Inhibition of SIRT1 catalytic activity increases p53 acetylation but does not alter cell survival following DNA damage. - Wikidata - awgldk - TriplyDB

Inhibition of SIRT1 catalytic activity increases p53 acetylation but does not alter cell survival following DNA damage.

Inhibition of SIRT1 catalytic activity increases p53 acetylation but does not alter cell survival following DNA damage.

http://www.wikidata.org/entity/Q40340028

about

p53-induced growth arrest is regulated by the mitochondrial SirT3 deacetylase AROS has a context-dependent effect on SIRT1 SIRT1 regulates the function of the Nijmegen breakage syndrome protein Sirt1 interacts with transducin-like enhancer of split-1 to inhibit nuclear factor kappaB-mediated transcription SIRT4 represses peroxisome proliferator-activated receptor α activity to suppress hepatic fat oxidation Transcriptional corepressor SMILE recruits SIRT1 to inhibit nuclear receptor estrogen receptor-related receptor gamma transactivation SIRT1 redistribution on chromatin promotes genomic stability but alters gene expression during aging Nutrient-sensitive mitochondrial NAD+ levels dictate cell survival Effect of nitroxoline on angiogenesis and growth of human bladder cancer Caloric restriction and resveratrol promote longevity through the Sirtuin-1-dependent induction of autophagy Sirtuin functions and modulation: from chemistry to the clinic Protective effects and mechanisms of sirtuins in the nervous system Epigenetic dysregulation in Epstein-Barr virus-associated gastric carcinoma: disease and treatments P53/microRNA-34-induced metabolic regulation: new opportunities in anticancer therapy Ex-527 inhibits Sirtuins by exploiting their unique NAD+-dependent deacetylation mechanism The role of p53 in cancer drug resistance and targeted chemotherapy Antidicer RNAse activity of monocyte chemotactic protein-induced protein-1 is critical for inducing angiogenesis NAD metabolism and sirtuins: metabolic regulation of protein deacetylation in stress and toxicity Synergistic interactions between HDAC and sirtuin inhibitors in human leukemia cells Resveratrol inhibits protein translation in hepatic cells SIRT1 activators suppress inflammatory responses through promotion of p65 deacetylation and inhibition of NF-κB activity Mir-34a mimics are potential therapeutic agents for p53-mutated and chemo-resistant brain tumour cells A potent and selective small molecule inhibitor of sirtuin 1 promotes differentiation of pluripotent P19 cells into functional neurons Mammalian sirtuins: biological insights and disease relevance Sirtuins in mammals: insights into their biological function Trans-resveratrol inhibits phosphorylation of Smad2/3 and represses FSHβ gene expression by a SirT1-independent pathway in LβT2 gonadotrope cells.Purkinje cell-specific males absent on the first (mMof) gene deletion results in an ataxia-telangiectasia-like neurological phenotype and backward walking in mice.Rejuvenating sirtuins: the rise of a new family of cancer drug targets tRNA synthetase counteracts c-Myc to develop functional vasculature.Fusaric Acid Induces DNA Damage and Post-Translational Modifications of p53 in Human Hepatocellular Carcinoma (HepG2 ) Cells.SIRT1 overexpression antagonizes cellular senescence with activated ERK/S6k1 signaling in human diploid fibroblasts Porphyrin homeostasis maintained by ABCG2 regulates self-renewal of embryonic stem cells Hypothalamic Sirt1 regulates food intake in a rodent model system.The class III histone deacetylase sirtuin 1 in immune suppression and its therapeutic potential in rheumatoid arthritis.Resveratrol regulates pathologic angiogenesis by a eukaryotic elongation factor-2 kinase-regulated pathway.Awakening p53 in senescent cells using nutlin-3.Expansion of oligodendrocyte progenitor cells following SIRT1 inactivation in the adult brain.SIRT1 regulates apoptosis and Nanog expression in mouse embryonic stem cells by controlling p53 subcellular localization SIRT1 promotes proliferation and inhibits the senescence-like phenotype in human melanoma cells.SIRT1 ameliorates age-related senescence of mesenchymal stem cells via modulating telomere shelterin.

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P2860

Inhibition of SIRT1 catalytic activity increases p53 acetylation but does not alter cell survival following DNA damage.

http://www.wikidata.org/entity/Q40340028

description

2006 nî lūn-bûn

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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2006年论文

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2006年论文

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name

Inhibition of SIRT1 catalytic ...... survival following DNA damage.

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type

label

Inhibition of SIRT1 catalytic ...... survival following DNA damage.

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Inhibition of SIRT1 catalytic ...... survival following DNA damage.

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MCB.26.1.28-38.2006

P1433

Molecular and Cellular Biology

P1476

Inhibition of SIRT1 catalytic ...... survival following DNA damage.

@en

P2093

Jonathan M Solomon

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

L Julie Huber

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

Lei Xu

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

Peter S DiStefano

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

Rao Pasupuleti

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Rory Curtis

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

Thomas McDonagh

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

P2860

Histone deacetylases specifically down-regulate p53-dependent gene activation

Negative control of p53 by Sir2alpha promotes cell survival under stress

hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase

Human Sir2-related protein SIRT1 associates with the bHLH repressors HES1 and HEY2 and is involved in HES1- and HEY2-mediated transcriptional repression

Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase.

Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-gamma

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

Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence.

Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase

Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state

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28-38

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10.1128/MCB.26.1.28-38.2006

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