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EC Number
General Information
Commentary
Reference
malfunction
NAD+-dependent SIRT1 deactivation has a key role on ischemia-reperfusion-induced apoptosis
malfunction
SIRT1 depletion by RNA interference attenuates capsaicin-induced apoptosis in A-549 cancer cells and autophagy in MRC-5 cells
metabolism
acetylation of Lys413 decreases catalysis and SIRT3 reactivates isocitrate dehydrogenase 2 upon deacetylation. SIRT3-dependent deacetylation of isocitrate dehydrogenase 2 suppresses cellular stress by reactive oxygen species (ROS). Acetylation of Lys413 is regulated by SIRT3 in response to calorie and glucose restriction
metabolism
caloric restriction can extend life-span by inducing SIRT1 expression and promoting the long-term survival of irreplaceable cells
metabolism
isoform SIRT3 levels modulate mitochondrial protein folding
metabolism
Sir2 is involved in the regulation of p53 function via deacetylation
metabolism
SIRT1 modulates DNA repair activity, which can be regulated by the acetylation status of repair protein Ku70 following DNA damage
metabolism
the deacetylation of [histone H4]-N6-acetyl-L-lysine16 by Sirt2 may be pivotal to the formation of condensed chromatin
metabolism
the enzyme can regulate flux and anapleurosis of this central metabolic cycle
physiological function
acetylation of heat shock protein 10 by isoform SIRT3 enhances medium-chain acyl-CoA dehydrogenase folding, enzyme activity, and fat oxidation
Results 1 - 10 of 20 > >>