Literature DB >> 20409078

Aging and disease: connections to sirtuins.

Gizem Donmez1, Leonard Guarente.   

Abstract

The sirtuins are highly conserved NAD-dependent deacetylases that were shown to regulate lifespan in lower organisms and affect diseases of aging in mammals, such as diabetes, cancer, and inflammation. Most relevant to the amelioration of disease, the SIR2 ortholog SIRT1 has been shown to deacetylate many important transcription factors to exert an overarching influence on numerous metabolic pathways. Here we discuss several diseases of aging for which SIRT1 has been recently shown to confer protection. These findings suggest that manipulating sirtuin activity pharmacologically may be a fruitful area to improve human health.

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Year:  2010        PMID: 20409078     DOI: 10.1111/j.1474-9726.2010.00548.x

Source DB:  PubMed          Journal:  Aging Cell        ISSN: 1474-9718            Impact factor:   9.304


  138 in total

1.  p63-microRNA feedback in keratinocyte senescence.

Authors:  Pia Rivetti di Val Cervo; Anna Maria Lena; Milena Nicoloso; Simona Rossi; Mara Mancini; Huiqing Zhou; Gaelle Saintigny; Elena Dellambra; Teresa Odorisio; Christian Mahé; George Adrian Calin; Eleonora Candi; Gerry Melino
Journal:  Proc Natl Acad Sci U S A       Date:  2012-01-06       Impact factor: 11.205

2.  SIRT1 contains N- and C-terminal regions that potentiate deacetylase activity.

Authors:  Min Pan; Hua Yuan; Michael Brent; Emily Chen Ding; Ronen Marmorstein
Journal:  J Biol Chem       Date:  2011-12-07       Impact factor: 5.157

3.  Regulation of glycolytic enzyme phosphoglycerate mutase-1 by Sirt1 protein-mediated deacetylation.

Authors:  William C Hallows; Wei Yu; John M Denu
Journal:  J Biol Chem       Date:  2011-12-07       Impact factor: 5.157

4.  FoxO1 mediates an autofeedback loop regulating SIRT1 expression.

Authors:  Shiqin Xiong; Gloria Salazar; Nikolay Patrushev; R Wayne Alexander
Journal:  J Biol Chem       Date:  2010-12-13       Impact factor: 5.157

5.  Heat shock and caloric restriction have a synergistic effect on the heat shock response in a sir2.1-dependent manner in Caenorhabditis elegans.

Authors:  Rachel Raynes; Bruce D Leckey; Kevin Nguyen; Sandy D Westerheide
Journal:  J Biol Chem       Date:  2012-07-09       Impact factor: 5.157

6.  Healthspan Pharmacology.

Authors:  Mahtab Jafari
Journal:  Rejuvenation Res       Date:  2015-11-10       Impact factor: 4.663

7.  HDAC3 is negatively regulated by the nuclear protein DBC1.

Authors:  Claudia C S Chini; Carlos Escande; Veronica Nin; Eduardo N Chini
Journal:  J Biol Chem       Date:  2010-10-28       Impact factor: 5.157

8.  A high-confidence interaction map identifies SIRT1 as a mediator of acetylation of USP22 and the SAGA coactivator complex.

Authors:  Sean M Armour; Eric J Bennett; Craig R Braun; Xiao-Yong Zhang; Steven B McMahon; Steven P Gygi; J Wade Harper; David A Sinclair
Journal:  Mol Cell Biol       Date:  2013-02-04       Impact factor: 4.272

Review 9.  Significance of epigenetic landscape in cartilage regeneration from the cartilage development and pathology perspective.

Authors:  Jingting Li; James Ohliger; Ming Pei
Journal:  Stem Cells Dev       Date:  2014-04-01       Impact factor: 3.272

10.  SIRT1 suppresses the epithelial-to-mesenchymal transition in cancer metastasis and organ fibrosis.

Authors:  Petra Simic; Eric O Williams; Eric L Bell; Jing Jing Gong; Michael Bonkowski; Leonard Guarente
Journal:  Cell Rep       Date:  2013-04-11       Impact factor: 9.423

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