ArticleFrontiers in pharmacology2017
Identification of Epigallocatechin-3- Gallate as an Inhibitor of Phosphoglycerate Mutase 1.
Article in Frontiers in pharmacology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 62 citations in OpenAlex.
- Targeting PGAM1 Y119 phosphorylation resensitizes non-small-cell lung cancer to cisplatin therapy by promoting oxidative stress and DNA damage.The Journal of biological chemistry · 2026Article
- Utilizing drugs, food, and natural product libraries: A computational approach to targeting PGAM1 in clinical cancer therapy.Medicine · 2026Article
- Glycolysis and glycolytic enzymes in acute myeloid leukemia: Warburg and beyond.Frontiers in pharmacology · 2026Review
- The function of phosphoglycerate mutase 1 (PGAM1) and its role in diseases.Frontiers in molecular biosciences · 2026Review
- Article
- The glycolytic reaction PGAM restrains Th17 pathogenicity and Th17-dependent autoimmunity.Cell reports · 2025Article
- The roles of epigallocatechin gallate in the tumor microenvironment, metabolic reprogramming, and immunotherapy.Frontiers in immunology · 2024Review
- Himalayan flora: targeting various molecular pathways in lung cancer.Medical oncology (Northwood, London, England) · 2023Review
- The Role of Reprogrammed Glucose Metabolism in Cancer.Metabolites · 2023Review
- Epigallocatechin Gallate: pH-Dependent Redox Properties and Effect on Respiration, Photosynthesis, and Cell Death in Pea Plants.Biochemistry. Biokhimiia · 2023Article
- Article
- Revisited Metabolic Control and Reprogramming Cancers by Means of the Warburg Effect in Tumor Cells.International journal of molecular sciences · 2022Review
- Targeting Energy Metabolism in Cancer Treatment.International journal of molecular sciences · 2022Review
- Tumor microenvironment-activated cancer cell membrane-liposome hybrid nanoparticle-mediated synergistic metabolic therapy and chemotherapy for non-small cell lung cancer.Journal of nanobiotechnology · 2021Article
- Current Development and Application of Anaerobic Glycolytic Enzymes in Urothelial Cancer.International journal of molecular sciences · 2021Review
- 3D-QSAR, Molecular Docking, and MD Simulations of Anthraquinone Derivatives as PGAM1 Inhibitors.Frontiers in pharmacology · 2021Article
- A Simple, Label-Free, and High-Throughput Method to Evaluate the Epigallocatechin-3-Gallate Impact in Plasma Molecular Profile.High-throughput · 2020Article
- Toward a structome of Acinetobacter baumannii drug targets.Protein science : a publication of the Protein Society · 2020Article
- Phosphoglycerate Mutase 1: Its Glycolytic and Non-Glycolytic Roles in Tumor Malignant Behaviors and Potential Therapeutic Significance.OncoTargets and therapy · 2020Review
- Decreased FBP1 expression rewires metabolic processes affecting aggressiveness of glioblastoma.Oncogene · 2020Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Targeting metabolic enzymes is believed to provide new therapeutic opportunities for cancer therapy. Phosphoglycerate mutase 1 (PGAM1) is a glycolytic enzyme that importantly coordinates glycolysis, pentose phosphate pathway (PPP) flux and serine biosynthesis in cancer cells and hence gains increasing interest of inhibitor discovery. Only few PGAM1 inhibitors have been reported and the molecular potency remains very limited. In an effort to discover new PGAM1 inhibitors, we carried out a biochemical assay-based screen that was focused on natural products derived small molecule compounds. (-)-Epigallocatechin-3-gallate (EGCG), the major natural catechins of green tea extract, was identified as a PGAM1 inhibitor that was tremendously more potent than known PGAM1 inhibitors. Further studies combining molecular docking and site-specific mutagenesis revealed that EGCG inhibited PGAM1 enzymatic activity in a manner independent of substrate competition. EGCG modulated the intracellular level of 2-phosphoglycerate, impaired glycolysis and PPP and inhibited proliferation of cancer cells. This study suggested EGCG as a chemical scaffold for the discovery of potent PGAM1 inhibitors and gained mechanistic insights to understand the previously appreciated anticancer properties of EGCG.
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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.