ArticleInternational journal of molecular sciences2017
Identification of Direct Activator of Adenosine Monophosphate-Activated Protein Kinase (AMPK) by Structure-Based Virtual Screening and Molecular Docking Approach.
Article in International journal of molecular sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Chemical Composition, Antioxidant Activity, Anti-Fatigue Function and Mechanism of Pomegranate Peel Polyphenols on Exercise-Induced Fatigue in Mice.Foods (Basel, Switzerland) · 2026Article
- Review
- Exploring natural AMPK activators from bioactive compounds in fenugreek and oyster mushroom for management of type 2 diabetes.Scientific reports · 2025Article
- AMPK: an enzyme that may be effective in cancer and metabolic diseases.Discover oncology · 2025Review
- AMPK in Intestinal Health and Disease: A Multifaceted Therapeutic Target for Metabolic and Inflammatory Disorders.Drug design, development and therapy · 2025Review
- Will AMPK be a potential therapeutic target for hepatocellular carcinoma?American journal of cancer research · 2024Review
- Synthesis and biological evaluation of 4-phenoxy-phenyl isoxazoles as novel acetyl-CoA carboxylase inhibitors.Journal of enzyme inhibition and medicinal chemistry · 2021Article
- Docking-based virtual screening of TβR1 inhibitors: evaluation of pose prediction and scoring functions.BMC chemistry · 2020Article
- Ethoxysanguinarine, a Novel Direct Activator of AMP-Activated Protein Kinase, Induces Autophagy and Exhibits Therapeutic Potential in Breast Cancer Cells.Frontiers in pharmacology · 2019Article
- All-Frontiers in pharmacology · 2019Article
- Special Protein Molecules Computational Identification.International journal of molecular sciences · 2018Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Adenosine monophosphate-activated protein kinase (AMPK) plays a critical role in the regulation of energy metabolism and has been targeted for drug development of therapeutic intervention in Type II diabetes and related diseases. Recently, there has been renewed interest in the development of direct β1-selective AMPK activators to treat patients with diabetic nephropathy. To investigate the details of AMPK domain structure, sequence alignment and structural comparison were used to identify the key amino acids involved in the interaction with activators and the structure difference between β1 and β2 subunits. Additionally, a series of potential β1-selective AMPK activators were identified by virtual screening using molecular docking. The retrieved hits were filtered on the basis of Lipinski's rule of five and drug-likeness. Finally, 12 novel compounds with diverse scaffolds were obtained as potential starting points for the design of direct β1-selective AMPK activators.
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