Results 11 to 20 of about 141,799 (322)

The MDM2–p53–pyruvate carboxylase signalling axis couples mitochondrial metabolism to glucose-stimulated insulin secretion in pancreatic β-cells [PDF]

open access: goldNature Communications, 2016
Mice lacking the tumour suppressor p53 are partially protected from developing diabetes. Here the authors show that p53 is upregulated in the pancreas of diabetic mice where it impairs β cell function by repressing expression of mitochondrial pyruvate ...
Xiaomu Li, Jin-Kui Yang, Baile Wang
exaly   +4 more sources

Fibroblast pyruvate carboxylase is required for collagen production in the tumour microenvironment [PDF]

open access: yesNature Metabolism, 2021
The aberrant production of collagen by fibroblasts is a hallmark of many solid tumours and can influence cancer progression. How the mesenchymal cells in the tumour microenvironment maintain their production of extracellular matrix proteins as the ...
Simon Schwörer   +2 more
exaly   +3 more sources

Sustained Control of Pyruvate Carboxylase by the Essential Second Messenger Cyclic di-AMP in Bacillus subtilis

open access: yesmBio, 2022
In Bacillus subtilis and other Gram-positive bacteria, cyclic di-AMP is an essential second messenger that signals potassium availability by binding to a variety of proteins.
Larissa Krüger   +8 more
doaj   +2 more sources

Pyruvate carboxylase supports the pulmonary tropism of metastatic breast cancer

open access: yesBreast Cancer Research, 2018
Background Overcoming systemic dormancy and initiating secondary tumor grow under unique microenvironmental conditions is a major rate-limiting step in metastatic progression.
Aparna Shinde   +4 more
doaj   +2 more sources

Targeting Pyruvate Carboxylase Reduces Gluconeogenesis and Adiposity and Improves Insulin Resistance [PDF]

open access: hybridDiabetes, 2013
We measured the mRNA and protein expression of the key gluconeogenic enzymes in human liver biopsy specimens and found that only hepatic pyruvate carboxylase protein levels related strongly with glycemia.
Naoki Kumashiro   +20 more
openalex   +2 more sources

A Substrate-induced Biotin Binding Pocket in the Carboxyltransferase Domain of Pyruvate Carboxylase [PDF]

open access: yesJournal of Biological Chemistry, 2013
Biotin-dependent enzymes catalyze carboxyl transfer reactions by efficiently coordinating multiple reactions between spatially distinct active sites. Pyruvate carboxylase (PC), a multifunctional biotin-dependent enzyme, catalyzes the bicarbonate- and ...
Lietzan, Adam D, Maurice, Martin St.
core   +3 more sources

Targeting Pyruvate Carboxylase by a Small Molecule Suppresses Breast Cancer Progression

open access: yesAdvanced Science, 2020
Rapid metabolism differentiates cancer cells from normal cells and relies on anaplerotic pathways. However, the mechanisms of anaplerosis‐associated enzymes are rarely understood.
Qingxiang Lin   +12 more
doaj   +2 more sources

A distinct holoenzyme organization for two-subunit pyruvate carboxylase

open access: yesNature Communications, 2016
Pyruvate carboxylases are homotetrameric enzymes in eukaryotes and most bacteria. Here, the authors report the structure of an unusual two-subunit form of the enzyme from the Gram-negative bacterium Methylobacillus flagellates, revealing an unexpected ...
Philip H. Choi   +6 more
doaj   +2 more sources

Pyruvate carboxylase deficiency: An underestimated cause of lactic acidosis

open access: yesMolecular Genetics and Metabolism Reports, 2015
Pyruvate carboxylase (PC) is a biotin-containing mitochondrial enzyme that catalyzes the conversion of pyruvate to oxaloacetate, thereby being involved in gluconeogenesis and in energy production through replenishment of the tricarboxylic acid (TCA ...
F. Habarou   +13 more
doaj   +2 more sources

The Metabolic Fates of Pyruvate in Normal and Neoplastic Cells

open access: yesCells, 2021
Pyruvate occupies a central metabolic node by virtue of its position at the crossroads of glycolysis and the tricarboxylic acid (TCA) cycle and its production and fate being governed by numerous cell-intrinsic and extrinsic factors.
Edward V. Prochownik, Huabo Wang
doaj   +2 more sources

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