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Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice

Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice

http://www.wikidata.org/entity/Q29619786

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Sirtuins: Sir2-related NAD-dependent protein deacetylases p53-induced growth arrest is regulated by the mitochondrial SirT3 deacetylase Epigenetic regulation of caloric restriction in aging The flavoring agent dihydrocoumarin reverses epigenetic silencing and inhibits sirtuin deacetylases Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase.SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity Regulation of unfolded protein response modulator XBP1s by acetylation and deacetylation Sirtuin 1 is required for antagonist-induced transcriptional repression of androgen-responsive genes by the androgen receptor Regulation of WRN protein cellular localization and enzymatic activities by SIRT1-mediated deacetylation Negative regulation of the deacetylase SIRT1 by DBC1 Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy SIRT1 regulates the function of the Nijmegen breakage syndrome protein SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis Deacetylation of FOXO3 by SIRT1 or SIRT2 leads to Skp2-mediated FOXO3 ubiquitination and degradation MST1 promotes apoptosis through regulating Sirt1-dependent p53 deacetylation CK2 is the regulator of SIRT1 substrate-binding affinity, deacetylase activity and cellular response to DNA-damage hSirT1-dependent regulation of the PCAF-E2F1-p73 apoptotic pathway in response to DNA damage p53 regulates Period2 expression and the circadian clock Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases SIRT1 redistribution on chromatin promotes genomic stability but alters gene expression during aging The NAD+-dependent deacetylase SIRT1 modulates CLOCK-mediated chromatin remodeling and circadian control SIRT1 suppresses beta-amyloid production by activating the alpha-secretase gene ADAM10.Human HMGCS2 regulates mitochondrial fatty acid oxidation and FGF21 expression in HepG2 cell line A novel pathway regulates memory and plasticity via SIRT1 and miR-134 SRT1720 improves survival and healthspan of obese mice SIRT1 promotes the central adaptive response to diet restriction through activation of the dorsomedial and lateral nuclei of the hypothalamus.Biochemical effects of SIRT1 activators Lysine acetylation: codified crosstalk with other posttranslational modifications A fasting inducible switch modulates gluconeogenesis via activator/coactivator exchange Nicotinamide restores cognition in Alzheimer's disease transgenic mice via a mechanism involving sirtuin inhibition and selective reduction of Thr231-phosphotau Calorie restriction and the exercise of chromatin miR-34a repression of SIRT1 regulates apoptosis SIRT6 in DNA repair, metabolism and ageing Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?SIRT1 regulates HIV transcription via Tat deacetylation Sirt1 regulates insulin secretion by repressing UCP2 in pancreatic beta cells Role of Sirtuins in Linking Metabolic Syndrome with Depression In Search of New Therapeutic Targets in Obesity Treatment: Sirtuins Sirt1 and the Mitochondria

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Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice

http://www.wikidata.org/entity/Q29619786

description

2003 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

article publié dans les Procee ...... f the United States of America

@fr

artículu científicu espublizáu en 2003

@ast

im September 2003 veröffentlichter wissenschaftlicher Artikel

@de

scientific article (publication date: 16 September 2003)

@en

wetenschappelijk artikel (gepubliceerd op 2003/09/16)

@nl

наукова стаття, опублікована у вересні 2003

@uk

مقالة علمية (نشرت في 16-9-2003)

@ar

name

Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice

@ast

Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice

@en

type

label

Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice

@ast

Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice

@en

prefLabel

Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice

@ast

Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice

@en

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PNAS.1934713100

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Proceedings of the National Academy of Sciences of the United States of America

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Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice

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Alt FW

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Appella E

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Bronson R

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Cheng HL

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Chua KF

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Gu Y

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Manis JP

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Mostoslavsky R

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Patel P

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Saito S

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P2860

Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity

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

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

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

Tetralogy of fallot and other congenital heart defects in Hey2 mutant mice

Fibroblast growth factor receptor 3 is a negative regulator of bone growth

SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria

MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation

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