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Sirtuins
Research News and Information
Definition of 'Sirtuins'A homologous family of proteins that includes the NAD-dependent protein deacetylases which deacetylate proteins by catalyzing the formation of O-acetyl-ADP-ribose from the ADP-RIBOSE moiety (of NAD) and the acetyl group that is being removed from the protein. Sir2p, from Saccharomyces cerevisiae, is the founding member and the family includes other homologs (HSTs - homologs of Sir Two). Some HISTONE DEACETYLASES (the Sir2-like HDACs) belong to this family of proteins. |
Monday, November 23, 2009
21 Oct 2009
There is emerging recognition of a novel fuel and redox sensing regulatory program that controls cellular adaptation via nonhistone protein lysine residue acetyl posttranslation modifications. This program functions in tissues with high energy ... Read more...
21 Oct 2009
On average, each human gene has approximately four SNPs (single nucleotide polymorphisms) in the coding region, half of which are nsSNPs (non-synonymous SNPs) or missense SNPs. Current attention is focused on those that are known to perturb function ... Read more...
MicroRNA 217 modulates endothelial cell senescence via silent information regulator 1.
26 Sep 2009
BACKGROUND: Aging is a major risk factor for the development of atherosclerosis and coronary artery disease. Through a microarray approach, we have identified a microRNA (miR-217) that is progressively expressed in endothelial cells with aging. ... Read more...
Latest indexed articles for 'Sirtuins'
These are the very latest articles for this heading:
- The emerging characterization of lysine residue deacetylation on the modulation of mitochondrial function and cardiovascular biology.
21 Oct 2009 - A survey of proteins encoded by non-synonymous single nucleotide polymorphisms reveals a significant fraction with altered stability and activity.
21 Oct 2009 - MicroRNA 217 modulates endothelial cell senescence via silent information regulator 1.
26 Sep 2009 - Reconstitution of heterochromatin-dependent transcriptional gene silencing.
22 Sep 2009 - Recombinational repair within heterochromatin requires ATP-dependent chromatin remodeling.
16 Sep 2009 - Resveratrol attenuates mitochondrial oxidative stress in coronary arterial endothelial cells.
9 Sep 2009 - Study of 1,4-dihydropyridine structural scaffold: discovery of novel sirtuin activators and inhibitors.
8 Sep 2009 - The role of sirtuins in the control of metabolic homeostasis.
30 Aug 2009 - SIRT1 regulation of apoptosis of human chondrocytes.
30 Aug 2009 - SIRT1 markedly extends replicative lifespan if the NAD+ salvage pathway is enhanced.
27 Aug 2009 - Cell cycle-dependent deacetylation of telomeric histone H3 lysine K56 by human SIRT6.
24 Aug 2009 - Caloric restriction, SIRT1 and longevity.
23 Aug 2009 - The sirtuin SIRT6 deacetylates H3 K56Ac in vivo to promote genomic stability.
20 Aug 2009 - Hyperinsulinism-hyperammonaemia syndrome: novel mutations in the GLUD1 gene and genotype-phenotype correlations.
16 Aug 2009 - Functional interplay between Parp-1 and SirT1 in genome integrity and chromatin-based processes.
10 Aug 2009 - Resveratrol inhibited Tat-induced HIV-1 LTR transactivation via NAD(+)-dependent SIRT1 activity.
3 Aug 2009 - Activation of SIRT1 by resveratrol represses transcription of the gene for the cytosolic form of phosphoenolpyruvate carboxykinase (GTP) by deacetylating hepatic nuclear factor 4alpha.
Aug 2009 - Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice.
Aug 2009 - Regulatory role of Sirt1 on the gene expression of fatty acid-binding protein 3 in cultured porcine adipocytes.
30 Jul 2009 - Distinct HIC1-SIRT1-p53 loop deregulation in lung squamous carcinoma and adenocarcinoma patients.
30 Jul 2009
See a longer list of these articles.
Technical information about 'Sirtuins'
Definition: A homologous family of proteins that includes the NAD-dependent protein deacetylases which deacetylate proteins by catalyzing the formation of O-acetyl-ADP-ribose from the ADP-RIBOSE moiety (of NAD) and the acetyl group that is being removed from the protein. Sir2p, from Saccharomyces cerevisiae, is the founding member and the family includes other homologs (HSTs - homologs of Sir Two). Some HISTONE DEACETYLASES (the Sir2-like HDACs) belong to this family of proteins.
Registry Number: EC 3.5.1.-
Descriptor UI: D037761
Alternative terms: Sirtuins; Silent Mating Type Information Regulator 2-like Proteins; Silent Mating Type Information Regulator 2 like Proteins; Sir2-like Proteins; Sir2 like Proteins; NAD-Dependent Protein Deacetylases; Deacetylases, NAD-Dependent Protein; NAD Dependent Protein Deacetylases; Protein Deacetylases, NAD-Dependent; Sir2-like Deacetylases; Deacetylases, Sir2-like; Sir2 like Deacetylases;
Related Mesh Headings: Histone Deacetylases; Silent Information Regulator Proteins, Saccharomyces cerevisiae;
Allowable Qualifiers: administration & dosage; adverse effects; analysis; antagonists & inhibitors; biosynthesis; blood; cerebrospinal fluid; chemical synthesis; classification; deficiency; diagnostic use; drug effects; economics; genetics; history; immunology; isolation & purification; metabolism; pharmacokinetics; pharmacology; physiology; poisoning; radiation effects; secretion; standards; supply & distribution; therapeutic use; toxicity; ultrastructure; urine; chemistry; contraindications; agonists;
Tree Number: D08.811.277.087.831; D08.811.913.400.725.115.845;
History Note: 2003
Technical Notes: note specific sirtuins in SCR