期刊
FUTURE MEDICINAL CHEMISTRY
卷 7, 期 6, 页码 765-782出版社
FUTURE SCI LTD
DOI: 10.4155/FMC.15.24
关键词
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资金
- European Union's Seventh Framework Programme for research, technological development and demonstration [241865, 602080]
- institutional funds from the Centre National de la Recherche Scientifique (CNRS)
- Institut National de la Sante et de la Recherche Medicale (INSERM)
- Universite de Strasbourg and the Universite de Lille 2
- French Infrastructure for Integrated Structural Biology (FRISBI) [ANR-10-INSB-05-01]
- Instruct (ESFRI)
- Deutsche Forschungsgemeinschaft [P10, RTG1976]
The sirtuins form a superfamily of evolutionarily conserved NAD(+)-dependent protein N-epsilon-acyl-lysine (AcK) deacylases with roles in a variety of key cellular processes. Sirtuins have a broadly conserved overall structure with a catalytic site formed by a hydrophobic channel between the NAD(+)-binding Rossmann fold domain and a smaller Zn2+-binding domain. Schistosomes express five members of the sirtuin family and generic sirtuin inhibitors induce apoptosis and death in schistosome larvae, the disruption of adult worm pairs, inhibition of egg laying and damage to the male and female worm reproductive systems. Sirtuins in schistosomes and other parasitic flatworms present structural differences from their human orthologues that should allow the development of selective inhibitors that can be developed as drug leads.
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