The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases.
By Joseph Landry, A. Sutton, S. Tafrov, Ryan C Heller, J. Stebbins, L. Pillus, R. Sternglanz. Proceedings of the National Academy of Sciences of the United States of America, 2000
987 citations recorded by the source corpus.
Subfields: Aging, Geriatrics and Gerontology, Physiology
View Paper: https://www.semanticscholar.org/paper/c67e3e124e937f3358dd7e8341394caf41d1dc69
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Citations in the corpus
- Calorie restriction, SIRT1 and metabolism: understanding longevity (2005, background): “Sir2 was shown to possess a remarkable enzymatic activity — NAD-dependent HISTONE-DEACETYLASE activit”
- SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis. (2006, background): “3, top panel) (Landry et al. 2000).”
- Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration (2002, background): “Sir2 exhibits an NAD-dependent histone deacetylase activity that is conserved among Sir2-family members and is required for chromatin silencing and lifespan extensio”
- Human SIR2 deacetylates p53 and antagonizes PML/p53‐induced cellular senescence (2002, background): “Recent studies have shown that ySir2 and its homologs possess NAD-dependent HDAC activity (Imai et al., 2000; Landry et al., 2000; Smith et al., 2000).”
- The SMRT and N-CoR Corepressors Are Activating Cofactors for Histone Deacetylase 3 (2001, background): “It has previously been shown that the yeast silencing protein Sir2 requires NAD cofactor to become an active deacetylase (24, 32 , 46).”
- Calorie restriction--the SIR2 connection. (2005, background): “The enzymatic activity of the SIR2 product was found r Tto be a highly unusual one, NAD-dependent histone deacetylase (Imai et al., 2000; Landry et al., 2000; Smith w eet al., 2000).”
- Therapeutic potential of NAD-boosting molecules: the in vivo evidence (2018, neutral): “In 1999, Frye discovered that mammalian sirtuins metabolize NAD+ (Frye, 1999), then the Guarente and Sternglanz labs revealed that yeast Sir2 is an NAD+-dependent histone deacetylase (Imai et al., 2000; Landry et al., 2000).”
- Histone deacetylases and cancer: causes and therapies (2001, background): “Three classes of HDAC have been identified that might be involved in modelling the structure of chromati”