Source:http://linkedlifedata.com/resource/pubmed/id/20975832
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
2010-10-26
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pubmed:abstractText |
The NAD-dependent deacetylase SIRT1 is a nutrient-sensitive coordinator of stress-tolerance, multiple homeostatic processes and healthspan, while p53 is a stress-responsive transcription factor and our paramount tumour suppressor. Thus, SIRT1-mediated inhibition of p53 has been identified as a key node in the common biology of cancer, metabolism, development and ageing. However, precisely how SIRT1 integrates such diverse processes remains to be elucidated.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
1932-6203
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
e13502
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pubmed:meshHeading |
pubmed-meshheading:20975832-Acetylation,
pubmed-meshheading:20975832-Alternative Splicing,
pubmed-meshheading:20975832-Animals,
pubmed-meshheading:20975832-Exons,
pubmed-meshheading:20975832-Humans,
pubmed-meshheading:20975832-Mice,
pubmed-meshheading:20975832-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:20975832-Sirtuin 1,
pubmed-meshheading:20975832-Tumor Suppressor Protein p53
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pubmed:year |
2010
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pubmed:articleTitle |
SIRT1 undergoes alternative splicing in a novel auto-regulatory loop with p53.
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pubmed:affiliation |
YCR p53 Research Unit, Department of Biology, University of York, York, United Kingdom. clynch@cnio.es
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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