ArticleAngewandte Chemie (International ed. in English)2017
Mechanism-Based Inhibitors of the Human Sirtuin 5 Deacylase: Structure-Activity Relationship, Biostructural, and Kinetic Insight.
Article in Angewandte Chemie (International ed. in English), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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
32 citing papers in PubMed.
- Substrate Specificity and Kinetic Mechanism of the NAD+-Dependent Deacylase from Mycobacterium tuberculosis, Rv1151c (Mt-Sirt).Biochemistry · 2026Article
- Comparative Structure-Based Analysis of Predicted BZD9L1 Binding Modes Across Human Sirtuins.International journal of molecular sciences · 2026Article
- From Pharmacophore to Warhead: NADAngewandte Chemie (International ed. in English) · 2025Article
- Sirtuins in mitophagy: key gatekeepers of mitochondrial quality.Molecular and cellular biochemistry · 2025Review
- Advancing Covalent Ligand and Drug Discovery beyond Cysteine.Chemical reviews · 2025Review
- Activation and inhibition of sirtuins: From bench to bedside.Medicinal research reviews · 2025Review
- Bioluminescence assay of lysine deacylase sirtuin activity.Cell chemical biology · 2024Article
- The Histone Deacetylase Family: Structural Features and Application of Combined Computational Methods.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Current Trends in Sirtuin Activator and Inhibitor Development.Molecules (Basel, Switzerland) · 2024Review
- Review
- Aryl Fluorosulfate Based Inhibitors That Covalently Target the SIRT5 Lysine Deacylase.Angewandte Chemie (International ed. in English) · 2022Article
- Identification of 2-hydroxybenzoic acid derivatives as selective SIRT5 inhibitors.European journal of medicinal chemistry · 2022Article
- SIRT5 is a proviral factor that interacts with SARS-CoV-2 Nsp14 protein.PLoS pathogens · 2022Article
- Therapeutic Potential and Activity Modulation of the Protein Lysine Deacylase Sirtuin 5.Journal of medicinal chemistry · 2022Review
- Insights on the Modulation of SIRT5 Activity: A Challenging Balance.Molecules (Basel, Switzerland) · 2022Review
- Sirtuin modulators: past, present, and future perspectives.Future medicinal chemistry · 2022Review
- Investigation of Carboxylic Acid Isosteres and Prodrugs for Inhibition of the Human SIRT5 Lysine Deacylase Enzyme.Angewandte Chemie (International ed. in English) · 2022Article
- Class I histone deacetylases (HDAC1-3) are histone lysine delactylases.Science advances · 2022Article
- Combining Metabolomics and Experimental Evolution Reveals Key Mechanisms Underlying Longevity Differences in Laboratory EvolvedInternational journal of molecular sciences · 2022Article
- SIRT5 is a proviral factor that interacts with SARS-CoV-2 Nsp14 protein.bioRxiv : the preprint server for biology · 2022Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
The sirtuin enzymes are important regulatory deacylases in a variety of biochemical contexts and may therefore be potential therapeutic targets through either activation or inhibition by small molecules. Here, we describe the discovery of the most potent inhibitor of sirtuin 5 (SIRT5) reported to date. We provide rationalization of the mode of binding by solving co-crystal structures of selected inhibitors in complex with both human and zebrafish SIRT5, which provide insight for future optimization of inhibitors with more "drug-like" properties. Importantly, enzyme kinetic evaluation revealed a slow, tight-binding mechanism of inhibition, which is unprecedented for SIRT5. This is important information when applying inhibitors to probe mechanisms in biology.
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Registered trials
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