ArticleNature communications2015
Crystallographic structure of a small molecule SIRT1 activator-enzyme complex.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
108 citing papers in PubMed, 198 citations in OpenAlex.
- Roles of Sirtuin-1 in the Prevention of Intracranial Aneurysm Rupture in Mice.Hypertension (Dallas, Tex. : 1979) · 2026Article
- SIRT1 in Neurodegenerative Diseases: Molecular Mechanisms, Disease Relevance, and Therapeutic Potential.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Review
- 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
- Revisiting the p53:Sirt1 interaction in light of controlling p53 acetylation levels.Communications chemistry · 2026Article
- In vivo and in silico wound healing potential of Cannabis Sativa seed oil through inflammation mediators.BMC complementary medicine and therapies · 2026Article
- Factors Determining Sirtuin-1 Target Engagement.Advanced biology · 2026Review
- 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
- Alisol B 23-acetate alleviates high-fat diet-induced insulin resistance by activating the SIRT1/FOXO1 axis and PI3K/AKT pathway.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- Elucidating binding hot spots and structural stability in sirtuin family proteins for selective inhibitors: a computational approach.Frontiers in bioinformatics · 2026Article
- Meiotic cohesion requires Sirt1 and preserving its activity in aging oocytes reduces missegregation.EMBO reports · 2025Article
- Article
- Melinjo-derived Gnetin C restores metabolic balance via dual adipose and hepatic effects in high-fat diet mice.Scientific reports · 2025Article
- Tandem Allosteric Effects of Reactant and Product that Promote Deacetylation Cycles in Sir2.Journal of chemical information and modeling · 2025Article
- Dimeric guaianolide sesquiterpenoids from the flowers of Chrysanthemum indicum ameliorate hepatic steatosis through mitigating SIRT1-mediated lipid accumulation and ferroptosis.Journal of advanced research · 2025Article
- Targeting DNA damage in ageing: towards supercharging DNA repair.Nature reviews. Drug discovery · 2025Review
- Co-administration of Spirulina and L-carnitine preserves ovarian reserve in a rat model of premature ovarian insufficiency via SIRT1 regulation of oxidative stress, inflammation, and apoptosis.Scientific reports · 2025Article
- Article
- Dietary compounds activates sirtuins - a computational modeling approach towards the management of ageing.BMC biotechnology · 2025Article
48 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
33 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SIRT1, the founding member of the mammalian family of seven NAD(+)-dependent sirtuins, is composed of 747 amino acids forming a catalytic domain and extended N- and C-terminal regions. We report the design and characterization of an engineered human SIRT1 construct (mini-hSIRT1) containing the minimal structural elements required for lysine deacetylation and catalytic activation by small molecule sirtuin-activating compounds (STACs). Using this construct, we solved the crystal structure of a mini-hSIRT1-STAC complex, which revealed the STAC-binding site within the N-terminal domain of hSIRT1. Together with hydrogen-deuterium exchange mass spectrometry (HDX-MS) and site-directed mutagenesis using full-length hSIRT1, these data establish a specific STAC-binding site and identify key intermolecular interactions with hSIRT1. The determination of the interface governing the binding of STACs with human SIRT1 facilitates greater understanding of STAC activation of this enzyme, which holds significant promise as a therapeutic target for multiple human diseases.
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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.