ArticleMethods in enzymology2016
Synthesis and Assay of SIRT1-Activating Compounds.
Article in Methods in enzymology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed, 12 citations in OpenAlex.
- Pharmacological Investigation of a Novel Resveratrol-like SIRT1 Activator Endowed with a Cardioprotective Profile.Molecules (Basel, Switzerland) · 2025Article
- The medicinal chemistry of mitochondrial dysfunction: a critical overview of efforts to modulate mitochondrial health.RSC medicinal chemistry · 2021Review
- Resveratrol and Resveratrol-Aspirin Hybrid Compounds as Potent Intestinal Anti-Inflammatory and Anti-Tumor Drugs.Molecules (Basel, Switzerland) · 2020Article
- Modular Protein Ligation: A New Paradigm as a Reagent Platform for Pre-Clinical Drug Discovery.Scientific reports · 2019Article
- Molecular and Cellular Characterization of SIRT1 Allosteric Activators.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Identification of a cellularly active SIRT6 allosteric activator.Nature chemical biology · 2018Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
Abstract
The NAD(+)-dependent deacetylase SIRT1 plays key roles in numerous cellular processes including DNA repair, gene transcription, cell differentiation, and metabolism. Overexpression of SIRT1 protects against a number of age-related diseases including diabetes, cancer, and Alzheimer's disease. Moreover, overexpression of SIRT1 in the murine brain extends lifespan. A number of small-molecule sirtuin-activating compounds (STACs) that increase SIRT1 activity in vitro and in cells have been developed. While the mechanism for how these compounds act on SIRT1 was once controversial, it is becoming increasingly clear that they directly interact with SIRT1 and enhance its activity through an allosteric mechanism. Here, we present detailed chemical syntheses for four STACs, each from a distinct structural class. Also, we provide a general protocol for purifying active SIRT1 enzyme and outline two complementary enzymatic assays for characterizing the effects of STACs and similar compounds on SIRT1 activity.
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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.