Modulation of NF‐κB‐dependent transcription and cell survival by the SIRT1 deacetylase
By F. Yeung, Jamie E. Hoberg, Catherine S. Ramsey, Michael D Keller, David R. Jones, Roy A. Frye, Marty W. Mayo. EMBO Journal, 2004
2,787 citations recorded by the source corpus.
Subfields: Cancer Research, Geriatrics and Gerontology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/b45f13cb45ac2ed5c8864448fc1c3c8bfbcb6c7a
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Cancer Research
- N. Perkins
- R. Medzhitov
- T. Gilmore
- Lin-Feng Chen
- Jamie E. Hoberg
- Catherine S. Ramsey
- Marty W. Mayo
- Y. Mu
In Geriatrics and Gerontology
In Molecular Biology
Citations in the corpus
- Good cop, bad cop: the different faces of NF-κB (2006, background): “Different histone acetyl transferases (HATs), such as p300 and PCAF, are responsible for inducing at least some of these acetylations while HDACs such as HDAC3 and SIRT1 can target their removal.(13,55,56) Recently, phosphorylation of RelA at Ser-276 and Ser-536 has been shown to promote acetylation”
- Sirtuins in aging and age-related disease. (2006, background): “Other stress response-related proteins linked to Sirt1 are Ku70 and NF-κB (see below) (Cohen et al., 2004; Yeung et al., 2004).”
- Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway (2006, background): “Furthermore, Lys-310 deacetylation by corepressor complexes also provides a mechanism to inhibit RelA activity (Hoberg et al., 2004; Yeung et al., 2004).”
- Inhibiting NF-κB Activation by Small Molecules As a Therapeutic Strategy (2010, positive): “The K221 and K310 acetylation are associated with increased NF-κB target gene transcription [112] and are required for p65 activation [24], which is supported by the observations that SIRT driven deacetylation at K310 inhibits NF-κB target gene transcription [113].”
- Mammalian sirtuins--emerging roles in physiology, aging, and calorie restriction. (2006, background): “SIRT1 deacetylates a large number of substrates, including p53, Ku70, NF- B, and forkhead proteins to affect stress resistance in cells (Luo et al. 2001; Vaziri et al. 2001; Brunet et al. 2004; Cohen et al. 2004; Motta et al. 2004; Yeung et al. 2004), which may relate to the observed stress resistan”
- Calorie restriction--the SIR2 connection. (2005, background): “An exception to this rule may occur in the case of NF-kB, which Sirt1 also deacetylated and downregulated (Yeung et al., 2004).”