Results 11 to 20 of about 28,180 (258)

Characterization of interaction and ubiquitination of phosphoenolpyruvate carboxykinase by E3 ligase UBR5 [PDF]

open access: yesBiology Open, 2018
Phosphoenolpyruvate carboxykinase (PEPCK1) is ubiquitinated by E3 ubiquitin ligase UBR5, which was thought to be facilitated by the acetylation of Lys70, Lys71 and Lys594 in PEPCK1.
Qingya Shen   +4 more
doaj   +2 more sources

Structural and functional studies of phosphoenolpyruvate carboxykinase from Mycobacterium tuberculosis. [PDF]

open access: yesPLoS ONE, 2015
Tuberculosis, the second leading infectious disease killer after HIV, remains a top public health priority. The causative agent of tuberculosis, Mycobacterium tuberculosis (Mtb), which can cause both acute and clinically latent infections, reprograms ...
Iva Machová   +9 more
doaj   +2 more sources

Association of mitochondrial phosphoenolpyruvate carboxykinase with prognosis and immune regulation in hepatocellular carcinoma [PDF]

open access: yesScientific Reports
Mitochondrial phosphoenolpyruvate carboxykinase (PCK2), a mitochondrial isoenzyme, supports the growth of cancer cells under glucose deficiency conditions in vitro.
Chenxuan Li   +5 more
doaj   +2 more sources

O-GlcNAcylation mediates the control of cytosolic phosphoenolpyruvate carboxykinase activity via Pgc1α. [PDF]

open access: yesPLoS ONE, 2017
PGC1α is a coactivator of many transcription factors and cytosolic phosphoenolpyruvate carboxykinase (PCK1) is a key enzyme for gluconeogenesis. PGC1α interacts with the transcription factor PPARγ to stimulate PCK1 expression and thus de novo glucose ...
Pedro Latorre   +4 more
doaj   +2 more sources

Phosphoenolpyruvate carboxykinase maintains glycolysis-driven growth in Drosophila tumors [PDF]

open access: yesSci Rep, 2017
Published online: 14 September 2017Tumors frequently fail to pass on all their chromosomes correctly during cell division, and this chromosomal instability (CIN) causes irregular aneuploidy and oxidative stress in cancer cells.
Gregory, S.   +4 more
core   +4 more sources

The phosphoenolpyruvate carboxykinase (PEPCK) inhibitor, 3-mercaptopicolinic acid (3-MPA), induces myogenic differentiation in C2C12 cells [PDF]

open access: yesScientific Reports, 2020
Phosphoenolpyruvate carboxykinase (PEPCK) is a gluconeogenic enzyme with a cytosolic (Pck1/PEPCK-C) and mitochondrial (Pck2/PEPCK-M) isoform. Here we investigate the effect of 3-mercaptopicolinic acid (3-MPA), a PEPCK inhibitor, on C2C12 muscle cells. We
Madelaine C. Brearley   +4 more
doaj   +2 more sources

Inhibition of Pig Phosphoenolpyruvate Carboxykinase Isoenzymes by 3-Mercaptopicolinic Acid and Novel Inhibitors. [PDF]

open access: yesPLoS ONE, 2016
There exist two isoforms of cytosolic phosphoenolpyruvate carboxykinase (PEPCK-C) in pig populations that differ in a single amino acid (Met139Leu). The isoenzymes have different kinetic properties, affecting more strongly the Km and Vmax of nucleotides.
Jorge Hidalgo   +5 more
doaj   +2 more sources

Inhibition of phosphoenolpyruvate carboxykinase blocks lactate utilization and impairs tumor growth in colorectal cancer [PDF]

open access: yesCancer & Metabolism, 2019
Background Metabolic reprogramming is a key feature of malignant cells. While glucose is one of the primary substrates for malignant cells, cancer cells also display a remarkable metabolic flexibility. Depending on nutrient availability and requirements,
Emily D. Montal   +8 more
doaj   +2 more sources

Correction: O-GlcNAcylation mediates the control of cytosolic phosphoenolpyruvate carboxykinase activity via Pgc1α. [PDF]

open access: yesPLoS ONE, 2017
[This corrects the article DOI: 10.1371/journal.pone.0179988.].
PLOS ONE Staff
doaj   +2 more sources

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