ArticleGenes & development2015
Structural basis for allosteric, substrate-dependent stimulation of SIRT1 activity by resveratrol.
Article in Genes & development, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 143 papers.
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Who cites it
143 citing papers in PubMed, 242 citations in OpenAlex.
- Impact of sirtuin-1 expression on H3K56 acetylation and oxidative stress: a double-blind randomized controlled trial with resveratrol supplementation.Acta diabetologica · 2018Trial
- Dietary polyphenols in atherosclerosis: a review of molecular mechanisms, endothelial dysfunction, oxidative stress, and vascular inflammation.Molecular biology reports · 2026Review
- Roles of Sirtuin-1 in the Prevention of Intracranial Aneurysm Rupture in Mice.Hypertension (Dallas, Tex. : 1979) · 2026Article
- Interplay of Ser273 Phosphorylation and K268 and K293 Acetylation in PPARγ: Implications for PPARγ Activation.Proteins · 2026Article
- ERα/SIRT1 signaling mediates the metabolic regulatory benefits of pterostilbene.The Journal of biological chemistry · 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
- The Effects of Phosphorylation on the Structure and Function of Motif A, an Intrinsically Disordered Region within SIRT1.Biochemistry · 2026Article
- Harnessing the structural determinants amenable for polypharmacological behavior of 7D against Sirt1 and CXCR3.iScience · 2026Article
- Molecular Mechanisms and Network Pharmacology Revealing Therapeutic Potential of Acetamidosulfonamides against Parkinsonian Model.ACS omega · 2026Article
- Mechanistic basis of N-terminal domain-mediated allostery in SIRT6: integrating molecular dynamics simulations and biochemical assays.Molecular diversity · 2026Article
- Caffeic Acid Phenethyl Ester Enhanced the Klotho/SIRT1/Nrf2/HO-1 Axis to Protect Against Methylmercury-Induced ALS-Like Neurodegeneration.Molecular neurobiology · 2026Article
- The Effects of Phosphorylation on the Structure and Function of Motif A, an Intrinsically Disordered Region within SIRT1.bioRxiv : the preprint server for biology · 2026Article
- Metformin Regulation of the Liver Circadian Clock and Metabolic Aging: A Systems Modeling Study.Metabolites · 2026Article
- Reexamining Fat: Exploring Diversity, Plasticity, Development, Functional Implication, and Therapeutic Options.International journal of molecular sciences · 2026Review
- Unraveling Network Pharmacology-Based Therapeutics of Anthranilate Sulfonamides via Sirtuins/FOXO3a Cascade in Alzheimer's Disease.Journal of neurochemistry · 2026Article
- Computational and experimental analysis of oleanolic acid as an allosteric activator of SIRT1.Turkish journal of chemistry · 2026Article
- Pharmacological Foundation and Novel Insights of Resveratrol in Cardiovascular System: A Review.Current cardiology reviews · 2026Review
- Discovery of 5-(Substituted Phenyl)-2-aryl Benzimidazole Derivatives as SIRT1 Activators: Their Design,Current medicinal chemistry · 2026Article
- Article
- Melinjo-derived Gnetin C restores metabolic balance via dual adipose and hepatic effects in high-fat diet mice.Scientific reports · 2025Article
83 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sirtuins with an extended N-terminal domain (NTD), represented by yeast Sir2 and human SIRT1, harbor intrinsic mechanisms for regulation of their NAD-dependent deacetylase activities. Elucidation of the regulatory mechanisms is crucial for understanding the biological functions of sirtuins and development of potential therapeutics. In particular, SIRT1 has emerged as an attractive therapeutic target, and the search for SIRT1-activating compounds (STACs) has been actively pursued. However, the effectiveness of a class of reported STACs (represented by resveratrol) as direct SIRT1 activators is under debate due to the complication involving the use of fluorogenic substrates in in vitro assays. Future efforts of SIRT1-based therapeutics necessitate the dissection of the molecular mechanism of SIRT1 stimulation. We solved the structure of SIRT1 in complex with resveratrol and a 7-amino-4-methylcoumarin (AMC)-containing peptide. The structure reveals the presence of three resveratrol molecules, two of which mediate the interaction between the AMC peptide and the NTD of SIRT1. The two NTD-bound resveratrol molecules are principally responsible for promoting tighter binding between SIRT1 and the peptide and the stimulation of SIRT1 activity. The structural information provides valuable insights into regulation of SIRT1 activity and should benefit the development of authentic SIRT1 activators.
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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.