway effectors and independent of the BRAF mutational status
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The findings of the present study reveal a novel survival pathway that functionally couples the unique glycolytic phenotype in cancer cells to hypoxia resistance via a PDK2-dependent mechanism that switches Bnip3 from cell death to survival.
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The final compound of this series, 2-[(2,4-dihydroxyphenyl)sulfonyl]isoindoline-4,6-diol, designated PS10, inhibits all four PDK isoforms with IC50 = 0.8 muM for PDK2.
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Germline mutations in PKD2 gene is associated with autosomal-dominant polycystic kidney disease.
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we for the first time demonstrated that a low-nutrient condition drives cancer cells to utilize glycolysis to produce ATP, and this increases the Warburg effect through a novel mechanism involving ROS/AMPK-dependent activation of PDK.
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Mitochondrial activation by inhibition of PDKII suppresses HIF1a signaling and angiogenesis in cancer.
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Inactivation of pyruvate dehydrogenase kinase 2 by mitochondrial reactive oxygen species.
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Results established that wild-type p53 prevents manifestation of the Warburg effect by controlling Pdk2. These findings elucidate a new mechanism by which p53 suppresses tumorigenesis acting at the level of cancer cell metabolism.
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PKD2 mutations are associated with autosomal dominant polycystic kidney disease.
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study of facilitated interaction between the pyruvate dehydrogenase kinase isoform 2 and the dihydrolipoyl acetyltransferase
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The increased PDK activity was independent of changes in intra-mitochondrial effectors, and PDK-2 and PDK-4 protein content, suggesting that it was caused by a change in the specific activity of the existing kinases.
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A mechanism for pyruvate dehydrogenase kinase isoform 2 regulation is supported in which kinase activity is limited by ADP dissociation and pyruvate binding.
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Reductive acetylation stimulates activity of pyruvate dehydrogenase kinase isoform 2 by speeding up ADP dissociation.
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in human muscle, hormonal and nutritional conditions may control PDK2 and PDK4 mRNA expression via a common signalling mechanism.
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Crystallographic studies reveal several PDHK2 structures with C-terminal cross arms that span a large trough region between the N-terminal regulatory (R) domains of the PDHK2 dimers. Three novel ligand binding sites are located in the R domain of PDHK2.
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analysis of ligand induced effects on pyruvate dehydrogenase kinase isoform 2
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These studies identify ORP9 as a PDK-2 substrate and negative regulator of Akt phosphorylation at the PDK-2 site.
