SIRT3-dependent GOT2 acetylation status affects the malate-aspartate NADH shuttle activity and pancreatic tumor growth - Wikidata - awgldk - TriplyDB

SIRT3-dependent GOT2 acetylation status affects the malate-aspartate NADH shuttle activity and pancreatic tumor growth

SIRT3-dependent GOT2 acetylation status affects the malate-aspartate NADH shuttle activity and pancreatic tumor growth

http://www.wikidata.org/entity/Q28258574

about

Pancreatic Cancer Metabolism: Breaking It Down to Build It Back Up SIRT3 regulates progression and development of diseases of aging.Sirtuins in metabolism, DNA repair and cancer Pioglitazone-mediated reversal of elevated glucose metabolism in the airway epithelium of mouse lung adenocarcinomas.Sirtuin regulation in aging and injury Mechanisms and Dynamics of Protein Acetylation in Mitochondria.Glutaminolysis as a target for cancer therapy.Amino Acid Profiling of Zinc Resistant Prostate Cancer Cell Lines: Associations With Cancer Progression.Mitochondrial Sirtuins in Cancer: Emerging Roles and Therapeutic Potential.New insights in the development of pancreatic cancer.The Current State of NAD(+) -Dependent Histone Deacetylases (Sirtuins) as Novel Therapeutic Targets.TNFR2 Stimulation Promotes Mitochondrial Fusion via Stat3- and NF-kB-Dependent Activation of OPA1 Expression.Circadian and Feeding Rhythms Orchestrate the Diurnal Liver Acetylome.IL-17A promotes the proliferation of human nasopharyngeal carcinoma cells through p300-mediated Akt1 acetylation.PIK3CA mutant tumors depend on oxoglutarate dehydrogenase.The Glycolytic Switch in Tumors: How Many Players Are Involved?An interferon-independent lncRNA promotes viral replication by modulating cellular metabolism.Metabolic reprogramming by PCK1 promotes TCA cataplerosis, oxidative stress and apoptosis in liver cancer cells and suppresses hepatocellular carcinoma.Enzyme Complexes Important for the Glutamate-Glutamine Cycle.Downregulation of PCK2 remodels tricarboxylic acid cycle in tumor-repopulating cells of melanoma.The protective effect of procyanidinson tert-butyl hydroperoxide induced human hepatocyte HL7702 cell injury

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P2860

SIRT3-dependent GOT2 acetylation status affects the malate-aspartate NADH shuttle activity and pancreatic tumor growth

http://www.wikidata.org/entity/Q28258574

description

2015 nî lūn-bûn

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2015 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2015 թվականի ապրիլին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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name

SIRT3-dependent GOT2 acetylati ...... ty and pancreatic tumor growth

@ast

SIRT3-dependent GOT2 acetylati ...... ty and pancreatic tumor growth

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SIRT3-dependent GOT2 acetylati ...... ty and pancreatic tumor growth

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type

label

SIRT3-dependent GOT2 acetylati ...... ty and pancreatic tumor growth

@ast

SIRT3-dependent GOT2 acetylati ...... ty and pancreatic tumor growth

@en

SIRT3-dependent GOT2 acetylati ...... ty and pancreatic tumor growth

@nl

prefLabel

SIRT3-dependent GOT2 acetylati ...... ty and pancreatic tumor growth

@ast

SIRT3-dependent GOT2 acetylati ...... ty and pancreatic tumor growth

@en

SIRT3-dependent GOT2 acetylati ...... ty and pancreatic tumor growth

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The EMBO Journal

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SIRT3-dependent GOT2 acetylati ...... ty and pancreatic tumor growth

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Dan Ye

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Huaipeng Lin

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Hui Yang

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Kun-Liang Guan

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Lisha Zhou

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Mengli Zhang

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Qian Shi

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Shimin Zhao

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

Yue Xiong

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Yuzheng Zhao

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P2860

Targeting aspartate aminotransferase in breast cancer

Regulation of cellular metabolism by protein lysine acetylation

The NAD+-dependent deacetylase SIRT1 modulates CLOCK-mediated chromatin remodeling and circadian control

The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase

Biochemical and structural characterization of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV

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

Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1

Oxidative stress activates SIRT2 to deacetylate and stimulate phosphoglycerate mutase

Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) cosubstrate specificity of a Sir2 enzyme

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

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1110-25

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10.15252/EMBJ.201591041

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8

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34

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