Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase - Wikidata - wikimedia - TriplyDB

Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase

Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase

http://www.wikidata.org/entity/Q28242315

about

Metabolism leaves its mark on the powerhouse: recent progress in post-translational modifications of lysine in mitochondria SIRT2 as a Therapeutic Target for Age-Related Disorders SIRT2 regulates tumour hypoxia response by promoting HIF-1α hydroxylation Regulation of G6PD acetylation by SIRT2 and KAT9 modulates NADPH homeostasis and cell survival during oxidative stress Acetylation negatively regulates glycogen phosphorylase by recruiting protein phosphatase 1 Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth Lysine-5 acetylation negatively regulates lactate dehydrogenase A and is decreased in pancreatic cancer Sir-two-homolog 2 (Sirt2) modulates peripheral myelination through polarity protein Par-3/atypical protein kinase C (aPKC) signaling Reprogramming of energy metabolism as a driver of aging Potential Modulation of Sirtuins by Oxidative Stress Regulation of glycolysis and gluconeogenesis by acetylation of PKM and PEPCK Sirtuins as regulators of metabolism and healthspan Metabolic reprogramming by class I and II histone deacetylases Energy metabolism in the liver Regulation of Akt signaling by sirtuins: its implication in cardiac hypertrophy and aging Sirtuins in Cancer: a Balancing Act between Genome Stability and Metabolism SIRT2, a multi-talented deacetylase From sirtuin biology to human diseases: an update Nonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylases Sirtuins in epigenetic regulation Protein lysine acylation and cysteine succination by intermediates of energy metabolism Role of Ostm1 Cytosolic Complex with Kinesin 5B in Intracellular Dispersion and Trafficking.Systematic approaches to identify E3 ligase substrates Sirtuins in metabolism, DNA repair and cancer Signalling scaffolds and local organization of cellular behaviour The tumor suppressor SirT2 regulates cell cycle progression and genome stability by modulating the mitotic deposition of H4K20 methylation The mitochondrial isoform of phosphoenolpyruvate carboxykinase (PEPCK-M) and glucose homeostasis: has it been overlooked?SIRT2 ablation has no effect on tubulin acetylation in brain, cholesterol biosynthesis or the progression of Huntington's disease phenotypes in vivo Prenatal ethanol exposure causes glucose intolerance with increased hepatic gluconeogenesis and histone deacetylases in adult rat offspring: reversal by tauroursodeoxycholic acid Sirt2 functions in spindle organization and chromosome alignment in mouse oocyte meiosis BCKDH: the missing link in apicomplexan mitochondrial metabolism is required for full virulence of Toxoplasma gondii and Plasmodium berghei Overexpression of cytoplasmic TcSIR2RP1 and mitochondrial TcSIR2RP3 impacts on Trypanosoma cruzi growth and cell invasion Inhibition of Pig Phosphoenolpyruvate Carboxykinase Isoenzymes by 3-Mercaptopicolinic Acid and Novel Inhibitors SGTA antagonizes BAG6-mediated protein triage Phosphoenolpyruvate carboxykinase 1 gene (Pck1) displays parallel evolution between Old World and New World fruit bats Lysophosphatidic acid counteracts glucagon-induced hepatocyte glucose production via STAT3.Insights into Lysine Deacetylation of Natively Folded Substrate Proteins by Sirtuins.MARCH5-mediated quality control on acetylated Mfn1 facilitates mitochondrial homeostasis and cell survival.Sirtinol promotes PEPCK1 degradation and inhibits gluconeogenesis by inhibiting deacetylase SIRT2.High-salt intake negatively regulates fat deposition in mouse.

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P2860

Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase

http://www.wikidata.org/entity/Q28242315

description

2011 nî lūn-bûn

@nan

2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հուլիսին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

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name

Acetylation regulates gluconeo ...... ting the UBR5 ubiquitin ligase

@ast

Acetylation regulates gluconeo ...... ting the UBR5 ubiquitin ligase

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Acetylation regulates gluconeo ...... ting the UBR5 ubiquitin ligase

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type

label

Acetylation regulates gluconeo ...... ting the UBR5 ubiquitin ligase

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Acetylation regulates gluconeo ...... ting the UBR5 ubiquitin ligase

@en

Acetylation regulates gluconeo ...... ting the UBR5 ubiquitin ligase

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prefLabel

Acetylation regulates gluconeo ...... ting the UBR5 ubiquitin ligase

@ast

Acetylation regulates gluconeo ...... ting the UBR5 ubiquitin ligase

@en

Acetylation regulates gluconeo ...... ting the UBR5 ubiquitin ligase

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J.MOLCEL.2011.04.028

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Acetylation regulates gluconeo ...... ting the UBR5 ubiquitin ligase

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Kun-Liang Guan

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Lisha Zhou

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Mengtao Xiao

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

Shimin Zhao

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

Shiwen Wang

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

Wenqing Jiang

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

Yan Lin

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

Yue Xiong

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P2860

Identification of a human HECT family protein with homology to the Drosophila tumor suppressor gene hyperplastic discs

The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase

Regulation of cellular metabolism by protein lysine acetylation

HLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-mediated acetylation of p53

Mitotic regulation of SIRT2 by cyclin-dependent kinase 1-dependent phosphorylation

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

The structural basis of protein acetylation by the p300/CBP transcriptional coactivator

F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex.

Molecular chaperone targeting and regulation by BAG family proteins

Cooperation of HECT-domain ubiquitin ligase hHYD and DNA topoisomerase II-binding protein for DNA damage response

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