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Keywords: Sirt1
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Biochem J (2013) 456 (1): 89–98.
Published: 24 October 2013
... deamination of 5-methyl-cytosine at the CpG dinucleotide, thereby preventing C to T mutations. SIRT1 is a member of class III NAD + -dependent histone/protein deacetylases. In the present study, we demonstrate that SIRT1 interacts with residues 67–110 of hTDG (human TDG). In addition, SIRT1 enhances TDG...
Includes: Supplementary data
Biochem J (2013) 451 (2): 227–234.
Published: 28 March 2013
... endogenous Kv1.5 attenuated apoptotic β-cell death. Both GIP and GLP-1 increased phosphorylation and acetylation of Kv1.5 and its Kvβ2 protein subunit, leading to their enhanced interaction. Further studies demonstrated that CBP [CREB (cAMP-response-element-binding protein)-binding protein]/SirT1 mediated...
Includes: Supplementary data
Biochem J (2010) 429 (2): 273–282.
Published: 28 June 2010
... + -dependent histone deacetylase SIRT1 (sirtuin 1) and QR2 (quinone reductase 2). Nonetheless, the health benefits elicited by resveratrol as a direct result of these interactions with molecular targets have been questioned, since it is rapidly and extensively metabolized to sulfate and glucuronide conjugates...
Includes: Supplementary data
Biochem J (2007) 408 (1): 105–111.
Published: 29 October 2007
...Hiyaa S. Ghosh; James V. Spencer; Bobby Ng; Michael W. McBurney; Paul D. Robbins Sirt1 is an NAD + -dependent deacetylase that plays a role in cellular processes such as transcriptional regulation, stress response, longevity and apoptosis. Sirt1 deacetylates histone proteins and certain...