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RELA — SIRT1

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: SIRT1 — RELA (physical association, affinity chromatography technology) Yang et al., Am J Physiol Lung Cell Mol Physiol 2007*
• IRef Hprd Interaction: SIRT1 — RELA (in vivo) Yeung et al., EMBO J 2004*
• IRef Intact Interaction: Complex of NFKB1-SIRT1-RELA (association, anti tag coimmunoprecipitation) Yeung et al., EMBO J 2004*
• IRef Intact Interaction: SIRT1 — RELA (physical association, anti tag coimmunoprecipitation) Yeung et al., EMBO J 2004*
• IRef Intact Interaction: SIRT1 — RELA (physical association, anti bait coimmunoprecipitation) Yeung et al., EMBO J 2004*
• IRef Intact Interaction: SIRT1 — RELA (deacetylation reaction, deacetylase assay) Yeung et al., EMBO J 2004*

Text-mined interactions from Literome

Yeung et al., EMBO J 2004 : In this study, we demonstrate that SIRT1 , a nicotinamide adenosine dinucleotide dependent histone deacetylase, regulates the transcriptional activity of NF-kappaB
Yang et al., Am J Physiol Lung Cell Mol Physiol 2007 (Inflammation) : We hypothesized that cigarette smoke mediated proinflammatory cytokine release is regulated by SIRT1 by its interaction with NF-kappaB in a monocyte-macrophage cell line ( MonoMac6 ) and in inflammatory cells of rat lungs
Ghosh et al., Biochem J 2007 : We have demonstrated using co-transfection assays that Sirt1 and TLE1 repress NF-kappaB activity ... The catalytic mutant of Sirt1, Sirt1-H363Y, and the N-terminal Sirt1 fragment ( amino acids 1-270 ) also show similar repression activity, suggesting that the deacetylase activity of Sirt1 may not be critical for its effect on NF-kappaB activity ... Furthermore, analysis in Sirt1-null MEFs ( murine embryonic fibroblasts ) and HeLa cells stably expressing siRNA ( small interfering RNA ) specific to Sirt1 or TLE1 demonstrate that both Sirt1 and TLE1 are required for negative regulation of NF-kappaB activity
Pediconi et al., Mol Cell Biol 2009 : The NAD ( + ) -dependent histone deacetylase hSirT1 regulates cell survival and stress responses by inhibiting p53-, NF-kappaB- , and E2F1 dependent transcription
Stein et al., Aging 2010 (Atherosclerosis...) : However, SIRT1 prevented endothelial superoxide production, inhibited NF-kappaB signaling, and diminished expression of adhesion molecules ... However, SIRT1 prevented endothelial superoxide production, inhibited NF-kappaB signaling, and diminished expression of adhesion molecules
Zhang et al., Biochem Biophys Res Commun 2010 (Inflammation) : Our study indicates that p65/RelA mediates the TNF-alpha induced elevated expression of SIRT1 in VSMCs, shedding new light on the regulation of SIRT1 under inflammatory conditions
Kong et al., J Biol Chem 2011 : The recruitment of Sirt1, but not p300, requires Rel-A because blocking Rel-A nuclear translocation in T cells and siRNA mediated knockdown of Rel-A can inhibit Sirt1 binding to bclaf1 promoter