MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it trans-(-)-ε-Viniferin increases mitochondrial sirtuin 3 (SIRT3), activates AMP-activated protein kinase (AMPK), and protects cells in models of Huntington Disease. trans-(-)-ε-Viniferin increases mitochondrial sirtuin 3 (SIRT3), activates AMP-activated protein kinase (AMPK), and protects cells in models of Huntington Disease. The Journal of biological chemistry 2012 imex curation Fu J., Jin J., Cichewicz RH., Hageman SA., Ellis TK., Xiang L., Peng Q., Jiang M., Arbez N., Hotaling K., Ross CA., Duan W. Huntington's - Publications describing interactions involved in Huntington's disease wduan2@jhmi.edu 24-May-2021: Contacted by IntAct-Help. Only protein-protein interactions imex curation mouse-STHdhq111/q111 immortalised embryonic striatal cells with humanised HTT Exon 1 and 111 CAG repeats sthdhq111 STHdh Q111/Q111 https://www.coriell.org/0/sections/Search/Sample_Detail.aspx?Ref=CH00095&PgId=166 Coriell Cell Repositories;CH00095 Cellosaurus STHdhQ111 (CVCL_M591) anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Fu J., Jin J., Cichewicz RH., Hageman SA., Ellis TK., Xiang L., Peng Q., Jiang M., Arbez N., Hotaling K., Ross CA., Duan W. Huntington's - Publications describing interactions involved in Huntington's disease wduan2@jhmi.edu Accepted 2021-APR-08 AT 13:05 BST AT 13:05 BST by KALPANAP The Journal of biological chemistry 2012 Only protein-protein interactions imex curation imex curation sir3_mouse NAD-dependent protein deacetylase sirtuin-3 Regulatory protein SIR2 homolog 3 Sirt3 Sir2l3 SIR2-like protein 3 protein protein mouse Mus musculus Mouse MALDPLGAVVLQSIMALSGRLALAALRLWGPGGGRRPISLCVGASGGFGGGGSSEKKFSLQDVAELLRTRACSRVVVMVGAGISTPSGIPDFRSPGSGLYSNLQQYDIPYPEAIFELGFFFHNPKPFFMLAKELYPGHYRPNVTHYFLRLLHDKELLLRLYTQNIDGLERASGIPASKLVEAHGTFVTATCTVCRRSFPGEDIWADVMADRVPRCPVCTGVVKPDIVFFGEQLPARFLLHMADFALADLLLILGTSLEVEPFASLSEAVQKSVPRLLINRDLVGPFVLSPRRKDVVQLGDVVHGVERLVDLLGWTQELLDLMQRERGKLDGQDR mint NAD-dependent deacetylase. Despite some ability to deacetylate histones in vitro, it is unlikely in vivo D8C936A83C4A8AF7 sodm_mouse Superoxide dismutase [Mn], mitochondrial Sod2 Sod-2 protein protein mouse Mus musculus Mouse MLCRAACSTGRRLGPVAGAAGSRHKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNATEEKYHEALAKGDVTTQVALQPALKFNGGGHINHTIFWTNLSPKGGGEPKGELLEAIKRDFGSFEKFKEKLTAVSVGVQGSGWGWLGFNKEQGRLQIAACSNQDPLQGTTGLIPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYTACKK 9AE804C55A8357D9 sirt3-1 1 2 unspecified role unspecified role prey prey physiological level physiological level endogenous level endogenous endogenous endogenous level 3 unspecified role unspecified role bait bait physiological level physiological level endogenous level endogenous endogenous endogenous level physical association physical association fig. 4g Cell extracts were immunoprecipitated (IP) with anti-Mn-SOD antibody, and the immunoprecipitation product was blotted with acetyl-lysine antibody to detect the levels of acetylated Mn-SOD. Note that there is an interaction between Mn-SOD and SIRT3, and viniferin treatment decreased acetylated Mn-SOD levels.