ArticleBioscience reports2013
Molecular architecture of the human protein deacetylase Sirt1 and its regulation by AROS and resveratrol.
Article in Bioscience reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 33 citations in OpenAlex.
- Site-specific programming characterizes dynamic post-translational acetylation of histone H2B lysine 108 in mouse embryonic stem cells.Nature communications · 2026Article
- Ginsenoside Re Attenuates D-Galactose-Induced Aging-like Oxidative Stress in Cultured Bovine Oocytes via Activation of the SIRT1/Nrf2 Signaling Pathway.International journal of molecular sciences · 2026Article
- Factors Determining Sirtuin-1 Target Engagement.Advanced biology · 2026Review
- Review
- Sirtuins in Central Nervous System Tumors-Molecular Mechanisms and Therapeutic Targeting.Cells · 2025Review
- Novel 1,4-Dihydropyridines as Specific Binders and Activators of SIRT3 Impair Cell Viability and Clonogenicity and Downregulate Hypoxia-Induced Targets in Cancer Cells.Journal of medicinal chemistry · 2023Article
- The Role of Sirtuin 1 (SIRT1) in Neurodegeneration.Cureus · 2023Review
- Molecular Mechanism of Sirtuin 1 Inhibition by Human Immunodeficiency Virus 1 Tat Protein.Life (Basel, Switzerland) · 2023Article
- Potent and Specific Activators for Mitochondrial Sirtuins Sirt3 and Sirt5.Journal of medicinal chemistry · 2022Article
- Molecular Mechanism of Sirtuin 1 Modulation by the AROS Protein.International journal of molecular sciences · 2022Article
- Prediction and confirmation of a switch-like region within the N-terminal domain of hSIRT1.Biochemistry and biophysics reports · 2022Article
- Synergistic protection of quercetin and lycopene against oxidative stress via SIRT1-Nox4-ROS axis in HUVEC cells.Current research in food science · 2022Article
- CSAG2 is a cancer-specific activator of SIRT1.EMBO reports · 2020Article
- An Insulin-Responsive Sensor in the SIRT1 Disordered Region Binds DBC1 and PACS-2 to Control Enzyme Activity.Molecular cell · 2018Article
- Sirtuin activators and inhibitors: Promises, achievements, and challenges.Pharmacology & therapeutics · 2018Review
- Using mitochondrial sirtuins as drug targets: disease implications and available compounds.Cellular and molecular life sciences : CMLS · 2016Review
- BET Inhibition Upregulates SIRT1 and Alleviates Inflammatory Responses.Chembiochem : a European journal of chemical biology · 2015Article
- VEGF Receptor-2-Linked PI3K/Calpain/SIRT1 Activation Mediates Retinal Arteriolar Dilations to VEGF and Shear Stress.Investigative ophthalmology & visual science · 2015Article
- Crystallographic structure of a small molecule SIRT1 activator-enzyme complex.Nature communications · 2015Article
- The N-Terminal Domain of SIRT1 Is a Positive Regulator of Endogenous SIRT1-Dependent Deacetylation and Transcriptional Outputs.Cell reports · 2015Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sirtuins are NAD+-dependent protein deacetylases regulating metabolism, stress responses and ageing processes. Among the seven mammalian Sirtuins, Sirt1 is the physiologically best-studied isoform. It regulates nuclear functions such as chromatin remodelling and gene transcription, and it appears to mediate beneficial effects of a low calorie diet which can partly be mimicked by the Sirt1 activating polyphenol resveratrol. The molecular details of Sirt1 domain architecture and regulation, however, are little understood. It has a unique N-terminal domain and CTD (C-terminal domain) flanking a conserved Sirtuin catalytic core and these extensions are assumed to mediate Sirt1-specific features such as homo-oligomerization and activation by resveratrol. To analyse the architecture of human Sirt1 and functions of its N- and C-terminal extensions, we recombinantly produced Sirt1 and Sirt1 deletion constructs as well as the AROS (active regulator of Sirt1) protein. We then studied Sirt1 features such as molecular size, secondary structure and stimulation by small molecules and AROS. We find that Sirt1 is monomeric and has extended conformations in its flanking domains, likely disordered especially in the N-terminus, resulting in an increased hydrodynamic radius. Nevertheless, both termini increase Sirt1 deacetylase activity, indicating a regulatory function. We also find an unusual but defined conformation for AROS protein, which fails, however, to stimulate Sirt1. Resveratrol, in contrast, activates the Sirt1 catalytic core independent of the terminal domains, indicating a binding site within the catalytic core and suggesting that small molecule activators for other isoforms might also exist.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.