SIRT3 deacetylates and increases pyruvate dehydrogenase activity in cancer cells. - Wikidata - awgldk - TriplyDB

SIRT3 deacetylates and increases pyruvate dehydrogenase activity in cancer cells.

SIRT3 deacetylates and increases pyruvate dehydrogenase activity in cancer cells.

http://www.wikidata.org/entity/Q42173205

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Potential Modulation of Sirtuins by Oxidative Stress SIRT3 regulates progression and development of diseases of aging.Transcriptome analysis around the onset of strawberry fruit ripening uncovers an important role of oxidative phosphorylation in ripening.PGC-1α and fasting-induced PDH regulation in mouse skeletal muscle High Sensitivity of SIRT3 Deficient Hearts to Ischemia-Reperfusion Is Associated with Mitochondrial Abnormalities.Mitochondrial sirtuins and their relationships with metabolic disease and cancer.Expression of pyruvate dehydrogenase is an independent prognostic marker in gastric cancer SIRT3 Enhances Glycolysis and Proliferation in SIRT3-Expressing Gastric Cancer Cells.Alpha-ketoglutarate dehydrogenase complex-dependent succinylation of proteins in neurons and neuronal cell lines.Using mitochondrial sirtuins as drug targets: disease implications and available compounds.Lack of Skeletal Muscle IL-6 Affects Pyruvate Dehydrogenase Activity at Rest and during Prolonged Exercise.Progressive mitochondrial protein lysine acetylation and heart failure in a model of Friedreich's ataxia cardiomyopathy.miRNA-regulated delivery of lincRNA-p21 suppresses β-catenin signaling and tumorigenicity of colorectal cancer stem cells Generation and Purification of Catalytically Active Recombinant Sirtuin5 (SIRT5) Protein.SIRT2-Mediated Deacetylation and Tetramerization of Pyruvate Kinase Directs Glycolysis and Tumor Growth An Artificial Reaction Promoter Modulates Mitochondrial Functions via Chemically Promoting Protein Acetylation.Caloric restriction increases brain mitochondrial calcium retention capacity and protects against excitotoxicity Sirtuins in glucose and lipid metabolism.Metabolic Catastrophe in Mice Lacking Transferrin Receptor in Muscle The pyruvate dehydrogenase complex in cancer: An old metabolic gatekeeper regulated by new pathways and pharmacological agents.Metabolic control of signalling pathways and metabolic auto-regulation.Sirtuins and the Metabolic Hurdles in Cancer.Hallmarks of Pulmonary Hypertension: Mesenchymal and Inflammatory Cell Metabolic Reprogramming.Regulation of cell growth and apoptosis through lactate dehydrogenase C over-expression in Chinese hamster ovary cells.Mitochondrial Sirtuins in Cancer: Emerging Roles and Therapeutic Potential.Post-translational modifications in mitochondria: protein signaling in the powerhouse.Manganese Superoxide Dismutase Acetylation and Dysregulation, Due to Loss of SIRT3 Activity, Promote a Luminal B-Like Breast Carcinogenic-Permissive Phenotype.SIRT3 deficiency promotes lung fibrosis by augmenting alveolar epithelial cell mitochondrial DNA damage and apoptosis.Cell-surface G-protein-coupled receptors for tumor-associated metabolites: A direct link to mitochondrial dysfunction in cancer.Palmitate-induced lipotoxicity alters acetylation of multiple proteins in clonal β cells and human pancreatic islets Nε- and O-Acetylation in Mycobacterium tuberculosis Lineage 7 and Lineage 4 Strains: Proteins Involved in Bioenergetics, Virulence, and Antimicrobial Resistance Are Acetylated.The Glycolytic Switch in Tumors: How Many Players Are Involved?Inflexibility of AMPK-mediated metabolic reprogramming in mitochondrial disease.SIRT3-Mediated Dimerization of IDH2 Directs Cancer Cell Metabolism and Tumor Growth.Metabolic Reprogramming and Redox Signaling in Pulmonary Hypertension.Effects of training status on PDH regulation in human skeletal muscle during exercise.Decreased Mitochondrial Pyruvate Transport Activity in the Diabetic Heart: ROLE OF MITOCHONDRIAL PYRUVATE CARRIER 2 (MPC2) ACETYLATION.Muscle interleukin-6 and fasting-induced PDH regulation in mouse skeletal muscle.Enzyme Complexes Important for the Glutamate-Glutamine Cycle.Loss of NAD-Dependent Protein Deacetylase Sirtuin-2 Alters Mitochondrial Protein Acetylation and Dysregulates Mitophagy.

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P2860

SIRT3 deacetylates and increases pyruvate dehydrogenase activity in cancer cells.

http://www.wikidata.org/entity/Q42173205

description

2014 nî lūn-bûn

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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2014年论文

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2014年论文

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name

SIRT3 deacetylates and increases pyruvate dehydrogenase activity in cancer cells.

@en

SIRT3 deacetylates and increases pyruvate dehydrogenase activity in cancer cells.

@nl

type

label

SIRT3 deacetylates and increases pyruvate dehydrogenase activity in cancer cells.

@en

SIRT3 deacetylates and increases pyruvate dehydrogenase activity in cancer cells.

@nl

prefLabel

SIRT3 deacetylates and increases pyruvate dehydrogenase activity in cancer cells.

@en

SIRT3 deacetylates and increases pyruvate dehydrogenase activity in cancer cells.

@nl

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J.FREERADBIOMED.2014.08.001

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Free Radical Biology and Medicine

P1476

SIRT3 deacetylates and increases pyruvate dehydrogenase activity in cancer cells

@en

P2093

Athanassios Vassilopoulos

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Barbara Jung

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Brett A Wagner

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David Gius

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Ha Yong Song

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Seong-Hoon Park

http://www.w3.org/2001/XMLSchema#string

Yueming Zhu

http://www.w3.org/2001/XMLSchema#string

P2860

Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2

Tyrosine phosphorylation of mitochondrial pyruvate dehydrogenase kinase 1 is important for cancer metabolism

Regulatory roles of the N-terminal domain based on crystal structures of human pyruvate dehydrogenase kinase 2 containing physiological and synthetic ligands

Pyruvate dehydrogenase complex activity controls metabolic and malignant phenotype in cancer cells

SIRT3 is a mitochondria-localized tumor suppressor required for maintenance of mitochondrial integrity and metabolism during stress

Links between metabolism and cancer

Lysine acetylation targets protein complexes and co-regulates major cellular functions

On the Origin of Cancer Cells

Substrate and functional diversity of lysine acetylation revealed by a proteomics survey

A mitochondria-K+ channel axis is suppressed in cancer and its normalization promotes apoptosis and inhibits cancer growth

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10.1016/J.FREERADBIOMED.2014.08.001

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76

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Garry R. Buettner

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265018661

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4364304

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