about
Sirtuin 1 is required for antagonist-induced transcriptional repression of androgen-responsive genes by the androgen receptorThe mammalian SIR2alpha protein has a role in embryogenesis and gametogenesisSirtuins deacetylate and activate mammalian acetyl-CoA synthetasesChromatin affinity-precipitation using a small metabolic molecule: its application to analysis of O-acetyl-ADP-riboseSRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1Hormonal control of androgen receptor function through SIRT1Apoptosis-like death in trypanosomatids: search for putative pathways and genes involvedSIRT1 regulates HIV transcription via Tat deacetylationExperimental study of the function of the excreted/secreted Leishmania LmSIR2 protein by heterologous expression in eukaryotic cell lineLocal and regional chromatin silencing in Candida glabrata: consequences for adhesion and the response to stressStructure and function of the BAH-containing domain of Orc1p in epigenetic silencingStructural basis for the role of the Sir3 AAA+ domain in silencing: interaction with Sir4 and unmethylated histone H3K79Dimerization of Sir3 via its C-terminal winged helix domain is essential for yeast heterochromatin formationRegulating repression: roles for the sir4 N-terminus in linker DNA protection and stabilization of epigenetic statesDifferential DNA affinity specifies roles for the origin recognition complex in budding yeast heterochromatinRestoration of silencing in Saccharomyces cerevisiae by tethering of a novel Sir2-interacting protein, Esc8.Dynamic changes in the subcellular distribution of Gpd1p in response to cell stress.Domain structure and protein interactions of the silent information regulator Sir3 revealed by screening a nested deletion library of protein fragments.HSP90 controls SIR2 mediated gene silencingStructure and function of the Saccharomyces cerevisiae Sir3 BAH domain.Rfm1, a novel tethering factor required to recruit the Hst1 histone deacetylase for repression of middle sporulation genes.Conversion of a replication origin to a silencer through a pathway shared by a Forkhead transcription factor and an S phase cyclin.Ribosome biogenesis factors bind a nuclear envelope SUN domain protein to cluster yeast telomeres.The nuclear GTPase Gsp1p can affect proper telomeric function through the Sir4 protein in Saccharomyces cerevisiae.Rpd3-dependent boundary formation at telomeres by removal of Sir2 substrateThe NAD(+)-dependent Sir2p histone deacetylase is a negative regulator of chromosomal DNA replication.Telomere tethering at the nuclear periphery is essential for efficient DNA double strand break repair in subtelomeric region.Dietary antiaging phytochemicals and mechanisms associated with prolonged survivalHistone deacetylases play a major role in the transcriptional regulation of the Plasmodium falciparum life cycleSIRT1 suppresses activator protein-1 transcriptional activity and cyclooxygenase-2 expression in macrophagesThe role of multiple marks in epigenetic silencing and the emergence of a stable bivalent chromatin stateHeterochromatin and gene positioning: inside, outside, any side?Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient miceNicotinamide clearance by Pnc1 directly regulates Sir2-mediated silencing and longevity.Proteome-wide prediction of acetylation substrates.Does heterochromatin protein 1 always follow code?Single-molecule analysis reveals clustering and epigenetic regulation of replication origins at the yeast rDNA locusIncrease in Ty1 cDNA recombination in yeast sir4 mutant strains at high temperature.Rtt107/Esc4 binds silent chromatin and DNA repair proteins using different BRCT motifs.Interfering with glycolysis causes Sir2-dependent hyper-recombination of Saccharomyces cerevisiae plasmids.
P2860
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P2860
description
2001 nî lūn-bûn
@nan
2001 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
The molecular biology of the SIR proteins.
@ast
The molecular biology of the SIR proteins.
@en
The molecular biology of the SIR proteins.
@nl
type
label
The molecular biology of the SIR proteins.
@ast
The molecular biology of the SIR proteins.
@en
The molecular biology of the SIR proteins.
@nl
prefLabel
The molecular biology of the SIR proteins.
@ast
The molecular biology of the SIR proteins.
@en
The molecular biology of the SIR proteins.
@nl
P1433
P1476
The molecular biology of the SIR proteins.
@en
P2093
P356
10.1016/S0378-1119(01)00741-7
P407
P577
2001-11-01T00:00:00Z