63 research outputs found
Real time reliability monitoring of hydro‐power plant by combined cognitive decision‐making technique
SET domain protein lysine methyltransferases: Structure, specificity and catalysis
Site- and state-specific lysine methylation of histones is catalyzed by a family of proteins that contain the evolutionarily conserved SET domain and plays a fundamental role in epigenetic regulation of gene activation and silencing in all eukaryotes. The recently determined three-dimensional structures of the SET domains from chromosomal proteins reveal that the core SET domain structure contains a two-domain architecture, consisting of a conserved anti-parallel β-barrel and a structurally variable insert that surround a unusual knot-like structure that comprises the enzyme active site. These structures of the SET domains, either in the free state or when bound to cofactor S-adenosyl-L-homocysteine and/or histone peptide, mimicking an enzyme/cofactor/substrate complex, further yield the structural insights into the molecular basis of the substrate specificity, methylation multiplicity and the catalytic mechanism of histone lysine methylation. © Birkhäuser Verlag, 2006.link_to_subscribed_fulltex
Operation Monitoring System Model of Small and Medium-sized Enterprises in Sichuan Province in 2012
- …