Sirtuin deacetylases in neurodegenerative diseases of aging

Sirtuin enzymes are a family of highly conserved protein deacetylases that depend on nicotinamide adenine dinucleotide (NAD+) for their activity. There are seven sirtuins in mammals and these proteins have been linked with caloric restriction and aging by modulating energy metabolism, genomic stabil...

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Bibliographic Details
Main Authors: Herskovits, A. Zara (Contributor), Guarente, Leonard Pershing (Contributor)
Other Authors: Massachusetts Institute of Technology. Department of Biology (Contributor)
Format: Article
Language:English
Published: Nature Publishing Group, 2014-01-24T17:17:02Z.
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Online Access:Get fulltext
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100 1 0 |a Herskovits, A. Zara  |e author 
100 1 0 |a Massachusetts Institute of Technology. Department of Biology  |e contributor 
100 1 0 |a Herskovits, A. Zara  |e contributor 
100 1 0 |a Guarente, Leonard Pershing  |e contributor 
700 1 0 |a Guarente, Leonard Pershing  |e author 
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520 |a Sirtuin enzymes are a family of highly conserved protein deacetylases that depend on nicotinamide adenine dinucleotide (NAD+) for their activity. There are seven sirtuins in mammals and these proteins have been linked with caloric restriction and aging by modulating energy metabolism, genomic stability and stress resistance. Sirtuin enzymes are potential therapeutic targets in a variety of human diseases including cancer, diabetes, inflammatory disorders and neurodegenerative disease. Modulation of sirtuin activity has been shown to impact the course of several aggregate-forming neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, Huntington's disease, amyotrophic lateral sclerosis and spinal and bulbar muscular atrophy. Sirtuins can influence the progression of neurodegenerative disorders by modulating transcription factor activity and directly deacetylating proteotoxic species. Here, we describe sirtuin protein targets in several aggregate-forming neurodegenerative diseases and discuss the therapeutic potential of compounds that modulate sirtuin activity in these disorders. 
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655 7 |a Article 
773 |t Cell Research