Nucleocytoplasmic shuttling of the NAD+-dependent histone deacetylase SIRT1
M Tanno, J Sakamoto, T Miura, K Shimamoto… - Journal of Biological …, 2007 - ASBMB
Sir2 (silent information regulator 2) is an NAD+-dependent histone deacetylase that
contributes to longevity in yeast. SIRT1, a mammalian Sir2 ortholog, deacetylates histones …
contributes to longevity in yeast. SIRT1, a mammalian Sir2 ortholog, deacetylates histones …
Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis
The human NAD+-dependent protein deacetylase SIRT2 resides predominantly in the
cytoplasm where it functions as a tubulin deacetylase. Here we report that SIRT2 maintains …
cytoplasm where it functions as a tubulin deacetylase. Here we report that SIRT2 maintains …
[HTML][HTML] Predominant expression of Sir2α, an NAD-dependent histone deacetylase, in the embryonic mouse heart and brain
J Sakamoto, T Miura, K Shimamoto, Y Horio - FEBS letters, 2004 - Elsevier
Sir2 is an NAD-dependent histone deacetylase that functions in longevity, gene silencing,
heterochromatin formation, DNA repair, and suppression of DNA recombination in yeast …
heterochromatin formation, DNA repair, and suppression of DNA recombination in yeast …
Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1
KJ Bitterman, RM Anderson, HY Cohen… - Journal of Biological …, 2002 - ASBMB
The Saccharomyces cerevisiae Sir2 protein is an NAD+-dependent histone deacetylase that
plays a critical role in transcriptional silencing, genome stability, and longevity. A human …
plays a critical role in transcriptional silencing, genome stability, and longevity. A human …
Human Sir2 and the 'silencing'of p53 activity
JS Smith - Trends in cell biology, 2002 - cell.com
Members of the evolutionarily conserved silent information regulator 2 (Sir2) protein family
are nicotinamide adenine dinucleotide (NAD+)-dependent histone deacetylases. In yeast …
are nicotinamide adenine dinucleotide (NAD+)-dependent histone deacetylases. In yeast …
Phosphorylation regulates SIRT1 function
T Sasaki, B Maier, KD Koclega, M Chruszcz, W Gluba… - PloS one, 2008 - journals.plos.org
Background SIR2 is an NAD+-dependent deacetylase–implicated in the regulation of
lifespan in species as diverse as yeast, worms, and flies. We previously reported that the …
lifespan in species as diverse as yeast, worms, and flies. We previously reported that the …
Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin
A Vaquero, M Scher, D Lee, H Erdjument-Bromage… - Molecular cell, 2004 - cell.com
We characterized human SirT1, one of the human homologs of the budding yeast Sir2p, an
NAD+-dependent histone deacetylase involved in establishing repressive chromatin and …
NAD+-dependent histone deacetylase involved in establishing repressive chromatin and …
Sir2: an NAD-dependent histone deacetylase that connects chromatin silencing, metabolism, and aging
S Imai, FB Johnson, RA Marciniak… - Cold Spring Harbor …, 2000 - symposium.cshlp.org
Under the condition of ADP-ribosylation reaction in vitro, NAD concentration is
approximately a few micromolar and the deacetylase activity of Sir2 is not detectable (Imai et …
approximately a few micromolar and the deacetylase activity of Sir2 is not detectable (Imai et …
Structure and chemistry of the Sir2 family of NAD+-dependent histone/protein deactylases
R Marmorstein - Biochemical Society Transactions, 2004 - portlandpress.com
The yeast Sir2 (silent information regulator-2) protein functions as an NAD+-dependent
histone deacetylase to silence gene expression from the mating-type locus, tolomeres and …
histone deacetylase to silence gene expression from the mating-type locus, tolomeres and …
[HTML][HTML] Human SIR2 deacetylates p53 and antagonizes PML/p53‐induced cellular senescence
E Langley, M Pearson, M Faretta, UM Bauer… - The EMBO …, 2002 - embopress.org
The yeast Sir2 protein mediates chromatin silencing through an intrinsic NAD‐dependent
histone deacetylase activity. Sir2 is a conserved protein and was recently shown to regulate …
histone deacetylase activity. Sir2 is a conserved protein and was recently shown to regulate …