L
Leonard Guarente
Researcher at Massachusetts Institute of Technology
Publications - 353
Citations - 86116
Leonard Guarente is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Gene & Saccharomyces cerevisiae. The author has an hindex of 143, co-authored 352 publications receiving 80169 citations. Previous affiliations of Leonard Guarente include Novartis & Harvard University.
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Journal ArticleDOI
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
TL;DR: The analysis of two SIR2 mutations supports the idea that this deacetylase activity accounts for silencing, recombination suppression and extension of life span in vivo, and provides a molecular framework of NAD-dependent histone de acetylation that connects metabolism, genomic silencing and ageing in yeast and, perhaps, in higher eukaryotes.
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hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase
Homayoun Vaziri,Scott K. Dessain,Scott K. Dessain,Elinor Ng Eaton,Shin-ichiro Imai,Roy A. Frye,Tej K. Pandita,Leonard Guarente,Robert A. Weinberg +8 more
TL;DR: It is proposed that hSir2, the human homolog of the S. cerevisiae Sir2 protein known to be involved in cell aging and in the response to DNA damage, binds and deacetylates the p53 protein with a specificity for its C-terminal Lys382 residue.
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The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
TL;DR: It is shown that life span regulation by the Sir proteins is independent of their role in nonhomologous end joining, and increasing the gene dosage extends the life span in wild-type cells.
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Negative Control of p53 by Sir2α Promotes Cell Survival under Stress
Jianyuan Luo,Anatoly Y. Nikolaev,Shin-ichiro Imai,Delin Chen,Fei Su,Ariel L. Shiloh,Leonard Guarente,Wei Gu +7 more
TL;DR: It is shown that mammalian Sir2alpha physically interacts with p53 and attenuates p53-mediated functions, and Nicotinamide inhibits an NAD-dependent p53 deacetylation induced by Sir2 alpha, and also enhances the p53 acetylation levels in vivo.
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Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-gamma.
Frederic Picard,Martin Kurtev,Namjin Chung,Acharawan Topark-Ngarm,Thanaset Senawong,Rita Machado de Oliveira,Rita Machado de Oliveira,Mark Leid,Michael W. McBurney,Leonard Guarente +9 more
TL;DR: It is shown that the mammalian SIR2 orthologue, Sirt1 (sirtuin 1), activates a critical component of calorie restriction in mammals; that is, fat mobilization in white adipocytes.